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(7-methoxycoumarin-4-yl)acetyl-AKVYPYPME-(2,4-dinitrophenyldiaminopropionic acid) + H2O
(7-methoxycoumarin-4-yl)acetyl-AKVYP + YPME-(2,4-dinitrophenyldiaminopropionic acid)
-
-
-
?
83 kDa full-length protective antigen + H2O
20 kDa N-terminal fragment of protective antigen + 63 kDa N-terminal fragment of protective antigen
-
-
-
?
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-4-nitroanilide + H2O
?
-
-
-
?
acetyl-Gly-Tyr-beta-Ala-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Arg-Val-Leu-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
acetyl-Gly-Tyr-betaAla-RRRRRRRRVLR-4-nitroanilide + H2O
?
-
-
-
-
?
acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide + H2O
?
AcG-Y-betaA-R-R-R-A-R-R-R-R-V-L-R-4-nitroanilide + H2O
AcG-Y-betaA-R-R-R-A-R-R-R-R-V-L-R + 4-nitroaniline
-
-
-
-
?
AcM-L-A-R-R-R-P-V-L-P-4-nitroanilide + H2O
AcM-L-A-R-R-R-P-V-L-P + 4-nitroaniline
-
-
-
-
?
AcR-R-R-R-V-L-R-4-methylcoumarin-7-amide + H2O
AcR-R-R-R-V-L-R + 7-amino-4-methylcoumarin
-
-
-
-
?
AcR-R-R-R-V-L-R-4-nitroanilide + H2O
AcR-R-R-R-V-L-R + 4-nitroaniline
-
-
-
-
?
dansyl-RDIRRITLFSLH
?
-
i.e. S20D, substrate isolated from phage library
-
-
?
Dsor1 kinase + H2O
?
-
Dsor1 is a Drosophila mitogen-activated protein kinase kinase
-
-
?
fluorescein-QRRKKVYPYPME + H2O
fluorescein-QRRKKVYP + YPME
-
i.e. LF15, peptide substrate isolated from second-iteration substrate phage library
-
-
?
fluorescence resonance energy transfer peptide MAPKKide + H2O
?
-
-
-
-
?
Hep kinase + H2O
?
-
Hep (Hemipterous) is a Drosophila mitogen-activated protein kinase kinase
incubation of Hep with anthrax lethal factor generates a product of about 44 kDa
-
?
In2LF + H2O
In2LF fragments
-
-
-
?
Lic kinase + H2O
?
-
Lic (Licorne) is a Drosophila mitogen-activated protein kinase kinase
-
-
?
MAP kinase kinase 3b + H2O
?
-
-
-
-
?
Mca-KKPTPIQLN-Dnp + H2O
Mca-KKPTP + IQLN-Dnp
-
-
-
-
?
Mca-KKVYPYPMEK-Dnp + H2O
Mca-KKVYP + YPMEK-Dnp
-
-
-
-
?
Mca-KKWLMYPLEK-Dnp + H2O
Mca-KKWLM + YPLEK-Dnp
-
-
-
-
?
MEK2 + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 10-11
-
-
?
mitogen activated protein kinase kinase + H2O
?
-
-
-
-
?
mitogen activated protein kinase kinase 1 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase + H2O
?
mitogen-activated protein kinase 3 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase + H2O
?
mitogen-activated protein kinase kinase 1 + H2O
?
mitogen-activated protein kinase kinase 2 + H2O
?
mitogen-activated protein kinase kinase 3 + H2O
?
mitogen-activated protein kinase kinase 3b + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
mitogen-activated protein kinase kinase 6 + H2O
?
mitogen-activated protein kinase kinase 7 + H2O
?
mitogen-activated protein kinase kinase-1 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase-3 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase-4 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase-6 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase-7 + H2O
?
-
-
-
?
MKK3b + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 26-27
-
-
?
MKK4 + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 45-46 and 58-59
-
-
?
MKK6b + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 14-15
-
-
?
MKK7beta + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 44-45 and 76-77
-
-
?
NACHT leucine-rich repeat and pyrin domain-containing protein 1B + H2O
?
-
-
-
?
NOD-like receptor protein-1 + H2O
?
lethal factor cleaves rat NOD-like receptor protein Nlrp1. Cleavage is required for toxin-induced inflammasome activation, interleukin IL-1beta release, and macrophage pyroptosis
-
-
?
phosphorylated ERK1/2 + H2O
?
-
-
-
?
phosphorylated JNK1/2 + H2O
?
-
-
-
?
phosphorylated p38 + H2O
?
-
-
-
?
R9LF-1 + H2O
svR9LF-1 + NH2OH
-
-
-
?
SKARRKKVYPYPXENFPPSTARPT + H2O
SKARRKKVYP + YPXENFPPSTARPT
-
-
-
-
?
additional information
?
-
acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide + H2O
?
-
-
-
?
acetyl-GYbetaARRRRRRRRVLR-4-nitroanilide + H2O
?
commercial substrate S-pNA
-
-
?
MEK1 + H2O
?
-
i.e. signal-regulated kinase activator kinase
-
-
?
MEK1 + H2O
?
-
mitogen-activated protein kinase kinase, cleavage between residues 8-9
-
-
?
mitogen-activated protein kinase + H2O
?
-
-
-
-
?
mitogen-activated protein kinase + H2O
?
-
cleavage within N-terminus of MAPKKs
-
-
?
mitogen-activated protein kinase + H2O
?
-
substrate: MAPKK4, MAPKK6, MAPKK7, no substrate: MAPKK5
-
-
?
mitogen-activated protein kinase + H2O
?
-
substrate: MAPKK3, i.e. MKK3
-
-
?
mitogen-activated protein kinase + H2O
?
-
substrates: MAPKK1, MAPKK2
-
-
?
mitogen-activated protein kinase + H2O
?
-
inactivation of substrate
-
-
?
mitogen-activated protein kinase kinase + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase + H2O
?
-
anthrax lethal toxin cleaves mitogen-activated protein kinase kinase/MEK/MAPKK 1-4 and 6, but not mitogen-activated protein kinase kinase 5 and 7 in murine neutrophils
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 1 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 2 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 2 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 2 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 2 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 3 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 3 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 3 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 3 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 4 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 6 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 6 + H2O
?
-
-
-
?
mitogen-activated protein kinase kinase 6 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 6 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
mitogen-activated protein kinase kinase 7 + H2O
?
-
-
-
-
?
mitogen-activated protein kinase kinase 7 + H2O
?
-
specifically cleaves the aminoterminal 7 amino acids of mitogen-activated protein kinase kinases
-
-
?
mitogen-activated protein kinase kinase 7 + H2O
?
-
all but one of the mitogen-activated protein kinase kinases (MEK) are cleaved within 3 h, and the cleavage of MEKs in keratinocytes leads to their subsequent proteasome-mediated degradation at different rates
-
-
?
additional information
?
-
-
cleavage occurs within the N-terminal proline-rich regions of MAPKKs, consensus motifs
-
-
?
additional information
?
-
-
lethal factor acts directly on T and B lymphocytes, blocking antigen receptor-dependent proliferation, cytokine production and Ig production. In this manner, lethal factor mounts a broad-based attack on host-immunity, thus providing Bacillus anthracis with multiple mechanisms for avoiding protective host responses
-
-
?
additional information
?
-
-
does not cleave MEK5
-
-
?
additional information
?
-
-
participates in the activation of caspase-1
-
-
?
additional information
?
-
-
anthrax lethal factor cleaves and inactivates extracellular signal-regulated kinase kinases of the mitogen-activated protein kinase pathway in human dermal microvascular endothelial cells
-
-
?
additional information
?
-
-
lethal toxin treatment of murine J774A.1 macrophages results in caspase-1 recruitment to the Nalp1b-containing complex, concurrent with processing of cytosolic caspase-1 substrates. Nalp1b belongs to the NLR family of intracellular surveillance proteins, which are able to recognize pathogen-associated molecular patterns, including lipopolysaccharide (LPS). Nalp1b and caspase-1 are able to interact with each other
-
-
?
additional information
?
-
-
prevention of inflammatory response of immune system by preventing interleukin-8 expression: selective blocking of histone H3 phosphorylation at serine 10 and acetylation at lysine 14, H3 normally promotes the accessibility of NF-kappaB (transcription factor for inflammatory gene expression) to target promoters, the histone blocking is mitigated by cleaving mitogen-activated protein kinase kinase, thus preventing the activation of p38-mitogen-activated protein kinase and extracellular signal-regulated kinase
-
-
?
additional information
?
-
-
lethal factor cleaves it substrates between P1 and P1 and has a broad specificity with preference toward hydrophobic residues, but not charged or branched residues. The most preferred residues are, from P1 to P3, Trp, Leu, Met, Tyr, Pro, and Leu
-
-
?
additional information
?
-
the enzyme does not degrade mitogen-activated protein kinase kinase 7, Erk1/2, p38 and JNK1/2
-
-
?
additional information
?
-
-
the enzyme does not degrade mitogen-activated protein kinase kinase 7, Erk1/2, p38 and JNK1/2
-
-
?
additional information
?
-
-
an extremely polymorphic gene in the locus Nalp1b, is the primary mediator of mouse macrophage susceptibility to LeTx. LeTx-induced macrophage death requires caspase-1, which is activated in susceptible, but not resistant, macrophages after intoxication, suggesting that Nalp1b directly or indirectly activates caspase-1 in response to LeTx
-
-
?
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(1E,6E)-4-(1,3-dithian-2-ylidene)-1,7-difuran-2-ylhepta-1,6-diene-3,5-dione
-
-
(1Z,6E)-4-(1,3-dithian-2-ylidene)-1,7-difuran-2-ylhepta-1,6-diene-3,5-dione
-
-
(2R)-2-[(4-fluoro-3-methoxybenzene-1-sulfonyl)(2-methylpropyl)amino]-N-hydroxy-3-methylbutanamide
-
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)(2-methylpropyl)amino]-N-hydroxy-3-methylbutanamide
-
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)amino]-N-hydroxy-2-(oxan-4-yl)acetamide
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)[(4-nitrophenyl)methyl]amino]-N-hydroxypropanamide
-
(2R)-N4-hydroxy-N1-[(2S)-3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
-
inhibitor identified by in silico high-throughput virtual screening protocol
(2S)-2-(3,4-dichlorophenyl)-N-hydroxy-3-(3-methylphenyl)propanamide
-
(2S)-2-(4-fluoro-3,5-dimethylbenzyl)-6-[[1-(4-fluorophenyl)propyl]amino]-N-hydroxyhexanamide
i.e. PT-8541
(2S)-2-[(2R)-2-(4-fluorophenyl)-2-methoxyethyl]-6-[[1-(4-fluorophenyl)propyl]amino]-N-hydroxyhexanamide
i.e. PT-8420
(2S)-6-[(1R)-N-1-(4-fluorophenyl)propan]aminoamino-2-(4-fluoro-3,5-dimethylbenzyl)-N-hydroxyhexanamide
inhibitor provides protection against lethal infection when administered as a monotherapy. Two doses (10 mg/kg) administered at 2 h and 8 h after spore infection are sufficient to provide a significant survival benefit in infected mice
(2S)-6-[(4-fluorobenzyl)amino]-2-[(2R)-2-(4-fluorophenyl)-2-methoxyethyl]-N-hydroxyhexanamide
i.e. LFI4
(2S)-6-[N-1-(4-fluorophenyl)propan]amino-2-[(2R)-2-(4-fluorophenyl)-2-methoxyethyl]-N-hydroxyhexanamide
inhibitor provides protection against lethal infection when administered as a monotherapy. Two doses (10 mg/kg) administered at 2 h and 8 h after spore infection are sufficient to provide a significant survival benefit in infected mice
(3S)-N-hydroxy-4-methyl-3-([[(2R)-1-(methylamino)-1-oxo-4-phenylbutan-2-yl]amino]methyl)pentanamide
-
inhibitor identified by in silico high-throughput virtual screening protocol
(4E)-4-[(2,4-dihydroxyphenyl)methylidene]-1,2,5-thiadiazolidin-3-one
-
-
(5E)-5-(1,3-benzothiazol-2-ylimino)-1-(4-sulfophenyl)-4,5-dihydro-1H-pyrazole-3-carboxylic acid
-
-
(5Z)-3-(4-hydroxyphenyl)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-(4-methoxyphenyl)-2-thioxo-5-([5-[3-(trifluoromethyl)phenyl]furan-2-yl]methylidene)-1,3-thiazolidin-4-one
-
-
(5Z)-3-(furan-2-ylmethyl)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-3-(furan-2-ylmethyl)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[(2,4-dihydroxyphenyl)methylidene]-2-thioxoimidazolidin-4-one
-
-
(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-3-(2-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[5-(4-bromo-3-chlorophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-(furan-2-ylmethyl)-2-thioxo-1,3-thiazolidin-4-one
-
-
(5Z)-5-[[5-(4-fluorophenyl)furan-2-yl]methylidene]-3-prop-2-en-1-yl-2-thioxo-1,3-thiazolidin-4-one
-
-
(9E)-N-[2-(2,4,5-trihydroxyphenyl)ethyl]octadec-9-enamide
-
-
(9E)-N-[2-(3,4,5-trihydroxyphenyl)ethyl]octadec-9-enamide
-
-
(9Z)-N-(3,4-dihydroxybenzyl)octadec-9-enamide
-
-
(9Z)-N-[2-(3,4-dihydroxyphenyl)ethyl]octadec-9-enamide
-
-
(D-Arg)9-Trp-Leu-Met-CONHOH
-
(D-Arg)9-Val-Leu-Arg-CONHOH
-
1,4-dihydroxy-10-methoxy-5,8-dimethyl-3,7-dioxo-1,3-dihydro-7H-2,6,12-trioxabenzo[5,6]cyclohepta[1,2-e]indene-11-carbaldehyde
i.e. stictic acid
1-[(1S,2R,3S,4S,6S)-2-amino-6-[(6-amino-2,6-dideoxy-a-D-arabino-hexopyranosyl)oxy]-3,4-dihydroxycyclohexyl]guanidine
-
-
1-[([1,1'-biphenyl]-4-yl)methyl]-3-hydroxy-2-methylpyridine-4(1H)-thione
i.e. 94G5
2-([benzyl(ethyl)amino]methyl)-6-iodo-4-methylphenol
-
inhibitor identified by in silico high-throughput virtual screening protocol
2-chloro-4-(5-[(Z)-[(3-cyano-4,5,6,7-tetrahydro-1-benzothiophen-2-yl)imino]methyl]furan-2-yl)benzoic acid
-
-
2-chloro-4-(5-[(Z)-[4-oxo-3-(pyridin-3-ylmethyl)-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
-
-
2-chloro-4-[5-[(Z)-(4-oxo-3-prop-2-en-1-yl-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]furan-2-yl]benzoic acid
-
-
2-chloro-4-[[(4Z)-4-[[4-(methylsulfanyl)phenyl]methylidene]-5-oxo-2-phenyl-4,5-dihydro-1H-imidazol-1-yl]sulfamoyl]benzoic acid
-
-
2-chloro-5-(2,5-dimethyl-1H-pyrrol-1-yl)benzoic acid
-
-
2-chloro-5-[(4Z)-3-methyl-4-[[4-(1-methylethyl)phenyl]methylidene]-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
-
2-chloro-5-[(4Z)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
-
-
2-chloro-5-[[(4Z)-4-[[4-(methylsulfanyl)phenyl]methylidene]-5-oxo-2-phenylimidazolidin-1-yl]sulfamoyl]benzoic acid
-
-
2-hydroxy-5-(5-[(Z)-[2-imino-4-oxo-3-(1,3-thiazol-2-yl)-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
-
-
2-hydroxy-5-[5-[(Z)-[2-imino-3-[imino(methylsulfanyl)methyl]-4-oxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl]benzoic acid
-
-
2-thiolacetyl-YPM-amide
-
-
2-[[(2-amino-2-carboxyethyl)sulfanyl]methyl]-5-phenylfuran-3-carboxylic acid
-
-
2-[[benzyl(ethyl)amino]methyl]-4,6-diiodophenol
-
2-[[benzyl(ethyl)amino]methyl]-4-bromophenol
-
2-[[benzyl(ethyl)amino]methyl]-4-chlorophenol
-
3,3'-methanediylbis(6-hydroxybenzoic acid)
-
-
3,4-dihydroxy-N'-[(1Z)-(2-hydroxy-5-nitrophenyl)methylidene]benzohydrazide
-
-
3,5-diphenyl-2,6-bis(sulfanyl)-4H-thiopyran-4-one
-
3-(5-[(Z)-[1-(3-chlorophenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)benzoic acid
-
-
3-(benzyloxy)-1-(3,4-dichlorobenzene-1-sulfonyl)-N-hydroxypyrrolidine-2-carboxamide
-
3-(N-hydroxycarboxamido)-2-isobutylpropanoyl-Trp-methylamide
inhibitor used for structure-based pharmacopore model
3-[(5E)-5-[(3-bromo-4-methoxyphenyl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[(3-bromo-4-methoxyphenyl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
3-[(5Z)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-
-
4-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
-
-
4-(5-[(Z)-[3-(4-nitrophenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
-
-
4-methyl-N-[(1R)-1-[5-(naphthalen-1-yl)-2-(prop-2-en-1-yl)tetrahydrofuran-3-yl]ethyl]benzenesulfonamide
i.e. SM157, non-competitive inhibition
-
4-phenylaminocarbonylbis-demethoxycurcumin
-
inhibitory potency is comparable with curcumin, while showing improved solubility and stability
4-[(5Z)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]butanoic acid
-
-
4-[(5Z)-5-[[5-(4-bromophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]butanoic acid
-
-
4-[5-[(E)-(5-cyano-2-hydroxy-4-methyl-6-oxopyridin-3(6H)-ylidene)methyl]furan-2-yl]benzenesulfonamide
-
-
4-[5-[(Z)-(3-benzyl-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]furan-2-yl]benzoic acid
-
-
4-[5-[(Z)-[4-oxo-2-thioxo-3-[3-(trifluoromethyl)phenyl]-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl]benzoic acid
-
-
4-[[(4-chlorophenyl)carbamoyl]amino]-N-(5-ethyl-1,3,4-thiadiazol-2-yl)benzenesulfonamide
-
-
5-(4-carboxy-3-chlorophenyl)-2-[(Z)-[(3-cyano-4,5,6,7-tetrahydro-1-benzothiophen-2-yl)imino]methyl]furan-3-carboxylic acid
-
-
5-bromo-2-(5-[(Z)-[1-(3-carboxyphenyl)-5-oxo-3-(trifluoromethyl)-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)benzoic acid
-
-
5-bromo-2-(5-[(Z)-[1-(3-carboxyphenyl)-5-oxo-3-(trifluoromethyl)-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]uran-2-yl)benzoic acid
-
-
5-chloro-2-[5-[(E)-(1,5-dioxo-6,7,8,9-tetrahydro-5H-[1]benzothieno[3,2-e][1,3]thiazolo[3,2-a]pyrimidin-2(1H)-ylidene)methyl]furan-2-yl]benzoic acid
-
-
5-[4-[(E)-2-[(2R,3R,3'R)-3'-(3,5-dihydroxyphenyl)-6'-hydroxy-2,2'-bis(4-hydroxyphenyl)-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-5-yl]ethenyl]-6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-1-benzofuran-3-yl]benzene-1,3-diol
-
6-S-(3-aminopropyl)-6-thio-beta-D-cyclodextrin
-
-
6-S-(8-aminooctyl)-6-thio-beta-D-cyclodextin
-
-
6-S-[3-(aminomethyl)benzyl]-6-thio-beta-D-cyclodextrin
-
-
6-S-[4-(aminomethyl)benzyl]-6-thio-beta-D-cyclodextrin
-
-
8-[(E)-[[4-(2,3-dihydro-1,3-thiazol-2-ylsulfamoyl)phenyl]imino]methyl]-4H-1,3-benzodioxine-6-carboxylic acid
-
-
acetyl-GYbetaARRRRRRRRVLR-hydroxamate
-
-
AcG-Y-betaA-R-R-R-A-R-R-R-R-V-L-R-4-nitroanilide
-
substrate inhibition
AcM-L-A-R-R-R-P-V-L-P-4-nitroanilide
-
substrate inhibition
AcR-R-R-R-V-L-R-4-methylcoumarin-7-amide
-
substrate inhibition
AcR-R-R-R-V-L-R-4-nitroanilide
-
substrate inhibition
C-terminal dimer of the protective antigen binding domain of anthrax lethal factor
-
-
-
C-terminal trimer of the protective antigen binding domain of anthrax lethal factor
-
-
-
celastrol
-
celastrol, a quinine methide triterpene derived from a plant extract used in herbal medicine, inhibits lethal toxin-induced death of RAW264.7 murine macrophages. Celastrol does not prevent cleavage of mitogen activated protein kinase kinase 1. Celastrol confers almost complete protection when it is added up to 1.5 h after intoxication, indicating that it can rescue cells in the late stages of intoxication. Celastrol inhibits the proteasome-dependent degradation of proteins in RAW264.7 cells. Celastrol blocks stimulation of IL-18 processing, indicating that celastrol acts upstream of inflammasome activation
curcumin
-
inhibits by both decreasing catalytic capacity and increasing substrate affinity
fluvastatin
-
statins attenuate lethal factor action action. statin treatment maintains macrophage cell viability above 60% of untreated control cells even after 9 h of lethal toxin treatment. Statins decrease mitogen-activated protein kinase cleavage
guanidine hydrochloride
-
guanidine isothiocyanate
-
In2LF
i.e. Ac-Gly-Tyr-betaAla-(L-Arg)8-Val-Leu-Arg-CONHOH, competitive inhibitor
mevastatin
-
statins attenuate lethal factor action action. statin treatment maintains macrophage cell viability above 60% of untreated control cells even after 9 h of lethal toxin treatment. Statins decrease mitogen-activated protein kinase cleavage
N'1,N'4-bis[(1E)-(2-hydroxy-5-methylphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(1E)-(2-hydroxyphenyl)methylidene]-N'4-[(1Z)-(2-hydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N'1-[(1E)-(5-fluoro-2-hydroxyphenyl)methylidene]-N'4-[(1Z)-(5-fluoro-2-hydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
-
-
N,N''',N'''''',N'''''''''-[[(1R,3S,4S,6R)-4,6-dicarbamimidamidocyclohexane-1,3-diyl]bis(oxybenzene-1,2,4-triyl)]tetraguanidine
-
-
N,N'''-[(1R,3S)-4-(2,4-dicarbamimidamidonaphthalen-1-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S)-4-(2-amino-1H-benzimidazol-7-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4R,5R,6S)-4-[(2,6-dicarbamimidamido-2,6-dideoxy-a-D-glucopyranosyl)oxy]-5,6-dihydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4R,6R)-4-(2-carbamimidamidophenyl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4R,6R)-4-(4-carbamimidamidonaphthalen-1-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4R,6R)-4-(4-carbamimidamidophenyl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4S,6R)-4-(3-carbamimidamidopyridin-2-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1R,3S,4S,6R)-4-(5-carbamimidamidopyridin-2-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
-
-
N,N'''-[(1S,2R,3S,4S,6S)-6-[(6-amino-2-carbamimidamido-2,6-dideoxy-a-D-glucopyranosyl)oxy]-3,4-dihydroxycyclohexane-1,2-diyl]diguanidine
-
-
N,N'''-[4-[(1R,2S,4R,5R)-2,4-dicarbamimidamido-5-hydroxycyclohexyl]benzene-1,3-diyl]diguanidine
-
-
N,N'-bis(4-amino-2-methylquinolin-6-yl)urea
i.e. NSC12155, competitive inhibition
N-(4-amino-2-methylquinolin-6-yl)-3-(2-methoxyphenyl)propanamide
-
N-(4-amino-2-methylquinolin-6-yl)-4-(quinolin-6-yl)benzamide
-
N-2-benzyl-N-2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-D-alaninamide
-
N-2-[4-(aminomethyl)benzyl]-N-2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-D-alaninamide
-
N-hydroxy-4-[2-[(9E)-octadec-9-enoylamino]ethyl]benzamide
-
-
N-hydroxy-4-[[(9Z)-octadec-9-enoylamino]methyl]benzamide
-
-
N-hydroxy-N2-[[3-(methoxymethyl)phenyl]sulfonyl]-N2-(2-methylpropyl)-D-valinamide
-
N-oleoyldopamine
-
uncompetitive inhibition
N-terminal dimer of the protective antigen binding domain of anthrax lethal factor
-
-
-
N-terminal trimer of the protective antigen binding domain of anthrax lethal factor
-
-
-
N-[([1,1'-biphenyl]-4-yl)methyl]-3-hydroxy-4-sulfanylidene-4H-pyran-2-carbothioamide
-
N-[([1,1'-biphenyl]-4-yl)methyl]-3-hydroxy-6-methyl-4-sulfanylidene-4H-pyran-2-carboxamide
i.e. AM-2S
N-[3-(1,3-benzothiazol-2-yl)-4-methylthiophen-2-yl]-4-chlorobenzene-1-sulfonamide
-
N-[3-(1,3-benzothiazol-2-yl)thiophen-2-yl]-4'-methoxy[1,1'-biphenyl]-4-sulfonamide
-
N2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-N-2-(4-nitrobenzyl)-D-alaninamide
-
neamine
-
mixed-type, noncompetitive inhibition
NH4Cl
-
blocks mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages
simvastatin
-
statins attenuate lethal factor action action. statin treatment maintains macrophage cell viability above 60% of untreated control cells even after 9 h of lethal toxin treatment. Statins decrease mitogen-activated protein kinase cleavage
verapamil
-
blocks mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages
[(5Z)-5-([5-[2-chloro-5-(trifluoromethyl)phenyl]furan-2-yl]methylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(3-chloro-4-sulfamoylphenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(4-bromophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(4-chloro-2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[(5Z)-5-[[5-(4-iodophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-
-
[4-(2,5-dimethyl-1H-pyrrol-1-yl)phenyl]acetic acid
-
-
[4-[(5Z)-5-(furan-2-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]phenyl]acetic acid
-
-
[[4-(2,5-dimethyl-1H-pyrrol-1-yl)phenyl]sulfanyl]acetic acid
-
-
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)amino]-N-hydroxy-2-(oxan-4-yl)acetamide
i.e. L915
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)amino]-N-hydroxy-2-(oxan-4-yl)acetamide
-
neomycin B
-
mixed-type, noncompetitive inhibition
additional information
-
peptides that can block toxin assembly. Minimal peptide sequence TYWWLD can be used to develop potent polyvalent inhibitors of anthrax toxin
-
additional information
-
complete caspase-1 inhibition is required to block antrax lethal toxin-mediated necrosis
-
additional information
-
Ca2+-free medium completely prevents mitogen-activated protein kinase kinase 3 proteolysis in anthrax lethal toxin-treated macrophages
-
additional information
-
statin-mediated effects on lethal toxin action are attributable to disruption of Rho GTPases. The Rho GTPase-inactivating toxin, toxin B, does not significantly affect lethal toxin binding or internalization, suggesting that the Rho GTPases regulate trafficking and/or localization of lethal toxin once internalized
-
additional information
-
fusion protein of N-terminal 27 amino acids deletion of protective antigen-binding domain of anthrax lethal factor Delta27LFn and protective antigen-binding domain of edema factor is a 62-fold more potent toxin inhibitor than protective antigen-binding domain of anthrax lethal factor or protective antigen-binding domain of edema factor in a cell model of intoxication, and this increased activity corresponds to a 39-fold higher protective antigen-binding affinity by Biacore analysis. The fusion protein can protect the highly susceptible Fischer 344 rats from anthrax lethal toxin challenge
-
additional information
-
micromolar-level anthrax lethal factor inhibition can be attained by compounds with non-hydroxamate zinc-binding groups that exhibit monodentate zinc chelation as long as key hydrophobic interactions with at least two anthrax lethal factor subsites are retained
-
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0.003
(1E,6E)-4-(1,3-dithian-2-ylidene)-1,7-difuran-2-ylhepta-1,6-diene-3,5-dione
Bacillus anthracis
-
-
0.003
(1Z,6E)-4-(1,3-dithian-2-ylidene)-1,7-difuran-2-ylhepta-1,6-diene-3,5-dione
Bacillus anthracis
-
-
0.267
(2R)-2-[(4-fluoro-3-methoxybenzene-1-sulfonyl)(2-methylpropyl)amino]-N-hydroxy-3-methylbutanamide
Bacillus anthracis
pH and temperature not specified in the publication
0.09
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)(2-methylpropyl)amino]-N-hydroxy-3-methylbutanamide
Bacillus anthracis
pH and temperature not specified in the publication
0.0001
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)amino]-N-hydroxy-2-(oxan-4-yl)acetamide
Bacillus anthracis
pH and temperature not specified in the publication
0.0149
(2R)-2-[(4-fluoro-3-methylbenzene-1-sulfonyl)[(4-nitrophenyl)methyl]amino]-N-hydroxypropanamide
Bacillus anthracis
pH and temperature not specified in the publication
0.0102
(2R)-N4-hydroxy-N1-[(2S)-3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
Bacillus anthracis
-
pH 8.0, 37°C
0.0071
(3S)-N-hydroxy-4-methyl-3-([[(2R)-1-(methylamino)-1-oxo-4-phenylbutan-2-yl]amino]methyl)pentanamide
Bacillus anthracis
-
pH 8.0, 37°C
0.0034
(4E)-4-[(2,4-dihydroxyphenyl)methylidene]-1,2,5-thiadiazolidin-3-one
Bacillus anthracis
-
-
0.0077
(5E)-5-(1,3-benzothiazol-2-ylimino)-1-(4-sulfophenyl)-4,5-dihydro-1H-pyrazole-3-carboxylic acid
Bacillus anthracis
-
-
0.0377
(5Z)-3-(4-hydroxyphenyl)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.3
(5Z)-3-(4-methoxyphenyl)-2-thioxo-5-([5-[3-(trifluoromethyl)phenyl]furan-2-yl]methylidene)-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.0383
(5Z)-3-(furan-2-ylmethyl)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.0126
(5Z)-3-(furan-2-ylmethyl)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.0034
(5Z)-5-[(2,4-dihydroxyphenyl)methylidene]-2-thioxoimidazolidin-4-one
Bacillus anthracis
-
-
0.0319
(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-3-(2-phenylethyl)-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.0074
(5Z)-5-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.007
(5Z)-5-[[5-(4-bromo-3-chlorophenyl)furan-2-yl]methylidene]-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.15
(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-(furan-2-ylmethyl)-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.05
(5Z)-5-[[5-(4-fluorophenyl)furan-2-yl]methylidene]-3-prop-2-en-1-yl-2-thioxo-1,3-thiazolidin-4-one
Bacillus anthracis
-
-
0.07
(9E)-N-[2-(2,4,5-trihydroxyphenyl)ethyl]octadec-9-enamide
Bacillus anthracis
-
-
0.013
(9E)-N-[2-(3,4,5-trihydroxyphenyl)ethyl]octadec-9-enamide
Bacillus anthracis
-
-
0.015
(9Z)-N-(3,4-dihydroxybenzyl)octadec-9-enamide
Bacillus anthracis
-
-
0.015
(9Z)-N-[2-(3,4-dihydroxyphenyl)ethyl]octadec-9-enamide
Bacillus anthracis
-
-
0.0007
1-[(1S,2R,3S,4S,6S)-2-amino-6-[(6-amino-2,6-dideoxy-a-D-arabino-hexopyranosyl)oxy]-3,4-dihydroxycyclohexyl]guanidine
Bacillus anthracis
-
-
0.0495
2-([benzyl(ethyl)amino]methyl)-6-iodo-4-methylphenol
Bacillus anthracis
-
pH 8.0, 37°C
0.0042
2-chloro-4-(5-[(Z)-[(3-cyano-4,5,6,7-tetrahydro-1-benzothiophen-2-yl)imino]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0099
2-chloro-4-(5-[(Z)-[4-oxo-3-(pyridin-3-ylmethyl)-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0027
2-chloro-4-[5-[(Z)-(4-oxo-3-prop-2-en-1-yl-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]furan-2-yl]benzoic acid
Bacillus anthracis
-
-
0.0036
2-chloro-4-[[(4Z)-4-[[4-(methylsulfanyl)phenyl]methylidene]-5-oxo-2-phenyl-4,5-dihydro-1H-imidazol-1-yl]sulfamoyl]benzoic acid
Bacillus anthracis
-
-
0.0068
2-chloro-5-(2,5-dimethyl-1H-pyrrol-1-yl)benzoic acid
Bacillus anthracis
-
-
0.0079
2-chloro-5-[(4Z)-3-methyl-4-[[4-(1-methylethyl)phenyl]methylidene]-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
Bacillus anthracis
-
-
0.0021 - 0.0107
2-chloro-5-[(4Z)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
0.0025
2-chloro-5-[[(4Z)-4-[[4-(methylsulfanyl)phenyl]methylidene]-5-oxo-2-phenylimidazolidin-1-yl]sulfamoyl]benzoic acid
Bacillus anthracis
-
-
0.0048
2-hydroxy-5-(5-[(Z)-[2-imino-4-oxo-3-(1,3-thiazol-2-yl)-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0048
2-hydroxy-5-[5-[(Z)-[2-imino-3-[imino(methylsulfanyl)methyl]-4-oxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl]benzoic acid
Bacillus anthracis
-
-
0.0036
2-[[(2-amino-2-carboxyethyl)sulfanyl]methyl]-5-phenylfuran-3-carboxylic acid
Bacillus anthracis
-
-
0.0031
3,3'-methanediylbis(6-hydroxybenzoic acid)
Bacillus anthracis
-
-
0.2
3,4-dihydroxy-N'-[(1Z)-(2-hydroxy-5-nitrophenyl)methylidene]benzohydrazide
Bacillus anthracis
-
DS-998
0.0083 - 0.0105
3-(5-[(Z)-[1-(3-chlorophenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)benzoic acid
0.0044
3-[(5E)-5-[(3-bromo-4-methoxyphenyl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Bacillus anthracis
-
-
0.0044
3-[(5Z)-5-[(3-bromo-4-methoxyphenyl)methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Bacillus anthracis
-
-
0.0128
3-[(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Bacillus anthracis
-
-
0.0008
3-[(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Bacillus anthracis
-
-
0.0027
3-[(5Z)-5-[[5-(4-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
Bacillus anthracis
-
-
0.0043
4-(2,5-dimethyl-1H-pyrrol-1-yl)-2-hydroxybenzoic acid
Bacillus anthracis
-
-
0.0048
4-(5-[(Z)-[3-(4-nitrophenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.02
4-[(5Z)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]butanoic acid
Bacillus anthracis
-
-
0.0023
4-[(5Z)-5-[[5-(4-bromophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]butanoic acid
Bacillus anthracis
-
-
0.0083
4-[5-[(E)-(5-cyano-2-hydroxy-4-methyl-6-oxopyridin-3(6H)-ylidene)methyl]furan-2-yl]benzenesulfonamide
Bacillus anthracis
-
-
0.006
4-[5-[(Z)-(3-benzyl-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene)methyl]furan-2-yl]benzoic acid
Bacillus anthracis
-
-
0.0029
4-[5-[(Z)-[4-oxo-2-thioxo-3-[3-(trifluoromethyl)phenyl]-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl]benzoic acid
Bacillus anthracis
-
-
0.0039
4-[[(4-chlorophenyl)carbamoyl]amino]-N-(5-ethyl-1,3,4-thiadiazol-2-yl)benzenesulfonamide
Bacillus anthracis
-
-
0.0042
5-(4-carboxy-3-chlorophenyl)-2-[(Z)-[(3-cyano-4,5,6,7-tetrahydro-1-benzothiophen-2-yl)imino]methyl]furan-3-carboxylic acid
Bacillus anthracis
-
-
0.0017
5-bromo-2-(5-[(Z)-[1-(3-carboxyphenyl)-5-oxo-3-(trifluoromethyl)-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0017
5-bromo-2-(5-[(Z)-[1-(3-carboxyphenyl)-5-oxo-3-(trifluoromethyl)-1,5-dihydro-4H-pyrazol-4-ylidene]methyl]uran-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0008
5-chloro-2-[5-[(E)-(1,5-dioxo-6,7,8,9-tetrahydro-5H-[1]benzothieno[3,2-e][1,3]thiazolo[3,2-a]pyrimidin-2(1H)-ylidene)methyl]furan-2-yl]benzoic acid
Bacillus anthracis
-
-
0.039
5-[4-[(E)-2-[(2R,3R,3'R)-3'-(3,5-dihydroxyphenyl)-6'-hydroxy-2,2'-bis(4-hydroxyphenyl)-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-5-yl]ethenyl]-6-hydroxy-2-(3-hydroxyphenyl)-2,3-dihydro-1-benzofuran-3-yl]benzene-1,3-diol
Bacillus anthracis
pH and temperature not specified in the publication
0.0029
6-S-(3-aminopropyl)-6-thio-beta-D-cyclodextrin
Bacillus anthracis
-
-
0.0003
6-S-(8-aminooctyl)-6-thio-beta-D-cyclodextin
Bacillus anthracis
-
-
0.0005
6-S-[3-(aminomethyl)benzyl]-6-thio-beta-D-cyclodextrin
Bacillus anthracis
-
-
0.0007
6-S-[4-(aminomethyl)benzyl]-6-thio-beta-D-cyclodextrin
Bacillus anthracis
-
-
0.0093
8-[(E)-[[4-(2,3-dihydro-1,3-thiazol-2-ylsulfamoyl)phenyl]imino]methyl]-4H-1,3-benzodioxine-6-carboxylic acid
Bacillus anthracis
-
-
0.08
N'1,N'4-bis[(1E)-(2-hydroxy-5-methylphenyl)methylidene]benzene-1,4-dicarbohydrazide
Bacillus anthracis
-
-
0.05
N'1-[(1E)-(2-hydroxyphenyl)methylidene]-N'4-[(1Z)-(2-hydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Bacillus anthracis
-
-
0.05
N'1-[(1E)-(5-fluoro-2-hydroxyphenyl)methylidene]-N'4-[(1Z)-(5-fluoro-2-hydroxyphenyl)methylidene]benzene-1,4-dicarbohydrazide
Bacillus anthracis
-
-
0.00065
N,N''',N'''''',N'''''''''-[[(1R,3S,4S,6R)-4,6-dicarbamimidamidocyclohexane-1,3-diyl]bis(oxybenzene-1,2,4-triyl)]tetraguanidine
Bacillus anthracis
-
-
0.0107
N,N'''-[(1R,3S)-4-(2,4-dicarbamimidamidonaphthalen-1-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.1537
N,N'''-[(1R,3S)-4-(2-amino-1H-benzimidazol-7-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0007
N,N'''-[(1R,3S,4R,5R,6S)-4-[(2,6-dicarbamimidamido-2,6-dideoxy-a-D-glucopyranosyl)oxy]-5,6-dihydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0306
N,N'''-[(1R,3S,4R,6R)-4-(2-carbamimidamidophenyl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0314
N,N'''-[(1R,3S,4R,6R)-4-(4-carbamimidamidonaphthalen-1-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0149
N,N'''-[(1R,3S,4R,6R)-4-(4-carbamimidamidophenyl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0041
N,N'''-[(1R,3S,4S,6R)-4-(3-carbamimidamidopyridin-2-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0066
N,N'''-[(1R,3S,4S,6R)-4-(5-carbamimidamidopyridin-2-yl)-6-hydroxycyclohexane-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0005
N,N'''-[(1S,2R,3S,4S,6S)-6-[(6-amino-2-carbamimidamido-2,6-dideoxy-a-D-glucopyranosyl)oxy]-3,4-dihydroxycyclohexane-1,2-diyl]diguanidine
Bacillus anthracis
-
-
0.0006
N,N'''-[4-[(1R,2S,4R,5R)-2,4-dicarbamimidamido-5-hydroxycyclohexyl]benzene-1,3-diyl]diguanidine
Bacillus anthracis
-
-
0.0015
N-(4-amino-2-methylquinolin-6-yl)-3-(2-methoxyphenyl)propanamide
Bacillus anthracis
pH and temperature not specified in the publication
0.003
N-(4-amino-2-methylquinolin-6-yl)-4-(quinolin-6-yl)benzamide
Bacillus anthracis
pH and temperature not specified in the publication
0.0152
N-2-benzyl-N-2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-D-alaninamide
Bacillus anthracis
pH not specified in the publication, temperature not specified in the publication
0.0056
N-2-[4-(aminomethyl)benzyl]-N-2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-D-alaninamide
Bacillus anthracis
pH not specified in the publication, temperature not specified in the publication
0.032
N-hydroxy-4-[2-[(9E)-octadec-9-enoylamino]ethyl]benzamide
Bacillus anthracis
-
-
0.042
N-hydroxy-4-[[(9Z)-octadec-9-enoylamino]methyl]benzamide
Bacillus anthracis
-
-
0.95
N-hydroxy-N2-[[3-(methoxymethyl)phenyl]sulfonyl]-N2-(2-methylpropyl)-D-valinamide
Bacillus anthracis
pH and temperature not specified in the publication
0.015
N-oleoyldopamine
Bacillus anthracis
-
-
0.0149
N2-[(4-fluoro-3-methylphenyl)sulfonyl]-N-hydroxy-N-2-(4-nitrobenzyl)-D-alaninamide
Bacillus anthracis
pH not specified in the publication, temperature not specified in the publication
0.0031
[(5Z)-5-[[5-(2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.000265
[(5Z)-5-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.000298
[(5Z)-5-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0091
[(5Z)-5-[[5-(3-chloro-4-sulfamoylphenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0031
[(5Z)-5-[[5-(3-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.00085
[(5Z)-5-[[5-(4-bromophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0005
[(5Z)-5-[[5-(4-chloro-2-nitrophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0009
[(5Z)-5-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0055
[(5Z)-5-[[5-(4-iodophenyl)furan-2-yl]methylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
Bacillus anthracis
-
-
0.0076
[4-(2,5-dimethyl-1H-pyrrol-1-yl)phenyl]acetic acid
Bacillus anthracis
-
-
0.14
[4-[(5Z)-5-(furan-2-ylmethylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]phenyl]acetic acid
Bacillus anthracis
-
-
0.0029
[[4-(2,5-dimethyl-1H-pyrrol-1-yl)phenyl]sulfanyl]acetic acid
Bacillus anthracis
-
-
0.0021
2-chloro-5-[(4Z)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
Bacillus anthracis
-
-
0.0107
2-chloro-5-[(4Z)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
Bacillus anthracis
-
-
0.0083
3-(5-[(Z)-[1-(3-chlorophenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
0.0105
3-(5-[(Z)-[1-(3-chlorophenyl)-3,5-dioxopyrazolidin-4-ylidene]methyl]furan-2-yl)benzoic acid
Bacillus anthracis
-
-
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Vitale, G.; Bernardi, L.; Napolitani, G.; Mock, M.; Montecucco, C.
Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
Biochem. J.
352
739-745
2000
Bacillus anthracis
brenda
Duesbery, N.S.; Webb, C.P.; Leppla, S.H.; Gordon, V.M.; Klimpel, K.R.; Copeland, T.D.; Ahn, N.G.; Oskarsson, M.K.; Fukasawa, K.; Paull, K.D.; Vande Woude, G.F.
Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
Science
280
734-737
1998
Bacillus anthracis
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Pannifer, A.D.; Wong, T.Y.; Schwarzenbacher, R.; Renatus, M.; Petosa, C.; Bienkowska, J.; Lacy, D.B.; Collier, R.J.; Park, S.; Leppla, S.H.; Hanna, P.; Liddington, R.C.
Crystal structure of the anthrax lethal factor
Nature
414
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2001
Bacillus anthracis
brenda
Tonello, F.; Ascenzi, P.; Montecucco, C.
The metalloproteolytic activity of the anthrax lethal factor is substrate-inhibited
J. Biol. Chem.
278
40075-40078
2003
Bacillus anthracis
brenda
Pellizzari, R.; Guidi-Rontani, C.; Vitale, G.; Mock, M.; Montecucco, C.
Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNFalpha
FEBS Lett.
462
199-204
1999
Bacillus anthracis
brenda
Rossetto, O.; de Bernard, M.; Pellizzari, R.; Vitale, G.; Caccin, P.; Schiavo, G.; Montecucco, C.
Bacterial toxins with intracellular protease activity
Clin. Chim. Acta
291
189-199
2000
Bacillus anthracis
brenda
Glomski, I.J.; Fritz, J.H.; Keppler, S.J.; Balloy, V.; Chignard, M.; Mock, M.; Goossens, P.L.
Murine splenocytes produce inflammatory cytokines in MyD88-dependent response to Bacillus anthracis spores
cell. Microbiol.
9
502-513
2007
Bacillus anthracis
brenda
Gubbins, M.J.; Berry, J.D.; Corbett, C.R.; Mogridge, J.; Yuan, X.Y.; Schmidt, L.; Nicolas, B.; Kabani, A.; Tsang, R.S.
Production and characterization of neutralizing monoclonal antibodies that recognize an epitope in domain 2 of Bacillus anthracis protective antigen
FEMS Immunol. Med. Microbiol.
47
436-443
2006
Bacillus anthracis
brenda
Bergman, N.H.; Passalacqua, K.D.; Gaspard, R.; Shetron-Rama, L.M.; Quackenbush, J.; Hanna, P.C.
Murine macrophage transcriptional responses to Bacillus anthracis infection and intoxication
Infect. Immun.
73
1069-1080
2005
Bacillus anthracis
brenda
Comer, J.E.; Galindo, C.L.; Chopra, A.K.; Peterson, J.W.
GeneChip analyses of global transcriptional responses of murine macrophages to the lethal toxin of Bacillus anthracis
Infect. Immun.
73
1879-1885
2005
Bacillus anthracis
brenda
Koya, V.; Moayeri, M.; Leppla, S.H.; Daniell, H.
Plant-based vaccine: mice immunized with chloroplast-derived anthrax protective antigen survive anthrax lethal toxin challenge
Infect. Immun.
73
8266-8274
2005
Bacillus anthracis
brenda
Xu, L.; Frucht, D.M.
Bacillus anthracis: A multi-faceted role for anthrax lethal toxin in thwarting host immune defenses
Int. J. Biochem. Cell Biol.
39
20-24
2007
Bacillus anthracis
brenda
Baillie, L.W.J.
Past, imminent and future human medical countermeasures for anthrax
J. Appl. Microbiol.
101
594-606
2006
Bacillus anthracis
brenda
Cui, X.; Li, Y.; Li, X.; Haley, M.; Moayeri, M.; Fitz, Y.; Leppla, S.H.; Eichacker, P.Q.
Sublethal doses of Bacillus anthracis lethal toxin inhibit inflammation with lipopolysaccharide and Escherichia coli challenge but have opposite effects on survival
J. Infect. Dis.
193
829-840
2006
Bacillus anthracis
brenda
Gujraty, K.; Sadacharan, S.; Frost, M.; Poon, V.; kane, R.S.; Mogridge, J.
Functional characterization of peptide-based anthrax toxin inhibitors
Mol. Pharmacol.
2
367-372
2005
Bacillus anthracis
-
brenda
Boyden, E.D.; Dietrich, W.F.
Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
Nat. Genet.
38
240-244
2006
Bacillus subtilis
brenda
Mendelson, I.; Gat, O.; Aloni-Grinstein, R.; Altboum, Z.; Inbar, I.; Kronman, C.; Bar-Haim, E.; Cohen, S.; Velan, B.; Shafferman, A.
Efficacious, nontoxigenic Bacillus anthracis spore vaccines based on strains expressing mutant variants of lethal toxin components
Vaccine
23
5688-5697
2005
Bacillus anthracis
brenda
Sloat, B.R.; Cui, Z.
Nasal immunozation with a dual antigen anthrax vaccine induced strong mucosal and systemic immune responses against toxins and bacilli
Vaccine
24
6405-6413
2006
Bacillus anthracis
brenda
Moayeri, M.; Robinson, T.M.; Leppla, S.H.; Karginov, V.A.
In vivo efficacy of beta-cyclodextrin derivatives against anthrax lethal toxin
Antimicrob. Agents Chemother.
52
2239-2241
2008
Bacillus anthracis
brenda
Chvyrkova, I.; Zhang, X.C.; Terzyan, S.
Lethal factor of anthrax toxin binds monomeric form of protective antigen
Biochem. Biophys. Res. Commun.
360
690-695
2007
Bacillus anthracis (Q52NH3), Bacillus anthracis
brenda
Karginov, V.A.; Nestorovich, E.M.; Schmidtmann, F.; Robinson, T.M.; Yohannes, A.; Fahmi, N.E.; Bezrukov, S.M.; Hecht, S.M.
Inhibition of S. aureus alpha-hemolysin and B. anthracis lethal toxin by beta-cyclodextrin derivatives
Bioorg. Med. Chem.
15
5424-5431
2007
Bacillus anthracis
brenda
Gaddis, B.D.; Avramova, L.V.; Chmielewski, J.
Inhibitors of anthrax lethal factor
Bioorg. Med. Chem. Lett.
17
4575-4578
2007
Bacillus anthracis
brenda
Muehlbauer, S.M.; Evering, T.H.; Bonuccelli, G.; Squires, R.C.; Ashton, A.W.; Porcelli, S.A.; Lisanti, M.P.; Brojatsch, J.
Anthrax lethal toxin kills macrophages in a strain-specific manner by apoptosis or caspase-1-mediated necrosis
Cell Cycle
6
758-766
2007
Bacillus anthracis
brenda
Wickliffe, K.E.; Leppla, S.H.; Moayeri, M.
Anthrax lethal toxin-induced inflammasome formation and caspase-1 activation are late events dependent on ion fluxes and the proteasome
Cell. Microbiol.
10
332-343
2008
Bacillus anthracis
brenda
Rossi Paccani, S.; Tonello, F.; Patrussi, L.; Capitani, N.; Simonato, M.; Montecucco, C.; Baldari, C.T.
Anthrax toxins inhibit immune cell chemotaxis by perturbing chemokine receptor signalling
Cell. Microbiol.
9
924-929
2007
Bacillus anthracis
brenda
During, R.L.; Gibson, B.G.; Li, W.; Bishai, E.A.; Sidhu, G.S.; Landry, J.; Southwick, F.S.
Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation
EMBO J.
26
2240-2250
2007
Bacillus anthracis
brenda
Kuzmic, P.; Cregar, L.; Millis, S.Z.; Goldman, M.
Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides
FEBS J.
273
3054-3062
2006
Bacillus anthracis
brenda
Juris, S.J.; Melnyk, R.A.; Bolcome, R.E.; Chan, J.; Collier, R.J.
Cross-linked forms of the isolated N-terminal domain of the lethal factor are potent inhibitors of anthrax toxin
Infect. Immun.
75
5052-5058
2007
Bacillus anthracis
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Liu, S.; Wang, H.; Currie, B.M.; Molinolo, A.; Leung, H.J.; Moayeri, M.; Basile, J.R.; Alfano, R.W.; Gutkind, J.S.; Frankel, A.E.; Bugge, T.H.; Leppla, S.H.
Matrix metalloproteinase-activated anthrax lethal toxin demonstrates high potency in targeting tumor vasculature
J. Biol. Chem.
283
529-540
2008
Bacillus anthracis
brenda
Chang, H.H.; Tsai, M.F.; Chung, C.P.; Chen, P.K.; Hu, H.I.; Kau, J.H.; Huang, H.H.; Lin, H.C.; Sun, D.S.
Single-step purification of recombinant anthrax lethal factor from periplasm of Escherichia coli
J. Biotechnol.
126
277-285
2006
Bacillus anthracis
brenda
Schepetkin, I.A.; Khlebnikov, A.I.; Kirpotina, L.N.; Quinn, M.T.
Novel small-molecule inhibitors of anthrax lethal factor identified by high-throughput screening
J. Med. Chem.
49
5232-5244
2006
Bacillus anthracis
brenda
Dalkas, G.A.; Papakyriakou, A.; Vlamis-Gardikas, A.; Spyroulias, G.A.
Low molecular weight inhibitors of the protease anthrax lethal factor
Mini Rev. Med. Chem.
8
290-306
2008
Bacillus anthracis
brenda
Alfano, R.W.; Leppla, S.H.; Liu, S.; Bugge, T.H.; Herlyn, M.; Smalley, K.S.; Bromberg-White, J.L.; Duesbery, N.S.; Frankel, A.E.
Cytotoxicity of the matrix metalloproteinase-activated anthrax lethal toxin is dependent on gelatinase expression and B-RAF status in human melanoma cells
Mol. Cancer Ther.
7
1218-1226
2008
Bacillus anthracis
brenda
Guichard, A.; Park, J.M.; Cruz-Moreno, B.; Karin, M.; Bier, E.
Anthrax lethal factor and edema factor act on conserved targets in Drosophila
Proc. Natl. Acad. Sci. USA
103
3244-3249
2006
Bacillus anthracis
brenda
Bolcome, R.E.; Sullivan, S.E.; Zeller, R.; Barker, A.P.; Collier, R.J.; Chan, J.
Anthrax lethal toxin induces cell death-independent permeability in zebrafish vasculature
Proc. Natl. Acad. Sci. USA
105
2439-2444
2008
Bacillus anthracis
brenda
Fink, S.L.; Bergsbaken, T.; Cookson, B.T.
Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms
Proc. Natl. Acad. Sci. USA
105
4312-4317
2008
Bacillus anthracis
brenda
Barson, H.V.; Mollenkopf, H.; Kaufmann, S.H.; Rijpkema, S.
Anthrax lethal toxin suppresses chemokine production in human neutrophil NB-4 cells
Biochem. Biophys. Res. Commun.
374
288-293
2008
Bacillus anthracis
brenda
Tan, Y.K.; Kusuma, C.M.; St John, L.J.; Vu, H.A.; Alibek, K.; Wu, A.
Induction of autophagy by anthrax lethal toxin
Biochem. Biophys. Res. Commun.
379
293-297
2009
Bacillus anthracis
brenda
Jung, K.H.; Seo, G.M.; Yoon, J.W.; Park, K.S.; Kim, J.C.; Kim, S.J.; Oh, K.G.; Lee, J.H.; Chai, Y.G.
Protein expression pattern of murine macrophages treated with anthrax lethal toxin
Biochim. Biophys. Acta
1784
1501-1506
2008
Bacillus anthracis
brenda
Gaddis, B.D.; Rubert Perez, C.M.; Chmielewski, J.
Inhibitors of anthrax lethal factor based upon N-oleoyldopamine
Bioorg. Med. Chem. Lett.
18
2467-2470
2008
Bacillus anthracis
brenda
Reig, N.; Jiang, A.; Couture, R.; Sutterwala, F.S.; Ogura, Y.; Flavell, R.A.; Mellman, I.; van der Goot, F.G.
Maturation modulates caspase-1-independent responses of dendritic cells to Anthrax lethal toxin
Cell. Microbiol.
10
1190-1207
2008
Bacillus anthracis
brenda
Wickliffe, K.E.; Leppla, S.H.; Moayeri, M.
Killing of macrophages by anthrax lethal toxin: involvement of the N-end rule pathway
Cell. Microbiol.
10
1352-1362
2008
Bacillus anthracis
brenda
Levin, T.C.; Wickliffe, K.E.; Leppla, S.H.; Moayeri, M.
Heat shock inhibits caspase-1 activity while also preventing its inflammasome-mediated activation by anthrax lethal toxin
Cell. Microbiol.
10
2434-2446
2008
Bacillus anthracis
brenda
Omland, K.S.; Brys, A.; Lansky, D.; Clement, K.; Lynn, F.; Lynn, F.
Interlaboratory comparison of results of an anthrax lethal toxin neutralization assay for assessment of functional antibodies in multiple species
Clin. Vaccine Immunol.
15
946-953
2008
Bacillus anthracis
brenda
Chou, P.J.; Newton, C.A.; Perkins, I.; Friedman, H.; Klein, T.W.
Suppression of dendritic cell activation by anthrax lethal toxin and edema toxin depends on multiple factors including cell source, stimulus used, and function tested
DNA Cell Biol.
27
637-648
2008
Bacillus anthracis
brenda
Shaw, C.A.; Starnbach, M.N.
Both CD4+ and CD8+ T cells respond to antigens fused to anthrax lethal toxin
Infect. Immun.
76
2603-2611
2008
Bacillus anthracis
brenda
Nour, A.M.; Yeung, Y.G.; Santambrogio, L.; Boyden, E.D.; Stanley, E.R.; Brojatsch, J.
Anthrax lethal toxin triggers the formation of a membrane-associated inflammasome complex in murine macrophages
Infect. Immun.
77
1262-1271
2009
Bacillus anthracis
brenda
deCathelineau, A.M.; Bokoch, G.M.
Inactivation of rho GTPases by statins attenuates anthrax lethal toxin activity
Infect. Immun.
77
348-359
2009
Bacillus anthracis
brenda
Kocer, S.S.; Matic, M.; Ingrassia, M.; Walker, S.G.; Roemer, E.; Licul, G.; Simon, S.R.
Effects of anthrax lethal toxin on human primary keratinocytes
J. Appl. Microbiol.
105
1756-1767
2008
Bacillus anthracis
brenda
Xu, L.; Fang, H.; Frucht, D.M.
Anthrax lethal toxin increases superoxide production in murine neutrophils via differential effects on MAPK signaling pathways
J. Immunol.
180
4139-4147
2008
Bacillus anthracis
brenda
Warfel, J.M.; DAgnillo, F.
Anthrax lethal toxin enhances TNF-induced endothelial VCAM-1 expression via an IFN regulatory factor-1-dependent mechanism
J. Immunol.
180
7516-7524
2008
Bacillus anthracis
brenda
Alfano, R.W.; Leppla, S.H.; Liu, S.; Bugge, T.H.; Meininger, C.J.; Lairmore, T.C.; Mulne, A.F.; Davis, S.H.; Duesbery, N.S.; Frankel, A.E.
Matrix metalloproteinase-activated anthrax lethal toxin inhibits endothelial invasion and neovasculature formation during in vitro morphogenesis
Mol. Cancer Res.
7
452-461
2009
Bacillus anthracis
brenda
Chapelsky, S.; Batty, S.; Frost, M.; Mogridge, J.
Inhibition of anthrax lethal toxin-induced cytolysis of RAW264.7 cells by celastrol
PLoS ONE
3
e1421
2008
Bacillus anthracis
brenda
Raymond, B.; Batsche, E.; Boutillon, F.; Wu, Y.Z.; Leduc, D.; Balloy, V.; Raoust, E.; Muchardt, C.; Goossens, P.L.; Touqui, L.
Anthrax lethal toxin impairs IL-8 expression in epithelial cells through inhibition of histone H3 modification
PLoS Pathog.
5
e1000359
2009
Bacillus anthracis
brenda
Ha, S.D.; Ham, B.; Mogridge, J.; Saftig, P.; Lin, S.; Kim, S.O.
Cathepsin B-mediated autophagy flux facilitates the anthrax toxin receptor 2-mediated delivery of anthrax lethal factor into the cytoplasm
J. Biol. Chem.
285
2120-2129
2010
Bacillus anthracis
brenda
Pentelute, B.L.; Barker, A.P.; Janowiak, B.E.; Kent, S.B.; Collier, R.J.
A semisynthesis platform for investigating structure-function relationships in the N-terminal domain of the anthrax Lethal Factor
ACS Chem. Biol.
5
359-364
2010
Bacillus anthracis
brenda
Raymond, B.; Ravaux, L.; Memet, S.; Wu, Y.; Sturny-Leclere, A.; Leduc, D.; Denoyelle, C.; Goossens, P.L.; Paya, M.; Raymondjean, M.; Touqui, L.
Anthrax lethal toxin down-regulates type-IIA secreted phospholipase A(2) expression through MAPK/NF-kappaB inactivation
Biochem. Pharmacol.
79
1149-1155
2010
Bacillus anthracis
brenda
Ngai, S.; Batty, S.; Liao, K.C.; Mogridge, J.
An anthrax lethal factor mutant that is defective at causing pyroptosis retains proapoptotic activity
FEBS J.
277
119-127
2010
Bacillus anthracis
brenda
Kong, Y.; Guo, Q.; Yu, C.; Dong, D.; Zhao, J.; Cai, C.; Hou, L.; Song, X.; Fu, L.; Xu, J.; Chen, W.
Fusion protein of DELTA 27LFn and EFn has the potential as a novel anthrax toxin inhibitor
FEBS Lett.
583
1257-1260
2009
Bacillus anthracis
brenda
Zakharova, M.Y.; Kuznetsov, N.A.; Dubiley, S.A.; Kozyr, A.V.; Fedorova, O.S.; Chudakov, D.M.; Knorre, D.G.; Shemyakin, I.G.; Gabibov, A.G.; Kolesnikov, A.V.
Substrate recognition of anthrax lethal factor examined by combinatorial and pre-steady-state kinetic approaches
J. Biol. Chem.
284
17902-17913
2009
Bacillus anthracis
brenda
Chiu, T.L.; Solberg, J.; Patil, S.; Geders, T.W.; Zhang, X.; Rangarajan, S.; Francis, R.; Finzel, B.C.; Walters, M.A.; Hook, D.J.; Amin, E.A.
Identification of novel non-hydroxamate anthrax toxin lethal factor inhibitors by topomeric searching, docking and scoring, and in vitro screening
J. Chem. Inf. Model.
49
2726-2734
2009
Bacillus anthracis
brenda
Hu, H.; Leppla, S.H.
Anthrax toxin uptake by primary immune cells as determined with a lethal factor-beta-lactamase fusion protein
PLoS ONE
4
e7946
2009
Bacillus anthracis
brenda
Moayeri, M.; Crown, D.; Dorward, D.W.; Gardner, D.; Ward, J.M.; Li, Y.; Cui, X.; Eichacker, P.; Leppla, S.H.
The heart is an early target of anthrax lethal toxin in mice: a protective role for neuronal nitric oxide synthase (nNOS)
PLoS Pathog.
5
e1000456
2009
Bacillus anthracis
brenda
Abrami, L.; Kunz, B.; van der Goot, F.G.
Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake
Proc. Natl. Acad. Sci. USA
107
1420-1424
2010
Bacillus anthracis
brenda
Dalkas, G.A.; Papakyriakou, A.; Vlamis-Gardikas, A.; Spyroulias, G.A.
Insights into the anthrax lethal factor-substrate interaction and selectivity using docking and molecular dynamics simulations
Protein Sci.
18
1774-1785
2009
Bacillus anthracis
brenda
Kuklenyik, Z.; Boyer, A.E.; Lins, R.; Quinn, C.P.; Gallegos-Candela, M.; Woolfitt, A.; Pirkle, J.L.; Barr, J.R.
Comparison of MALDI-TOF-MS and HPLC-ESI-MS/MS for endopeptidase activity-based quantification of anthrax lethal factor in serum
Anal. Chem.
83
1760-1765
2011
Bacillus anthracis
brenda
Li, F.; Terzyan, S.; Tang, J.
Subsite specificity of anthrax lethal factor and its implications for inhibitor development
Biochem. Biophys. Res. Commun.
407
400-405
2011
Bacillus anthracis
brenda
Saebel, C.E.; Carbone, R.; Dabous, J.R.; Lo, S.Y.; Siemann, S.
Preparation and characterization of cobalt-substituted anthrax lethal factor
Biochem. Biophys. Res. Commun.
416
106-110
2011
Bacillus anthracis
brenda
Dalkas, G.A.; Chasapis, C.T.; Gkazonis, P.V.; Bentrop, D.; Spyroulias, G.A.
Conformational dynamics of the anthrax lethal factor catalytic center
Biochemistry
49
10767-10769
2010
Bacillus anthracis (P15917)
brenda
Little, S.F.; Webster, W.M.; Fisher, D.E.
Monoclonal antibodies directed against protective antigen of Bacillus anthracis enhance lethal toxin activity in vivo
FEMS Immunol. Med. Microbiol.
62
11-22
2011
Bacillus anthracis, Bacillus anthracis BH450
brenda
Liu, T.; Milia, E.; Warburton, R.R.; Hill, N.S.; Gaestel, M.; Kayyali, U.S.
Anthrax lethal toxin disrupts the endothelial permeability barrier through blocking p38 signaling
J. Cell. Physiol.
227
1438-1445
2012
Bacillus anthracis
brenda
Thomas, J.; Epshtein, Y.; Chopra, A.; Ordog, B.; Ghassemi, M.; Christman, J.W.; Nattel, S.; Cook, J.L.; Levitan, I.
Anthrax lethal factor activates K+ channels to induce IL-1beta secretion in macrophages
J. Immunol.
186
5236-5243
2011
Bacillus anthracis
brenda
Vuyisich, M.; Sanders, C.; Graves, S.
Binding and cell intoxication studies of anthrax lethal toxin
Mol. Biol. Rep.
2012
1-7
2012
Bacillus anthracis
brenda
Guichard, A.; McGillivray, S.; Cruz-Moreno, B.; Van Sorge, N.; Nizet, V.; Bier, E.
Anthrax toxins cooperatively inhibit endocytic recycling by the Rab11/Sec15 exocyst
Nature
467
854-858
2010
Bacillus anthracis
brenda
Rivera, J.; Cordero, R.; Nakouzi, A.; Frases, S.; Nicola, A.; Casadevall, A.
Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins
Proc. Natl. Acad. Sci. USA
107
19002-19007
2010
Bacillus anthracis, Bacillus anthracis 34F2
brenda
Bromberg-White, J.; Lee, C.S.; Duesbery, N.
Consequences and utility of the zinc-dependent metalloprotease activity of anthrax lethal toxin
Toxins
2
1038-1053
2010
Bacillus anthracis
brenda
Xie, T.; Auth, R.D.; Frucht, D.M.
The effects of anthrax lethal toxin on host barrier function
Toxins
3
591-607
2011
Bacillus anthracis
brenda
Maize, K.; Kurbanov, E.; De La Mora-Rey, T.; Geders, T.; Hwang, D.; Walters, M.; Johnson, R.; Amin, E.; Finzel, B.
Anthrax toxin lethal factor domain 3 is highly mobile and responsive to ligand binding
Acta Crystallogr. Sect. D
70
2813-2822
2014
Bacillus anthracis (P15917)
brenda
Moayeri, M.; Crown, D.; Jiao, G.; Kim, S.; Johnson, A.; Leysath, C.; Leppla, S.
Small-molecule inhibitors of lethal factor protease activity protect against anthrax infection
Antimicrob. Agents Chemother.
57
4139-4145
2013
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Vourtsis, D.; Chasapis, C.; Pairas, G.; Bentrop, D.; Spyroulias, G.
NMR conformational properties of an Anthrax lethal factor domain studied by multiple amino acid-selective labeling
Biochem. Biophys. Res. Commun.
450
335-340
2014
Bacillus anthracis (P15917)
brenda
Montpellier, L.; Siemann, S.
Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor
FEBS Lett.
587
317-321
2013
Bacillus anthracis (P15917)
brenda
Ouyang, W.; Torigoe, C.; Fang, H.; Xie, T.; Frucht, D.
Anthrax lethal toxin inhibits translation of hypoxia-inducible factor 1alpha and causes decreased tolerance to hypoxic stress
J. Biol. Chem.
289
4180-4190
2014
Bacillus anthracis
brenda
Antonelli, A.; Zhang, Y.; Golub, L.; Johnson, F.; Simon, S.
Inhibition of anthrax lethal factor by curcumin and chemically modified curcumin derivatives
J. Enzyme Inhib. Med. Chem.
29
663-669
2014
Bacillus anthracis
brenda
Lo, S.; Sbel, C.; Webb, M.; Walsby, C.; Siemann, S.
High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue
J. Inorg. Biochem.
140
12-22
2014
Bacillus anthracis (P15917)
brenda
Liao, H.; Liu, H.; Chen, W.; Ho, Y.
Structure-based pharmacophore modeling and virtual screening to identify novel inhibitors for anthrax lethal factor
Med. Chem. Res.
23
3725-3732
2014
Bacillus anthracis (P15917)
-
brenda
Sun, C.; Fang, H.; Xie, T.; Auth, R.; Patel, N.; Murray, P.; Snoy, P.; Frucht, D.
Anthrax lethal toxin disrupts intestinal barrier function and causes systemic infections with enteric bacteria
PLoS ONE
7
e33583
2012
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Levinsohn, J.; Newman, Z.; Hellmich, K.; Fattah, R.; Getz, M.; Liu, S.; Sastalla, I.; Leppla, S.; Moayeri, M.
Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome
PLoS Pathog.
8
e1002638
2012
Bacillus anthracis (P15917)
brenda
Kassab, E.; Darwish, M.; Timsah, Z.; Liu, S.; Leppla, S.; Frankel, A.; Abi-Habib, R.
Cytotoxicity of anthrax lethal toxin to human acute myeloid leukemia cells is nonapoptotic and dependent on extracellular signal-regulated kinase 1/2 activity
Transl. Oncol.
6
25-32
2013
Bacillus anthracis (P15917)
brenda
Lo, S.Y.; Saebel, C.E.; Mapletoft, J.P.J.; Siemann, S.
Influence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor
Biochem. Biophys. Rep.
1
68-77
2015
Bacillus anthracis (P15917)
brenda
Goldberg, A.B.; Turk, B.E.
Inhibitors of the metalloproteinase anthrax lethal factor
Curr. Top. Med. Chem.
16
2350-2358
2016
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Maize, K.M.; Kurbanov, E.K.; Johnson, R.L.; Amin, E.A.; Finzel, B.C.
Ligand-induced expansion of the S1 site in the anthrax toxin lethal factor
FEBS Lett.
589
3836-3841
2015
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Zhang, W.W.; Wang, X.; Xie, P.; Yuan, S.T.; Liu, Q.H.
Anthrax lethal toxin suppresses high glucose induced VEGF over secretion through a post-translational mechanism
Int. J. Ophthalmol.
8
453-458
2015
Bacillus anthracis (P15917)
brenda
Ma, P.; Cardenas, A.E.; Chaudhari, M.I.; Elber, R.; Rempe, S.B.
The impact of protonation on early translocation of anthrax lethal factor kinetics from molecular dynamics simulations and milestoning theory
J. Am. Chem. Soc.
139
14837-14840
2017
Bacillus anthracis (P15917)
brenda
Ouyang, W.; Guo, P.; Fang, H.; Frucht, D.M.
Anthrax lethal toxin rapidly reduces c-Jun levels by inhibiting c-Jun gene transcription and promoting c-Jun protein degradation
J. Biol. Chem.
292
17919-17927
2017
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Goldberg, A.B.; Cho, E.; Miller, C.J.; Lou, H.J.; Turk, B.E.
Identification of a substrate-selective exosite within the metalloproteinase anthrax lethal factor
J. Biol. Chem.
292
814-825
2017
Bacillus anthracis (P15917), Bacillus anthracis
brenda
Krantz, B.
Anthrax lethal toxin co-complexes are stabilized by contacts between adjacent lethal factors
J. Gen. Physiol.
148
1966-1970
2016
Bacillus anthracis (P15917)
brenda
Young, C.J.; Richard, K.; Beruar, A.; Lo, S.Y.; Siemann, S.
An investigation of the pH dependence of copper-substituted anthrax lethal factor and its mechanistic implications
J. Inorg. Biochem.
182
1-8
2018
Bacillus anthracis (P15917)
brenda
Kong, Q.; Song, Y.; Mu, M.; Han, X.; Si, C.; Li, F.
Effects of metalloprotease anthrax lethal factor on its peptide-based inhibitor R9LF-1
Mol. Cell. Biochem.
406
293-299
2015
Bacillus anthracis (P15917), Bacillus anthracis
brenda