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ATP + a protein
ADP + a phosphoprotein
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
ATP + AGD9
ADP + phosphorylated AGD9
-
-
-
?
ATP + AGDSTPEELANATQVQGDYLPIVR
ADP + AGDSpTPEELANATQVQGDYLPIVR
-
-
-
?
ATP + AML1
ADP + phosphorylated AML1
-
-
-
?
ATP + AP1
ADP + phosphorylated AP1
ATP + Arabidopsis thaliana protein AT1G7815
ADP + phosphorylated Arabidopsis thaliana proteins AT1G78150
-
-
-
?
ATP + Arabidopsis thaliana protein AT2G26530
ADP + phosphorylated Arabidopsis thaliana proteins AT2G26530
-
-
-
?
ATP + Arabidopsis thaliana protein AT3G11330
ADP + phosphorylated Arabidopsis thaliana proteins AT3G11330
-
-
-
?
ATP + Arabidopsis thaliana protein AT4G38710
ADP + phosphorylated Arabidopsis thaliana proteins AT4G38710
-
-
-
?
ATP + ARF-GAP domain 9
ADP + phosphorylated ARF-GAP domain 9
-
-
-
?
ATP + ASGSPPVPVMHSPPRPVTVK
ADP + ASGSPPVPVMHpSPPRPVTVK
-
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
ATP + ATF2
ADP + a phosphorylated ATF2
substrate in assay, biotinylated ATF2
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
ATP + ATF2DELTA109
ADP + phosphorylated ATF2DELTA109
-
-
-
-
?
ATP + ATMIN7
ADP + phosphorylated ATMIN7
-
-
-
?
ATP + ATMKP1 mitogen-activated protein kinase phosphatase 1
ADP + phosphorylated ATMKP1 mitogen-activated protein kinase phosphatase 1
-
-
-
?
ATP + ATP-dependent RNA helicase
ADP + phosphorylated ATP-dependent RNA helicase
-
-
-
?
ATP + Axl2
ADP + phospho-Axl2
-
substrate of Hog1
-
-
?
ATP + Bcl-2
ADP + phosphorylated Bcl-2
-
-
-
?
ATP + BES1
ADP + phosphorylated BES1
ATP + c-Jun
ADP + phosphorylated c-Jun
ATP + c-Jun activation domain
ADP + phosphorylated c-Jun activation domain
ATP + c-Jun transcription factor
ADP + phosphorylated c-Jun transcription factor
-
JNK phosphorylates the N-terminal transactivation domain of c-Jun transcription factor
-
-
?
ATP + casein
ADP + phosphocasein
-
substrate of Hog1
-
-
?
ATP + cdc42
ADP + phosphorylated cdc42
-
substrate of Gic2
-
-
?
ATP + COP1-interacting protein 7
ADP + phosphorylated COP1-interacting protein 7
-
-
-
?
ATP + DAETVNQTSHPTEEEAQVTVSSNADVEDSHETVSPR
ADP + DAETVNQTSHPTEEEAQVTVSSNADVEDSHETVpSPR
-
-
-
?
ATP + DIQGSDNAIPLSPQWLLSKPGENK
ADP + DIQGSDNAIPLpSPQWLLSKPGENK
-
-
-
?
ATP + DLSMNKFDWDHPLHLQPMSPTTVK
ADP + DLSMNKFDWDHPLHLQPMpSPTTVK
-
-
-
?
ATP + DNA polymerase II
ADP + phosphorylated DNA polymerase II
-
substrate of Hog1p
-
-
?
ATP + EB1c
ADP + phosphorylated EB1c
ATP + EGF receptor peptide
ADP + phosphorylated EGF receptor peptide
-
-
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
ATP + Elk1
ADP + phosphorylated Elk1
ATP + ELKERK
?
-
ERK1
-
-
?
ATP + epsin N-terminal homology domain-containing protein
ADP + phosphorylated epsin N-terminal homology domain-containing protein
-
-
-
?
ATP + ERKMEK1
?
-
ERK1
-
-
?
ATP + ERKMEK2
?
-
ERK1
-
-
?
ATP + ERKSTE7
?
-
ERK1
-
-
?
ATP + ERKSub
?
-
ERK1 and p38alpha kinase
-
-
?
ATP + Ets-1
ADP + phosphorylated Ets-1
-
-
-
-
?
ATP + FDWDHPLHLQPMSPTTVK
ADP + FDWDHPLHLQPMpSPTTVK
-
-
-
?
ATP + FITC-Aca-Ala-Ala-Ala-Thr-Gly-Pro-Leu-Ser-Pro-Gly-Pro-Phe-Ala-NH2
ADP + phosphorylated FITC-Aca-Ala-Ala-Ala-Thr-Gly-Pro-Leu-Ser-Pro-Gly-Pro-Phe-Ala-NH2
-
FITC-labeled ERK substrate peptide
-
-
?
ATP + FKVTSADLSPK
ADP + FKVTSADLpSPK
-
-
-
?
ATP + focal adhesion kinase
ADP + phosphorylated focal adhesion kinase
phosphorylation of FAK at S910, which promotes the disassembly of focal adhesion (hemidesmosome disruption) during cell migration
-
-
?
ATP + fructose-2,6-bisphosphatase
ADP + phosphorylated fructose-2,6-bisphosphatase
-
-
-
?
ATP + FTDSALASAVFSPTHK
ADP + FTDSALASAVFpSPTHK
-
-
-
?
ATP + GATA type zinc finger transcription factor family protein
ADP + phosphorylated GATA type zinc finger transcription factor family protein
-
-
-
?
ATP + Gic2
ADP + phosphorylated Gic2
-
substrate of Fus3, and of Hog1
-
-
?
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
ATP + GMVSSGGPVSPGPVYPGGRPGAGGLMPGMPGTR
ADP + GMVSSGGPVpSPGPVYPGGRPGAGGLMPGMPGTR
-
-
-
?
ATP + GST-c-Jun
ADP + phosphorylated GST-c-Jun
-
substrate in kinase activity assay
-
-
?
ATP + HAP5 cation-chloride co-transporter 1
ADP + phosphorylated HAP5 cation-chloride co-transporter 1
-
-
-
?
ATP + heat shock factor 1
ADP + phosphorylated heat shock factor 1
-
phosphorylation at Ser-326, Ser-303 and Ser-307, better substrate for p38gamma than for any of the other p38 isoforms
-
-
?
ATP + histone H1
ADP + phospho-histone H1
-
substrate of Hog1
-
-
?
ATP + Hog1D
ADP + phospho-Hog1D
-
substrate of Hog1
-
-
?
ATP + Hot1p
ADP + phosphorylated Hot1p
ATP + Hsl1
ADP + phospho-Hsl1
-
substrate of Hog1
-
-
?
ATP + human glucocorticoid receptor
ADP + phosphorylated human glucocorticoid receptor
ATP + HVVDEPANEEKPSESSAALSPEK
ADP + HVVDEPANEEKPSESSAALpSPEK
-
-
-
?
ATP + iqd2 IQ-domain 2
ADP + phosphorylated iqd2 IQ-domain 2
-
-
-
?
ATP + iqd32 IQ-domain 31
ADP + phosphorylated iqd32 IQ-domain 31
-
-
-
?
ATP + iqd32 IQ-domain 32
ADP + phosphorylated iqd32 IQ-domain 32
-
-
-
?
ATP + IRS-1
ADP + phosphorylated IRS-1
-
phosphorylation of the insulin receptor substrate IRS-1 at serine 307
-
-
?
ATP + JAL30 PYK10-binding protein 1
ADP + phosphorylated JAL30 PYK10-binding protein 1
-
-
-
?
ATP + JunD
ADP + phosphorylated JunD
-
-
-
-
?
ATP + KFSEQNIGAPPSYEEAVSDSRSPVYSER
ADP + KFpSEQNIGAPPSYEEAVSDSRpSPVYSER
-
-
-
?
ATP + La protein 1
ADP + phosphorylated La protein 1
-
-
-
?
ATP + Lin-1
ADP + phosphorylated Lin-1
ATP + MAP65-1
ADP + phosphorylated MAP65-1
microtubule-associated protein, phosphorylation in vitro by MPK6, recombinant GST-tagged substrate protein
-
-
?
ATP + MAPK
ADP + phosphorylated MAPK
-
-
-
-
?
ATP + MAPKAP kinase-2
ADP + phosphorylated MAPKAP kinase-2
-
-
-
?
ATP + MAPKAP kinase-3
ADP + phosphorylated MAPKAP kinase-3
-
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
-
-
-
-
?
ATP + MAPKAPK2
ADP + phosphorylated MAPKAPK2
-
-
-
?
ATP + MAPKAPK2-peptide
ADP + phosphorylated MAPKAPK2-peptide
-
the peptide substrate is derived from a sequence of a mitogen-activated protein kinase activated protein kinase-2, MAPKAPK2, phopshorylation site
-
-
?
ATP + MBP
ADP + phospho-MBP
-
substrate of Hog1
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
-
-
-
-
?
ATP + MEK
ADP + phosphorylated MEK
-
-
binding to ERK requires docking domain and the kinase interaction motif
-
?
ATP + Mek1
ADP + phospho-Mek1
-
substrate of Hog1
-
-
?
ATP + MEK1ERK
?
-
ERK1 and p38alpha kinase
-
-
?
ATP + MEK2ERK
?
-
ERK1 and p38alpha kinase
-
-
?
ATP + mitogen-activated protein kinase phosphatase 1
ADP + phosphorylated mitogen-activated protein kinase phosphatase 1
-
-
-
?
ATP + MK2
ADP + phosphorylated MK2
ATP + MKS1
ADP + phosphorylated MSK1
ATP + MMP-9
ADP + phosphorylated MMP-9
ATP + Mps1
ADP + phosphorylated Mps1
-
Mps1 phosphorylation by MAPK at S844, spindle checkpoint requires phosphorylation at S844, may create a phosphoepitope that allows Mps1 to interact with kinetochores
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
ATP + MYB32
ADP + phosphorylated MYB32
-
-
-
-
?
ATP + myelin basic protein
ADP + a phosphorylated myelin basic protein
-
substrate in kinase assay
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
ATP + Net
ADP + phosphorylated Net
ATP + NLSLNPTASAAPVTPPKKDDKPEDILFK
ADP + NLSLNPTASAAPVpTPPKKDDKPEDILFK
-
-
-
?
ATP + nodulation outer protein L
ADP + a phosphorylated nodulation outer protein L
nodulation outer protein L variants with six or eight serine to alanine substitutions are partially active, whereas nodulation outer protein L forms with 10 or 12 substituted serine residues are inactive
-
-
?
ATP + NTEEGEMVNNNVSPMMHSR
ADP + NTEEGEMVNNNVpSPMMHSR
-
-
-
?
ATP + NVEKVEEIRSPQTINK
ADP + NVEKVEEIRpSPQTINK
-
-
-
?
ATP + p38
ADP + phosphorylated p38
-
-
-
-
?
ATP + phosphoenolpyruvate carboxykinase 1
ADP + phosphorylated phosphoenolpyruvate carboxykinase 1
-
-
-
?
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
ATP + protein
ADP + phosphoprotein
ATP + protein APP
ADP + phosphorylated protein APP
-
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
ATP + protein EGFRP
ADP + phosphorylated protein EGFRP
-
epidermal growth factor receptor peptide, substrate in kinase activity assay
-
-
?
ATP + protein tyrosine kinase 2
ADP + phosphorylated protein tyrosine kinase 2
-
substrate of Hog1
-
-
?
ATP + RAD9
ADP + phospho-RAD9
-
high activity with Fus3, low activity with Hog1
-
-
?
ATP + RAD9p
ADP + phospho-RAD9p
-
substrate of Hog1
-
-
?
ATP + Rck2
ADP + phosphorylated Rck2
-
-
-
-
?
ATP + Red1
ADP + phospho-Red1
-
preferred substrate of Hog1
-
-
?
ATP + RRPSLSPPPPYR
ADP + RRPpSLpSPPPPYR
-
-
-
?
ATP + RSK
ADP + phosphorylated RSK
-
-
binding to ERK requires docking domain
-
?
ATP + RSYSPGYEGAAAAAPDRDR
ADP + RpSYpSPGYEGAAAAAPDRDR
-
-
-
?
ATP + SAIPDTRPRTPIHESAATGR
ADP + SAIPDTRPRpTPIHESAATGR
-
-
-
?
ATP + SC35-like splicing factor 30
ADP + phosphorylated SC35-like splicing factor 30
-
-
-
?
ATP + SCRAMMMEK2
?
-
ERK1
-
-
?
ATP + SKDSNVTPDDDVSGMRSPSAFFK
ADP + SKDSNVTPDDDVSGMRpSPSAFFK
-
-
-
?
ATP + Smad1
ADP + phosphorylated Smad1
ATP + Smad3
ADP + phosphorylated Smad3
ATP + sodium channel Na(v)1.6
ADP + phosphorylated sodium channel Na(v)1.6
-
-
-
-
?
ATP + sodium channel Na(v)1.7
ADP + phosphorylated sodium channel Na(v)1.7
-
-
-
-
?
ATP + sodium channel Na(v)1.8
ADP + phosphorylated sodium channel Na(v)1.8
-
-
-
-
?
ATP + SPRH1
ADP + phosphorylated SPRH1
-
phosphorylation at Ser-49, Ser-52 and Ser-94
-
-
?
ATP + Ste50
ADP + phosphorylated Ste50
ATP + STE7ERK
?
-
ERK1
-
-
?
ATP + Swe1
ADP + phospho-Swe1
-
substrate of Hog1
-
-
?
ATP + Swi6
ADP + phospho-Swi6
-
substrate of Hog1
-
-
?
ATP + SYSPGYEGAAAAAPDRDR
ADP + phosphorylated SYpSPGYEGAAAAAPDRDR
-
-
-
?
ATP + target of Myb protein 1
ADP + phosphorylated target of Myb protein 1
-
-
-
?
ATP + TBP
ADP + phosphorylated TBP
-
substrate of p38 MAPK
-
-
?
ATP + TEEGEMVNNNVSPMMHSR
ADP + TEEGEMVNNNVpSPMMHSR
-
-
-
?
ATP + TLSYPTPPLNLQSPR
ADP + TLSYPTPPLNLQpSPR
-
-
-
?
ATP + TPSRLAGMFSGTQDK
ADP + pTPpSRLAGMFSGTQDK
-
-
-
?
ATP + transcription factor ATF2
ADP + phosphorylated transcription factor ATF2
-
-
-
?
ATP + transcription factor Djun
ADP + phosphorylated transcription factor Djun
-
-
-
?
ATP + transcription factor Elk-1
ADP + phosphorylated transcription factor Elk-1
-
-
-
?
ATP + transcription factor SAP-1
ADP + phosphorylated transcription factor SAP-1
-
-
-
?
ATP + trehalose-6-phosphatase synthase S8
ADP + phosphorylated trehalose-6-phosphatase synthase S8
-
-
-
?
ATP + TTFVPSTPPALKTTFVPSTPPALK
ADP + TTFVPpSpTPPALKTTFVPpSTPPALK
-
-
-
?
ATP + Tub4p
ADP + phospho-Tub4
-
substrate of Hog1
-
-
?
ATP + TVANSPEALQSPHSSESAFALK
ADP + TVANSPEALQpSPHSSESAFALK
-
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
ATP + VLN3
ADP + phosphorylated VLN3
-
-
-
?
ATP + VVEEKPASPEPVKAEAEKPVEK
ADP + VVEEKPApSPEPVKAEAEKPVEK
-
-
-
?
ATP + WRKY1
ADP + phosphorylated WRKY1
-
-
-
?
ATP + WRKY25
ADP + phosphorylated WRKY25
-
the transcription factor is an in vitro substrate of MPK4
-
-
?
ATP + WRKY33
ADP + phosphorylated WRKY33
-
the transcription factor is an in vitro substrate of MPK4
-
-
?
ATP + WSIP1
ADP + phosphorylated WSIP1
-
-
-
?
ATP + YEEMNKPSAPLTSHEPAMIPVAEEPDDSPIHGREESLVR
ADP + YEEMNKPSAPLTSHEPAMIPVAEEPDDpSPIHGREESLVR
-
-
-
?
ATP + YSLVLDPNLDAGTPR
ADP + YSLVLDPNLDAGpTPR
-
-
-
?
ATP + YVEEWVGPGSPMNSPR
ADP + YVEEWVGPGSPMNpSPR
-
-
-
?
ATPgammaS + myelin basic protein
ADP + thiophosphorylated myelin basic protein
Arabidopsis thaliana MPKs use ATPgammaS to thiophosphorylate myelin basic protein
-
-
?
N6-benzyl-ATPgammaS + myelin basic protein
ADP + benzylthiophosphorylated myelin basic protein
Arabidopsis thaliana MPK3 mutant T119A uses N6-benzyl-ATPgammaS to thiophosphorylate myelin basic protein
-
-
?
phosphoprotein
?
-
the MAPK is regulated in the MAPK signaling cascade by 2 mechanisms: 1. by MEK, EC 2.7.11.25, docking at the allosteric ED domain or the CD domain of MAPKs, or 2. by MKK7, MLK, JNK or MKP-7 docking at the scaffolding protein JIP in the JNK signaling pathway
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
ERK2 phosphorylates MBP, p38 phosphorylates the protein substrate MAPKAP2 and the peptide substrate KRELVEPLTPSGEAPNQALLR, other substrates of MAPK are transcription factors, such as c-Jun, ATF-2, and MEF2A
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
702641, 702692, 702942, 703019, 703255, 703573, 704471, 705276, 705321, 705447, 706080, 706863 -
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
MAPK activate mitogen-activated proteins in several signal transduction pathways, overview
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2
-
-
?
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2, recombinant GST-tagged ATF2DELTA115
-
-
?
ATP + AP1
ADP + phosphorylated AP1
-
substrate of ERK1/2, ERK access to the substrate is regulated by the all-trans retinoic acid receptor, RAR
-
-
?
ATP + AP1
ADP + phosphorylated AP1
-
substrate of ERK1/2
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
-
-
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
assay substrate biotinylated ATF-2
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
-
substrate in kinase activity assay
-
-
?
ATP + ATF-2
ADP + phosphorylated ATF-2
-
substrate in kinase assay
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
-
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
-
substrate in in vitro kinase assay, LanthaScreen
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
phosphorylation by p38 MAPK at threonine residues
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor. S286 and S137 residues are required for flg22-induced BES1 full phosphorylation in vivo, in which S286 plays a greater role than S137
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor. S286 and S137 residues are required for flg22-induced BES1 full phosphorylation in vivo, in which S286 plays a greater role than S137
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
activity assay
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
substrate of JNK
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
substrate of JNK, binding via delta domain of c-Jun substrate
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
recombinant GST-tagged substrate, the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
recombinant GST-tagged substrate, the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + c-Jun activation domain
ADP + phosphorylated c-Jun activation domain
enzyme binds to the c-Jun transactivation domain and phosphorylates it on Ser63 and Ser73
-
-
?
ATP + c-Jun activation domain
ADP + phosphorylated c-Jun activation domain
JNK2 binds c-Jun approximately 25 times more efficiently than JNK1
-
-
?
ATP + EB1c
ADP + phosphorylated EB1c
the microtubule plus end protein
-
-
?
ATP + EB1c
ADP + phosphorylated EB1c
the microtubule plus end protein, recombinant GST-tagged substrate protein, phosphorylation on a threonine residue
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor with modified D-site by swapping two hydrophobic residues
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
-
recombinant GST-tagged Elk1, substrate of ERK2
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
-
-
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
recombinant GST-tagged substrate, the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
recombinant GST-tagged substrate, the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + Hot1p
ADP + phosphorylated Hot1p
-
substrate of Hog1p
-
-
?
ATP + Hot1p
ADP + phosphorylated Hot1p
-
substrate of Hog1p, phosphorylation of Hot1p is not required for Hot1p-mediated gene expression
-
-
?
ATP + human glucocorticoid receptor
ADP + phosphorylated human glucocorticoid receptor
-
specific phosphorylation at Ser211 by p38 MAPK, p38 MAPK is a mediator in glucocorticoid-induced apoptosis of lymphoid cells, interaction of MAPK and glucocorticoid pathways, overview
-
-
?
ATP + human glucocorticoid receptor
ADP + phosphorylated human glucocorticoid receptor
-
specific phosphorylation at Ser211 by p38 MAPK
-
-
?
ATP + Lin-1
ADP + phosphorylated Lin-1
substrate of ERK2, negative regulation of Lin-1
-
-
?
ATP + Lin-1
ADP + phosphorylated Lin-1
Lin-1 is an ETS transcription factor, substrate of ERK2, binding via the docking sequence of the substrate
-
-
?
ATP + MK2
ADP + phosphorylated MK2
-
-
-
-
?
ATP + MK2
ADP + phosphorylated MK2
-
-
-
?
ATP + MK2
ADP + phosphorylated MK2
-
-
-
?
ATP + MKS1
ADP + phosphorylated MSK1
-
MPK4 acts as a regulator of pathogen defense responses and is required for repression of salicylic acid-dependent resistance and for activation of jasmonate-dependent defense gene expression via MSK1, which interacts with the transcription factors WRKY25 and WRKY33
-
-
?
ATP + MKS1
ADP + phosphorylated MSK1
-
substrate of MPK4
-
-
?
ATP + MMP-9
ADP + phosphorylated MMP-9
-
activity of p38 MAP kinase, TNF-alpha stimulates MMP-9 expression via the p38 MAP kinase signaling pathway in 5637 cells, and p38 MAP kinase-mediated MMP-9 gene regulation in response to TNF-alpha is involved in the NF-kappaB response element in 5637 cells, regulation, overview
-
-
?
ATP + MMP-9
ADP + phosphorylated MMP-9
-
activity of p38 MAP kinase
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
CAD initiates and regulates de novo pyrimidine biosynthesis and is activated by phosphorylation at Thr456 by nuclear MAPKs, nuclear import of CAD is required for optimal cell growth
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
phosphorylation at Thr456, native and recombinant CAD
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
CAD initiates and regulates de novo pyrimidine biosynthesis and is activated by phosphorylation at Thr456 by nuclear MAPKs, nuclear import of CAD is required for optimal cell growth
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
phosphorylation at Thr456, native and recombinant multifunctional protein CAD
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
substrate in in vitro kinase assay
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
substrate of ERK2
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor with modified D-site by swapping two hydrophobic residues
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
-
-
?
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
the reaction is performed by activated phosphorylated ERK2, phosphorylation inhibits phospholipase C-gamma1
-
-
?
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
recombinant substrate, the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylates both Thr and Tyr residues
-
-
?
ATP + protein
ADP + phosphoprotein
Ser/Thr kinase
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation
-
-
?
ATP + protein
ADP + phosphoprotein
proline-directed kinase
-
-
?
ATP + protein
ADP + phosphoprotein
autophosphorylation on both tyrosine and threonine residues, autophosphorylation is probably involved in the MAP kinase activation process in vitro, but it may not be sufficient for full activation
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
-
recombinant GST-tagged ATF2 substrate
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
-
recombinant GST-tagged ATF2DELTA115
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
-
-
-
?
ATP + Smad1
ADP + phosphorylated Smad1
-
the MAP kinase antagonizes Smad1 in signaling during development of axis and neural specification, Smad1 is involved in dorsal-ventral patterning in embryos
-
-
?
ATP + Smad1
ADP + phosphorylated Smad1
-
phosphorylation by MAP kinase inhibits Smad1 and the BMP-4/Smad1 signaling pathway, phosphorylation sites are S187, S195, S205, and S213, activity with Smad1 mutant S187/S195/S205/S213, overview
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2, identification of phosphorylation sites Ser203, Ser207, and Thr187, Ser207 is the best phosphorylation site for ERK2, other MAPKs than ERK2 also phosphorylate Ser212
-
-
?
ATP + Ste50
ADP + phosphorylated Ste50
Hog1 phosphorylates Ste50 in response to osmotic stress, and phosphorylation of Ste50 limits the duration of Kss1 activation and prevents invasive growth under high osmolarity growth conditions. The feedback phosphorylation event leads to more transient activation of Hog1, regulation, overview
-
-
?
ATP + Ste50
ADP + phosphorylated Ste50
Hog1 phosphorylates Ste50 in response to osmotic stress, and phosphorylation of Ste50 limits the duration of Kss1 activation and prevents invasive growth under high osmolarity growth conditions. The feedback phosphorylation event leads to more transient activation of Kss1, regulation, overview
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
-
phosphorylation of tyrosine hydroxylase at Ser8 and Ser31 by ERK1 and ERK2 is involved in regulation of catecholamine biosynthesis
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
-
recombinant rat wild-type and S8A, S31A, S19A, and S40A mutant tyrosine hydroxylase substrates, phosphorylation at Ser8 and Ser31 by ERK1 and ERK2, ERK2 prefers the Ser31 phosphorylation site, no activity with substrate mutant S8A/S31A
-
-
?
additional information
?
-
FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
-
-
?
additional information
?
-
FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
-
-
?
additional information
?
-
FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
-
-
?
additional information
?
-
-
FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
-
-
?
additional information
?
-
-
MPK6 interacts with gamma-tubulin and co-sediments with plant microtubules polymerized in vitro. The active form of MAP kinase is enriched with microtubules and follows similar dynamics to gamma-tubulin, moving from poles to midzone during the anaphase-to-telophase transition
-
-
?
additional information
?
-
MPK6 interacts with gamma-tubulin and co-sediments with plant microtubules polymerized in vitro. The active form of MAP kinase is enriched with microtubules and follows similar dynamics to gamma-tubulin, moving from poles to midzone during the anaphase-to-telophase transition
-
-
?
additional information
?
-
-
no activity with recombinant GST-tagged EB1a protein. MPK6 is recruited to gamma-tubulin or gamma-tubulin complexes, but no direct phosphorylation of either gamma-tubulin or gamma-tubulin complex protein GCP4 wby MPK6 is detectable in vitro
-
-
?
additional information
?
-
no activity with recombinant GST-tagged EB1a protein. MPK6 is recruited to gamma-tubulin or gamma-tubulin complexes, but no direct phosphorylation of either gamma-tubulin or gamma-tubulin complex protein GCP4 wby MPK6 is detectable in vitro
-
-
?
additional information
?
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
-
enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
-
-
?
additional information
?
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
-
-
?
additional information
?
-
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
-
-
?
additional information
?
-
the mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
-
-
?
additional information
?
-
-
the mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
enzyme plays an important role in egg maturation or ectogenetic early development
-
-
?
additional information
?
-
enzyme plays an important role in egg maturation or ectogenetic early development
-
-
?
additional information
?
-
-
enzyme plays an important role in egg maturation or ectogenetic early development
-
-
?
additional information
?
-
possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
-
-
?
additional information
?
-
possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
-
-
?
additional information
?
-
possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
-
-
?
additional information
?
-
-
possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
-
-
?
additional information
?
-
-
spatiotemporal control of the Ras/ERK MAP kinase signaling pathway, involving multiple factors, is a key factor for determining the specificity of cellular responses including cell proliferation, cell differentiation, and cell survival, the fidelity of the signaling is regulated by docking interactions and by scaffolding, molecular mechanism of negative regulation of Ras/ERK signaling
-
-
?
additional information
?
-
ERK1 plays an essential role during the growth and differentiation
-
-
?
additional information
?
-
-
ERK1 plays an essential role during the growth and differentiation
-
-
?
additional information
?
-
JUN N-terminal kinase signaling is required to initiate the cell shape change at the onset of the epithelial wound healing. The embryonic JUN N-terminal kinase gene cassette is induced at the edge of the wound
-
-
?
additional information
?
-
functions of D-p38 is to attenuate antimicrobial peptide gene expression following exposure to lipopolysaccharide
-
-
?
additional information
?
-
functions of D-p38 is to attenuate antimicrobial peptide gene expression following exposure to lipopolysaccharide
-
-
?
additional information
?
-
DJNK signal transduction pathway mediates an immune response and morphogenesis
-
-
?
additional information
?
-
dorsal closure, a morphogenetic movement during Drosophila embryogenesis, is controlled by the Drosophila JNK pathway, D-Fos and the phosphatase Puckered
-
-
?
additional information
?
-
MAP kinase, ERK-A is required downstream of raf in the Sev signal transduction pathway
-
-
?
additional information
?
-
-
MAP kinase, ERK-A is required downstream of raf in the Sev signal transduction pathway
-
-
?
additional information
?
-
enzyme may function to modulate Dpp signaling
-
-
?
additional information
?
-
-
enzyme may function to modulate Dpp signaling
-
-
?
additional information
?
-
the JNK pathway is conserved and it is involved in controlling cell morphogenesis in Drosophila
-
-
?
additional information
?
-
during Drosophila embryogenesis, ectodermal cells of the lateral epithelium stretch in a coordinated fashion to internalize the amnioserosa cells and close the embryo dorsally. This process, dorsal closure, requires two signaling pathways: the Drosophila Jun-amino-terminal kinase pathway and the Dpp pathway
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
enzyme is part of mitogen-activated protein kinase pathways, crosstalk and regulation mechanism, overview
-
-
?
additional information
?
-
-
poor activity on free amino acids, consensus sequence of ERK2 is P-XS/TP, substrate specificity and recognition elements, e.g. PXTP, the activity on the protein substrate is much higher compared to a 14-residue peptide containing the phosphorylation site
-
-
?
additional information
?
-
-
Gpmk1 MAP kinase regulates the induction of secreted lipolytic enzymes
-
-
?
additional information
?
-
-
Gpmk1 MAP kinase regulates the induction of secreted lipolytic enzymes
-
-
?
additional information
?
-
-
ceramide activation of mitochondrial p38 mitogen-activated protein kinase is a potential mechanism for loss of mitochondrial transmembrane potential and apoptosis
-
-
?
additional information
?
-
-
p38 MAPK, ERK1, and ERK2 are involved in regulation of connective tissue growth factor, CTGF, in chondrocyte maturation and function, particularly in the hypertrophic zone, as part of the retinoid and BMP signaling pathways, overview, p38 MAPK stimulates CTGF expression, while ERK1 and ERK2 supress it
-
-
?
additional information
?
-
no phosphorylation of the activation domain of c-Jun
-
-
?
additional information
?
-
no phosphorylation of the activation domain of c-Jun
-
-
?
additional information
?
-
-
no phosphorylation of the activation domain of c-Jun
-
-
?
additional information
?
-
no phosphorylation of MAPK-activated protein kinase-2 and -3
-
-
?
additional information
?
-
-
no phosphorylation of MAPK-activated protein kinase-2 and -3
-
-
?
additional information
?
-
enzyme is implicated in signal transduction pathways
-
-
?
additional information
?
-
enzyme is implicated in signal transduction pathways
-
-
?
additional information
?
-
-
enzyme is implicated in signal transduction pathways
-
-
?
additional information
?
-
BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes
-
-
?
additional information
?
-
-
BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes
-
-
?
additional information
?
-
the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
-
-
?
additional information
?
-
JNK1 is a component of a novel signal transduction pathway that is activated by oncoproteins and UV irradiation, JNK1 activation may play an important role in tumor promotion
-
-
?
additional information
?
-
enzyme is involved in the signal transduction pathway initiated by proinflammatory cytokines and UV radiation
-
-
?
additional information
?
-
p493F12 gene maps to the human chromosome 21q21 region, a region that may be important in the pathogenesis of AD and Down's syndrome
-
-
?
additional information
?
-
-
p493F12 gene maps to the human chromosome 21q21 region, a region that may be important in the pathogenesis of AD and Down's syndrome
-
-
?
additional information
?
-
enzyme is activated by cellular stresses and plays an important role in regulating gene expression
-
-
?
additional information
?
-
-
enzyme is activated by cellular stresses and plays an important role in regulating gene expression
-
-
?
additional information
?
-
-
signaling pathway, including ERK, regulation, overview
-
-
?
additional information
?
-
-
the enzyme is part of a signalling cascade resulting in an increase in Ca2+-fluxes, activation of NF-kappaB, and expression of interleukin-8, the cascade is stimulated by pathogens, e.g. Pseudomonas aeruginosa PAO1 and Staphylococcus aureus RN6390, binding to asialo-glycolipid receptors, e.g. the asialoGM1 receptor, in epithelial membranes, no activation occurs with the pil mutant of Pseudomonas aeruginosa and the agr mutant of Staphylococcus aureus RN6911, Ca2+-dependent signaling, overview
-
-
?
additional information
?
-
interaction motifs of substrates are crucial for MAPK activity, motif Leu-Xaa-Leu preceded by 3-5 basic residues is abundant, docking mechanism in MAPK signalling, the recognition modules can function synergistically or competitively, MAPK determinants recognizing docking motifs, overview
-
-
?
additional information
?
-
-
MAPKs play a pivotal role in signal transduction
-
-
?
additional information
?
-
-
MAPKs, e.g. p38, play a key role in the transductin of biological signals from cell surface receptors, through the cytoplasm, to the transcriptional machinery in the nucleus
-
-
?
additional information
?
-
-
p38 isozymes are involved in multiple cellular functions such as cell proliferation, cell differentiation, apoptosis, and inflammation response, p38 expression and activity in signaling in erythroid cells is independent of erythropoietin
-
-
?
additional information
?
-
-
p38 MAP kinase mediates the activation of neutrophils and repression of TNF-alpha-induced apoptosis in response to inhibition by plasma opsonized crystals of calcium diphosphate dihydrate, p38 MAP kinase is involved in apoptosis of neutrophils, regulation overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, aas well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
the p38 MAPKalpha is involved in cell signal transduction and mediates responses to cell stresses and to growth factors
-
-
?
additional information
?
-
-
arsenic trioxide induces apoptosis and mitogen-activated protein kinases in promyelocytes and cancer cells. It enhances adhesion, migration, phagocytosis, release, and activity of gelatinase and degranulation of secretory, specific, and gelatinase, but not azurophilic granules, and is dependent upon activation of p38 and/or JNK. Activation of p38 and JNK is not associated with the ability of arsenic trioxide to induce human neutrophil apoptosis, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
JNK2 shows conformational flexibility in the MAP kinase insert and its involvement in the regulation of catalytic activity, the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners, overview
-
-
?
additional information
?
-
-
JNK2 shows conformational flexibility in the MAP kinase insert and its involvement in the regulation of catalytic activity, the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners, overview
-
-
?
additional information
?
-
-
p38 MAP kinase inhibitor SB203580 decreases TNF-alpha-mediated DNA binding activity of NF-?B, which is is involved in p38MAP kinase-mediated control of the MMP-9 gene in 5637 cells, overview
-
-
?
additional information
?
-
p38 MAPK is a central signaling molecule in many proinflammatory pathways, regulating the cellular response to a multitude of external stimuli including heat, ultraviolet radiation, osmotic shock, and a variety of cytokines especially interleukin-1beta and tumor necrosis factor alpha
-
-
?
additional information
?
-
-
p38 MAPK is a central signaling molecule in many proinflammatory pathways, regulating the cellular response to a multitude of external stimuli including heat, ultraviolet radiation, osmotic shock, and a variety of cytokines especially interleukin-1beta and tumor necrosis factor alpha
-
-
?
additional information
?
-
The mitogen-activated protein kinase p38 is a key regulator in the signaling pathways controlling the production of pro-inflammatory cytokines such as TNF-alpha and IL-1beta
-
-
?
additional information
?
-
-
The mitogen-activated protein kinase p38 is a key regulator in the signaling pathways controlling the production of pro-inflammatory cytokines such as TNF-alpha and IL-1beta
-
-
?
additional information
?
-
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The short hydrophobic region at the distal end of the D-site plays a critical role in determining the high selectivity of JNK MAPKs for docking sites in their cognate MAPK kinases. These specificity-determining differences are also found in the D-sites of the ETS family transcription factors Elk-1 and Net. Swapping two hydrophobic residues between these D-sites switches the relative efficiency of Elk-1 and Net as substrates for ERK versus JNK. Comparison of the hydrophobic submotif in strong versus weak JNK-binding D-sites, overview. The D-sites of the JNK pathway activator MKK4 contains LXL, as do all three of the D-sites in activator MKK7 in the first 3 residues of the hydrophobic submotif. MKK D-sites that bind JNK weakly lack an extended hydrophobic motif
-
-
?
additional information
?
-
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The short hydrophobic region at the distal end of the D-site plays a critical role in determining the high selectivity of JNK MAPKs for docking sites in their cognate MAPK kinases. These specificity-determining differences are also found in the D-sites of the ETS family transcription factors Elk-1 and Net. Swapping two hydrophobic residues between these D-sites switches the relative efficiency of Elk-1 and Net as substrates for ERK versus JNK. Comparison of the hydrophobic submotif in strong versus weak JNK-binding D-sites, overview. The D-sites of the JNK pathway activator MKK4 contains LXL, as do all three of the D-sites in activator MKK7 in the first 3 residues of the hydrophobic submotif. MKK D-sites that bind JNK weakly lack an extended hydrophobic motif
-
-
?
additional information
?
-
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The short hydrophobic region at the distal end of the D-site plays a critical role in determining the high selectivity of JNK MAPKs for docking sites in their cognate MAPK kinases. These specificity-determining differences are also found in the D-sites of the ETS family transcription factors Elk-1 and Net. Swapping two hydrophobic residues between these D-sites switches the relative efficiency of Elk-1 and Net as substrates for ERK versus JNK. Comparison of the hydrophobic submotif in strong versus weak JNK-binding D-sites, overview. The D-sites of the JNK pathway activator MKK4 contains LXL, as do all three of the D-sites in activator MKK7 in the first 3 residues of the hydrophobic submotif. MKK D-sites that bind JNK weakly lack an extended hydrophobic motif
-
-
?
additional information
?
-
p38beta can autophosphorylate and thus autoactivate itself, the C tail of p38beta inhibits autophosphorylation
-
-
?
additional information
?
-
p38beta can autophosphorylate and thus autoactivate itself, the C tail of p38beta inhibits autophosphorylation
-
-
?
additional information
?
-
-
the enzyme depends on basic residues for substrate recognition, autoregulation by a pseudosubstrate mechanism, overview
-
-
?
additional information
?
-
-
MAPK pathways overview, interaction of MAPKs and transcription factors, overview, the MAPKs act as structural adaptors and enzymatic activators in transcription complexes, e.g. ERK1 and ERK2 interact with AP1-complex, which is regulated via the all-trans retinoic acid receptor and TPA, overview
-
-
?
additional information
?
-
-
transcription factor protein domains consisting of the LXL motif, the FXFP motif, the LXLXXXF motif, or the ETS motif, are involved in stable interaction of MAPKs with transcription complexes
-
-
?
additional information
?
-
kinase activation may play a role in the mitogenic induction of symbiotic root nodules on alfalfa by Rhizobium signal molecules
-
-
?
additional information
?
-
-
kinase activation may play a role in the mitogenic induction of symbiotic root nodules on alfalfa by Rhizobium signal molecules
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
Jnk3-mediated signalling pathway is an important component in the pathogenesis of glutamate neurotoxicity
-
-
?
additional information
?
-
MKK4 is a JNK activator in vivo and an essential component of the JNK signal transduction pathway
-
-
?
additional information
?
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
ERK, but not p38 and JNK, is involved in TGF-beta production in macrophages, the phosphatidylserine-receptor is involved in the ERK signaling pathway, overview
-
-
?
additional information
?
-
-
regulation mechanism of p38 MAPK activity involving the protein kinases MKK3, MKK4, and MKK6, overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
measurement of ATPase activity of p38 MAPK in an NADH-coupled assay
-
-
?
additional information
?
-
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
-
-
?
additional information
?
-
-
MAP kinases are essential signaling molecules that mediate many cellular effects of growth factors, cytokines, and stress stimuli
-
-
?
additional information
?
-
-
MAPKs are involved in the upstream regulation of inducible nitric oxide synthase, iNOS
-
-
?
additional information
?
-
-
p38 MAPK is induced in response to environmental stress, it is implicated in diverse cellular processes, including cell proliferation, differentiation, and survival of differentiated cells in the central nervous system, expression profile and roles of p38 MAPK in the developing brain, overview. Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
MAPK cascades play a key role in plant growth and development as well as in biotic and abiotic stress responses
-
-
?
additional information
?
-
-
MAPK cascades play a key role in plant growth and development as well as in biotic and abiotic stress responses
-
-
?
additional information
?
-
PMK1 is part of a highly conserved MAP kinase signal transduction pathway that acts cooperatively with a cAMP signaling pathway for fungal pathogenesis
-
-
?
additional information
?
-
-
PMK1 is part of a highly conserved MAP kinase signal transduction pathway that acts cooperatively with a cAMP signaling pathway for fungal pathogenesis
-
-
?
additional information
?
-
p38-delta is activated by environmental stress, extracellular stimulants, and MAPK kinase-3, -4, -6, and -7, suggesting that p38-delta is a unique stress-responsive protein kinase
-
-
?
additional information
?
-
the enzyme is involved in regulating the response of eukaryotic cells to extracellular signals
-
-
?
additional information
?
-
the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
-
-
?
additional information
?
-
-
p38 MAPK, but not ERKs or JNKs, regulates the serotonin transporter, SERT, and subsequent signaling induced by 5-hydroxytryptamine, overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, aas well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
tert-butyl hydroperoxide activation of MAPK might be involved in vascular dysfunction in oxidative stress responses and the vascular inflammatory process
-
-
?
additional information
?
-
-
MAPK phosphorylation consensus sequences
-
-
?
additional information
?
-
MAPK phosphorylation consensus sequences
-
-
?
additional information
?
-
-
stoichiometry of phosphorylation of wild-type and mutant tyrosine hydroxylase substrates by ERK2
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
enzyme is required for the transition from mitosis into conjugation
-
-
?
additional information
?
-
enzyme is required for restoring the osmotic gradient across the cell membrane
-
-
?
additional information
?
-
-
enzyme is required for restoring the osmotic gradient across the cell membrane
-
-
?
additional information
?
-
enzyme is involved in polarized cell growth
-
-
?
additional information
?
-
-
enzyme is involved in polarized cell growth
-
-
?
additional information
?
-
enzyme is required for spore wall assembly
-
-
?
additional information
?
-
-
enzyme is required for spore wall assembly
-
-
?
additional information
?
-
signal transduction in Saccharomyces cerevisiae requires Tyr and Thr phosphorylation of FUS3 and KSS1
-
-
?
additional information
?
-
signal transduction in Saccharomyces cerevisiae requires Tyr and Thr phosphorylation of FUS3 and KSS1
-
-
?
additional information
?
-
DAC2/FUS3 protein kinase is not essential for transcriptional activation of the mating pheromone response pathway
-
-
?
additional information
?
-
enzyme is involved in growth control pathway
-
-
?
additional information
?
-
-
Hog1 is related to osmotic stress
-
-
?
additional information
?
-
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
-
Fus3, Kss1, and Hog1 function during the mating pheromone response, the switch of filamentous growth, and the response to high osmolarity, respectively, detailed pathway overview, MAPK signaling pathways and specificity, pathway sequestering mechanism modeling, separation via subcellular compartmentalization, temporal separation, scaffolding, combinatorial signaling, detailed overview
-
-
?
additional information
?
-
-
MAPK pathways overview, the MAPKs act as structural adaptors and enzymatic activators in transcription complexes, e.g. Hog1p, Hot1p, and Sko1p, overview
-
-
?
additional information
?
-
-
transcription factor protein domains consisting of the LXL motif, the FXFP motif, the LXLXXXF motif, or the ETS motif, are involved in stable interaction of MAPKs with transcription complexes
-
-
?
additional information
?
-
-
kinase activity of Hog1 is required to promote its own dephosphorylation after hyperosmotic-stress-induced activation, moreover, catalytic activity of Hog1 is required continuously to prevent cross talk between the the high-osmolarity glycerol pathway and both the pheromone response and invasive growth pathways
-
-
?
additional information
?
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
enzyme plays a pivotal role in a variety of signal transduction pathways
-
-
?
additional information
?
-
-
enzyme plays a pivotal role in a variety of signal transduction pathways
-
-
?
additional information
?
-
enzyme functions as a part of the fission yeast growth control pathway
-
-
?
additional information
?
-
the enzyme regulates cell integrity and functions coordinately with the protein kinase C pathway
-
-
?
additional information
?
-
-
the enzyme regulates cell integrity and functions coordinately with the protein kinase C pathway
-
-
?
additional information
?
-
stress-activated MAP kinase regulates morphogenesis in Schizosaccharomyces pombe
-
-
?
additional information
?
-
-
stress-activated MAP kinase regulates morphogenesis in Schizosaccharomyces pombe
-
-
?
additional information
?
-
conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast
-
-
?
additional information
?
-
-
conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast
-
-
?
additional information
?
-
acts downstream of the Wis1 MAP kinase kinase to control cell size at division in fission yeast
-
-
?
additional information
?
-
-
acts downstream of the Wis1 MAP kinase kinase to control cell size at division in fission yeast
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
a peptide docking sequence derived from either a downstream substrate or an upstream activator is appended to an ERK substrate peptide to yield a high-efficiency substrate for ERK without loss of specificity
-
-
?
additional information
?
-
the enzyme is involved in biocontrol properties and repression of conidiation of the fungal hosts in the dark, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in biocontrol properties and repression of conidiation of the fungal hosts in the dark, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
-
-
?
additional information
?
-
-
spatiotemporal control of the Ras/ERK MAP kinase signaling pathway, involving multiple factors, is a key factor for determining the specificity of cellular responses including cell proliferation, cell differentiation, and cell survival, the fidelity of the signaling is regulated by docking interactions and by scaffolding, molecular mechanism of negative regulation of Ras/ERK signaling
-
-
?
additional information
?
-
MAP kinase functions as an intermediate between MPF and the interphase-M phase transition of microtubule organization
-
-
?
additional information
?
-
RKK, RK, and MAPKAP kinase-2 constitute a new stress-activated signal transduction pathway in vertebrates that is distinct from the classical MAPK cascade
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + a protein
ADP + a phosphoprotein
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2
-
-
?
ATP + AP1
ADP + phosphorylated AP1
-
substrate of ERK1/2, ERK access to the substrate is regulated by the all-trans retinoic acid receptor, RAR
-
-
?
ATP + Arabidopsis thaliana protein AT1G7815
ADP + phosphorylated Arabidopsis thaliana proteins AT1G78150
-
-
-
?
ATP + Arabidopsis thaliana protein AT2G26530
ADP + phosphorylated Arabidopsis thaliana proteins AT2G26530
-
-
-
?
ATP + Arabidopsis thaliana protein AT3G11330
ADP + phosphorylated Arabidopsis thaliana proteins AT3G11330
-
-
-
?
ATP + Arabidopsis thaliana protein AT4G38710
ADP + phosphorylated Arabidopsis thaliana proteins AT4G38710
-
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
-
-
-
?
ATP + BES1
ADP + phosphorylated BES1
ATP + c-Jun
ADP + phosphorylated c-Jun
ATP + DNA polymerase II
ADP + phosphorylated DNA polymerase II
-
substrate of Hog1p
-
-
?
ATP + EB1c
ADP + phosphorylated EB1c
the microtubule plus end protein
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
ATP + Elk1
ADP + phosphorylated Elk1
ATP + GLH-1
ADP + phosphorylated GLH-1
-
-
-
?
ATP + Hot1p
ADP + phosphorylated Hot1p
-
substrate of Hog1p, phosphorylation of Hot1p is not required for Hot1p-mediated gene expression
-
-
?
ATP + human glucocorticoid receptor
ADP + phosphorylated human glucocorticoid receptor
-
specific phosphorylation at Ser211 by p38 MAPK, p38 MAPK is a mediator in glucocorticoid-induced apoptosis of lymphoid cells, interaction of MAPK and glucocorticoid pathways, overview
-
-
?
ATP + Lin-1
ADP + phosphorylated Lin-1
substrate of ERK2, negative regulation of Lin-1
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
-
-
-
-
?
ATP + MAPKAPK2
ADP + phosphorylated MAPKAPK2
-
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
-
-
-
-
?
ATP + MKS1
ADP + phosphorylated MSK1
-
MPK4 acts as a regulator of pathogen defense responses and is required for repression of salicylic acid-dependent resistance and for activation of jasmonate-dependent defense gene expression via MSK1, which interacts with the transcription factors WRKY25 and WRKY33
-
-
?
ATP + MMP-9
ADP + phosphorylated MMP-9
-
activity of p38 MAP kinase, TNF-alpha stimulates MMP-9 expression via the p38 MAP kinase signaling pathway in 5637 cells, and p38 MAP kinase-mediated MMP-9 gene regulation in response to TNF-alpha is involved in the NF-kappaB response element in 5637 cells, regulation, overview
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
ATP + MYB32
ADP + phosphorylated MYB32
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
-
-
?
ATP + Net
ADP + phosphorylated Net
ATP + nodulation outer protein L
ADP + a phosphorylated nodulation outer protein L
nodulation outer protein L variants with six or eight serine to alanine substitutions are partially active, whereas nodulation outer protein L forms with 10 or 12 substituted serine residues are inactive
-
-
?
ATP + phospholipase C-gamma1
ADP + phosphorylated phospholipase C-gamma1
the reaction is performed by activated phosphorylated ERK2, phosphorylation inhibits phospholipase C-gamma1
-
-
?
ATP + Smad1
ADP + phosphorylated Smad1
-
the MAP kinase antagonizes Smad1 in signaling during development of axis and neural specification, Smad1 is involved in dorsal-ventral patterning in embryos
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2
-
-
?
ATP + SPRH1
ADP + phosphorylated SPRH1
-
phosphorylation at Ser-49, Ser-52 and Ser-94
-
-
?
ATP + Ste50
ADP + phosphorylated Ste50
ATP + TBP
ADP + phosphorylated TBP
-
substrate of p38 MAPK
-
-
?
ATP + tyrosine hydroxylase
ADP + phosphorylated tyrosine hydroxylase
-
phosphorylation of tyrosine hydroxylase at Ser8 and Ser31 by ERK1 and ERK2 is involved in regulation of catecholamine biosynthesis
-
-
?
ATP + WRKY1
ADP + phosphorylated WRKY1
-
-
-
?
ATPgammaS + myelin basic protein
ADP + thiophosphorylated myelin basic protein
Arabidopsis thaliana MPKs use ATPgammaS to thiophosphorylate myelin basic protein
-
-
?
N6-benzyl-ATPgammaS + myelin basic protein
ADP + benzylthiophosphorylated myelin basic protein
Arabidopsis thaliana MPK3 mutant T119A uses N6-benzyl-ATPgammaS to thiophosphorylate myelin basic protein
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
702641, 702692, 702942, 703019, 703255, 703573, 704471, 705276, 705321, 705447, 706080, 706863 -
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
MAPK activate mitogen-activated proteins in several signal transduction pathways, overview
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor. S286 and S137 residues are required for flg22-induced BES1 full phosphorylation in vivo, in which S286 plays a greater role than S137
-
-
?
ATP + BES1
ADP + phosphorylated BES1
i.e. brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, an Arabidospis thaliana transcription factor. S286 and S137 residues are required for flg22-induced BES1 full phosphorylation in vivo, in which S286 plays a greater role than S137
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
substrate of JNK
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
the reaction is performed by activated phosphorylated ERK2
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
the reaction is performed by activated phosphorylated JNK3
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
CAD initiates and regulates de novo pyrimidine biosynthesis and is activated by phosphorylation at Thr456 by nuclear MAPKs, nuclear import of CAD is required for optimal cell growth
-
-
?
ATP + multifunctional protein CAD
ADP + phosphorylated multifunctional protein CAD
-
CAD initiates and regulates de novo pyrimidine biosynthesis and is activated by phosphorylation at Thr456 by nuclear MAPKs, nuclear import of CAD is required for optimal cell growth
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
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?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
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ATP + Ste50
ADP + phosphorylated Ste50
Hog1 phosphorylates Ste50 in response to osmotic stress, and phosphorylation of Ste50 limits the duration of Kss1 activation and prevents invasive growth under high osmolarity growth conditions. The feedback phosphorylation event leads to more transient activation of Hog1, regulation, overview
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ATP + Ste50
ADP + phosphorylated Ste50
Hog1 phosphorylates Ste50 in response to osmotic stress, and phosphorylation of Ste50 limits the duration of Kss1 activation and prevents invasive growth under high osmolarity growth conditions. The feedback phosphorylation event leads to more transient activation of Kss1, regulation, overview
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additional information
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FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
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additional information
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FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
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?
additional information
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FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
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?
additional information
?
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FLAG-tagged Arabidopsis thaliana proteins AT1G78150, AT2G26530, AT3G11330, and AT4G38710 are good MPK3/6 substrates, but are poor substrates for the closely related Arabidopsis thaliana MPK4
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?
additional information
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MPK6 interacts with gamma-tubulin and co-sediments with plant microtubules polymerized in vitro. The active form of MAP kinase is enriched with microtubules and follows similar dynamics to gamma-tubulin, moving from poles to midzone during the anaphase-to-telophase transition
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additional information
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MPK6 interacts with gamma-tubulin and co-sediments with plant microtubules polymerized in vitro. The active form of MAP kinase is enriched with microtubules and follows similar dynamics to gamma-tubulin, moving from poles to midzone during the anaphase-to-telophase transition
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additional information
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enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
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?
additional information
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enzyme is activated in response to a variety of cellular stresses and is involved in apoptosis in neurons
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additional information
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UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
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?
additional information
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UNC-16 may regulate the localization of vesicular cargo by integrating JNK signaling and kinesin-1 transport
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?
additional information
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promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
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additional information
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promoting influence of JNK-1 on both nuclear DAF-16 translocations and DAF-16 target gene sod-3, encoding superoxide dismutase 3, expressions within peripheral, non-neuronal tissue, JNK-1 modulates the intestinal stress-induced translocation of DAF-16 from the cytosol into the cell nucleus. JNK-1 is controlled by the MAPK JKK-1 under heat stress
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additional information
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the mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
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additional information
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the mitogen-activated protein kinase homolog HOG1 gene controls glycerol accumulation in the pathogenic fungus Candida albicans
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additional information
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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?
additional information
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enzyme plays an important role in egg maturation or ectogenetic early development
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?
additional information
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enzyme plays an important role in egg maturation or ectogenetic early development
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additional information
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enzyme plays an important role in egg maturation or ectogenetic early development
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additional information
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possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
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?
additional information
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possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
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?
additional information
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possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
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additional information
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possible role of asymmetric p38 activation in zebrafish in symmetric and synchronous cleavage
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additional information
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spatiotemporal control of the Ras/ERK MAP kinase signaling pathway, involving multiple factors, is a key factor for determining the specificity of cellular responses including cell proliferation, cell differentiation, and cell survival, the fidelity of the signaling is regulated by docking interactions and by scaffolding, molecular mechanism of negative regulation of Ras/ERK signaling
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additional information
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ERK1 plays an essential role during the growth and differentiation
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additional information
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ERK1 plays an essential role during the growth and differentiation
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additional information
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JUN N-terminal kinase signaling is required to initiate the cell shape change at the onset of the epithelial wound healing. The embryonic JUN N-terminal kinase gene cassette is induced at the edge of the wound
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additional information
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functions of D-p38 is to attenuate antimicrobial peptide gene expression following exposure to lipopolysaccharide
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?
additional information
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functions of D-p38 is to attenuate antimicrobial peptide gene expression following exposure to lipopolysaccharide
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?
additional information
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DJNK signal transduction pathway mediates an immune response and morphogenesis
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additional information
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dorsal closure, a morphogenetic movement during Drosophila embryogenesis, is controlled by the Drosophila JNK pathway, D-Fos and the phosphatase Puckered
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additional information
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MAP kinase, ERK-A is required downstream of raf in the Sev signal transduction pathway
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additional information
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MAP kinase, ERK-A is required downstream of raf in the Sev signal transduction pathway
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additional information
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enzyme may function to modulate Dpp signaling
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additional information
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enzyme may function to modulate Dpp signaling
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additional information
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the JNK pathway is conserved and it is involved in controlling cell morphogenesis in Drosophila
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additional information
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during Drosophila embryogenesis, ectodermal cells of the lateral epithelium stretch in a coordinated fashion to internalize the amnioserosa cells and close the embryo dorsally. This process, dorsal closure, requires two signaling pathways: the Drosophila Jun-amino-terminal kinase pathway and the Dpp pathway
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additional information
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enzyme is part of mitogen-activated protein kinase pathways, crosstalk and regulation mechanism, overview
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additional information
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Gpmk1 MAP kinase regulates the induction of secreted lipolytic enzymes
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additional information
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Gpmk1 MAP kinase regulates the induction of secreted lipolytic enzymes
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additional information
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ceramide activation of mitochondrial p38 mitogen-activated protein kinase is a potential mechanism for loss of mitochondrial transmembrane potential and apoptosis
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additional information
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p38 MAPK, ERK1, and ERK2 are involved in regulation of connective tissue growth factor, CTGF, in chondrocyte maturation and function, particularly in the hypertrophic zone, as part of the retinoid and BMP signaling pathways, overview, p38 MAPK stimulates CTGF expression, while ERK1 and ERK2 supress it
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additional information
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enzyme is implicated in signal transduction pathways
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additional information
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enzyme is implicated in signal transduction pathways
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additional information
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enzyme is implicated in signal transduction pathways
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additional information
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BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes
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additional information
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BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes
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additional information
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the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
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?
additional information
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the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
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additional information
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JNK1 is a component of a novel signal transduction pathway that is activated by oncoproteins and UV irradiation, JNK1 activation may play an important role in tumor promotion
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additional information
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enzyme is involved in the signal transduction pathway initiated by proinflammatory cytokines and UV radiation
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additional information
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p493F12 gene maps to the human chromosome 21q21 region, a region that may be important in the pathogenesis of AD and Down's syndrome
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?
additional information
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p493F12 gene maps to the human chromosome 21q21 region, a region that may be important in the pathogenesis of AD and Down's syndrome
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additional information
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enzyme is activated by cellular stresses and plays an important role in regulating gene expression
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additional information
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enzyme is activated by cellular stresses and plays an important role in regulating gene expression
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additional information
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signaling pathway, including ERK, regulation, overview
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additional information
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the enzyme is part of a signalling cascade resulting in an increase in Ca2+-fluxes, activation of NF-kappaB, and expression of interleukin-8, the cascade is stimulated by pathogens, e.g. Pseudomonas aeruginosa PAO1 and Staphylococcus aureus RN6390, binding to asialo-glycolipid receptors, e.g. the asialoGM1 receptor, in epithelial membranes, no activation occurs with the pil mutant of Pseudomonas aeruginosa and the agr mutant of Staphylococcus aureus RN6911, Ca2+-dependent signaling, overview
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?
additional information
?
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MAPKs play a pivotal role in signal transduction
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additional information
?
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MAPKs, e.g. p38, play a key role in the transductin of biological signals from cell surface receptors, through the cytoplasm, to the transcriptional machinery in the nucleus
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additional information
?
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p38 isozymes are involved in multiple cellular functions such as cell proliferation, cell differentiation, apoptosis, and inflammation response, p38 expression and activity in signaling in erythroid cells is independent of erythropoietin
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?
additional information
?
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p38 MAP kinase mediates the activation of neutrophils and repression of TNF-alpha-induced apoptosis in response to inhibition by plasma opsonized crystals of calcium diphosphate dihydrate, p38 MAP kinase is involved in apoptosis of neutrophils, regulation overview
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?
additional information
?
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, aas well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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?
additional information
?
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the p38 MAPKalpha is involved in cell signal transduction and mediates responses to cell stresses and to growth factors
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additional information
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arsenic trioxide induces apoptosis and mitogen-activated protein kinases in promyelocytes and cancer cells. It enhances adhesion, migration, phagocytosis, release, and activity of gelatinase and degranulation of secretory, specific, and gelatinase, but not azurophilic granules, and is dependent upon activation of p38 and/or JNK. Activation of p38 and JNK is not associated with the ability of arsenic trioxide to induce human neutrophil apoptosis, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
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?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
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?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
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?
additional information
?
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JNK2 shows conformational flexibility in the MAP kinase insert and its involvement in the regulation of catalytic activity, the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners, overview
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additional information
?
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JNK2 shows conformational flexibility in the MAP kinase insert and its involvement in the regulation of catalytic activity, the MAP kinase insert of JNK2 plays a role in the regulation of JNK2 activation, possibly by interacting with intracellular binding partners, overview
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?
additional information
?
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p38 MAP kinase inhibitor SB203580 decreases TNF-alpha-mediated DNA binding activity of NF-?B, which is is involved in p38MAP kinase-mediated control of the MMP-9 gene in 5637 cells, overview
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?
additional information
?
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p38 MAPK is a central signaling molecule in many proinflammatory pathways, regulating the cellular response to a multitude of external stimuli including heat, ultraviolet radiation, osmotic shock, and a variety of cytokines especially interleukin-1beta and tumor necrosis factor alpha
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additional information
?
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p38 MAPK is a central signaling molecule in many proinflammatory pathways, regulating the cellular response to a multitude of external stimuli including heat, ultraviolet radiation, osmotic shock, and a variety of cytokines especially interleukin-1beta and tumor necrosis factor alpha
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additional information
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The mitogen-activated protein kinase p38 is a key regulator in the signaling pathways controlling the production of pro-inflammatory cytokines such as TNF-alpha and IL-1beta
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additional information
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The mitogen-activated protein kinase p38 is a key regulator in the signaling pathways controlling the production of pro-inflammatory cytokines such as TNF-alpha and IL-1beta
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?
additional information
?
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MAPK pathways overview, interaction of MAPKs and transcription factors, overview, the MAPKs act as structural adaptors and enzymatic activators in transcription complexes, e.g. ERK1 and ERK2 interact with AP1-complex, which is regulated via the all-trans retinoic acid receptor and TPA, overview
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additional information
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kinase activation may play a role in the mitogenic induction of symbiotic root nodules on alfalfa by Rhizobium signal molecules
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additional information
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kinase activation may play a role in the mitogenic induction of symbiotic root nodules on alfalfa by Rhizobium signal molecules
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additional information
?
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additional information
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additional information
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additional information
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additional information
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Jnk3-mediated signalling pathway is an important component in the pathogenesis of glutamate neurotoxicity
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additional information
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MKK4 is a JNK activator in vivo and an essential component of the JNK signal transduction pathway
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additional information
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JNK is necessary for T-cell differentiation but not for naive T-cell activation
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additional information
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JNK is necessary for T-cell differentiation but not for naive T-cell activation
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additional information
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the enzyme functions as a Scaffold factor in the JNK signaling pathway
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additional information
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the enzyme functions as a Scaffold factor in the JNK signaling pathway
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additional information
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the enzyme functions as a Scaffold factor in the JNK signaling pathway
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additional information
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the enzyme functions as a Scaffold factor in the JNK signaling pathway
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additional information
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ERK, but not p38 and JNK, is involved in TGF-beta production in macrophages, the phosphatidylserine-receptor is involved in the ERK signaling pathway, overview
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?
additional information
?
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regulation mechanism of p38 MAPK activity involving the protein kinases MKK3, MKK4, and MKK6, overview
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?
additional information
?
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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?
additional information
?
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activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
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?
additional information
?
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activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
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?
additional information
?
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activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
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?
additional information
?
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activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
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?
additional information
?
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MAP kinases are essential signaling molecules that mediate many cellular effects of growth factors, cytokines, and stress stimuli
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?
additional information
?
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MAPKs are involved in the upstream regulation of inducible nitric oxide synthase, iNOS
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?
additional information
?
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p38 MAPK is induced in response to environmental stress, it is implicated in diverse cellular processes, including cell proliferation, differentiation, and survival of differentiated cells in the central nervous system, expression profile and roles of p38 MAPK in the developing brain, overview. Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells, overview
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additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
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?
additional information
?
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trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
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?
additional information
?
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activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
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?
additional information
?
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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?
additional information
?
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MAPK cascades play a key role in plant growth and development as well as in biotic and abiotic stress responses
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?
additional information
?
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MAPK cascades play a key role in plant growth and development as well as in biotic and abiotic stress responses
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additional information
?
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PMK1 is part of a highly conserved MAP kinase signal transduction pathway that acts cooperatively with a cAMP signaling pathway for fungal pathogenesis
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additional information
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PMK1 is part of a highly conserved MAP kinase signal transduction pathway that acts cooperatively with a cAMP signaling pathway for fungal pathogenesis
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?
additional information
?
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p38-delta is activated by environmental stress, extracellular stimulants, and MAPK kinase-3, -4, -6, and -7, suggesting that p38-delta is a unique stress-responsive protein kinase
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additional information
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the enzyme is involved in regulating the response of eukaryotic cells to extracellular signals
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additional information
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the enzyme plays a crucial role in stress and inflammatory responses and is also involved in activation of the human immunodeficiency virus gene expression
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?
additional information
?
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p38 MAPK, but not ERKs or JNKs, regulates the serotonin transporter, SERT, and subsequent signaling induced by 5-hydroxytryptamine, overview
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?
additional information
?
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, aas well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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?
additional information
?
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tert-butyl hydroperoxide activation of MAPK might be involved in vascular dysfunction in oxidative stress responses and the vascular inflammatory process
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?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk1, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk1 pathway, mechanism, overview
-
-
?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
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-
?
additional information
?
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cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of Erk2, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of Erk2 pathway, mechanism, overview
-
-
?
additional information
?
-
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
-
-
?
additional information
?
-
cadmium induces neuronal apoptosis in part through activation of JNK, Cd-induced reactive oxygen species inhibit serine/threonine protein phosphatases 2A and 5, PP2A andPP5, leading to activation of JNK pathway, mechanism, overview
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?
additional information
?
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enzyme is required for the transition from mitosis into conjugation
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?
additional information
?
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enzyme is required for restoring the osmotic gradient across the cell membrane
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?
additional information
?
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enzyme is required for restoring the osmotic gradient across the cell membrane
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?
additional information
?
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enzyme is involved in polarized cell growth
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?
additional information
?
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enzyme is involved in polarized cell growth
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additional information
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enzyme is required for spore wall assembly
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?
additional information
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enzyme is required for spore wall assembly
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additional information
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signal transduction in Saccharomyces cerevisiae requires Tyr and Thr phosphorylation of FUS3 and KSS1
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additional information
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signal transduction in Saccharomyces cerevisiae requires Tyr and Thr phosphorylation of FUS3 and KSS1
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additional information
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DAC2/FUS3 protein kinase is not essential for transcriptional activation of the mating pheromone response pathway
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additional information
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enzyme is involved in growth control pathway
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additional information
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Hog1 is related to osmotic stress
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additional information
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Fus3, Kss1, and Hog1 function during the mating pheromone response, the switch of filamentous growth, and the response to high osmolarity, respectively, detailed pathway overview, MAPK signaling pathways and specificity, pathway sequestering mechanism modeling, separation via subcellular compartmentalization, temporal separation, scaffolding, combinatorial signaling, detailed overview
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additional information
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MAPK pathways overview, the MAPKs act as structural adaptors and enzymatic activators in transcription complexes, e.g. Hog1p, Hot1p, and Sko1p, overview
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additional information
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the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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-
?
additional information
?
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the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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-
?
additional information
?
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-
the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Hog1 activity is transient and promotes cell adaptation to osmotic stress, Ste50 is a target for feedback regulation of the two pathways, overview. Hog1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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additional information
?
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the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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?
additional information
?
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the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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?
additional information
?
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the adaptor protein Ste50 functions in multiple MAP kinase pathways, each with unique dynamical and developmental properties. Kss1 activity is sustained and promotes invasive growth, Ste50 is a target for feedback regulation of the two pathways, overview. Kss1 mediates gene induction, e.g. the Ty1 or TEC1 promoters, overview
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additional information
?
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additional information
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enzyme plays a pivotal role in a variety of signal transduction pathways
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additional information
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enzyme plays a pivotal role in a variety of signal transduction pathways
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additional information
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enzyme functions as a part of the fission yeast growth control pathway
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additional information
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the enzyme regulates cell integrity and functions coordinately with the protein kinase C pathway
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additional information
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the enzyme regulates cell integrity and functions coordinately with the protein kinase C pathway
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additional information
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stress-activated MAP kinase regulates morphogenesis in Schizosaccharomyces pombe
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additional information
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stress-activated MAP kinase regulates morphogenesis in Schizosaccharomyces pombe
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additional information
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conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast
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additional information
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conjugation, meiosis, and the osmotic stress response are regulated by Spc1 kinase through Atf1 transcription factor in fission yeast
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additional information
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acts downstream of the Wis1 MAP kinase kinase to control cell size at division in fission yeast
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additional information
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acts downstream of the Wis1 MAP kinase kinase to control cell size at division in fission yeast
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additional information
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signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
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additional information
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the enzyme is involved in biocontrol properties and repression of conidiation of the fungal hosts in the dark, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
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additional information
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the enzyme is involved in biocontrol properties and repression of conidiation of the fungal hosts in the dark, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
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additional information
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spatiotemporal control of the Ras/ERK MAP kinase signaling pathway, involving multiple factors, is a key factor for determining the specificity of cellular responses including cell proliferation, cell differentiation, and cell survival, the fidelity of the signaling is regulated by docking interactions and by scaffolding, molecular mechanism of negative regulation of Ras/ERK signaling
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additional information
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MAP kinase functions as an intermediate between MPF and the interphase-M phase transition of microtubule organization
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additional information
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RKK, RK, and MAPKAP kinase-2 constitute a new stress-activated signal transduction pathway in vertebrates that is distinct from the classical MAPK cascade
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(1R)-2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
-
(1R,2S)-2-[([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)methyl]cyclohexanol
-
(2R)-2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
-
(2S)-2-([6-[(2-aminobenzyl)amino]-9-(1-methylethyl)-9H-purin-2-yl]amino)butan-1-ol
-
-
(2S,3S)-2-[(R)-4-[4-(2-hydroxy-ethoxy)-phenyl]-2,5-dioxo-imidazolidin-1-yl]-3-phenyl-N-(4-propionyl-thiazol-2-yl)-butyramide
-
RO4927350
(3-amino-1-oxido-2-phenylpyridin-4-yl)(phenyl)methanone
-
(3R)-3-([4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)butanoic acid
-
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
(hydroxy-2-naphthalenylmethyl)phosphonic acid
-
inhibits the insulin receptor tyrosine kinase, IC50 is 0.01 mM
(R)-2-(sec-butylamino)-N-(2-methyl-5-(methylcarbamoyl)phenyl) thiazole-5-carboxamide
-
i.e. BMS-640994, a potent and efficacious p38alpha MAP kinase inhibitor; inhibition of p38alpha MAP kinase
(R)-N-(2-hydroxyl-1-phenylethyl)-4-[5-methyl-2-(phenylamino)-pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2,3-dimethylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-chlorophenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-ethylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-ethylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-fluorophenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-hydroxyphenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-methylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-methylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(2-trifluoromethylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-phenyl-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(3-fluoro-2-methylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(4-chloro-2-fluorophenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(4-chloro-2-methylphenylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-4-[2-(benzo[d]1,3-dioxolylamino)-5-methylpyrimidin-4-yl]-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-1H-pyrrole-2-carboxamide
-
(S)-N-(2-hydroxyl-1-phenylethyl)-4-[5-methyl-2-(phenylamino)-pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-4-[-2-(2,2-difluorobenzo[d][1,3]dioxol-4-ylamino)-5-methylpyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-4-[-2-(2,3-dihydro-1H-inden-4-ylamino)-5-methylpyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-4-[-2-(2,3-dihydrobenzo[b][1,4]dioxin-5-ylamino)-5-methylpyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-4-[5-methyl-2(5,6,7,8-tetrahydronaphthalen-1-ylamino)pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-chlorophenyl)-2-hydroxyethyl]-4-[5-methyl-2-(phenylamino)pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-fluorophenyl)-2-hydroxyethyl]-4-[5-methyl-2-(phenylamino)pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
(S)-N-[1-(3-methylphenyl)-2-hydroxyethyl]-4-[5-methyl-2-(phenylamino)pyrimidin-4-yl]-1H-pyrrole-2-carboxamide
-
1,4-diamino-2,3-dicyano-1,4-bis(o-aminophenylmercapto)butadiene
-
U0126
1-((S)-4-(6-(3-(cyclopropylamino)-6-methylbenzo[d]isoxazol-7-yl)phthalazin-1-yl)-3-methylpiperazin-1-yl)ethanone
-
1-(2,6-dichloro-phenyl)-1-(4-(4-fluorophenyl)thiazol-2-yl)urea
-
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperazin-1-yl-3,4-dihydro-1H-quinazolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 3.2 nM, the IC50 for mutants G110A and G110D are 37 nM and 56 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperidin-4-yl-3,4-dihydro-1H-quinolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 0.74 nM, the IC50 for mutants G110A and G110D are 26 nM and 67 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 4.3 nM, the IC50 for mutants G110A and G110D are 61 nM and 160 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-2-ol
-
1-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-2-ol
-
1-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
2,2'-(1,3,4-thiadiazole-2,5-diyl)bis(sulfanediyl)dithiazole-5-carboxylic acid
-
-
2,2'-disulfanediylbis(1,3-benzothiazole)
-
-
2,2'-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]imino]diethanol
-
-
2,5-bis(3-nitrobenzylthio)-1,3,4-thiadiazole
-
-
2,5-bis(4-fluorobenzylthio)-1,3,4-thiadiazole
-
-
2,5-bis(4-methoxybenzylthio)-1,3,4-thiadiazole
-
-
2,5-bis(4-nitrobenzylthio)-1,3,4-thiadiazole
-
-
2,5-bis(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazole
-
-
2,5-bis(benzylthio)-1,3,4-thiadiazole
-
-
2-(2'-amino-3'-methoxyphenyl)oxanaphthalen-4-one
-
PD98059
2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one
-
PD98059
2-(2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]amino]ethoxy)ethanol
-
-
2-(3-tert-butyl-1-methyl-1H-pyrazol-5-yl)-N-[4-(2-morpholin-4-ylethoxy)naphthalen-1-yl]-2-oxoacetamide
-
-
2-(4-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-phenyl-4H-1,2,4-triazol-3-ylthio)-5-nitrothiazole
-
-
2-(4-(2,4-dichlorophenyl)-5-(1-methyl-1H-pyrrol-2-yl)-4H-1,2,4-triazol-3-ylthio)-5-nitrothiazole
-
-
2-(4-(3-methoxyphenyl)-5-phenyl-4H-1,2,4-triazol-3-ylthio)-5-nitrothiazole
-
-
2-(4-(furan-2-ylmethyl)-5-(naphthalen-1-yl)-4H-1,2,4-triazol-3-ylthio)-5-nitrothiazole
-
-
2-(4-chlorphenyl)-4-(4-fluorophenyl)-5-pyridin-4-yl-1,2-dihydropyrazol-3-one
-
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
-
-
2-(4-fluorophenyl)-6-methoxy-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
2-(5-tert-butyl-2-methylfuran-3-yl)-2-oxo-N-[4-(pyrimidin-2-ylamino)-5,8-dihydronaphthalen-1-yl]acetamide
-
-
2-(5-tert-butyl-2-methylfuran-3-yl)-2-oxo-N-[4-(pyrimidin-4-ylamino)-5,8-dihydronaphthalen-1-yl]acetamide
-
-
2-(5-tert-butyl-2-methylfuran-3-yl)-N-(4-[[6-(morpholin-4-ylmethyl)pyridin-3-yl]methyl]-5,8-dihydronaphthalen-1-yl)-2-oxoacetamide
-
-
2-(5-tert-butyl-2-methylfuran-3-yl)-N-[4-(2-morpholin-4-ylethoxy)naphthalen-1-yl]-2-oxoacetamide
-
-
2-(benzyloxy)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-(ethylamino)-N-[5-(ethylcarbamoyl)-2-methylphenyl]-4-methyl-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
2-(ethylsulfanyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
-
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)-3-methylbutan-1-ol
-
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)butan-1-ol
-
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)ethanol
-
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
-
2-([6-[(3-methylbut-2-en-1-yl)amino]-9-(1-methylethyl)-9H-purin-2-yl]amino)ethanol
-
-
2-([9-methyl-6-[(3-methylbut-2-en-1-yl)amino]-9H-purin-2-yl]amino)ethanol
-
-
2-([[2-[[(1S)-1-(hydroxymethyl)propyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
2-([[2-[[1-(hydroxymethyl)-2-methylbutyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
2-([[9-(1-methylethyl)-2-(4-prop-2-yn-1-ylpiperazin-1-yl)-9H-purin-6-yl]amino]methyl)phenol
-
-
2-([[9-(1-methylethyl)-2-piperazin-1-yl-9H-purin-6-yl]amino]methyl)phenol
-
-
2-([[9-(1-methylethyl)-2-propyl-9H-purin-6-yl]amino]methyl)phenol
-
-
2-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-5-carboxamide
-
2-bromothiazole-5-carboxylic acid
-
inhibition of p38alpha MAP kinase
2-chloro-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-chloro-4-[4-(4-fluorophenyl)-2-(phenylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-chloro-N-(cyclohexylmethyl)-9H-purin-6-amine
-
-
2-fluoro-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridine
-
2-fluoro-4-[2-(phenylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridine
-
2-fluoro-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-fluoro-4-[4-(4-fluorophenyl)-2-(phenylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-[(1,5-dimethylhexyl)oxy]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
-
2-[(1-methylethyl)amino]-N-[2-methyl-5-(1H-pyrazol-5-ylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
2-[(1-methylethyl)amino]-N-[2-methyl-5-(methylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
2-[(1-methylethyl)amino]-N-[2-methyl-5-[(1-methyl-1H-pyrazol-5-yl)carbamoyl]phenyl]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
2-[(2,4-difluorophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
-
-
2-[(2,4-difluorophenyl)amino]-5H-dibenzo[a,d][7]annulen-5-one
-
-
2-[(2,4-dinitrophenyl)sulfanyl]-1,3-benzoxazole
-
-
2-[(2-amino-4-fluorophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
-
-
2-[(2-aminophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
-
-
2-[(2-aminophenyl)amino]-5H-dibenzo[a,d][7]annulen-5-one
-
-
2-[(2-methoxyethyl)amino]-N-[2-methyl-5-(methylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
-
-
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
-
-
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole-5-sulfonic acid
-
-
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-5-(trifluoromethyl)-1H-benzimidazole
-
-
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl][1,3]thiazolo[4,5-b]pyridine
-
-
2-[(6-amino-9H-purin-2-yl)amino]ethanol
-
-
2-[3-tert-butyl-1-(3-methylphenyl)-1H-pyrazol-5-yl]-2-(hydroxyamino)-N-[4-(2-morpholin-4-ylethoxy)naphthalen-1-yl]acetamide
-
-
2-[4-[3-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-5-yl]piperidin-1-yl]-2-oxoethanol
-
2-[6-(benzylamino)-2-[(2-hydroxyethyl)amino]-9H-purin-9-yl]ethanol
-
-
2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]amino]ethanol
-
-
2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]sulfanyl]ethanol
-
-
3-(3-bromo-4-[(2,4-difluorobenzyl)oxy]-6-methyl-2-oxopyridin-1(2H)-yl)-N,4-dimethylbenzamide
-
PH-797804, ATP-competitive, readily reversible inhibitor of the alpha isoform of human p38 MAP kinase
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
-
-
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzamide
-
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzonitrile
-
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl)benzamide
-
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl)benzonitrile
-
3-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexanol
-
-
3-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
-
3-([5-[2-(cyclopropylamino)pyrimidin-4-yl]-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzamide
-
3-([5-[2-(cyclopropylamino)pyrimidin-4-yl]-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzonitrile
-
3-([[2-(heptylamino)-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
3-([[2-[[1-(hydroxymethyl)-2-methylbutyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
3-([[2-[[1-(hydroxymethyl)propyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
3-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]benzamide
-
3-[(2,4-difluorophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
-
-
3-[(2-amino-4-fluorophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
-
-
3-[(2-aminophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
-
-
3-[(4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-yl)amino]propan-1-ol
-
3-[([2-[(3-hydroxypropyl)amino]-9-(1-methylethyl)-9H-purin-6-yl]amino)methyl]phenol
-
-
3-[2-(cyclopropylamino)-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]-N,4-dimethylbenzamide
-
inhibition of p38alpha MAP kinase
3-[2-(cyclopropylamino)-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]-N-ethyl-4-methylbenzamide
-
inhibition of p38alpha MAP kinase
3-[4-(N-benzyl-N-methylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
-
3-[4-(N-benzylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
crystal structure analysis of the inhibitor bound to p38
3-[4-(N-tert-butylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
-
3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]benzonitrile
-
3-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[4-(4-fluorophenyl)-5-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[5-(2-aminopyrimidin-4-yl)-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[5-(2-aminopyrimidin-4-yl)-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzamide
-
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzamide
-
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-1-yl]methyl]benzonitrile
-
3-[[5-(4-fluorophenyl)-4-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-2-yl]methyl]benzonitrile
-
3-[[6-(benzylsulfanyl)-9-(1-methylethyl)-9H-purin-2-yl]amino]propan-1-ol
-
-
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3,4-thiadiazol-2-yl)sulfanyl]-4H-1,2,4-triazol-3-ol
-
-
4-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(2,4-dimethoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(2,5-dimethoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(2-methoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(3,4-difluorophenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(3,4-dimethoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(3,5-dimethoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(3-fluorophenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(3-methoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl)-N-[(1S)-1-phenylethyl]pyridin-2-amine
-
4-(4-fluorophenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(4-methoxyphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(4-nitrophenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(4-tert-butylphenyl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(benzo[d][1,3]dioxol-5-yl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-(naphthalen-1-yl)-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
-
4-([[2-(benzylamino)-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
-
-
4-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-2-carboxamide
-
4-chloro-3-[[1-(2-chlorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-N-cyclopropylbenzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]oxy]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,5-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,6-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(2,6-difluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(3-fluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(4-fluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-chloro-N-cyclopropyl-3-[[1-(4-fluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]benzamide
-
4-cyclohexyl-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-ol
-
-
4-fluoro-N-(5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-yl)benzamide
-
-
4-[(1H-benzimidazol-2-ylsulfanyl)methyl]benzoic acid
-
-
4-[2-(benzylsulfanyl)-4-(4-fluorophenyl)-1H-imidazol-5-yl]-2-chloropyridine
-
4-[2-(benzylsulfanyl)-4-(4-fluorophenyl)-1H-imidazol-5-yl]-2-fluoropyridine
-
4-[2-(benzylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-2-fluoropyridine
-
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)pyridin-2-amine
-
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
-
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(2-phenylethyl)pyridin-2-amine
-
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(thiophen-2-ylmethyl)pyridin-2-amine
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)pyrimidin-2-amine
-
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-(1-methylpiperidin-4-yl)pyrimidin-2-amine
-
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclohexylpyrimidin-2-amine
-
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclopentylpyrimidin-2-amine
-
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclopropylpyrimidin-2-amine
-
-
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-methylpyrimidin-2-amine
-
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-3-methyl-N-(2-morpholin-4-ylethyl)benzamide
-
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-3-methylbenzoic acid
-
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-N-(2-methoxyethyl)-3-methylbenzamide
-
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-phenylpyridin-2-amine
-
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
-
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
-
4-[4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(1-phenylethoxy)pyridine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(4-methylphenoxy)pyridine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(tetrahydrofuran-2-ylmethoxy)pyridine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(thiophen-2-ylmethoxy)pyridine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1,2,2-trimethylpropyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-methyl-3-phenylpropyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylpropyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-methylbutyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-methylcyclohexyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-phenylpropyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-thiophen-2-ylethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(3-methylbutyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(4-methylcyclohexyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(furan-2-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(naphthalen-1-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-2-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-3-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-4-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydrofuran-2-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(thiophen-2-ylmethyl)pyridin-2-amine
-
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(5-methylfuran-2-yl)methyl]pyridin-2-amine
-
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
4-[[(6-amino-9H-purin-8-yl)sulfanyl]methyl]benzoic acid
-
-
4-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
4-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
4-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
4-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
4-[[5-(4-fluorophenyl)-4-(2-hydroxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
4-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
4-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
-
4-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
-
5,6-dichloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
5-((4-methyl-5-(5-nitrothiazol-2-ylthio)-4H-1,2,4-triazol-3-yl)methyl)-3-(pyrazin-2-yl)-1,2,4-oxadiazole
-
-
5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
5-(5-nitrothiazol-2-ylthio)-4-(3-(trifluoromethyl)phenyl)-4H-1,2,4-triazol-3-ol
-
-
5-(5-nitrothiazol-2-ylthio)-4-(4-(trifluoromethoxy)phenyl)-4H-1,2,4-triazol-3-ol
-
-
5-(5-nitrothiazol-2-ylthio)-4-(4-(trifluoromethyl)phenyl)-4H-1,2,4-triazol-3-ol
-
-
5-(5-nitrothiazol-2-ylthio)-N-((tetrahydrofuran-2-yl)methyl)-1,3,4-thiadiazol-2-amine
-
-
5-(5-nitrothiazol-2-ylthio)-N-propyl-1,3,4-thiadiazol-2-amine
-
-
5-(5-nitrothiophen-2-ylthio)-4-phenyl-4H-1,2,4-triazol-3-ol
-
-
5-(acetylamino)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-(benzylthio)-1,3,4-thiadiazol-2-amine
-
-
5-(butylthio)-4-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4H-1,2,4-triazol-3-ol
-
-
5-(butylthio)-4-phenyl-4H-1,2,4-triazol-3-ol
-
-
5-(difluoromethyl)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-(ethylthio)-4-phenyl-4H-1,2,4-triazol-3-ol
-
-
5-benzyl-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-bromo-N-(3-chloro-2-piperazin-1-ylphenyl)furan-2-carboxamide
-
5-bromo-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-bromo-N-[2-(4-prop-2-en-1-ylpiperazin-1-yl)-3-(trifluoromethyl)phenyl]furan-2-carboxamide
-
5-bromo-N-[2-(4-prop-2-en-1-ylpiperazin-1-yl)biphenyl-3-yl]furan-2-carboxamide
-
5-bromo-N-[3-(phenylamino)-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-bromo-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-cyclopropylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-ethylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-methylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-propylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-(4-pyridin-2-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-[4-(1-methylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-[4-(2-methylprop-2-en-1-yl)piperazin-1-yl]phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-[4-(2-phenylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-[4-(furan-2-ylmethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
-
5-bromo-N-[3-chloro-2-[4-(trifluoroacetyl)piperazin-1-yl]phenyl]furan-2-carboxamide
-
5-bromo-N-[3-fluoro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-bromo-N-[3-methyl-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
-
5-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
-
-
5-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
-
-
5-chloro-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-cyano-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
-
5-methoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
-
-
5-methoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
5-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
5-nitro-2-(4-phenyl-5-(pyridin-4-yl)-4H-1,2,4-triazol-3-ylthio)-thiazole
-
-
5-nitro-2-(4-phenyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-ylthio)-thiazole
-
-
5-nitro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
-
-
5-tert-butyl-N-cyclopropyl-2-methoxy-3-[2-[4-(2-morpholin-4-yl-ethoxy)-naphthalen-1-yl]-2-oxo-acetylamino]-benzamide
-
KR-003048
6,7-dichloro-2-(4-fluorophenyl)-3-pyridin-4-ylquinoxaline
-
-
6-(3-(cyclopropylamino)-6-methylbenzo[d]isoxazol-7-yl)-N,N-dimethylphthalazin-1-amine
-
6-(benzylsulfanyl)-2-chloro-9-(1-methylethyl)-9H-purine
-
-
6-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]pyridine-2-carboxamide
-
6-chloro-2-[(4-methyl-5-thiophen-2-yl-4H-1,2,4-triazol-3-yl)sulfanyl]-1,3-benzothiazole
-
-
6-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
-
-
6-chloro-2-[[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
-
-
6-chloro-2-[[5-(2,4-dichlorophenyl)-4-methyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
-
-
6-chloro-2-[[5-(2-methoxyphenyl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
-
-
6-chloro-N-cyclopropyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
-
6-chloro-N-isopropyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
-
6-ethoxy-1,3-benzothiazole-2-sulfonamide
-
-
6-ethoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
-
-
6-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
-
-
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-1H-indazol-3-amine
-
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isothiazol-3-amine
-
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
-
6-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-9H-purin-2-amine
-
-
6-[1-(2-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(2-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(3-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(4-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[1-(4-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazole
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
-
6-[5-amino-1-ethyl-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1S)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
-
6-[5-[(6-chloro-1,3-benzothiazol-2-yl)sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl]quinoline
-
-
7-(1-isopropoxyphthalazin-6-yl)-N,6-dimethylbenzo[d]isoxazol-3-amine
-
7-(1-isopropylphthalazin-6-yl)-N,6-dimethylbenzo[d]isoxazol-3-amine
-
7-(6-N-phenylaminohexyl)amino-2H-anthra[1,9-cd]pyrazol-6-one
8-[(2,4-difluorophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
-
-
8-[(2,4-difluorophenyl)amino]-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
-
-
8-[(2,4-difluorophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
-
-
8-[(2-amino-4-fluorophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
-
-
8-[(2-amino-4-fluorophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
-
-
8-[(2-aminophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
-
-
8-[(2-aminophenyl)amino]-11H-benzo[5,6]cyclohepta[1,2-c]pyridin-11-one
-
-
8-[(2-aminophenyl)amino]-5,6-dihydro-11H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-one
-
-
8-[(2-aminophenyl)amino]-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
-
-
8-[(2-aminophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
-
-
8-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-9H-purin-6-amine
-
-
adenylyl-beta,gamma-methylene diphosphonic acid
-
i.e. AMP-PCP, MgAMP-PCP shows a mixed inhibition pattern in the kinase reaction, and a competitive pattern in the ATPase reaction
ADP
-
MgADP- shows an uncompetitive inhibition pattern
all-trans retinoic acid receptor
-
ERK access to the substrate is regulated by the all-trans retinoic acid receptor, RAR
-
anthra[1-9-cd]pyrazol-6(2H)-one
-
SP600125
AZD6244
-
ARRY-142886, MEK1/2 inhibitor
Butyrolactone
-
BLI, MAPK is indirectly inhibited by the CDK inhibitor BLI
C2-alkylaminothiazole
-
-
calcium diphosphate
-
crystals in plasma inhibit the p38 MAP kinase mediating the activation of neutrophils and repression of TNF-alpha-induced apoptosis
Cl-1040
a potent inhibitor of MEK
ethyl 1-[5-([5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]carbamoyl)-2-methylphenyl]-2,3-dihydro-1H-1,2,3-triazole-4-carboxylate
-
FR180204
-
ERK inhibitor, 5-(2-phenyl-pyrazolo[1,5-a]pyridin-3-yl)-1H-pyrazolo[3,4-c]pyridazin-3-ylamine
furan-2-carboxylic acid (3-[5-(4H-[1,2,4]triazol-3-yl)-1H-indazol-3-yl]-phenyl)-amide
inhibits JNK2alpha2 enzyme in vitro
hypericin
-
hypericin-mediated inhibition of glutamate release appears to involve the suppression of mitogen-activated protein kinase pathway
II/SP600125
inhibits SAPK/JNK; inhibits SAPK/JNK; inhibits SAPK/JNK
indirubin-3'-monoxime
-
79% inhibition at 0.01 mM of JNK/SAPK1c, 17% inhibition at 0.01 mM of SAPK2a/p38, 55% inhibition at 0.01 mM of SAPK2b/p38beta, 26% inhibition at 0.01 mM of SAPK3/p38gamma, and 35% inhibition at 0.01 mM of SAPK4/p38delta
lignocaine
-
the enzyme inhibition by lignocine may involve voltage-sensitive sodium channels, the enzyme attenuates the induction of MAPK activation by lipopolysaccharides, overview
MKK4
wild-type and L44I mutant MKK4, the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2; wild-type MKK4, the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2
-
MKK4 mutant F48K
the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2, but to a lesser degree compared to the wild-type MKK4; the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2, but to a lesser degree compared to the wild-type MKK4
-
MKK4 mutant L44I
the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2; wild-type and L44I mutant MKK4, the D-site from enzyme MKK4 competitively inhibits JNK-mediated phosphorylation of c-Jun and ATF2
-
MKP1/2
-
may dampen ERK activity during the G1/S transition, is involved in reducing strength and duration of ERK signaling
-
MKP3
-
selective for ERK1 and 2
-
N,4-dimethyl-3-[2-[(1-methylethyl)amino]-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
-
inhibition of p38alpha MAP kinase
N,4-dimethyl-3-[6-oxo-2-(propylamino)-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
-
inhibition of p38alpha MAP kinase
N,6-dimethyl-7-(1-((R)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-amine
-
N,6-dimethyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-amine
-
N-(1,2-dimethylpropyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-(1,2-dimethylpropyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1,2-diphenylethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1,3-dimethylbutyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1,5-dimethylhexyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1-benzothiophen-2-ylmethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1-benzyl-2-phenylethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1-cyclohexylethyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1-methyl-4-phenylbutyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
-
N-(1-methylethyl)-4-(1H-pyrazol-4-yl)pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-(3-piperidin-3-yl-1H-pyrazol-4-yl)pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-[3-(6-methylpyridin-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-2-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-4-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-(1-methylethyl)-4-[3-[1-(methylsulfonyl)piperidin-4-yl]-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-(1-methylethyl)-6-(1-phenyl-1H-pyrazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-(4-phenyl-1,3-oxazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-(4-phenyl-1H-imidazol-5-yl)-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(2-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(3-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-(1-methylethyl)-6-[1-(4-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
-
N-(2,3-dihydro-1H-inden-1-yl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(2-aminobenzyl)-2-chloro-9-(1-methylethyl)-9H-purin-6-amine
-
-
N-(2-chloro-6-methylphenyl)-2-(cyclobutylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(2-chloro-6-methylphenyl)-2-(ethylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(2-chloro-6-methylphenyl)-2-(phenylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(2-chloro-6-methylphenyl)-2-(propylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(2-chloro-6-methylphenyl)-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(2-methoxyethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
N-(3,3-dimethylbutyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(3,4-dimethoxyphenethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
N-(4-fluorobenzyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(4-methoxybenzyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
N-(4-tert-butylbenzyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
-
N-(5-carbamoyl-2-methylphenyl)-2-(propylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(5-carbamoyl-2-methylphenyl)-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-(6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-yl)acetamide
-
N-(cyclohexylmethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-(furan-2-ylmethyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
-
N-(S)-sec-butyl-6-(6-methyl-3-(methylamino)benzo[d]isoxazol-7-yl)phthalazin-1-amine
-
N-benzyl-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
-
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-benzyl-4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-9-(1-methylethyl)-2-(methylsulfanyl)-9H-purin-6-amine
-
-
N-benzyl-9-(1-methylethyl)-9H-purin-6-amine
-
-
N-benzyl-9-methyl-2-morpholin-4-yl-9H-purin-6-amine
-
-
N-cyclohexyl-4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-cyclohexyl-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-cyclopentyl-4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
-
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-fluorobenzamide
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]oxy]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-5-fluoro-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,4-difluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]oxy]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,6-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(2,6-difluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]oxy]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(3-fluorophenyl)-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(4-fluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]amino]-4-methylbenzamide
-
N-cyclopropyl-3-[[1-(4-fluorophenyl)-7-methyl-1H-pyrazolo[3,4-d]pyridazin-4-yl]oxy]-4-methylbenzamide
-
N-cyclopropyl-6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
-
N-cyclopropyl-6-methyl-7-(1-o-tolylphthalazin-6-yl)benzo[d]-isoxazol-3-amine
-
N-ethyl-4-methyl-3-[2-[(1-methylethyl)amino]-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
-
inhibition of p38alpha MAP kinase
N-ethyl-4-methyl-3-[6-oxo-2-(propylamino)-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
-
inhibition of p38alpha MAP kinase
N-ethyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
N-ethyl-6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
-
N-ethyl-6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
-
N-isopropyl-6-(6-methyl-3-(methylamino)benzo[d]isoxazol-7-yl)phthalazin-1-amine
-
N-methyl-9-(1-methylethyl)-9H-purin-6-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
-
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
-
-
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
-
-
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
-
-
N-[(1R)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-[(1S)-1-(3-chloro-4-fluorophenyl)-2-hydroxyethyl]-4-[4-(3-chlorophenyl)-1H-pyrazol-3-yl]-1H-pyrrole-3-carboxamide
-
N-[(1S)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-[(1S)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-(phenylamino)furan-2-carboxamide
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-ethylfuran-2-carboxamide
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-fluorofuran-2-carboxamide
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methoxyfuran-2-carboxamide
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methylfuran-2-carboxamide
-
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-prop-1-yn-1-ylfuran-2-carboxamide
-
N-[2-(2,5-dimethylphenyl)ethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
-
N-[2-(4-acetylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
-
N-[2-(4-benzylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
-
N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-(propylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-[[(1S)-1-methylpropyl]amino]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-4-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1H-pyrrole-2-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-2-methyl-1,3-thiazole-4-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-5-cyanopyridine-2-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-6-methylpyridine-2-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]isoxazole-5-carboxamide
-
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]pyrimidine-2-carboxamide
-
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
N-[5-(ethylcarbamoyl)-2-methylphenyl]-2-(propylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[5-(ethylcarbamoyl)-2-methylphenyl]-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[5-(ethylcarbamoyl)-2-methylphenyl]-4-methyl-2-(propylamino)-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[5-(isoxazol-3-ylcarbamoyl)-2-methylphenyl]-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
-
inhibition of p38alpha MAP kinase
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1R)-1-cyclohexylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1S)-1-cyclohexylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1S)-2-(dimethylamino)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[2-(dimethylamino)-2-methylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[3-(dimethylamino)-2,2-dimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-(N-cyclopropylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(2,2-dimethylpropyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(2-hydroxy-2-methylpropyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(cyclohexylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1-methylpiperidin-3-yl)methyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1-methylpiperidin-4-yl)methyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1R)-1,2,2-trimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1R)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1S)-1,2,2-trimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1S)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-(N-methylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-[N-(pyridin-3-ylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
-
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-[N-(pyridin-4-ylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
-
N-[trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexyl]acetamide
-
-
N-[trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexyl]methanesulfonamide
-
-
N6-(2-aminobenzyl)-N2-(4-aminocyclohexyl)-9-(1-methylethyl)-9H-purine-2,6-diamine
-
-
N6-benzyl-9-(1-methylethyl)-9H-purine-2,6-diamine
-
-
nobiletin
-
inhibits angiotensin II-induced activation of JNK
pep-JIP1
-
peptide corresponding to the D-domain of JIP-1, final sequence of the most extensively used peptide is GRKKRRQRRRPPRPKRPTTLNLFPQVPRSQDT
phospholipase C-gamma1 D-domain
a peptide containing the phospholipase C-gamma1 D-domain competitively inhibits the phosphorylation of Elk1 and c-Jun by ERK2, overview; a peptide containing the phospholipase C-gamma1 D-domain competitively inhibits the phosphorylation of Elk1 and c-Jun by JNK3, overview
-
pyridinyl imidazole-type inhibitors
IC50 of 15-48 nM
-
S-1,3-benzothiazol-2-yl (2Z)-(2-amino-1,3-thiazol-4-yl)(methoxyimino)ethanethioate
-
-
SB 203580
-
no preference for either active or inactive p38alpha, no preincubation required to achieve maximum inhibition
SB202
-
p38 inhibitor SB202
skepinone-L
-
the specificity by which SCD-1 modulates the phospholipid composition and inhibits p38 MAPK signaling (among survival/stress pathways), thereby preventing endoplasmic reticulum stress (but not other SCD-1-dependent responses), suggests selective protein-lipid interactions
tert-butyl 4-(2-[[(5-bromofuran-2-yl)carbonyl]amino]-6-chlorophenyl)piperazine-1-carboxylate
-
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexanol
-
-
trans-4-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
-
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
trans-4-[(4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-yl)amino]cyclohexanol
-
[3-amino-2-(1,3-benzodioxol-4-yl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,3-dimethoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,4-difluorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,6-dichlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,6-difluoro-4-methoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,6-difluorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,6-dimethoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2,6-dimethylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-chlorophenyl)methanone
-
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-methoxyphenyl)methanone
-
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-trifluoromethylphenyl)methanone
-
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](phenyl)methanone
-
[3-amino-2-(2-isopropylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2-methoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(2-methylphenyl)-1-oxidopyridin-4-yl](phenyl)methanone
-
[3-amino-2-(3-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(4-chloro-2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(4-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-(4-chlorophenyl)-1-oxidopyridin-4-yl](phenyl)methanone
-
[3-amino-2-(4-hydroxy-2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-[2-methyl-4-(2-morpholin-4-ylethoxy)phenyl]-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[3-amino-2-[4-(2-methoxyethoxy)-2-methylphenyl]-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
-
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
highly selective for p38 isozyme alpha wild-type and mutants with IC50 of 0.10-0.14 nM, IC50 for JNK2 is 680 nM, for JNK3 970 nM and for ERK 660 nM
[Nle4, D-Phe7]alpha-melanocyte stimulating hormone
-
NDP-MSH, the melanocortin agonist dose-dependently inhibits JNK activity in HEK-293 cells stably expressing the human melanocortin receptor type 4
-
7-(6-N-phenylaminohexyl)amino-2H-anthra[1,9-cd]pyrazol-6-one
AV-7
7-(6-N-phenylaminohexyl)amino-2H-anthra[1,9-cd]pyrazol-6-one
-
AV-7
alsterpaullone
-
inhibition of JNK/SAPK1c, SAPK2a/p38, SAPK2b/p38beta, SAPK3/p38gamma, and SAPK4/p38delta
alsterpaullone
-
36% inhibition of MAPK2/ERK2 at 0.01 mM
BIRB 796
-
no preference for either active or inactive p38alpha, slow association kinetics of BIRB 796 as compared to SB 203580, corresponding with the requirement of a relatively long preincubation time to obtain maximal effect in a cellular assay
BIRB 796
a clinical compound, binds to Asp168 and Glu71, and to Met109 in the ATP binding site
BIRB-796
-
BIRB796
-
-
BIRB796
binding structure with isozyme p38alpha
kenpaullone
-
slight inhibition of SAPK2a/p38 and SAPK3/p38gamma, no inhibition of SAPK4/p38delta, JNK/SAPK1c, SAPK2b/p38beta, and SAPK4/p38delta
kenpaullone
-
30% inhibition of MAPK2/ERK2 at 0.01 mM
ML3403
an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to strong dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to strong dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells
PD098059
-
ERK inhibitor, significantly reduces hemocyte spreading in a dose-dependent manner, impairs sheep red blood cell phagocytosis, severely inhibits H2O2 production during phagocytosis, significantly impairs the cellular encapsulation of trematode larvae and H2O2 production during encapsulation
PD098059
-
selective inhibitor of mitogen-activated extracellular regulated kinase phosphorylation, arrests cells in G(0)/G(1), increases P21/waf1 antigen expression
PD098059
-
ERK inhibitor, significantly reduces hemocyte spreading in a dose-dependent manner, impairs sheep red blood cell phagocytosis, severely inhibits H2O2 production during phagocytosis, significantly impairs the cellular encapsulation of trematode larvae and H2O2 production during encapsulation
PD169316
-
PD169316
-
i.e. 4-(4-fluorophenyl)-2-(4-nitrophenyl)-5-(4-pyridyl)-1H-imidazole, a specific p38 MAPK inhibitor, reduces 5-hydroxytryptamine uptake in cells, inhibits SERT phosphorylation
PD98059
-
ERK1/2 inhibitor
PD98059
-
specific p42/44 mitogen-activated protein (MAP) kinase cascade inhibitor
PD98059
-
inhibits ERK1/2 or JNK
PD98059
-
MEK1 inhibitor, i.e. 2-(2'-amino-3'-methoxyphenyl)-oxanaphthalen-4-one
PD98059
an ERK inhibitor; an ERK inhibitor
PD98059
-
inhibits ERK1 and ERK2
PD98059
-
inhibition of neurite outgrowth induced by ADAMTS4 treatment
purvalanol
-
16% inhibition at 0.01 mM of JNK/SAPK1c, no inhibition of SAPK2a/p38, SAPK3/p38gamma, and SAPK4/p38delta
purvalanol
-
74% inhibition of MAPK2/ERK2 at 0.01 mM
roscovitine
-
19% inhibition of MAPK2/ERK2 at 0.01 mM
SB202190
an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells; an ATP-competitive pyridinyl imidazole inhibitor of p38 MAPK, leads to dephosphorylation of MPK2 in the parasite and effective killing of parasite vesicles at concentrations that do not affect cultivated mammalian cells
SB202190
-
specific p38 MAPK inhibitor
SB202190
-
selective to p38 MAPKalpha and -beta isoforms, enhances strain-induced ERK1/2 activation but also restricts strain-induced ERK1/2 activation at longer times
SB202190
-
i.e. 4-(4-fluorophenyl)-2-(4-hydroxyphenyl)-5-(4-pyridyl)1H-imidazole, a specific p38beta isozyme inhibitor
SB202190
-
benzyl coumarin derivative
SB202190
-
isoform p38alpha/beta inhibitor
SB202190
inhibitor of p38 MAPKalpha, little or no inhibition of p38 MAPK beta, gamma, and delta
SB202190
-
a p38 MAPK specific inhibitor
SB202190
-
inhibition of p38 MAPK and modulation of ERK, enhanced strain-induced ERK1/2 activation at 20 min and its restriction after 24 h
SB203580
-
p38 kinase inhibitor,has no effect on hemocyte spreading, impairs sheep red blood cell phagocytosis
SB203580
-
p38 MAPK inhibitor
SB203580
-
selective to p38 MAPKalpha and -beta isoforms, addition to AS cells reveals marked reduction in coat size, both basal and strain-induced hyaluronan release is significantly reduced, enhances strain-induced ERK1/2 activation but also restricts strain-induced ERK1/2 activation at longer times
SB203580
-
i.e. 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole, a specific p38alpha isozyme inhibitor
SB203580
-
p38 MAP kinase specific inhibitor
SB203580
-
p38 isozyme alpha-specific inhibitor
SB203580
-
P38 MAPK inhibitor, has no effect on cell proliferation
SB203580
-
inhibits MK2 phosphorylation
SB203580
-
inhibitor of p38 MAP kinase, inhibition of the activation by TNF-alpha
SB203580
-
p38 kinase inhibitor,has no effect on hemocyte spreading, impairs sheep red blood cell phagocytosis
SB203580
-
noncompetitive in the kinase reaction, competitive versus ATP in the ATPase reaction, no classical linear inhibition kinetics at concentrations below 100 nM
SB203580
inhibits the p38 isozymes isozymes alpha, beta, and gamma
SB203580
-
specific inhibitor of p38alpha MAP kinase, interaction analysis with immobilized enzyme in a surface plasmon resonance study, binding structure from the cyrstal structure of the enzyme-inhibitor complex
SB203580
-
inhibits p38 MAP kinase in T cells, administration of the pharmacological inhibitor of the kinase during the course of infection with the spirochete Borrelia burgdorferi results in reduced levels of IFN-gamma in the sera of infected mice
SB203580
inhibitor of p38 MAPKalpha, little or no inhibition of p38 MAPK beta, gamma, and delta
SB203580
-
a p38 MAPK specific inhibitor
SB203580
-
inhibits p38 MAP kinase
SB203580
-
i.e. 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-1H-imidazole, a specific p38 MAPK inhibitor, reduces 5-hydroxytryptamine uptake in cells, inhibits SERT phosphorylation
SB203580
-
inhibition of p38 MAPK and modulation of ERK, enhanced strain-induced ERK1/2 activation at 20 min and its restriction after 24 h
SB203580
blocks stress-induced phosphorlyation of MK2 in CHSE-214 cells; blocks stress-induced phosphorlyation of MK2 in CHSE-214 cells; blocks stress-induced phosphorlyation of MK2 in CHSE-214 cells, completely abolishes LPS-stimulated TNF-2 and IL-1beta mRNA expression in macrophages
SB242235
-
SP600125
-
JNK inhibitor has no effect on hemocyte spreading, impairs sheep red blood cell phagocytosis
SP600125
inhibitor of JNK
SP600125
-
JNK1/2 inhibitor
SP600125
-
JNK inhibitor has no effect on hemocyte spreading, impairs sheep red blood cell phagocytosis
SP600125
inhibitor of JNK; inhibitor of JNK
SP600125
-
SP600125 inhibits lipopolysaccharide- and lipoteichoic acid-induced iNOS/NO production by reducing lipopolysaccharide- and lipoteichoic acid-induced JNK protein phosphorylation
SP600125
inhibitor of JNK
SR3451
-
-
SR3576
-
-
SR3582
-
-
SR4018
-
-
SR4276
-
-
SR4326
-
-
SR4642
-
-
SR4643
-
-
staurosporine
-
U0126
the activity of MAPKs is inhibited by treatment of cells with the selective MEK inhibitor
U0126
inhibitor of Erk1; inhibitor of Erk2
U0126
-
MEK1/2 inhibitor, i.e. 1,4-diamino-2,3-dicyano-1,4-bis[2-aminophenylthio] butadiene
U0126
-
specific inhibitor of ERK
U0126
inhibitor of Erk1; inhibitor of Erk2
U0126
-
inhibition of neurite outgrowth induced by ADAMTS4 treatment
U0126
-
MAPK inhibitor, treatment of metaphase egg extracts reduces Mps1 phosphorylation
additional information
-
not inhibited by diethyldithiocarbamic acid or ethylene action, treatments with hormones JA and SA together with diethyldithiocarbamic acid can repress TIPK expression when compared to control. Plants expressing TIPK-AS reveal increased sensitivity to pathogen attack, Trichoderma preinoculation can not protect antisense plants against subsequent pathogen attack
-
additional information
-
molecular mechanism of negative regulation of Ras/ERK signaling, Sef negatively regulates ERK phosphorylation by blocking dissocation of MEK and ERK
-
additional information
-
synthesis of peptides behaving as pseudosubstrates, determination of inhibitory potential
-
additional information
-
no inhibition by PD98059
-
additional information
-
inhibition of the MEK-ERK pathway by either U0126 or PD98059 has no discernable effect on p38 MAPK phosphorylation, U0126 treatment also fails to modify pervanadate-induced p38 MAPK activity
-
additional information
p38alpha kinase inhibitor AMG 2372 minimally inhibits the kinase activity of p38delta
-
additional information
-
p38alpha kinase inhibitor AMG 2372 minimally inhibits the kinase activity of p38delta
-
additional information
activity is not blocked by the pyridinyl imidazole, 4-(4-fluorophenyl)-2-2(4-hydroxyphenyl)-5-(4-pyridyl)-imidazole (identical to SB202190)
-
additional information
not inhibited by the drugs SB 203580 and SB 202190
-
additional information
not inhibited by the drugs SB 203580 and SB 202190
-
additional information
-
not inhibited by the drugs SB 203580 and SB 202190
-
additional information
-
roscovitine is a poor inhibitor of MAPKs
-
additional information
-
inhibition of the Ca2+-dependent signaling and expression of interleukin-8 in 1HAEo cells by BAPTA/AM, verapamil, cyclosporin A, FK-506, and TEMPO, and by an anti-asialoGM1 receptor antibody
-
additional information
-
PKC isozymes, EC 2.7.11.13, suppress p38 activating phosphorylation under mechanical pressure of cells
-
additional information
-
PD 98059 inhibits EGF-induced nuclear translocation of CAD
-
additional information
-
phosphorylation of p38alpha occurs in vivo only in absence of growth factor in primary erythroid progenitors
-
additional information
effects of inhibitors on ATLAS technology assay, overview
-
additional information
computer-aided drug design and synthesis of p38 inhibitors based on the 2-tolyl-(1,2,3-triazol-1-yl-4-carboxamide) scaffold, 2-alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles-O-alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK. Binding affinity of inhibitors to p38 is determined by a thermal denaturation assay, overview
-
additional information
-
computer-aided drug design and synthesis of p38 inhibitors based on the 2-tolyl-(1,2,3-triazol-1-yl-4-carboxamide) scaffold, 2-alkylamino- and alkoxy-substituted 2-amino-1,3,4-oxadiazoles-O-alkyl benzohydroxamate esters replacements retain the desired inhibition and selectivity against MEK. Binding affinity of inhibitors to p38 is determined by a thermal denaturation assay, overview
-
additional information
-
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
synthesis of diverse inhibitors, inhibitor binding structures and inhibition mechanism, overview
-
additional information
-
synthesis of diverse inhibitors, inhibitor binding structures and inhibition mechanism, overview
-
additional information
synthesis of 3-amino-7-phthalazinylbenzoisoxazole-based inhibitors, structure-activity realationship, overview
-
additional information
-
synthesis of 3-amino-7-phthalazinylbenzoisoxazole-based inhibitors, structure-activity realationship, overview
-
additional information
-
GluR2 overexpression in U-87MG cells inhibits proliferation by inactivating extracellular signal-regulated kinase 1/2-Src phosphorylation
-
additional information
no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site; no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site
-
additional information
no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site; no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site
-
additional information
no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site; no inhibition by MKK4 mutant L44I/F48K. Creation of MEK1-like, MEK2-like, MKK3-like, and MKK6-like alleles of MKK4 by changing 2 residues, L44 and F48, in the MKK4 D-site
-
additional information
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
PD98059 inhibits EGF-induced nuclear translocation of multifunctional protein CAD
-
additional information
-
indirubin-3'-monoxime is no inhibitor of MAPK2/ERK2
-
additional information
-
PD98059 and U0126 inhibit EGF-induced phosphorylation of Smad3
-
additional information
-
no inhibition by AMP and adenine
-
additional information
structural basis for inhibitor selectivity for p38 over other MAPKs such as ERK or JNK, overview
-
additional information
-
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM; PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM; PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM; PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM; PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
-
downregulation of MAP kinase activity can be initiated by dephosphorylation through multiple serine/threonine phosphatases, tyrosine-specific phosphatases, and dual specificity phosphatases, i.e. MAP kinase phosphatases, leading to the formation of monophosphorylated MAP kinases
-
additional information
-
some monounsaturated fatty acids inhibit p38 MAPK via selective protein-lipid interactions
-
additional information
phosphorylation of the enzyme by MAPK kinase MEK activates the enzyme. U0126, a specific inhibitor of MEK (MAPK kinase), blocks the activation of MAPK3/1 and subsequently of EGF-mediated downstream MAPK3/1 pathway
-
additional information
phosphorylation of the enzyme by MAPK kinase MEK activates the enzyme. U0126, a specific inhibitor of MEK (MAPK kinase), blocks the activation of MAPK3/1 and subsequently of EGF-mediated downstream MAPK3/1 pathway
-
additional information
-
in vitro the recombinant phospholipase C-gamma1 activity is not inhibited by phosphorylation through activated ERK2
-
additional information
in vitro the recombinant phospholipase C-gamma1 activity is not inhibited by phosphorylation through activated ERK2
-
additional information
-
genes encoding Sef prevent dissociation of the MEK-ERK complex, thereby inhibiting translocation of ERK to the nucleus, but ERK can still signal to cytoplasmic targets
-
additional information
synthesis of benzothiazole based inhibitors of p38alpha MAP kinase
-
additional information
-
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk1; overexpression of PP2A or PP5 partially prevents Cd-induced activation of Erk2; overexpression of PP2A or PP5 partially prevents Cd-induced activation of JNK
-
additional information
-
pheromones can influence the phosphorylation of MAPKs
-
additional information
-
wild-type Hog1 phosphorylation is unaffected by 1-NM-PP1
-
additional information
Msg5 is a MAPK phosphatase that deactivates Fus3 by dephosphorylation. Building synthetic feedback loops by dynamically regulating recruitment of modulators to the Ste5 scaffold, negative- and positive-feedback loop design, leads to activation of inhibition of the Fus3, overview
-
additional information
-
Msg5 is a MAPK phosphatase that deactivates Fus3 by dephosphorylation. Building synthetic feedback loops by dynamically regulating recruitment of modulators to the Ste5 scaffold, negative- and positive-feedback loop design, leads to activation of inhibition of the Fus3, overview
-
additional information
-
molecular mechanism of negative regulation of Ras/ERK signaling, Sef negatively regulates ERK phosphorylation by blocking dissocation of MEK and ERK
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
12-O-tetradecanoylphorbol-13-acetate
-
activates ERK1 and ERK2
arsenite
treatment of worms with arsenite, a toxic ROS-producing compound, induces a robust phosphorylation of PMK-1, induction of oxidative stress-responsive genes, and eventual lethality. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress
beta-phorbol-13-acetate
-
stimulates SERT phosphorylation
citrinin
-
the exposure of HEK-293 and HeLa cells to citrinin results in a dose-dependent increase in the phosphorylation of ERK1/2 and JNK
D-amphetamine
-
stimulates SERT phosphorylation
EGF
-
induces phosphorylation of Smad3
-
glial cell line-derived neurotrophic factor
-
GDNF
-
glucocorticoids
-
activate p38 MAPK, e.g. by induction of activating MKK3
-
hepatocyte
-
host hepatocytes lead to maximal induction of MPK1 phosphorylation
-
Insulin
-
causes weak activation
-
interleukin-1beta
-
activates the MAPKs, dexamethasone inhibits this activation
-
MEF2D
-
is crucial for activating phosphorylation of substrates within a transcription complex by BMK1, possibly by anchoring BMK1 to specific genes
-
mitogen-activated protein kinase kinase 6
-
MKK6
-
mycosporine-glycine
mycosporine-like amino acids shinorine, mycosporine-glycine, and porphyra are purified from Chlamydomonas hedlyei and Porphyra yezoensis activate kinase ERK and JNK, especially JNK
N-acetylsphingosine
-
i.e. C2-ceramide, an intracellular mediator of apoptosis, cell-permeable N-acetylsphingosine activates mitochondrial p38 MAPK
nerve growth factor
-
alters outcome of ERK signaling
-
neurotrophic growth factor
-
NGF
-
palmitate
-
activates p38 MAPK phosphorylation and activates it
phenethyl isothiocyanate
-
the enzyme is activated by exposure to 0.02 mM phenethyl isothiocyanate
porphyra
mycosporine-like amino acids shinorine, mycosporine-glycine, and porphyra are purified from Chlamydomonas hedlyei and Porphyra yezoensis activate kinase ERK and JNK, especially JNK
Porphyromonas gingivalis supernatant
-
-
-
purvalanol
-
17% activation of SAPK2b/p38beta
serum
-
host serum positively effects MPK1 phosphorylation
-
shinorine
mycosporine-like amino acids shinorine, mycosporine-glycine, and porphyra are purified from Chlamydomonas hedlyei and Porphyra yezoensis activate kinase ERK and JNK, especially JNK
thapsigargin
-
stimulates 4-5fold the expression of p44/p42
transforming growth factor-beta
-
i.e. TGF-beta, activates p38, butenoside inhibits this activation
-
tumor necrosis factor-alpha
-
-
-
UV radiation
-
activates p38 MAPK mediated by protein kinases, overview
-
amitriptyline
-
up-regulates ERK1/2 phosphorylation and activity 8fold at 0.01 mM, the addition of nor-binaltorphimine (100 nM) reduces the amitriptyline stimulatory effect by 70%
amitriptyline
-
up-regulates ERK1/2 phosphorylation and activity 8fold at 0.01 mM, the addition of nor-binaltorphimine (100 nM) reduces the amitriptyline stimulatory effect by 70%
cytokines
-
-
Epidermal growth factor
-
MPK1 is responsive to exogenous host epidermal growth factor, which increases MPK1 phosphorylation
Epidermal growth factor
-
induces potent transient activation of the ERK pathway
MKK3
activates
-
MKK3
strongly activates
-
MKK3
activation of p38alpha occurs through bisphosphorylation by the dual-specificity Ser/Thr MAP kinases MKK3 and MKK6 on the Thr180-Gly181-Tyr182 motif located on the activation loop
-
MKK6
-
-
-
MKK6
strongly activates
-
MKK6
activation of p38alpha occurs through bisphosphorylation by the dual-specificity Ser/Thr MAP kinases MKK3 and MKK6 on the Thr180-Gly181-Tyr182 motif located on the activation loop
-
Ras
Ras induces phosphorylation of c-Jun by JNKs
-
Ras
-
Ras induces phosphorylation of c-Jun by JNKs
-
Ras
-
essential for ERK activation, the three isoforms N-Ras, K-Ras and H-Ras have an important role in spatial and temporal ERK signaling
-
sorbitol
-
upon exposure to 1000 mM sorbitol, Hog1 is phosphorylated rapidly, with modification peaking at 10 to 20 min and then declining as cells adapt
TNF-alpha
-
-
-
TNF-alpha
-
activates p38 MAP kinase 6fold in neutrophils
-
TNF-alpha
-
activates the MAPKs, dexamethasone inhibits this activation
-
TNF-alpha
-
p38 MAP kinase is significantly activated by TNF-alpha, however, activation of ERK1/2 and JNK remain essentially unchanged. TNF-alpha-induced phosphorylation of the p38 MAP kinase is inhibited by SB203580
-
TNF-alpha
-
activates p38 MAPK mediated by protein kinases MKK3, MKK4, and MKK6, overview
-
additional information
-
MPK6 is activated by MKK4 MAPK kinase
-
additional information
MPK6 is activated by MKK4 MAPK kinase
-
additional information
pathogen-associated molecular patterns (PAMPs) are recognized by plant pattern recognition receptors to activate PAMP-triggered immunity. PAMP perception enhances phosphorylation of BES1. Flagellin perception, e.g. of Flg22, enhances BES1 phosphorylation. Enzyme MKK5 phosphorylates and activates MPK6
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK3 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK3 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK3 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
-
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK3 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK4 is activated by constitutively active MKK1 and MKK2, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK4 is activated by constitutively active MKK1 and MKK2, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK4 is activated by constitutively active MKK1 and MKK2, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
-
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK4 is activated by constitutively active MKK1 and MKK2, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK6 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK6 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK6 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
-
the enzyme is phosphorylated and activated by a mitogen-activated protein kinase kinase, GST-tagged MPK6 is activated by constitutively active MKK4 and MKK5, which cause a dual phosphorylation of the TEY motif in the activation loop
-
additional information
-
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
JNK-1 is activated by phosphorylation, ambient temperature of 1-37°C specifically influences the activation/phosphorylation of the MAPkinase JNK-1
-
additional information
-
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
C493C.10 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-5
-
additional information
-
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
jnk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-4. Activation of JNK signaling occurs under conditions of heavy metal stress
-
additional information
-
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
kgb-1 is phosphorylated and activated by mitogen-activated protein kinase kinase jkk-1
-
additional information
-
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
kgb-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-3
-
additional information
-
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
pmk-1 is phosphorylated and activated by mitogen-activated protein kinase kinase mkk-4. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
-
additional information
-
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
pmk-2 is phosphorylated and activated by mitogen-activated protein kinase kinase sek-1
-
additional information
-
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
pmk-3 is phosphorylated and activated by mitogen-activated protein kinase kinase mek-1
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
-
Trichoderma inoculation increases MAPK mRNA levels, hormones JA or SA do not affect the TIPK expression in roots, expression of TIPK in roots of Trichoderma inoculated and Psl-challenged plants is higher than in plants subjected to only one of those treatments, leaves of Trichoderma inoculated plants do not differ in TIPK expression level from the controls, leaves of plants inoculated with Trichoderma and challenged with Psl express 3- to 4fold higher TIPK mRNA levels than plants challenged only with Psl
-
additional information
-
phosphorylation activates ERK
-
additional information
addition of lipopolysaccharide does not significantly affect the phosphorylation of Dp38 in the LPS-responsive l(2)mbn cell line
-
additional information
-
activation mechanism, phosphorylation/activation of ERK1 and ERK2 by the MAPK kinase-1
-
additional information
-
phosphorylation activates the enzyme
-
additional information
-
the enzyme is activated by mitogens, activation is induced by epidermal growth factor tyrosine protein kinase and nucelar growth factor tyrosine protein kinase
-
additional information
-
p38 MAPK is activated by phosphorylation
-
additional information
-
mechanical strain activates ERK but not p38 MAPK. ERK1/2, but not p38 MAPK, exhibits dose-dependent FGF2-, epidermal growth factor- or sodium pervanadate-induced activation
-
additional information
-
-
additional information
-
-
additional information
-
-
-
additional information
activated by cellular stress and proinflammatory cytokines
-
additional information
-
activated by cellular stress and proinflammatory cytokines
-
additional information
activated by dual phosphorylation at Thr and Tyr during the UV response. Ha-Ras partially activates JNK1 and potentiates the activation caused by UV
-
additional information
when expressed in KB cells, SAPK4 is activated in response to cellular stresses and pro-inflammatory cytokines
-
additional information
when expressed in KB cells, SAPK4 is activated in response to cellular stresses and pro-inflammatory cytokines
-
additional information
-
when expressed in KB cells, SAPK4 is activated in response to cellular stresses and pro-inflammatory cytokines
-
additional information
activated by a group of extracellular stimuli including cytokines and environmental stresses
-
additional information
p38beta is activated by proinflammatory cytokines and environmental stress
-
additional information
-
p38beta is activated by proinflammatory cytokines and environmental stress
-
additional information
-
activation of the Ca2+-dependent signaling and expression of interleukin-8 in 1HAEo cells by EGTA at 1 mM and NiCl2 at 5-500 nM
-
additional information
-
ERK phosphorylation activates the enzyme activity, stimulation by 7TMD receptors, e.g. the serotonin 5-HT2c receptor
-
additional information
interaction motifs, i.e. docking sites or recognition sequences, of substrates are crucial for MAPK activity, i.e. motif Leu-Xaa-Leu preceded by 3-5 basic residues, overview
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
-
MAPKs are up-regulated by upstream kinases such as BRAF and KRAS
-
additional information
-
oxidative stress activates the MAPKs, dexamethasone inhibits this activation
-
additional information
-
p38 expression and activity in signaling in erythroid cells is independent of erythropoietin
-
additional information
-
p38 is activated by phosphorylation through kinase Src, EC 2.7.10.2, mechanical pressure on the cell induces p38alpha and beta isozyme phosphorylation, which is suppressed by PKC isozymes, EC 2.7.11.13
-
additional information
-
p38 MAPk is activated through phosphorylation by MKK3, a MAPK kinase EC 2.7.11.25
-
additional information
-
the recombinant detagged enzyme is activated by specific phosphorylation at Thr180 and Tyr182 through recombinant GST-tagged MKK6 mutant S207E/T211E
-
additional information
-
increased ability of phosphorylated ERK2 to dimerize as the salt concentration is increased, ERK2 fails to dimerize in the presence of EDTA and EGTA
-
additional information
-
MKK6-DD phosphorylates the p38a-MK2 heterodimer
-
additional information
-
MKP5 regulates the signaling activity of the MAP kinase
-
additional information
-
arsenic trioxide induces apoptosis and mitogen-activated protein kinases in promyelocytes and cancer cells. It enhances adhesion, migration, phagocytosis, release, and activity of gelatinase and degranulation of secretory, specific, and gelatinase, but not azurophilic granules, and is dependent upon activation of p38 and/or JNK. Activation of p38 and JNK is not associated with the ability of arsenic trioxide to induce human neutrophil apoptosis
-
additional information
phosphorylation activates MAPKs, PD98059 inhibits ERK1/2 phosphorylation by MEK1/2, i.e. mitogen-activated kinase-extracellular signal-regulated kinase kinase, p38 MAPK is activated in asthma patient airway cells, overview
-
additional information
phosphorylation activates MAPKs, PD98059 inhibits ERK1/2 phosphorylation by MEK1/2, i.e. mitogen-activated kinase-extracellular signal-regulated kinase kinase, p38 MAPK is activated in asthma patient airway cells, overview
-
additional information
-
phosphorylation activates MAPKs, PD98059 inhibits ERK1/2 phosphorylation by MEK1/2, i.e. mitogen-activated kinase-extracellular signal-regulated kinase kinase, p38 MAPK is activated in asthma patient airway cells, overview
-
additional information
phosphorylation at the activation loop residue Y185 by MKK4 activates JNK
-
additional information
-
phosphorylation at the activation loop residue Y185 by MKK4 activates JNK
-
additional information
-
activated by a range of stress stimuli
-
additional information
-
activated by a range of stress stimuli, such as heat shock, irradiation, hypoxia, chemotoxins, and peroxides, also activated in response to various cytokines
-
additional information
-
activated by growth factors, cellular stresses, and cytokines
-
additional information
-
activated by phosphorylation
-
additional information
-
activated by phosphorylation
-
additional information
-
JNK can be activated in response to various stimuli such as environmental stress, cytokines and fatty acids
-
additional information
JNK can be activated in response to various stimuli such as environmental stress, cytokines and fatty acids
-
additional information
-
the MAPK pathway is also activated after exposure to ionizing radiation
-
additional information
activation of ERK by FAK in turn phosphorylates FAK at S910, which promotes the disassembly of focal adhesion (hemidesmosome disruption) during cell migration
-
additional information
activation of ERK by FAK in turn phosphorylates FAK at S910, which promotes the disassembly of focal adhesion (hemidesmosome disruption) during cell migration
-
additional information
activation of ERK by FAK in turn phosphorylates FAK at S910, which promotes the disassembly of focal adhesion (hemidesmosome disruption) during cell migration
-
additional information
-
ERK1/2 are phosphorylated and activated by MAPK kinases MEK1/MEK2
-
additional information
-
p38 is phosphorylated and activated by MAPK kinases MEK
-
additional information
p38gamma is phosphorylated and activated by MAPK kinase MKK6
-
additional information
-
p38gamma is phosphorylated and activated by MAPK kinase MKK6
-
additional information
the JNK1 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the JNK1 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the JNK1 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the JNK2 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the JNK2 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the JNK2 MAPK is activated by phosphorylation through MKK4 and MKK7
-
additional information
the p38 MAPK is activated by phosphorylation through MKK3, MKK6, and MKK4
-
additional information
the p38 MAPK is activated by phosphorylation through MKK3, MKK6, and MKK4
-
additional information
the p38 MAPK is activated by phosphorylation through MKK3, MKK6, and MKK4
-
additional information
-
autoregulation by a pseudosubstrate mechanism, overview
-
additional information
-
phosphorylation at Thr183 and Tyr185 activates the enzyme
-
additional information
-
AP1 and NF-kappaB recruit p38 MAPK to activate TBP
-
additional information
-
some heavy metals induce MAPK pathways in the plant
-
additional information
-
ERK2 is activated by phosphorylation
-
additional information
-
inhibition of the phosphatidylserine-receptor activates ERK and TGF-beta production in vivo
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
-
mechanism of p38 MAP kinase activation in vivo, coordinated and selective actions of protein kinases MKK3, MKK4, and MKK6 in response to cytokines and exposure to environmental stress are part of the regulation, overview
-
additional information
-
the recombinant detagged enzyme is activated by specific phosphorylation at Thr180 and Tyr182 through recombinant GST-tagged MKK6 mutant S207E/T211E
-
additional information
-
full activation of the MAP kinases requires dual phosphorylation of the Thr and Tyr residues in the TXY motif of the activation loop by MAP kinase kinases, p38alpha phosphorylated at both Thr180 and Tyr182 is 10-20fold more active than p38alpha phosphorylated at Thr180 only, p38alpha phosphorylation by MKK6
-
additional information
-
H2O2 and 4-hydroxy-2-nonenal increase phosphorylation and activation of p38 MAPK, but not of ERK1/2
-
additional information
H2O2 and 4-hydroxy-2-nonenal increase phosphorylation and activation of p38 MAPK, but not of ERK1/2
-
additional information
H2O2 and 4-hydroxy-2-nonenal increase phosphorylation and activation of p38 MAPK, but not of ERK1/2
-
additional information
-
lipolysaccharide induces the MAPK activation, which is inhibited by lignocaine in case of ERK and p38, but not of JNK, overview
-
additional information
-
MAPKs are activated by phosphorylation through MAPK kinases
-
additional information
MAPKs are activated by phosphorylation through MAPK kinases
-
additional information
MAPKs are activated by phosphorylation through MAPK kinases
-
additional information
MAPKs are activated by phosphorylation through MAPK kinases
-
additional information
MAPKs are activated by phosphorylation through MAPK kinases, overview. TNF induces p38 MAP kinase, JNK is induced by TNF and lipopolysaccharide
-
additional information
-
no activation JNK1 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
no activation JNK1 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
no activation JNK1 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
-
no activation JNK2 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
no activation JNK2 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
no activation JNK2 by H2O2 and 4-hydroxy-2-nonenal
-
additional information
-
activated by infection or cellular stressors such as mechanical wear, heat, or osmotic shock
-
additional information
-
p38 MAPK is activated by phosphorylation. Inhibition of SCD-1 decreases the proportion of monounsaturated fatty acid-containing phospholipids and activates p38 MAPK
-
additional information
the ERK2 MAPK is activated by phosphorylation through MEK1 and MEK2
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
phosphorylation of the enzyme by MAPK kinase MEK activates the enzyme. U0126, a specific inhibitor of MEK (MAPK kinase), blocks the activation of MAPK3/1 and subsequently of EGF-mediated downstream MAPK3/1 pathway
-
additional information
phosphorylation of the enzyme by MAPK kinase MEK activates the enzyme. U0126, a specific inhibitor of MEK (MAPK kinase), blocks the activation of MAPK3/1 and subsequently of EGF-mediated downstream MAPK3/1 pathway
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
-
p38 MAPK needs to be activated by phosphorylation
-
additional information
-
tert-butyl hydroperoxide, causing oxidative stress incells, induces activation of ERK and p38 MAP kinase by increased phosphorylation, MAPKs are activated in response to intracellular reactive species, MAPK signaling cascade activation mechanism, overview
-
additional information
-
cell-surface receptor density, expression of scaffolding proteins, the surrounding extracellular matrix, and the interplay between kinases and phosphatases modulate the strength and duration of ERK signaling, c-Fos transcription factor can function as a sensor for ERK activation dynamics
-
additional information
-
activated by phosphorylation
-
additional information
-
arterial injury activates the mitogen-activated ERK kinase/extracellular signal-regulated kinase signaling pathway
-
additional information
-
extracts of cyanobacteria Microcystis aeruginosa and Aphanizomenon flos-aquae
-
additional information
-
JNK is activated by cellular stress, cytokines, and growth factors
-
additional information
-
pheromones can influence the phosphorylation of MAPKs, the scaffolding proteins Ste mediate MAPK function in signaling by recruitment of the kinases to reaction sites, e.g. the plasma membrane, or by concentrating and maybe also by orientating relevant reaction components, e.g. Ste5, overview
-
additional information
-
upon hyperosmotic stress, Hog1 is activated by phosphorylation
-
additional information
Fus3 is phosphorylated and activated by Ste7. Building synthetic feedback loops by dynamically regulating recruitment of modulators to the Ste5 scaffold, negative- and positive-feedback loop design, leads to activation of inhibition of the Fus3, overview
-
additional information
-
Fus3 is phosphorylated and activated by Ste7. Building synthetic feedback loops by dynamically regulating recruitment of modulators to the Ste5 scaffold, negative- and positive-feedback loop design, leads to activation of inhibition of the Fus3, overview
-
additional information
osmotic stress activates Hog1. Ste11 is a MAP kinase kinase kinase upstream of Hog1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
osmotic stress activates Hog1. Ste11 is a MAP kinase kinase kinase upstream of Hog1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
-
osmotic stress activates Hog1. Ste11 is a MAP kinase kinase kinase upstream of Hog1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
osmotic stress activates Kss1. Ste11 is a MAP kinase kinase kinase upstream of Kss1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
osmotic stress activates Kss1. Ste11 is a MAP kinase kinase kinase upstream of Kss1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
-
osmotic stress activates Kss1. Ste11 is a MAP kinase kinase kinase upstream of Kss1. Ste50 is an adaptor protein required for the catalytic activity of Ste11
-
additional information
lipopolysaccharide, CpG oligonucleotides and recombinant trout IL-1beta induce endogenous phosphorylation of p38 in a dose-dependent manner
-
additional information
lipopolysaccharide, CpG oligonucleotides and recombinant trout IL-1beta induce endogenous phosphorylation of p38 in a dose-dependent manner
-
additional information
lipopolysaccharide, CpG oligonucleotides and recombinant trout IL-1beta induce endogenous phosphorylation of p38 in a dose-dependent manner
-
additional information
-
lipopolysaccharide, CpG oligonucleotides and recombinant trout IL-1beta induce endogenous phosphorylation of p38 in a dose-dependent manner
-
additional information
-
activation of MAPKs from photoautotrophic cultures of tomato by treatment with E-Fol, the elicitor preparation of the wilt-inducing fungus Fusarium oxysporum lycopersici
-
additional information
-
MAPKs are activated by phosphorxylation through MEK/MAPK kinases
-
additional information
-
the factors Sprouty1 and Sprouty2 are involved in ERK regulation, mechanism, phosphorylation activates ERK
-
additional information
enzyme is activated in vitro by the p42 and p44 isoforms of MAPK, p42/p44MAPK
-
additional information
-
ERK activation in oocytes can be bistable or irreversible owing to a strong positive feedback loop regulated by the Mos kinase
-
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0.000311
(1R)-2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
Homo sapiens
-
0.000235
(1R,2S)-2-[([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)methyl]cyclohexanol
Homo sapiens
-
0.000485
(2R)-2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
Homo sapiens
-
0.000023
(2S,3S)-2-[(R)-4-[4-(2-hydroxy-ethoxy)-phenyl]-2,5-dioxo-imidazolidin-1-yl]-3-phenyl-N-(4-propionyl-thiazol-2-yl)-butyramide
Homo sapiens
-
MEK1
0.000967
(3-amino-1-oxido-2-phenylpyridin-4-yl)(phenyl)methanone
Homo sapiens
-
0.00252
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.000041
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.000019
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.01
(hydroxy-2-naphthalenylmethyl)phosphonic acid
eukaryota
-
inhibits the insulin receptor tyrosine kinase, IC50 is 0.01 mM
0.0000035
(R)-2-(sec-butylamino)-N-(2-methyl-5-(methylcarbamoyl)phenyl) thiazole-5-carboxamide
Homo sapiens
-
-
0.0000008
1-((S)-4-(6-(3-(cyclopropylamino)-6-methylbenzo[d]isoxazol-7-yl)phthalazin-1-yl)-3-methylpiperazin-1-yl)ethanone
Homo sapiens
THP-1 cells
0.000822
1-(2,6-dichloro-phenyl)-1-(4-(4-fluorophenyl)thiazol-2-yl)urea
Homo sapiens
-
0.0000043 - 0.00016
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
0.000146
1-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-2-ol
Homo sapiens
-
0.000021
1-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-2-ol
Homo sapiens
-
0.05
1-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
larger than 0.050
0.05
2,2'-disulfanediylbis(1,3-benzothiazole)
Homo sapiens
-
-
0.000333
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00315
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.0037
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
Mus musculus
-
-
0.00156
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
-
0.000436
2-(benzyloxy)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.00033
2-(ethylamino)-N-[5-(ethylcarbamoyl)-2-methylphenyl]-4-methyl-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.000087
2-(ethylsulfanyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.000292
2-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
Homo sapiens
-
0.000034
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)-3-methylbutan-1-ol
Homo sapiens
-
0.00001
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)butan-1-ol
Homo sapiens
-
0.000045
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)ethanol
Homo sapiens
-
0.000006
2-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
Homo sapiens
-
0.00031 - 0.00033
2-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-5-carboxamide
0.001
2-chloro-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.00037
2-chloro-4-[4-(4-fluorophenyl)-2-(phenylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.0011
2-fluoro-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.00066
2-fluoro-4-[2-(phenylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.00056
2-fluoro-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.00021
2-fluoro-4-[4-(4-fluorophenyl)-2-(phenylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.000641
2-[(1,5-dimethylhexyl)oxy]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridine
Homo sapiens
-
0.0000042
2-[(1-methylethyl)amino]-N-[2-methyl-5-(1H-pyrazol-5-ylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000035
2-[(1-methylethyl)amino]-N-[2-methyl-5-(methylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000054
2-[(1-methylethyl)amino]-N-[2-methyl-5-[(1-methyl-1H-pyrazol-5-yl)carbamoyl]phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.00013
2-[(2,4-difluorophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
Mammalia
-
-
0.00253
2-[(2,4-difluorophenyl)amino]-5H-dibenzo[a,d][7]annulen-5-one
Mammalia
-
-
0.1
2-[(2,4-dinitrophenyl)sulfanyl]-1,3-benzoxazole
Homo sapiens
-
larger than 0.100
0.00013
2-[(2-amino-4-fluorophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
Mammalia
-
-
0.0001
2-[(2-aminophenyl)amino]-10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-one
Mammalia
-
-
0.00106
2-[(2-aminophenyl)amino]-5H-dibenzo[a,d][7]annulen-5-one
Mammalia
-
-
0.000022
2-[(2-methoxyethyl)amino]-N-[2-methyl-5-(methylcarbamoyl)phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0018
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
-
0.0027
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
Homo sapiens
-
-
0.0081
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
-
0.05
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole-5-sulfonic acid
Homo sapiens
-
larger than 0.050
0.0202
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-5-(trifluoromethyl)-1H-benzimidazole
Homo sapiens
-
-
0.0042
2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl][1,3]thiazolo[4,5-b]pyridine
Homo sapiens
-
-
0.000026
3-(3-bromo-4-[(2,4-difluorobenzyl)oxy]-6-methyl-2-oxopyridin-1(2H)-yl)-N,4-dimethylbenzamide
Homo sapiens
-
-
0.000038
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00319
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00614
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.001
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzamide
Homo sapiens
above
0.001
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzonitrile
Homo sapiens
above
0.000031
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl)benzamide
Homo sapiens
-
0.0000544
3-([4-[2-(cyclopropylamino)pyrimidin-4-yl]-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl)benzonitrile
Homo sapiens
-
0.000209
3-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexanol
Homo sapiens
-
-
0.000015
3-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)propan-1-ol
Homo sapiens
-
0.0000276
3-([5-[2-(cyclopropylamino)pyrimidin-4-yl]-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzamide
Homo sapiens
-
0.0000626
3-([5-[2-(cyclopropylamino)pyrimidin-4-yl]-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl)benzonitrile
Homo sapiens
-
0.0064 - 0.0071
3-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]benzamide
0.00024
3-[(2,4-difluorophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
Mammalia
-
-
0.00004
3-[(2-amino-4-fluorophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
Mammalia
-
-
0.0003
3-[(2-aminophenyl)amino]dibenzo[b,e]oxepin-11(6H)-one
Mammalia
-
-
0.000061
3-[(4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-yl)amino]propan-1-ol
Homo sapiens
-
0.00011
3-[2-(cyclopropylamino)-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]-N,4-dimethylbenzamide
Homo sapiens
-
-
0.000053
3-[2-(cyclopropylamino)-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]-N-ethyl-4-methylbenzamide
Homo sapiens
-
-
0.000029
3-[4-(N-benzyl-N-methylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.00004
3-[4-(N-benzylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000084
3-[4-(N-tert-butylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.001
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
above
0.001
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.000028
3-[[4-(2-aminopyrimidin-4-yl)-5-(4-fluorophenyl)-1H-imidazol-2-yl]methyl]benzonitrile
Homo sapiens
-
0.000225
3-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
-
0.00026
3-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.0000551
3-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
-
0.00014
3-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.000191
3-[[4-(4-fluorophenyl)-5-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.000344
3-[[5-(2-aminopyrimidin-4-yl)-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
-
0.000101
3-[[5-(2-aminopyrimidin-4-yl)-4-(4-fluorophenyl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.001
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
above
0.001
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.0000485
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzamide
Homo sapiens
-
0.0000628
3-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzonitrile
Homo sapiens
-
0.001
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
above
0.001
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.000078
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzamide
Homo sapiens
-
0.0000954
3-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-2-yl]methyl]benzonitrile
Homo sapiens
-
0.001
3-[[5-(4-fluorophenyl)-4-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.000148
3-[[5-(4-fluorophenyl)-4-[2-[(4-methoxybenzyl)amino]pyrimidin-4-yl]-1H-imidazol-2-yl]methyl]benzonitrile
Homo sapiens
-
0.00028 - 0.0005
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3,4-thiadiazol-2-yl)sulfanyl]-4H-1,2,4-triazol-3-ol
0.000002
4-([4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
Homo sapiens
-
0.0018
4-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-2-carboxamide
Homo sapiens
-
0.1
4-[(1H-benzimidazol-2-ylsulfanyl)methyl]benzoic acid
Homo sapiens
-
larger than 0.100
0.0029
4-[2-(benzylsulfanyl)-4-(4-fluorophenyl)-1H-imidazol-5-yl]-2-chloropyridine
Homo sapiens
-
0.00026
4-[2-(benzylsulfanyl)-4-(4-fluorophenyl)-1H-imidazol-5-yl]-2-fluoropyridine
Homo sapiens
-
0.00195
4-[2-(benzylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-2-fluoropyridine
Homo sapiens
-
0.000248
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)pyridin-2-amine
Homo sapiens
-
0.000199
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
Homo sapiens
-
0.000093
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(2-phenylethyl)pyridin-2-amine
Homo sapiens
-
0.000239
4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]-N-(thiophen-2-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.00092
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)pyrimidin-2-amine
Homo sapiens
-
-
0.0011
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclohexylpyrimidin-2-amine
Homo sapiens
-
-
0.00046
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclopentylpyrimidin-2-amine
Homo sapiens
-
-
0.00084
4-[3-(4-chlorophenyl)-1H-pyrazol-4-yl]-N-cyclopropylpyrimidin-2-amine
Homo sapiens
-
-
0.00045
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
Mus musculus
-
0.000006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
Mus musculus
-
0.00006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
Mus musculus
-
0.000238
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.00072
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
Mus musculus
-
-
0.000794
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
Mus musculus
-
-
0.000642
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
Mus musculus
-
-
0.000081
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
Mus musculus
-
-
0.00479
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.000431
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.00159
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00576
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000042
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-3-methyl-N-(2-morpholin-4-ylethyl)benzamide
Homo sapiens
-
0.000491
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-3-methylbenzoic acid
Homo sapiens
-
0.00007
4-[3-amino-4-(2,4-difluorobenzoyl)-1-oxidopyridin-2-yl]-N-(2-methoxyethyl)-3-methylbenzamide
Homo sapiens
-
0.000038
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
Homo sapiens
-
0.000051
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-phenylpyridin-2-amine
Homo sapiens
-
0.00004
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
Homo sapiens
-
0.00061
4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
Homo sapiens
-
0.00022
4-[4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
Homo sapiens
-
0.00007
4-[4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
Homo sapiens
-
0.00096
4-[4-(4-fluorophenyl)-1-methyl-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
Homo sapiens
-
0.000639
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(1-phenylethoxy)pyridine
Homo sapiens
-
0.000033
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(4-methylphenoxy)pyridine
Homo sapiens
-
0.000542
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(tetrahydrofuran-2-ylmethoxy)pyridine
Homo sapiens
-
0.000424
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-2-(thiophen-2-ylmethoxy)pyridine
Homo sapiens
-
0.000023
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1,2,2-trimethylpropyl)pyridin-2-amine
Homo sapiens
-
0.000047
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1,2,3,4-tetrahydronaphthalen-1-yl)pyridin-2-amine
Homo sapiens
-
0.000013
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-methyl-3-phenylpropyl)pyridin-2-amine
Homo sapiens
-
0.00038
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylethyl)pyridin-2-amine
Homo sapiens
-
0.000068
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(1-phenylpropyl)pyridin-2-amine
Homo sapiens
-
0.000023
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-methylbutyl)pyridin-2-amine
Homo sapiens
-
0.000013
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-methylcyclohexyl)pyridin-2-amine
Homo sapiens
-
0.000017
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-phenylpropyl)pyridin-2-amine
Homo sapiens
-
0.000023
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(2-thiophen-2-ylethyl)pyridin-2-amine
Homo sapiens
-
0.00009
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(3-methylbutyl)pyridin-2-amine
Homo sapiens
-
0.000015 - 0.000031
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(4-methylcyclohexyl)pyridin-2-amine
0.00006
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(furan-2-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.000171
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(naphthalen-1-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.00007
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-2-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.000098
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-3-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.000119
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(pyridin-4-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.00005
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
Homo sapiens
-
0.000035
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(tetrahydrofuran-2-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.000046
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(thiophen-2-ylmethyl)pyridin-2-amine
Homo sapiens
-
0.000113
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-[(5-methylfuran-2-yl)methyl]pyridin-2-amine
Homo sapiens
-
0.000211
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
Mus musculus
-
-
0.00946
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
Mus musculus
-
-
0.000412
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.07
4-[[(6-amino-9H-purin-8-yl)sulfanyl]methyl]benzoic acid
Homo sapiens
-
-
0.000916
4-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
-
0.000859
4-[[4-(4-fluorophenyl)-5-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.0000556
4-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
-
0.0000871
4-[[4-(4-fluorophenyl)-5-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
-
0.001
4-[[5-(4-fluorophenyl)-4-(2-hydroxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.001
4-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
above
0.001
4-[[5-(4-fluorophenyl)-4-(2-methoxypyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzonitrile
Homo sapiens
above
0.001
4-[[5-(4-fluorophenyl)-4-(2-[[(1S)-1-phenylethyl]amino]pyrimidin-4-yl)-1H-imidazol-1-yl]methyl]benzamide
Homo sapiens
above
0.023
5,6-dichloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
-
0.00047 - 0.01
5-(5-nitrothiazol-2-ylthio)-N-((tetrahydrofuran-2-yl)methyl)-1,3,4-thiadiazol-2-amine
0.00029 - 0.0067
5-(5-nitrothiazol-2-ylthio)-N-propyl-1,3,4-thiadiazol-2-amine
0.0058 - 0.011
5-(acetylamino)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.00026 - 0.00035
5-(difluoromethyl)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.0032 - 0.0048
5-benzyl-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.0041 - 0.0099
5-bromo-N-(3-chloro-2-piperazin-1-ylphenyl)furan-2-carboxamide
0.00006 - 0.00009
5-bromo-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.02
5-bromo-N-[2-(4-prop-2-en-1-ylpiperazin-1-yl)-3-(trifluoromethyl)phenyl]furan-2-carboxamide
Homo sapiens
larger than 0.020
0.02
5-bromo-N-[2-(4-prop-2-en-1-ylpiperazin-1-yl)biphenyl-3-yl]furan-2-carboxamide
Homo sapiens
larger than 0.020
0.02
5-bromo-N-[3-(phenylamino)-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
larger than 0.020
0.02
5-bromo-N-[3-bromo-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
larger than 0.020
0.00018 - 0.00096
5-bromo-N-[3-chloro-2-(4-cyclopropylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00036 - 0.0011
5-bromo-N-[3-chloro-2-(4-ethylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00036 - 0.0012
5-bromo-N-[3-chloro-2-(4-methylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00024 - 0.00033
5-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00014 - 0.00016
5-bromo-N-[3-chloro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00063 - 0.0009
5-bromo-N-[3-chloro-2-(4-propylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.001 - 0.0012
5-bromo-N-[3-chloro-2-(4-pyridin-2-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.0015 - 0.0022
5-bromo-N-[3-chloro-2-[4-(1-methylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
0.0004 - 0.00054
5-bromo-N-[3-chloro-2-[4-(2-methylprop-2-en-1-yl)piperazin-1-yl]phenyl]furan-2-carboxamide
0.0009 - 0.0014
5-bromo-N-[3-chloro-2-[4-(2-phenylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
0.00025 - 0.00027
5-bromo-N-[3-chloro-2-[4-(furan-2-ylmethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
0.02
5-bromo-N-[3-chloro-2-[4-(trifluoroacetyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
larger than 0.020
0.00011 - 0.00029
5-bromo-N-[3-fluoro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.00018 - 0.0002
5-bromo-N-[3-methyl-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
0.05
5-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.027
5-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
Homo sapiens
-
-
0.00004 - 0.00008
5-chloro-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.00021 - 0.00023
5-cyano-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
0.0018
5-methoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
-
0.0047
5-methoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
-
0.0038
5-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
-
0.0064
5-nitro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1H-benzimidazole
Homo sapiens
-
-
0.000022
5-tert-butyl-N-cyclopropyl-2-methoxy-3-[2-[4-(2-morpholin-4-yl-ethoxy)-naphthalen-1-yl]-2-oxo-acetylamino]-benzamide
Homo sapiens
-
-
0.0000004
6-(3-(cyclopropylamino)-6-methylbenzo[d]isoxazol-7-yl)-N,N-dimethylphthalazin-1-amine
Homo sapiens
THP-1 cells
0.002
6-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]pyridine-2-carboxamide
Homo sapiens
-
0.05
6-chloro-2-[(4-methyl-5-thiophen-2-yl-4H-1,2,4-triazol-3-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.05
6-chloro-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.05
6-chloro-2-[[4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-methyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.05
6-chloro-2-[[5-(2,4-dichlorophenyl)-4-methyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.05
6-chloro-2-[[5-(2-methoxyphenyl)-4-phenyl-4H-1,2,4-triazol-3-yl]sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.0000013
6-chloro-N-cyclopropyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.0000036
6-chloro-N-isopropyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.05
6-ethoxy-1,3-benzothiazole-2-sulfonamide
Homo sapiens
-
larger than 0.050
0.05
6-ethoxy-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzothiazole
Homo sapiens
-
larger than 0.050
0.05
6-methyl-2-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-1,3-benzoxazole
Homo sapiens
-
larger than 0.050
0.00012
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-1H-indazol-3-amine
Homo sapiens
THP-1 cells
0.000029
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isothiazol-3-amine
Homo sapiens
THP-1 cells
0.0000036
6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.055
6-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-9H-purin-2-amine
Homo sapiens
-
-
0.000175
6-[1-(2-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.00002
6-[1-(2-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000072
6-[1-(3-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000033
6-[1-(3-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.001
6-[1-(4-chlorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
above, inhibition of p38alpha MAP kinase
0.000048
6-[1-(4-fluorophenyl)-1H-pyrazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000016
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000047
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazole
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000064
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.00001
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000065
6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000033
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000027
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1R)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000016
6-[4-(2-fluorophenyl)-1H-imidazol-5-yl]-N-[(1S)-1-methylpropyl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000017
6-[5-amino-1-ethyl-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000011
6-[5-amino-3-(2-fluorophenyl)-1-methyl-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000037
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-(1-methylethyl)-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000032
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1R)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000055
6-[5-amino-3-(2-fluorophenyl)-1H-pyrazol-4-yl]-N-[(1S)-1-methylpropyl]-2,3-dihydro-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.05
6-[5-[(6-chloro-1,3-benzothiazol-2-yl)sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl]quinoline
Homo sapiens
-
larger than 0.050
0.0000007
7-(1-isopropoxyphthalazin-6-yl)-N,6-dimethylbenzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.0000011
7-(1-isopropylphthalazin-6-yl)-N,6-dimethylbenzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.00024
8-[(2,4-difluorophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
Mammalia
-
-
0.00033
8-[(2,4-difluorophenyl)amino]-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
Mammalia
-
-
0.00018
8-[(2,4-difluorophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
Mammalia
-
-
0.00119
8-[(2-amino-4-fluorophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
Mammalia
-
-
0.00273
8-[(2-amino-4-fluorophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
Mammalia
-
-
0.00031
8-[(2-aminophenyl)amino]-10,11-dihydro-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
Mammalia
-
-
0.00195
8-[(2-aminophenyl)amino]-11H-benzo[5,6]cyclohepta[1,2-c]pyridin-11-one
Mammalia
-
-
0.00044
8-[(2-aminophenyl)amino]-5,6-dihydro-11H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-one
Mammalia
-
-
0.00108
8-[(2-aminophenyl)amino]-5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one
Mammalia
-
-
0.00268
8-[(2-aminophenyl)amino][1]benzoxepino[3,4-b]pyridin-5(11H)-one
Mammalia
-
-
0.027
8-[(5-nitro-1,3-thiazol-2-yl)sulfanyl]-9H-purin-6-amine
Homo sapiens
-
-
0.000011 - 0.000079
BIRB 796
0.000035
BIRB796
Homo sapiens
-
-
0.000039
C2-alkylaminothiazole
Homo sapiens
-
inhibition of isozyme p38 MAPK alpha
0.005
ethyl 1-[5-([5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]carbamoyl)-2-methylphenyl]-2,3-dihydro-1H-1,2,3-triazole-4-carboxylate
Homo sapiens
above, IC50 with THP-1 cells
0.00012
furan-2-carboxylic acid (3-[5-(4H-[1,2,4]triazol-3-yl)-1H-indazol-3-yl]-phenyl)-amide
Homo sapiens
-
0.00004 - 0.00009
II/SP600125
0.3 - 0.4
MKK4 mutant F48K
-
0.003 - 0.045
MKK4 mutant L44I
-
0.00063
ML3375
Homo sapiens
-
0.00004
ML3403
Homo sapiens
-
0.00011
N,4-dimethyl-3-[2-[(1-methylethyl)amino]-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
Homo sapiens
-
-
0.00027
N,4-dimethyl-3-[6-oxo-2-(propylamino)-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
Homo sapiens
-
-
0.000001
N,6-dimethyl-7-(1-((R)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.0000004
N,6-dimethyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.000034
N-(1,2-dimethylpropyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00138
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000011
N-(1,2-dimethylpropyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000348
N-(1,2-diphenylethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000026
N-(1,3-dimethylbutyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00002
N-(1,5-dimethylhexyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000314
N-(1-benzothiophen-2-ylmethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00215
N-(1-benzyl-2-phenylethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000036
N-(1-cyclohexylethyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000049
N-(1-methyl-4-phenylbutyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00602
N-(1-methylethyl)-4-[3-(6-methylpyridin-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.0035
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-2-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.000357
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.000814
N-(1-methylethyl)-4-[3-(tetrahydro-2H-pyran-4-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.000221
N-(1-methylethyl)-4-[3-[1-(methylsulfonyl)piperidin-4-yl]-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.000021
N-(1-methylethyl)-6-(1-phenyl-1H-pyrazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000021
N-(1-methylethyl)-6-(4-phenyl-1,3-oxazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000033
N-(1-methylethyl)-6-(4-phenyl-1H-imidazol-5-yl)-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000146
N-(1-methylethyl)-6-[1-(2-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.000033
N-(1-methylethyl)-6-[1-(3-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.001
N-(1-methylethyl)-6-[1-(4-methylphenyl)-1H-pyrazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
above, inhibition of p38alpha MAP kinase
0.000028
N-(2,3-dihydro-1H-inden-1-yl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000036
N-(2-chloro-6-methylphenyl)-2-(cyclobutylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.00014
N-(2-chloro-6-methylphenyl)-2-(ethylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.000062
N-(2-chloro-6-methylphenyl)-2-(phenylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.000028
N-(2-chloro-6-methylphenyl)-2-(propylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.000013
N-(2-chloro-6-methylphenyl)-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.00016 - 0.0048
N-(2-methoxyethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
0.000126
N-(3,3-dimethylbutyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.0001 - 0.0057
N-(3,4-dimethoxyphenethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
0.000173
N-(4-fluorobenzyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.0001 - 0.0091
N-(4-methoxybenzyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
0.00134
N-(4-tert-butylbenzyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00089
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
Mus musculus
-
0.0000041
N-(5-carbamoyl-2-methylphenyl)-2-(propylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000032
N-(5-carbamoyl-2-methylphenyl)-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000007
N-(6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)-benzo[d]isoxazol-3-yl)acetamide
Homo sapiens
THP-1 cells
0.00008
N-(cyclohexylmethyl)-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000191
N-(furan-2-ylmethyl)-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.0000013
N-(S)-sec-butyl-6-(6-methyl-3-(methylamino)benzo[d]isoxazol-7-yl)phthalazin-1-amine
Homo sapiens
THP-1 cells
0.000282
N-benzyl-4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00153
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000139
N-benzyl-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000042
N-cyclohexyl-4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.00002
N-cyclohexyl-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000245
N-cyclopentyl-4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-amine
Homo sapiens
-
-
0.0000006
N-cyclopropyl-6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.0000004
N-cyclopropyl-6-methyl-7-(1-o-tolylphthalazin-6-yl)benzo[d]-isoxazol-3-amine
Homo sapiens
THP-1 cells
0.000034
N-ethyl-4-methyl-3-[2-[(1-methylethyl)amino]-6-oxo-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
Homo sapiens
-
-
0.00016
N-ethyl-4-methyl-3-[6-oxo-2-(propylamino)-4,6-dihydro-5H-pyrrolo[3,4-d][1,3]thiazol-5-yl]benzamide
Homo sapiens
-
-
0.0001 - 0.1
N-ethyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
0.0000004
N-ethyl-6-methyl-7-(1-((S)-3-methylmorpholino)phthalazin-6-yl)benzo[d]isoxazol-3-amine
Homo sapiens
THP-1 cells
0.000012
N-ethyl-6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-1,3-benzothiazol-2-amine
Rattus norvegicus
inhibition of p38alpha MAP kinase
0.0000007
N-isopropyl-6-(6-methyl-3-(methylamino)benzo[d]isoxazol-7-yl)phthalazin-1-amine
Homo sapiens
THP-1 cells
0.00003
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
Mus musculus
-
0.000595
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000114
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00014 - 0.003
N-sec-butyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
0.000522
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.000522
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.000153
N-[(1R)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000359
N-[(1S)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-1-(2-methoxyethyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.000009
N-[(1S)-1-cyclohexylethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.02
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-(phenylamino)furan-2-carboxamide
Homo sapiens
larger than 0.020
0.001 - 0.0014
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-ethylfuran-2-carboxamide
0.00021 - 0.00041
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-fluorofuran-2-carboxamide
0.00045 - 0.00062
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methoxyfuran-2-carboxamide
0.00033 - 0.00053
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methylfuran-2-carboxamide
0.00011
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-prop-1-yn-1-ylfuran-2-carboxamide
Homo sapiens
-
0.000082
N-[2-(2,5-dimethylphenyl)ethyl]-4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-amine
Homo sapiens
-
0.0006 - 0.00081
N-[2-(4-acetylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
0.00088 - 0.0011
N-[2-(4-benzylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
0.0000045
N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-(propylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000023
N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-[[(1S)-1-methylpropyl]amino]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0023
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-4-carboxamide
Homo sapiens
-
0.0045 - 0.0089
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1H-pyrrole-2-carboxamide
0.0058
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-2-methyl-1,3-thiazole-4-carboxamide
Homo sapiens
-
0.02
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-5-cyanopyridine-2-carboxamide
Homo sapiens
larger than 0.020
0.0018 - 0.002
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-6-methylpyridine-2-carboxamide
0.005
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]isoxazole-5-carboxamide
Homo sapiens
-
0.02
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]pyrimidine-2-carboxamide
Homo sapiens
larger than 0.020
0.0003
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
-
0.000002
N-[5-(ethylcarbamoyl)-2-methylphenyl]-2-(propylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000034
N-[5-(ethylcarbamoyl)-2-methylphenyl]-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.00013
N-[5-(ethylcarbamoyl)-2-methylphenyl]-4-methyl-2-(propylamino)-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.0000038
N-[5-(isoxazol-3-ylcarbamoyl)-2-methylphenyl]-2-[(1-methylethyl)amino]-1,3-thiazole-5-carboxamide
Homo sapiens
-
-
0.000016
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1R)-1-cyclohexylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000066
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1S)-1-cyclohexylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000035
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[(1S)-2-(dimethylamino)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.00014
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[2-(dimethylamino)-2-methylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000022
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-(4-[N-[3-(dimethylamino)-2,2-dimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.00011
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-(N-cyclopropylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000014
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(2,2-dimethylpropyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000018
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(2-hydroxy-2-methylpropyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000014
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-3-[4-[N-(cyclohexylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]-4-methylbenzamide
Homo sapiens
IC50 with THP-1 cells
0.000028
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1-methylpiperidin-3-yl)methyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.0002
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1-methylpiperidin-4-yl)methyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.00004
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1R)-1,2,2-trimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.000013
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1R)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.000035
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1S)-1,2,2-trimethylpropyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.000027
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-(4-[N-[(1S)-1-phenylethyl]glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl)benzamide
Homo sapiens
IC50 with THP-1 cells
0.00011
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-(N-methylglycyl)-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
Homo sapiens
IC50 with THP-1 cells
0.000038
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-[N-(pyridin-3-ylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
Homo sapiens
IC50 with THP-1 cells
0.000074
N-[5-tert-butyl-2-methoxy-3-[(methylsulfonyl)amino]phenyl]-4-methyl-3-[4-[N-(pyridin-4-ylmethyl)glycyl]-2,3-dihydro-1H-1,2,3-triazol-1-yl]benzamide
Homo sapiens
IC50 with THP-1 cells
0.000299
N-[trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexyl]acetamide
Homo sapiens
-
-
0.000114
N-[trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexyl]methanesulfonamide
Homo sapiens
-
-
0.000015 - 0.000048
pyridinyl imidazole-type inhibitors
Mus musculus
IC50 of 15-48 nM
-
0.05
S-1,3-benzothiazol-2-yl (2Z)-(2-amino-1,3-thiazol-4-yl)(methoxyimino)ethanethioate
Homo sapiens
-
larger than 0.050
0.00008 - 0.00015
SB 203580
0.000026 - 0.0006
SB203580
0.002 - 0.005
SC68376
Homo sapiens
pH 7.2, 25°C
0.000025 - 0.00005
skepinone-L
Mus musculus
-
pH 7.4, 22°C
0.001
SKF86002
Homo sapiens
pH 7.2, 25°C
0.00048
SR3583
Homo sapiens
-
-
0.0063 - 0.02
tert-butyl 4-(2-[[(5-bromofuran-2-yl)carbonyl]amino]-6-chlorophenyl)piperazine-1-carboxylate
0.000259
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.000098
trans-4-([4-[3-(tetrahydro-2H-pyran-3-yl)-1H-pyrazol-4-yl]pyrimidin-2-yl]amino)cyclohexanol
Homo sapiens
-
-
0.00003
trans-4-([4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]pyridin-2-yl]amino)cyclohexanol
Homo sapiens
-
0.000608
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.000011
trans-4-[(4-[2-(methylsulfanyl)-4-[3-(trifluoromethyl)phenyl]-1H-imidazol-5-yl]pyridin-2-yl)amino]cyclohexanol
Homo sapiens
-
0.000024
[3-amino-2-(1,3-benzodioxol-4-yl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000037
[3-amino-2-(2,3-dimethoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000126
[3-amino-2-(2,4-difluorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000009
[3-amino-2-(2,6-dichlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000005
[3-amino-2-(2,6-difluoro-4-methoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000017
[3-amino-2-(2,6-difluorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000015
[3-amino-2-(2,6-dimethoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000017
[3-amino-2-(2,6-dimethylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000039
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000024
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-chlorophenyl)methanone
Homo sapiens
-
0.000149
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-methoxyphenyl)methanone
Homo sapiens
-
0.001655
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](2-trifluoromethylphenyl)methanone
Homo sapiens
-
0.000174
[3-amino-2-(2-chlorophenyl)-1-oxidopyridin-4-yl](phenyl)methanone
Homo sapiens
-
0.000208
[3-amino-2-(2-isopropylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000023
[3-amino-2-(2-methoxyphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000021
[3-amino-2-(2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000411
[3-amino-2-(2-methylphenyl)-1-oxidopyridin-4-yl](phenyl)methanone
Homo sapiens
-
0.000228
[3-amino-2-(3-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000038
[3-amino-2-(4-chloro-2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000802
[3-amino-2-(4-chlorophenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.00253
[3-amino-2-(4-chlorophenyl)-1-oxidopyridin-4-yl](phenyl)methanone
Homo sapiens
-
0.000008
[3-amino-2-(4-hydroxy-2-methylphenyl)-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.000014
[3-amino-2-[2-methyl-4-(2-morpholin-4-ylethoxy)phenyl]-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.00002
[3-amino-2-[4-(2-methoxyethoxy)-2-methylphenyl]-1-oxidopyridin-4-yl](2,4-difluorophenyl)methanone
Homo sapiens
-
0.0000001 - 0.00097
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
additional information
(2S)-2-([6-[(2-aminobenzyl)amino]-9-(1-methylethyl)-9H-purin-2-yl]amino)butan-1-ol
0.0000043
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
highly selective for p38 isozyme alpha wild-type with IC50 of 4.3 nM, respectively, no inhibition of JNK3, JNK2, and ERK
0.000061
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
IC50 for mutant G110A 61 nM
0.00016
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
IC50 mutant G110D 160 nM, respectively, no inhibition of JNK3, JNK2, and ERK
0.00031
2-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
0.00033
2-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1,3-thiazole-5-carboxamide
Homo sapiens
-
0.0064
3-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]benzamide
Homo sapiens
-
0.0071
3-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]benzamide
Homo sapiens
-
0.00028
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3,4-thiadiazol-2-yl)sulfanyl]-4H-1,2,4-triazol-3-ol
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.0005
4-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-[(5-nitro-1,3,4-thiadiazol-2-yl)sulfanyl]-4H-1,2,4-triazol-3-ol
Homo sapiens
-
-
0.000015
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(4-methylcyclohexyl)pyridin-2-amine
Homo sapiens
-
0.00002
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(4-methylcyclohexyl)pyridin-2-amine
Homo sapiens
-
0.000031
4-[4-(4-fluorophenyl)-2-(methylsulfanyl)-1H-imidazol-5-yl]-N-(4-methylcyclohexyl)pyridin-2-amine
Homo sapiens
-
0.00047
5-(5-nitrothiazol-2-ylthio)-N-((tetrahydrofuran-2-yl)methyl)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.01
5-(5-nitrothiazol-2-ylthio)-N-((tetrahydrofuran-2-yl)methyl)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.00029
5-(5-nitrothiazol-2-ylthio)-N-propyl-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.0067
5-(5-nitrothiazol-2-ylthio)-N-propyl-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.0058
5-(acetylamino)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.011
5-(acetylamino)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00026
5-(difluoromethyl)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00035
5-(difluoromethyl)-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.0032
5-benzyl-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.0048
5-benzyl-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.0041
5-bromo-N-(3-chloro-2-piperazin-1-ylphenyl)furan-2-carboxamide
Homo sapiens
-
0.0099
5-bromo-N-(3-chloro-2-piperazin-1-ylphenyl)furan-2-carboxamide
Homo sapiens
-
0.00006
5-bromo-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00009
5-bromo-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00018
5-bromo-N-[3-chloro-2-(4-cyclopropylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00096
5-bromo-N-[3-chloro-2-(4-cyclopropylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00036
5-bromo-N-[3-chloro-2-(4-ethylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0011
5-bromo-N-[3-chloro-2-(4-ethylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00036
5-bromo-N-[3-chloro-2-(4-methylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0012
5-bromo-N-[3-chloro-2-(4-methylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00024
5-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00033
5-bromo-N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00014
5-bromo-N-[3-chloro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00016
5-bromo-N-[3-chloro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00063
5-bromo-N-[3-chloro-2-(4-propylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0009
5-bromo-N-[3-chloro-2-(4-propylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.001
5-bromo-N-[3-chloro-2-(4-pyridin-2-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0012
5-bromo-N-[3-chloro-2-(4-pyridin-2-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0015
5-bromo-N-[3-chloro-2-[4-(1-methylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.0022
5-bromo-N-[3-chloro-2-[4-(1-methylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.0004
5-bromo-N-[3-chloro-2-[4-(2-methylprop-2-en-1-yl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.00054
5-bromo-N-[3-chloro-2-[4-(2-methylprop-2-en-1-yl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.0009
5-bromo-N-[3-chloro-2-[4-(2-phenylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.0014
5-bromo-N-[3-chloro-2-[4-(2-phenylethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.00025
5-bromo-N-[3-chloro-2-[4-(furan-2-ylmethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.00027
5-bromo-N-[3-chloro-2-[4-(furan-2-ylmethyl)piperazin-1-yl]phenyl]furan-2-carboxamide
Homo sapiens
-
0.00011
5-bromo-N-[3-fluoro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00029
5-bromo-N-[3-fluoro-2-(4-prop-2-yn-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00018
5-bromo-N-[3-methyl-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.0002
5-bromo-N-[3-methyl-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]furan-2-carboxamide
Homo sapiens
-
0.00004
5-chloro-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00008
5-chloro-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00021
5-cyano-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.00023
5-cyano-N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]furan-2-carboxamide
Homo sapiens
-
0.000011
BIRB 796
Homo sapiens
-
EFC binding assay with active P38alpha
0.000011
BIRB 796
Homo sapiens
-
EFC binding assay with inactive P38alpha
0.000018
BIRB 796
Homo sapiens
IC50 with THP-1 cells
0.000057
BIRB 796
Homo sapiens
-
in cell-based assay measuring LPS-induced TNFalpha secretion
0.000079
BIRB 796
Homo sapiens
-
IMAP enzyme activity assay
0.00004
II/SP600125
Mus musculus
inhibition of JNK1
0.00004
II/SP600125
Mus musculus
inhibition of JNK2
0.00009
II/SP600125
Mus musculus
inhibition of JNK3
0.002
MKK4
Homo sapiens
pH 7.5, 30°C, wild-type MKK4, JNK1, substrate ATF2
-
0.006
MKK4
Homo sapiens
pH 7.5, 30°C, wild-type MKK4, JNK2, substrate c-Jun
-
0.3
MKK4 mutant F48K
Homo sapiens
pH 7.5, 30°C, JNK1, wild-type MKK4, substrate ATF2
-
0.4
MKK4 mutant F48K
Homo sapiens
pH 7.5, 30°C, JNK2, wild-type MKK4, substrate c-Jun
-
0.003
MKK4 mutant L44I
Homo sapiens
pH 7.5, 30°C, JNK1, wild-type MKK4, substrate ATF2
-
0.045
MKK4 mutant L44I
Homo sapiens
pH 7.5, 30°C, JNK2, wild-type MKK4, substrate c-Jun
-
0.00016
N-(2-methoxyethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.0048
N-(2-methoxyethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.0001
N-(3,4-dimethoxyphenethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.0057
N-(3,4-dimethoxyphenethyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.0001
N-(4-methoxybenzyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.0091
N-(4-methoxybenzyl)-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.0001
N-ethyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.1
N-ethyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.00014
N-sec-butyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
pepJIP1 displacement assay DELFIA, GST-JNK2 is applied
0.003
N-sec-butyl-5-(5-nitrothiazol-2-ylthio)-1,3,4-thiadiazol-2-amine
Homo sapiens
-
JNK1 kinase inhibition assay LANTHA
0.001
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-ethylfuran-2-carboxamide
Homo sapiens
-
0.0014
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-ethylfuran-2-carboxamide
Homo sapiens
-
0.00021
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-fluorofuran-2-carboxamide
Homo sapiens
-
0.00041
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-fluorofuran-2-carboxamide
Homo sapiens
-
0.00045
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methoxyfuran-2-carboxamide
Homo sapiens
-
0.00062
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methoxyfuran-2-carboxamide
Homo sapiens
-
0.00033
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
0.00053
N-[2-(1,4-dioxa-8-azaspiro[4.5]dec-8-yl)-3-methylphenyl]-5-methylfuran-2-carboxamide
Homo sapiens
-
0.0006
N-[2-(4-acetylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
Homo sapiens
-
0.00081
N-[2-(4-acetylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
Homo sapiens
-
0.00088
N-[2-(4-benzylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
Homo sapiens
-
0.0011
N-[2-(4-benzylpiperazin-1-yl)-3-chlorophenyl]-5-bromofuran-2-carboxamide
Homo sapiens
-
0.0045
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1H-pyrrole-2-carboxamide
Homo sapiens
-
0.0089
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-1H-pyrrole-2-carboxamide
Homo sapiens
-
0.0018
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
0.002
N-[3-chloro-2-(4-prop-2-en-1-ylpiperazin-1-yl)phenyl]-6-methylpyridine-2-carboxamide
Homo sapiens
-
0.00008
SB 203580
Homo sapiens
-
EFC binding assay with active P38alpha
0.000083
SB 203580
Homo sapiens
-
IMAP enzyme activity assay
0.0001
SB 203580
Homo sapiens
-
EFC binding assay with inactive P38alpha
0.00015
SB 203580
Homo sapiens
-
in cell-based assay measuring LPS-induced TNFalpha secretion
0.000026
SB203580
Homo sapiens
-
0.00003 - 0.0006
SB203580
Homo sapiens
pH 7.2, 25°C
0.000033
SB203580
Homo sapiens
-
-
0.00005
SB203580
Mammalia
-
-
0.000025
SR3451
Homo sapiens
-
-
0.0004
SR3451
Mammalia
-
-
0.0037
SR3451
Mammalia
-
-
0.000007
SR3576
Homo sapiens
-
-
0.00017
SR3576
Mammalia
-
-
0.02
SR3576
Mammalia
-
larger than 0.020
0.000023
SR3582
Homo sapiens
-
-
0.00056
SR3582
Mammalia
-
-
0.02
SR3582
Mammalia
-
larger than 0.020
0.0021
SR4018
Homo sapiens
-
-
0.02
SR4018
Mammalia
-
larger than 0.020
0.00035
SR4276
Homo sapiens
-
-
0.02
SR4276
Mammalia
-
larger than 0.020
0.000055
SR4326
Homo sapiens
-
-
0.0014
SR4326
Mammalia
-
-
0.02
SR4326
Mammalia
-
larger than 0.020
0.0022
SR4642
Homo sapiens
-
-
0.02
SR4642
Mammalia
-
larger than 0.020
0.0015
SR4643
Homo sapiens
-
-
0.02
SR4643
Mammalia
-
larger than 0.020
0.0063
tert-butyl 4-(2-[[(5-bromofuran-2-yl)carbonyl]amino]-6-chlorophenyl)piperazine-1-carboxylate
Homo sapiens
-
0.02
tert-butyl 4-(2-[[(5-bromofuran-2-yl)carbonyl]amino]-6-chlorophenyl)piperazine-1-carboxylate
Homo sapiens
larger than 0.020
0.0000001 - 0.00000014
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
highly selective for p38 isozyme alpha wild-type and mutants with IC50 of 0.10-0.14 nM
0.00066
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
Ic50 for ERK 660 nM
0.00068
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
IC50 for JNK2 is 680 nM
0.00097
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
IC50 for JNK3 970 nM
additional information
(2S)-2-([6-[(2-aminobenzyl)amino]-9-(1-methylethyl)-9H-purin-2-yl]amino)butan-1-ol
Solanum peruvianum
-
relative activity, 58% of control
additional information
2,2'-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]imino]diethanol
Solanum peruvianum
-
relative activity, 37% of control
additional information
2-(2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]amino]ethoxy)ethanol
Solanum peruvianum
-
relative activity, 56% of control
additional information
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
46% at 10 microM
additional information
2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
Mus musculus
-
33% at 10 microM, mixture of 3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine and 2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
additional information
2-(4-fluorophenyl)-6-methoxy-3-(pyridin-4-yl)quinoxaline
Mus musculus
-
33% at 10 microM
additional information
2-([6-[(3-methylbut-2-en-1-yl)amino]-9-(1-methylethyl)-9H-purin-2-yl]amino)ethanol
Solanum peruvianum
-
relative activity, 96% of control
additional information
2-([9-methyl-6-[(3-methylbut-2-en-1-yl)amino]-9H-purin-2-yl]amino)ethanol
Solanum peruvianum
-
relative activity, 44% of control
additional information
2-([[2-[[(1S)-1-(hydroxymethyl)propyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 23% of control
additional information
2-([[2-[[1-(hydroxymethyl)-2-methylbutyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 50% of control
additional information
2-([[9-(1-methylethyl)-2-(4-prop-2-yn-1-ylpiperazin-1-yl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 67% of control
additional information
2-([[9-(1-methylethyl)-2-piperazin-1-yl-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 52% of control
additional information
2-([[9-(1-methylethyl)-2-propyl-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 54% of control
additional information
2-chloro-N-(cyclohexylmethyl)-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 125% of control
additional information
2-[(6-amino-9H-purin-2-yl)amino]ethanol
Solanum peruvianum
-
relative activity, 138% of control
additional information
2-[6-(benzylamino)-2-[(2-hydroxyethyl)amino]-9H-purin-9-yl]ethanol
Solanum peruvianum
-
relative activity, 100% of control
additional information
2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]amino]ethanol
Solanum peruvianum
-
relative activity, 43% of control
additional information
2-[[6-(benzylamino)-9-(1-methylethyl)-9H-purin-2-yl]sulfanyl]ethanol
Solanum peruvianum
-
relative activity, 24% of control
additional information
3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine
Mus musculus
-
33% at 10 microM, mixture of 3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine and 2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
additional information
3-([[2-(heptylamino)-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 58% of control
additional information
3-([[2-[[1-(hydroxymethyl)-2-methylbutyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 62% of control
additional information
3-([[2-[[1-(hydroxymethyl)propyl]amino]-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 44% of control
additional information
3-[([2-[(3-hydroxypropyl)amino]-9-(1-methylethyl)-9H-purin-6-yl]amino)methyl]phenol
Solanum peruvianum
-
relative activity, 38% of control
additional information
3-[[6-(benzylsulfanyl)-9-(1-methylethyl)-9H-purin-2-yl]amino]propan-1-ol
Solanum peruvianum
-
relative activity, 115% of control
additional information
4-([[2-(benzylamino)-9-(1-methylethyl)-9H-purin-6-yl]amino]methyl)phenol
Solanum peruvianum
-
relative activity, 127% of control
additional information
6,7-dichloro-2-(4-fluorophenyl)-3-pyridin-4-ylquinoxaline
Mus musculus
-
39% at 10 microM
additional information
6-(benzylsulfanyl)-2-chloro-9-(1-methylethyl)-9H-purine
Solanum peruvianum
-
relative activity, 135% of control
additional information
bohemine
Solanum peruvianum
-
relative activity, 44% of control
additional information
additional information
Mammalia
-
the inhibitors are tested in LanthaScreen kinase activity assays and pepJIP1 DELFIA displacement assays
-
additional information
N-(2-aminobenzyl)-2-chloro-9-(1-methylethyl)-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 50% of control
additional information
N-benzyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
9% at 10 microM
additional information
N-benzyl-4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
37% at 10 microM
additional information
N-benzyl-9-(1-methylethyl)-2-(methylsulfanyl)-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 69% of control
additional information
N-benzyl-9-(1-methylethyl)-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 41% of control
additional information
N-benzyl-9-methyl-2-morpholin-4-yl-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 91% of control
additional information
N-methyl-9-(1-methylethyl)-9H-purin-6-amine
Solanum peruvianum
-
relative activity, 56% of control
additional information
N6-(2-aminobenzyl)-N2-(4-aminocyclohexyl)-9-(1-methylethyl)-9H-purine-2,6-diamine
Solanum peruvianum
-
relative activity, 46% of control
additional information
N6-benzyl-9-(1-methylethyl)-9H-purine-2,6-diamine
Solanum peruvianum
-
relative activity, 48% of control
additional information
olomucine
Solanum peruvianum
-
relative activity, 57% of control
additional information
roscovitine
Solanum peruvianum
-
relative activity, 20% of control
additional information
staurosporine
Solanum peruvianum
-
relative activity, 10% of control
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evolution
C493C.10 is an orthologue of mammalian JNK
evolution
jnk-1 is an orthologue of mammalian JNK
evolution
kgb-1 is an orthologue of mammalian JNK
evolution
kgb-2 is an orthologue of mammalian JNK. The JNK homologue KGB-2 shows 84% identity with KGB-1
evolution
pmk-1 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-2 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
pmk-3 is an orthologue of mammalian p38. The three pmk genes pmk1, pmk-2, and pmk-3, are encoded by a single polycistronic transcript (operon), precluding the generation of double mutants by traditional genetic crosses
evolution
the enzyme contains the conserved catalytic domain of the serine/threonine kinases
evolution
-
the enzyme contains the conserved catalytic domain of the serine/threonine kinases
-
malfunction
a kgb-1 null mutant, obtained by targeted deletion, shows extra germ cells, increased number of P granules, and temperature-sensitive sterility. RNAi-mediated knockdown of glh-1 in kgb-1 mutants partially rescues the P granule number and temperature-sensitive sterility. Null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3
malfunction
ERK inhibition using PD98059 causes reduction of wound healing by up to 15%
malfunction
-
inhibition of ERK MAPK activity increased E-cadherin expression at both the transcriptional and protein level. Knockdown of EKR1/2 expression by siRNA in A-549 cells produces a similar up-regulation of E-cadherin. Inhibition of p38 and ERK1/2 activities but not JNK and PI3K abrogates DU145 cells survival advantage
malfunction
inhibition of JNK completely blocks mycosporine-like amino acids-mediated wound closure
malfunction
-
inhibition of p38 MAPK activity increased E-cadherin expression at both the transcriptional and protein level. Knockdown of p38alpha expression by siRNA in A-549 cells produces a similar upregulation of E-cadherin. Inhibition of p38 and ERK1/2 activities but not JNK and PI3K abrogates DU145 cells survival advantage
malfunction
MKKs 1 and 2 induce dual phosphorylation of the TEY motif in the activation loop of the kinase-death version of MPK4KD, but do not stimulate MPK4KD to phosphorylate myelin basic protein
malfunction
MKKs 4 and 5 induce dual phosphorylation of the TEY motif in the activation loop of the kinase-death version of MPK3KD, but do not stimulate MPK3KD to phosphorylate myelin basic protein
malfunction
MKKs 4 and 5 induce dual phosphorylation of the TEY motif in the activation loop of the kinase-death version of MPK6KD, but do not stimulate MPK6KD to phosphorylate myelin basic protein
malfunction
no morphological changes are observed in the DELTACshog1 knockout mutant in comparison with the wild-type, but they are slightly reduced in growth under oxidative stress and are hypersensitive to hyperosmotic stress. The DELTACshog1 mutants form normal appressoria-like structures but are reduced in virulence when inoculated on Bowman leaves. The DELTACshog1 mutant is able to infect barley roots, no significant difference in virulence is observed for DELTACshog1 mutants compared to the wild-type
malfunction
null mutations in vhp-1 cause larval lethality, which can be suppressed by null mutations in mlk-1, mek-1, kgb-1, dlk-1, or pmk-3. DLK-1/PMK-3 are identified to affect cilia length, via regulation of RAB-5 endosomes
malfunction
pre-treatment of human synovial sarcoma cells with inhibitors of ERK1/2, p38 MAPK, and JNK attenuates the IL-17A-induced phosphorylation of activator protein-1 (AP-1) subunits and the expression of MMP-3 mRNA
malfunction
removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants. The Esp mutant phenotype worms show enhanced susceptibility to Pseudomonas aeruginosa that causes an intestinal infection and eventual death of the worm
malfunction
root elongation in seedlings of the loss-of-function mutants mpk6-2 and mpk6-3 is less sensitive to NaCl or Na-glutamate, but not to KCl or mannitol, as compared with that of wild-type seedlings. The tolerance of mpk6 to Na+ toxicity is Ca2+-dependent. At the plasma membrane, increased concentrations of NaCl increase the inward Na+-conducted currents while decreasing the outward Na+-conducted currents in wild-type root cells, attended by a positive shift in membrane potential. In mpk6 mutant root cells, NaCl significantly increases outward but not inward Na+-conducted currents, accompanied by a negative shift in membrane potential. Mutant mpk6 decreases NaCl-induced the Na+ accumulation by modifying PM Na+ flux in root cells. Mutant mpk6 accumulates less Na+ in response to NaCl because of the increased cytosolic Ca2+ level in root cells; thus, its root elongation is less inhibited than that of WT by NaCl
malfunction
the DELTACsfus3 knockout mutant is defective in conidiation and formation of appressoria-like structures, showing hypersensitivity to oxidative stress and loss of pathogenicity on non-wounded leaves of Hordeum vulgare cv. Bowman. When inoculated on wounded leaves of Bowman, the DELTACsfus3 knockout mutant is reduced in virulence compared to the wild-type. The DELTACsfus3 mutant fails to cause any symptoms on barley roots
malfunction
the DELTACsslt2 knockout mutant produces more vegetative hyphae, has lighter pigmentation, are more sensitive to cell wall degrading enzymes, and are reduced in virulence on Bowman leaves compared to the wild-type, although they formed normal appressoria like the wild-type. The DELTACsslt2 mutant is able to infect barley roots. DELTACsslt2 mutants show significantly reduced virulence on barley roots in comparison with the wild-type
malfunction
the enzyme knockout mutant shows colonies that are smaller and more compact thant the wild-type colonies. Additionally, while the wild-type produces abundant aerial hyphae on PDA plates, the mutant produces fewer and shorter aerial hyphae. Although mutation of the MAP kinase gene shows substantial effect on the fungal hyphal structure and colony morphology, the conidia produced by the mutant are similar to the wild-type with normal size and morphology. The mutant has reduced production of chitin and reduced expression levels of chitin biosynthetic genes. The mutant DELTAFoSlt2 shows lower chitin contents than wild-type and complemented strain DELTAFoSlt2-c. The mutant strain also shows reduced levels of different chitin syntases, overview. The mutant is sensitive to H2O2. The siderophore biosynthetic gene sidA is 2fold upregulated in mutant DELTAFoSlt2. The expression levels of beauvericin biosynthetic genes, beas, kivr and abc3, are significantly reduced in mutants DELTAFoSlt2 by 12fold, 4fold, and 5fold, respectively as compared to the wild-type, while the expression of fusaric acid biosynthetic genes FUB1 to FUB5 is significantly reduced in the mutant by 100fold, 11fold, 10fold, 25fold, and 50fold, respectively. Hyphal growth rates of the mutant DELTAFoSlt2 is reduced on solid media but not affected in liquid media
malfunction
the mpk6-2 mutant is sensitive to 3-nitro-L-tyrosine (NO2-Tyr) treatment with respect to mitotic abnormalities, and root cells overexpressing the MAP kinase-inactivating phosphatase AP2C3 show defects in chromosome segregation and spindle orientation
malfunction
-
enzyme inhibition can counteract triptolide-induced apoptosis
malfunction
-
enzyme silencing in transgenic tomato plants results in enhanced tolerance to high temperature
malfunction
-
knockout of mitogen-activated protein kinase 20 significantly reduces the expression of a large number of genes controlling sugar and auxin metabolism and signaling in anthers. Suppression or knockout of the enzyme expression leads to abnormal pollen development
malfunction
-
the DELTACsfus3 knockout mutant is defective in conidiation and formation of appressoria-like structures, showing hypersensitivity to oxidative stress and loss of pathogenicity on non-wounded leaves of Hordeum vulgare cv. Bowman. When inoculated on wounded leaves of Bowman, the DELTACsfus3 knockout mutant is reduced in virulence compared to the wild-type. The DELTACsfus3 mutant fails to cause any symptoms on barley roots
-
malfunction
-
the DELTACsslt2 knockout mutant produces more vegetative hyphae, has lighter pigmentation, are more sensitive to cell wall degrading enzymes, and are reduced in virulence on Bowman leaves compared to the wild-type, although they formed normal appressoria like the wild-type. The DELTACsslt2 mutant is able to infect barley roots. DELTACsslt2 mutants show significantly reduced virulence on barley roots in comparison with the wild-type
-
malfunction
-
no morphological changes are observed in the DELTACshog1 knockout mutant in comparison with the wild-type, but they are slightly reduced in growth under oxidative stress and are hypersensitive to hyperosmotic stress. The DELTACshog1 mutants form normal appressoria-like structures but are reduced in virulence when inoculated on Bowman leaves. The DELTACshog1 mutant is able to infect barley roots, no significant difference in virulence is observed for DELTACshog1 mutants compared to the wild-type
-
malfunction
-
root elongation in seedlings of the loss-of-function mutants mpk6-2 and mpk6-3 is less sensitive to NaCl or Na-glutamate, but not to KCl or mannitol, as compared with that of wild-type seedlings. The tolerance of mpk6 to Na+ toxicity is Ca2+-dependent. At the plasma membrane, increased concentrations of NaCl increase the inward Na+-conducted currents while decreasing the outward Na+-conducted currents in wild-type root cells, attended by a positive shift in membrane potential. In mpk6 mutant root cells, NaCl significantly increases outward but not inward Na+-conducted currents, accompanied by a negative shift in membrane potential. Mutant mpk6 decreases NaCl-induced the Na+ accumulation by modifying PM Na+ flux in root cells. Mutant mpk6 accumulates less Na+ in response to NaCl because of the increased cytosolic Ca2+ level in root cells; thus, its root elongation is less inhibited than that of WT by NaCl
-
malfunction
-
the enzyme knockout mutant shows colonies that are smaller and more compact thant the wild-type colonies. Additionally, while the wild-type produces abundant aerial hyphae on PDA plates, the mutant produces fewer and shorter aerial hyphae. Although mutation of the MAP kinase gene shows substantial effect on the fungal hyphal structure and colony morphology, the conidia produced by the mutant are similar to the wild-type with normal size and morphology. The mutant has reduced production of chitin and reduced expression levels of chitin biosynthetic genes. The mutant DELTAFoSlt2 shows lower chitin contents than wild-type and complemented strain DELTAFoSlt2-c. The mutant strain also shows reduced levels of different chitin syntases, overview. The mutant is sensitive to H2O2. The siderophore biosynthetic gene sidA is 2fold upregulated in mutant DELTAFoSlt2. The expression levels of beauvericin biosynthetic genes, beas, kivr and abc3, are significantly reduced in mutants DELTAFoSlt2 by 12fold, 4fold, and 5fold, respectively as compared to the wild-type, while the expression of fusaric acid biosynthetic genes FUB1 to FUB5 is significantly reduced in the mutant by 100fold, 11fold, 10fold, 25fold, and 50fold, respectively. Hyphal growth rates of the mutant DELTAFoSlt2 is reduced on solid media but not affected in liquid media
-
metabolism
distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
-
endoplasmic reticulum homeostasis is regulated by a network of signaling pathways which include stearoyl-CoA desaturase (SCD)-1, p38 mitogen-activated protein kinase (MAPK) and the unfolded protein response (UPR). All these pathways are located at the interface of cell cycle control and cell stress. Inhibition or silencing of SCD-1, via inhibitor CAY10566 or siRNA, specifically induces phosphorylation and activation of p38 MAPK. SCD-1 counteracts palmitate-induced endoplasmic reticulum stress by reducing p38 MAPK activation. Role of SCD-1 and p38 MAPK for neutral lipid biosynthesis, cell proliferation, and viability and insulin-dependent glucose uptake, overview
metabolism
-
hepatocyte coculture induces the re-expression of E-cadherin via abrogation of autocrine EGFR signaling pathway in prostate cancer (PCa) cells and this confers a survival advantage. Hepatocytes educate PCa cells to undergo mesenchymal to epithelial reverting transition (MErT) by modulating the activity of p38 and ERK1/2. Hepatocytes inhibit p38 and ERK1/2 activity in prostate cancer cells, which allows E-cadherin re-expression. Introduction of constitutively active MEK6 and MEK1 to DU-145 cells cocultured with hepatocytes abrogates E-cadherin re-expression. At least a partial phenotypic reversion can be achieved by suppression of p38 and ERK1/2 activation in DU-145 cells even in the absence of hepatocytes
metabolism
MAPK cascade proteins bind to each other selectively via docking interactions
metabolism
MAPK cascade proteins bind to each other selectively via docking interactions
metabolism
MAPK cascade proteins bind to each other selectively via docking interactions. The high selectivity of JNK family MAPKs for cognate binding partners is controlled by two key hydrophobic residues in the docking site
metabolism
mycosporine-like amino acids promote wound healing through focal adhesion kinase (FAK, EC 2.7.10.2) and mitogen-activated protein kinases (MAP kinases) signaling pathway in keratinocytes
metabolism
mycosporine-like amino acids promote wound healing through focal adhesion kinase (FAK, EC 2.7.10.2, HaCaT cells) and mitogen-activated protein kinases (MAP kinases) signaling pathway in keratinocytes
metabolism
pathogen-associated molecular patterns (PAMPs) are recognized by plant pattern recognition receptors to activate PAMP-triggered immunity. PAMP perception enhances phosphorylation of BES1. BES1 is a unique direct substrate of MPK6 in PAMP-triggered immunity signaling. MAPK-mediated BES1 phosphorylation is another BES1 modulation mechanism in plant cell signaling, in addition to GSK3-like kinase-mediated BES1 phosphorylation and F box protein-mediated BES1 degradation. BES1 phosphorylation induced by flg22 occurs downstream of MAPK activation. MKK5K99M acts as a dominant negative mutant that partially blocks MAPK activation and downstream PTI signaling
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. Functional redundancy of pmk-1 and pmk-2
metabolism
the core MAPK signaling cassette consists of a MAPKKK/MAPKK/MAPK cascade, stress-activated MAPK components involved in non-stress-associated processes, overview. Distinct p38 and JNK MAPK cascades regulate a diverse class of normal biological processes during development and nervous system function. The three kinases DLK-1/MKK-4/PMK-3 constitute a linear pathway. MAK-2 is the homologue of MAPKAPK2 (MK2), and acts downstream of PMK-3. The conserved pathway, the DLK-1/MKK-4/PMK-3 cascade, activation is necessary to initiate axonal regrowth. The cascade is tightly regulated by protein ubiquitination during synapse development
metabolism
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pathogen-associated molecular patterns (PAMPs) are recognized by plant pattern recognition receptors to activate PAMP-triggered immunity. PAMP perception enhances phosphorylation of BES1. BES1 is a unique direct substrate of MPK6 in PAMP-triggered immunity signaling. MAPK-mediated BES1 phosphorylation is another BES1 modulation mechanism in plant cell signaling, in addition to GSK3-like kinase-mediated BES1 phosphorylation and F box protein-mediated BES1 degradation. BES1 phosphorylation induced by flg22 occurs downstream of MAPK activation. MKK5K99M acts as a dominant negative mutant that partially blocks MAPK activation and downstream PTI signaling
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physiological function
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involved in the pathways of apoptosis and growth
physiological function
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JNK1 disrupts the insulin signaling cascade via phosphorylation of the insulin receptor substrate IRS-1, which leads to the degradation of IRS-1
physiological function
JNK1 has been suggested to play a central role in the development of obesity-induced insulin resistance
physiological function
JNK3 has been shown to mediate neuronal apoptosis
physiological function
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monocyte, macrophage production of tumor necrosis factor-alpha is largely driven by p38 mitogen-activated protein kinase
physiological function
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p38 alpha mitogen-activated protein kinase is a key component of the cascade leading to pro-inflammatory cytokines such as tumor necrosis factor-alpha and interleukin-1beta
physiological function
p38alpha mitogen-activated protein kinase is involved in the signaling cascade responsible for the development of inflammation, increased activity of the p38 enzyme results in cytokine overproduction
physiological function
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pERK1/2 appears to specifically modulate gating properties of Na(v)1.7, an effect that may contribute to the role of this channel in dorsal root ganglion neuron excitability
physiological function
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signal transduction through the p38 mitogen-activated protein kinase pathway is central to the transcriptional and translational control of cytokine and inflammatory mediator production
physiological function
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the JNKs signal transduction pathway plays an important role in coordinating cellular responses including apoptosis, proliferation, and neoplastic transformation
physiological function
the JNKs signal transduction pathway plays an important role in coordinating cellular responses including apoptosis, proliferation, and neoplastic transformation
physiological function
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the MAPK pathway is important for cell proliferation, survival and differentiation
physiological function
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the MAPK pathway, via the Ras/Raf/MEK/ERK signal cascade, is responsible for transmitting and amplifying mitogenic signals from the cell surface to the nucleus where activated transcription factors regulate gene expression and determine cell fate
physiological function
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the mitogen-activated protein kinase signaling pathway is one of the major second messenger systems regulating glutamate release at the presynaptic level
physiological function
activation of JNK signaling occurs under conditions of heavy metal stress. Olfactory memory in Caenorhabditis elegans allows for the association of cues with positive or negative experiences. The loss of these memories proceeds through the UNC-43/TIR-1/NSY-1/SEK-1/JNK-1 cascade
physiological function
brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, BES1, is phosphorylted by Arabidospis thaliana MPK6. MAPK-mediated phosphorylation alters BES1 subcellular accumulation in PAMP-triggered immunity
physiological function
dual specificity phosphatases play a crucial role in MAP kinase regulation. Dual specificity phosphatase DUSP16 (MKP7) and p38alpha interact in a unique manner that is different from other dual specificity phosphatases, DUSP16 binds p38alpha via an extended binding surface that includes helix alpha4. KIM-containing MAPK-specific dual specificity phosphatase DUSP10 also uses a unique binding mode to interact with p38alpha. The interaction of the MAPK binding domain of DUSP16 with p38alpha shows that despite belonging to the same dual specificity phosphatase (DUSP) family, its interaction mode differs from that of DUSP10, detailed overview. DUSP16 selectively inactivates JNK and p38 following stress activation
physiological function
effect of EGF-mediated mitogen-activated protein kinases 3 and 1 (MAPK3/1) pathway on in vitro cytoplasmic maturation of sheep oocytes, overview. The key downstream effectors of EGFR signaling in cumulus cells, mitogen-activated protein kinases 3 and 1 (MAPK3/1, also known as ERK1/2), is essential for mammalian oocyte maturation. Maturation of mammalian oocytes is a complex and dynamic process involving the maturation of nucleus and cytoplasm
physiological function
ERK2 is a critical component in the mitogen-activated protein kinase signal cascade, where it helps regulate many cellular processes including proliferation, differentiation, and survival
physiological function
essential role of mitogen-activated protein kinases in IL-17A-induced matrix metalloproteinase MMP-3 expression in human synovial sarcoma cells, overview
physiological function
essential role of mitogen-activated protein kinases in IL-17A-induced matrix metalloproteinase MMP-3 expression in human synovial sarcoma cells, overview. IL-17A induces MMP-1 and MMP-9 via ERK1/2 and p38 MAPK-dependent activation of the transcriptional factors activator protein-1 (AP-1) and nuclear factor-kappa B (NF-kappaB)
physiological function
JNK is a factor involved in inflammation, proliferation, and apoptosis. In addition JNK is essential for cell migration and keratinocyte movement through phosphorylation of paxillin. Activation of JNK1 is involved in wound repair. The activation of JNK is involved in the mycosporine-like amino acid-induced cell migration
physiological function
mitogen-activated protein kinase 6 controls root growth in Arabidopsis thaliana by modulating Ca2+-based Na+ flux in root cell under salt stress
physiological function
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mitogen-activated protein kinases (MAPKs) are important components of the tripartite mitogen-activated protein kinase signaling cascade and play an important role in plant growth and development. Involvement of specific MAPK family members in different stages of fruit ripening, overview. Some MaMPKs might be negatively regulated by ethylene, their expression increases in post-ethylene. MaMPKs might play an important role in senescence or in the response to pathogen stress, as at this stage of ripening, fungal infection begins to take place
physiological function
PMK-3 acts during neuronal development. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The avoidance of high CO2 environments and pathogens is mediated by MOM-4/MKK-4/PMK-3 in the BAG neuron
physiological function
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role of p38 mitogen-activated protein kinase in linking stearoyl-CoA desaturase-1 activity with endoplasmic reticulum homeostasis. During lipotoxic and cell cycle stress, prolonged activation of p38 MAPK due to SCD-1 inhibition induced endoplasmic reticulum stress, the unfolded protein response, and endoplasmic reticulum/Golgi remodeling. The negative regulation of p38 MAPK mediates the protective effects of SCD-1 on endoplasmic reticulum homeostasis under distinct stress conditions. Role of SCD-1 and p38 MAPK for neutral lipid biosynthesis, cell proliferation, and viability and insulin-dependent glucose uptake, overview
physiological function
roles for KGB-2 are in excess carbon dioxide (hypercapnia)-induced fertility defects and a slight negative role in axon injury response
physiological function
the active form of MAP kinase interacts with gamma-tubulin on specific subsets of mitotic microtubules during late mitosis. MPK6 phosphorylates EB1c, but not EB1a, and has a role in maintaining regular planes of cell division under stress conditions. MPK6 activtes the micotubule-associated protein MAP65-1 that has a redundant function in Arabidopsis with MAP65-3 in cytokinesis. MPK6 is required for regulation of the alignment of cell division on NO2-Tyr treatment
physiological function
the enzyme is involved in P granule formation in germ cell proliferation. KGB-1 can bind and phosphorylate GLH-1, which leads to degradation of phosphorylated GLH-1. KGB-1 activity negatively regulates GLH-1 and the steady state level of P granules to maintain fertility. vhp-1 regulates MAP kinases in axon regeneration. svh-1 and svh-2 likely provide a layer of specificity in controlling the KGB-1/JNK pathway, independently of PMK-3 in axon injury response, crosstalk between the KGB-1 and PMK-3 cascades. The aversive reaction to microbial exposure is mediated by a MLK-1/MEK-1(SEK-1)/KGB-1 pathway
physiological function
the enzyme is involved in siderophore biosynthesis and plays a vital role in regulation of fusaric acid production. The MAP kinase is necessary for the fungal virulence on banana plants and is required for the full virulence of Fusarium oxysporum f. sp. cubense
physiological function
the intrinsic activity of wild-type p38beta is regulated in mammalian cells
physiological function
the MAPK gene is involved in the regulation of fungal development under normal and stress conditions and is required for full virulence on barley plants
physiological function
the MAPK gene is involved in the regulation of fungal development under normal and stress conditions and is required for full virulence on barley plants. Enzyme CsSLT2 has a role in the maintenance of cell-wall integrity in Bipolaris sorokiniana
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development
physiological function
the NSY-1/SEK-1/PMK-1 and PMK-2 cascade acts during neuronal development to regulate AWC asymmetry. The activation of this cascade is regulated in part by calcium, via calmodulin kinase II, as well as the conserved protein TIR-1. PMK-1 and PMK-2 act redundantly downstream of TIR-1/NSY-1/SEK-1 to induce TPH-1 expression in the ADF neuron following exposure to bacteria. Genes pmk-1 and pmk-2 function redundantly during olfactory neuronal development. Activation of PMK-1 following arsenite treatment is dependent on SEK-1 but independent of NSY-1, differing from the NSY-1/SEK-1/PMK-1 cascade used during infection and osmotic stress. Unique upstream components activating PMK-1 induce SKN-1 activation following toxin and bacterial exposure
physiological function
the p38gamma C-terminus is an efficient inducer of cell death after its intracellular delivery. Binding of the C-terminal sequence of p38gamma to PTPN4 abolishes the catalytic autoinhibition of PTPN4 and thus activates the phosphatase, which can efficiently dephosphorylate the activation loop of p38gamma. The p38gamma-PTPN4 interaction promotes cellular signaling, preventing cell death induction
physiological function
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enzyme overexpression in transgenic tomato plants results in reduced tolerance to high temperature
physiological function
A0A0S2SW99, A0A0S2SWA2, A0A0S2SWA5, A0A0S2SWD0, A0A0S2SWD3, A0A0S2SWD4, A0A0S2SWD5, A0A0S2SWD8, A0A0S2SWG7, A0A0S2SWI1, A0A0S2SWI9, A0A0S2SWS3 isoform MPK18 is potentially involved in plant resistance to environmental stress
physiological function
A0A0S2SW99, A0A0S2SWA2, A0A0S2SWA5, A0A0S2SWD0, A0A0S2SWD3, A0A0S2SWD4, A0A0S2SWD5, A0A0S2SWD8, A0A0S2SWG7, A0A0S2SWI1, A0A0S2SWI9, A0A0S2SWS3 isoform MPK3 is potentially involved in plant resistance to environmental stress
physiological function
A0A0S2SW99, A0A0S2SWA2, A0A0S2SWA5, A0A0S2SWD0, A0A0S2SWD3, A0A0S2SWD4, A0A0S2SWD5, A0A0S2SWD8, A0A0S2SWG7, A0A0S2SWI1, A0A0S2SWI9, A0A0S2SWS3 isoform MPK4-1 is potentially involved in plant resistance to environmental stress
physiological function
A0A0S2SW99, A0A0S2SWA2, A0A0S2SWA5, A0A0S2SWD0, A0A0S2SWD3, A0A0S2SWD4, A0A0S2SWD5, A0A0S2SWD8, A0A0S2SWG7, A0A0S2SWI1, A0A0S2SWI9, A0A0S2SWS3 isoform MPK4-2 is potentially involved in plant resistance to environmental stress
physiological function
A0A0S2SW99, A0A0S2SWA2, A0A0S2SWA5, A0A0S2SWD0, A0A0S2SWD3, A0A0S2SWD4, A0A0S2SWD5, A0A0S2SWD8, A0A0S2SWG7, A0A0S2SWI1, A0A0S2SWI9, A0A0S2SWS3 isoform MPK6 is potentially involved in plant resistance to environmental stress
physiological function
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mitogen-activated protein kinase 20 exerts its role specifically at the uni-to-binucleate transition during microgametogenesis. The enzyme specifically regulates post-meiotic pollen development through modulating sugar and auxin metabolism and signaling
physiological function
the enzyme is involved in innate immune defense in oysters
physiological function
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the modulation of dual-specificity protein phosphatase1/mitogen-activated protein kinase cascade is associated with the apoptosis of osteosarcoma cells. The dual-specificity protein phosphatase1-dependent activation of the enzyme enhances antitumor effect of triptolide
physiological function
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the MAPK gene is involved in the regulation of fungal development under normal and stress conditions and is required for full virulence on barley plants
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physiological function
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the MAPK gene is involved in the regulation of fungal development under normal and stress conditions and is required for full virulence on barley plants. Enzyme CsSLT2 has a role in the maintenance of cell-wall integrity in Bipolaris sorokiniana
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physiological function
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mitogen-activated protein kinase 6 controls root growth in Arabidopsis thaliana by modulating Ca2+-based Na+ flux in root cell under salt stress
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physiological function
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brassinosteroid insensitive1-ethyl methanesulfonate-suppressor1, BES1, is phosphorylted by Arabidospis thaliana MPK6. MAPK-mediated phosphorylation alters BES1 subcellular accumulation in PAMP-triggered immunity
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physiological function
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the enzyme is involved in siderophore biosynthesis and plays a vital role in regulation of fusaric acid production. The MAP kinase is necessary for the fungal virulence on banana plants and is required for the full virulence of Fusarium oxysporum f. sp. cubense
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additional information
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The D-sites of the ERK pathway activators MEK1 and MEK2 contain IXL and LXI, respectively, in the first 3 residues of the hydrophobic submotif
additional information
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The D-sites of the p38 activators MKK3 and MKK6 both contain LXI in the first 3 residues of the hydrophobic submotif
additional information
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The D-sites of the p38 activators MKK3 and MKK6 both contain LXI in the first 3 residues of the hydrophobic submotif
additional information
MAPKs that are in different families (e.g. ERK, JNK, and p38) can bind selectively to D-sites in their authentic substrates and regulators while discriminating against D-sites in other pathways. The D-sites of the p38 activators MKK3 and MKK6 both contain LXI in the first 3 residues of the hydrophobic submotif
additional information
molecular basis of the interaction of the human protein tyrosine phosphatase non-receptor type 4 (PTPN4) with the mitogen-activated protein kinase p38gamma, the main contribution to the p38gamma-PTPN4 complex formation is the tight interaction between the C-terminus of p38gamma and the PDZ domain of PTPN4, overview. NMR titration study at pH 7.5, 25°C
additional information
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molecular basis of the interaction of the human protein tyrosine phosphatase non-receptor type 4 (PTPN4) with the mitogen-activated protein kinase p38gamma, the main contribution to the p38gamma-PTPN4 complex formation is the tight interaction between the C-terminus of p38gamma and the PDZ domain of PTPN4, overview. NMR titration study at pH 7.5, 25°C
additional information
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p38 MAPK might show selective protein-lipid interactions
additional information
regulation of MAPKs is achieved via a plethora of regulatory proteins including activating MAPKKs and an abundance of deactivating phosphatases. Although all regulatory proteins use an identical interaction site on MAPKs, the common docking and hydrophobic pocket, they use distinct kinase interaction motif (KIM or D-motif) sequences that are present in linear, peptide-like, or well folded protein domains. Fine-tuning necessary to achieve MAPK specificity and regulation among multiple regulatory proteins
additional information
residue Y119 is the gatekeeper in the MPK3 enzyme structure
additional information
residue Y119 is the gatekeeper in the MPK3 enzyme structure
additional information
residue Y119 is the gatekeeper in the MPK3 enzyme structure
additional information
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residue Y119 is the gatekeeper in the MPK3 enzyme structure
additional information
residue Y124 is the gatekeeper in the MPK4 enzyme structure
additional information
residue Y124 is the gatekeeper in the MPK4 enzyme structure
additional information
residue Y124 is the gatekeeper in the MPK4 enzyme structure
additional information
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residue Y124 is the gatekeeper in the MPK4 enzyme structure
additional information
residue Y144 is the gatekeeper in the MPK6 enzyme structure
additional information
residue Y144 is the gatekeeper in the MPK6 enzyme structure
additional information
residue Y144 is the gatekeeper in the MPK6 enzyme structure
additional information
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residue Y144 is the gatekeeper in the MPK6 enzyme structure
additional information
structure-based assignment of Ile, Leu, and Val methyl groups in the active and inactive forms of extracellular signal-regulated kinase 2, overview
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C177S/C222S/K250A/K251A/K265A/K270A
site-directed mutagenesis, the hexa-surfaced mutant forms crystallization complexes with inhibitor furan-2-carboxylic acid (3-[5-(4H-[1,2,4]triazol-3-yl)-1H-indazol-3-yl]-phenyl)-amide in contrast to other mutant variants or the wild-type enzyme
D176A
site-directed mutagenesis of p38beta, the intrinsically active variant is spontaneously phosphorylated and active toward MK2, the mutant manifests elevated catalytic activity when immunoprecipitated from cells not exposed to any activating signal
D176A/F327S
site-directed mutagenesis of p38alpha, the intrinsically active variant is spontaneously phosphorylated and active toward MK2, the mutant manifests elevated catalytic activity when immunoprecipitated from cells not exposed to any activating signal
D3K/C6V/S8N/14E
site-directed mutagenesis using JNK2 1-362 or 1-364, the mutant does not crystallize
E339A
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in 100 mM KCl completely dimeric
F329A
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retains ability to dimerize significantly in 100 mM KCl
H176A/F181A/L4A
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retains ability to dimerize significantly in 100 mM KCl
H176E
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retains ability to dimerize significantly in 100 mM KCl
H176E/E343A
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retains ability to dimerize significantly in 100 mM KCl
H176E/L2E/E343A
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retains ability to dimerize significantly in 100 mM KCl
H176E/L4A
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in 100 mM KCl almost completely monomeric
K203A/E204A
site-directed mutagenesis, the mutant does not crystallize
K340A
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in 100 mM KCl completely dimeric
K340E/L3E
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retains ability to dimerize significantly in 100 mM KCl
K53A
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kinase-negative mutant
L2E
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in 100 mM KCl completely dimeric
L4A
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retains ability to dimerize significantly in 100 mM KCl
T106M
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inhibitor-insensitive mutant
D176A
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active p38alpha mutant, crystals do not appear spontaneously, cross-seeding approaches using crystals of mutant D176A+F327L as the source of microseeds results in crystals suitable for X-ray analysis
D176A/F327L
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most active p38alpha mutant, improvement of crystallization assays, obtained with abolishing phosphorylation completely by reducing both the temperature and duration of induction and by significantly shortening the N-terminal hexahistidine spacer, facilitating the growth of well diffracting crystals
D176A/F327S
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active p38alpha mutant, crystals do not appear spontaneously, cross-seeding approaches using crystals of mutant D176A+F327L as the source of microseeds results in crystals suitable for X-ray analysis
G110A
site-directed mutagenesis of isozyme alpha, the mutant shows a slightly decreased Km value for ATP, but unaltered activity compared to the wild-type enzyme, decreased sensitivity for inhibitors compared to the wild-type enzyme
G110D
site-directed mutagenesis of isozyme alpha, the mutant shows a decreased Km value for ATP, but unaltered activity compared to the wild-type enzyme, decreased sensitivity for inhibitors compared to the wild-type enzyme
K61A
site-directed mutagenesis, inactive mutant, the point mutation within the beta-3 sheet of subdomain II disrupts the ATP-binding site in PsMPK2
D546V
site-directed mutagenesis, the mutant enzyme is exclusively localized in the nucleus and especially in the Golgi apparatus, not in the cytoplasm, in contrast to the wild-type enzyme
I101A
site-directed mutagenesis
I124A
site-directed mutagenesis
I238A
site-directed mutagenesis
K717S
site-directed mutagenesis, the mutant enzyme is exclusively localized in the nucleus and Golgi apparatus, not in the cytoplasm, in contrast to the wild-type enzyme
L102A/Q103A
site-directed mutagenesis
L105A
site-directed mutagenesis
L110A
site-directed mutagenesis
L113A
site-directed mutagenesis
L154A
site-directed mutagenesis
L155A
site-directed mutagenesis
L161A
site-directed mutagenesis
L198A
site-directed mutagenesis
L235A
site-directed mutagenesis
D144A
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kinase-dead mutant, is unable to grow on 1000 mM sorbitol
K52R
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retains residual activity that permitts slow but readily detectable growth on 1000 mM sorbitol, residual growth is eliminated in the presence of 1-NM-PP1
T100A
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Hog1-as-mutant, fully functional analog-sensitive allele of HOG1, is unable to grow in the presence of 1-NM-PP1, permits acute inhibition of the enzyme without other detectable perturbations of the cell, in the presence of inhibitor Rck2 modification is completely abrogated
additional information
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overexpression of MPK4 substrate MSK1 in wild-type plants leads to activated salicylic-dependent resistance, but does not interfere with induction of a defense gene by jasmonate
additional information
generation of the T-DNA insertion lines mpk6-2 (Salk 073907) and mpk6-3(Salk 127507), that are loss-of-function mutants, the mutants are less sensitive to NaCl or Na-glutamate, but not to KCl or mannitol, as compared with that of wild-type seedlings
additional information
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generation of the T-DNA insertion lines mpk6-2 (Salk 073907) and mpk6-3(Salk 127507), that are loss-of-function mutants, the mutants are less sensitive to NaCl or Na-glutamate, but not to KCl or mannitol, as compared with that of wild-type seedlings
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additional information
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generation of a gene replacement DELTACsFUS3 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
additional information
generation of a gene replacement DELTACsFUS3 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
additional information
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generation of a gene replacement DELTACsHOG1 knockout mutant. DELTACshog1 mutants are significantly reduced in growth under the oxidative stress produced by 10mM H2O2 and the salt stress produced by 1.5mM KCl. Fungal development and conidial productivity of the knockout mutant, overview
additional information
generation of a gene replacement DELTACsHOG1 knockout mutant. DELTACshog1 mutants are significantly reduced in growth under the oxidative stress produced by 10mM H2O2 and the salt stress produced by 1.5mM KCl. Fungal development and conidial productivity of the knockout mutant, overview
additional information
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generation of a gene replacement DELTACsSLT2 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
additional information
generation of a gene replacement DELTACsSLT2 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
additional information
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generation of a gene replacement DELTACsFUS3 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
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additional information
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generation of a gene replacement DELTACsSLT2 knockout mutant. Fungal development and conidial productivity of the knockout mutant, overview
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additional information
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generation of a gene replacement DELTACsHOG1 knockout mutant. DELTACshog1 mutants are significantly reduced in growth under the oxidative stress produced by 10mM H2O2 and the salt stress produced by 1.5mM KCl. Fungal development and conidial productivity of the knockout mutant, overview
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additional information
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transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
transgenic jnk-1 deletion mutant, exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures
additional information
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construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
construction of a JNK-1 deletion mutant expressing daf-16-GFP, the mutant exhibits a reduced thermal tolerance and reproductive fitness at higher temperatures compared to the wild-type enzyme, jnk-1 overexpression leads to enhanced translocation of DAF-16
additional information
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a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
a kgb-1 null mutant is obtained by targeted deletion
additional information
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a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection
additional information
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a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
a strain with mutations in both pmk-1 and pmk-2 is serendipitously identified in a screen searching for suppressors of the pmk-1 loss of function phenotype following bacterial infection. Removing the 3'-UTR of pmk-2 causes its expression in the intestine, which is sufficient to rescue the Esp phenotype of pmk-1 mutants
additional information
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Gpmk1 MAP kinase disruption mutants of Fusarium graminearum are fully viable in vitro but are unable to infect wheat due to lack of secreted lipolytic enzymes, amylolytic and pectinolytic enzymes are not affected by gpmk1 gene disruption, apathogenic phenotype
additional information
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Gpmk1 MAP kinase disruption mutants of Fusarium graminearum are fully viable in vitro but are unable to infect wheat due to lack of secreted lipolytic enzymes, amylolytic and pectinolytic enzymes are not affected by gpmk1 gene disruption, apathogenic phenotype
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additional information
generation of the knockout mutant DELTAFoSlt2 by targeted gene disruption, complementation with the wild-type gene
additional information
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generation of the knockout mutant DELTAFoSlt2 by targeted gene disruption, complementation with the wild-type gene
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additional information
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at least five residues must be mutated simultaneously to produce an ERK2 mutant that is predominantly monomeric. Mutants, whether monomers or dimers, have specific protein kinase activities under fixed assay conditions that are roughly equivalent to wild-type ERK2
additional information
development and evaluation of a high-throughput affinity-based screening technology, ATLAS, for soluble proteins, e.g. p38 MAP kinase, effects of p38 MAP kinase inhibitors, overview
additional information
elevating expression levels of p38alpha wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha
additional information
elevating expression levels of p38alpha wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha
additional information
elevating expression levels of p38beta wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Construction of enzyme mutants by insertion of premature stop codons p38beta generating p38beta C-terminal truncation mutants p38betaT341, p38betaV345, p38betaF348, and p38betaK355, the mutants lacking the C-terminus show elevated spontaneous MKK6-independent autophosphorylation activities. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha
additional information
elevating expression levels of p38beta wild-type results in only a slight increase in their apparent phosphorylation that is not sufficient to induce phosphorylation of the p38 substrate MAPKAPK2. Expression of the chimera containing Gln218-Val246, which possesses the highest intrinsic activity as a recombinant purified protein, leads to its spontaneously phosphorylation at high levels in HEK-293 cells and to a spontaneous, signal-independent phosphorylation of MK2. Construction of enzyme mutants by insertion of premature stop codons p38beta generating p38beta C-terminal truncation mutants p38betaT341, p38betaV345, p38betaF348, and p38betaK355, the mutants lacking the C-terminus show elevated spontaneous MKK6-independent autophosphorylation activities. Generation of a p38alpha/beta/alpha/beta chimera that has, in addition to the G-helix-MKI (Gln218-Val246) region from p38beta, also the C-terminus of p38beta, Leu334-Gln364. The p38alpha/beta/alpha/beta chimera shows lose spontaneous activity and is more active than the parental chimera. p38alpha/beta/alpha/beta is phosphorylated at higher levels and shows higher phosphorylation of MK2 in HEK-293 cells than p38alpha/beta/alpha
additional information
Tyr-215 mutant shows no autophosphorylation and no phosphorylation of myelin basic protein
additional information
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Tyr-215 mutant shows no autophosphorylation and no phosphorylation of myelin basic protein
additional information
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enzyme-deficient mutant mice show defects in growth arrest and increased tumorigenesis
additional information
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transgenic mice expressing a dominant negative mutant MAP kinase, inhibits the activity of endogenous p38 MAP kinase and reduces levels of IFN-gamma in serum
additional information
construction of mutant knockout p38alphaLPC-KO mice, hepatocyte-specific ablation of p38alpha in mice results in activation of MKK4 and MKK3/6 and excessive activation of JNK in the liver after in vivo challenge with bacterial lipopolysaccharide. Despite increased JNK activity, p38alpha-deficient hepatocytes are not sensitive to LPS/TNF toxicity showing that JNK activation is not sufficient to mediate TNF-induced liver damage. Lipopolysaccharide injection causes liver failure in mice lacking both p38alpha and IkappaB kinase 2 in hepatocytes, when combined with partial nuclear factor-kappaB inhibition, p38alpha deficiency sensitizes the liver to cytokine-induced damage
additional information
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enzyme silencing by selective siRNA
additional information
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transgenic mice expressing a dominant negative mutant MAP kinase, inhibits the activity of endogenous p38 MAP kinase and reduces levels of IFN-gamma in serum
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additional information
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construction of mutant knockout p38alphaLPC-KO mice, hepatocyte-specific ablation of p38alpha in mice results in activation of MKK4 and MKK3/6 and excessive activation of JNK in the liver after in vivo challenge with bacterial lipopolysaccharide. Despite increased JNK activity, p38alpha-deficient hepatocytes are not sensitive to LPS/TNF toxicity showing that JNK activation is not sufficient to mediate TNF-induced liver damage. Lipopolysaccharide injection causes liver failure in mice lacking both p38alpha and IkappaB kinase 2 in hepatocytes, when combined with partial nuclear factor-kappaB inhibition, p38alpha deficiency sensitizes the liver to cytokine-induced damage
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additional information
metabolic effects and regulation of recombinant MPK2 in transgenic Arabidopsis thaliana plants, detailed overview
additional information
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metabolic effects and regulation of recombinant MPK2 in transgenic Arabidopsis thaliana plants, detailed overview
additional information
Construction of several truncation mutants
additional information
wild-type and mutant binding analysis with nonphosphorylated and phosphorylated cofactor and derivative, i.e. ATP and AMP-PNP, overview
additional information
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hog1delta mutant, is unable to grow in the presence of 1-NM-PP1
additional information
the Ste5 scaffold protein can be used as a platform to systematically reshape output of the yeast mating MAP kinase pathway, construction of synthetic positive- and negative-feedback loops by dynamically regulating recruitment of pathway modulators to an artificial binding site on Ste5, they show ultrasensitive dose response, accelerated or delayed response times, and tunable adaptation, overview
additional information
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the Ste5 scaffold protein can be used as a platform to systematically reshape output of the yeast mating MAP kinase pathway, construction of synthetic positive- and negative-feedback loops by dynamically regulating recruitment of pathway modulators to an artificial binding site on Ste5, they show ultrasensitive dose response, accelerated or delayed response times, and tunable adaptation, overview
additional information
isolation of several MTK loss-of-function mutants of TmkA, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
additional information
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isolation of several MTK loss-of-function mutants of TmkA, effects of wild-type and mutant enzymes on host growth, morphology, and conidiation, overview
additional information
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effects of overexpression of substrate Smad1 mutant S187A/S195A/S205A/S213A compared to overexpression of Smad1 wild-type, ventralizing of embryos, overview
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