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5'-tetramethylrhodamine-5(6)-carboxamide-DEVD-cyanine 5 + H2O
?
-
-
-
-
?
70kDa U1 small ribonucleoprotein + H2O
?
-
cleavage site is DGPD-/-
-
-
?
Ac-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
Ac-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DEVD-4-methylcoumarin 7-amide + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
an artificial caspase-3 substrate
-
-
?
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
Ac-DMQD-4-nitroanilide + H2O
Ac-DMQD + 4-nitroaniline
weak substrate
-
-
?
Ac-IETD-4-nitroanilide + H2O
Ac-IETD + 4-nitroaniline
an artificial caspase-8 substrate, low activity
-
-
?
Ac-LEHD-4-nitroanilide + H2O
Ac-LEHD + 4-nitroaniline
an artificial caspase-9 substrate, low activity
-
-
?
Ac-VDQQD-4-nitroanilide + H2O
Ac-VDQQD + 4-nitroaniline
weak substrate
-
-
?
acetyl-Asp-Glu-Val-Asp-4-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + 4-nitroaniline
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
?
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
acetyl-CDEVDK + H2O
acetyl-CDEVD + Lys
-
-
-
-
?
acetyl-DEVD-4-methylcoumarin-7-amide + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
-
-
-
-
?
acetyl-DEVD-4-trifluoromethylcoumarin-7-amide + H2O
?
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
-
-
-
-
?
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
low activity towards the caspase-6 and caspase-8 substrate
-
-
?
acetyl-L-Asp-L-Glu-L-Val-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Glu-L-Val-L-Asp + 4-nitroaniline
-
-
-
?
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Asp-L-Glu-L-Val-L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-L-Asp-L-Met-L-Gln-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Met-L-Gln-L-Asp + 4-nitroaniline
-
-
-
?
acetyl-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
-
-
-
?
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
-
-
-
?
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
-
-
-
?
acetyl-LEHD-4-methylcoumarin-7-amide + H2O
acetyl-LEHD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-LEHD-7-amido-4-methylcoumarin + H2O
acetyl-LEHD + 7-amino-4-methylcoumarin
-
low activity towards the caspase-9 substrate
-
-
?
acetyl-VDQMDGW-amide + H2O
?
acetyl-VDQQD-4-nitroanilide + H2O
acetyl-VDQQD + 4-nitroaniline
-
-
-
-
?
acetyl-VDVAD-4-nitroanilide + H2O
acetyl-VAVAD + 4-nitroaniline
-
-
-
-
?
acetyl-VEID-4-methylcoumarin-7-amide + H2O
acetyl-VEID + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
-
-
-
-
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
-
-
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
-
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
low activity towards the caspase-1 substrate
-
-
?
alpha-spectrin + H2O
?
-
-
production of a 120 kDa fragment
-
?
anamorsin + H2O
?
-
specifically cleaved by caspase-3 at DSVD209 L generating 25- and 10-kDa fragments
-
-
?
Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin + H2O
benzoyl-L-Asp-L-Glu-L-Val-L-Asp + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-DEVD-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
beta-catenin + H2O
?
-
processing of beta-catenin, production of a 70000 Da fragment
-
-
?
beta-N-acetylglucosaminidase + H2O
?
biotinylated acetyl-CDEVDK + H2O
biotinylated acetyl-CDEVD + Lys
-
-
-
-
?
caspase 9 + H2O
?
-
cleavage by caspase 3 does not result in activation of caspase 9, but enhances apoptosis by alleviating XIAP inhibition of the apical caspase
-
-
?
D4 G-protein dissociation inhibitor + H2O
?
-
cleavage site is DELD-/-
-
-
?
D4-GDI(Rho-GDI 2) + H2O
?
-
differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
DEVD-7-amido-4-methylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
DEVD-7-amido-4-trifluoromethylcoumarin + H2O
DEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
DEVD-amido-4-trifluoromethylcoumarin + H2O
DEVD + amino-4-trifluoromethylcoumarin
-
-
-
?
DEVD-FQ + H2O
N2-acetyl-L-lysyl-L-lysyl-L-lysyl-L-arginyl-L-lysyl-L-valyl-beta-alanyl-N6-[[1-([2-[(3E)-3-(2,3-dihydro-1H-indolium-1-ylidene)-6-(2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]phenyl]sulfonyl)piperidin-4-yl]carbonyl]-L-lysyl-N-[(2R)-2-(carboxymethyl)-3-[[(2S)-1-[[(1S)-1,2-dicarboxyethyl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-oxopropyl]-D-phenylalaninamide + L-alanyl-N-[2-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]ethyl]-L-prolinamide
-
highly selective substrate for caspase-3
-
-
?
DEVD-NucView488 + H2O
?
-
the highly cell-permeable caspase-3 substrate is obtained by linking a fluorogenic DNA-binding dye to the caspase-3 recognition sequence that renders the dye nonfunctional. On substrate cleavage, the dye is released and becomes highly fluorescent on binding to DNA. DEVD-NucView488 detects caspase-3 activation within a live-cell population much earlier and with higher sensitivity compared with other apoptosis reagents. Cells incubated with DEVD-NucView488 exhibit no toxicity and normal apoptotic progression. DEVD-NucView488 is an ideal substrate for kinetic studies of caspase-3 activation because it detects caspase-3 activity in real-time and also efficiently labels DNA in nuclei of caspase-3-activated cells for real-time fluorescent visualization of apoptotic morphology
-
-
?
DNA-dependent protein kinase CS + H2O
?
-
cleavage site is DEVD-/-
-
-
?
DW3-FQ + H2O
N2-acetyl-L-lysyl-L-lysyl-L-lysyl-L-arginyl-L-lysyl-L-valyl-beta-alanyl-N6-[[1-([2-[(3E)-3-(2,3-dihydro-1H-indolium-1-ylidene)-6-(2,3-dihydro-1H-indol-1-yl)-3H-xanthen-9-yl]phenyl]sulfonyl)piperidin-4-yl]carbonyl]-L-lysyl-N-[(2R)-2-(carboxymethyl)-3-[[(3S)-1-[[(2S)-1-[[(1S)-1,2-dicarboxyethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]amino]-3-oxopropyl]-D-phenylalaninamide + L-alanyl-N-[2-[(6-[3,3-dimethyl-2-[(1E,3E,5E)-5-(1,3,3-trimethyl-1,3-dihydro-2H-indol-2-ylidene)penta-1,3-dien-1-yl]-3H-indolium-1-yl]hexanoyl)amino]ethyl]-L-prolinamide
-
-
-
-
?
epidermal growth factor receptor + H2O
?
glutaredoxin-1 + H2O
?
-
murine or human protein substrate, the putative cleavage site of caspase-3, amino acids 56-59 EFVD and 56-59 AIQD, which has predicted affiffinity toward glutamic and aspartic acid residues
cleavage produces a 8 kDA fragment
-
?
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
IETD-7-amido-4-fluoromethylcoumarin + H2O
IETD + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
Ile-Glu-Thr-Asp-4-nitroanilide + H2O
Ile-Glu-Thr-Asp + 4-nitroaniline
-
-
-
-
?
LLVY-4-methylcoumarin 7-amide + H2O
LLVY + 7-amino-4-methylcoumarin
-
-
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
myeloid cell leukemia 1 + H2O
?
-
i.e. Mcl-1, apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand requires specific cleavage of Mcl-1 at D127 and D157 by enzyme. Removal of N-terminal domain of Mcl-1 by enzyme allows for the maximal mitochondrial perturbation that potentiates apoptosis
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Ala-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Asn-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Glu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Gly-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Pro-Asp-N6-[methyl red]-Lys-6-aminohexanoyl-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
the substrate is able to detect and quantify caspase-3 activity in apoptotic cells without cross-reactivity by caspase-7
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Leu-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Pro-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-(5(6)-carboxyfluoresceinyl)-6-aminohexanoyl-Asp-Val-Val-Asp-6-aminohexanoyl-N6-[methyl red]-Lys-[N-(6-aminohexyl)-Gly]8-N2-(6-aminohexyl)-Gly-NH2 + H2O
?
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp 4-nitroanilide + H2O
?
-
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-acetyl-DEVD-4-trifluoromethylcoumarin 7-amide + H2O
N-acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-DEVD-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
-
-
-
-
?
N-acetyl-L-Asp-L-Glu-L-Val-L-Asp-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
-
cell-permeable substrate, high turnover rate and sensitivity both in enzyme solution and in living cells
-
-
?
N-acetyl-LDEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-LDEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzyloxy-DEVD-R110 + H2O
?
-
a fluorescent substrate
-
-
?
nuclear mitotic apparatus protein + H2O
?
PAK2 + H2O
?
-
caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
poly(ADP-ribose) polymerase + H2O
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-caspase-6 + H2O
?
-
caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
-
-
?
pro-interleukin-18 + H2O
IL18 + ?
-
virus infection by influenzy A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
procaspase-3 + H2O
caspase-3 + ?
procaspase-6 + H2O
caspase-6 + ?
protein kinase Cdelta + H2O
?
protein kinase Czeta + H2O
?
protein phosphatase-1 inhibitor-3 + H2O
?
RelB + H2O
?
-
the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
-
-
?
Rho-GDI 1 + H2O
?
-
differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
-
-
?
sterol regulatory element-binding protein + H2O
?
-
cleavage site is DEPD-/-
-
-
?
topoisomerase I + H2O
?
-
cleavage at DDVD146-/-Y and EEED170-/-G
-
-
?
transcription factor Pax7 + H2O
?
additional information
?
-
19 S proteasome + H2O
?
-
-
-
-
?
19 S proteasome + H2O
?
-
caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity
-
-
?
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
-
-
-
?
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
an artificial caspase-3 substrate
-
-
?
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
-
-
-
?
Ac-DEVD-4-nitroanilide + H2O
Ac-DEVD + 4-nitroaniline
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
the active site of caspase-3 is located at Cys163, which plays a key role in substrate hydration
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
high activity
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
DEVD is the optimal tetrapeptide recognition motif
-
-
?
acetyl-VDQMDGW-amide + H2O
?
-
-
-
-
?
acetyl-VDQMDGW-amide + H2O
?
-
preferred peptide substrate
-
-
?
Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
-
-
-
?
Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
caspase-3 specific substrate
-
-
?
Asp-Glu-Val-Asp-4-nitroanilide + H2O
Asp-Glu-Val-Asp + 4-nitroaniline
-
-
-
-
?
beta-N-acetylglucosaminidase + H2O
?
-
cleavage during apoptosis into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyltransferases, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo. O-GlcNAcase activity is not affected by caspase-3 cleavage because the N- and C-terminal O-GlcNAcase fragments remain associated after the cleavage
-
-
?
beta-N-acetylglucosaminidase + H2O
?
-
mapping of the celavage site by Edman sequencing, the site is a noncanonical recognition site that occurs after Asp413 of the SVVD sequence in human substrate O-GlcNAcase, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo
-
-
?
Bid peptide + H2O
?
-
-
-
-
?
Bid peptide + H2O
?
-
-
-
-
?
cytokeratine 18 + H2O
?
-
-
-
-
?
cytokeratine 18 + H2O
?
-
caspase-induced cytokeratine 18 cleavage in apoptotic cell populations
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
-
-
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
-
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
-
-
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
-
-
-
-
?
DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
eIF4G + H2O
?
-
-
-
-
?
eIF4G + H2O
?
-
caspase 3 is capable of cleaving eIF4G as part of the translationally active complex eIF4F, thereby inactivating this complex and subsequently causing inhibition of translation in apoptotic cells
-
-
?
epidermal growth factor receptor + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
cleavage during apoptosis
-
-
?
huntingtin + H2O
?
-
-
-
?
huntingtin + H2O
?
-
cleavage site is DEED-/-
-
-
?
ICAD + H2O
?
-
activity of caspase-activated deoxyribonuclease, CAD, is affected by the caspase 3-mediated cleavage of the CAD inhibitor, ICAD
-
-
?
ICAD + H2O
?
-
caspase 3-mediated cleavage of the caspase-activated deoxyribonuclease inhibitor, ICAD
-
-
?
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
-
-
-
-
?
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
-
-
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
-
i.e. Mst1. Caspase 3 preferentially activates extracellular signal-regulated kinase preferentially through 36000 Da cleaved forms of Mst1. The 36000 Da form of Mst1 selectively phosphorylates extracellular signal-regulated kinase
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
-
i.e. Mst1
-
-
?
Mcl-1 + H2O
?
-
antiapoptotic protein. Caspase-3 -mediated Mcl-1 downregulation appears to be responsible for the pro-apoptotic effects of EXEL-0862 on FIP1L1-PDGFRalpha-expressing cells
-
-
?
Mcl-1 + H2O
?
-
antiapoptotic protein
-
-
?
MDM2 oncoprotein + H2O
?
-
-
-
-
?
MDM2 oncoprotein + H2O
?
-
because MDM2 functions as a negative regulator of the p53 tumor suppressor and because p53 induces apoptosis in response to a variety of stimuli, this cleavage of MDM2 by CPP32-like proteases may result in deregulation of p53 and contribute directly to the process of apoptotic cell death
-
-
?
nuclear mitotic apparatus protein + H2O
?
-
-
-
-
?
nuclear mitotic apparatus protein + H2O
?
-
cleavage at sites distinct from caspase-6
-
-
?
p65/RelA + H2O
?
-
caspase-3-mediated carboxy-terminal fragment of p65/RelA production, cells producing this truncated p65/RelA do not undergo apoptosis but show a high viability, in spite of caspase-3 activation, overview. The substrate translocate to the nucleus, associates with NF-kappaB1/p50 and IkappaBalpha, but cannot bind -kappaB consensus sites
-
-
?
p65/RelA + H2O
?
-
caspase-3-mediated carboxy-terminal fragment of p65/RelA production, no activity with substrate mutants V91L/D94E, D97E, and D94E/D97E
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
caspase cleaves at a DEVD-G motif
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
bovine poly(ADP-ribose) polymerase
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
very high cleavage
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
cleavage site: DEVD-/-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
-
-
?
pro-Mch2alpha + H2O
?
-
the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme
-
-
?
pro-Mch2alpha + H2O
?
-
the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme. Mch2alpha is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
-
-
?
pro-Mch6 + H2O
?
-
the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da
-
-
?
pro-Mch6 + H2O
?
-
the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da. Mch6 is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation requires caspase-3
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation requires caspase-3
-
-
?
protein kinase Cdelta + H2O
?
-
protein kinase Cdelta plays a major role in the regulation of cell apoptosis and survival. PKCdelta is cleaved by caspase 3 to generate a constitutively active catalytic domain that mediates both its apoptotic and anti-apoptotic effects. The phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
-
-
?
protein kinase Cdelta + H2O
?
-
the phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
-
-
?
protein kinase Czeta + H2O
?
-
major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L
-
-
?
protein kinase Czeta + H2O
?
-
major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L. Caspase-3 is involved in processing of protein kinase Czeta to carboxyl-terminal fragments that are catalytically active and that are degraded by the ubiquitin-proteasome pathway
-
-
?
protein phosphatase-1 inhibitor-3 + H2O
?
-
the substrate is an in vivo target of caspase-3 and participates in the apoptotic response to induction by actinomycin D, overview
-
-
?
protein phosphatase-1 inhibitor-3 + H2O
?
-
recombinant His6-tagged substrate protein expressed in Escherichia coli, substrate mutant D49A is not cleaved by caspase-3
-
-
?
RFC140 + H2O
?
-
cleavage at three sites: DEVD723G, DLVD922S and IETD1117A
-
-
?
RFC140 + H2O
?
-
cleavage of RFC140 during apoptosis inactivates its function in DNA replication and generates truncated forms that further inhibit DNA replication
-
-
?
Rpt5 + H2O
?
-
-
-
-
?
Rpt5 + H2O
?
-
in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes
-
-
?
tau protein + H2O
?
cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
-
-
?
tau protein + H2O
?
peptides are designed from 441-mer major human Tau protein sequence that encompasses the proposed caspase-3 cleavage site (Asp421-/-Ser422). While the control peptide is efficiently cleaved by caspase-3 at Asp421-/-Ser422 site producing the expected N- and C-terminal fragment peptides, the corresponding phospho-Ser422 peptide remains completely resistant to the cleavage. Substitution of Asp421 by its dextro isoform also blocks peptide cleavage by caspase-3. However substitution of Ser422 by its dextro isoform in the peptide does not affect the cleavage significantly
-
-
?
transcription factor Pax7 + H2O
?
-
-
-
?
transcription factor Pax7 + H2O
?
compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7. Continued expression of this protein inhibits the myoblast differentiation program. Caspase 3 cleavage inactivation of Pax7 is a crucial step for terminating the self-renewal process
-
-
?
additional information
?
-
-
apoptosis is a result of a complex network of signaling pathways initiating from both inside and outside the cell, culminating in the activation of caspases, cyteine aspartate proteases, that execute the final stages of cell death
-
-
?
additional information
?
-
-
characterization of 14 natural zebrafish caspase-3 substrates
-
-
?
additional information
?
-
-
no cleavage of lamin A
-
-
?
additional information
?
-
-
the preferred cleavage sequence is DEVD-/-
-
-
?
additional information
?
-
-
the preferred cleavage sequence is DEVD-/-
-
-
?
additional information
?
-
-
emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
-
-
?
additional information
?
-
-
interaction of Hsp27 with the caspase-3 prodomain inhibits the second proteolytic cleavage necessary for caspase-3 activation
-
-
?
additional information
?
-
-
no cleavage of Nogo-B
-
-
?
additional information
?
-
-
active caspase-3 is involved in apoptosis in epithelial cells of the intestine
-
-
?
additional information
?
-
-
azinomycin epoxide leads to activation and apoptosis in THP-1 cells in a p53-independent manner
-
-
?
additional information
?
-
-
caspase 3 acts as executioner proteases causing proteolysis of key proteins leading to DNA fragmentation and apoptosis
-
-
?
additional information
?
-
-
caspase family proteases are key proteins in apoptotic signaling pathways, which are activated in both the death receptor-mediated and the mitochondria-mediated apoptosis pathways
-
-
?
additional information
?
-
-
caspase-3 activation results in apoptosis, ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning and ischemic tolerance can diminish the activation of caspase-3, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 has a downstream effector function in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is activated by the death receptor pathway leading to apoptosis. Human herpesvirus HHV-6A-induced apoptosis is associated with activation of caspase-8, caspase-9, and caspase-3, suggesting the involvement of death receptor and mitochondrial signaling pathways, overview. HHV-6 differentially influences the functions of naive T cells and different subsets of memory CD4+ and CD8+ T cells, which in part may be due to differential susceptibility to HHV-6A-induced apoptosis, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis in myeloid leukemia cells, Bcl-2 family proteins are the central regulators of caspases activation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-3 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is ivolved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is playing a central role in the execution of apoptosis, its activation induces Dox resistance, mechanism, overview
-
-
?
additional information
?
-
-
caspase-3, an effector caspase, is involved in MDA-MB-231 apoptotic cell death, overview. Caspase-3 is activated when procaspase-3 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand
-
-
?
additional information
?
-
-
caspase-3, convergent with a variety of death signals, plays a key role in the induction of apoptosis
-
-
?
additional information
?
-
-
caspases 3, 8 and 9 are essential to rhein-induced apoptosis, inhibitors of caspases 3, 8 and 9 are efficiently blocked by rhein-induced apoptosis in TNF-alpha-treated human aortic smooth muscle cells, overview
-
-
?
additional information
?
-
caspases are key effectors in the processes of apoptosis and inflammation, executioner caspases selectively hydrolyze cellular proteins in the pathways leading to cell death
-
-
?
additional information
?
-
-
constitutive caspase-3 is one of the downstream effectors of TNF-alpha receptor-1 binding, that increases in parallel with the loss of CD28 in long-term T lymphocyte cultures, but this effect is blunted in the presence of the TNF-alpha inhibitors
-
-
?
additional information
?
-
-
external lactic acid induces apoptosis via the caspase-dependent pathway activating caspase-3, -8, and -9, and the caspase-independent pathway causing increased expressions of AIF and EndoG, overview
-
-
?
additional information
?
-
-
homocysteine-mediated EPC toxicity is due to apoptosis involving caspase-8, cytochrome c release, and caspase-3 activation. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, overview
-
-
?
additional information
?
-
-
human adenovirus type 5 early region 1A, E1A, significantly inhibits the cell proliferation of HeLa by the apoptosis induction through HER-2/Neu/caspase-3 pathway, overview
-
-
?
additional information
?
-
-
hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-3 or caspase-7
-
-
?
additional information
?
-
-
initial activation of caspase-3 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview
-
-
?
additional information
?
-
-
insulin inhibits caspase-3 activity in renal tubular epithelial cells via the PI3-kinase/Akt pathway
-
-
?
additional information
?
-
-
lipopeptide-induced apoptosis in MCF-7 cells is associated with caspase-3
-
-
?
additional information
?
-
-
mechanisms of plasma free fatty acid-triggered vascular smooth muscle cell-apoptosis essentially include activation of caspase-3, overview
-
-
?
additional information
?
-
-
mycotoxin citrinin has a strong impact on the expression levels of diverse proteins including the caspase-3, citrinin-directed caspase 3 activation involves MAPK signaling pathways, overview
-
-
?
additional information
?
-
-
netrin-1 siRNA-induced H-358 cell death is mediated by caspase-3 and -9 activities, but not by caspase-8 activity
-
-
?
additional information
?
-
-
the apoptotic effect of cisplatin is caspase-dependent. Caspase-3 inhibitors prevent HA14-1-induced apoptosis in follicular lymphoma B cells
-
-
?
additional information
?
-
-
the extrinsic death receptor pathway of apoptosis proceeding entirely via an intrinsic, Bcl-2-controlled, mitochondrial pathway, does not rely on caspase-9 and requires only limited activation of caspase-3 relative to other chemotherapeutic drugs, overview
-
-
?
additional information
?
-
-
TRAIL and TRAIL death receptors form a complex, which transmits an apoptotic signal via the Fas associated death domain leading to activation of caspase-8 or other initiator caspases, which in turn activate downstream caspases, such as caspase-3, 9, 6 and 7, that cause cell death, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase
-
-
?
additional information
?
-
caspase-3 recognizes various P4 residues in its numerous protein substrates, Asp is the most frequent P4 residue in peptide substrates. Although a wide variety of P4 residues in the cellular proteins are cleaved by caspase-3. Hydrophobic residues appear in the relative frequency of Val-Ala-Leu-Met-Phe-Ile/Cys in descending order. The P4 residues forms favorable hydrophobic interactions in two separate hydrophobic regions of the binding site. The side chains of P4 Ile and Tyr form hydrophobic interactions with caspase-3 residues Trp206 and Trp214 within a non-polar pocket of the S4 subsite, while P4 Trp interacts with Phe250 and Phe252 that can also form the S5 subsite, adaptability of caspase-3 for binding diverse P4 residues, substrate specificity, overview
-
-
?
additional information
?
-
-
caspases contain a reactive cysteine critical for enzymatic activity. Increased S-glutathionylation of Fas, caspase-3 activity, and cell death in cells lacking Grx1
-
-
?
additional information
?
-
-
the aspartic acid residue in position P1 is a nearly absolute requirement for the caspase activity, at least three additional amino acids at positions P2 to P4 are required to complete the specificity
-
-
?
additional information
?
-
-
caspase-3 cleaves the the DEVD sequence
-
-
?
additional information
?
-
-
apoptosis is triggered through intrinsic mitochondrial pathway by caspase 3-activation involving mitochondrial membrane potential damage and reactive oxygen species production
-
-
?
additional information
?
-
-
caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
-
-
?
additional information
?
-
-
caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
-
-
?
additional information
?
-
-
caspase-3 is activated during apoptosis, overexpression of bovine growth hormone has antiapoptotic effects in several cell lines, including human colonic adenocarcinoma cells, and in colonic mucosa reducing the activation of caspase-3, molecular mechanisms and regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is one of the key executioners of apoptosis and responsible for the partial or total proteolytic cleavage of many proteins. Senescence-accelerated prone mice 8 and senescence-accelerated resistant mice 1 show a drop in age-related proteolytic activity of caspase-3, but the caspase-independent cell death, owing to high p53 and apoptosis-inducing factor levels, might be an alternative pathway of cell death in the aged brain
-
-
?
additional information
?
-
-
caspases are a family of cysteine aspartic acid-specific proteases playing an important role in apoptotic processes in mammalian cells. Among them, caspase-3 is an essential protease that degrades other protein substrates inside the cells at an early stage of apoptosis
-
-
?
additional information
?
-
-
inotodiol, a lanostane triterpenoid, from Inonotus obliquus, inhibits P388 cell proliferation through caspase-3-dependent apoptosis
-
-
?
additional information
?
-
-
nonobese diabetic mouse acinar cells at 16 weeks show increased caspase 3 activity, as well as increased expression of TNF-alpha receptor1, increased Bax, tumour protein 53-induced nuclear protein1alpha, and chromatin condensation, apoptosis patterns, overview
-
-
?
additional information
?
-
-
caspase-3 causes chromatin condensation through DNA fragmentation
-
-
?
additional information
?
-
-
the caspase-3 cleavage site is present within the ATPase domain of Rpt subunits
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
-
-
?
additional information
?
-
-
caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
-
-
?
additional information
?
-
-
caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
-
-
?
additional information
?
-
-
activated caspase-3 in irradiation-induced microglia death. This age-dependent irradiation-induced loss of microglia likely affects both the response to irradiation and further brain development, overview
-
-
?
additional information
?
-
-
activation of caspase-3, an executioner caspase, plays a key role in the apoptotic cascade
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis in thymocytes, enzyme inhibition increases cell survival, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in glutamate-induced neuronal cell death, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in the ischemic brain injury during experimental stroke. In vitro nitric oxide regulates calpain and caspase-3 activation, and in vivo neuronal nitric oxide synthase, calpain and caspase-3 participate in the ischemic brain injury, inhibition of the neuronal nitric oxide synthase by 7-nitroindazole leads to downregulation of caspase-3, mechanism, overview
-
-
?
additional information
?
-
-
direct activation of procaspase-3 by caspase-9 and caspase-8 in type I cells, radiation-induced sensitization of hepatocytes to TNF-alpha-mediated apoptosis additionally requires changes upstream of caspase-8 activation, regulation of caspase-8 and apoptosis in hepatocytes, overview. Irradiation induces TNF-alpha-mediated activation of caspase-8, -9, and -3, and apoptosis in hepatocytes. Apoptosis induction is prevented by IkappaB antisense oligonucleotides mediated by suppression of caspases-9 and -3 activation but not of caspase-8 activation, overview
-
-
?
additional information
?
-
-
enzyme regulation in response to damaging agents like ethanol and acetylsalicylic acid in gastric mucosa, overview
-
-
?
additional information
?
-
-
increased cytosolic cytochrome c and subsequently caspase-3 activation are additional signs of neuronal death via the mitochondrial pathway. Bradykinin administration significantly attenuates ischemia-induced neuronal death, and also suppresses the release of MnSOD, and cytochrome c, and prevents caspase-3 activation
-
-
?
additional information
?
-
-
N-methyl-D-aspartate induces the activation of caspase-3 and the caspase-3-dependent apoptotic pathway, the activation is prevented by the autocamtide-2-related inhibitory peptide, overview. Blockade of calcium/calmodulin-dependent protein kinase II-alpha activity prevents N-methyl-D-aspartate-induced caspase-3 activation and provides significant neuroprotection against N-methyl-D-aspartate-induced ganglion cell loss in a retina toxicity model
-
-
?
additional information
?
-
-
T-cells show activated caspase-3 with the preservation of photoreceptors
-
-
?
additional information
?
-
-
procaspase-3 is activated by caspase-9 and caspase-8
-
-
?
pre-interleukin-1beta + H2O
additional information
-
-
a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
pre-interleukin-1beta + H2O
additional information
-
-
-
a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
pre-interleukin-1beta + H2O
additional information
-
-
a 28000 Da fragement and a 17000 Da fragement, less efficient hydrolysis than with caspase-1
?
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19 S proteasome + H2O
?
-
caspase-3 specifically cleaves the 19 S component of 26 S proteasome Rpt2, Rpt6, and Rpn2 in skeletal muscle stimulating proteasome activity
-
-
?
anamorsin + H2O
?
-
specifically cleaved by caspase-3 at DSVD209 L generating 25- and 10-kDa fragments
-
-
?
beta-catenin + H2O
?
-
processing of beta-catenin, production of a 70000 Da fragment
-
-
?
beta-N-acetylglucosaminidase + H2O
?
-
cleavage during apoptosis into two fragments during apoptosis, an N-terminal fragment containing the O-GlcNAcase active site and a C-terminal fragment containing a region with homology to GCN5 histone acetyltransferases, mutation D413A abrogates cleavage by caspase-3 both in vitro and in vivo. O-GlcNAcase activity is not affected by caspase-3 cleavage because the N- and C-terminal O-GlcNAcase fragments remain associated after the cleavage
-
-
?
caspase 9 + H2O
?
-
cleavage by caspase 3 does not result in activation of caspase 9, but enhances apoptosis by alleviating XIAP inhibition of the apical caspase
-
-
?
cytokeratine 18 + H2O
?
-
caspase-induced cytokeratine 18 cleavage in apoptotic cell populations
-
-
?
D4-GDI(Rho-GDI 2) + H2O
?
-
differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
-
-
?
eIF4G + H2O
?
-
caspase 3 is capable of cleaving eIF4G as part of the translationally active complex eIF4F, thereby inactivating this complex and subsequently causing inhibition of translation in apoptotic cells
-
-
?
epidermal growth factor receptor + H2O
?
-
cleavage during apoptosis
-
-
?
ICAD + H2O
?
-
activity of caspase-activated deoxyribonuclease, CAD, is affected by the caspase 3-mediated cleavage of the CAD inhibitor, ICAD
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
-
i.e. Mst1. Caspase 3 preferentially activates extracellular signal-regulated kinase preferentially through 36000 Da cleaved forms of Mst1. The 36000 Da form of Mst1 selectively phosphorylates extracellular signal-regulated kinase
-
-
?
Mcl-1 + H2O
?
-
antiapoptotic protein. Caspase-3 -mediated Mcl-1 downregulation appears to be responsible for the pro-apoptotic effects of EXEL-0862 on FIP1L1-PDGFRalpha-expressing cells
-
-
?
MDM2 oncoprotein + H2O
?
-
because MDM2 functions as a negative regulator of the p53 tumor suppressor and because p53 induces apoptosis in response to a variety of stimuli, this cleavage of MDM2 by CPP32-like proteases may result in deregulation of p53 and contribute directly to the process of apoptotic cell death
-
-
?
myeloid cell leukemia 1 + H2O
?
-
i.e. Mcl-1, apoptosis induced by tumor necrosis factor-related apoptosis-inducing ligand requires specific cleavage of Mcl-1 at D127 and D157 by enzyme. Removal of N-terminal domain of Mcl-1 by enzyme allows for the maximal mitochondrial perturbation that potentiates apoptosis
-
-
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
nuclear mitotic apparatus protein + H2O
?
-
-
-
-
?
p65/RelA + H2O
?
-
caspase-3-mediated carboxy-terminal fragment of p65/RelA production, cells producing this truncated p65/RelA do not undergo apoptosis but show a high viability, in spite of caspase-3 activation, overview. The substrate translocate to the nucleus, associates with NF-kappaB1/p50 and IkappaBalpha, but cannot bind -kappaB consensus sites
-
-
?
PAK2 + H2O
?
-
caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
pro-caspase-6 + H2O
?
-
caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
-
-
?
pro-interleukin-18 + H2O
IL18 + ?
-
virus infection by influenzy A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
pro-Mch2alpha + H2O
?
-
the enzyme processes pro-Mch2alpha at three aspartate processing sites, Asp23, Asp179, and Asp193, to produce the large p18 and small p11 subunits of the mature Mch2alpha enzyme. Mch2alpha is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
-
-
?
pro-Mch6 + H2O
?
-
the enzyme processes proMch6 preferentially at Asp330 to generate two subunits of molecular masses 37000 Da and 10000 Da. Mch6 is a downstream protease activated in CPP32- and granzyme B-mediated apoptosis
-
-
?
procaspase-3 + H2O
caspase-3 + ?
procaspase-6 + H2O
caspase-6 + ?
protein kinase Cdelta + H2O
?
-
protein kinase Cdelta plays a major role in the regulation of cell apoptosis and survival. PKCdelta is cleaved by caspase 3 to generate a constitutively active catalytic domain that mediates both its apoptotic and anti-apoptotic effects. The phosphorylation of Tyr332 is necessary for the caspase 3-dependent cleavage of protein kinase Cdelta
-
-
?
protein kinase Czeta + H2O
?
-
major cleavage site EETD-/-G, also cleaves at DGMD-/-G and DSED-/-L. Caspase-3 is involved in processing of protein kinase Czeta to carboxyl-terminal fragments that are catalytically active and that are degraded by the ubiquitin-proteasome pathway
-
-
?
protein phosphatase-1 inhibitor-3 + H2O
?
-
the substrate is an in vivo target of caspase-3 and participates in the apoptotic response to induction by actinomycin D, overview
-
-
?
RelB + H2O
?
-
the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
-
-
?
RFC140 + H2O
?
-
cleavage of RFC140 during apoptosis inactivates its function in DNA replication and generates truncated forms that further inhibit DNA replication
-
-
?
Rho-GDI 1 + H2O
?
-
differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
-
-
?
Rpt5 + H2O
?
-
in myoblasts, Rpt5 is sensitive to caspase-3-induced cleavage but in myotubes, it is not sensitive. Caspase-3 cleavage of Rpt5 is responsible for the difference in the patterns of proteasome subunit cleavage in myoblasts compared with myotubes
-
-
?
tau protein + H2O
?
cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
-
-
?
topoisomerase I + H2O
?
-
cleavage at DDVD146-/-Y and EEED170-/-G
-
-
?
transcription factor Pax7 + H2O
?
compensatory growth and regeneration of skeletal muscle is dependent on the resident stem cell population, satellite cells (SCs). Self-renewal and maintenance of the SC niche is coordinated by the paired-box transcription factor Pax7. Continued expression of this protein inhibits the myoblast differentiation program. Caspase 3 cleavage inactivation of Pax7 is a crucial step for terminating the self-renewal process
-
-
?
additional information
?
-
Bid peptide + H2O
?
-
-
-
-
?
Bid peptide + H2O
?
-
-
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
-
-
?
poly(ADP-ribose) polymerase + H2O
85000 Da fragment + ?
caspase-3 is the predominant poly(ADP-ribose) polymerase cleaving enzyme
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation requires caspase-3
-
-
?
procaspase-6 + H2O
caspase-6 + ?
-
activation requires caspase-3
-
-
?
additional information
?
-
-
apoptosis is a result of a complex network of signaling pathways initiating from both inside and outside the cell, culminating in the activation of caspases, cyteine aspartate proteases, that execute the final stages of cell death
-
-
?
additional information
?
-
-
characterization of 14 natural zebrafish caspase-3 substrates
-
-
?
additional information
?
-
-
emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
-
-
?
additional information
?
-
-
interaction of Hsp27 with the caspase-3 prodomain inhibits the second proteolytic cleavage necessary for caspase-3 activation
-
-
?
additional information
?
-
-
active caspase-3 is involved in apoptosis in epithelial cells of the intestine
-
-
?
additional information
?
-
-
azinomycin epoxide leads to activation and apoptosis in THP-1 cells in a p53-independent manner
-
-
?
additional information
?
-
-
caspase 3 acts as executioner proteases causing proteolysis of key proteins leading to DNA fragmentation and apoptosis
-
-
?
additional information
?
-
-
caspase family proteases are key proteins in apoptotic signaling pathways, which are activated in both the death receptor-mediated and the mitochondria-mediated apoptosis pathways
-
-
?
additional information
?
-
-
caspase-3 activation results in apoptosis, ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning and ischemic tolerance can diminish the activation of caspase-3, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 has a downstream effector function in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is activated by the death receptor pathway leading to apoptosis. Human herpesvirus HHV-6A-induced apoptosis is associated with activation of caspase-8, caspase-9, and caspase-3, suggesting the involvement of death receptor and mitochondrial signaling pathways, overview. HHV-6 differentially influences the functions of naive T cells and different subsets of memory CD4+ and CD8+ T cells, which in part may be due to differential susceptibility to HHV-6A-induced apoptosis, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis in myeloid leukemia cells, Bcl-2 family proteins are the central regulators of caspases activation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-3 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is ivolved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is playing a central role in the execution of apoptosis, its activation induces Dox resistance, mechanism, overview
-
-
?
additional information
?
-
-
caspase-3, an effector caspase, is involved in MDA-MB-231 apoptotic cell death, overview. Caspase-3 is activated when procaspase-3 is cleaved subsequently from the recruitment of Fas associated protein with death domain, FADD, to the death-effector domain site of procaspase-8 during the oligomerization of death receptor and its ligand
-
-
?
additional information
?
-
-
caspase-3, convergent with a variety of death signals, plays a key role in the induction of apoptosis
-
-
?
additional information
?
-
-
caspases 3, 8 and 9 are essential to rhein-induced apoptosis, inhibitors of caspases 3, 8 and 9 are efficiently blocked by rhein-induced apoptosis in TNF-alpha-treated human aortic smooth muscle cells, overview
-
-
?
additional information
?
-
caspases are key effectors in the processes of apoptosis and inflammation, executioner caspases selectively hydrolyze cellular proteins in the pathways leading to cell death
-
-
?
additional information
?
-
-
constitutive caspase-3 is one of the downstream effectors of TNF-alpha receptor-1 binding, that increases in parallel with the loss of CD28 in long-term T lymphocyte cultures, but this effect is blunted in the presence of the TNF-alpha inhibitors
-
-
?
additional information
?
-
-
external lactic acid induces apoptosis via the caspase-dependent pathway activating caspase-3, -8, and -9, and the caspase-independent pathway causing increased expressions of AIF and EndoG, overview
-
-
?
additional information
?
-
-
homocysteine-mediated EPC toxicity is due to apoptosis involving caspase-8, cytochrome c release, and caspase-3 activation. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, overview
-
-
?
additional information
?
-
-
human adenovirus type 5 early region 1A, E1A, significantly inhibits the cell proliferation of HeLa by the apoptosis induction through HER-2/Neu/caspase-3 pathway, overview
-
-
?
additional information
?
-
-
hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-3 or caspase-7
-
-
?
additional information
?
-
-
initial activation of caspase-3 causes degradation of glutaredoxin-1, resulting in S-glutathionylation of Fas at cysteine 294, which subsequently enhances binding of FasL, aggregation of Fas, accumulation of Fas in lipid rafts, DISC assembly, and further activation of caspases, causing a propagation of apoptotic cell death. activation of caspases is required for degradation of glutaredoxin-1 and S-glutathionylation of Fas, engagement of Fas causes a rapid activation of caspase-8. Overexpression of Grx1 prevents increases in S-glutathionylation of Fas and attenuates caspase activation and apoptosis in response to receptor ligation. Cleaved caspase-8 and -3 demonstrate an association between active caspases and Grx1 in cells after ligation of Fas, whereas in control cells, these associations are not observed, regulation, overview
-
-
?
additional information
?
-
-
insulin inhibits caspase-3 activity in renal tubular epithelial cells via the PI3-kinase/Akt pathway
-
-
?
additional information
?
-
-
lipopeptide-induced apoptosis in MCF-7 cells is associated with caspase-3
-
-
?
additional information
?
-
-
mechanisms of plasma free fatty acid-triggered vascular smooth muscle cell-apoptosis essentially include activation of caspase-3, overview
-
-
?
additional information
?
-
-
mycotoxin citrinin has a strong impact on the expression levels of diverse proteins including the caspase-3, citrinin-directed caspase 3 activation involves MAPK signaling pathways, overview
-
-
?
additional information
?
-
-
netrin-1 siRNA-induced H-358 cell death is mediated by caspase-3 and -9 activities, but not by caspase-8 activity
-
-
?
additional information
?
-
-
the apoptotic effect of cisplatin is caspase-dependent. Caspase-3 inhibitors prevent HA14-1-induced apoptosis in follicular lymphoma B cells
-
-
?
additional information
?
-
-
the extrinsic death receptor pathway of apoptosis proceeding entirely via an intrinsic, Bcl-2-controlled, mitochondrial pathway, does not rely on caspase-9 and requires only limited activation of caspase-3 relative to other chemotherapeutic drugs, overview
-
-
?
additional information
?
-
-
TRAIL and TRAIL death receptors form a complex, which transmits an apoptotic signal via the Fas associated death domain leading to activation of caspase-8 or other initiator caspases, which in turn activate downstream caspases, such as caspase-3, 9, 6 and 7, that cause cell death, overview
-
-
?
additional information
?
-
-
apoptosis is triggered through intrinsic mitochondrial pathway by caspase 3-activation involving mitochondrial membrane potential damage and reactive oxygen species production
-
-
?
additional information
?
-
-
caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
-
-
?
additional information
?
-
-
caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
-
-
?
additional information
?
-
-
caspase-3 is activated during apoptosis, overexpression of bovine growth hormone has antiapoptotic effects in several cell lines, including human colonic adenocarcinoma cells, and in colonic mucosa reducing the activation of caspase-3, molecular mechanisms and regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase. The intrinsic death pathway involves mitochondrial release of cytochrome c, which interacts with Apaf-1 and dATP to promote procaspase-9 autoactivation, which in turn activates downstream effectors such as caspase-3, -6, and -7. Increased caspase-3 activation is involved in apoptosis, inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 and -6 activation, as well as PARP and lamin A/C cleavage and apoptosis, overview. Leptospira interrogans-induced apoptosis in macrophages is mediated by caspase-3 and -6 activation through a FADDcaspase-8-dependent pathway, independently of mitochondrial cytochrome ccaspase-9-dependent signaling. Caspase-3 is required for the activation of caspase-6 and seems to be involved in caspase-9 activation through a feedback amplification loop. Regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis
-
-
?
additional information
?
-
-
caspase-3 is one of the key executioners of apoptosis and responsible for the partial or total proteolytic cleavage of many proteins. Senescence-accelerated prone mice 8 and senescence-accelerated resistant mice 1 show a drop in age-related proteolytic activity of caspase-3, but the caspase-independent cell death, owing to high p53 and apoptosis-inducing factor levels, might be an alternative pathway of cell death in the aged brain
-
-
?
additional information
?
-
-
caspases are a family of cysteine aspartic acid-specific proteases playing an important role in apoptotic processes in mammalian cells. Among them, caspase-3 is an essential protease that degrades other protein substrates inside the cells at an early stage of apoptosis
-
-
?
additional information
?
-
-
inotodiol, a lanostane triterpenoid, from Inonotus obliquus, inhibits P388 cell proliferation through caspase-3-dependent apoptosis
-
-
?
additional information
?
-
-
nonobese diabetic mouse acinar cells at 16 weeks show increased caspase 3 activity, as well as increased expression of TNF-alpha receptor1, increased Bax, tumour protein 53-induced nuclear protein1alpha, and chromatin condensation, apoptosis patterns, overview
-
-
?
additional information
?
-
-
caspase-3 is an effector caspase lying downstream from both intrinsic apoptotic pathway mediators and extrinsic apoptotic pathway mediators
-
-
?
additional information
?
-
-
caspase-3 activity is absent in case of coronary occlusion with and without subsequent revascularization in C57BL6 mice after transient ligation followed by 24 h of reperfusion, or 24 h persistent ligation, overview
-
-
?
additional information
?
-
-
caspase-3 activity is involved in cell death, e.g. induced by simulated ischemia and reperfusion with pH playing an important role, overview
-
-
?
additional information
?
-
-
activated caspase-3 in irradiation-induced microglia death. This age-dependent irradiation-induced loss of microglia likely affects both the response to irradiation and further brain development, overview
-
-
?
additional information
?
-
-
activation of caspase-3, an executioner caspase, plays a key role in the apoptotic cascade
-
-
?
additional information
?
-
-
caspase-3 is involved in apoptosis in thymocytes, enzyme inhibition increases cell survival, regulation, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in glutamate-induced neuronal cell death, overview
-
-
?
additional information
?
-
-
caspase-3 is involved in the ischemic brain injury during experimental stroke. In vitro nitric oxide regulates calpain and caspase-3 activation, and in vivo neuronal nitric oxide synthase, calpain and caspase-3 participate in the ischemic brain injury, inhibition of the neuronal nitric oxide synthase by 7-nitroindazole leads to downregulation of caspase-3, mechanism, overview
-
-
?
additional information
?
-
-
direct activation of procaspase-3 by caspase-9 and caspase-8 in type I cells, radiation-induced sensitization of hepatocytes to TNF-alpha-mediated apoptosis additionally requires changes upstream of caspase-8 activation, regulation of caspase-8 and apoptosis in hepatocytes, overview. Irradiation induces TNF-alpha-mediated activation of caspase-8, -9, and -3, and apoptosis in hepatocytes. Apoptosis induction is prevented by IkappaB antisense oligonucleotides mediated by suppression of caspases-9 and -3 activation but not of caspase-8 activation, overview
-
-
?
additional information
?
-
-
enzyme regulation in response to damaging agents like ethanol and acetylsalicylic acid in gastric mucosa, overview
-
-
?
additional information
?
-
-
increased cytosolic cytochrome c and subsequently caspase-3 activation are additional signs of neuronal death via the mitochondrial pathway. Bradykinin administration significantly attenuates ischemia-induced neuronal death, and also suppresses the release of MnSOD, and cytochrome c, and prevents caspase-3 activation
-
-
?
additional information
?
-
-
N-methyl-D-aspartate induces the activation of caspase-3 and the caspase-3-dependent apoptotic pathway, the activation is prevented by the autocamtide-2-related inhibitory peptide, overview. Blockade of calcium/calmodulin-dependent protein kinase II-alpha activity prevents N-methyl-D-aspartate-induced caspase-3 activation and provides significant neuroprotection against N-methyl-D-aspartate-induced ganglion cell loss in a retina toxicity model
-
-
?
additional information
?
-
-
T-cells show activated caspase-3 with the preservation of photoreceptors
-
-
?
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(3R)-3-ethyl-1-[methyl(octyl)amino]-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]octane-2,5-dione
-
50% inhibition at 9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[2-oxo-3-[(1,3-thiazol-5-ylmethyl)amino]pyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 12 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 7.9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[5-ethyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-[hexyl(methyl)amino]octane-2,5-dione
-
50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[hexyl(methyl)amino]octane-2,5-dione
-
i.e. M826, 50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[methyl(pentyl)amino]octane-2,5-dione
-
i.e. M867, 50% inhibition at 0.1 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3S)-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-(benzylsulfanyl)-4-oxopentanoic acid
-
50% inhibition at 52 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-4-oxopentanoic acid
-
50% inhibition at 0.3 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[[(2R)-2-[3-[(naphthalen-2-ylcarbonyl)amino]-2-oxopyridin-1(2H)-yl]-2-phenylacetyl]amino]-4-oxo-5-phenoxypentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(benzylsulfanyl)-3-([N-[(2,5-dimethoxyphenyl)acetyl]-L-valyl]amino)-4-oxopentanoic acid
-
50% inhibition at 48 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-(benzylsulfanyl)-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 86 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
-
-
(3S)-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 53 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(4S,7S,10S,13S)-7-(2-carboxyethyl)-4-(carboxymethyl)-13-(cyclobutylcarbonyl)-10-(1-methylethyl)-2,5,8,11-tetraoxo-3,6,9,12-tetraazapentadecan-15-oic acid
-
non-preferred name, comparison with inhibition of caspase-7
(R)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
IC50: 0.018 mM
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 0.0055 mM
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 44 nM
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
-
-
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 4.2 nM
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 170 nM
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 5.2 nM
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 4.6 nM
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 2.5 nM
(S)-1-butyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-ethyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-methyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 30 nM
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
-
-
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 3.1 nM
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
-
-
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
-
-
(S)-3-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyridin-2-ylmethyl]sulfamoyl]benzoic acid
-
-
(S)-3-[[6-(benzenesulfonylamino-methyl)pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-acetylsulfamoyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylamino-benzenesulfonylamino)methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylaminocarbonyl-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxobutyric acid
-
-
(S)-3-[[6-[(4-hydroxy-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(4-methanesulfonylamino-benzenesulfonylamino)methyl]pyridien-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-4-oxo-3-[[6-[[3-(1H-tetrazol-5-yl)benzenesulfonylamino]methyl]pyridine-3-carbonyl]amino]butyric acid
-
-
(S)-4-oxo-3-[[6-[[3-(5-oxo-4,5-dihydro[1,2,4]oxadiazol-3-yl)benzenesulfonylamino]methyl]pyridien-3-carbonyl]amino]butyric acid
-
-
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
-
-
(S)-4-[[4-(hydroxy-3-methyl-benzenesulfonylamino)methyl]thiophene]-2-carboxylic acid [3-(2-chloro-benzylsulfanyl)-1-ethyl-2-oxo-propyl]amide
-
-
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
IC50: 120 nM
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
-
-
(S)-5-[1-[(2-methoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 170 nM
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 70 nM
(S)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 31 nM
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 44 nM
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 140 nM
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
IC50: 410 nM
(S)-5-[[3-(1-carboxymethyl-2-oxo-ethylcarbamoyl)isooxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[3-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]isoxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[4-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-4-methyl-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxybenzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-3-methylsulfanyl-2-oxo-propylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-3-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-4-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]-4-methyl-thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-5-(2-chloro-phenyl)-2-oxopentylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
1,2-benzisothiazol-3-one
-
-
1,2-butanedithiol
-
60% inhibition
1,4-dihydroxy-2-naphthoic acid
-
-
1-(3-oxo-1,2-benzothiazol-2(3H)-yl)-4-(thiophen-2-yl)butane-1,4-dione
-
-
1-methyl-5-nitro-1H-indole-2,3-dione
-
-
1-methyl-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-methyl-5-[[(3R)-3-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
i.e. GSK-31, inhibitory effect is greatest in presence of 2-mercaptoethanol and decreases 2fold by substitution of 2-mercaptoethanol with dithiothreitol
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
2,4-dimethyl-8-(morpholin-4-ylsulfonyl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000044 mM
2-(1,3-dihydro-2-benzofuran-5-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-(2-hydroxyethyl)-4-methyl-8-[(4-methylpiperidin-1-yl)sulfonyl]-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
i.e. CD-001-0011, 50% inhibition at 130 nM, reversible, inhibitory effect is greatest in presence of dithiothreitol and decreases 3-4fold by substitution of dithiothreitol with 2-mercaptoethanol
2-(2-phenylethyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(1H-pyrrol-1-yl)phenyl]acetamide
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(piperidin-1-yl)phenyl]acetamide
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(pyridin-2-yl)phenyl]acetamide
-
-
2-(3-phenylpropanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-fluorobenzyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-methoxybenzyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-methylphenyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-phenylbutanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(5-phenylpentanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(biphenyl-4-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-(naphthalen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(phenylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(prop-2-en-1-yl)-1,2-benzothiazol-3(2H)-one
-
-
2-(thiophen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-benzyl-1,2-benzothiazol-3(2H)-one
-
-
2-chloro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)acetamide
-
50% inhibition at 92 nM
2-ethyl-1,2-benzothiazol-3(2H)-one
-
-
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 96 nM
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 103 nM
2-methyl-1,2-benzothiazol-3(2H)-one
-
-
2-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 62 nM
2-phenyl-1,2-benzothiazol-3(2H)-one
-
-
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(2-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(2-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3,4-dichlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(3-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-hydroxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(4-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
most potent inhibitor
2-[3-(4-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(trifluoromethyl)phenyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(4-methoxyphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(4-methylphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(thiophen-2-yl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
3,3-dimethyl-8-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
-
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
3-chloro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)propanamide
-
50% inhibition at 83 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
3-hydroxyl-anthranilamide
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
3-morpholinosydnonimine
-
i.e. SIN-1, 1 mM, complete inhibition
3-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 53 nM
3-oxo-N-(1-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-(3-phenylpropyl)-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-phenyl-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[2-(pyridin-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[2-(thiophen-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(1H-pyrrol-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(piperidin-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(piperidin-1-ylsulfonyl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(pyridin-2-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(pyrrolidin-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-oxo-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
-
-
3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
-
-
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
-
-
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
-
-
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
-
-
3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
-
-
4-(ethoxycarbonylmethoxy)-1-hydroxy-2-naphthoic acid
-
CS4566, a caspase-3-specific small molecular inhibitor, binding mode, overview
4-fluoro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 99 nM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-carbonitrile
-
50% inhibition at 0.000016 mM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000033 mM
4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonic acid
-
50% inhibition at 0.00009 mM
4-methyl-2-(1-methylethyl)-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-(morpholin-4-ylsulfonyl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.00021 mM
4-methyl-8-(morpholin-4-ylsulfonyl)-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000004 mM
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(1,3-thiazol-2-yl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(2,4,6-trihydroxyphenyl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(phenylamino)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-[(2,4,6-trihydroxyphenyl)amino]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
4-methyl-8-[[(2R)-2-phenoxypyrrolidin-1-yl]sulfonyl]-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000055 mM
4-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 54 nM
4-oxo-4-piperidin-1-yl-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)butanamide
-
50% inhibition at 25 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
4-oxo-4-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]butanoic acid
-
50% inhibition at 68 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
4-[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl]benzoic acid
-
-
4-[5-([(3S)-1-[(2,6-dichlorobenzoyl)oxy]-2,5-dioxohexan-3-yl]carbamoyl)-1,3-dioxo-8-(thiophen-2-yl)-5,8-dihydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-2(3H)-yl]butanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-(2,6-difluorophenoxy)-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-([(2R)-2-[(2,4-difluorophenoxy)methyl]pyrrolidin-1-yl]sulfonyl)-1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-([(2S)-2-[(pyridin-3-yloxy)methyl]pyrrolidin-1-yl]sulfonyl)-1H-indole-2,3-dione
-
-
5-fluoro-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-fluoro-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-fluoro-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
-
-
5-oxo-5-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]pentanoic acid
-
50% inhibition at 79 nM
5-[1-(azetidinyl)sulfonyl]isatin
IC50: 170 nM
5-[1-(hexamethyleneimino)sulfonyl]isatin
IC50: 0.0019 mM
5-[1-(piperidinyl)sulfonyl]isatin
IC50: 0.0022 mM
5-[1-(pyrrolidinyl)sulfonyl]isatin
IC50: 0.0028 mM
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-phenyl-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
5-[[5-[1-carboxymethyl-2-(7-methyl-benzoxazol-2-yl)-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
5-[[5-[1-carboxymethyl-2-[5-(2,6-dichloro-phenyl)-oxazol-2-yl]-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
6-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
8-hydroxyl-2,4-dioxoquinazoline
-
inhibits caspase-3, the compound is isolated from Streptomyces sp., a mangrove actinomycete, strain 061316
8-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,3-dimethyl-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
-
Ac-Asp-Glu-Val-Asp-H
-
the molecule can be truncated to Z-tLeu-Asp-H retaining nanomolar inhibitory activity in vitro and displaying action in whole cells, overview
Ac-DEVD-7-amido-4-methylcoumarin
-
a caspase-3 inhibitor
Ac-DNLD-CHO
-
from rational computational design, the inhibitor is specific due to the specific interaction of the NLD moiety with the active site of caspase-3, docking mode and site-directed mutagenesis analysis. In the active site of caspase-3, Asn in Ac-DNLDCHO specifically interacts with Ser209 in the S3 subsite, and Leu tightly interacts with the hydrophobic S2 subsite, overview
Ac-F-D-beta-hLeu-hLeu-D-KE
-
-
Ac-IEPD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-WEHD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-YVAD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
-
acetyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
Acetyl-Asp-Glu-Val-Asp-aldehyde
acetyl-Asp-Met-Gln-Asp-aldehyde
acetyl-DEVD-fluoromethylketone
-
-
acetyl-Val-Asp-Val-Ala-Asp-aldehyde
-
alpha-fetoprotein
interacts with caspase-3 through precise amino acids, namely loop-4 residues Glu-248, Asp-253 and His-257. alpha-Fetoprotein plays a critical role in the inhibition of the apoptotic signal transduction that mediated by caspase-3
-
Asp-Glu-Val-Asp-chloromethylketone
-
Asp-Glu-Val-Asp-fluoromethylketone
Asp-Phe-Leu-Asp-aldehyde
-
IC50 for membrane enzyme: 4.7 nM
baculovirus p35
-
IC50 for membrane enzyme: 0.074 nM
-
Bcl-2
-
an antiapoptotic protein that is localized to the intracellular membrane, nuclear membrane and endoplasmic reticulum, and blocks caspase activation by inhibiting the mitochondrial release of cytochrome c
-
Bcl2-Like12
-
is a nuclear and cytoplasmic oncoprotein that inhibits caspase-3 and apoptosis, mechanism, overview
-
benzyloxycarbonyl-Asp-Glu-Val-aza-aspartyl-(S,S) Glu-Pro-CO-N(CH2Ph)2
-
-
benzyloxycarbonyl-Asp-Glu-Val-aza-aspartyl-(S,S) Glu-Pro-CO-NHCH2Ph
-
-
benzyloxycarbonyl-Asp-Glu-Val-aza-aspartyl-(S,S) Glu-Pro-COO-CH2Ph
-
-
benzyloxycarbonyl-DEVD-fluoromethylketone
-
-
benzyloxycarbonyl-Glu-Val-aza-aspartyl-(S,S) Glu-Pro-CO-NH-CH2CH2Ph
-
-
benzyloxycarbonyl-Leu-Glu-Val-aza-aspartyl-(S,S) Glu-Pro-CO-Ala-NH-CH2Ph
-
-
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
-
benzyloxycarbonyl-Val-Ala-Asp(OMe)-fluoromethylketone
-
a specific caspase 3 inhibitor
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone
-
a general caspase inhibitor
benzyloxycarbonyl-WEHD-fluoromethylketone
-
-
BF4NO
-
0.1 mM, complete inhibition
Boc-D(OMe)-fluoromethyl ketone
a pan-caspase irreversible inhibitor
bradykinin
-
prevents caspase-3 activation in neurons
calbindin D28k
-
prevents osteoblast apoptosis by interaction and direct inhibition of caspase-3
-
carbobenzyloxy-DEVD-fluoromethyl ketone
-
a caspase-3 inhibitor
carbobenzyloxy-VAD-fluoromethyl ketone
-
a pan-caspase inhibitor
DEVD-CHO
-
a potent caspase-3 inhibitor
DEVD-fluoromethylketone
-
-
ethyl 2-amino-6-bromo-4-(1-cyano-2-ethoxy-2-oxoethyl)-4H-chromene-3-carboxylate
-
a BH3 mimetic compound, inhibits activation of procaspase-3
Fe3+
-
50% inhibition at 0.007 mM
FLICE-inhibitory proteins
-
some isoforms, including FLIPR inhibit Fas-mediated apoptosis by impeding caspase 3 activity as well as poly(ADP-ribose) polymerase cleavage
-
G-CSF
-
a caspase-3 inhibitor that also inhibits the steady increase in cytosolic free Ca2 during neutrophil aging, which is essential for apoptosis
-
glutathione disulfide
-
glutathionylation of caspase can occur at physiologically relevant concentrations of glutathione disulfide and results in the inhibition of caspase activation and activity
HBx
-
hepatitis virus Hbx protein, potent
-
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-Bpa-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-photoLeu-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-Asp-Glu-Val-Asp(triazolo)-Ala-Bpa-Gly-NH2
-
weak inhibition
hexynoyl-Bpa-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
hexynoyl-photoLeu-Asp-Glu-Val-Asp(psi)(CH2NH)-Ala-NH2
-
no ihibition without irradiation, complete inhibition when the sample is irradiated
human poly(ADP-ribose) polymerase autoantibodies
-
-
-
inhibitor of apoptosis protein
-
IAP, the family members block effector caspase-3 further downstream, which potentially inhibits apoptosis
-
isoquinoline-1,3,4(2H)-trione
-
50% inhibition at 149 nM
lipoic acid
-
80% inhibition
m-(Ac-L-Asp-L-Val-NH)-N-nitroso-N-phenylglycine
-
-
m-(acetyl-L-Asp-L-Val-NH)-N-nitroso-N-phenylglycine
-
-
methyl (8-bromo-4-methyl-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl)acetate
-
50% inhibition at 0.00046 mM
methyl 3-nitro-5-[[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]carbonyl]benzoate
-
50% inhibition at 104 nM
methyl 3-nitro-5-[[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)amino]carbonyl]benzoate
-
50% inhibition at 66 nM
methyl N-acetyl-3-(pyridin-3-yl)-D-alanyl-N-[[(3S)-1-[(2R)-1-[(3S)-1-methoxy-5-[[(5-methylthiophen-2-yl)carbonyl]oxy]-1,4-dioxopentan-3-yl]amino-1-oxo-3-phenylpropan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparaginate
-
low nanomolar potency against caspase-3 with more than 120fold selectivity over caspase-7
methyl N-[[4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinolin-8-yl]sulfonyl]-D-phenylalaninate
-
50% inhibition at 0.000023 mM
methyl [4-methyl-8-(morpholin-4-ylsulfonyl)-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl]acetate
-
50% inhibition at 0.000016 mM
methyl [4-methyl-8-(morpholin-4-ylsulfonyl)-1,3-dioxo-1,3-dihydro-2H-pyrrolo[3,4-c]quinolin-2-yl]propionate
-
50% inhibition at 0.000037 mM
myricetin
-
myricetin directly interacts with the active site of caspase-3 via three hydrogen bonds, via two hydroxyl groups on the B ring of myricetin interacting with Glu123 and the ether oxygen on the C ring interacting with Arg207, and myricetin directly inhibits caspase-3 activity, thereby inhibiting glutamate-induced cell death, but myricetin inhibits glutamate-induced neuronal toxicity by multiple biochemical pathways, e.g. inhibition of NMDA receptor 1 Ser-890 phosphorylation, overview. Molecular docking analysis by Monte Carlo and molecular dynamics simulations
N-(2-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(2-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(2-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(2-hydroxyethyl)-4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000020 mM
N-(2-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(2-methoxyethyl)-4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonamide
-
50% inhibition at 0.000021 mM
N-(2-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(2-methoxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 113 nM, comparison with inhibitory effect on caspase-2, caspase-6, caspase-7, caspase-8, papain, proteasome, trypsin and thrombin
N-(2-nitrophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-ethoxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 55 nM
N-(3-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(3-propyloxyphenyl)-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 71 nM
N-(4-benzoylphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-iodophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(4-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(5-methylpyridin-2-yl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-(furan-2-ylmethyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-acetyl-3-(pyridin-3-yl)-L-alanyl-N-[(3S)-1-[[(2S)-1-([(2S)-1-carboxy-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]amino)-5-methyl-1-oxohexan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparagine
-
low nanomolar potency against caspase-3 with more than 30fold selectivity over caspase-7
N-acetyl-Asp-Glu-Val-Asp-aldehyde
-
a caspase-3 inhibitor, i.e. DEVD-CHO, partially inhibits the DNA fragmentation and growth-inhibition induced by inotodiol
N-acetyl-Asp-Glu-Val-Asp-CHO
-
-
N-acetyl-L-alpha-aspartyl-L-alanyl-N-[(1S)-1-(carboxymethyl)-2-oxo-5-phenylpentyl]-L-valinamide
-
50% inhibition at 2 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-alanyl-N-[(1S)-3-(benzylsulfanyl)-1-(carboxymethyl)-2-oxopropyl]-L-valinamide
-
50% inhibition at 0.5 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-3-phenylpropyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-4-phenylbutyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxoheptyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxooctyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(2,5-dimethylphenyl)-2-oxobutyl]-L-valinamide
-
comparison with inhibition of caspase-7
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(3-methylphenyl)-2-oxobutyl]-L-valinamide
-
-
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-2-carboxy-1-formylethyl]-L-valinamide
-
50% inhibition at 27 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
N-acetyl-L-alpha-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
-
N-acetyl-L-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
-
N-allyl-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 44 nM
N-alpha-tosyl-L-lysinyl-chloromethylketone
-
TLCK, a serine protease inhibitor and potent but nonspecific inhibitor of mature caspases, TLCK has no or only slight effect on caspase-3 processing, but TLCK substantially inhibits caspase-3 enzymatic DEVDase activity, but does not prevent cells from death
N-benxylozycarbonyl-tLeu-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro. Z-tLeu-Asp-H impairs apoptosis in human DLD-1 colon adenocarcinoma cells without affecting caspase-8, in vivo effects, overview
N-benxylozycarbonyl-tLeu-Val-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro
N-benxylozycarbonyl-Val-tLeu-Asp
-
a peptide adehyde, competitively inhibits human caspase-3 activity in vitro
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-benzyloxycarbonyl-VAD-fluoromethyl ketone
-
a general caspase inhibitor
N-benzyloxycarbonyl-VAD-fluoromethylketone
-
a irreversible caspase inhibitor
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
-
N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
-
N-benzyloxycarbonyl-valyl-alanyl-aspartic-acid fluoromethyl ketone
-
-
N-butyl-(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
N-carbobenzyloxy-D(OMe)E(OMe)VD(OMe)-fluoromethyl ketone
-
a caspase-3 inhibitor
N-carbobenzyloxy-DEVD-fluoromethyl ketone
N-carbobenzyloxy-VAD(OMe)-fluoromethyl ketone
-
a Pan caspase inhibitor
N-carbobenzyloxy-VAD-fluoromethyl ketone
N-ethyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-propyl-(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
N-propyl-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)succinamide
-
50% inhibition at 59 nM
N-tosyl-L-phenylalaninyl-chloromethylketone
-
TPCK, a serine protease inhibitor and potent but nonspecific inhibitor of mature caspases, enhances caspase-3 processing although it substantially inhibits caspase-3 enzymatic DEVDase activity in HL-60 cells exposed to various cell death inducing stimuli, but does not prevent cells from death, overview
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[2-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[3-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(1,3-dioxolan-2-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-yl)benzyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-yl)phenyl]-2-(3-oxo-1,2-benzothiazol-2(3H)-yl)acetamide
-
-
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
peroxynitrite
-
0.01 mM, 50% inhibition
S-nitrosoglutathione
-
0.1 mM, complete inhibition
sodium 4-methyl-1,3-dioxo-2-(1,3,5-trimethyl-1H-pyrazol-4-yl)-2,3-dihydro-1H-pyrrolo[3,4-c]quinoline-8-sulfonate
-
50% inhibition at 0.00014 mM
spermine-NO
-
1 mM, complete inhibition
taurocholate
-
at low concentrations of 0.00001-0.1 mM it increases caspase-3 activity, but at larger doses of 0.5-10 mM it reverses stimulation to inhibition. It inhibits the caspase-3 pathway and prevents ethanol-induced caspase-3 activation leading to inhibition of apoptosis, overview
triptolide
-
a diterpenoid triepoxide derived from the herb Tripterygium wilfordii that is used as a natural medicine in China, activates caspase-3 4-119fold in KB cells, 4-70fold in SCC25 cells, and 7.5-90.5fold in OEC-M1 cells, all cancer cells, within 2 days, overview
Tyr-Val-Ala-Asp-chloromethylketone
-
-
Val-Ala-Asp-fluoromethylketone
-
-
Val-Glu-Ile-Asp-aldehyde
-
IC50 for membrane enzyme: 34 nM
VhhCasp31
-
reduces the enzyme activity by 39% at 0.0047 mM and by 85.5% at 0.0145 mM, which is a concentration three times that of caspase 3, the VHH proteins, expresed in SHSY-5Y cells and isolated from heavy chain antibody variable domain, i.e. VHH phage display library, are specific to caspase 3 and antagonist and agonist of apoptosis, effects of transiently-expressed VhhCasp31 and VhhCasp32 intrabodies on oxidative-stress-induced apoptosis in SHSY-5Y cells, overview
-
X inhibitor of apoptosis protein
-
recombinant, a member of the inhibitor of apoptosis protein family, inhibits caspase-3
-
XIAP
-
inhibitor of apoptosis
-
XIAP inhibitors
-
peptide inhibitors
-
Z-Asp-2,6-dichlorobenzoyloxymethylketone
-
a caspase-3-specific inhibitor
Z-DEVD-fluoromethylketone
-
a caspase 3 specific inhibitor
Z-IETD-fluoromethylketone
-
a caspase 8 specific inhibitor, delays the activation of caspase 3 and caspase 9 significantly
ZINC13341044
screening of caspase-3 inhibitors from natural molecule database using e-pharmacophore and docking studies
ZINC13507846
screening of caspase-3 inhibitors from natural molecule database using e-pharmacophore and docking studies
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
-
-
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
-
a chemical and reversible caspase-3 inhibitor, M867 reduces clonogenic survival in H460 lung cancer cells
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
-
a chemical and reversible caspase-3 inhibitor, M867 with ionizing radiation in an in vivo mouse hind limb lung cancer model is well tolerated, and produces a significant tumor growth delay compared to radiation alone
Ac-DEVD-CHO
-
Ac-DEVD-CHO
-
a caspase-3 inhibitor
Ac-DMQD-CHO
-
Acetyl-Asp-Glu-Val-Asp-aldehyde
-
Acetyl-Asp-Glu-Val-Asp-aldehyde
-
-
acetyl-Asp-Met-Gln-Asp-aldehyde
-
-
acetyl-Asp-Met-Gln-Asp-aldehyde
-
acetyl-DEVD-aldehyde
-
acetyl-DEVD-aldehyde
-
50% inhibition at 21 nM
Asp-Glu-Val-Asp-aldehyde
-
Asp-Glu-Val-Asp-aldehyde
-
IC50 for membrane enzyme: 1 nM
Asp-Glu-Val-Asp-fluoromethylketone
-
-
Asp-Glu-Val-Asp-fluoromethylketone
-
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
t1/2 at 0.001 mM is 43 s
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
-
DEVD-fluoromethyl ketone
-
-
DEVD-fluoromethyl ketone
-
a caspase-3-specific inhibitor
M826
-
IC50: 0.00003 mM; i.e. (R,S)-[[(2S)-2-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]butanoyl]amino]-5-[hexyl(methyl)amino]-4-oxopentanoic acid hydrochloride, selectively and potently inhibits both caspase-3 enzymatic activity and apoptosis in cultured cell in vitro
M826
-
IC50 for enzyme from cerebellar granule neuron: 0.00005 mM. IC50 for enzyme from cortical neuron: 0.00012 mM; i.e. (R,S)-[[(2S)-2-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]butanoyl]amino]-5-[hexyl(methyl)amino]-4-oxopentanoic acid hydrochloride, selectively and potently inhibits both caspase-3 enzymatic activity and apoptosis in cultured cell in vitro
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
effects on the activation of caspase-3 through cell infection with Leptospira interrogans
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
-
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
a caspase-3-specific inhibitor, that efficiently reduces rhein-induced apoptosis by 61% at 0.01 mM resulting in 28% apoptotic cells, overview
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
effects on the activation of caspase-3 through cell infection with Leptospira interrogans
N-carbobenzyloxy-DEVD-fluoromethyl ketone
-
a specific caspase-3 inhibitor
N-carbobenzyloxy-VAD-fluoromethyl ketone
-
a generic caspase inhibitor, that effectively blocks FasL-induced cleavage of caspase-3 and completely prevents FasL-induced degradation of Grx1
N-carbobenzyloxy-VAD-fluoromethyl ketone
-
a general caspase inhibitor
N-carbobenzyloxy-VAD-fluoromethyl ketone
-
-
N-carbobenzyloxy-VAD-fluoromethyl ketone
-
a general caspase inhibitor
NO
-
-
NO
-
NO supplied by exogenous NO donors serves in vivo as an antiapoptotic regulator of caspase activity via S-nitrosation of the Cys163 residue of caspase-3
survivin
-
-
-
survivin
-
inhibits processing of procaspase-3 and specifically binds the active form of caspase-3 through a baculovirus inhibitor of apoptosis, IAP, repeat domain
-
Z-VAD-fluoromethylketone
-
-
Z-VAD-fluoromethylketone
-
a pan-caspase inhibitor
additional information
-
screening of caspase-3 inhibitors using a dual-step fluorescence resonance energy transfer-based quenching assay for, method development with fluorescent europium(III)-chelate-doped nanoparticle donors coated with streptavidin in conjunction with a dual-labeled caspase-3-specific peptide substrate modified with a biotinyl moiety, overview
-
additional information
-
xanthorrhizol does not affect caspase-8
-
additional information
-
inhibitor synthesis, overview
-
additional information
-
N-propyl- and N-butyl isatins, as well as the corresponding terminal alcohols and regioisomeric fluorobutyl derivatives are excellent inhibitors, fluorinated N-benzyl isatins as well as trifluoroalkyl and difluoroalkyl derivatives are moderate inhibitors, while isatins bearing different alkylether groups at N-1 are very weak or not active as inhibitors of caspases-3, inhibitory potencies and structure-activity relationships, overview
-
additional information
-
insulin inhibits caspase-3 activity 30-60% in renal tubular epithelial cells via the PI3-kinase/Akt pathway, insulin deprivation for 24 or 48 h leads to a significant increase of the caspase-3 enzyme activity by 15% and 58%, respectively
-
additional information
-
inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 activation
-
additional information
-
caspase-3 is S-nitrosylated under basal conditions to prevent activation
-
additional information
-
processing of caspase-3 is affected only negligibly in cells treated with etoposide or N6-(2-isopentenyl)adenosine
-
additional information
-
caspase-3 inhibitory activity of 1,3-dioxo-4-methyl-2,3-dihydro-1h-pyrrolo[3,4-c] quinolines, quantitative structure-activity relationships, overview
-
additional information
-
ischemic/reperfusion in brain leads to increased release of cytochrome c from mitochondria and activation of caspase-3, ischemic preconditioning with 6,7,8,9-tetrahydro-5-nitro-1 H-benz[g]indole-2,3-dione-3-oxime, i.e. NS102, and ischemic tolerance can diminish the activation of caspase-3, overview
-
additional information
-
survivin, a member of the inhibitor of apoptosis protein family, does not inhibit caspase-3
-
additional information
-
structure-based drug design approach, synthesis of beta-strand urazole ring-containing irreversible peptidomimetic compounds. Z-VAD-fmk and the peptidomimetic inhibitors inhibit caspase-3 via a three-step kinetic mechanism, i.e. two rapid equilibrium steps followed by a relatively fast inactivation step, caspase-inhibitor interactions, overview
-
additional information
-
isatin 1,2,3-triazoles as potent inhibitors against caspase-3 via competitive inhibitory mechanism, synthesis by the Huisgen cycloaddition reaction, inhibitory potencies, overview
-
additional information
-
Z-LEHD-fluoromethylketone, a caspase 9 specific inhibitor, does not affect caspase 3 activation
-
additional information
-
1,2-benzisothiazol-3(2H)-one, lacks caspase-3 inhibitory activity
-
additional information
-
molecules with psi(CH2NH) or triazole uncleavable peptide bond do not show any inhibition of caspase activity without irradiation. When the samples are irradiated, the psi(CH2NH) peptides with benzophenone or diazirine photocrosslinkers show complete inhibition
-
additional information
-
interleukin-1 downregulates caspase-3 expression and reduces apoptsis within the gastrointestinal crypts
-
additional information
-
inhibition of caspase-8 impairs Leptospira interrogans-induced caspase-3 activation
-
additional information
-
Phyllanthus amarus inhibits cell growth and induces apoptosis in Dalton's lymphoma ascites cells through activation of caspase 3 and downregulation of bcl-2, overview
-
additional information
inhibition of caspase 3 activity leads to a profound disruption in skeletal muscle regeneration with an accumulation of satellite cells within the niche
-
additional information
-
thiorphan, a specific NEP/CD10 inhibitor, causes downregulation of procaspase-3 mRNA levels and suppression of caspase-3 activity in a neurokinin-1 receptor-dependent manner. The effect is abrogated by the NK1R antagonist (S)1-{2-[3(3-4-dichlorophenyl)-1-(3-iso-propoxyphenylacetyl)-piperidine-3-yl]ethyl}-4-pheny-1-azoniabicyclo[2.2.2]octane, chloride, i.e. SR140333, overview
-
additional information
-
IkappaB-antisense oligonucleotides inhibit caspase-9 but also caspase-3 activity
-
additional information
-
no inhibitory activity of compounds 3-hydroxyl-2-N-iso-butyryl-anthranilamide, anthranilamide, 8-hydroxyl-4(3H)-quinazoline, and 8-hydroxyl-2-methyl-4(3H)-quinazoline from Streptomyces sp., a mangrove actinomycete, strain 061316
-
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0.0142
(3S)-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00066
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00681
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00524
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00505
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0172
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00754
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0134
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0084
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0252
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00967
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00347
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00203
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.018
(R)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 0.018 mM
0.0055
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 0.0055 mM
0.000044
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.000017
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000066
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0005
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00184
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000133
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00009
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000025
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00512
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000078
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000041
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00003
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000042
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 4.2 nM
0.00017
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.0000052
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 5.2 nM
0.0000046
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 4.6 nM
0.0000025
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 2.5 nM
0.000029
(S)-1-butyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000183
(S)-1-ethyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000024
(S)-1-methyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00003
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 30 nM
0.0000053
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
Homo sapiens
-
37°C
0.0000031
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 3.1 nM
0.1
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
above, 37°C
0.0609
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00943
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
Homo sapiens
-
37°C
0.0068
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
37°C
0.1
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
above, 37°C
0.000043
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.1
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
Homo sapiens
-
above, 37°C
0.000187
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
Homo sapiens
-
37°C
0.00023
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
Homo sapiens
-
37°C
0.000191
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000082
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000056
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
Homo sapiens
-
37°C
0.00012
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 120 nM
0.000359
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
Homo sapiens
-
37°C
0.000083
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
Homo sapiens
-
37°C
0.000213
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
Homo sapiens
-
37°C
0.00017
(S)-5-[1-[(2-methoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.00007
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 70 nM
0.000031
(S)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 31 nM
0.000044
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.00014
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 140 nM
0.00041
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 410 nM
0.04674
1,2-benzisothiazol-3-one
Homo sapiens
-
at pH 7.5 and 22°C
0.000245
1-(3-oxo-1,2-benzothiazol-2(3H)-yl)-4-(thiophen-2-yl)butane-1,4-dione
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001
1-methyl-5-nitro-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0000167
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0002217
2-(1,3-dihydro-2-benzofuran-5-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000203
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.01855
2-(2-phenylethyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.000729
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(1H-pyrrol-1-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000501
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(pyridin-2-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001084
2-(3-phenylpropanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.01364
2-(4-fluorobenzyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.01209
2-(4-methoxybenzyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0004657
2-(4-methylphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0001816
2-(4-phenylbutanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003061
2-(5-phenylpentanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5,temperature not specified in the publication
0.0001406
2-(biphenyl-4-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000008
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002646
2-(naphthalen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002921
2-(phenylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.02272
2-(prop-2-en-1-yl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0322
2-(thiophen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000622
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0108
2-benzyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.09124
2-ethyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.04239
2-methyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0005328
2-phenyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.00000019
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001926
2-[(2-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001857
2-[(2-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000425
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002186
2-[(2-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001999
2-[(2-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0006543
2-[(3,4-dichlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000263
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002719
2-[(3-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.008985
2-[(3-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000548
2-[(3-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003392
2-[(3-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002151
2-[(4-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001196
2-[(4-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003263
2-[(4-hydroxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000033
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001344
2-[(4-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002143
2-[(4-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000473
2-[3-(2-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001297
2-[3-(2-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001357
2-[3-(2-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000877
2-[3-(3-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000349
2-[3-(3-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000095
2-[3-(3-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000569
2-[3-(4-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001116
2-[3-(4-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000497
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000119
2-[3-(4-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003897
2-[4-(4-methoxyphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002659
2-[4-(4-methylphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001266
2-[4-(thiophen-2-yl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.032
3-hydroxyl-anthranilamide
Rattus norvegicus
-
pH 7.5, 35°C
0.000085
3-oxo-N-(1-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
0.00004904
3-oxo-N-(3-phenylpropyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000076
3-oxo-N-phenyl-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00004939
3-oxo-N-[2-(pyridin-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00003105
3-oxo-N-[2-(thiophen-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00009792
3-oxo-N-[4-(piperidin-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000221
3-oxo-N-[4-(pyridin-2-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00082
3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000988
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0012
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00058
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00011
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0208
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00035
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00084
3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00111
3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000000228
4-methyl-2-(1-methylethyl)-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000324
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(1,3-thiazol-2-yl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000446
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(2,4,6-trihydroxyphenyl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000124
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(phenylamino)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000243
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-[(2,4,6-trihydroxyphenyl)amino]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.00000161
4-[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl]benzoic acid
Homo sapiens
-
-
0.00913
4-[5-([(3S)-1-[(2,6-dichlorobenzoyl)oxy]-2,5-dioxohexan-3-yl]carbamoyl)-1,3-dioxo-8-(thiophen-2-yl)-5,8-dihydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-2(3H)-yl]butanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0025
5-(2,6-difluorophenoxy)-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0257
5-(2,6-difluorophenoxy)-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0471
5-(2,6-difluorophenoxy)-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0000005
5-([(2R)-2-[(2,4-difluorophenoxy)methyl]pyrrolidin-1-yl]sulfonyl)-1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00123
5-fluoro-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00112
5-fluoro-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00129
5-fluoro-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00017
5-[1-(azetidinyl)sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.0019
5-[1-(hexamethyleneimino)sulfonyl]isatin
Homo sapiens
IC50: 0.0019 mM
0.0022
5-[1-(piperidinyl)sulfonyl]isatin
Homo sapiens
IC50: 0.0022 mM
0.0028
5-[1-(pyrrolidinyl)sulfonyl]isatin
Homo sapiens
IC50: 0.0028 mM
0.000018
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000267
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000103
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000243
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000207
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00007
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000213
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
5-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
6-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
37°C
0.036
8-hydroxyl-2,4-dioxoquinazoline
Rattus norvegicus
-
pH 7.5, 35°C
0.0000068
Ac-CV3-KE
Homo sapiens
-
at pH 7.4 and 22°C
0.0000012
Ac-DEVD-CHO
Homo sapiens
-
0.000012
Ac-DMQD-CHO
Homo sapiens
-
0.01
Ac-DW3-KE
Homo sapiens
-
at pH 7.4 and 22°C
-
0.000012
Ac-F-D-beta-hLeu-hLeu-D-KE
Homo sapiens
-
at pH 7.4 and 22°C
0.0012
Ac-IEPD-CHO
Homo sapiens
-
0.0019
Ac-WEHD-CHO
Homo sapiens
-
0.01
Ac-YVAD-CHO
Homo sapiens
-
0.000001
Asp-Glu-Val-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 1 nM
0.0000047
Asp-Phe-Leu-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 4.7 nM
0.000074
baculovirus p35
Homo sapiens
-
IC50 for membrane enzyme: 0.074 nM
-
0.000012
carbobenzyloxy-DEVD-fluoromethyl ketone
Homo sapiens
-
-
0.0136
CS4566
Homo sapiens
-
-
0.000027
FAM-Ahx2-CV3-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000018
FAM-DEVD-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000035
IDN6556
Homo sapiens
-
at pH 7.4 and 30°C
0.0102
myricetin
Rattus norvegicus
-
pH 7.4, 37°C
0.008093
N-(2-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000206
N-(2-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.01627
N-(2-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000088
N-(2-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.004167
N-(2-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.009823
N-(2-nitrophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.009628
N-(3-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000241
N-(3-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000438
N-(3-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000074
N-(3-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.001167
N-(3-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.0004307
N-(4-benzoylphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.003071
N-(4-bromophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000115
N-(4-fluorobenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000593
N-(4-fluorophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.1
N-(4-iodophenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
IC50 above 0.1 mM, at pH 7.5 and 22°C
0.00004
N-(4-methoxybenzyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.01071
N-(4-methoxyphenyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.04674
N-(5-methylpyridin-2-yl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00008055
N-(furan-2-ylmethyl)-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000023
N-acetyl-3-(pyridin-3-yl)-L-alanyl-N-[(3S)-1-[[(2S)-1-([(2S)-1-carboxy-4-[(2,6-dimethylbenzoyl)oxy]-3-oxobutan-2-yl]amino)-5-methyl-1-oxohexan-2-yl]amino]-5-methyl-1-oxohexan-3-yl]-L-alpha-asparagine
Homo sapiens
-
at pH 7.4 and 22°C
0.0000002 - 0.0757
N-acetyl-DEVD-CHO
0.00004153 - 0.000086
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
0.04
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
Homo sapiens
pH 7.4, 37°C
0.04474
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.06096
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.05149
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.02508
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.6
0.02926
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.01356
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002697
N-[2-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001808
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000555
N-[3-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00006201
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00005685
N-[4-(morpholin-4-yl)benzyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000115 - 0.0001063
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
0.0007834
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.02205
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.0000606
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00001
Rho-DEVD-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000034
Val-Glu-Ile-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 34 nM
0.000000008
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
Homo sapiens
-
-
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00003
M826
Homo sapiens
-
IC50: 0.00003 mM
0.00012
M826
Mus musculus
-
IC50 for enzyme from cerebellar granule neuron: 0.00005 mM. IC50 for enzyme from cortical neuron: 0.00012 mM
0.0000002
N-acetyl-DEVD-CHO
Homo sapiens
-
at pH 7.5 and 22°C
0.0757
N-acetyl-DEVD-CHO
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00004153
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000086
N-benzyl-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00000115
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001063
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
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