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Information on EC 3.4.22.56 - caspase-3 and Organism(s) Homo sapiens and UniProt Accession P42574

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.56 caspase-3
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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P42574 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
Synonyms
caspase-3, caspase 3, casp3, sca-1, cpp32, casp-3, cas-3, cpp-32, apopain, cgcaspase-3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
apopain
-
-
-
-
C14.003
-
-
-
-
Cas-3
-
-
CASP-3
CASP3
-
-
caspase 3
CPP-32
-
-
-
-
CPP32
-
-
-
-
CPP32/apopain
-
-
-
-
cysteine aspartic acid-specific protease
-
-
cysteine protease CPP32
-
-
-
-
DEVDase
-
-
IRP
-
-
-
-
SCA-1
-
-
-
-
SREBP cleavage activity 1
-
-
-
-
Yama protein
-
-
-
-
Yama/CPP32
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-/- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position
show the reaction diagram
hydrophobic S5 site, where the side-chains of F250 and F252 interact with substrate. Kinetic importance of P5 site
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
169592-56-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
acetyl-L-Asp-L-Glu-L-Val-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Glu-L-Val-L-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
acetyl-L-Asp-L-Met-L-Gln-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Met-L-Gln-L-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
?
acetyl-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide + H2O
acetyl-L-Asp-L-Val-L-Ala-L-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
DEVD-4-nitroanilide + H2O
DEVD + 4-nitroaniline
show the reaction diagram
DEVD-amido-4-trifluoromethylcoumarin + H2O
DEVD + amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
?
huntingtin + H2O
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
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
?
show the reaction diagram
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
show the reaction diagram
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
show the reaction diagram
-
-
-
?
SETbeta + H2O
?
show the reaction diagram
-
-
-
?
tau protein + H2O
?
show the reaction diagram
5'-tetramethylrhodamine-5(6)-carboxamide-DEVD-cyanine 5 + H2O
?
show the reaction diagram
-
-
-
-
?
70kDa U1 small ribonucleoprotein + H2O
?
show the reaction diagram
-
cleavage site is DGPD-/-
-
-
?
Ac-DEVD-4-methylcoumarin 7-amide + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
an artificial caspase-3 substrate
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-CDEVDK + H2O
acetyl-CDEVD + Lys
show the reaction diagram
-
-
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-DEVD-4-trifluoromethylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VDQMDGW-amide + H2O
?
show the reaction diagram
acetyl-VDQQD-4-nitroanilide + H2O
acetyl-VDQQD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VDVAD-4-nitroanilide + H2O
acetyl-VAVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
anamorsin + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-DEVD-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
beta-N-acetylglucosaminidase + H2O
?
show the reaction diagram
Bid peptide + H2O
?
show the reaction diagram
-
-
-
-
?
biotinylated acetyl-CDEVDK + H2O
biotinylated acetyl-CDEVD + Lys
show the reaction diagram
-
-
-
-
?
caspase 9 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
D4 G-protein dissociation inhibitor + H2O
?
show the reaction diagram
-
cleavage site is DELD-/-
-
-
?
D4-GDI(Rho-GDI 2) + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
DEVD-7-amido-4-fluoromethylcoumarin + H2O
DEVD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
DEVD-7-amido-4-methylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
DEVD-7-amido-4-trifluoromethylcoumarin + H2O
DEVD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
highly selective substrate for caspase-3
-
-
?
DEVD-NucView488 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
eIF4G + H2O
?
show the reaction diagram
epidermal growth factor receptor + H2O
?
show the reaction diagram
glutaredoxin-1 + H2O
?
show the reaction diagram
-
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
-
?
huntingtin + H2O
?
show the reaction diagram
-
cleavage site is DEED-/-
-
-
?
ICAD + H2O
?
show the reaction diagram
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
IETD-7-amido-4-fluoromethylcoumarin + H2O
IETD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Ile-Glu-Thr-Asp-4-nitroanilide + H2O
Ile-Glu-Thr-Asp + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
show the reaction diagram
Mcl-1 + H2O
?
show the reaction diagram
MDM2 oncoprotein + H2O
?
show the reaction diagram
myeloid cell leukemia 1 + H2O
?
show the reaction diagram
-
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-Asp-Glu-Val-Asp 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-acetyl-DEVD-4-trifluoromethylcoumarin 7-amide + H2O
N-acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
N-acetyl-DEVD-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Asp-L-Glu-L-Val-L-Asp-N'-morpholinecarbonyl-rhodamine 110 + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
nuclear mitotic apparatus protein + H2O
?
show the reaction diagram
p65/RelA + H2O
?
show the reaction diagram
PAK2 + H2O
?
show the reaction diagram
-
caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
-
-
?
poly(ADP-ribose) polymerase + H2O
?
show the reaction diagram
pre-interleukin-18 + H2O
interleukin-18 + ?
show the reaction diagram
-
-
-
-
?
pro-caspase-6 + H2O
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
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
?
show the reaction diagram
pro-Mch6 + H2O
?
show the reaction diagram
procaspase-3 + H2O
caspase-3 + ?
show the reaction diagram
-
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
show the reaction diagram
protein kinase Cdelta + H2O
?
show the reaction diagram
protein kinase Czeta + H2O
?
show the reaction diagram
protein phosphatase-1 inhibitor-3 + H2O
?
show the reaction diagram
RelB + H2O
?
show the reaction diagram
-
the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
-
-
?
RFC140 + H2O
?
show the reaction diagram
Rho-GDI 1 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage site is DEPD-/-
-
-
?
topoisomerase I + H2O
?
show the reaction diagram
-
cleavage at DDVD146-/-Y and EEED170-/-G
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
procaspase-6 + H2O
caspase-6 + ?
show the reaction diagram
-
-
-
?
SETbeta + H2O
?
show the reaction diagram
-
-
-
?
tau protein + H2O
?
show the reaction diagram
cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
-
-
?
anamorsin + H2O
?
show the reaction diagram
-
specifically cleaved by caspase-3 at DSVD209 L generating 25- and 10-kDa fragments
-
-
?
beta-N-acetylglucosaminidase + H2O
?
show the reaction diagram
-
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
-
-
?
Bid peptide + H2O
?
show the reaction diagram
-
-
-
-
?
caspase 9 + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
caspase-induced cytokeratine 18 cleavage in apoptotic cell populations
-
-
?
D4-GDI(Rho-GDI 2) + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
cleavage during apoptosis
-
-
?
ICAD + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
nuclear mitotic apparatus protein + H2O
?
show the reaction diagram
-
-
-
-
?
p65/RelA + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
caspase-3 is mainly responsible for the apoptotic cleavage of PAK2 in Fas-stimulated Jurkat cells
-
-
?
pro-caspase-6 + H2O
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
procaspase-6 + H2O
caspase-6 + ?
show the reaction diagram
-
activation requires caspase-3
-
-
?
protein kinase Cdelta + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
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
?
show the reaction diagram
-
the substrate is an in vivo target of caspase-3 and participates in the apoptotic response to induction by actinomycin D, overview
-
-
?
RelB + H2O
?
show the reaction diagram
-
the Asp205 site in RelB is specifically cleaved by caspase-3 in vinblastine-treated HAT-1080 cells
-
-
?
RFC140 + H2O
?
show the reaction diagram
-
cleavage of RFC140 during apoptosis inactivates its function in DNA replication and generates truncated forms that further inhibit DNA replication
-
-
?
Rho-GDI 1 + H2O
?
show the reaction diagram
-
differential regulation of the homologous GDP dissociation inhibitors Rho-GDI 1 and D4-GDI during drug-induced apoptosis by proteolysis mediated by caspase-3
-
-
?
topoisomerase I + H2O
?
show the reaction diagram
-
cleavage at DDVD146-/-Y and EEED170-/-G
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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-(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-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 30 nM
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 3.1 nM
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
IC50: 120 nM
(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
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
Ac-DEVD-CHO
-
Ac-DMQD-CHO
-
Ac-DQMD-CHO
-
Ac-DQVD-aldehyde
-
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-Asp-Glu-Val-Asp-aldehyde
-
acetyl-Asp-Met-Gln-Asp-aldehyde
-
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-aldehyde
-
Asp-Glu-Val-Asp-chloromethylketone
-
Boc-D(OMe)-fluoromethyl ketone
a pan-caspase irreversible inhibitor
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
-
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
-
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
(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
(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-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-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
-
-
(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-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-[[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
-
a chemical and reversible caspase-3 inhibitor, M867 reduces clonogenic survival in H460 lung cancer cells
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-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-[[(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-[[(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-CV3-KE
-
-
Ac-DEVD-7-amido-4-methylcoumarin
-
a caspase-3 inhibitor
Ac-DEVD-CHO
-
a caspase-3 inhibitor
Ac-DMQD-CHO
-
-
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-DW3-KE
-
-
-
Ac-F-D-beta-hLeu-hLeu-D-KE
-
-
acetyl-AEVD-aldehyde
-
-
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
-
Acetyl-Asp-Glu-Val-Asp-aldehyde
-
-
acetyl-Asp-Met-Gln-Asp-aldehyde
-
-
acetyl-DEVD-aldehyde
acetyl-DEVD-CHO
-
-
acetyl-IETD-aldehyde
-
-
acetyl-WEHD-aldehyde
-
-
acetyl-YVAD-aldehyde
-
-
Asp-Glu-Val-Asp-aldehyde
-
IC50 for membrane enzyme: 1 nM
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-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
calbindin D28k
-
prevents osteoblast apoptosis by interaction and direct inhibition of caspase-3
-
carbobenzyloxy-DEVD-fluoromethyl ketone
-
a caspase-3 inhibitor
carbobenzyloxy-VAD
-
-
carbobenzyloxy-VAD-fluoromethyl ketone
-
a pan-caspase inhibitor
Cd2+
-
-
cIAP
-
-
-
cIAP2
-
-
-
cowpox serpin CrmA
-
-
-
DEVD-fluoromethyl ketone
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
FAM-Ahx2-CV3-AOMK
-
-
FAM-DEVD-AOMK
-
-
FAM-DEVD-FMK
-
-
Fe3+
-
50% inhibition at 0.007 mM
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
Hg2+
-
-
human poly(ADP-ribose) polymerase autoantibodies
-
-
-
IDN6556
-
-
inhibitor of apoptosis protein
-
IAP, the family members block effector caspase-3 further downstream, which potentially inhibits apoptosis
-
iodoacetamide
-
-
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
MX-1013
-
-
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-CHO
-
-
N-acetyl-DEVD-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-fluoromethylketone
-
-
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-(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
pralnacasan
-
-
Rho-DEVD-AOMK
-
-
RU36384/VRT-18858
-
-
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
survivin
-
-
-
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-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
-
VX-765
-
-
X inhibitor of apoptosis protein
-
recombinant, a member of the inhibitor of apoptosis protein family, inhibits caspase-3
-
XIAP
-
inhibitor of apoptosis
-
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
Z-VAD-fluoromethylketone
-
-
Zn2+
-
-
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Mch4
activation of CPP32
-
1,2-benzenedithiol
-
4-5fold activation
1,3-benzenedithiol
-
6fold activation
2-mercaptoethanol
-
half-maximal activation at 1.4 mM
2-methoxyestradiol
-
increases the enzyme activity 2fold at 100 nM
3-[(dodecylthiocarbonyl)methyl]glutarimide
-
-
4,4-thiobisbenzenethiol
-
4-5fold activation
actinomycin D
-
significantly activates caspase-3
arachidonic acid
-
-
azinomycin epoxide
-
i.e. (2S,3S)-benzyl 3,4-epoxy-2-(3-methoxy-5-methyl-1-naphthoyloxy)-3-methylbutanamide, leads to activation and apoptosis in THP-1 cells in a p53-independent manner, while human apoptosis signal-regulating kinase 1, ASK1, is highly required for caspase-3 activation by (2S,3S)-benzyl 3,4-epoxy-2-(3-methoxy-5-methyl-1-naphthoyloxy)-3-methylbutanamide, transient expression of the dominant-negative human ASK1 with kinase-dead domain in THP-1 cells abolishes the caspase-3 activating effect of azinomycin epoxide, overview
C2-ketoCer
-
i.e. (2S,4E)-2-acetylamino-3-oxo-4-octadecen-1-ol, a ceramide analogue, activates caspase-3 and induces apoptosis
cisplatin
-
with or without pre-treatment with HA14-1 it increases the cleavage of caspase-3
cytochrome c
dithiothreitol
-
half-maximal activation at 1.1 mM
doxorubicin
-
augments caspase-3 activity
doxorubicin/2-methoxyestradiol
-
both in combination activate the enzyme 27fold
FADD
-
adapter molecule, required for caspase-3 activation
-
gamma-linolenic-acid
-
-
homocysteine
-
induces the enzyme activation 2.5fold and 4fold in endothelial progenitor cells at 0.1 mM and 0.2 mM, respectively. Vitamin B6, and B9 significantly impair homocysteine-mediated EPC caspase-3 activation in vitro, and inhibitor N-carbobenzyloxy-VAD-fluoromethyl ketone highly reduces the activating effect, overview
Lactic acid
-
induces the activation of caspase-3 in keratinocytes, the activation can be inhibited by N-carbobenzyloxy-VAD-fluoromethyl ketone, overview
linoleic acid
-
-
oleic acid
-
-
paclitaxel
-
pre-treatment of cells with HA14-1 followed by paclitaxel induces cleavage of pro-caspase-3 to active form
palmitic acid
-
-
stearic acid
-
-
trichothecin
-
trichothecin increases caspase-9, EC 3.4.22.62, expression and caspase-3 activity, and induces apoptosis of HepG2 cells via caspase-9 mediated activation of the mitochondrial death pathway
VhhCasp32
-
increases the enzyme activity by 38% at 0.0047 mM, 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
-
xanthorrhizol
-
a natural sesquiterpenoid compound isolated from the rhizome of Curcuma xanthorrhizza, modulates MDA-MB-231 cell apoptosis through the mitochondria-mediated pathway subsequent to the disruption of mitochondrial transmembrane potential, release of cytochrome c, activation of caspase-3 and caspase-9, and the modulation of PARP-1 protein, overview
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067
acetyl-L-Asp-L-Glu-L-Val-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.0048 - 0.0335
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
1.6
acetyl-L-Asp-L-Met-L-Gln-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.222
acetyl-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.147
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.164
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.002 - 0.0255
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
0.0625
DEVD-4-nitroanilide
-
0.0004
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
pH and temperature not specified in the publication
0.0015
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
pH and temperature not specified in the publication
0.0008
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
pH and temperature not specified in the publication
0.0004
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
pH and temperature not specified in the publication
0.0006
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
pH and temperature not specified in the publication
0.0006
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
pH and temperature not specified in the publication
0.0003
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
pH and temperature not specified in the publication
0.0002
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
pH and temperature not specified in the publication
0.0008
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
pH and temperature not specified in the publication
0.0002
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
pH and temperature not specified in the publication
0.0018
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
pH and temperature not specified in the publication
0.0016
5'-tetramethylrhodamine-5(6)-carboxamide-DEVD-cyanine 5
-
pH and temperature not specified in the publication
0.0337
Ac-DEVD-4-methylcoumarin 7-amide
-
pH 7.5, 25°C
0.011
acetyl-DEVD-4-nitroanilide
-
pH 7.5, 30°C
0.005 - 10.7
acetyl-DEVD-7-amido-4-methylcoumarin
0.044
acetyl-DQMD-4-nitroanilide
-
pH 7.5, 30°C
0.2
acetyl-VDQMDGW-amide
-
pH 7.5, 30°C
0.067
acetyl-VDVAD-4-nitroanilide
-
pH 7.5, 30°C
0.25
acetyl-VEID-4-nitroanilide
-
pH 7.5, 30°C
0.51
acetyl-VQVD-4-nitroanilide
-
pH 7.5, 30°C
0.37
acetyl-YEVD-4-nitroanilide
-
pH 7.5, 30°C
29
acetyl-YVAD-4-nitroanilide
-
pH 7.5, 30°C
0.00073
DEVD-FQ
-
pH and temperature not specified in the publication
0.0023
DEVD-NucView488
-
-
0.00077
DW3-FQ
-
pH and temperature not specified in the publication
additional information
additional information
-
stopped-flow and steady-state kinetic kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88
acetyl-L-Asp-L-Glu-L-Val-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.08 - 19.56
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
3.5
acetyl-L-Asp-L-Met-L-Gln-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.9
acetyl-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.84
acetyl-L-Leu-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.8
acetyl-L-Val-L-Asp-L-Val-L-Ala-L-Asp-4-nitroanilide
pH 7.5, 22°C
0.03 - 19.04
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
0.0217
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
pH and temperature not specified in the publication
0.0183
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
pH and temperature not specified in the publication
0.017
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
pH and temperature not specified in the publication
0.013
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
pH and temperature not specified in the publication
0.015
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
pH and temperature not specified in the publication
0.00917
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
pH and temperature not specified in the publication
0.0083
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
pH and temperature not specified in the publication
0.023
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
pH and temperature not specified in the publication
0.015
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
pH and temperature not specified in the publication
0.028
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
pH and temperature not specified in the publication
0.023
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
pH and temperature not specified in the publication
9.1 - 14
acetyl-DEVD-7-amido-4-methylcoumarin
additional information
acetyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56.7
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
pH and temperature not specified in the publication
11.7
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
pH and temperature not specified in the publication
20
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
pH and temperature not specified in the publication
33.3
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
pH and temperature not specified in the publication
25
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
pH and temperature not specified in the publication
13.3
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
pH and temperature not specified in the publication
28.3
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
pH and temperature not specified in the publication
96.7
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
pH and temperature not specified in the publication
20
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
pH and temperature not specified in the publication
135
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
pH and temperature not specified in the publication
13.3
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
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.0000012
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.000019
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.00006
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
pH 7.5, 30°C
0.000015
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
pH 7.5, 30°C
0.0014
5-[1-(pyrrolidinyl)sulfonyl]isatin
pH 7.5, 30°C
0.0000013
Acetyl-Asp-Glu-Val-Asp-aldehyde
pH 7.5, 22°C
0.0000124
acetyl-Asp-Met-Gln-Asp-aldehyde
pH 7.5, 22°C
0.0000065
acetyl-Val-Asp-Val-Ala-Asp-aldehyde
pH 7.5, 22°C
0.000165
(3S)-3-[[(2R)-2-[3-[(naphthalen-2-ylcarbonyl)amino]-2-oxopyridin-1(2H)-yl]-2-phenylacetyl]amino]-4-oxo-5-phenoxypentanoic acid
-
Ki-value is calculated from the initial rates
0.0021
(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
-
-
0.00016
(S)-3-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyridin-2-ylmethyl]sulfamoyl]benzoic acid
-
pH 7.4
0.0017
(S)-3-[[6-(benzenesulfonylamino-methyl)pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.00047
(S)-3-[[6-[(3-acetylsulfamoyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0017
(S)-3-[[6-[(3-methanesulfonyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0013
(S)-3-[[6-[(3-methanesulfonylamino-benzenesulfonylamino)methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0014
(S)-3-[[6-[(3-methanesulfonylaminocarbonyl-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxobutyric acid
-
pH 7.4
0.0023
(S)-3-[[6-[(4-hydroxy-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.0019
(S)-3-[[6-[(4-methanesulfonylamino-benzenesulfonylamino)methyl]pyridien-3-carbonyl]amino]-4-oxo-butyric acid
-
pH 7.4
0.00044
(S)-4-oxo-3-[[6-[[3-(1H-tetrazol-5-yl)benzenesulfonylamino]methyl]pyridine-3-carbonyl]amino]butyric acid
-
pH 7.4
0.0004
(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
-
pH 7.4
0.00021
(S)-4-[[4-(hydroxy-3-methyl-benzenesulfonylamino)methyl]thiophene]-2-carboxylic acid [3-(2-chloro-benzylsulfanyl)-1-ethyl-2-oxo-propyl]amide
-
pH 7.4
0.00016
(S)-5-[[3-(1-carboxymethyl-2-oxo-ethylcarbamoyl)isooxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00006
(S)-5-[[3-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]isoxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.0025
(S)-5-[[4-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00029
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-4-methyl-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.0125
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00048
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00007
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00012
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.004
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00005
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxybenzoic acid
-
pH 7.4
0.00019
(S)-5-[[5-(1-carboxymethyl-3-methylsulfanyl-2-oxo-propylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-3-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-4-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00004
(S)-5-[[5-[1-carboxymethyl-3(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]-4-methyl-thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.004
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00009
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00003
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00002
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00027
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00024
(S)-5-[[5-[1-carboxymethyl-5-(2-chloro-phenyl)-2-oxopentylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.000011
1-methyl-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.000077
3,3-dimethyl-8-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
Ki-value is calculated from the initial rates
0.0000161
5-([(2S)-2-[(pyridin-3-yloxy)methyl]pyrrolidin-1-yl]sulfonyl)-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.0000025
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-phenyl-1H-indole-2,3-dione
-
Ki-value is calculated from the initial rates
0.00029
5-[[5-[1-carboxymethyl-2-(7-methyl-benzoxazol-2-yl)-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.00038
5-[[5-[1-carboxymethyl-2-[5-(2,6-dichloro-phenyl)-oxazol-2-yl]-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
pH 7.4
0.000478
8-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,3-dimethyl-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
Ki-value is calculated from the initial rates
0.000042
acetyl-AEVD-aldehyde
-
pH 7.5, 25°C
0.045
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.0058
Acetyl-Asp-Glu-Val-Asp-aldehyde
-
-
0.00000023 - 0.0008
acetyl-DEVD-aldehyde
0.000195
acetyl-IETD-aldehyde
-
pH 7.5, 25°C
0.00196
acetyl-WEHD-aldehyde
-
pH 7.5, 25°C
0.012
acetyl-YVAD-aldehyde
-
pH 7.5
0.022
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.000108
c-IAP-1
-
37°C
-
0.000035
c-IAP-2
-
37°C
-
0.0016
cowpox serpin CrmA
-
pH 7.5, 25°C
-
0.022
m-(Ac-L-Asp-L-Val-NH)-N-nitroso-N-phenylglycine
-
pH 7.5, 37°C
0.0015
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-3-phenylpropyl]-L-valinamide
-
-
0.0035
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxo-4-phenylbutyl]-L-valinamide
-
-
0.0011
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxoheptyl]-L-valinamide
-
-
0.0013
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-2-oxooctyl]-L-valinamide
-
-
0.0002
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(2,5-dimethylphenyl)-2-oxobutyl]-L-valinamide
-
-
0.0007
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(1S)-1-(carboxymethyl)-4-(3-methylphenyl)-2-oxobutyl]-L-valinamide
-
-
0.002
N-acetyl-L-alpha-aspartyl-L-valyl-N-[(1S)-2-carboxy-1-[[(4-methylphenyl)(nitroso)amino]methyl]ethyl]-L-alaninamide
-
pH 7.5, 30°C
0.0000036
N-benxylozycarbonyl-tLeu-Asp
-
pH 7.4, 25°C
0.0000182
N-benxylozycarbonyl-tLeu-Val-Asp
-
pH 7.4, 25°C
0.000109
N-benxylozycarbonyl-Val-tLeu-Asp
-
pH 7.4, 25°C
0.000036
survivin
-
pH 7.5, 37°C
-
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.0000042
(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
0.00003
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 30 nM
0.0000031
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 3.1 nM
0.00012
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 120 nM
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
0.00017
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
0.0000012
Ac-DEVD-CHO
Homo sapiens
-
0.000012
Ac-DMQD-CHO
Homo sapiens
-
0.0012
Ac-IEPD-CHO
Homo sapiens
-
0.0019
Ac-WEHD-CHO
Homo sapiens
-
0.01
Ac-YVAD-CHO
Homo sapiens
-
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
0.0142
(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
0.000017
(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
0.000029
(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
0.0000053
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
Homo sapiens
-
37°C
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
0.000359
(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
0.04674
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
0.000085
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
0.000018
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
0.0000068
Ac-CV3-KE
Homo sapiens
-
at pH 7.4 and 22°C
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
0.000001
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
0.00003
M826
Homo sapiens
-
IC50: 0.00003 mM
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
0.01356
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
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
reaction with acetyl-DEVD-7-amido-4-methylcoumarin
7.2
-
assay at
7.5
-
assay at
8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
endometrial carcinoma cell line
Manually annotated by BRENDA team
-
primary
Manually annotated by BRENDA team
-
platelet-derived microparticles
Manually annotated by BRENDA team
-
arteriosclerotic carotid artery
Manually annotated by BRENDA team
-
overexpressing Bcl2-Like12 nuclear and cytoplasmic oncoprotein
Manually annotated by BRENDA team
-
endometrial carcinoma cell line
Manually annotated by BRENDA team
-
endometrial carcinoma cell line
Manually annotated by BRENDA team
-
emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
Manually annotated by BRENDA team
-
ovarian epithelial cell line
Manually annotated by BRENDA team
-
ovarian epithelial cell line
Manually annotated by BRENDA team
-
ovarian epithelial cell line
Manually annotated by BRENDA team
-
a oral squamous cell carcinoma cell line
Manually annotated by BRENDA team
-
a oral squamous cell carcinoma cell line
Manually annotated by BRENDA team
-
renal tubule
Manually annotated by BRENDA team
-
chronic lymphocytic
Manually annotated by BRENDA team
-
the caspase-3 activity is about 2.4, 3.3, and 4.7fold higher in hepatitis C virus noncirrhosis, nonalcoholic fatty liver disease, and HCV cirrhosis cohorts, respectively, compared to healthy volunteers
Manually annotated by BRENDA team
-
expression patterns of the major caspases, CASP3, 6, 7, 8, 9, and 10, and inhibitor of apoptosis proteins, survivin, CIAP1, CIAP2, XIAP, and livin, overview
Manually annotated by BRENDA team
-
expression patterns of the major caspases, CASP3, 6, 7, 8, 9, and 10, and inhibitor of apoptosis proteins, survivin, CIAP1, CIAP2, XIAP, and livin, overview
Manually annotated by BRENDA team
-
ovarian carcinoma cell line
Manually annotated by BRENDA team
-
ovarian carcinoma cell line
Manually annotated by BRENDA team
-
ovarian carcinoma cell line
Manually annotated by BRENDA team
-
ovarian carcinoma cell line
Manually annotated by BRENDA team
-
endometrial carcinoma cell line
Manually annotated by BRENDA team
-
ovarian carcinoma cell line
Manually annotated by BRENDA team
-
from healthy and arthritic individuals
Manually annotated by BRENDA team
-
upper part, expression of caspase-3 is associated with the pathologic stage in urothelial carcinomas, immunohistochemic analysis, overview
Manually annotated by BRENDA team
-
from umbilical cord
Manually annotated by BRENDA team
additional information
-
the MCF-7 human breast carcinoma cell line is caspase-3-deficient because of the deletion of exon 3 in the caspase-3 gene
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
bound to heavy membrane fraction, the N-termini of activated heavy-membrane-bound and cytoplasmic caspase-3 are slightly different: the heavy membrane caspase-3 begins at Lys14, whereas the cytoplasmic enzyme begins at Ser10
Manually annotated by BRENDA team
-
activated enzyme, the enzyme harbors one crm-1-independent nuclear export signal but no nuclear localization signal residing at the small subunit of caspase-3. The nuclear entry of active caspase-3 is not mediated by passive diffusion, but by its p3-recognition-based specific cleavage activity. The p3-mediated cleavage activity abrogates the function of the nuclear localization signal in caspase-3, which is essential for the active caspase-3 to enter into the nucleus
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
cleavage by caspase-3 is a crucial upstream event associated with Tau self-assembly leading to Alzheimer's Disease pathogenesis
evolution
-
caspase-3 is an executioner caspase
malfunction
-
mutations disrupting the cleavage activity or the p3 recognition site cause a defect in the nuclear entry of active caspase-3
metabolism
-
tumour necrosis factor, TNF, induced ceramide production by endosomal acid sphingomyelinase, A-SMase, couples to apoptosis signalling via activation of cathepsin D and cleavage of Bid, resulting in caspase-9 and caspase-3 activation
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP3_HUMAN
277
0
31608
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
x * 15000, recombinant, active processed enzyme, SDS-PAGE, x * 35000, recombinant, inactive unprocessed enzyme, SDS-PAGE
19000
-
x * 19000, cleaved caspase-3, SDS-PAGE
35000
-
x * 15000, recombinant, active processed enzyme, SDS-PAGE, x * 35000, recombinant, inactive unprocessed enzyme, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
dimer
-
active caspase-3 is a homodimer of two heterodimer subunits, with one active site on each subunit
heterotetramer
-
2 * p17, large subunit, + 2 * p12, small subunit, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
both Mch4 and granzyme B cleave recombinant proCPP32 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Granzyme B cleaves at Asp175 to generate the small C-terminal subunit, 12000 Da, and te large N-terminal subunit. Cleavage of the prodomain is an autocatalytic activity of the activated CPP32
proteolytic modification
additional information
-
caspase-3 is S-nitrosylated under basal conditions to prevent activation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor Asp-Glu-Val-Asp-chloromethylketone
in complex with inhibitors acetyl-Asp-Glu-Val-Asp-aldehyde, acetyl-Val-Asp-Val-Ala-Asp-aldehyde, acetyl-Asp-Met-Gln-Asp-aldehyde
recombinant enzyme in complex with inhibitors Ac-IEPD-Cho, Ac-WEHD-Cho, Ac-YVADCho, and Boc-D(OMe)-fluoromethyl ketone, caspase-3 is incubated at room temperature with the inhibitor at 10 to 20fold molar excess, followed by crystallization via the hanging-drop vapor diffusion method, 0.001 ml of 4 mg/ml protein in solution is mixed with an equal volume of mother liquid containing 100 mM sodium citrate, 5% glycerol, 10 mM DTT, and 14-18% PEG 6000, pH 6.5, 24 h at room temperature, X-ray diffraction structure determination and analysis at 1.9-2.6 A resolution, molecular replacement, modelling, overview
caspase-3 in complex with beta-strand urazole ring-containing irreversible peptidomimetic inhibitor compound-1, vapor diffusion, at 4°C, from 0.005 ml drops containing equal volumes of 16% ethanol, 0.1 M Tris buffer, pH 7.8, and the protein complex solution, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement
-
co-crystals of the complex between recombinant human caspase-3 and azapeptide epoxide inhibitors are grown from hanging drops
-
complex of caspase-3 with (S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid and (S)-5-[[5-[1-carboxylmethyl-3-(2-chlorobenzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid, hanging drop vapor diffusion method
-
crystal structure of recombinant enzyme in complex with acetyl-Asp-Val-Ala-Asp fluoromethyl ketone, hanging and sitting drop vapor diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D179A
increase both in kcat- and KM-value. D179 is involved in substrate recognition
DELTA176-181
decrease both in kcat- and KM-value
C143A
-
inactive enzyme. Catalytically inactive p17 polypeptide is expressed in a stable manner, while wild-type p17 is rapidly degraded
R207E/C163S
-
site-directed mutagenesis, the mutant resides in the cytoplasm
R64E
-
site-directed mutagenesis, the mutant existed in the nuclear fraction, the subcellular localization signal in the rev-caspase-3 is not disrupted by the R64E mutation
R64E/C163S
-
site-directed mutagenesis, the mutant resides in the cytoplasm
R64E/R207E
-
site-directed mutagenesis, the mutant resides in the cytoplasm
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by nickel affinity chromatography, ion exchange chromatography, and gel filtration
recombinant enzyme, inclusion bodies produced in Escherichia coli
Ni-NTA agarose column chromatography and Resource Q column chromatography
-
recombinant His6-tagged caspase-3 from Escherichia coli by nickel affinity chromatography
-
upon purification and activation, caspase-3 subunits A and B are processed to yield the sequences S29GIS...IETD175 and S176GVD…YFYH277-(H)7, the purified enzyme shows 90% of maximum activity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3)
expression of FLAG-tagged caspase-3 in DKD cells. Simultaneous expression of HA-procaspase-3 and HA-procaspase-7, EC 3.4.22.60, in DKD HeLa cells together with FLAG-caspase-3 or FLAG-caspase-7. HA-procaspase-3 is coimmunoprecipitated with FLAG-procaspase-3 but not with FLAG-procaspase-7. Similarly, HA-procaspase-7 is co-immunoprecipitated with FLAG-procaspase-7 but not with FLAG-procaspase-3
the full-length caspase-3 gene containing an N-terminal 6His-tag is expressed in Escherichia coli
CASP3, expression analysis in melanoma cells
-
caspase-3 expression analysis
-
caspase-3 expression analysis in CLL cells
-
engineering of a light-activated human caspase-3 (Caspase-LOV) by exploiting its natural spring-loaded activation mechanism through rational insertion of the light-sensitive LOV2 domain that expands upon illumination. Using the tissue-specific expression system (UAS)-GAL4, Caspase-LOV is specifically expressed in three neuronal cell types: retinal, sensory, and motor neuron of Drosophila
expressed in Escherichia coli Transetta (DE3) cells
-
expression of His6-tagged caspase-3 in Escherichia coli, effects of transiently-expressed VhhCasp31 and VhhCasp32 intrabodies on oxidative-stress-induced apoptosis in SHSY-5Y cells, overview
-
GFP-tagged subunit and enzyme expression, the small subunit as well as the full-length caspase-3 display evident cytoplasm localization, while the large subunit and its truncated forms are distributed throughout the whole cell
-
quantitative expression analysis in several ovarian and endometrial cancer cell lines by RT-PCR
-
sequence encoding the caspase-3 catalytic domain (no prodomain) with a C-terminal hexa-His tag is inserted into vector pET-16b and expressed in Escherichia coli BL21
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
0.05 mM lunasin-induced apoptosis increases caspase-3 activity by 77%
-
cooperative apoptosis induction by melatonin and doxorubicin is associated with increased expression of caspase 3
-
in contrast to low XIAP expression, the A5-16 strain shows enhanced cleavage of caspase-3 as early as 8 hours post infection with a 6-8fold increase by 12 hours post infection. There is a significant increase in caspase-3 activity (2-3fold) at an early stage of infection (4-8 hours post infection) in mutant strain A5-16-infected cells compared to the A5-13 infection. At 12-18 hours post infection, the caspase-3 activity in A5-13-infected cells increases significantly relative to mock-infected controls
-
significant correlation is seen between plasma nitrite/nitrate-concentrations and caspase-3 activity, which is significantly higher in patients with schizophrenia than in controls
-
there is an about 4fold increase of activated caspase-3 expression 4 days after high dose treatment with 100 nM L-arginase in Panc-1 and Hep-3B cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
drug development
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Srinivasula, S.M.; Fernandes-Alnemri, T.; Zangrilli, J.; Robertson, N.; Armstrong, R.C.; Wang, L.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri E.S.
The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32
J. Biol. Chem.
271
27099-27106
1996
Homo sapiens
Manually annotated by BRENDA team
Zhivotovsky, B.; Samali, A.; Gahm, A.; Orrenius, S.
Caspases: their intracellular localization and translocation during apoptosis
Cell Death Differ.
6
644-651
1999
Homo sapiens
Manually annotated by BRENDA team
Garcia-Calvo, M.; Peterson, E.P.; Leiting, B.; Ruel, R.; Nicholson, D.W.; Thornberry, N.A.
Inhibition of human caspases by peptide-based and macromolecular inhibitors
J. Biol. Chem.
273
32608-32613
1998
Homo sapiens
Manually annotated by BRENDA team
Garcia-Calvo, M.; Peterson, E.P.; Rasper, D.M.; Vaillancourt, J.P.; Zamboni, R.; Nicholson, D.W.; Thornberry, N.A.
Purification and catalytic properties of human caspase family members
Cell Death Differ.
6
362-369
1999
Homo sapiens
Manually annotated by BRENDA team
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens
Manually annotated by BRENDA team
Thornberry, N.A.; Rano, T.A.; Peterson, E.P.; et al.
A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
J. Biol. Chem.
272
17907-17911
1997
Homo sapiens
Manually annotated by BRENDA team
Fernandes-Alnemri, T.; Armstrong, R.C.; Krebs, J.F.; Srinivasula, S.M.; Wang, L.; Bullrich, F.; Fritz, L.C.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri, E.S.
In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
Proc. Natl. Acad. Sci. USA
93
7464-7469
1996
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Talanian, R.V.; Quinlan, C.; Trautz, S.; Hackett, M.C.; Mankovich, J.A.; Banach, D.; Ghayur, T.; Brady, K.D.; Wong, W.W.
Substrate specificities of caspase family proteases
J. Biol. Chem.
272
9677-9682
1997
Homo sapiens
Manually annotated by BRENDA team
Samejima, K.; Svigen, P.A.; Basi, G.S.; Kottke, T.; Mesner, P.W.; Stewart, L.; Durrieu, F.; Poirier, G.G.; Alnemri, E.S.; Champoux, J.J.; Kaufmann, S.H.; Earnshaw, W.C.
caspase-mediated cleavage of DNA topoisomerase I at unconventional sites during apoptosis
J. Biol. Chem.
274
4335-4340
1999
Homo sapiens
Manually annotated by BRENDA team
Hirata, H.; Takahashi, A.; Kobayashi, S.; Yonehara, S.; Sawai, H.; Okazaki, T.; Yamamoto, K.; Sasada, M.
Caspases are activated in a branched protease cascade and control didtinct downstream processes in fas-induced apoptosis
J. Exp. Med.
187
587-600
1998
Homo sapiens
Manually annotated by BRENDA team
Fernandes-Alnemri, T.; Litwack, G.; Alnemri E.S.
CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme
J. Biol. Chem.
269
30761-30764
1994
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Tewari, M.; Quan, L.T.; O'Rourke, K.; Desnoyers, S.; Zeng, Z.; Beidler, D.R.; Poirier, G.G.; Salvesen, G.S.; Dixit, V.M.
Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
Cell
81
801-809
1995
Homo sapiens (P42574)
Manually annotated by BRENDA team
Lee, D.; Long, S.A.; Adams, J.L.; Chan, G.; et al.
Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit apoptosis and maintain cell functionality
J. Biol. Chem.
275
16007-16014
2000
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Goldberg, Y.P.; Nicholson, D.W.; Rasper, D.M.; Kalchman, M.A.; Koide, H.B.; et al.
Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
Nat. Genet.
13
442-449
1996
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Bellido, T.; Huening, M.; Raval-Pandya, M.; Manolagas, S.C.; Christakos, S.
Calbindin-D28k is expressed in osteoblastic cells and suppresses their apoptosis by inhibiting caspase-3 activity
J. Biol. Chem.
275
26328-26332
2000
Homo sapiens
Manually annotated by BRENDA team
Decker, P.; Isenberg, D.; Muller, S.
Inhibition of caspase-3-mediated poly(ADP-ribose) polymerase (PARP) apoptotic cleavage by human PARP autoantibodies and effect on cells undergoing apoptosis
J. Biol. Chem.
275
9043-9046
2000
Homo sapiens
Manually annotated by BRENDA team
Mohr, S.; Zech, B.; Lapetina, E.G.; Brune, B.
Inhibition of caspase-3 by S-nitrosation and oxidation caused by nitric oxide
Biochem. Biophys. Res. Commun.
238
387-391
1997
Homo sapiens
Manually annotated by BRENDA team
Guo, Z.; Xian, M.; Zhang, W.; McGill, A.; Wang, P.G.
N-nitrosoanilines: a new class of caspase-3 inhibitors
Bioorg. Med. Chem.
9
99-106
2001
Homo sapiens
Manually annotated by BRENDA team
Han, B.H.; Xu, D.; Choi, J.; Han, Y.; Xanthoudakis, S.; Roy, S.; Tam, J.; Vaillancourt, J.; Colucci, J.; Siman, R.; Giroux, A.; Robertson, G.S.; Zamboni, R.; Nicholson, D.W.; Holtzman, D.M.
Selective, reversible caspase-3 inhibitor is neuroprotective and reveals distinct pathways of cell death after neonatal hypoxic-ischemic brain injury
J. Biol. Chem.
277
30128-30136
2002
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Erhadt, P.; Tomaselli, K.J.; Cooper, G.M.
Identification of the MDM2 oncoprotein as a substrate for CPP32-like apoptotic proteases
J. Biol. Chem.
272
15049-15052
1997
Homo sapiens
Manually annotated by BRENDA team
Krebs, J.F.; Srinivasan, A.; Wong, A.M.; Tomaselli, K.J.; Fritz, L.C.; Wu, J.C.
Heavy membrane-associated caspase 3: identification, isolation, and characterization
Biochemistry
39
16056-16063
2000
Homo sapiens
Manually annotated by BRENDA team
Marissen, W.E.; Lloyd, R.E.
Eukaryotic translation initiation factor 4G is targeted for proteolytic cleavage by caspase 3 during inhibition of translation in apoptotic cells
Mol. Cell. Biol.
18
7565-7574
1998
Homo sapiens
Manually annotated by BRENDA team
Rheaume, E.; Cohen, L.Y.; Uhlmann, F.; Lazure, C.; Alam, A.; Hurwitz, J.; Sekaly, R.P.; Denis, F.
The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosis
EMBO J.
16
6346-6354
1997
Homo sapiens
Manually annotated by BRENDA team
Rssig, L.; Fichtlscherer, B.; Breitschopf, K.; Haendeler, J.; Zeiher, A.M.; Mulsch, A.; Dimmeler, S.
Nitric oxide inhibits caspase-3 by S-nitrosation in vivo
J. Biol. Chem.
274
6823-6826
1999
Homo sapiens
Manually annotated by BRENDA team
Schlegel, J.; Peters, I.; Orrenius, S.; Miller, D.K.; Thornberry, N.A.; Yamin, T.T.; Nicholson, D.W.
CPP32/apopain is a key interleukin 1beta converting enzyme-like protease involved in Fas-mediated apoptosis
J. Biol. Chem.
271
1841-1844
1996
Homo sapiens
Manually annotated by BRENDA team
Roy, N.; Deveraux, Q.L.; Takahashi, R.; Salvesen, G.S.; Reed, J.C.
The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
EMBO J.
16
6914-6925
1997
Homo sapiens
Manually annotated by BRENDA team
Shin, S.; Sung, B.J.; Cho, Y.S.; Kim, H.J.; Ha, N.C.; Hwang, J.I.; Chung, C.W.; Jung, Y.K.; Oh, B.H.
An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7
Biochemistry
40
1117-1123
2001
Homo sapiens
Manually annotated by BRENDA team
Smith, L.; Chen, L.; Reyland, M.E.; DeVries, T.A.; Talanian, R.V.; Omura, S.; Smith, J.B.
Activation of atypical protein kinase C zeta by caspase processing and degradation by the ubiquitin-proteasome system
J. Biol. Chem.
275
40620-40627
2000
Homo sapiens
Manually annotated by BRENDA team
Takahashi, A.; Alnemri, E.S.; Lazebnik, Y.A.; Fernandes-Alnemri, T.; Litwack, G.; Moir, R.D.; Goldman, R.D.; Poirier, G.G.; Kaufmann, S.H.; Earnshaw, W.C.
Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis
Proc. Natl. Acad. Sci. USA
93
8395-8400
1996
Homo sapiens
Manually annotated by BRENDA team
Choong, I.C.; Lew, W.; Lee, D.; Pham, P.; Burdett, M.T.; Lam, J.W.; Wiesmann, C.; Luong, T.N.; Fahr, B.; DeLano, W.L.; McDowell, R.S.; Allen, D.A.; Erlanson, D.A.; Gordon, E.M.; O'Brien, T.
Identification of potent and selective small-molecule inhibitors of caspase-3 through the use of extended tethering and structure-based drug design
J. Med. Chem.
45
5005-5022
2002
Homo sapiens
Manually annotated by BRENDA team
Essmann, F.; Wieder, T.; Otto, A.; Muller, E.C.; Dorken, B.; Daniel, P.T.
GDP dissociation inhibitor D4-GDI (Rho-GDI 2), but not the homologous rho-GDI 1, is cleaved by caspase-3 during drug-induced apoptosis
Biochem. J.
346
777-783
2000
Homo sapiens
Manually annotated by BRENDA team
Perry, D.K.; Smyth, M.J.; Stennicke, H.R.; Salvesen, G.S.; Duriez, P.; Poirier, G.G.; Hannun, Y.A.
Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis
J. Biol. Chem.
272
18530-18533
1997
Homo sapiens
Manually annotated by BRENDA team
Deveraux, Q.L.; Roy, N.; Stennicke, H.R.; Van Arsdale, T.; Zhou, Q.; Srinivasula, S.M.; Alnemri, E.S.; Salvesen, G.S.; Reed, J.C.
IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
EMBO J.
17
2215-2223
1998
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mittl, P.R.E.; di Marco, S.; Krebs, J.F.; et al.
Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone
J. Biol. Chem.
272
6539-6547
1997
Homo sapiens
Manually annotated by BRENDA team
Margolin, N.; Raybuck, S.A.; Wilson, K.P.; Chen, W.; Fox, T.; Gu, Y.; Livingston, D.J.
Substrate and inhibitor specificity of interleukin-1beta-converting enzyme and related caspases
J. Biol. Chem.
272
7223-7228
1997
Homo sapiens
Manually annotated by BRENDA team
Pirhonen, J.; Sareneva, T.; Julkunen, I.; Matikainen, S.
Virus infection induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
Eur. J. Immunol.
31
726-733
2001
Homo sapiens
Manually annotated by BRENDA team
Bae, S.S.; Choi, J.H.; Oh, Y.S.; Perry, D.K.; Ryu, S.H.; Suh, P.G.
Proteolytic cleavage of epidermal growth factor receptor by caspases
FEBS Lett.
491
16-20
2001
Homo sapiens
Manually annotated by BRENDA team
Kisselev, A.F.; Garcia-Calvo, M.; Overkleeft, H.S.; Peterson, E.; Pennington, M.W.; Ploegh, H.L.; Thornberry, N.A.; Goldberg, A.L.
the caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites
J. Biol. Chem.
278
35869-35877
2003
Homo sapiens
Manually annotated by BRENDA team
Tawa, P.; Giroux, A.; Grimm, E.; Han, Y.; Nicholson, D.W.; Xanthoudakis, S.
Correlating the fractional inhibition of caspase-3 in NT2 cells with apoptotic markers using an active-caspase-3 enzyme-linked immunosorbent assay
Anal. Biochem.
350
32-40
2006
Homo sapiens
Manually annotated by BRENDA team
Han, Y.; Giroux, A.; Colucci, J.; Bayly, C.I.; Mckay, D.J.; Roy, S.; Xanthoudakis, S.; Vaillancourt, J.; Rasper, D.M.; Tam, J.; Tawa, P.; Nicholson, D.W.; Zamboni, R.J.
Novel pyrazinone mono-amides as potent and reversible caspase-3 inhibitors
Bioorg. Med. Chem. Lett.
15
1173-1180
2005
Homo sapiens
Manually annotated by BRENDA team
Wang, Z.Q.; Liao, J.; Diwu, Z.
N-DEVD-N-morpholinecarbonyl-rhodamine 110: novel caspase-3 fluorogenic substrates for cell-based apoptosis assay
Bioorg. Med. Chem. Lett.
15
2335-2338
2005
Homo sapiens
Manually annotated by BRENDA team
Schlittenhardt, D.; Schmiedt, W.; Bonaterra, G.A.; Metz, J.; Kinscherf, R.
Colocalization of oxidized low-density lipoprotein, caspase-3, cyclooxygenase-2, and macrophage migration inhibitory factor in arteriosclerotic human carotid arteries
Cell Tissue Res.
322
425-435
2005
Homo sapiens
Manually annotated by BRENDA team
Kravchenko, D.V.; Kysil, V.M.; Tkachenko, S.E.; Maliarchouk, S.; Okun, I.M.; Ivachtchenko, A.V.
Pyrrolo[3,4-c]quinoline-1,3-diones as potent caspase-3 inhibitors. Synthesis and SAR of 2-substituted 4-methyl-8-(morpholine-4-sulfonyl)-pyrrolo[3,4-c]quinoline-1,3-diones
Eur. J. Med. Chem.
40
1377-1383
2005
Homo sapiens
Manually annotated by BRENDA team
Sliskovic, I.; Mutus, B.
Reversible inhibition of caspase-3 activity by iron(III): potential role in physiological control of apoptosis
FEBS Lett.
580
2233-2237
2006
Homo sapiens
Manually annotated by BRENDA team
Weng, C.; Li, Y.; Xu, D.; Shi, Y.; Tang, H.
Specific cleavage of Mcl-1 by caspase-3 in tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis in Jurkat leukemia T cells
J. Biol. Chem.
280
10491-10500
2005
Homo sapiens
Manually annotated by BRENDA team
Okun, I.; Malarchuk, S.; Dubrovskaya, E.; Khvat, A.; Tkachenko, S.; Kysil, V.; Ilyin, A.; Kravchenko, D.; Prossnitz, E.R.; Sklar, L.; Ivachtchenko, A.
Screening for caspase-3 inhibitors: a new class of potent small-molecule inhibitors of caspase-3
J. Biomol. Screen.
11
277-285
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.H.; Zhang, Y.H.; Zhang, H.J.; Liu, D.Z.; Gu, M.; Li, J.Y.; Wu, F.; Zhu, X.Z.; Li, J.; Nan, F.J.
Design, synthesis, and biological evaluation of isoquinoline-1,3,4-trione derivatives as potent caspase-3 inhibitors
J. Med. Chem.
49
1613-1623
2006
Homo sapiens
Manually annotated by BRENDA team
Ganesan, R.; Mittl, P.R.; Jelakovic, S.; Gruetter, M.G.
Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis
J. Mol. Biol.
359
1378-1388
2006
Homo sapiens (P42574)
Manually annotated by BRENDA team
Fang, B.; Boross, P.I.; Tozser, J.; Weber, I.T.
Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition
J. Mol. Biol.
360
654-666
2006
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Goode, D.R.; Sharma, A.K.; Hergenrother, P.J.
Using peptidic inhibitors to systematically probe the S1 site of caspase-3 and caspase-7
Org. Lett.
7
3529-3532
2005
Homo sapiens
Manually annotated by BRENDA team
Denault, J.B.; Eckelman, B.P.; Shin, H.; Pop, C.; Salvesen, G.S.
Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9
Biochem. J.
405
11-19
2007
Homo sapiens
Manually annotated by BRENDA team
Huang, Z.; Pinto, J.T.; Deng, H.; Richie, J.P.
Inhibition of caspase-3 activity and activation by protein glutathionylation
Biochem. Pharmacol.
75
2234-2244
2008
Homo sapiens
Manually annotated by BRENDA team
Ganesan, R.; Jelakovic, S.; Campbell, A.J.; Li, Z.Z.; Asgian, J.L.; Powers, J.C.; Gruetter, M.G.
Exploring the S4 and S1 prime subsite specificities in caspase-3 with aza-peptide epoxide inhibitors
Biochemistry
45
9059-9067
2006
Homo sapiens
Manually annotated by BRENDA team
Aulabaugh, A.; Kapoor, B.; Huang, X.; Dollings, P.; Hum, W.T.; Banker, A.; Wood, A.; Ellestad, G.
Biochemical and biophysical characterization of inhibitor binding to caspase-3 reveals induced asymmetry
Biochemistry
46
9462-9471
2007
Homo sapiens
Manually annotated by BRENDA team
Lu, W.; Lee, H.K.; Xiang, C.; Finniss, S.; Brodie, C.
The phosphorylation of tyrosine 332 is necessary for the caspase 3-dependent cleavage of PKCdelta and the regulation of cell apoptosis
Cell. Signal.
19
2165-2173
2007
Homo sapiens
Manually annotated by BRENDA team
Song, J.J.; Lee, Y.J.
Differential cleavage of Mst1 by caspase-7/-3 is responsible for TRAIL-induced activation of the MAPK superfamily
Cell. Signal.
20
892-906
2008
Homo sapiens
Manually annotated by BRENDA team
Cen, H.; Mao, F.; Aronchik, I.; Fuentes, R.J.; Firestone, G.L.
DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells
FASEB J.
22
2243-2252
2008
Homo sapiens
Manually annotated by BRENDA team
Voss, O.H.; Batra, S.; Kolattukudy, S.J.; Gonzalez-Mejia, M.E.; Smith, J.B.; Doseff, A.I.
Binding of caspase-3 prodomain to heat shock protein 27 regulates monocyte apoptosis by inhibiting caspase-3 proteolytic activation
J. Biol. Chem.
282
25088-25099
2007
Homo sapiens
Manually annotated by BRENDA team
Wales, S.Q.; Li, B.; Laing, J.M.; Aurelian, L.
The herpes simplex virus type 2 gene ICP10PK protects from apoptosis caused by nerve growth factor deprivation through inhibition of caspase-3 activation and XIAP up-regulation
J. Neurochem.
103
365-379
2007
Homo sapiens
Manually annotated by BRENDA team
Hote, P.T.; Sahoo, R.; Jani, T.S.; Ghare, S.S.; Chen, T.; Joshi-Barve, S.; McClain, C.J.; Barve, S.S.
Ethanol inhibits methionine adenosyltransferase II activity and S-adenosylmethionine biosynthesis and enhances caspase-3-dependent cell death in T lymphocytes: relevance to alcohol-induced immunosuppression
J. Nutr. Biochem.
19
384-391
2007
Homo sapiens
Manually annotated by BRENDA team
Pan, J.; Quintas-Cardama, A.; Manshouri, T.; Giles, F.J.; Lamb, P.; Tefferi, A.; Cortes, J.; Kantarjian, H.; Verstovsek, S.
The novel tyrosine kinase inhibitor EXEL-0862 induces apoptosis in human FIP1L1-PDGFR-alpha-expressing cells through caspase-3-mediated cleavage of Mcl-1
Leukemia
21
1395-1404
2007
Homo sapiens
Manually annotated by BRENDA team
Schweigreiter, R.; Stasyk, T.; Contarini, I.; Frauscher, S.; Oertle, T.; Klimaschewski, L.; Huber, L.A.; Bandtlow, C.E.
Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site
Proteomics
7
4457-4467
2007
Homo sapiens
Manually annotated by BRENDA team
Wang, C.; Wu, X.; Chen, M.; Duan, W.; Sun, L.; Yan, M.; Zhang, L.
Emodin induces apoptosis through caspase 3-dependent pathway in HK-2 cells
Toxicology
231
120-128
2007
Homo sapiens
Manually annotated by BRENDA team
Valanne, A.; Malmi, P.; Appelblom, H.; Niemelae, P.; Soukka, T.
A dual-step fluorescence resonance energy transfer-based quenching assay for screening of caspase-3 inhibitors
Anal. Biochem.
375
71-81
2008
Homo sapiens
Manually annotated by BRENDA team
Cheah, Y.H.; Nordin, F.J.; Tee, T.T.; Azimahtol, H.L.; Abdullah, N.R.; Ismail, Z.
Antiproliferative property and apoptotic effect of xanthorrhizol on MDA-MB-231 breast cancer cells
Anticancer Res.
28
3677-3689
2009
Homo sapiens
Manually annotated by BRENDA team
Ideo, A.; Hashimoto, K.; Shimada, J.; Kawase, M.; Sakagami, H.
Type of cell death induced by alpha-trifluoromethyl acyloins in oral squamous cell carcinoma
Anticancer Res.
29
175-181
2009
Homo sapiens
Manually annotated by BRENDA team
Fang, B.; Fu, G.; Agniswamy, J.; Harrison, R.W.; Weber, I.T.
Caspase-3 binds diverse P4 residues in peptides as revealed by crystallography and structural modeling
Apoptosis
14
741-752
2009
Homo sapiens (P42574)
Manually annotated by BRENDA team
McGonigal, K.; Tanha, J.; Palazov, E.; Li, S.; Gueorguieva-Owens, D.; Pandey, S.
Isolation and functional characterization of single domain antibody modulators of caspase-3 and apoptosis
Appl. Biochem. Biotechnol.
157
226-236
2008
Homo sapiens
Manually annotated by BRENDA team
Dharmapatni, A.A.; Smith, M.D.; Findlay, D.M.; Holding, C.A.; Evdokiou, A.; Ahern, M.J.; Weedon, H.; Chen, P.; Screaton, G.; Xu, X.N.; Haynes, D.R.
Elevated expression of caspase-3 inhibitors, survivin and xIAP correlates with low levels of apoptosis in active rheumatoid synovium
Arthritis Res. Ther.
11
R13
2009
Homo sapiens
Manually annotated by BRENDA team
Artwohl, M.; Lindenmair, A.; Roden, M.; Waldhaeusl, W.K.; Freudenthaler, A.; Klosner, G.; Ilhan, A.; Luger, A.; Baumgartner-Parzer, S.M.
Fatty acids induce apoptosis in human smooth muscle cells depending on chain length, saturation, and duration of exposure
Atherosclerosis
202
351-362
2009
Homo sapiens
Manually annotated by BRENDA team
Colantonio, P.; Leboffe, L.; Bolli, A.; Marino, M.; Ascenzi, P.; Luisi, G.
Human caspase-3 inhibition by Z-tLeu-Asp-H: tLeu(P2) counterbalances Asp(P4) and Glu(P3) specific inhibitor truncation
Biochem. Biophys. Res. Commun.
377
757-762
2008
Homo sapiens
Manually annotated by BRENDA team
Sakai, J.; Yoshimori, A.; Nose, Y.; Mizoroki, A.; Okita, N.; Takasawa, R.; Tanuma, S.
Structure-based discovery of a novel non-peptidic small molecular inhibitor of caspase-3
Bioorg. Med. Chem.
16
4854-4859
2008
Homo sapiens
Manually annotated by BRENDA team
Podichetty, A.K.; Faust, A.; Kopka, K.; Wagner, S.; Schober, O.; Schaefers, M.; Haufe, G.
Fluorinated isatin derivatives. Part 1: synthesis of new N-substituted (S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatins as potent caspase-3 and -7 inhibitors
Bioorg. Med. Chem.
17
2680-2688
2009
Homo sapiens
Manually annotated by BRENDA team
Cao, X.H.; Liao, Z.Y.; Wang, C.L.; Cai, P.; Yang, W.Y.; Lu, M.F.; Huang, G.W.
Purification and antitumour activity of a lipopeptide biosurfactant produced by Bacillus natto TK-1
Biotechnol. Appl. Biochem.
52
97-106
2009
Homo sapiens
Manually annotated by BRENDA team
van Raam, B.J.; Drewniak, A.; Groenewold, V.; van den Berg, T.K.; Kuijpers, T.W.
Granulocyte colony-stimulating factor delays neutrophil apoptosis by inhibition of calpains upstream of caspase-3
Blood
112
2046-2054
2008
Homo sapiens
Manually annotated by BRENDA team
Azab, S.S.; Salama, S.A.; Abdel-Naim, A.B.; Khalifa, A.E.; El-Demerdash, E.; Al-Hendy, A.
2-Methoxyestradiol and multidrug resistance: can 2-methoxyestradiol chemosensitize resistant breast cancer cells?
Breast Cancer Res. Treat.
113
9-19
2009
Homo sapiens
Manually annotated by BRENDA team
Arisan, E.D.; Kutuk, O.; Tezil, T.; Bodur, C.; Telci, D.; Basaga, H.
Small inhibitor of Bcl-2, HA14-1, selectively enhanced the apoptotic effect of cisplatin by modulating Bcl-2 family members in MDA-MB-231 breast cancer cells
Breast Cancer Res. Treat.
119
271-281
2009
Homo sapiens
Manually annotated by BRENDA team
Chan, Q.K.; Ngan, H.Y.; Ip, P.P.; Liu, V.W.; Xue, W.C.; Cheung, A.N.
Tumor suppressor effect of follistatin-like 1 in ovarian and endometrial carcinogenesis: a differential expression and functional analysis
Carcinogenesis
30
114-121
2009
Homo sapiens
Manually annotated by BRENDA team
Meier, M.; Nitschke, M.; Hocke, C.; Kramer, J.; Jabs, W.; Steinhoff, J.; Schutt, M.
Insulin inhibits caspase-3 activity in human renal tubular epithelial cells via the PI3-kinase/Akt pathway
Cell. Physiol. Biochem.
21
279-286
2008
Homo sapiens
Manually annotated by BRENDA team
Schrieber, S.J.; Wen, Z.; Vourvahis, M.; Smith, P.C.; Fried, M.W.; Kashuba, A.D.; Hawke, R.L.
The pharmacokinetics of silymarin is altered in patients with hepatitis C virus and nonalcoholic fatty liver disease and correlates with plasma caspase-3/7 activity
Drug Metab. Dispos.
36
1909-1916
2008
Homo sapiens
Manually annotated by BRENDA team
Casely-Hayford, M.A.; Nicholas, S.A.; Sumbayev, V.V.
Azinomycin epoxide induces activation of apoptosis signal-regulating kinase 1 (ASK1) and caspase 3 in a HIF-1alpha-independent manner in human leukaemia myeloid macrophages
Eur. J. Pharmacol.
602
262-267
2009
Homo sapiens
Manually annotated by BRENDA team
Epple, H.J.; Schneider, T.; Troeger, H.; Kunkel, D.; Allers, K.; Moos, V.; Amasheh, M.; Loddenkemper, C.; Fromm, M.; Zeitz, M.; Schulzke, J.D.
Impairment of the intestinal barrier is evident in untreated but absent in suppressively treated HIV-infected patients
Gut
58
220-227
2009
Homo sapiens
Manually annotated by BRENDA team
Jeong, I.G.; Kim, S.H.; Jeon, H.G.; Kim, B.H.; Moon, K.C.; Lee, S.E.; Lee, E.
Prognostic value of apoptosis-related markers in urothelial cancer of the upper urinary tract
Hum. Pathol.
40
668-677
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, N.; Gong, J.; Chen, X.; Meng, W.; Huang, Y.; Zhao, F.; Wang, L.; Zhou, Q.
Caspases and inhibitor of apoptosis proteins in cutaneous and mucosal melanoma: expression profile and clinicopathologic significance
Hum. Pathol.
40
950-956
2009
Homo sapiens
Manually annotated by BRENDA team
Jin, D.; Ojcius, D.M.; Sun, D.; Dong, H.; Luo, Y.; Mao, Y.; Yan, J.
Leptospira interrogans induces apoptosis in macrophages via caspase-8- and caspase-3-dependent pathways
Infect. Immun.
77
799-809
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bairey, O.; Vanichkin, A.; Shpilberg, O.
Arsenic-trioxide-induced apoptosis of chronic lymphocytic leukemia cells
Int. J. Lab. Hematol.
32
e77-85
2009
Homo sapiens
Manually annotated by BRENDA team
Huang, H.S.; Lee, E.Y.
Protein phosphatase-1 inhibitor-3 is an in vivo target of caspase-3 and participates in the apoptotic response
J. Biol. Chem.
283
18135-18146
2008
Homo sapiens
Manually annotated by BRENDA team
Butkinaree, C.; Cheung, W.D.; Park, S.; Park, K.; Barber, M.; Hart, G.W.
Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis
J. Biol. Chem.
283
23557-23566
2008
Homo sapiens
Manually annotated by BRENDA team
Anathy, V.; Aesif, S.W.; Guala, A.S.; Havermans, M.; Reynaert, N.L.; Ho, Y.S.; Budd, R.C.; Janssen-Heininger, Y.M.
Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
J. Cell Biol.
184
241-252
2009
Homo sapiens
Manually annotated by BRENDA team
Frydrych, I.; Mlejnek, P.
Serine protease inhibitors N-alpha-tosyl-L-lysinyl-chloromethylketone (TLCK) and N-tosyl-L-phenylalaninyl-chloromethylketone (TPCK) do not inhibit caspase-3 and caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli
J. Cell. Biochem.
105
1501-1506
2008
Homo sapiens
Manually annotated by BRENDA team
Alam, M.M.; Mohammad, A.A.; Shuaib, U.; Wang, C.; Ghani, U.; Schwindt, B.; Todd, K.G.; Shuaib, A.
Homocysteine reduces endothelial progenitor cells in stroke patients through apoptosis
J. Cereb. Blood Flow Metab.
29
157-165
2009
Homo sapiens
Manually annotated by BRENDA team
Hsiao, Y.P.; Huang, H.L.; Lai, W.W.; Chung, J.G.; Yang, J.H.
Antiproliferative effects of lactic acid via the induction of apoptosis and cell cycle arrest in a human keratinocyte cell line (HaCaT)
J. Dermatol. Sci.
54
175-184
2009
Homo sapiens
Manually annotated by BRENDA team
Sharma, S.; Ravichandran, V.; Jain, P.K.; Mourya, V.K.; Agrawal, R.K.
Prediction of caspase-3 inhibitory activity of 1,3-dioxo-4-methyl-2,3-dihydro-1h-pyrrolo[3,4-c] quinolines: QSAR study
J. Enzyme Inhib. Med. Chem.
23
424-431
2008
Homo sapiens
Manually annotated by BRENDA team
Parish, S.T.; Wu, J.E.; Effros, R.B.
Modulation of T lymphocyte replicative senescence via TNF-{alpha} inhibition: role of caspase-3
J. Immunol.
182
4237-4243
2009
Homo sapiens
Manually annotated by BRENDA team
Delloye-Bourgeois, C.; Brambilla, E.; Coissieux, M.M.; Guenebeaud, C.; Pedeux, R.; Firlej, V.; Cabon, F.; Brambilla, C.; Mehlen, P.; Bernet, A.
Interference with netrin-1 and tumor cell death in non-small cell lung cancer
J. Natl. Cancer Inst.
101
237-247
2009
Homo sapiens
Manually annotated by BRENDA team
Heo, S.K.; Yun, H.J.; Park, W.H.; Park, S.D.
Rhein inhibits TNF-alpha-induced human aortic smooth muscle cell proliferation via mitochondrial-dependent apoptosis
J. Vasc. Res.
46
375-386
2009
Homo sapiens
Manually annotated by BRENDA team
Gupta, S.; Agrawal, S.; Gollapudi, S.
Differential effect of human herpesvirus 6A on cell division and apoptosis among naive and central and effector memory CD4+ and CD8+ T-cell subsets
J. Virol.
83
5442-5450
2009
Homo sapiens
Manually annotated by BRENDA team
Park, M.J.; Kwon, H.Y.; Lee, E.O.; Lee, H.J.; Ahn, K.S.; Kim, M.O.; Kim, C.H.; Ahn, K.S.; Kim, S.H.
DMNQ-S17 inhibits constitutive NF-kappaB activation leading to induction of apoptosis through the activation of caspase-3 in human myeloid leukemia U937 cells
Life Sci.
83
460-467
2008
Homo sapiens
Manually annotated by BRENDA team
Shen, L.; Zeng, S.; Chen, J.; Zhong, M.; Yang, H.; Yao, R.; Shen, H.
E1A inhibits the proliferation of human cervical cancer cells (HeLa cells) by apoptosis induction through activation of HER-2/Neu/caspase-3 pathway
Med. Oncol.
25
222-228
2008
Homo sapiens
Manually annotated by BRENDA team
Cheng, G.; Zhu, L.; Mahato, R.I.
Caspase-3 gene silencing for inhibiting apoptosis in insulinoma cells and human islets
Mol. Pharm.
5
1093-1102
2009
Homo sapiens
Manually annotated by BRENDA team
Du, Y.; Li, C.; Hu, W.W.; Song, Y.J.; Zhang, G.Y.
Neuroprotection of preconditioning against ischemic brain injury in rat hippocampus through inhibition of the assembly of GluR6-PSD95-mixed lineage kinase 3 signaling module via nuclear and non-nuclear pathways
Neuroscience
161
370-380
2009
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.W.; Lin, G.J.; Chia, W.T.; Lin, C.K.; Chuang, Y.P.; Sytwu, H.K.
Triptolide exerts anti-tumor effect on oral cancer and KB cells in vitro and in vivo
Oral Oncol.
45
562-568
2009
Homo sapiens
Manually annotated by BRENDA team
Azuma, H.; Yoshida, Y.; Paul, D.; Shinoda, S.; Tsukube, H.; Nagasaki, T.
Cytochrome c-binding "proteo-dendrimers" as new types of apoptosis inhibitors working in HeLa cell systems
Org. Biomol. Chem.
7
1700-1704
2009
Homo sapiens
Manually annotated by BRENDA team
Bondarava, M.; Li, T.; Endl, E.; Wehner, F.
alpha-ENaC is a functional element of the hypertonicity-induced cation channel in HepG2 cells and it mediates proliferation
Pflugers Arch.
458
675-687
2009
Homo sapiens
Manually annotated by BRENDA team
Kim, K.W.; Moretti, L.; Lu, B.
M867, a novel selective inhibitor of caspase-3 enhances cell death and extends tumor growth delay in irradiated lung cancer models
PLoS ONE
3
e2275
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Stegh, A.H.; Kesari, S.; Mahoney, J.E.; Jenq, H.T.; Forloney, K.L.; Protopopov, A.; Louis, D.N.; Chin, L.; DePinho, R.A.
Bcl2L12-mediated inhibition of effector caspase-3 and caspase-7 via distinct mechanisms in glioblastoma
Proc. Natl. Acad. Sci. USA
105
10703-10708
2008
Homo sapiens
Manually annotated by BRENDA team
Li, C.; Wu, Z.; Liu, M.; Pazgier, M.; Lu, W.
Chemically synthesized human survivin does not inhibit caspase-3
Protein Sci.
17
1624-1629
2008
Homo sapiens
Manually annotated by BRENDA team
Coiras, M.; Lopez-Huertas, M.R.; Mateos, E.; Alcami, J.
Caspase-3-mediated cleavage of p65/RelA results in a carboxy-terminal fragment that inhibits IkappaBalpha and enhances HIV-1 replication in human T lymphocytes
Retrovirology
5
109
2008
Homo sapiens
Manually annotated by BRENDA team
Chang, C.H.; Yu, F.Y.; Wang, L.T.; Lin, Y.S.; Liu, B.H.
Activation of ERK and JNK signaling pathways by mycotoxin citrinin in human cells
Toxicol. Appl. Pharmacol.
237
281-287
2009
Homo sapiens
Manually annotated by BRENDA team
Dia, V.P.; Mejia, E.G.
Lunasin promotes apoptosis in human colon cancer cells by mitochondrial pathway activation and induction of nuclear clusterin expression
Cancer Lett.
295
44-53
2010
Homo sapiens
Manually annotated by BRENDA team
Djordjevic, V.V.; Stojanovic, I.; Stankovic-Ferlez, D.; Ristic, T.; Lazarevic, D.; Cosic, V.; Djordjevic, V.B.
Plasma nitrite/nitrate concentrations in patients with schizophrenia
Clin. Chem. Lab. Med.
48
89-94
2010
Homo sapiens
Manually annotated by BRENDA team
Bagchi, P.; Dutta, D.; Chattopadhyay, S.; Mukherjee, A.; Halder, U.C.; Sarkar, S.; Kobayashi, N.; Komoto, S.; Taniguchi, K.; Chawla-Sarkar, M.
Rotavirus nonstructural protein 1 suppresses virus-induced cellular apoptosis to acilitate viral growth by activating the cell survival pathways during early stages of infection
J. Virol.
84
6834-6845
2010
Homo sapiens
Manually annotated by BRENDA team
Glazer, E.S.; Kaluarachchi, W.D.; Massey, K.L.; Zhu, C.; Curley, S.A.
Bioengineered arginase I increases caspase-3 expression of hepatocellular and pancreatic carcinoma cells despite induction of argininosuccinate synthetase-1
Surgery
148
310-318
2010
Homo sapiens
Manually annotated by BRENDA team
Fan, L.L.; Sun, G.P.; Wei, W.; Wang, Z.G.; Ge, L.; Fu, W.Z.; Wang, H.
Melatonin and doxorubicin synergistically induce cell apoptosis in human hepatoma cell lines
World J. Gastroenterol.
16
1473-1481
2010
Homo sapiens
Manually annotated by BRENDA team
Wang, Z.; Watt, W.; Brooks, N.A.; Harris, M.S.; Urban, J.; Boatman, D.; McMillan, M.; Kahn, M.; Heinrikson, R.L.; Finzel, B.C.; Wittwer, A.J.; Blinn, J.; Kamtekar, S.; Tomasselli, A.G.
Kinetic and structural characterization of caspase-3 and caspase-8 inhibition by a novel class of irreversible inhibitors
Biochim. Biophys. Acta
1804
1817-1831
2010
Homo sapiens
Manually annotated by BRENDA team
Jiang, Y.; Hansen, T.V.
Isatin 1,2,3-triazoles as potent inhibitors against caspase-3
Bioorg. Med. Chem. Lett.
21
1626-1629
2011
Homo sapiens
Manually annotated by BRENDA team
Luo, M.; Lu, Z.; Sun, H.; Yuan, K.; Zhang, Q.; Meng, S.; Wang, F.; Guo, H.; Ju, X.; Liu, Y.; Ye, T.; Lu, Z.; Zhai, Z.
Nuclear entry of active caspase-3 is facilitated by its p3-recognition-based specific cleavage activity
Cell Res.
20
211-222
2010
Homo sapiens
Manually annotated by BRENDA team
Wu, Y.; Wang, D.; Wang, X.; Wang, Y.; Ren, F.; Chang, D.; Chang, Z.; Jia, B.
Caspase 3 is activated through caspase 8 instead of caspase 9 during H2O2-induced apoptosis in HeLa cells
Cell. Physiol. Biochem.
27
539-546
2011
Homo sapiens
Manually annotated by BRENDA team
Edelmann, B.; Bertsch, U.; Tchikov, V.; Winoto-Morbach, S.; Perrotta, C.; Jakob, M.; Adam-Klages, S.; Kabelitz, D.; Schuetze, S.
Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes
EMBO J.
30
379-394
2011
Homo sapiens
Manually annotated by BRENDA team
Nakatsumi, H.; Yonehara, S.
Identification of functional regions defining different activity in caspase-3 and caspase-7 within cells
J. Biol. Chem.
285
25418-25425
2010
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Du, R.H.; Cui, J.T.; Wang, T.; Zhang, A.H.; Tan, R.X.
Trichothecin induces apoptosis of HepG2 cells via caspase-9 mediated activation of the mitochondrial death pathway
Toxicon
59
143-150
2012
Homo sapiens
Manually annotated by BRENDA team
Vickers, C.J.; Gonzalez-Paez, G.E.; Wolan, D.W.
Discovery of a highly selective caspase-3 substrate for imaging live cells
ACS Chem. Biol.
9
2199-2203
2014
Homo sapiens
Manually annotated by BRENDA team
Lee, G.H.; Lee, E.J.; Hah, S.S.
TAMRA- and Cy5-labeled probe for efficient kinetic characterization of caspase-3
Anal. Biochem.
446
22-24
2014
Homo sapiens
Manually annotated by BRENDA team
Kuboki, M.; Ito, A.; Simizu, S.; Umezawa, K.
Activation of apoptosis by caspase-3-dependent specific RelB cleavage in anticancer agent-treated cancer cells: involvement of positive feedback mechanism
Biochem. Biophys. Res. Commun.
456
810-814
2015
Homo sapiens
Manually annotated by BRENDA team
Liu, D.; Tian, Z.; Yan, Z.; Wu, L.; Ma, Y.; Wang, Q.; Liu, W.; Zhou, H.; Yang, C.
Design, synthesis and evaluation of 1,2-benzisothiazol-3-one derivatives as potent caspase-3 inhibitors
Bioorg. Med. Chem.
21
2960-2967
2013
Homo sapiens
Manually annotated by BRENDA team
Wu, L.; Lu, M.; Yan, Z.; Tang, X.; Sun, B.; Liu, W.; Zhou, H.; Yang, C.
1,2-benzisothiazol-3-one derivatives as a novel class of small-molecule caspase-3 inhibitors
Bioorg. Med. Chem.
22
2416-2426
2014
Homo sapiens
Manually annotated by BRENDA team
Li, Z.; Pan, Y.; Zhong, W.; Zhu, Y.; Zhao, Y.; Li, L.; Liu, W.; Zhou, H.; Yang, C.
Synthesis and evaluation of N-acyl-substituted 1,2-benzisothiazol-3-one derivatives as caspase-3 inhibitors
Bioorg. Med. Chem.
22
6735-6745
2014
Homo sapiens
Manually annotated by BRENDA team
Vickers, C.J.; Gonzalez-Paez, G.E.; Wolan, D.W.
Selective detection and inhibition of active caspase-3 in cells with optimized peptides
J. Am. Chem. Soc.
135
12869-12876
2013
Homo sapiens
Manually annotated by BRENDA team
Yun, N.; Lee, Y.M.; Kim, C.; Shibayama, H.; Tanimura, A.; Hamanaka, Y.; Kanakura, Y.; Park, I.S.; Jo, A.; Shin, J.H.; Ju, C.; Kim, W.K.; Oh, Y.J.
Anamorsin, a novel caspase-3 substrate in neurodegeneration
J. Biol. Chem.
289
22183-22195
2014
Homo sapiens
Manually annotated by BRENDA team
Samiulla, D.S.; Naidu, A.; Rao, G.V.; Ramachandra, M.
Discovery of indole tetrafluorophenoxymethylketone-based potent novel small molecule inhibitors of caspase-3
Org. Med. Chem. Lett.
2
27
2012
Homo sapiens
Manually annotated by BRENDA team
Eda, S.R.; Veeramachaneni, G.K.; Bondili, J.S.; Jinka, R.
Screening of caspase-3 inhibitors from natural molecule database using e-pharmacophore and docking studies
Bioinformation
15
240-245
2019
Homo sapiens (P42574)
Manually annotated by BRENDA team
Sandhu, P.; Naeem, M.M.; Lu, C.; Kumarathasan, P.; Gomes, J.; Basak, A.
Ser422 phosphorylation blocks human Tau cleavage by caspase-3 Biochemical implications to Alzheimers Disease
Bioorg. Med. Chem. Lett.
27
642-652
2017
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Lin, B.; Zhu, M.; Wang, W.; Li, W.; Dong, X.; Chen, Y.; Lu, Y.; Guo, J.; Li, M.
Structural basis for alpha fetoprotein-mediated inhibition of caspase-3 activity in hepatocellular carcinoma cells
Int. J. Cancer
141
1413-1421
2017
Homo sapiens (P42574), Homo sapiens
Manually annotated by BRENDA team
Tavari, M.; Malan, S.; Joubert, J.
Design, synthesis, biological evaluation and docking studies of sulfonyl isatin derivatives as monoamine oxidase and caspase-3 inhibitors
MedChemComm
7
1628-1639
2016
Homo sapiens (P42574)
-
Manually annotated by BRENDA team
Perez-Lopez, A.M.; Soria-Gila, M.L.; Marsden, E.R.; Lilienkampf, A.; Bradley, M.
Fluorogenic substrates for in situ monitoring of caspase-3 activity in live cells
PLoS ONE
11
e0153209
2016
Homo sapiens (P42574)
Manually annotated by BRENDA team
Smart, A.D.; Pache, R.A.; Thomsen, N.D.; Kortemme, T.; Davis, G.W.; Wells, J.A.
Engineering a light-activated caspase-3 for precise ablation of neurons in vivo
Proc. Natl. Acad. Sci. USA
114
E8174-E8183
2017
Homo sapiens (P20807), Homo sapiens
Manually annotated by BRENDA team