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acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
benzoyl-Phe-Val-Arg-4-methylcoumarin 7-amide + H2O
benzoyl-Phe-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-Arg + 7-amino-4-methylcoumarin
-
1.2% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
benzyloxycarbonyl-Gly-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-Gly-L-Arg + 7-amino-4-methylcoumarin
ratio kcat/KM-value is 1000 M/s
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
ratio kcat/KM-value is 1000 M/s
-
-
?
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Val-L-Val-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
?
Boc-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
Boc-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
?
D-Val-Leu-Arg-4-nitroanilide + H2O
D-Val-Leu-Arg + 4-nitroaniline
native and recombinant enzyme
-
?
D-Val-Leu-Lys-4-nitroanilide + H2O
D-Val-Leu-Lys + 4-nitroaniline
native and recombinant enzyme
-
?
Fibrinogen + H2O
?
-
-
-
?
GDDSTPSILPAPRGYPGQV + H2O
GDDSTPSILPAPR + GYPGQV
-
the tethered ligand is GYPGQV
-
-
?
GPNSKGRSLIGRLDTPYGGC + H2O
GPNSKGR + SLIGRLDTPYGC
-
the tethered ligand is SLIGRL
-
-
?
GTNRSSKGRSLIGKVDGTSHVTGKGVT + H2O
GTNRSSKGR + SLIGKVDGTSHVTGKGVT
-
the tethered ligand is SLIGKV
-
-
?
high-molecular weight kininogen + H2O
?
-
-
-
?
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
L-Pro-L-Phe-L-Arg + 7-amino-4-methylcoumarin
best substrate
-
-
?
LL-37 antimicrobial peptide + H2O
?
-
i.e. LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES
-
-
?
papillomavirus major capsid protein L1 + H2O
?
-
-
-
?
polypeptide + H2O
peptides
pro-kallikrein 1 + H2O
kallikrein 1
-
-
-
-
?
pro-kallikrein 11 + H2O
kallikrein 11
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
Pro-Phe-Arg-7-amido-4-methylcoumarin + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
10% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
promeprin beta + H2O
meprin beta
-
KLK8 activates promeprin beta
-
-
?
proteinase-activated receptor 2 peptide precursor + H2O
?
-
the enzyme can unmask a PAR2 receptor-activating sequence from a peptide precursor
-
-
?
Rattus norvegicus proteinase-activated receptor 2 + H2O
?
-
no activity witht the human proteinase-activated receptor 2
-
-
?
single-chain tissue-type plasminogen activator + H2O
two-chain tissue-type plasminogen activator
specific cleavage of Arg275-Ile276 bond
-
-
?
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg + 7-amino-4-methylcoumarin
wild-type and mutants
-
?
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
11% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Arg-Arg + 7-amino-4-methylcoumarin
-
5.0% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Gln-Gly-Arg + 7-amino-4-methylcoumarin
-
1.4% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
4.9% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Leu-Lys-Arg + 7-amino-4-methylcoumarin
-
3.9% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
4.2% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
-
3.8% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
100% activity
-
-
?
tosyl-Gly-L-Pro-L-Lys-7-amido-4-methylcoumarin + H2O
tosyl-Gly-L-Pro-L-Lys + 7-amino-4-methylcoumarin
ratio kcat/KM-value is 670 M/s
-
-
?
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin + H2O
tosyl-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
1.0% activity compared to tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
low activity
-
?
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O
acetyl-Pro-Phe-Arg + 4-nitroaniline
recombinant, not native enzyme
-
?
Boc-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
Boc-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
Boc-Val-Pro-Arg-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
proteins produced from KLK8 splice variants modify the extracellular microenvironment by cleaving fibronectin. Degradation of fibronectin by hK8 suppresses integrin signaling and retards cancer cell motility by inhibiting actin polymerization
-
-
?
Fibronectin + H2O
?
recombinant enzyme
-
-
?
Fibronectin + H2O
?
-
recombinant enzyme
-
-
?
Fibronectin + H2O
?
affects cell adhesion or cell migration by modulating the content and/or chemical characteristics of fibronectin in the extracellular matrix
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
-
-
?
polypeptide + H2O
peptides
enzyme has significant limbic effects by changing the extracellular matrix environment
-
?
polypeptide + H2O
peptides
involvement in neural plasticity
-
?
polypeptide + H2O
peptides
involvement in neural plasticity
-
?
polypeptide + H2O
peptides
enzyme is implicated in various neurological processes including formation of memory
-
?
polypeptide + H2O
peptides
-
-
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
Pro-Phe-Arg-4-methylcoumaryl-7-amide
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg + 7-amino-4-methylcoumarin
ratio kcat/KM-value is 21000 M/s
-
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
recombinant and native enzyme
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
low activity
-
?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
recombinant, not native, enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
no activity
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
best substrate
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
native and recombinant enzyme
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
recombinant wild-type and mutants
-
?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
enzyme might be involved in ovarian cancer, brain damage and kindling epilepsy
-
-
?
additional information
?
-
enzyme may be impicated in extracellular matrix protein degradation in the area surrounding enzyme producing cells
-
-
?
additional information
?
-
-
enzyme may be impicated in extracellular matrix protein degradation in the area surrounding enzyme producing cells
-
-
?
additional information
?
-
enzyme shows trypsin-like specificity. Synthetic substrates containing either Arg or Lys at P1 positions are cleaved
-
-
?
additional information
?
-
-
enzyme shows trypsin-like specificity. Synthetic substrates containing either Arg or Lys at P1 positions are cleaved
-
-
?
additional information
?
-
trypsin-like specificity with strong preference for Arg over Lys in P1-position. No substrate: plasminogen
-
-
?
additional information
?
-
-
trypsin-like specificity with strong preference for Arg over Lys in P1-position. No substrate: plasminogen
-
-
?
additional information
?
-
-
kallikrein 8 shows highest preference for (R/K)(S/T)(A/V) at P1-P1-P2
-
-
?
additional information
?
-
-
KLK8 does not degrade and activate promeprin alpha
-
-
?
additional information
?
-
-
KLK8 has a strong preference for Arg in P1, and Arg and Lys in P3 position and prefers hydrophobic residues in P2 and small hydrophobic residues in P4 position
-
-
?
additional information
?
-
-
no activity with Ala-Ala-Pro-Val-7-amido-4-methylcoumarin, Ala-Ala-Pro-Phe-7-amido-4-methylcoumarin, Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin, tosyl-Gly-Pro-Lys-7-amido-4-methylcoumarin, and ter-butyloxycarbonyl-Glu-Lys-Lys-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with NATLDPRSFLLRNPNDKYE. Analysis of processing of synthetic human and rat proteinase-activated receptor 2, PAR2, derived sequences, representing the cleavage activation domain of PAR2, by kallikrein 8 versus kallikrein 14. KLKs 8 and 14 can both cleave the synthetic PAR2 tethered ligand-containing synthetic peptides to unmask a potential receptor-activating sequence, but each KLK exhibits distinct signalling properties via PARs 1 and 2
-
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
-
recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus
-
-
?
additional information
?
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
-
loop C and the N-linked oligosaccharide chain on the kallikrein loop affect the catalytic efficiency and P2 specificity, respectively
-
-
?
additional information
?
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
-
substrate specificty of native and recombinant enzyme
-
-
?
additional information
?
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
disulfide bonds SS1 in loop E, Gly142-Leu155, and SS6 in loop G, Ser185-Gly197, are essential for catalytic activity
-
-
?
additional information
?
-
-
enzyme is involved in the synaptogenesis/maturation of orphan and small synaptic boutons in the Schaffer-collateral pathway
-
-
?
additional information
?
-
-
enzyme is necessary for establishment of long-term potentiation and has a significant role in memory acquisition
-
-
?
additional information
?
-
-
kallikrein k8 exhibits a marked preference for cleavage downstream of Arg residues
-
-
?
additional information
?
-
-
no activity with tert-butyloxycarbonyl-Leu-Gly-Arg-4-methylcoumarin 7-amide
-
-
?
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(4-amidinohenyl)methanesulfonyl 1-fluoride
61% inhibition at 1 mM
1-(2-bromobenzene-1-sulfonyl)-5-methyl-3-(2-methyl-4,5-dihydro-1H-imidazol-4-yl)-1H-indole
compound is a promising lead for development of novel kallikrein-8 inhibitors. It binds stably to the kallikrein-8 S1 binding site
1-(3,5-difluorophenyl)-5-hydroxy-7-(4-hydroxy-3,5-dimethoxyphenyl)-6,7-dihydro-1H-pyrrolo[3,2-b] pyridine-3-carboxylic acid
-
i.e. ZINC61720639
2-[[5-(2-chlorophenyl)-4-imino-3-methyl-4,5-dihydro-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]-N-(2,5-dimethoxyphenyl)acetamide
-
-
4,4'-[pentane-1,5-diylbis(oxy)]bis(3,5-dibromobenzenecarboximidamide)
-
-
4-amino-N3-[(2R)-1-(tert-butylamino)-1-oxopropan-2-yl]-N3-(3-chloro-4-fluorophenyl)-2H-pyrrole-3,5-dicarboxamide
-
-
diisopropyl fluorophosphate
2 mM, 100% inhibition
diisopropylfluorophosphate
16% inhibition at 0.1 mM
human alpha1-antichymotrypsin
weak, 16% inhibition at 2 mM
-
human alpha1-antitrypsin
weak, 20% inhibition at 10 mM
-
murinoglobulin I
24% inhibition at enzyme-inhibitor ratio of 1:2; formation of a SDS-stable complex; i.e. MUG I
-
N-(7-amino-1-chloro-2-oxoheptan-3-yl)-4-methylbenzenesulfonamide
-
-
N-[[5-([2-[(4-bromo-2-fluorophenyl)amino]-2-oxoethyl]sulfanyl)-4-methyl-4H-1,2,4-triazol-3-yl]methyl]furan-2-carboxamide
-
-
Ni2+
50% inhibition at 0.011 mM
NP STOP
-
neuropsin-specific inhibitor. Single stimulus in S1 during application of NP STOP completely eliminates the late associativity between S0 and S1 synapses. When a strong (four) stimulus in S0 is followed by the application of NP STOP, the late associativity between S0 and S1 synapses is not eliminated
-
phenylmethylsulfonyl fluoride
-
-
Protein C inhibitor
-
-
-
serine protease inhibitor-3
formation of a SDS-stable complex, bimolecular kinetics; from pyramidal neurons; slowly and tightly binding inhibitor
-
shRNA
-
inhibition of endogenous KLK8 expression, reduces cancer cell invasiveness
-
trans-epoxysuccinyl-L-leucylamido(4-guanidinobutane)
i.e. E-64, 15% inhibition at 0.1 mM
antipain
50% inhibition at 0.00046 mM
antipain
0.2 mM, 100% inhibition
antipain
95% inhibition at 0.1 mM
Aprotinin
0.01 mg/ml, 98% inhibition
Aprotinin
65% inhibition at 0.1 mM
benzamidine
0.2 mM, 18% inhibition
benzamidine
56% inhibition at 1 mM
chymostatin
50% inhibition at 0.008 mM
chymostatin
80% inhibition at 0.1 mM
leupeptin
50% inhibition at 0.066 mM
leupeptin
0.2 mM, 95% inhibition
leupeptin
complete inhibition at 0.1 mM
serpinB6
-
is a physiologically relevant inhibitor of hK8 in skin. SerpinB6 protects the intracellular compartment of keratinocytes from ectopic hK8
-
Zn2+
50% inhibition at 0.0033 mM
Zn2+
-
28.6% residual activity at 10 mM
additional information
not inhibitory: Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone, pepstatin, o-phenynthroline, E-64
-
additional information
-
not inhibitory: Nalpha-p-tosyl-L-phenylalanine chloromethyl ketone, pepstatin, o-phenynthroline, E-64
-
additional information
-
KLK8 is not inhibited by EDTA and alpha1-antitrypsin; mature KLK8 activity is attenuated by autocleavage after Arg164
-
additional information
-
inhibitor screening by molecular modeling and ligand docking study, interactions with the active site, overview
-
additional information
enzyme is strongly inhibited by low molecular weight protease inhibitors that bind to His and Ser residues in the active center of serine proteases; no or very slight inhibition by pepstatin A, trypsin inhibitor, Ca2+, Mg2+, and metal chelators
-
additional information
-
enzyme is strongly inhibited by low molecular weight protease inhibitors that bind to His and Ser residues in the active center of serine proteases; no or very slight inhibition by pepstatin A, trypsin inhibitor, Ca2+, Mg2+, and metal chelators
-
additional information
-
no inhibition by soybean trypsin inhibitor
-
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0.4312
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.07
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
0.23 - 0.28
D-Val-Leu-Arg-4-nitroanilide
0.07
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
8.36
Pro-Phe-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.1533
Pro-Phe-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.1
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
0.07
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
0.1
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
37°C, pH 8.0
0.07
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
0.32
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.34
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.1844
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.2247
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.3699
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.1165
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.1407
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.22 - 0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
0.2983
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.3326
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.27 - 0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
0.0238
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.6897
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
0.23
D-Val-Leu-Arg-4-nitroanilide
recombinant enzyme, pH 8.0, 37°C
0.28
D-Val-Leu-Arg-4-nitroanilide
native enzyme, pH 8.0, 37°C
0.22
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.5
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.54
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
0.27
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant enzyme, pH 8.0, 37°C
0.28
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
0.3
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
native enzyme, pH 8.0, 37°C
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1.49
benzyloxycarbonyl-Gly-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
140
benzyloxycarbonyl-L-Val-L-Val-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
180
L-Pro-L-Phe-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
193
Pro-Phe-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
4.45
Pro-Phe-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
65
t-butyloxycarbonyl-L-Leu-L-Lys-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
40
t-butyloxycarbonyl-L-Phe-L-Ser-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
48
t-butyloxycarbonyl-L-Val-L-Leu-L-Lys-7-amido-4-methylcoumarin
37°C, pH 8.0
98
t-butyloxycarbonyl-L-Val-L-Pro-L-Arg-7-amido-4-methylcoumarin
37°C, pH 8.0
31.3
tert-butyloxycarbonyl-Asp(benzyloxy)-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
5.75
tert-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
3.39
tert-butyloxycarbonyl-Gln-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
1.43
tert-butyloxycarbonyl-Gln-Gly-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
1.62
tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
1.56
tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
34.8
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
3.57
tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
9.64
tert-butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
100
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide
recombinant wild-type enzyme, pH 8.0, 25°C
6.76
tert-butyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
2.11
tosyl-Gly-Pro-Arg-7-amido-4-methylcoumarin
-
in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C
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Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (O60259), Rattus norvegicus (O88780), Rattus norvegicus (P36374), Mus musculus (P07628), Mus musculus (Q61955)
brenda
Kishi, T.; Kato, M.; Shimizu, T.; Kato, K.; Matsumoto, K.; Yoshida, S.; Shiosaka, S.; Hakoshima, T.
Crystallization and preliminary X-ray analysis of neuropsin, a serine protease expressed in the limbic system of mouse brain
J. Struct. Biol.
118
248-251
1997
Mus musculus (Q61955), Mus musculus
brenda
Yoshida, S.; Taniguchi, M.; Hirata, A.; Shiosaka, S.
Sequence analysis and expression of human neuropsin cDNA and gene
Gene
213
9-16
1998
Homo sapiens (O60259), Homo sapiens, Mus musculus (Q61955), Mus musculus
brenda
Shimizu, C.; Yoshida, S.; Shibata, M.; Kato, K.; Momota, Y.; Matsumoto, K.; Shiosaka, T.; Midorikawa, R.; Kamachi, T.; Kawabe, A.; Shiosaka, S.
Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
J. Biol. Chem.
273
11189-11196
1998
Mus musculus (Q61955), Mus musculus
brenda
Underwood, L.J.; Tanimoto, H.; Wang, Y.; Shigemasa, K.; Parmley, T.H.; O'Brien, T.J.
Cloning of tumor-associated differentially expressed gene-14, a novel serine protease overexpressed by ovarian carcinoma
Cancer Res.
59
4435-4439
1999
Homo sapiens (O60259)
brenda
Kishi, T.; Kato, M.; Shimizu, T.; Kato, K.; Matsumoto, K.; Yoshida, S.; Shiosaka, S.; Hakoshima, T.
Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis
J. Biol. Chem.
274
4220-4224
1999
Mus musculus (Q61955), Mus musculus
brenda
Tani, N.; Matsumoto, K.; Ota, I.; Yoshida, S.; Takada, Y.; Shiosaka, S.; Matsuura, N.
Effects of fibronectin cleaved by neuropsin on cell adhesion and migration
Neurosci. Res.
39
247-251
2001
Mus musculus (Q61955), Mus musculus
brenda
Kato, K.; Kishi, T.; Kamachi, T.; Akisada, M.; Oka, T.; Midorikawa, R.; Takio, K.; Dohmae, N.; Bird, P.I.; Sun, J.; Scott, F.; Miyake, Y.; Yamamoto, K.; Machida, A.; Tanaka, T.; Matsumoto, K.; Shibata, M.; Shiosaka, S.
Serine proteinase inhibitor 3 and murinoglobulin I are potent inhibitors of neuropsin in adult mouse brain
J. Biol. Chem.
276
14562-14571
2001
Mus musculus (Q61955), Mus musculus
brenda
Oka, T.; Hakoshima, T.; Itakura, M.; Yamamori, S.; Takahashi, M.; Hashimoto, Y.; Shiosaka, S.; Kato, K.
Role of loop structures of neuropsin in the activity of serine protease and regulated secretion
J. Biol. Chem.
277
14724-14730
2002
Mus musculus (Q61955), Mus musculus
brenda
Matsumoto-Miyai, K.; Kitagawa, R.; Ninomiya, A.; Momota, Y.; Yoshida, S.; Shiosaka, S.
Decidualization induces the expression and activation of an extracellular protease neuropsin in mouse uterus
Biol. Reprod.
67
1414-1418
2002
Mus musculus (Q61955), Mus musculus
brenda
El Moujahed, A.; Gutman, N.; Brillard, M.; Gauthier, F.
Substrate specificity of two kallikrein family gene products isolated from the rat submandibular gland
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265
137-140
1990
Rattus norvegicus
brenda
Yousef, G.M.; Diamandis, E.P.
The new human tissue kallikrein gene family: structure, function, and association to disease
Endocr. Rev.
22
184-204
2001
Homo sapiens (O60259)
brenda
Chen, Z.L.; Yoshida, S.; Kato, K.; Momota, Y.; Suzuki, J.; Tanaka, T.; Ito, J.; Nishino, H.; Aimoto, S.; Kiyama, H.; Shiosaka, S.
Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
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15
5088-5097
1995
Mus musculus (Q61955), Mus musculus
brenda
Kishi, T.; Cloutier, S.M.; Kuendig, C.; Deperthes, D.; Diamandis, E.P.
Activation and enzymatic characterization of recombinant human kallikrein 8
Biol. Chem.
387
723-731
2006
Homo sapiens (O60259), Homo sapiens
brenda
Borgono, C.A.; Kishi, T.; Scorilas, A.; Harbeck, N.; Dorn, J.; Schmalfeldt, B.; Schmitt, M.; Diamandis, E.P.
Human kallikrein 8 protein is a favorable prognostic marker in ovarian cancer
Clin. Cancer Res.
12
1487-1493
2006
Homo sapiens
brenda
Rajapakse, S.; Ogiwara, K.; Takano, N.; Moriyama, A.; Takahashi, T.
Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins
FEBS Lett.
579
6879-6884
2005
Homo sapiens (O60259), Homo sapiens
brenda
Nakamura, Y.; Tamura, H.; Horinouchi, K.; Shiosaka, S.
Role of neuropsin in formation and maturation of Schaffer-collateral L1cam-immunoreactive synaptic boutons
J. Cell Sci.
119
1341-1349
2006
Mus musculus
brenda
Tamura, H.; Ishikawa, Y.; Hino, N.; Maeda, M.; Yoshida, S.; Kaku, S.; Shiosaka, S.
Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo
J. Physiol.
570
541-551
2006
Mus musculus
brenda
Li, Y.; Qian, Y.P.; Yu, X.J.; Wang, Y.Q.; Dong, D.G.; Sun, W.; Ma, R.M.; Su, B.
Recent origin of a hominoid-specific splice form of neuropsin, a gene involved in learning and memory
Mol. Biol. Evol.
21
2111-2115
2004
Homo sapiens (O60259), Homo sapiens
brenda
Shigemasa, K.; Tian, X.; Gu, L.; Tanimoto, H.; Underwood, L.J.; OBrien, T.J.; Ohama, K.
Human kallikrein 8 (hK8/TADG-14) expression is associated with an early clinical stage and favorable prognosis in ovarian cancer
Oncol. Rep.
11
1153-1159
2004
Homo sapiens
brenda
Sher, Y.P.; Chou, C.C.; Chou, R.H.; Wu, H.M.; Wayne Chang, W.S.; Chen, C.H.; Yang, P.C.; Wu, C.W.; Yu, C.L.; Peck, K.
Human kallikrein 8 protease confers a favorable clinical outcome in non-small cell lung cancer by suppressing tumor cell invasiveness
Cancer Res.
66
11763-11770
2006
Homo sapiens
brenda
Lu, Z.X.; Peng, J.; Su, B.
A human-specific mutation leads to the origin of a novel splice form of neuropsin (KLK8), a gene involved in learning and memory
Hum. Mutat.
28
978-984
2007
Homo sapiens (O60259), Homo sapiens, Macaca mulatta (Q5V9S7), Pan troglodytes (Q5V9U8)
brenda
Singh, J.; Naran, A.; Misso, N.L.; Rigby, P.J.; Thompson, P.J.; Bhoola, K.D.
Expression of kallikrein-related peptidases (KRP/hK5, 7, 6, 8) in subtypes of human lung carcinoma
Int. Immunopharmacol.
8
300-306
2008
Homo sapiens
brenda
Scott, F.L.; Sun, J.; Whisstock, J.C.; Kato, K.; Bird, P.I.
SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes
J. Biochem.
142
435-442
2007
Homo sapiens, Mus musculus
brenda
Kishibe, M.; Bando, Y.; Terayama, R.; Namikawa, K.; Takahashi, H.; Hashimoto, Y.; Ishida-Yamamoto, A.; Jiang, Y.P.; Mitrovic, B.; Perez, D.; Iizuka, H.; Yoshida, S.
Kallikrein 8 is involved in skin desquamation in cooperation with other kallikreins
J. Biol. Chem.
282
5834-5841
2007
Mus musculus, Mus musculus C57BL/6
brenda
Ishikawa, Y.; Horii, Y.; Tamura, H.; Shiosaka, S.
Neuropsin (KLK8)-dependent and -independent synaptic tagging in the Schaffer-collateral pathway of mouse hippocampus
J. Neurosci.
28
843-849
2008
Mus musculus
brenda
Pettus, J.R.; Johnson, J.J.; Shi, Z.; Davis, J.W.; Koblinski, J.; Ghosh, S.; Liu, Y.; Ravosa, M.J.; Frazier, S.; Stack, M.S.
Multiple kallikrein (KLK 5, 7, 8, and 10) expression in squamous cell carcinoma of the oral cavity
Histol. Histopathol.
24
197-207
2009
Homo sapiens, Mus musculus
brenda
Chow, T.F.; Crow, M.; Earle, T.; El-Said, H.; Diamandis, E.P.; Yousef, G.M.
Kallikreins as microRNA targets: an in silico and experimental-based analysis
Biol. Chem.
389
731-738
2008
Homo sapiens
brenda
Lu, Z.X.; Huang, Q.; Su, B.
Functional characterization of the human-specific (type II) form of kallikrein 8, a gene involved in learning and memory
Cell Res.
19
259-267
2009
Homo sapiens
brenda
Planque, C.; Li, L.; Zheng, Y.; Soosaipillai, A.; Reckamp, K.; Chia, D.; Diamandis, E.P.; Goodglick, L.
A multiparametric serum kallikrein panel for diagnosis of non-small cell lung carcinoma
Clin. Cancer Res.
14
1355-1362
2008
Homo sapiens
brenda
Yoshida, S.
Klk8, a multifunctional protease in the brain and skin: analysis of knockout mice
Biol. Chem.
391
375-380
2010
Mus musculus
brenda
Ohler, A.; Debela, M.; Wagner, S.; Magdolen, V.; Becker-Pauly, C.
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
Biol. Chem.
391
455-460
2010
Homo sapiens
brenda
Shingaki, K.; Matsuzaki, S.; Taniguchi, M.; Kubo, T.; Fujiwara, T.; Yamamoto, A.; Tamura, H.; Maeda, T.; Ooi, K.; Matsumoto, K.; Shiosaka, S.; Tohyama, M.
Molecular mechanism of kallikrein-related peptidase 8/neuropsin-induced hyperkeratosis in inflamed skin
Br. J. Dermatol.
163
466-475
2010
Homo sapiens, Mus musculus
brenda
Eissa, A.; Amodeo, V.; Smith, C.R.; Diamandis, E.P.
Kallikrein-related peptidase-8 (KLK8) is an active serine protease in human epidermis and sweat and is involved in a skin barrier proteolytic cascade
J. Biol. Chem.
286
687-706
2011
Homo sapiens
brenda
Ramachandran, R.; Eissa, A.; Mihara, K.; Oikonomopoulou, K.; Saifeddine, M.; Renaux, B.; Diamandis, E.; Hollenberg, M.D.
Proteinase-activated receptors (PARs): differential signalling by kallikrein-related peptidases KLK8 and KLK14
Biol. Chem.
393
421-427
2012
Homo sapiens
brenda
Azam, S.; Raza, S.
Structure modeling and hybrid virtual screening study of Alzheimers associated protease kallikrein 8 for the identification of novel inhibitors
Med. Chem. Res.
23
3516-3527
2014
Homo sapiens
-
brenda
Iinuma, S.; Kishibe, M.; Saito, N.; Igawa, S.; Honma, M.; Takahashi, H.; Bando, Y.; Yoshida, S.; Iizuka, H.; Ishida-Yamamoto, A.
Klk8 is required for microabscess formation in a mouse imiquimod model of psoriasis
Exp. Dermatol.
24
887-889
2015
Mus musculus (Q61955)
brenda
Wang, H.; Lin, C.; Pan, T.; Yeh, C.
Increase of serum kallikrein-8 level after long-term telbivudine treatment
In Vivo
32
955-960
2018
Homo sapiens (O60259), Homo sapiens
brenda
Raza, S.; Ranaghan, K.E.; van der Kamp, M.W.; Woods, C.J.; Mulholland, A.J.; Azam, S.S.
Visualizing protein-ligand binding with chemical energy-wise decomposition (CHEWD) application to ligand binding in the kallikrein-8 S1 site
J. Comput. Aided Mol. Des.
33
461-475
2019
Homo sapiens (O60259)
brenda
Cerqueira, C.; Samperio Ventayol, P.; Vogeley, C.; Schelhaas, M.
Kallikrein-8 proteolytically processes human papillomaviruses in the extracellular space to facilitate entry into host cells
J. Virol.
89
7038-7052
2015
Homo sapiens (O60259), Homo sapiens
brenda
Cao, B.; Yu, Q.; Zhao, W.; Tang, Z.; Cong, B.; Du, J.; Lu, J.; Zhu, X.; Ni, X.
Kallikrein-related peptidase 8 is expressed in myocardium and induces cardiac hypertrophy
Sci. Rep.
7
20024
2016
Rattus norvegicus (O88780)
brenda
Konar, A.; Kumar, A.; Maloney, B.; Lahiri, D.; Thakur, M.
A serine protease KLK8 emerges as a regulator of regulators in memory Microtubule protein dependent neuronal morphology and PKA-CREB signaling
Sci. Rep.
8
9928
2018
Mus musculus (Q61955), Mus musculus
brenda