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Information on EC 3.4.22.60 - caspase-7 and Organism(s) Homo sapiens and UniProt Accession P55210
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3.4.22.60 caspase-7Specify your search results
Word Map
- 3.4.22.60
- caspase-3
- bcl-2
- parp
-
anti-apoptotic
-
pro-apoptotic
-
executioner
- necrosis
-
polyadp-ribose
-
caspase-dependent
-
annexin
-
tunel
- survivin
- cyclin
-
apoptosis-inducing
- adp-ribose
-
apoptosis-related
- bid
- xiap
- calpains
-
pan-caspase
- jnk
- cdk2
-
hoechst
-
caspase-mediated
-
antiproliferative
- apaf-1
- z-vad-fmk
-
caspase-3-like
-
pyroptosis
- ac-devd-cho
- apoptosome
-
template-based
- puma
-
trail-induced
- devd
-
caspase-3-deficient
-
mitochondria-dependent
-
procaspase
-
apoptosis-associated
- molecular biology
- casp10
-
spinocerebellar
-
sub-g1
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/-
Synonyms
caspase-7, caspase 7, casp7, sca-2, cmh-1, casp-7, ice-lap3, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apoptotic protease Mch-3
-
-
-
-
C14.004
-
-
-
-
caspase 7
CMH-1
-
-
-
-
ICE-LAP3
-
-
-
-
ICE-like apoptotic protease 3
-
-
-
-
LICE2 cysteine protease
-
-
-
-
SCA-2
-
-
-
-
SREBP cleavage activity 2
-
-
-
-
additional information
-
caspase-7 is a member of the caspase family of cysteine proteases
caspase 7
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/-
catalytic mechanism of caspase-7 consisting of three distinct kinetic steps leading to the protonation of the catalytic His144 and the deprotonation of Cys186, which is activated as a nucleophile, DFT computational investigation using crystal structure with PDB code 1FIJ, the catalytic dyad is formed by His144 and Cys186, existence of an alternative reaction channel leading directly from the initial complex to the peptide bond cleavage in a single kinetic step, detailed overview. The reaction pathway is characterized by a high energy barrier
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
189258-14-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
?
Ac-VEID-7-amido-4-methylcoumarin + H2O
Ac-VEID + 7-amino-4-methylcoumarin
-
-
-
?
DEVD-7-amido-4-methylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-fluoromethylcoumarin
-
-
-
?
N-acetyl-DEVD-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-DEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
N-acetyl-PEVD-7-amido-4-trifluoromethylcoumarin + H2O
acetyl-PEVD + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
poly(ADP ribose) polymerase 1 + H2O
?
better substrate for caspase-7 than caspase-3, PARP-1 is cleaved at the canonical caspase-3/7 site DEVD*G
-
-
?
26S proteasome subunit + H2O
?
-
during apoptosis, the activated caspase-7 directly cleaves certain subunits of 26S proteasomes, which then result in a decline in the proteasomal activity
-
-
?
Ac-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
Ac-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
a caspase-3 substrate
-
-
?
Ac-DEVD-7-amido-4-methylcoumarin + H2O
Ac-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-DQTD-7-amido-4-methylcoumarin + H2O
Ac-DQTD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
-
-
-
?
acetyl-DEVD-7-amido-4-fluoromethylcoumarin + H2O
acetyl-DEVD + 7-amino-4-fluoromethylcoumarin
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
acetyl-DEVD + 7-amino-4-methylcoumarin
-
iDEVD s the optimal tetrapeptide recognition motif
-
-
?
claspin + H2O
?
-
cleaved by caspase-7 during the initiation of apoptosis, cleavage at a single aspartate residue into a large N-terminal fragment and a smaller C-terminal fragment that contain different functional domains
-
-
?
DEVD-7-amido-4-trifluoromethylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
human telomerase + H2O
?
-
caspase-7 cleaves human telomerase, hTERT, at residues E286 and D628, generation of three major proteolytic fragments, cleavage site determination using caspase-7 resistant substrate mutants D129A, D637A, and D129A/D637A, overview
-
-
?
inhibitor of caspase-actived DNase + H2O
?
-
human caspase-7 is less efficient than caspase-3 at cleaving
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide + H2O
N-acetyl-Asp-Glu-Val-Asp + p-nitroaniline
-
-
-
-
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
-
-
-
?
pLyn-yellow-fluorescent protein-DEVD-DEVD-C fluorescent protein + H2O
pLyn-yellow-fluorescent protein-DEVD + DEVD-cyan fluorescent protein
-
-
-
-
?
tumor necrosis factor receptor-I + H2O
?
-
mutation E260Q of tumor necrosis factor receptor-I is sufficient to prevent cleavage
-
-
?
p23 + H2O
?
better substrate for caspase-7 than caspase-3. p23 is cleaved at site PEVD*G
-
-
?
p23 + H2O
?
i.e. Hsp90 cochaperone p23. Residues 36-45 of caspase-7 participate in p23 recognition. The caspase-7 N-terminal domain binds close to the cleavage site in the C-terminal tail of p23, and cleavage occurs at residues PEVD142-G bearing a P4 Pro residue
-
-
?
poly(ADP-ribose) polymerase + H2O
?
the cleavage of poly(ADP-ribose) polymerase observed during apoptosis cannot solely be attributed to CPP32 but can also be an activity of Mch2alpha
-
-
?
acid sphingomyelinase + H2O
?
-
caspase-7 activates acid sphingomyelinase induced by TNF, overview. Generation of the active 57 kDa fragment of endogenous A-SMase in wild-type HeLa cells. Direct association of caspase-7 and A-SMase within TNF receptosomes
-
-
?
acid sphingomyelinase + H2O
?
-
A-SMase, caspase-7 activates acid sphingomyelinase induced by TNF, overview
-
-
?
acid sphingomyelinase + H2O
?
-
acid sphingomyelinase, i.e. A-SMase, free or as fusion protein A-SMase-EGFP, a glycosylated protein, caspase-7 activates A-SMase induced by TNF, overview
-
-
?
ataxin-7 + H2O
?
-
ataxin-7 is cleaved by caspase-7, cleavage sites to Asp residues at positions 266 and 344 of the ataxin-7 protein. Proteolytic processing of ataxin-7 by caspase-7 may contribute to SCA7 disease pathogenesis
-
-
?
ataxin-7 + H2O
?
-
ataxin-7 is cleaved by caspase-7, cleavage sites to Asp residues at positions 266 and 344 of the ataxin-7 protein
-
-
?
caspase-7 biosensor vDEVDc + H2O
?
-
wild-type caspase-7 binds to caspase-7 biosensor vDEVDc, but does not cleave it, while an mutant isozymes of caspase-7 with the 24 or 56 N-terminal residues truncated, i.e. 24casp7 and 57casp7, respectively, cleave vDEVDc at the recognition sequence
-
-
?
caspase-7 biosensor vDEVDc + H2O
?
-
wild-type caspase-7 binds to caspase-7 biosensor vDEVDc, but does not cleave it, while an mutant isozymes of caspase-7 with the 24 or 56 N-terminal residues truncated, i.e. 24casp7 and 57casp7, respectively, cleave vDEVDc at the recognition sequence. Computational modeling of the vDEVDc biosensor, overview
-
-
?
Kaposi sarcoma-associated herpesvirus ORF57 + H2O
?
-
a viral early protein essential for KSHV multiplication. Cleavage of wild-type or mutant D33A ORF57 by valproate-induced BCBL-1 cell extracts containing active caspases
-
-
?
Kaposi sarcoma-associated herpesvirus ORF57 + H2O
?
-
a viral early protein essential for KSHV multiplication, caspase-7 cleavage site is 30DETD33
-
-
?
kinectin + H2O
?
-
proteolytic cleavage of the 160000 Da enzyme form to a 120000 Da fragment
-
-
?
kinectin + H2O
?
-
kinectin is cleaved by caspase 7 during apoptosis induced by different stimuli. Kinectin functions as a membrane anchor for kinesin and may be relevant to the disruption of vesicle trafficking during apoptosis
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
-
i.e. Mst1. Caspase 7 preferentially activates c-Jun NH2-terminal kinase and p38 preferentially through 40000 Da cleaved forms of Mst1. The 40000 Da form of Mst1 selectively phosphorylates c-Jun NH2-terminal kinase and p38
-
-
?
PARP + H2O
?
-
cleaved by caspase-7 during the initiation of apoptosis, cleavage at a single aspartate residue into a large N-terminal fragment and a smaller C-terminal fragment that contains different functional domains
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
whereas caspase-7 can cleave poly(ADP-ribose) polymerase in vivo, a collaborating caspase facilitates access to poly(ADP-ribose) polymerase, possibly by enhancing nucear entry
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
whereas caspase-7 can cleave poly(ADP-ribose) polymerase in vivo, a collaborating caspase facilitates access to poly(ADP-ribose) polymerase, possibly by enhancing nuclear entry
-
-
?
poly-ADPribose polymerase 1 + H2O
poly-ADPribose polymerase 1 peptide fragments
-
-
i.e. c-PARP, frgaments of 24 and 89 kDa
-
?
poly-ADPribose polymerase 1 + H2O
poly-ADPribose polymerase 1 peptide fragments
-
i.e. PARP-1
i.e. c-PARP, frgaments of 24 and 89 kDa
-
?
valosin-containing protein + H2O
?
-
cleavage by caspase-7 during apoptosis
-
-
?
valosin-containing protein + H2O
?
-
i.e. VCP or transitional endoplasmic reticulum ATPase, recombinant His-tagged substrate expressed in MCF-7 cells, cleavage at both DELD307 and DELD580, no activity with substrate mutant D307A/D580A
-
-
?
viral nucleocapsid protein of transmissible gastroenteritis coronovirus + H2O
?
-
cleavage site VVPD359-/-
-
-
?
viral nucleocapsid protein of transmissible gastroenteritis coronovirus + H2O
?
-
cleavage site VVPD359-/-. Destruction of viral protein by the host cell death machinery
-
-
?
additional information
?
-
no cleavage of YVAD-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
no cleavage of interleukin 1beta precursor
-
-
?
additional information
?
-
the enzyme is activated during Fas- and tumor necrosis factor-induced apoptosis
-
-
?
additional information
?
-
no activity with N-acetyl-PEVD-7-amido-4-fluoromethylcoumarin
-
-
?
additional information
?
-
-
caspase-7 is the most downstream caspase, overexpression does not lead to the activation of other caspases
-
-
?
additional information
?
-
-
the enzyme is activated during Fas- and tumor necrosis factor-induced apoptosis
-
-
?
additional information
?
-
-
caspase-7 is an executioner protease in cellular apoptosis
-
-
?
additional information
?
-
-
caspase-7 is an important executioner caspase capable of conducting most of apoptotic program in cells
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis and glioblastoma, regulation, overview
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis in cancer cells
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-7 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
-
-
?
additional information
?
-
-
functions of caspase-7 during apoptosis, overview
-
-
?
additional information
?
-
-
hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-7 or caspase-3
-
-
?
additional information
?
-
-
inhibition of executioner caspase enzymatic activity by TLCK and TPCK in dying HL-60 cells is important in prevention of cell death
-
-
?
additional information
?
-
-
members of the caspase family of cysteine proteases play central roles in coordinating the stereotypical events that occur during apoptosis, the major executioner caspases are caspase-3 and caspase-7, which show overlapping substrate specificities, overview
-
-
?
additional information
?
-
-
possible involvement of caspase-7 in cell cycle progression at mitosis, caspases including caspase-3, caspase-7, caspase-8 and caspase-9, are activated during mitosis and are potentially involved in the regulation at M phase. Chemically synthesized caspase inhibitors delay mitotic progression and induce accumulation of mitotic cells, which exhibits abnormal chromatin condensation and incomplete chromosome segregation
-
-
?
additional information
?
-
-
tyrosine kinase TrkA overexpression induces substantial cell death even in the absence of NGF, by stimulating ERK phosphorylation and caspase-7 activation leading to PARP cleavage, mechanism, overview
-
-
?
additional information
?
-
-
caspase-7, like caspase-3, shows substrate specificity with special preference for the DEVD motif, peptide products, overview
-
-
?
additional information
?
-
-
no activity of mutant 57casp7 isozyme with control biosensor v4Gc
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
p23 + H2O
?
better substrate for caspase-7 than caspase-3. p23 is cleaved at site PEVD*G
-
-
?
poly(ADP ribose) polymerase 1 + H2O
?
better substrate for caspase-7 than caspase-3, PARP-1 is cleaved at the canonical caspase-3/7 site DEVD*G
-
-
?
poly(ADP-ribose) polymerase + H2O
?
the cleavage of poly(ADP-ribose) polymerase observed during apoptosis cannot solely be attributed to CPP32 but can also be an activity of Mch2alpha
-
-
?
26S proteasome subunit + H2O
?
-
during apoptosis, the activated caspase-7 directly cleaves certain subunits of 26S proteasomes, which then result in a decline in the proteasomal activity
-
-
?
acid sphingomyelinase + H2O
?
-
caspase-7 activates acid sphingomyelinase induced by TNF, overview. Generation of the active 57 kDa fragment of endogenous A-SMase in wild-type HeLa cells. Direct association of caspase-7 and A-SMase within TNF receptosomes
-
-
?
ataxin-7 + H2O
?
-
ataxin-7 is cleaved by caspase-7, cleavage sites to Asp residues at positions 266 and 344 of the ataxin-7 protein. Proteolytic processing of ataxin-7 by caspase-7 may contribute to SCA7 disease pathogenesis
-
-
?
caspase-7 biosensor vDEVDc + H2O
?
-
wild-type caspase-7 binds to caspase-7 biosensor vDEVDc, but does not cleave it, while an mutant isozymes of caspase-7 with the 24 or 56 N-terminal residues truncated, i.e. 24casp7 and 57casp7, respectively, cleave vDEVDc at the recognition sequence
-
-
?
Kaposi sarcoma-associated herpesvirus ORF57 + H2O
?
-
a viral early protein essential for KSHV multiplication. Cleavage of wild-type or mutant D33A ORF57 by valproate-induced BCBL-1 cell extracts containing active caspases
-
-
?
kinectin + H2O
?
-
kinectin is cleaved by caspase 7 during apoptosis induced by different stimuli. Kinectin functions as a membrane anchor for kinesin and may be relevant to the disruption of vesicle trafficking during apoptosis
-
-
?
mammalian sterile 20-like kinase 1 + H2O
?
-
i.e. Mst1. Caspase 7 preferentially activates c-Jun NH2-terminal kinase and p38 preferentially through 40000 Da cleaved forms of Mst1. The 40000 Da form of Mst1 selectively phosphorylates c-Jun NH2-terminal kinase and p38
-
-
?
poly-ADPribose polymerase 1 + H2O
poly-ADPribose polymerase 1 peptide fragments
-
-
i.e. c-PARP, frgaments of 24 and 89 kDa
-
?
valosin-containing protein + H2O
?
-
cleavage by caspase-7 during apoptosis
-
-
?
viral nucleocapsid protein of transmissible gastroenteritis coronovirus + H2O
?
-
cleavage site VVPD359-/-. Destruction of viral protein by the host cell death machinery
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
whereas caspase-7 can cleave poly(ADP-ribose) polymerase in vivo, a collaborating caspase facilitates access to poly(ADP-ribose) polymerase, possibly by enhancing nuclear entry
-
-
?
additional information
?
-
the enzyme is activated during Fas- and tumor necrosis factor-induced apoptosis
-
-
?
additional information
?
-
-
caspase-7 is the most downstream caspase, overexpression does not lead to the activation of other caspases
-
-
?
additional information
?
-
-
the enzyme is activated during Fas- and tumor necrosis factor-induced apoptosis
-
-
?
additional information
?
-
-
caspase-7 is an executioner protease in cellular apoptosis
-
-
?
additional information
?
-
-
caspase-7 is an important executioner caspase capable of conducting most of apoptotic program in cells
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis and glioblastoma, regulation, overview
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis in cancer cells
-
-
?
additional information
?
-
-
caspase-7 is involved in apoptosis. Follistatin-like 1, FSTL1, induces apoptosis in cancer cells and leads to activation of caspase-7 when transfected to ovarian or endometrial cancer or healthy cells, regulation, overview
-
-
?
additional information
?
-
-
functions of caspase-7 during apoptosis, overview
-
-
?
additional information
?
-
-
hypertonicity-induced cation channels, HICC, inhibition by flufenamate and silencing of alpha-ENaC increases the rate of apoptosis in HepG2 cells via activation of caspase-7 or caspase-3
-
-
?
additional information
?
-
-
inhibition of executioner caspase enzymatic activity by TLCK and TPCK in dying HL-60 cells is important in prevention of cell death
-
-
?
additional information
?
-
-
members of the caspase family of cysteine proteases play central roles in coordinating the stereotypical events that occur during apoptosis, the major executioner caspases are caspase-3 and caspase-7, which show overlapping substrate specificities, overview
-
-
?
additional information
?
-
-
possible involvement of caspase-7 in cell cycle progression at mitosis, caspases including caspase-3, caspase-7, caspase-8 and caspase-9, are activated during mitosis and are potentially involved in the regulation at M phase. Chemically synthesized caspase inhibitors delay mitotic progression and induce accumulation of mitotic cells, which exhibits abnormal chromatin condensation and incomplete chromosome segregation
-
-
?
additional information
?
-
-
tyrosine kinase TrkA overexpression induces substantial cell death even in the absence of NGF, by stimulating ERK phosphorylation and caspase-7 activation leading to PARP cleavage, mechanism, overview
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(S)-1-(3-chloro-2-hydroxypropyl)-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)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
-
-
(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)-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)-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
-
-
Bcl2L12
-
is a direct caspase-7-binding and inhibitory protein affecting effector caspase activation, knockdown of Bcl2L12 or to a lesser extent of XIAP and Bcl-2 results in enhanced caspase-7 activation, regulation, overview
-
ketonic peptides
-
in the straight-chain aliphatic series, increasing inhibition with increasing chain length, for the unsubstituted aromatic P1' inhibitors increasing potency with decreasing linker length
-
N-alpha-tosyl-L-lysyl-chloromethylketone
-
i.e. TLCK, substantially inhibits caspase-7 enzymatic DEVDase activity, but does not affect caspase-7 processing in cells exposed to pro-apoptotic inducing stimuli, irreversibly alkylates cysteine residues of the active site of cysteine proteases
N-tosyl-L-phenylalanyl-chloromethylketone
-
i.e. TPCK, enhances caspase-7 processing although it substantially inhibits caspase-7 enzymatic DEVDase activity in HL-60 cells exposed to various cell death inducing stimuli, irreversibly alkylates cysteine residues of the active site of cysteine proteases
Z-Val-Ala-Asp-fluoromethylketone
-
inhibits Enterovirus 70-induced apoptosis and virus release, but not intracellular viral production
additional information
-
KI-values higher than 0.01 mM are determined for acetyl-WEHD-aldehyde and acetyl-YVAD-aldehyde and cowpox serin CrmA
-
additional information
-
alphaB-crystallin specifically interacts with and inhibits caspase-3, but not caspase-7
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(4-methoxyphenyl)-4-(piperazin-1-yl)quinoline
-
9% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
2-(4-methoxyphenyl)-N-[2-(morpholin-4-yl)ethyl]quinolin-4-amine
-
4% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N'-[2-(4-ethylphenyl)quinolin-4-yl]-N,N-dimethylethane-1,2-diamine
-
17% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N'-[2-(4-ethylphenyl)quinolin-4-yl]-N,N-dimethylpropane-1,3-diamine
-
26% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N'-[2-(4-methoxyphenyl)quinolin-4-yl]-N,N-dimethylethane-1,2-diamine
-
123% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N'-[2-(4-methoxyphenyl)quinolin-4-yl]-N,N-dimethylpropane-1,3-diamine
-
117% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N,N-diethyl-N'-[2-(4-ethylphenyl)quinolin-4-yl]propane-1,3-diamine
-
24% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
N,N-diethyl-N'-[2-(4-methoxyphenyl)quinolin-4-yl]propane-1,3-diamine
-
124% stimulation of caspase-7 cleavage of TDP-43 at 0.01 mM
etoposide
-
procaspase-7 cleavage (= activation of caspase-7), which is abrogated in cells with ectopically expressed p53
additional information
-
procaspase-7 is physiologically cleaved and activated by caspase-2, optimal conditions, overview
-
additional information
-
tyrosine kinase TrkA activates caspase-7 in apoptosis
-
additional information
-
TNF-induced caspase-7 activation takes place exclusively within TNF receptosomes
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
binding between the mutant 24casp7 isozyme and the vDEVDc biosensor occurs exponentially
-
0.041
Ac-DEVD-7-amido-4-methylcoumarin
wild-type, pH not specified in the publication, temperature not specified in the publication
0.041
Ac-DEVD-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
0.0054
Ac-VEID-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
0.2
Ac-VEID-7-amido-4-methylcoumarin
wild-type, value above 0.2 mM, pH not specified in the publication, temperature not specified in the publication
0.0298
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K40A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0319
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
wild type enzyme, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0357
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K38A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0366
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K39A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0375
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme S37A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0478
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K41A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0687
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme D23A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.0848
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203, processed with thrombin
0.1193
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203
0.415
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200, processed with thrombin
0.9365
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
Ac-VEID-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
0.9
Ac-DEVD-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
2.4
Ac-DEVD-7-amido-4-methylcoumarin
wild-type, pH not specified in the publication, temperature not specified in the publication
2.9
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K40A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
3.4
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
wild type enzyme, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
3.9
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K39A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
4.1
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K41A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
4.3
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K38A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
4.4
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme S37A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
9.5
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme D23A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.008
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200
0.1
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203
1.9
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200, processed with thrombin
4.4
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203, processed with thrombin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
30
Ac-VEID-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
30
Ac-DEVD-7-amido-4-methylcoumarin
Y230V/W232Y/S234V/Q276D, pH not specified in the publication, temperature not specified in the publication
60
Ac-DEVD-7-amido-4-methylcoumarin
wild-type, pH not specified in the publication, temperature not specified in the publication
86
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K41A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
97
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K40A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
110
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K39A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
110
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
wild type enzyme, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
120
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme K38A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
120
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme S37A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
140
N-acetyl-DEVD-7-amido-4-fluoromethylcoumarin
mutant enzyme D23A, in 10 mM PIPES (pH 7.4), 100 mM NaCl, 10% sucrose (w/v), 0.1% CHAPS, 1 mM EDTA and 10 mM dithiothreitol, at 37°C
0.009
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200
0.83
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203
4.7
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and 195-200, processed with thrombin
51.7
N-acetyl-Asp-Glu-Val-Asp-p-nitroanilide
-
mutant protein with thrombin cleavage sites (LVPRGS) at residues 20-25 and inserted after Asp-203, processed with thrombin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.5
2-[(2-acetylphenyl)sulfanyl]benzoic acid
pH not specified in the publication, temperature not specified in the publication
0.667
[2-(phenylsulfanyl)phenyl]acetic acid
pH not specified in the publication, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.98
2-[(2-acetylphenyl)sulfanyl]benzoic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.637
[2-(phenylsulfanyl)phenyl]acetic acid
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.000111
(S)-1-(11,11-difluoroundecyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000266
(S)-1-(2-fluoroallyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.00294
(S)-1-(2-fluoroethyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000123
(S)-1-(3-chloro-2-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000079
(S)-1-(3-chloropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.0000068
(S)-1-(3-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.00144
(S)-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000052
(S)-1-(3-hydroxypropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000028
(S)-1-(4-fluorobutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000011
(S)-1-(4-hydroxybutyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.113
(S)-1-[3-(3-hydroxypropoxy)propyl]-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.0194
(S)-1-[3-[3-(2-fluoroethoxy)propoxy]propyl]-5-[1-(2-methoxymethylpyrrolidinyl)-sulfonyl]isatin
Homo sapiens
-
-
0.00564
(S)-3,3-difluoro-1-(3-fluoropropyl)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]indolin-2-one
Homo sapiens
-
-
0.000135
(S)-3,5-bis-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000129
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propanoic acid
Homo sapiens
-
-
0.000217
(S)-3-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]propyl methanesulfonate
Homo sapiens
-
-
0.000044
(S)-4-fluorobenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000011
(S)-4-trifluoromethylbenzyl-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]isatin
Homo sapiens
-
-
0.000029
(S)-4-[5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-2,3-dioxoindolin-1-yl]butyl 4-methyl-benzenesulfonate
Homo sapiens
-
-
0.00004
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,3,3-trifluoropropyl)isatin
Homo sapiens
-
-
0.000178
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(3,4,4-trifluorobut-3-enyl)isatin
Homo sapiens
-
-
0.0001
(S)-5-[1-(2-methoxymethylpyrrolidinyl)sulfonyl]-1-(4,4,4-trifluorobutyl)isatin
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
human caspase-7 is not a nuclear caspase removal of the N-peptide does not allow an active transport or accumulation of human caspase-7 in the nuclei
-
additional information
-
active caspase-7 colocalizes with internalized TNF-R1 receptosomes, molecular components of a potential signalling cascade from TNF-R1 to A-SMase via caspase-7 actually localize in the same subcellular compartment. Direct association of caspase-7 and A-SMase within TNF receptosomes
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
-
active caspase-7 colocalizes with internalized TNF-R1 receptosomes. TNF-induced caspase-7 activation takes place exclusively within TNF receptosomes
malfunction
-
deletion of caspase-7 inhibits TNF-induced cleavage and activation of A-SMase
malfunction
-
depletion of caspase-7 from the cytoplasmic extracts of valproate-induced BCBL-1 cells reduces the cleavage of ORF57, and inhibition of caspase-7 activity promotes the expression of ORF59
physiological function
-
caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 in the cytoplasm confers a cellular function against viral lytic gene expression. But only initiator caspase-8, EC 3.4.22.61, is triggered in BCBL-1 cells with lytic KSHV induction by valproate, along with cleavage of expressed ORF57. Caspase-7 is an essential caspase in the cleavage of KSHV ORF57 and plays a key role in ORF57 cleavage in BCBL-1 cells during KSHV lytic infection
physiological function
-
caspase-7 activation is sufficient to start apoptosis, but it requires mitochondrial contribution to fully commit
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CASP7_HUMAN
303
0
34277
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
2 * 35000, procaspase-7 C285A mutant, in the homodimeric procaspase-7 each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
-
caspase-7 domain organization comprising large and small subunit, and the prodomain, overview
additional information
2 * 35000, procaspase-7 C285A mutant, in the homodimeric procaspase-7 each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, SDS-PAGE
additional information
-
2 * 35000, procaspase-7 C285A mutant, in the homodimeric procaspase-7 each monomer is organized in two structured subdomains connected by partially flexible linkers, which asymmetrically occupy and block the central cavity, SDS-PAGE
additional information
it is proposed that the 22000 Da peptide and the 12000 Da peptide are two subunits of the enzyme
additional information
it is proposed that the 22000 Da peptide and the 12000 Da peptide are two subunits of the enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
proteolytic modification
Mch3alpha is made of two subunits derived from a precursor ProMch3alpha. Asp23 and Asp198 are the most likely processing sites. Bacterially expressed Mch3 has intrinsic autocatalytic and autoactivation activity
proteolytic modification
both Mch4 and the serine protease granzyme B cleave proMch3 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Mch3 is a target of mature protease in apoptotic cells
proteolytic modification
-
viral nucleocapsid protein of transmissible gastroenteritis coronavirus triggers the processing of procaspase 6 in human rectal tumor cell line HRT18jap1
proteolytic modification
-
the N-peptide of caspase-7 must be removed, probably be caspase-3, before efficient activation of the zymogen can occur in vivo. The N-peptide serves to physically sequester the caspase-7 zymogen in a cytosolic location that prevents access by upstream activators, caspase-8, caspase-9 and caspase-10
proteolytic modification
-
the 12000 Da and the 11000 Da polypeptides are generated by processing of the CMH-1 protein at Asp198-Ser199 and to a lesser extent at Asp206-Ala207
proteolytic modification
-
caspase-7 possesses two cleavage sites after Asp23 and Asp198
proteolytic modification
-
procaspase-7 is activated by processing to the mature caspase-7
proteolytic modification
-
procaspase-7 is cleaved at Asp198 and Asp206 and activated by caspase-2
proteolytic modification
-
the procaspase-7 is cleaved to active enzyme by eliminating the prodomain, blocked by inhibitor carbobenzyloxy-DEVD-fluoromethyl ketone
proteolytic modification
-
cleavage of procaspase-7 of 35 kDa to the active forms of 31 and 20 kDa, TNF-induced caspase-7 activation takes place exclusively within TNF receptosomes
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.9 A crystal structure of recombinant C285A procaspase, sitting drop vapor diffusion method
hanging drop method, crystal structures of caspase-7 are determined in complexes with six peptide analogs (acetyl-DMQD-CHO, acetyl-DQMD-CHO, acetyl-DNLD-CHO, acetyl-IEPD-CHO, acetyl-ESMD-CHO, acetyl-WEHD-CHO)
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C290N
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
D23A
the mutation shows increased catalytic activity but is unable to cleave PARP
G188L
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
G188P
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
R187M
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
Y223A
molecular dynamics simulation, changes in catalytic activity upon mutation are reflected in corresponding changes in the global dynamics
Y230V/W232Y/S234V/Q276D
variant closely micks the substrate specificty of caspase 6, but does not cleave lamin C, a known caspase-6-specific substrate
D198A
-
additionally, amino acid residues 20-25 are replaced with a thrombin cleavage site (LVPRGS) and a thrombin cleavage site (LVPRGS) is inserted between Asp-203 and Thr-204
D628A
-
site-directed mutagenesis, caspase-7 resistant mutant, retains telomerase activity
additional information
additional information
caspase-7 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7 activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
-
caspase-7 knockout by shRNA, generation of double knockdown cells lacking caspase-3 and caspase-7 activity. Generation of caspase-7-based chimeric constructs with various regions of caspase-3, EC 3.4.22.56
additional information
mutational analysis to introduce the specificity of caspase-6 into caspase-7. Substitution of substrate-contacting residues from caspase-6 into caspase-7 is ineffective, yielding an inactive enzyme, whereas saturation mutagenesis at these positions and selection by directed evolution produces active caspases. The structures of the evolved-specificity caspase-7 reveal alternate binding modes for the substrate, including reorganization of an active site loop
additional information
-
mutational analysis to introduce the specificity of caspase-6 into caspase-7. Substitution of substrate-contacting residues from caspase-6 into caspase-7 is ineffective, yielding an inactive enzyme, whereas saturation mutagenesis at these positions and selection by directed evolution produces active caspases. The structures of the evolved-specificity caspase-7 reveal alternate binding modes for the substrate, including reorganization of an active site loop
additional information
-
comparison of phenotypes of caspase-7 with caspase-3 deficient cells, overview
additional information
-
construction of two truncated mutant isozymes 24casp7 and 57casp7, which lack the first 24 and 57 amino acid residues, respectively, and thus the cleavage site at Asp23
additional information
-
knockdown of caspase-7 by using siRNAs results in the inhibition of Hep-G2 cell proliferation, but knockdown of other caspases does not show a significant effect on cell growth. The expression of His-tagged shRNA directed against caspase-7 induce the cell cycle arrest at mitosis, which is rescued by the re-expression of caspase-7 containing silent mutations at the target site for the shRNA
additional information
-
caspase cleavage site is substituted and a thrombin cleavage site inserted: amino acid residues 20-25 are replaced with a thrombin cleavage site (LVPRGS) and a thrombin cleavage site (LVPRGS) is inserted between Asp-203 and Thr-204
additional information
-
caspase cleavage sites are substituted: amino acid residues 20-25 and 195-200 are replaced with thrombin cleavage sites (LVPRGS)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by nickel affinity chromatography, anion exchange chromatography and gel filtration
-
partially purified X-linked inhibitor of apoptosis-caspase-7 complex by gel filtration and immunopurification, SDS-PAGE
-
recombinant C-terminally His-tagged caspase-7 from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant procaspase-2 from Escherichia coli strain BL21(DE3) by nickel affinity and ion exchange chromatography to over 95%
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
bacterially expressed Mch3 has intrinsic autocatalytic and autoactivation activity
expression of FLAG-tagged caspase-7 in DKD cells. Simultaneous expression of HA-procaspase-3, EC 3.4.22.56, and HA-procaspase-7 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 in Escherichia coli BL21 (DE3) transformed with a pET-21b plasmid expression vector
-
expression of C-terminally His-tagged caspase-7 in Escherichia coli strain BL21 (DE3)
-
quantitative expression analysis in several ovarian and endometrial cancer cell lines by RT-PCR
-
two truncated mutant isozymes 24casp7 and 57casp7 are cloned from a skeletal muscle cDNA library, expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
-
apoptosis is preceded by proteolytic cleavage of e.g. caspase 7, prolonged nuclear localization of activated signal transducer and activator of transcription 1 results in apoptosis involving specific regulation of caspase pathway
medicine
-
Actinobacillus actinomycetemcomitans cytolethal distending toxin acts as an immunosuppressive factor, it possesses the ability to induce human T-cell apoptosis through activation of caspase-7
medicine
-
acute hemorrhagic conjunctivitis, Enterovirus 70 infection induces caspase-7-mediated apoptosis
medicine
-
cleavage of claspin by caspase-7 inactivates the Chk1 signaling pathway, this mechanism may regulate the balance between cell cycle arrest and induction of apoptosis during response of genotoxic stress
medicine
-
hydrophobic P5 residue has a favorable contribution to the recognition and hydrolysis of substrates but not by caspase-7, this information helps to design specific inhibitors for each caspase
medicine
-
low-dosage topoisomerase II inhibitor etoposide effectively inhibits proliferation rate
medicine
-
strong correlation between caspase-7 activity, normal brain development, and apoptotic DNA fragmenation in Casp3-/-mice
medicine
-
substitution in the P1' position could be used in synergy with other elements to obtain highly potent and isozyme-selective caspase inhibitors
medicine
-
SUMO-1 modification in caspase-7 may contribute to the cleavage of nuclear substrates during neuronal apoptosis
medicine
-
caspase-7 may play a role in ataxin-7 proteolysis and pathology of spinocerebellar ataxia type 7. Inhibition of this protease may be therapeutically important
medicine
-
involvement of the CASP7 gene in the susceptibility to rheumatoid arthritis. The higher production of the no functional variant of CASP7 by individuals with a particular genotype could be the basis of this association
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Strausberg R.L.; Feingold E.A.; Grouse L.H.; Derge J.G.; et al.
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
Proc. Natl. Acad. Sci. USA
99
16899-16903
2002
Homo sapiens (P55210), Mus musculus (P97864)
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
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
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens
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
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 (P55210)
Eleouet, J.F.; Slee, E.A.; Saurini, F.; Castagne, N.; Poncet, D.; Garrido, C.; Solary, E.; Martin, S.J.
The viral nucleocapsid protein of transmissible gastroenteritis coronavirus (TGEV) is cleaved by caspase-6 and -7 during TGEV-induced apoptosis
J. Virol.
74
3975-3983
2000
Homo sapiens
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
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
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
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
Lippke, J.A.; Gu, Y.; Sarnecki, C.; Caron, P.R.; Su, M.S.S.
Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32
J. Biol. Chem.
271
1825-1828
1996
Homo sapiens (P55210)
Fernandes-Alnemri, T.; Takahashi, A.; Armstrong, R.C.; Krebs, J.; Fritz, L.C.; Tomaselli, K.J.; Wang, L.; Yu, Z.; Croce, C.M.; Salveson, G.; Earnshaw, W.C.; Litwack, G.; Alnemri, E.S.
Mch3, a novel human apoptotic cysteine protease highly related to CPP32
Cancer Res.
55
6045-6052
1995
Homo sapiens (P55210)
Juan, T.S.C.; McNiece, I.K.; Argento, J.M.; Jenkins, N.A.; Gilbert, D.J.; Copeland, N.G.; Fletcher, F.A.
Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3
Genomics
40
86-93
1997
Homo sapiens (P55210), Homo sapiens, Mus musculus (P97864), Mus musculus
Machleidt, T.; Geller, P.; Schwandner, R.; Scherer, G.; Kronke, M.
Caspase 7-induced cleavage of kinectin in apoptotic cells
FEBS Lett.
436
51-54
1998
Homo sapiens
Ethell, D.W.; Bossy-Wetzel, E.; Bredesen, D.E.
Caspase 7 can cleave tumor necrosis factor receptor-I (p60) at a non-consensus motif, in vitro
Biochim. Biophys. Acta
1541
231-238
2001
Homo sapiens
Riedl, S.J.; Fuentes-Prior, P.; Renatus, M.; Kairies, N.; Krapp, S.; Huber, R.; Salvesen, G.S.; Bode, W.
Structural basis for the activation of human procaspase-7
Proc. Natl. Acad. Sci. USA
98
14790-14795
2001
Homo sapiens (P55210), Homo sapiens
Denault, J.B.; Salvesen, G.S.
Human caspase-7 activity and regulation by its N-terminal peptide
J. Biol. Chem.
278
34042-34050
2003
Homo sapiens
Duan, H.; Chinnaiyan, A.M.; Hudson, P.L.; Wing, J.P.; He, W.W.; Dixit, V.M.
ICE-LAP-3, a novel mammalian homologue at the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
J. Biol. Chem.
271
1621-1625
1996
Homo sapiens (P55210)
Chiu, C.C.; Lin, C.H.; Fang, K.
Etoposide (VP-16) sensitizes p53-deficient human non-small cell lung cancer cells to caspase-7-mediated apoptosis
Apoptosis
10
643-650
2005
Homo sapiens
Ohara, M.; Hayashi, T.; Kusunoki, Y.; Miyauchi, M.; Takata, T.; Sugai, M.
Caspase-2 and caspase-7 are involved in cytolethal distending toxin-induced apoptosis in Jurkat and MOLT-4 T-cell lines
Infect. Immun.
72
871-879
2004
Homo sapiens
Sironi, J.J.; Ouchi, T.
STAT1-induced apoptosis is mediated by caspases 2, 3, and 7
J. Biol. Chem.
279
4066-4074
2004
Homo sapiens
Clarke, C.A; Bennett, L.N.; Clarke, P.R.
Cleavage of claspin by caspase-7 during apoptosis inhibits the Chk1 pathway
J. Biol. Chem.
280
35337-35345
2005
Homo sapiens, Xenopus laevis
Twiddy, D.; Cohen, G.M.; Macfarlane, M.; Cain, K.
Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex
J. Biol. Chem.
281
3876-3888
2006
Homo sapiens
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
Houde, C.; Banks, K.G.; Coulombe, N.; Rasper, D.; Grimm, E.; Roy, S.; Simpson, E.M.; Nicholson, D.W.
Caspase-7 expanded function and intrinsic expression level underlies strain-specific brain phenotype of caspase-3-null mice
J. Neurosci.
24
9977-9984
2004
Homo sapiens, Mus musculus
Hayashi, N.; Shirakura, H.; Uehara, T.; Nomura, Y.
Relationship between SUMO-1 modification of caspase-7 and its nuclear localization in human neuronal cells
Neurosci. Lett.
397
5-9
2006
Homo sapiens
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
Chen, D.; Texada, D.E.; Duggan, C.; Deng, Y.; Redens, T.B.; Langford, M.P.
Caspase-3 and -7 mediate apoptosis of human Chang's conjunctival cells induced by enterovirus 70
Virology
347
307-322
2006
Homo sapiens
Jang, M.; Park, B.C.; Lee, A.Y.; Na, K.S.; Kang, S.; Bae, K.H.; Myung, P.K.; Chung, B.C.; Cho, S.; Lee, d.o.H.; Park, S.G.
Caspase-7 mediated cleavage of proteasome subunits during apoptosis
Biochem. Biophys. Res. Commun.
363
388-394
2007
Homo sapiens
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
Agniswamy, J.; Fang, B.; Weber, I.T.
Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis
FEBS J.
274
4752-4765
2007
Homo sapiens
Young, J.E.; Gouw, L.; Propp, S.; Sopher, B.L.; Taylor, J.; Lin, A.; Hermel, E.; Logvinova, A.; Chen, S.F.; Chen, S.; Bredesen, D.E.; Truant, R.; Ptacek, L.J.; La Spada, A.R.; Ellerby, L.M.
Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation
J. Biol. Chem.
282
30150-30160
2007
Homo sapiens
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
Garcia-Lozano, J.R.; Torres, B.; Fernandez, O.; Orozco, G.; Alvarez-Marquez, A.; Garcia, A.; Gonzalez-Gay, M.A.; Garcia, A.; Nunez-Roldan, A.; Martin, J.; Gonzalez-Escribano, M.F.
Caspase 7 influences susceptibility to rheumatoid arthritis
Rheumatology
46
1243-1247
2007
Homo sapiens
Li, I.T.; Pham, E.; Chiang, J.J.; Truong, K.
FRET evidence that an isoform of caspase-7 binds but does not cleave its substrate
Biochem. Biophys. Res. Commun.
373
325-329
2008
Homo sapiens
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
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
Hashimoto, T.; Yamauchi, L.; Hunter, T.; Kikkawa, U.; Kamada, S.
Possible involvement of caspase-7 in cell cycle progression at mitosis
Genes Cells
13
609-621
2008
Homo sapiens
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
Bressenot, A.; Marchal, S.; Bezdetnaya, L.; Garrier, J.; Guillemin, F.; Plenat, F.
Assessment of apoptosis by immunohistochemistry to active caspase-3, active caspase-7, or cleaved PARP in monolayer cells and spheroid and subcutaneous xenografts of human carcinoma
J. Histochem. Cytochem.
57
289-300
2009
Homo sapiens
Jung, E.J.; Kim, D.R.
Apoptotic cell death in TrkA-overexpressing cells: kinetic regulation of ERK phosphorylation and caspase-7 activation
Mol. Cells
26
12-17
2008
Homo sapiens
Jang, M.; Park, B.C.; Kang, S.; Lee, d.o..H.; Cho, S.; Lee, S.C.; Bae, K.H.; Park, S.G.
Mining of caspase-7 substrates using a degradomic approach
Mol. Cells
26
152-157
2008
Homo sapiens
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
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
Walsh, J.G.; Cullen, S.P.; Sheridan, C.; Luethi, A.U.; Gerner, C.; Martin, S.J.
Executioner caspase-3 and caspase-7 are functionally distinct proteases
Proc. Natl. Acad. Sci. USA
105
12815-12819
2008
Homo sapiens, Mus musculus
Karki, P.; Dahal, G.R.; Shin, S.Y.; Lee, J.S.; Cho, B.; Park, I.S.
Efficient cleavage of Bid and procaspase-7 by caspase-2 at lower pH
Protein Pept. Lett.
15
1044-1049
2008
Homo sapiens
Agniswamy, J.; Fang, B.; Weber, I.T.
Conformational similarity in the activation of caspase-3 and -7 revealed by the unliganded and inhibited structures of caspase-7
Apoptosis
14
1135-1144
2009
Homo sapiens
Lee, Y.M.; Kang, H.J.; Jang, M.; Kim, M.; Bae, K.H.; Chung, S.J.
Large-scale expression in Escherichia coli and efficient purification of precursor and active caspase-7 by introduction of thrombin cleavage sites
Protein Expr. Purif.
69
29-33
2010
Homo sapiens
Soares, J.; Lowe, M.M.; Jarstfer, M.B.
The catalytic subunit of human telomerase is a unique caspase-6 and caspase-7 substrate
Biochemistry
50
9046-9055
2011
Homo sapiens
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
Majerciak, V.; Kruhlak, M.; Dagur, P.K.; McCoy, J.P.; Zheng, Z.M.
Caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 confers a cellular function against viral lytic gene expression
J. Biol. Chem.
285
11297-11307
2010
Homo sapiens
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 (P55210), Homo sapiens
Miscione, G.P.; Calvaresi, M.; Bottoni, A.
Computational evidence for the catalytic mechanism of caspase-7. A DFT investigation
J. Phys. Chem. B
114
4637-4645
2010
Homo sapiens
Mills, E.; Chen, X.; Pham, E.; Wong, S.; Truong, K.
Engineering a photoactivated caspase-7 for rapid induction of apoptosis
ACS Synth. Biol.
1
75-82
2012
Homo sapiens
Cassel, J.A.; McDonnell, M.E.; Velvadapu, V.; Andrianov, V.; Reitz, A.B.
Characterization of a series of 4-aminoquinolines that stimulate caspase-7 mediated cleavage of TDP-43 and inhibit its function
Biochimie
94
1974-1981
2012
Homo sapiens
Boucher, D.; Blais, V.; Denault, J.B.
Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis
Proc. Natl. Acad. Sci. USA
109
5669-5674
2012
Homo sapiens (P55210)
Hill, M.E.; MacPherson, D.J.; Wu, P.; Julien, O.; Wells, J.A.; Hardy, J.A.
Reprogramming caspase-7 specificity by regio-specific mutations and selection provides alternate solutions for substrate recognition
ACS Chem. Biol.
11
1603-1612
2016
Homo sapiens (P55210), Homo sapiens
Vance, N.R.; Gakhar, L.; Spies, M.A.
Allosteric tuning of caspase-7 A fragment-based drug discovery approach
Angew. Chem. Int. Ed. Engl.
56
14443-14447
2017
Homo sapiens (P55210), Homo sapiens
Martini, C.; Bedard, M.; Lavigne, P.; Denault, J.B.
Characterization of Hsp90 co-chaperone p23 cleavage by caspase-7 uncovers a peptidase-substrate interaction involving intrinsically disordered regions
Biochemistry
56
5099-5111
2017
Homo sapiens (P55210)
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