Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.22.56 - caspase-3 and Organism(s) Homo sapiens and UniProt Accession P20807

for references in articles please use BRENDA:EC3.4.22.56
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.56 caspase-3
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P20807 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
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
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-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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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-amido-4-trifluoromethylcoumarin + H2O
DEVD + 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
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-(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
-
-
-
?
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
-
-
?
SETbeta + H2O
?
show the reaction diagram
-
-
-
?
sterol regulatory element-binding protein + H2O
?
show the reaction diagram
-
cleavage site is DEPD-/-
-
-
?
tau protein + H2O
?
show the reaction diagram
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
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
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
-
-
?
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
-
-
?
topoisomerase I + H2O
?
show the reaction diagram
-
cleavage at DDVD146-/-Y and EEED170-/-G
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(3R)-3-ethyl-1-[methyl(octyl)amino]-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]octane-2,5-dione
-
50% inhibition at 9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[2-oxo-3-[(1,3-thiazol-5-ylmethyl)amino]pyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 12 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-(phenylsulfanyl)octane-2,5-dione
-
50% inhibition at 7.9 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-3-ethyl-6-[5-ethyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-1-[hexyl(methyl)amino]octane-2,5-dione
-
50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[hexyl(methyl)amino]octane-2,5-dione
-
i.e. M826, 50% inhibition at 6 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3R)-6-[5-tert-butyl-3-[[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino]-2-oxopyrazin-1(2H)-yl]-3-ethyl-1-[methyl(pentyl)amino]octane-2,5-dione
-
i.e. M867, 50% inhibition at 0.1 nM, reversible. Comparison with inhibition of caspase-1, caspase-7, caspase-8 and NT2 whole cells
(3S)-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-(benzylsulfanyl)-4-oxopentanoic acid
-
50% inhibition at 52 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[(2-[3-[(N-acetyl-L-alpha-aspartyl)amino]-2-oxopyridin-1(2H)-yl]butanoyl)amino]-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-4-oxopentanoic acid
-
50% inhibition at 0.3 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
-
-
(3S)-3-[[(2R)-2-[3-[(naphthalen-2-ylcarbonyl)amino]-2-oxopyridin-1(2H)-yl]-2-phenylacetyl]amino]-4-oxo-5-phenoxypentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-(benzylsulfanyl)-3-([N-[(2,5-dimethoxyphenyl)acetyl]-L-valyl]amino)-4-oxopentanoic acid
-
50% inhibition at 48 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-(benzylsulfanyl)-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 86 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
-
-
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
-
-
(3S)-5-[(2-chloro-6-fluorobenzyl)sulfanyl]-3-[(N-[[2-ethoxy-5-(2-methoxy-2-oxoethoxy)phenyl]acetyl]-L-valyl)amino]-4-oxopentanoic acid
-
50% inhibition at 53 nM. Comparison of inhibition with caspase 1, caspase 7, caspase 6 and with induction of apoptosis. Increase in stability of otherwise rapidly degraded enzyme heterotetramer
(4S,7S,10S,13S)-7-(2-carboxyethyl)-4-(carboxymethyl)-13-(cyclobutylcarbonyl)-10-(1-methylethyl)-2,5,8,11-tetraoxo-3,6,9,12-tetraazapentadecan-15-oic acid
-
non-preferred name, comparison with inhibition of caspase-7
(R)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
IC50: 0.018 mM
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 0.0055 mM
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 44 nM
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
-
-
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 4.2 nM
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 170 nM
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
IC50: 5.2 nM
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 4.6 nM
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 2.5 nM
(S)-1-butyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-ethyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-methyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 30 nM
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
-
-
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 3.1 nM
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
-
-
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
-
-
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
-
-
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
-
-
(S)-3-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyridin-2-ylmethyl]sulfamoyl]benzoic acid
-
-
(S)-3-[[6-(benzenesulfonylamino-methyl)pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-acetylsulfamoyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonyl-benzenesulfonylamino)-methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylamino-benzenesulfonylamino)methyl]pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(3-methanesulfonylaminocarbonyl-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxobutyric acid
-
-
(S)-3-[[6-[(4-hydroxy-benzenesulfonylamino)methyl]-pyridine-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-3-[[6-[(4-methanesulfonylamino-benzenesulfonylamino)methyl]pyridien-3-carbonyl]amino]-4-oxo-butyric acid
-
-
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-4-oxo-3-[[6-[[3-(1H-tetrazol-5-yl)benzenesulfonylamino]methyl]pyridine-3-carbonyl]amino]butyric acid
-
-
(S)-4-oxo-3-[[6-[[3-(5-oxo-4,5-dihydro[1,2,4]oxadiazol-3-yl)benzenesulfonylamino]methyl]pyridien-3-carbonyl]amino]butyric acid
-
-
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
-
-
(S)-4-[[4-(hydroxy-3-methyl-benzenesulfonylamino)methyl]thiophene]-2-carboxylic acid [3-(2-chloro-benzylsulfanyl)-1-ethyl-2-oxo-propyl]amide
-
-
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
IC50: 120 nM
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
-
-
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
-
-
(S)-5-[1-[(2-methoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 170 nM
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 70 nM
(S)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 31 nM
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
IC50: 44 nM
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
IC50: 140 nM
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
IC50: 410 nM
(S)-5-[[3-(1-carboxymethyl-2-oxo-ethylcarbamoyl)isooxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[3-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]isoxazol-5-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[4-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-4-methyl-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)-thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-2-oxo-ethylcarbamoyl)pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxybenzoic acid
-
-
(S)-5-[[5-(1-carboxymethyl-3-methylsulfanyl-2-oxo-propylcarbamoyl)pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-3-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-2-oxo-3-(pyridin-4-ylmethylsulfanyl)propylcarbamoyl]thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]-4-methyl-thiophen-2-ylmethyl]-sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]furan-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrazin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyridin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]pyrimidin-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiazol-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-3-(2-chloro-benzylsulfanyl)-2-oxo-propylcarbamoyl]thiophen-3-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
(S)-5-[[5-[1-carboxymethyl-5-(2-chloro-phenyl)-2-oxopentylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
1,2-benzisothiazol-3-one
-
-
1,2-butanedithiol
-
60% inhibition
1,4-dihydroxy-2-naphthoic acid
-
-
1-(3-oxo-1,2-benzothiazol-2(3H)-yl)-4-(thiophen-2-yl)butane-1,4-dione
-
-
1-methyl-5-nitro-1H-indole-2,3-dione
-
-
1-methyl-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-methyl-5-[[(3R)-3-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
i.e. GSK-31, inhibitory effect is greatest in presence of 2-mercaptoethanol and decreases 2fold by substitution of 2-mercaptoethanol with dithiothreitol
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
2,4-dimethyl-8-(morpholin-4-ylsulfonyl)-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
50% inhibition at 0.000044 mM
2-(1,3-dihydro-2-benzofuran-5-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-(2-hydroxyethyl)-4-methyl-8-[(4-methylpiperidin-1-yl)sulfonyl]-1H-pyrrolo[3,4-c]quinoline-1,3(2H)-dione
-
i.e. CD-001-0011, 50% inhibition at 130 nM, reversible, inhibitory effect is greatest in presence of dithiothreitol and decreases 3-4fold by substitution of dithiothreitol with 2-mercaptoethanol
2-(2-phenylethyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(1H-pyrrol-1-yl)phenyl]acetamide
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(piperidin-1-yl)phenyl]acetamide
-
-
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(pyridin-2-yl)phenyl]acetamide
-
-
2-(3-phenylpropanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-fluorobenzyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-methoxybenzyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-methylphenyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(4-phenylbutanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(5-phenylpentanoyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(biphenyl-4-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-(naphthalen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(phenylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-(prop-2-en-1-yl)-1,2-benzothiazol-3(2H)-one
-
-
2-(thiophen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
-
-
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-benzyl-1,2-benzothiazol-3(2H)-one
-
-
2-chloro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)acetamide
-
50% inhibition at 92 nM
2-ethyl-1,2-benzothiazol-3(2H)-one
-
-
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)benzamide
-
50% inhibition at 96 nM
2-methoxy-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 103 nM
2-methyl-1,2-benzothiazol-3(2H)-one
-
-
2-nitro-N-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)benzamide
-
50% inhibition at 62 nM
2-phenyl-1,2-benzothiazol-3(2H)-one
-
-
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(2-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(2-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(2-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3,4-dichlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(3-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(3-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-hydroxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
-
-
2-[(4-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[(4-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(2-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(3-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
most potent inhibitor
2-[3-(4-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[3-(trifluoromethyl)phenyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(4-methoxyphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(4-methylphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
2-[4-(thiophen-2-yl)butanoyl]-1,2-benzothiazol-3(2H)-one
-
-
3,3-dimethyl-8-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-3,4-dihydropyrimido[1,2-a]indol-10(2H)-one
-
-
3-({2-[5-tert-butyl-3-{[(4-methyl-1,2,5-oxadiazol-3-yl)methyl]amino}-2-oxopyrazin-1(2H)-yl]butanoyl}amino)-5-[methyl(pentyl)amino]-4-oxopentanoic acid
-
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-[1-(azetidinyl)sulfonyl]isatin
IC50: 170 nM
5-[1-(hexamethyleneimino)sulfonyl]isatin
IC50: 0.0019 mM
5-[1-(piperidinyl)sulfonyl]isatin
IC50: 0.0022 mM
5-[1-(pyrrolidinyl)sulfonyl]isatin
IC50: 0.0028 mM
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-phenyl-1H-indole-2,3-dione
-
-
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
5-[[5-[1-carboxymethyl-2-(7-methyl-benzoxazol-2-yl)-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
5-[[5-[1-carboxymethyl-2-[5-(2,6-dichloro-phenyl)-oxazol-2-yl]-2-oxo-ethylcarbamoyl]thiophen-2-ylmethyl]sulfamoyl]-2-hydroxy-benzoic acid
-
-
6-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
-
-
8-[[(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
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-DQMD-CHO
-
Ac-DQVD-aldehyde
-
Ac-DW3-KE
-
-
-
Ac-F-D-beta-hLeu-hLeu-D-KE
-
-
Ac-IEPD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-WEHD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
Ac-YVAD-CHO
a reversible aldehyde caspase-3 inhibitor, bound in extended conformation in the S1-S4 substrate binding sites of caspase-3, binding structure with hydrogen bond and ionic interactions, overview
acetyl-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-Val-Asp-Val-Ala-Asp-aldehyde
-
acetyl-WEHD-aldehyde
-
-
acetyl-YVAD-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
-
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
Boc-D(OMe)-fluoromethyl ketone
a pan-caspase irreversible inhibitor
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(O-Me) fluoromethyl ketone
-
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-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
-
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[2-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[3-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(1,3-dioxolan-2-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-yl)benzyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-yl)phenyl]-2-(3-oxo-1,2-benzothiazol-2(3H)-yl)acetamide
-
-
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
-
-
peroxynitrite
-
0.01 mM, 50% inhibition
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
-
-
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
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
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
-
-
Mch4
activation of CPP32
-
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
0.0016
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
0.067
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
0.2
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
0.002 - 0.0255
benzoyl-L-Asp-L-Glu-L-Val-L-Asp-7-amido-4-methylcoumarin
0.0625
DEVD-4-nitroanilide
-
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
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
additional information
additional information
-
stopped-flow and steady-state kinetic kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.1 - 14
acetyl-DEVD-7-amido-4-methylcoumarin
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
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
0.000165
(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
-
-
0.012
(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
0.00016
(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
0.00006
(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
0.00016
(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
0.0014
5-[1-(pyrrolidinyl)sulfonyl]isatin
pH 7.5, 30°C
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
0.0000013 - 0.0058
Acetyl-Asp-Glu-Val-Asp-aldehyde
0.0000124
acetyl-Asp-Met-Gln-Asp-aldehyde
pH 7.5, 22°C
0.00000023 - 0.0008
acetyl-DEVD-aldehyde
0.000195
acetyl-IETD-aldehyde
-
pH 7.5, 25°C
0.0000065
acetyl-Val-Asp-Val-Ala-Asp-aldehyde
pH 7.5, 22°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
0.0142
(3S)-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00066
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(2-phenylethyl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00681
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-(pyridin-3-yl)-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00524
(3S)-3-([[2-(3-carboxypropyl)-1,3-dioxo-8-[2-[(thiophen-2-ylacetyl)amino]ethyl]-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00505
(3S)-3-([[2-(3-carboxypropyl)-8-(2-[[(4-chlorophenyl)acetyl]amino]ethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0172
(3S)-3-([[2-[2-[(1H-benzimidazol-6-ylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.00754
(3S)-3-([[2-[2-[(cyclohexylcarbonyl)amino]ethyl]-7-(cyclohexylmethyl)-1,3-dioxo-2,3,5,8-tetrahydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-5-yl]carbonyl]amino)-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0134
(3S)-3-[[(2-[4-carboxy-2-[(phenylacetyl)amino]butyl]-1,3-dioxo-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl)carbonyl]amino]-5-[(2,6-dichlorobenzoyl)oxy]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0084
(3S)-5-(2,6-difluorophenoxy)-3-([[(2-methoxyphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0252
(3S)-5-(2,6-difluorophenoxy)-3-([[(3-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00967
(3S)-5-(2,6-difluorophenoxy)-3-([[(4-methylphenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00347
(3S)-5-fluoro-3-([[(4-fluorophenyl)amino](oxo)acetyl]amino)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00203
(3S)-5-[(2,6-dichlorobenzoyl)oxy]-3-[([1,3-dioxo-2-[2-(1H-tetrazol-5-yl)ethyl]-2,3,5,7,8,9,10,10a-octahydro-1H-[1,2,4]triazolo[1,2-a]cinnolin-5-yl]carbonyl)amino]-4-oxopentanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.018
(R)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 0.018 mM
0.0055
(R)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 0.0055 mM
0.000044
(S)-(+)-5-[1-[2-(thiophenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.000017
(S)-1-((1-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-1H-1,2,3-triazol-4-yl)methyl)-5-((2-(methoxymethyl)pyrrolidin-1-yl)sulfonyl)indoline-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000066
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0005
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00184
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000133
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00009
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000025
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00512
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000078
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000041
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00003
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000042
(S)-1-(4-pyridinylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 4.2 nM
0.00017
(S)-1-(carboxymethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.0000052
(S)-1-(cyclohexylmethyl)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonal]isatin
Homo sapiens
IC50: 5.2 nM
0.0000046
(S)-1-allyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 4.6 nM
0.0000025
(S)-1-benzyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 2.5 nM
0.000029
(S)-1-butyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000183
(S)-1-ethyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.0000024
(S)-1-methyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00003
(S)-1-methyl-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 30 nM
0.0000053
(S)-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-isatin
Homo sapiens
-
37°C
0.0000031
(S)-1-[(tert-butyloxycarbonyl)methyl]-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 3.1 nM
0.1
(S)-1-[3-(3-fluoropropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
above, 37°C
0.0609
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.00943
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
Homo sapiens
-
37°C
0.0068
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
37°C
0.1
(S)-3,3-difluoro-1-propyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
above, 37°C
0.000043
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.1
(S)-3-[3-[5-(1-(2-methoxymethylpyrrolidinyl)sulfonyl)-2,3-dioxoindolin-1-yl]propoxy]-propyl methanesulfonate
Homo sapiens
-
above, 37°C
0.000187
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
Homo sapiens
-
37°C
0.00023
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
Homo sapiens
-
37°C
0.000191
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000082
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
37°C
0.000056
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
Homo sapiens
-
37°C
0.00012
(S)-5-[1-(2-methoxymethyl)pyrrolidinylsulfonyl]isatin
Homo sapiens
IC50: 120 nM
0.000359
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
Homo sapiens
-
37°C
0.000083
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
Homo sapiens
-
37°C
0.000213
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
Homo sapiens
-
37°C
0.00017
(S)-5-[1-[(2-methoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.00007
(S)-5-[1-[(2-tert-butoxycarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 70 nM
0.000031
(S)-5-[1-[2-(anilinomethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 31 nM
0.000044
(S)-5-[1-[2-(phenoxymethyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 44 nM
0.00014
(S)-5-[1-[2-(phenylaminocarbonyl)pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 140 nM
0.00041
(S)-5-[1-[[2-(dimethylamino)carbonyl]pyrrolidinyl]sulfonyl]isatin
Homo sapiens
IC50: 410 nM
0.04674
1,2-benzisothiazol-3-one
Homo sapiens
-
at pH 7.5 and 22°C
0.000245
1-(3-oxo-1,2-benzothiazol-2(3H)-yl)-4-(thiophen-2-yl)butane-1,4-dione
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001
1-methyl-5-nitro-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(2,3-dihydro-1,4-benzodioxin-6-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0000167
1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000023
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-4-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000136
1-[[1-(biphenyl-4-yl)-1H-1,2,3-triazol-5-yl]methyl]-5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.0002217
2-(1,3-dihydro-2-benzofuran-5-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000203
2-(2,6-dihydroxyphenyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.01855
2-(2-phenylethyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.000729
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(1H-pyrrol-1-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000501
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-[4-(pyridin-2-yl)phenyl]acetamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001084
2-(3-phenylpropanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.01364
2-(4-fluorobenzyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.01209
2-(4-methoxybenzyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0004657
2-(4-methylphenyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0001816
2-(4-phenylbutanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003061
2-(5-phenylpentanoyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5,temperature not specified in the publication
0.0001406
2-(biphenyl-4-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000008
2-(chloroacetyl)-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002646
2-(naphthalen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002921
2-(phenylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.02272
2-(prop-2-en-1-yl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0322
2-(thiophen-2-ylacetyl)-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000622
2-amino-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0108
2-benzyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.09124
2-ethyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.04239
2-methyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.0005328
2-phenyl-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5 and 22°C
0.00000019
2-[(2,6-dihydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001926
2-[(2-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001857
2-[(2-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000000425
2-[(2-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002186
2-[(2-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001999
2-[(2-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0006543
2-[(3,4-dichlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000263
2-[(3,5-diamino-4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.0002719
2-[(3-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.008985
2-[(3-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000548
2-[(3-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003392
2-[(3-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002151
2-[(4-chlorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.001196
2-[(4-fluorophenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003263
2-[(4-hydroxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000033
2-[(4-hydroxyphenyl)amino]-4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.001344
2-[(4-methoxyphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002143
2-[(4-methylphenyl)acetyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000473
2-[3-(2-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001297
2-[3-(2-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001357
2-[3-(2-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000877
2-[3-(3-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000349
2-[3-(3-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000095
2-[3-(3-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000569
2-[3-(4-chlorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001116
2-[3-(4-fluorophenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000497
2-[3-(4-methoxyphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000119
2-[3-(4-methylphenyl)propanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0003897
2-[4-(4-methoxyphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002659
2-[4-(4-methylphenyl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001266
2-[4-(thiophen-2-yl)butanoyl]-1,2-benzothiazol-3(2H)-one
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000085
3-oxo-N-(1-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.000031
3-oxo-N-(2-phenylethyl)-1,2-benzothiazole-2(3H)-carboxamide
0.00004904
3-oxo-N-(3-phenylpropyl)-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.000076
3-oxo-N-phenyl-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.00004939
3-oxo-N-[2-(pyridin-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00003105
3-oxo-N-[2-(thiophen-2-yl)ethyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00009792
3-oxo-N-[4-(piperidin-1-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000221
3-oxo-N-[4-(pyridin-2-yl)phenyl]-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00082
3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000988
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0012
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00058
3-[[(5-bromo-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00011
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0208
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-(2,6-difluorophenoxy)-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00035
3-[[(5-chloro-1H-indol-1-yl)acetyl]amino]-5-fluoro-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00084
3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00111
3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxo-5-(2,3,5,6-tetrafluorophenoxy)pentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.000000228
4-methyl-2-(1-methylethyl)-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000324
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(1,3-thiazol-2-yl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000446
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(2,4,6-trihydroxyphenyl)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000124
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-(phenylamino)-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.000000243
4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-2-[(2,4,6-trihydroxyphenyl)amino]-1H-cyclopenta[c]quinoline-1,3(2H)-dione
Homo sapiens
-
-
0.00000161
4-[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl]benzoic acid
Homo sapiens
-
-
0.00913
4-[5-([(3S)-1-[(2,6-dichlorobenzoyl)oxy]-2,5-dioxohexan-3-yl]carbamoyl)-1,3-dioxo-8-(thiophen-2-yl)-5,8-dihydro-1H-[1,2,4]triazolo[1,2-a]pyridazin-2(3H)-yl]butanoic acid
Homo sapiens
-
pH 7.5, 25°C
0.0025
5-(2,6-difluorophenoxy)-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0257
5-(2,6-difluorophenoxy)-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0471
5-(2,6-difluorophenoxy)-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.0000005
5-([(2R)-2-[(2,4-difluorophenoxy)methyl]pyrrolidin-1-yl]sulfonyl)-1-[[1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00123
5-fluoro-3-[[(2-methyl-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00112
5-fluoro-3-[[(5-fluoro-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00129
5-fluoro-3-[[(5-methoxy-1H-indol-1-yl)acetyl]amino]-4-oxopentanoic acid
Homo sapiens
-
at pH 7.4 and 30°C
0.00017
5-[1-(azetidinyl)sulfonyl]isatin
Homo sapiens
IC50: 170 nM
0.0019
5-[1-(hexamethyleneimino)sulfonyl]isatin
Homo sapiens
IC50: 0.0019 mM
0.0022
5-[1-(piperidinyl)sulfonyl]isatin
Homo sapiens
IC50: 0.0022 mM
0.0028
5-[1-(pyrrolidinyl)sulfonyl]isatin
Homo sapiens
IC50: 0.0028 mM
0.000018
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-4-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000267
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-([1-[4-(trifluoromethyl)phenyl]-1H-1,2,3-triazol-5-yl]methyl)-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00003
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000009
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenoxy-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-4-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000103
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[(1-phenyl-1H-1,2,3-triazol-5-yl)methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000243
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-4-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000207
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[2-(1-phenyl-1H-1,2,3-triazol-5-yl)ethyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00007
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-methoxyphenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000021
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-4-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000213
5-[[(2R)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1-[[1-(4-nitrophenyl)-1H-1,2,3-triazol-5-yl]methyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
5-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.000044
5-[[(2S)-2-(phenoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
pH and temperature not specified in the publication
0.00012
6-[[(2S)-2-(methoxymethyl)pyrrolidin-1-yl]sulfonyl]-1H-indole-2,3-dione
Homo sapiens
-
37°C
0.0000068
Ac-CV3-KE
Homo sapiens
-
at pH 7.4 and 22°C
0.0000012
Ac-DEVD-CHO
Homo sapiens
-
0.000012
Ac-DMQD-CHO
Homo sapiens
-
0.01
Ac-DW3-KE
Homo sapiens
-
at pH 7.4 and 22°C
-
0.000012
Ac-F-D-beta-hLeu-hLeu-D-KE
Homo sapiens
-
at pH 7.4 and 22°C
0.0012
Ac-IEPD-CHO
Homo sapiens
-
0.0019
Ac-WEHD-CHO
Homo sapiens
-
0.01
Ac-YVAD-CHO
Homo sapiens
-
0.000001
Asp-Glu-Val-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 1 nM
0.0000047
Asp-Phe-Leu-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 4.7 nM
0.000074
baculovirus p35
Homo sapiens
-
IC50 for membrane enzyme: 0.074 nM
-
0.000012
carbobenzyloxy-DEVD-fluoromethyl ketone
Homo sapiens
-
-
0.0136
CS4566
Homo sapiens
-
-
0.000027
FAM-Ahx2-CV3-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000018
FAM-DEVD-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000035
IDN6556
Homo sapiens
-
at pH 7.4 and 30°C
0.00003
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
0.04
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethyl ketone
Homo sapiens
pH 7.4, 37°C
0.04474
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.06096
N-[(2-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.05149
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-1-(prop-2-yn-1-yl)-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.02508
N-[(3-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.6
0.02926
N-[(4-fluorophenyl)methyl]-N-methyl-2,3-dioxo-2,3-dihydro-1H-indole-5-sulfonamide
Homo sapiens
37°C, pH 7.4
0.01356
N-[2-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0002697
N-[2-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0001808
N-[3-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.0000555
N-[3-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00006201
N-[4-(4-methylpiperazin-1-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00005685
N-[4-(morpholin-4-yl)benzyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00000115 - 0.0001063
N-[4-(morpholin-4-yl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
0.0007834
N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.02205
N-[4-chloro-3-(trifluoromethyl)phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5 and 22°C
0.0000606
N-[4-[(4-methylpiperazin-1-yl)sulfonyl]phenyl]-3-oxo-1,2-benzothiazole-2(3H)-carboxamide
Homo sapiens
-
at pH 7.5, temperature not specified in the publication
0.00001
Rho-DEVD-AOMK
Homo sapiens
-
at pH 7.4 and 22°C
0.000034
Val-Glu-Ile-Asp-aldehyde
Homo sapiens
-
IC50 for membrane enzyme: 34 nM
0.000000008
[4-methyl-8-[(2-nitropyrrolidin-1-yl)sulfonyl]-1,3-dioxo-2,3-dihydro-1H-cyclopenta[c]quinolin-2-yl](oxo)acetyl chloride
Homo sapiens
-
-
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
-
SwissProt
Manually annotated by BRENDA team
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
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?
CAN3_HUMAN
821
0
94254
Swiss-Prot
-
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
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
homodimer
-
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
-
caspase-3 is S-nitrosylated under basal conditions to prevent activation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C143A
-
inactive enzyme. Catalytically inactive p17 polypeptide is expressed in a stable manner, while wild-type p17 is rapidly degraded
D179A
increase both in kcat- and KM-value. D179 is involved in substrate recognition
DELTA176-181
decrease both in kcat- and KM-value
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
Ni-NTA agarose column chromatography and Resource Q column chromatography
-
recombinant enzyme from Escherichia coli by nickel affinity chromatography, ion exchange chromatography, and gel filtration
recombinant enzyme, inclusion bodies produced in Escherichia coli
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
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
CASP3, expression analysis in melanoma cells
-
caspase-3 expression analysis
-
caspase-3 expression analysis in CLL cells
-
expressed in Escherichia coli Transetta (DE3) cells
-
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
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
-
the full-length caspase-3 gene containing an N-terminal 6His-tag is expressed in Escherichia coli
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
medicine
light-activated caspase-3 can be used for precise ablation of neurons in vivo
analysis
diagnostics
drug development
medicine
-
in macrophages from arteriosclerotic carotid artery, presence of proapoptotic markers such as enzyme, poly(ADP-ribose) polymerase, apoptosis-inducing factor, c-Jun/AP-1, and proinflammatory markers such as macrophage migration inhibitory factor and cyclooxygenase-2. Colocalization of proapoptic markers and proinflammatory markers and oxidized low-density lipoproteins
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