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(Ac-VEID)2-Rh110 + H2O
?
-
-
-
-
?
(N-acetyl-VEID)2-rhodamine110 + H2O
?
-
-
-
?
Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
Ac-VEID-4-trifluoromethylcoumarin 7-amide + H2O
Ac-VEID + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Ac-VEID-7-amido-4-methylcoumarin + H2O
Ac-VEID + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
-
-
-
-
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
-
-
-
-
?
acetyl-LEVD-4-nitroanilide + H2O
acetyl-LEVD + 4-nitroaniline
-
-
-
-
?
acetyl-VDQQD-4-nitroanilide + H2O
acetyl-VDQQD + 4-nitroaniline
-
-
-
-
?
acetyl-VEHD-7-amido-4-methylcoumarin + H2O
acetyl-VEHD + 7-amino-4-methylcoumarin
-
VEHD is the optimal tetrapeptide recognition motif
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
-
-
-
-
?
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
-
-
-
-
?
alpha-actinin-4 + H2O
?
-
-
-
-
?
alpha-drebrin + H2O
?
-
-
-
-
?
alpha-spinophilin + H2O
?
-
-
-
-
?
amyloid precursor protein + H2O
?
annexin V + H2O
?
-
-
-
-
?
beta-actin + H2O
?
-
-
-
-
?
capping protein alpha + H2O
?
-
-
-
-
?
caspase-8 + H2O
?
-
caspase-6 cleaves, but does not activate caspase-8
-
-
?
cofilin I + H2O
?
-
-
-
-
?
cyclin B1 + H2O
truncated cyclin B1 + ?
DEVD-7-amido-4-methylcoumarin + H2O
DEVD + 7-amino-4-methylcoumarin
-
-
-
?
eukaryotic elongation factor 1 + H2O
?
-
-
-
-
?
glial fibrillary acidic protein + H2O
?
-
-
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
?
-
-
-
-
?
heat shock protein gp96 precursor + H2O
?
-
-
-
-
?
herpesvirus associated ubiquitin-specific protease + H2O
?
-
-
-
?
Hsp90alpha + H2O
?
-
-
-
-
?
huntingtin + H2O
huntingtin peptide fragments
IETD-7-amido-4-trifluoromethylcoumarin + H2O
IETD + 7-amino-4-trifluoromethylcoumarin
inhibitor-2 of protein phosphatase 2A + H2O
?
-
-
-
-
?
inorganic pyrophosphatase + H2O
?
-
-
-
-
?
kinesin5B + H2O
?
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
N-acetyl-Asp-Leu-Asn-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Leu-Asn-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Asp-Val-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Val-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Ile-Val-Leu-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Ile-Val-Leu-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Thr-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Thr-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Val-Glu-His-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Val-Glu-His-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Val-Glu-Ile-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Val-Glu-Ile-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
N-acetyl-VEID-4-nitroanilide + H2O
N-acetyl-VEID + 4-nitroaniline
-
-
-
?
N-acetyl-VEID-7-amido-4-methylcoumarin + H2O
N-acetyl-VEID + 7-amino-4-methylcoumarin
neurolysin + H2O
?
-
-
-
-
?
NF-kappaB + H2O
?
-
-
-
-
?
nuclear mitotic apparatus protein + H2O
?
-
cleavage at sites distict from caspase-3
-
-
?
partitioning-defective 3-like protein splice variant c + H2O
?
-
-
-
?
poly(ADP-ribose) polymerase + H2O
?
-
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
pro-caspase-2 + H2O
caspase-2 + ?
-
-
-
-
?
pro-caspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
pro-caspase-6 + H2O
?
-
caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
pro-caspase-8 + H2O
caspase-8 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
procaspase-6 mutant C163S + H2O
?
cleavage at the intersubunit linker position Asp-193
-
-
?
procaspase-8 + H2O
caspase-8 + ?
prolyl endopeptidase + H2O
?
-
-
-
-
?
protein 14-3-3epsilon + H2O
?
-
-
-
-
?
protein 14-3-3zeta + H2O
?
-
-
-
-
?
Rab GDP dissociation factor inhibitor alpha + H2O
?
-
-
-
-
?
receptor-interacting protein kinase-1 + H2O
?
serologically defined colon cancer antigen 3 + H2O
?
-
-
-
?
topoisomerase I + H2O
?
-
cleavage at PEDD123-/-G and EEED170-/-G
-
-
?
transcription factor AP-2alpha + H2O
?
Val-Glu-Ile-Asp 4-nitroanilide + H2O
?
-
-
-
-
?
Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
valosin-containing protein + H2O
?
-
-
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
viral nucleocapsid protein of transmissible gastroenteritis coronovirus + H2O
?
Z-VEID-R110 + H2O
2 Z-VEID + R110
caspase-6 recognition peptide covalently linked to two amine groups of the fluorescent dye rhodamine 110, fluorogenic assay
-
-
?
additional information
?
-
Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
actinin-4 + H2O
?
-
-
-
?
actinin-4 + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
-
-
?
alpha-tubulin + H2O
?
cleaved at Asp438
-
-
?
alpha-tubulin + H2O
?
-
cleaved at Asp438
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
beta-catenin + H2O
?
-
-
-
-
?
beta-catenin + H2O
?
-
processing of beta-catenin, production of a 70000 Da fragment
-
-
?
CBP + H2O
?
-
-
-
-
?
CBP + H2O
?
-
i.e. cAMP response element binding binding protein
-
-
?
cyclin B1 + H2O
truncated cyclin B1 + ?
-
overriding the G2 DNA damage checkpoint permits precocious entry into mitosis that ultimately leads to mitotic catastrophe, caused by caffeine. Mitotic catastrophe is manifested by an unscheduled activation of CDK1, caspase activation and apoptotic cell death. Cyclin B1 is required for mitotic catastrophe, but is also cleaved into a 35 kDa protein by a caspase-dependent mechanism during the process, overview
expression of the truncated product enhanced cell death
-
?
cyclin B1 + H2O
truncated cyclin B1 + ?
-
cleavage occurs after Asp123 in the motif ILVD123k, mutation of this motif to D123N attenuates the cleavage, cleavage still occurred in the control D160N mutant
lacking part of the NH2-terminal regulatory domain including the destruction box sequence
-
?
drebrin + H2O
?
-
-
-
?
drebrin + H2O
?
-
-
-
-
?
ezrin + H2O
?
-
-
-
-
?
human telomerase + H2O
?
-
caspase-6 cleaves human telomerase, hTERT, during apoptosis in cultured cells
-
-
?
human telomerase + H2O
?
-
caspase-6 cleaves human telomerase, hTERT, at residues D129 and D637, generation of three major proteolytic fragments, cleavage site determination using caspase-6 resistant substrate mutants D129A, D637A, and D129A/D637A, overview
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586 in the nucleus, proteolysis of mutant huntingtin is crucial to the development of Huntington disease. Cell stress induced by staurosporine results in the nuclear translocation and activation of caspase-6 and increased cleavage of huntingtin, overview. Differential localization of different endogenous caspase-cleaved huntingtin fragments in perinuclear and nuclear regions, overview
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586, a position 586 mutant of huntingtin is not cleaved by caspase-6, mutational caspase cleavage site analysis of huntingtin, overview
-
-
?
huntingtin + H2O
?
-
the enzyme cleaves at Asp-586
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586 in the nucleus, proteolysis of mutant huntingtin is crucial to the development of Huntington disease. Cell stress induced by staurosporine results in the nuclear translocation and activation of caspase-6 and increased cleavage of huntingtin, overview. Differential localization of different endogenous caspase-cleaved huntingtin fragments in perinuclear and nuclear regions, overview
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586, a position 586 mutant of huntingtin is not cleaved by caspase-6, mutational caspase cleavage site analysis of huntingtin, overview
-
-
?
huntingtin + H2O
huntingtin peptide fragments
-
-
-
-
?
huntingtin + H2O
huntingtin peptide fragments
-
a key step in the onset of Huntingtons disease is the caspase-6 mediated cleavage of the protein huntingtin into toxic fragments
-
-
?
IETD-7-amido-4-trifluoromethylcoumarin + H2O
IETD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
IETD-7-amido-4-trifluoromethylcoumarin + H2O
IETD + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
IETD-7-amido-4-trifluoromethylcoumarin + H2O
IETD + 7-amino-4-trifluoromethylcoumarin
-
very low cleavage activity
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A + H2O
?
-
cleavage site is VEID-/-
-
-
?
lamin A + H2O
?
-
apoptotic cleavage
-
-
?
lamin A + H2O
?
-
specific cleavage by caspase-6
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A/C + H2O
?
-
-
-
-
?
lamin A/C + H2O
?
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
N-acetyl-VEID-7-amido-4-methylcoumarin + H2O
N-acetyl-VEID + 7-amino-4-methylcoumarin
-
-
-
-
?
N-acetyl-VEID-7-amido-4-methylcoumarin + H2O
N-acetyl-VEID + 7-amino-4-methylcoumarin
-
-
-
?
p97 + H2O
?
the main cleavage site is at VAPD179
-
-
?
p97 + H2O
?
-
the main cleavage site is at VAPD179
-
-
?
periplakin + H2O
?
-
caspase 6 cleaves periplakin at an unconventional recognition site, amino acid sequence TVAD
-
-
?
periplakin + H2O
?
-
caspase 6 has a specific epidermal target which is periplakin
-
-
?
poly(ADP-ribose)polymerase + H2O
?
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
the enzyme may participate in poly(ADP-ribose)polymerase cleavage observed during apoptosis
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
the enzyme can self-process and self-activate
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
-
the enzyme can self-process and self-activate
-
-
?
pro-caspase-8 + H2O
?
-
caspase-8 precursor is initially cleaved between the p18 and p10 domains resulting in fragments of 42000 Da and 10000 Da. The 42000 Da fragment is further cleaved resulting in fragments of 25000 Da and 18000 Da
-
-
?
pro-caspase-8 + H2O
?
-
caspase-6 is the major activator of caspase-8 in the cytochrome c-induced apoptosis pathway. Caspase-8 precursor is initially cleaved between the p18 and p10 domains resulting in fragments of 42000 Da and 10000 Da. The 42000 Da fragment is further cleaved resulting in fragments of 25000 Da and 18000 Da
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
-
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
activation
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
-
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
activation
-
-
?
receptor-interacting protein kinase-1 + H2O
?
-
-
-
-
?
receptor-interacting protein kinase-1 + H2O
?
-
cleavage site between 324-Asp and 325-Cys
-
-
?
SATB1 + H2O
?
-
specifically cleaves at amino acid position 254 to produce a 65000 Da major fragment containing both a base-unpairing region (BUR)-binding domain and a homeodomain. This cleavage separates the DNA-binding domains from amino acids 90 to 204, a region which is a dimerization domain. The resulting SATB1 monomer loses its BUR-binding activity
-
-
?
SATB1 + H2O
?
-
cleavage disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis
-
-
?
spinophilin + H2O
?
-
-
-
?
spinophilin + H2O
?
-
-
-
-
?
Tau + H2O
?
-
cleavage of the microtubule-stabilizing protein by Csp-6
-
-
?
Tau + H2O
?
-
microtubule-associated protein, caspase-6 cleaves the N-terminus at D13 of tau in vitro
-
-
?
tau protein + H2O
?
-
-
-
-
?
tau protein + H2O
?
cleaved at Asp402
-
-
?
tau protein + H2O
?
-
cleaved at Asp402
-
-
?
transcription factor AP-2alpha + H2O
?
-
cleaves at Asp19 of the sequence DRHD19
-
-
?
transcription factor AP-2alpha + H2O
?
-
AP-2alpha is cleaved is at Asp19 of the sequence DRHD19 by caspase-6 before DNA framentation during TNF-alpha-induced apoptosis
-
-
?
transcription factor AP-2alpha + H2O
?
-
activates caspase-6 which in turn cleaves transcription factor AP2alpha
-
-
?
Ufd2p + H2O
?
-
polyubiquitination factor Ufd2p is cleaved at Asp123
-
-
?
Ufd2p + H2O
?
-
cleavage of polyubiquitination factor Ufd2p at Asp123 within the putative regulatory N-terminal domain might have important functional consequences within the apoptotic cascade
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
preferred substrate for caspase-6
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
preferred substrate for caspase-6
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
VEID-7-amido-4-trifluoromethylcoumarin + H2O
VEID + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
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
?
-
Mch2alpha but not Mch2beta possesses protease activity
-
-
?
additional information
?
-
-
the preferred cleavage sequence is VEHD-/-
-
-
?
additional information
?
-
-
the preferred cleavage sequence is VEHD-/-
-
-
?
additional information
?
-
-
the enzyme has a major role in nuclear apoptosis
-
-
?
additional information
?
-
-
bile acid-induced apoptosis, e.g. by glycochenodeoxycholic acid, in hepatocytes is caspase-6-dependent. Caspase-6 appears to play an important regulatory role in the promotion of bile acid-induced apoptosis as part of a feedback loop. Inhibition of caspase-9 reduces glycochenodeoxycholic acid-induced activation of caspase-6, whereas inhibition of caspase-6 reduces activation of caspase-8 placing caspase-6 between caspase-9 and caspase-8
-
-
?
additional information
?
-
-
caspase 6, an apoptosis-related cysteine peptidase, is upregulated in the skin of keloid prone patients. Caspase-6 plays a crucial role during apoptosis
-
-
?
additional information
?
-
-
caspase-6 activation occurs early in Alzheimer's disease and sometimes precedes the clinical manifestation of the disease in aged individuals. Early and neuritic activation of caspase-6 in Alzheimer disease can disrupt the cytoskeleton network of neurons, resulting in impaired neuronal structure and function in the absence of cell death. Proteomics analysis of caspase-6-mediated cleavage of human neuronal proteins, cleavage site determinations and cleavage specificity, overview
-
-
?
additional information
?
-
-
caspase-6 is a short pro-domain caspase that is activated early in Alzheimer disease, its activation does not induce apoptosis in HEK-293T cells, overview
-
-
?
additional information
?
-
-
possible involvement of caspase-6 and -7 but not caspase-3 in the regulation of hypoxia-induced apoptosis in tube-forming endothelial cells, caspase-6 is responsible for DNA ladder formation durirng hypoxia, overview
-
-
?
additional information
?
-
-
resveratrol-mediated activation of caspase-6 leads to apoptosis in HCT-116 colon cancer cells involving also p53, overview
-
-
?
additional information
?
-
-
ZBP-89, a Kruppel-type, zinc finger transcription factor, induces caspase-6 activation leading to inhibition of cell death in hepatoccellular carcinoma cells, inhibition of caspase-6 abolishes the effect of ZBP-89
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
CLK3, alcohol dehydrogenase 4 and malate dehydrogenase 1B are not cleaved by caspase-6
-
-
?
additional information
?
-
-
the enzyme does not cleave receptor-interacting protein kinase-3
-
-
?
additional information
?
-
stabilization of the N- and C-terminal loops by the tri-arginine patch is critical for the dynamics of caspase-6. This change in dynamics plays a key role in the mechanism by which the enzyme recognizes protein substrates
-
-
?
additional information
?
-
overexpression induces apoptosis
-
-
?
additional information
?
-
-
caspase 6 is an effector caspase in apoptosis pathways and regulates B cell activation and differentiation into plasma cells by modifying cell cycle entry, Casp6 is cleaved after B cell activation
-
-
?
additional information
?
-
-
caspase-6 is a key caspase known to play both initiator and effector roles in programmed cell death, excessive activation of the enzyme is an early marker of neuronal dysfunction and implicated in the pathogenesis of Huntington disease, Alzheimer's disease and other forms of cognitive impairment
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
-
caspase 6 is an effector caspase in apoptosis pathways and regulates B cell activation and differentiation into plasma cells by modifying cell cycle entry, Casp6 is cleaved after B cell activation
-
-
?
additional information
?
-
-
caspase-6 is a key caspase known to play both initiator and effector roles in programmed cell death, excessive activation of the enzyme is an early marker of neuronal dysfunction and implicated in the pathogenesis of Huntington disease, Alzheimer's disease and other forms of cognitive impairment
-
-
?
additional information
?
-
-
bile acid-induced apoptosis, e.g. by glycochenodeoxycholic acid, in hepatocytes is caspase-6-dependent. Caspase-6 appears to play an important regulatory role in the promotion of bile acid-induced apoptosis as part of a feedback loop. Inhibition of caspase-9 reduces glycochenodeoxycholic acid-induced activation of caspase-6, whereas inhibition of caspase-6 reduces activation of caspase-8 placing caspase-6 between caspase-9 and caspase-8
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ac-Val-Glu-Ile-Asp-7-amido-4-trifluoromethylcoumarin + H2O
Ac-Val-Glu-Ile-Asp + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
alpha-actinin-4 + H2O
?
-
-
-
-
?
alpha-drebrin + H2O
?
-
-
-
-
?
alpha-spinophilin + H2O
?
-
-
-
-
?
amyloid precursor protein + H2O
?
annexin V + H2O
?
-
-
-
-
?
beta-actin + H2O
?
-
-
-
-
?
beta-catenin + H2O
?
-
processing of beta-catenin, production of a 70000 Da fragment
-
-
?
capping protein alpha + H2O
?
-
-
-
-
?
caspase-8 + H2O
?
-
caspase-6 cleaves, but does not activate caspase-8
-
-
?
cofilin I + H2O
?
-
-
-
-
?
cyclin B1 + H2O
truncated cyclin B1 + ?
-
overriding the G2 DNA damage checkpoint permits precocious entry into mitosis that ultimately leads to mitotic catastrophe, caused by caffeine. Mitotic catastrophe is manifested by an unscheduled activation of CDK1, caspase activation and apoptotic cell death. Cyclin B1 is required for mitotic catastrophe, but is also cleaved into a 35 kDa protein by a caspase-dependent mechanism during the process, overview
expression of the truncated product enhanced cell death
-
?
eukaryotic elongation factor 1 + H2O
?
-
-
-
-
?
glial fibrillary acidic protein + H2O
?
-
-
-
-
?
glyceraldehyde-3-phosphate dehydrogenase + H2O
?
-
-
-
-
?
heat shock protein gp96 precursor + H2O
?
-
-
-
-
?
herpesvirus associated ubiquitin-specific protease + H2O
?
-
-
-
?
Hsp90alpha + H2O
?
-
-
-
-
?
human telomerase + H2O
?
-
caspase-6 cleaves human telomerase, hTERT, during apoptosis in cultured cells
-
-
?
huntingtin + H2O
huntingtin peptide fragments
-
a key step in the onset of Huntingtons disease is the caspase-6 mediated cleavage of the protein huntingtin into toxic fragments
-
-
?
inhibitor-2 of protein phosphatase 2A + H2O
?
-
-
-
-
?
inorganic pyrophosphatase + H2O
?
-
-
-
-
?
kinesin5B + H2O
?
-
-
-
?
neurolysin + H2O
?
-
-
-
-
?
NF-kappaB + H2O
?
-
-
-
-
?
partitioning-defective 3-like protein splice variant c + H2O
?
-
-
-
?
periplakin + H2O
?
-
caspase 6 has a specific epidermal target which is periplakin
-
-
?
poly(ADP-ribose)polymerase + H2O
?
the enzyme may participate in poly(ADP-ribose)polymerase cleavage observed during apoptosis
-
-
?
pro-caspase-2 + H2O
caspase-2 + ?
-
-
-
-
?
pro-caspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
pro-caspase-6 + H2O
?
-
caspase-8 activates caspase-3, and caspase-3 in turn activates caspase-6. Caspase 3 has a major role in nuclear apoptosis
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
pro-caspase-8 + H2O
?
-
caspase-6 is the major activator of caspase-8 in the cytochrome c-induced apoptosis pathway. Caspase-8 precursor is initially cleaved between the p18 and p10 domains resulting in fragments of 42000 Da and 10000 Da. The 42000 Da fragment is further cleaved resulting in fragments of 25000 Da and 18000 Da
-
-
?
pro-caspase-8 + H2O
caspase-8 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
procaspase-8 + H2O
caspase-8 + ?
prolyl endopeptidase + H2O
?
-
-
-
-
?
protein 14-3-3epsilon + H2O
?
-
-
-
-
?
protein 14-3-3zeta + H2O
?
-
-
-
-
?
Rab GDP dissociation factor inhibitor alpha + H2O
?
-
-
-
-
?
receptor-interacting protein kinase-1 + H2O
?
-
-
-
-
?
SATB1 + H2O
?
-
cleavage disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis
-
-
?
serologically defined colon cancer antigen 3 + H2O
?
-
-
-
?
transcription factor AP-2alpha + H2O
?
Ufd2p + H2O
?
-
cleavage of polyubiquitination factor Ufd2p at Asp123 within the putative regulatory N-terminal domain might have important functional consequences within the apoptotic cascade
-
-
?
valosin-containing protein + H2O
?
-
-
-
-
?
viral nucleocapsid protein of transmissible gastroenteritis coronovirus + H2O
?
-
cleavage site VVPD359-/-. Destruction of viral protein by the host cell death machinery
-
-
?
additional information
?
-
actinin-4 + H2O
?
-
-
-
?
actinin-4 + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
-
-
-
?
alpha-tubulin + H2O
?
-
-
-
?
alpha-tubulin + H2O
?
cleaved at Asp438
-
-
?
alpha-tubulin + H2O
?
-
cleaved at Asp438
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
drebrin + H2O
?
-
-
-
?
drebrin + H2O
?
-
-
-
-
?
ezrin + H2O
?
-
-
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586 in the nucleus, proteolysis of mutant huntingtin is crucial to the development of Huntington disease. Cell stress induced by staurosporine results in the nuclear translocation and activation of caspase-6 and increased cleavage of huntingtin, overview. Differential localization of different endogenous caspase-cleaved huntingtin fragments in perinuclear and nuclear regions, overview
-
-
?
huntingtin + H2O
?
-
the enzyme cleaves at Asp-586
-
-
?
huntingtin + H2O
?
-
cleavage at the capase-6 consensus sequence at amino acid 586 in the nucleus, proteolysis of mutant huntingtin is crucial to the development of Huntington disease. Cell stress induced by staurosporine results in the nuclear translocation and activation of caspase-6 and increased cleavage of huntingtin, overview. Differential localization of different endogenous caspase-cleaved huntingtin fragments in perinuclear and nuclear regions, overview
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A + H2O
?
-
cleavage site is VEID-/-
-
-
?
lamin A + H2O
?
-
specific cleavage by caspase-6
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A + H2O
?
-
-
-
-
?
lamin A/C + H2O
?
-
-
-
-
?
lamin A/C + H2O
?
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
lamin c + H2O
?
-
-
-
-
?
p97 + H2O
?
the main cleavage site is at VAPD179
-
-
?
p97 + H2O
?
-
the main cleavage site is at VAPD179
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
the enzyme can self-process and self-activate
-
-
?
pro-caspase-6 + H2O
caspase-6 + ?
-
the enzyme can self-process and self-activate
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-3 + H2O
caspase-3 + ?
-
-
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
activation
-
-
?
procaspase-8 + H2O
caspase-8 + ?
-
activation
-
-
?
spinophilin + H2O
?
-
-
-
?
spinophilin + H2O
?
-
-
-
-
?
tau protein + H2O
?
-
-
-
-
?
tau protein + H2O
?
cleaved at Asp402
-
-
?
tau protein + H2O
?
-
cleaved at Asp402
-
-
?
transcription factor AP-2alpha + H2O
?
-
AP-2alpha is cleaved is at Asp19 of the sequence DRHD19 by caspase-6 before DNA framentation during TNF-alpha-induced apoptosis
-
-
?
transcription factor AP-2alpha + H2O
?
-
activates caspase-6 which in turn cleaves transcription factor AP2alpha
-
-
?
additional information
?
-
-
the enzyme has a major role in nuclear apoptosis
-
-
?
additional information
?
-
-
bile acid-induced apoptosis, e.g. by glycochenodeoxycholic acid, in hepatocytes is caspase-6-dependent. Caspase-6 appears to play an important regulatory role in the promotion of bile acid-induced apoptosis as part of a feedback loop. Inhibition of caspase-9 reduces glycochenodeoxycholic acid-induced activation of caspase-6, whereas inhibition of caspase-6 reduces activation of caspase-8 placing caspase-6 between caspase-9 and caspase-8
-
-
?
additional information
?
-
-
caspase 6, an apoptosis-related cysteine peptidase, is upregulated in the skin of keloid prone patients. Caspase-6 plays a crucial role during apoptosis
-
-
?
additional information
?
-
-
caspase-6 activation occurs early in Alzheimer's disease and sometimes precedes the clinical manifestation of the disease in aged individuals. Early and neuritic activation of caspase-6 in Alzheimer disease can disrupt the cytoskeleton network of neurons, resulting in impaired neuronal structure and function in the absence of cell death. Proteomics analysis of caspase-6-mediated cleavage of human neuronal proteins, cleavage site determinations and cleavage specificity, overview
-
-
?
additional information
?
-
-
caspase-6 is a short pro-domain caspase that is activated early in Alzheimer disease, its activation does not induce apoptosis in HEK-293T cells, overview
-
-
?
additional information
?
-
-
possible involvement of caspase-6 and -7 but not caspase-3 in the regulation of hypoxia-induced apoptosis in tube-forming endothelial cells, caspase-6 is responsible for DNA ladder formation durirng hypoxia, overview
-
-
?
additional information
?
-
-
resveratrol-mediated activation of caspase-6 leads to apoptosis in HCT-116 colon cancer cells involving also p53, overview
-
-
?
additional information
?
-
-
ZBP-89, a Kruppel-type, zinc finger transcription factor, induces caspase-6 activation leading to inhibition of cell death in hepatoccellular carcinoma cells, inhibition of caspase-6 abolishes the effect of ZBP-89
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
CLK3, alcohol dehydrogenase 4 and malate dehydrogenase 1B are not cleaved by caspase-6
-
-
?
additional information
?
-
-
the enzyme does not cleave receptor-interacting protein kinase-3
-
-
?
additional information
?
-
overexpression induces apoptosis
-
-
?
additional information
?
-
-
caspase 6 is an effector caspase in apoptosis pathways and regulates B cell activation and differentiation into plasma cells by modifying cell cycle entry, Casp6 is cleaved after B cell activation
-
-
?
additional information
?
-
-
caspase-6 is a key caspase known to play both initiator and effector roles in programmed cell death, excessive activation of the enzyme is an early marker of neuronal dysfunction and implicated in the pathogenesis of Huntington disease, Alzheimer's disease and other forms of cognitive impairment
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
-
development of an assay method for specifically detecting caspase-6 activity in an intact cell environment, evaluation of a 384-well whole-cell chemiluminescent ELISA assay that monitors the proteolytic degradation of endogenously expressed lamin A/C during the early stages of caspase-dependent apoptosis, overview
-
-
?
additional information
?
-
-
caspase 6 is an effector caspase in apoptosis pathways and regulates B cell activation and differentiation into plasma cells by modifying cell cycle entry, Casp6 is cleaved after B cell activation
-
-
?
additional information
?
-
-
caspase-6 is a key caspase known to play both initiator and effector roles in programmed cell death, excessive activation of the enzyme is an early marker of neuronal dysfunction and implicated in the pathogenesis of Huntington disease, Alzheimer's disease and other forms of cognitive impairment
-
-
?
additional information
?
-
-
bile acid-induced apoptosis, e.g. by glycochenodeoxycholic acid, in hepatocytes is caspase-6-dependent. Caspase-6 appears to play an important regulatory role in the promotion of bile acid-induced apoptosis as part of a feedback loop. Inhibition of caspase-9 reduces glycochenodeoxycholic acid-induced activation of caspase-6, whereas inhibition of caspase-6 reduces activation of caspase-8 placing caspase-6 between caspase-9 and caspase-8
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(2-methylpiperidin-1-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
-
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(morpholin-4-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(morpholin-4-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
-
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-oxo-2-(piperidin-1-yl)ethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
-
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-oxo-2-(pyrrolidin-1-yl)ethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
-
1-(3,4-dichlorobenzyl)-5-(morpholin-4-ylsulfonyl)-1H-indole-2,3-dione
-
slight inhibition
1-benzyl-5-(thiomorpholin-4-ylsulfonyl)-1H-indole-2,3-dione
-
-
2-(3-[(E)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(2-methoxyethyl)acetamide
-
2-(3-[(E)-[1-(furan-2-ylmethyl)-4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(2-methoxyethyl)acetamide
-
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(3-methoxypropyl)acetamide
-
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(tetrahydrofuran-2-ylmethyl)acetamide
-
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetamide
-
2-(3-[(Z)-[1-(furan-2-ylmethyl)-4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(tetrahydrofuran-2-ylmethyl)acetamide
-
2-([[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl]amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide
-
2-([[1-(4-chlorophenyl)-1H-tetrazol-5-yl]sulfanyl]methyl)quinazolin-4(1H)-one
-
2-amino-7-[4-[(3-fluorobenzyl)oxy]phenyl]-6,7-dihydro[1,3]thiazolo[4,5-b]pyridin-5(4H)-one
-
2-[(4-methylquinazolin-2-yl)amino]-6-[(pyridin-2-ylsulfanyl)methyl]pyrimidin-4(3H)-one
-
2-[1-(2-chloro-4-fluorobenzyl)-3-oxopiperazin-2-yl]-N-cyclooctylacetamide
-
2-[1-(3-methoxybenzyl)-3-oxopiperazin-2-yl]-N-[[1-(2-methylphenyl)-1H-pyrazol-4-yl]methyl]acetamide
-
3-[(5E)-5-(2-chlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-(adamantan-1-yl)propanamide
-
4-hydroxy-5-iodo-3-nitrophenylacetyl-Leu-Leu-Leu-vinylsulfone
-
-
5-(azetidin-1-ylsulfonyl)-1-benzyl-1H-indole-2,3-dione
-
-
5-(morpholin-4-ylsulfonyl)-1H-indole-2,3-dione
-
slight inhibition
6-amino-4-[3-(benzyloxy)phenyl]-3-methyl-1-phenyl-1,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
-
Ac-Val-Glu-Ile-Asp-CHO
-
-
acetyl-Val-Ile-Asp-aldehyde
-
-
benzyloxycarbonyl-DRHD-fluoromethylketone
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
benzyloxycarbonyl-Val-Glu(OMe)-Ile-Asp(OMe)-fluoromethyl ketone
-
caspase-6-selective inhibitor
benzyloxycarbonyl-VEID-fluoromethylketone
-
-
BOC-Asp(OMe)-fluoromethyl ketone
-
for general caspase inhibition
carbobenzoxy-Val-Ala-Asp-fluoromethylketone
-
-
carbobenzyloxy-LEHD-fluoromethyl ketone
carbobenzyloxy-VAD-fluoromethyl ketone
-
i.e. zVAD-fmk, a broad-spectrum caspase inhibitor, which inhibits activation of caspase-6 and caspase-3, but not of caspase-7
carbobenzyloxy-VEID-fluoromethyl ketone
IETD-CHO
-
caspase-6 in lens extracts from neonatal mice partially inhibited by 0.0005 mM
methyl 3-(aminomethyl)-5-[(furan-2-ylcarbonyl)amino]benzoate
-
methyl 3-([[(2,3-dimethyl-1H-indol-7-yl)carbonyl]amino]methyl)-5-[(furan-2-ylcarbonyl)amino]benzoate
-
methyl 3-[(furan-2-ylcarbonyl)amino]-5-([[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl)benzoate
-
methyl 3-[([[1-(4-chlorophenyl)cyclobutyl]carbonyl]amino)methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
-
methyl 3-[[(2,2-dimethylpropanoyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
-
methyl 3-[[(2,3-dihydro-1-benzofuran-2-ylcarbonyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
-
methyl 3-[[(2,3-dihydro-1-benzofuran-2-ylcarbonyl)amino]methyl]-5-[(phenylacetyl)amino]benzoate
-
methyl 3-[[(3,5-dimethylbenzoyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
-
N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-3-methyl-1-phenyl-1H-thieno[2,3-c]pyrazole-5-carboxamide
-
N-(furan-2-ylmethyl)-2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetamide
-
N-(furan-2-ylmethyl)-2-[3-(phenoxyacetyl)-1H-indol-1-yl]acetamide
-
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-valinamide
N-acetyl-Val-Glu-Ile-Asp-aldehyde
-
N-carbobenzyloxy-IETD-fluoromethyl ketone
N-[(2R)-1-(3-cyanophenyl)-3-hydroxypropan-2-yl]-5-(3,4-dimethoxyphenyl)furan-3-carboxamide
selective inhibitor
N-[[5-(3,4-dimethoxyphenyl)-2-methylfuran-3-yl]carbonyl]phenylalanine
-
SB203580
-
a p38 inhibitor, also inhibits activation of caspase-6, caspase-3, and caspase-7
siRNA
-
silencing of caspase-6 expression
-
Sox11
reduces caspase-6 activity and prevents caspase-6 self-cleavage. Several regions, including amino acids 117-214 and 362-395 within sox11 as well as a nuclear localization signal (NLS) all contribute to the reduction in caspase-6 activity
-
sulfonamide isatin Michael acceptors
-
small molecule inhibitors of caspase-6
-
VEID-fluoromethylketone
-
Z -VEID-fluoromethylketone
-
Z-DEVD-fluoromethylketone
-
-
Z-IETD-fluoromethylketone
-
for Csp-6- and caspase-8-like inhibition
Z-Val-Ala-Asp-fluoromethylketone
Z-VE(OMe)ID(OMe)-fluoromethylketone
-
specific inhibitor
Z-VEID-fluoromethylketone
Zn2+
caspase-6 is allosterically inhibited by zinc and binds one zinc/monomer at an exosite distal from the active site. Complete inhibition at 0.0015 mM
ZVEID
-
specific caspase 6 inhibitor
ZVEID-fmk
-
caspase 6-specific inhibitor, reduces apoptosis and prevents periplakin cleavage in adherent cells, although it does not completely prevent cells from detaching
[1-(3,4-dichlorobenzyl)-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(3,4-dichlorobenzyl)-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(3,4-dichlorobenzyl)-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(3,4-dichlorobenzyl)-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(4-methoxybenzyl)-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(4-methoxybenzyl)-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(4-methoxybenzyl)-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-(4-methoxybenzyl)-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-benzyl-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-benzyl-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-benzyl-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[1-benzyl-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[5-(azetidin-1-ylsulfonyl)-1-(3,4-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[5-(azetidin-1-ylsulfonyl)-1-(4-methoxybenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
[5-(azetidin-1-ylsulfonyl)-1-benzyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
-
-
Ac-VEID-CHO
-
a caspase-6-specific inhibitor
Ac-VEID-CHO
a reversible caspase-6 inhibitor, enzyme-inhibitor complex structure, overview
benzyloxycarbonyl-VAD-fluoromethylketone
-
t1/2 at 0.001 mM is 98 s
benzyloxycarbonyl-VAD-fluoromethylketone
-
-
carbobenzyloxy-LEHD-fluoromethyl ketone
-
-
carbobenzyloxy-LEHD-fluoromethyl ketone
-
-
carbobenzyloxy-VEID-fluoromethyl ketone
-
-
carbobenzyloxy-VEID-fluoromethyl ketone
-
-
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-valinamide
-
pan-caspase inhibitor
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-valinamide
-
-
N-acetyl-L-alpha-aspartyl-L-alpha-glutamyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-valinamide
-
N-carbobenzyloxy-IETD-fluoromethyl ketone
-
-
N-carbobenzyloxy-IETD-fluoromethyl ketone
-
-
Q-VD-OPH
-
a Pan caspase inhibitor
VEID-CHO
-
VEID-CHO
-
caspase-6 in lens extracts from neonatal mice efficiently inhibited by 0.0005 mM
Z-VAD-fluoromethylketone
-
a Pan caspase inhibitor
Z-VAD-fluoromethylketone
-
-
Z-VAD-fluoromethylketone
-
Z-VAD-fluoromethylketone
-
-
Z-Val-Ala-Asp-fluoromethylketone
-
inhibitor of caspases
Z-Val-Ala-Asp-fluoromethylketone
-
-
Z-VEID-fluoromethylketone
-
for Csp-6-like inhibition
Z-VEID-fluoromethylketone
-
a caspase-6 inhibitor
Z-VEID-fluoromethylketone
-
-
Z-VEID-fluoromethylketone
specific inhibitor
additional information
-
KI-value above 0.01 mM for acetyl-YVAD-aldehyde
-
additional information
-
because the mutant pro-Casp6C163A is not cleaved in serum-deprived conditions and is a dominant negative inhibitor of Casp6 activation
-
additional information
-
carbobenzyloxy-LEHD-fluoromethyl ketone specifically inhibits initiator caspase-9 upstream of caspase-3 and caspase-3 activation, but fails to inhibit caspase-6 and caspase-7 activation
-
additional information
-
development and synthesis of nonpeptidic caspase-6 inhibitors, overview. No inhibition of caspase-6 by Ac-IETD-CHO, Ac-YVAD-CHO, and Ac-DEVD-CHO
-
additional information
-
alternatively spliced caspase-6B isoform inhibits the proteolytic self-activation of caspase-6A in vitro and in cells. But purified bacterially expressed recombinant pro-Casp6b does not possess catalytic activity and does not inhibit the active form of Casp6a
-
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0.0164
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(2-methylpiperidin-1-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
37°C, pH 6.8
0.0076
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(morpholin-4-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
37°C, pH 6.8
0.0128
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-(morpholin-4-yl)-2-oxoethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
37°C, pH 6.8
0.011
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-oxo-2-(piperidin-1-yl)ethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
37°C, pH 6.8
0.0098
(5Z)-1-(furan-2-ylmethyl)-5-([1-[2-oxo-2-(pyrrolidin-1-yl)ethyl]-1H-indol-3-yl]methylidene)pyrimidine-2,4,6(1H,3H,5H)-trione
Homo sapiens
37°C, pH 6.8
0.0015
1-(3,4-dichlorobenzyl)-5-(morpholin-4-ylsulfonyl)-1H-indole-2,3-dione
Homo sapiens
-
above
0.00128
1-benzyl-5-(thiomorpholin-4-ylsulfonyl)-1H-indole-2,3-dione
Homo sapiens
-
-
0.0165
2-(3-[(E)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(2-methoxyethyl)acetamide
Homo sapiens
37°C, pH 6.8
0.0168
2-(3-[(E)-[1-(furan-2-ylmethyl)-4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(2-methoxyethyl)acetamide
Homo sapiens
37°C, pH 6.8
0.0129
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(3-methoxypropyl)acetamide
Homo sapiens
37°C, pH 6.8
0.0302
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(tetrahydrofuran-2-ylmethyl)acetamide
Homo sapiens
37°C, pH 6.8
0.0105
2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetamide
Homo sapiens
37°C, pH 6.8
0.0044
2-(3-[(Z)-[1-(furan-2-ylmethyl)-4,6-dioxo-2-thioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)-N-(tetrahydrofuran-2-ylmethyl)acetamide
Homo sapiens
37°C, pH 6.8
0.1095
2-([[(6-oxo-4-phenyl-1,6-dihydropyrimidin-2-yl)sulfanyl]acetyl]amino)-4,5,6,7-tetrahydro-1-benzothiophene-3-carboxamide
Homo sapiens
37°C, pH 6.8
0.1418
2-([[1-(4-chlorophenyl)-1H-tetrazol-5-yl]sulfanyl]methyl)quinazolin-4(1H)-one
Homo sapiens
37°C, pH 6.8
0.289
2-amino-7-[4-[(3-fluorobenzyl)oxy]phenyl]-6,7-dihydro[1,3]thiazolo[4,5-b]pyridin-5(4H)-one
Homo sapiens
37°C, pH 6.8
0.2334
2-[(4-methylquinazolin-2-yl)amino]-6-[(pyridin-2-ylsulfanyl)methyl]pyrimidin-4(3H)-one
Homo sapiens
37°C, pH 6.8
0.0464
2-[1-(2-chloro-4-fluorobenzyl)-3-oxopiperazin-2-yl]-N-cyclooctylacetamide
Homo sapiens
37°C, pH 6.8
0.0441
2-[1-(3-methoxybenzyl)-3-oxopiperazin-2-yl]-N-[[1-(2-methylphenyl)-1H-pyrazol-4-yl]methyl]acetamide
Homo sapiens
37°C, pH 6.8
0.123
3-[(5E)-5-(2-chlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-N-(adamantan-1-yl)propanamide
Homo sapiens
37°C, pH 6.8
0.00983
5-(azetidin-1-ylsulfonyl)-1-benzyl-1H-indole-2,3-dione
Homo sapiens
-
-
0.002
5-(morpholin-4-ylsulfonyl)-1H-indole-2,3-dione
Homo sapiens
-
above
0.159
6-amino-4-[3-(benzyloxy)phenyl]-3-methyl-1-phenyl-1,4-dihydropyrano[2,3-c]pyrazole-5-carbonitrile
Homo sapiens
37°C, pH 6.8
0.0000305
Ac-DEVD-CHO
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
0.0000532
Ac-IETD-CHO
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
0.0000162
Ac-VEID-CHO
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
1.922
methyl 3-(aminomethyl)-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
0.719
methyl 3-([[(2,3-dimethyl-1H-indol-7-yl)carbonyl]amino]methyl)-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
2.047
methyl 3-[(furan-2-ylcarbonyl)amino]-5-([[(5-methyl-3-phenyl-1,2-oxazol-4-yl)carbonyl]amino]methyl)benzoate
Homo sapiens
37°C, pH 6.8
0.027
methyl 3-[([[1-(4-chlorophenyl)cyclobutyl]carbonyl]amino)methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
3.37
methyl 3-[[(2,2-dimethylpropanoyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
0.0132
methyl 3-[[(2,3-dihydro-1-benzofuran-2-ylcarbonyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
1.545
methyl 3-[[(2,3-dihydro-1-benzofuran-2-ylcarbonyl)amino]methyl]-5-[(phenylacetyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
0.0215
methyl 3-[[(3,5-dimethylbenzoyl)amino]methyl]-5-[(furan-2-ylcarbonyl)amino]benzoate
Homo sapiens
37°C, pH 6.8
0.09
N-(1,5-dimethyl-3-oxo-2-phenyl-2,3-dihydro-1H-pyrazol-4-yl)-3-methyl-1-phenyl-1H-thieno[2,3-c]pyrazole-5-carboxamide
Homo sapiens
37°C, pH 6.8
0.0042
N-(furan-2-ylmethyl)-2-(3-[(Z)-[1-(furan-2-ylmethyl)-2,4,6-trioxotetrahydropyrimidin-5(2H)-ylidene]methyl]-1H-indol-1-yl)acetamide
Homo sapiens
37°C, pH 6.8
0.0799
N-(furan-2-ylmethyl)-2-[3-(phenoxyacetyl)-1H-indol-1-yl]acetamide
Homo sapiens
37°C, pH 6.8
0.000011
N-[(2R)-1-(3-cyanophenyl)-3-hydroxypropan-2-yl]-5-(3,4-dimethoxyphenyl)furan-3-carboxamide
Homo sapiens
in 50 mM HEPES (pH 7.0), 25 mM MgSO4, 0.5 mM EGTA, 5 mM glutathione, 0.01% (v/v) Triton X-100 containing 0.1% (w/v) bovine gamma-globulin, at 22°C
0.02
N-[[5-(3,4-dimethoxyphenyl)-2-methylfuran-3-yl]carbonyl]phenylalanine
Homo sapiens
in 50 mM HEPES (pH 7.0), 25 mM MgSO4, 0.5 mM EGTA, 5 mM glutathione, 0.01% (v/v) Triton X-100 containing 0.1% (w/v) bovine gamma-globulin, at 22°C
0.0004023
Z-DEVD-fluoromethylketone
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
0.002112
Z-VAD-fluoromethylketone
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
0.0001286
Z-VEID-fluoromethylketone
Homo sapiens
-
pH 7.2, 37°C, recombinant enzyme
0.000568
[1-(3,4-dichlorobenzyl)-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000468
[1-(3,4-dichlorobenzyl)-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.00023
[1-(3,4-dichlorobenzyl)-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000592
[1-(3,4-dichlorobenzyl)-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000545
[1-(4-methoxybenzyl)-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000358
[1-(4-methoxybenzyl)-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000188
[1-(4-methoxybenzyl)-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000453
[1-(4-methoxybenzyl)-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000325
[1-benzyl-2-oxo-5-(piperidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000241
[1-benzyl-2-oxo-5-(pyrrolidin-1-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000151
[1-benzyl-2-oxo-5-(thiomorpholin-4-ylsulfonyl)-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000425
[1-benzyl-5-(morpholin-4-ylsulfonyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.00028
[5-(azetidin-1-ylsulfonyl)-1-(3,4-dichlorobenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000197
[5-(azetidin-1-ylsulfonyl)-1-(4-methoxybenzyl)-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.000156
[5-(azetidin-1-ylsulfonyl)-1-benzyl-2-oxo-1,2-dihydro-3H-indol-3-ylidene]propanedinitrile
Homo sapiens
-
-
0.0034
Zn2+
Homo sapiens
wild type enzyme, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C
0.0107
Zn2+
Homo sapiens
mutant enzyme E244A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C
0.0158
Zn2+
Homo sapiens
mutant enzyme K36A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C
0.0249
Zn2+
Homo sapiens
mutant enzyme H287A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C
0.0256
Zn2+
Homo sapiens
mutant enzyme E244A/H287A, in 100 mM HEPES, pH 7.5, 10% (w/v) sucrose, 0.1% (w/v) CHAPS, 20 mM TCEP, and 120 mM NaCl, at 37°C
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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 (P55212)
brenda
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 (P55212)
brenda
Nakajima, K.; Takahashi, A.; Yaoita, Y.
Structure, expression, and function of the Xenopus laevis caspase family
J. Biol. Chem.
275
10484-10491
2000
Xenopus laevis
brenda
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
brenda
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
brenda
Chang, H.Y.; Yang, X.
Proteases from cell suicide: functions and regulation of caspases
Microbiol. Mol. Biol. Rev.
64
821-846
2000
Homo sapiens
brenda
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
brenda
van de Craen, M.; Berx, G.; van den Brande, I.; Fiers, W.; Declercq, W.; Vandenabeele, P.
Proteolytic cleavage of beta-catenin by caspases: an in vitro analysis
FEBS Lett.
458
167-170
1999
Mus musculus
brenda
Fernandes-Alnemri, T.; Litwack, G.; Alnemri, E.S.
Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family
Cancer Res.
55
2737-2742
1995
Homo sapiens (P55212)
brenda
van de Craen, M.; Vandenabeele, P.; Declercq, W.; van den Brande, I.; van Loo, G.; Molemans, F.; Schotte, P.; van Criekinge, W.; Beyaert, R.; Fiers, W.
Characterization of seven murine caspase family members
FEBS Lett.
403
61-69
1997
Mus musculus (O08738)
brenda
Cowling, V.; Downward, J.
Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain
Cell Death Differ.
9
1046-1056
2002
Homo sapiens
brenda
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
brenda
Galande, S.; Dickinson, L.A.; Mian, I.S.; Sikorska, M.; Kohwi-Shigematsu, T.
SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis
Mol. Cell. Biol.
21
5591-5604
2001
Homo sapiens
brenda
Mahoney, J.A.; Odin, J.A.; White, S.M.; Shaffer, D.; Koff, A.; Casciola-Rosen, L.; Rosen, A.
The human homologue of the yeast polyubiquitination factor Ufd2p is cleaved by caspase 6 and granzyme B during apoptosis
Biochem. J.
361
587-595
2002
Homo sapiens
brenda
Nyormoi, O.; Wang, Z.; Doan, D.; Ruiz, M.; McConkey, D.; Bar-Eli, M.
Transcription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cells
Mol. Cell. Biol.
21
4856-4867
2001
Homo sapiens
brenda
Nyormoi, O.; Wang, Z.; Bar-Eli, M.
Sequence-based discovery of a synthetic peptide inhibitor of caspase 6
Apoptosis
8
371-376
2003
Homo sapiens
brenda
Hill, J.; Duckworth, M.; Murdock, P.; Rennie, G.; Sabido-David, C.; Ames, R.S.; Szekeres, P.; Wilson, S.; Bergsma, D.J.; Gloger, I.S.; Levy, D.S.; Chambers, J.K.; Muir, A.I.
Molecular cloning and functional characterization of MCH2, a novel human MCH receptor
J. Biol. Chem.
276
20125-20129
2001
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
Guo, H.; Albrecht, S.; Bourdeau, M.; Petzke, T.; Bergeron, C.; LeBlanc, A.C.
Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
Am. J. Pathol.
165
523-531
2004
Homo sapiens
brenda
Kang, B.H.; Ko, E.; Kwon, O.K.; Choi, K.Y.
The structure of procaspase 6 is similar to that of active mature caspase 6
Biochem. J.
364
629-634
2002
Homo sapiens
brenda
Guo, H.; Petrin, D.; Zhang, Y.; Bergeron, C.; Goodyer, C.G.; LeBlanc, A.C.
Caspase-1 activation of caspase-6 in human apoptotic neurons
Cell Death Differ.
13
285-292
2006
Homo sapiens
brenda
Loegering, D.A.; Ruchaud, S.; Earnshaw, W.C.; Kaufmann, S.H.
Evaluation of the role of caspase-6 in anticancer drug-induced apoptosis
Cell Death Differ.
13
346-347
2006
Gallus gallus, Homo sapiens
brenda
Schmeck, B.; Gross, R.; N'Guessan, P.D.; Hocke, A.C.; Hammerschmidt, S.; Mitchell, T.J.; Rosseau, S.; Suttorp, N.; Hippenstiel, S.
Streptococcus pneumoniae-induced caspase 6-dependent apoptosis in lung epithelium
Infect. Immun.
72
4940-4947
2004
Homo sapiens
brenda
Foley, J.D.; Rosenbaum, H.; Griep, A.E.
Temporal regulation of VEID-7-amino-4-trifluoromethylcoumarin cleavage activity and caspase-6 correlates with organelle loss during lens development
J. Biol. Chem.
279
32142-32150
2004
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Kalinin, A.E.; Kalinin, A.E.; Aho, M.; Uitto, J.; Aho, S.
Breaking the connection: caspase 6 disconnects intermediate filament-binding domain of periplakin from its actin-binding N-terminal region
J. Invest. Dermatol.
124
46-55
2005
Homo sapiens
brenda
Horowitz, P.M.; Patterson, K.R.; Guillozet-Bongaarts, A.L.; Reynolds, M.R.; Carroll, C.A.; Weintraub, S.T.; Bennett, D.A.; Cryns, V.L.; Berry, R.W.; Binder, L.I.
Early N-terminal changes and caspase-6 cleavage of tau in Alzheimer's disease
J. Neurosci.
24
7895-7902
2004
Homo sapiens
brenda
Narkilahti, S.; Pitkanen, A.
Caspase 6 expression in the rat hippocampus during epileptogenesis and epilepsy
Neuroscience
131
887-897
2005
Rattus norvegicus
brenda
Suzuki, A.; Kusakai, G.; Kishimoto, A.; Shimojo, Y.; Miyamoto, S.; Ogura, T.; Ochiai, A.; Esumi, H.
Regulation of caspase-6 and FLIP by the AMPK family member ARK5
Oncogene
23
7067-7075
2004
Homo sapiens
brenda
MacLachlan, T.K.; El-Deiry, W.S.
Apoptotic threshold is lowered by p53 transactivation of caspase-6
Proc. Natl. Acad. Sci. USA
99
9492-9497
2002
Homo sapiens
brenda
Lee, S.C.; Chan, J.; Clement, M.V.; Pervaiz, S.
Functional proteomics of resveratrol-induced colon cancer cell apoptosis: caspase-6-mediated cleavage of lamin A is a major signaling loop
Proteomics
6
2386-2394
2006
Homo sapiens
brenda
Torres, F.; Quintana, J.; Diaz, J.G.; Carmona, A.J.; Estevez, F.
Trifolin acetate-induced cell death in human leukemia cells is dependent on caspase-6 and activates the MAPK pathway
Apoptosis
13
716-728
2008
Homo sapiens
brenda
Garner, E.; Martinon, F.; Tschopp, J.; Beard, P.; Raj, K.
Cells with defective p53-p21-pRb pathway are susceptible to apoptosis induced by p84N5 via caspase-6
Cancer Res.
67
7631-7637
2007
Homo sapiens
brenda
Takle, H.; McLeod, A.; Andersen, O.
Cloning and characterization of the executioner caspases 3, 6, 7 and Hsp70 in hyperthermic Atlantic salmon (Salmo salar) embryos
Comp. Biochem. Physiol. B
144B
188-198
2006
Salmo salar (Q4ZHU8), Salmo salar (Q4ZHV1)
-
brenda
Blazquez, S.; Sirvent, J.J.; Olona, M.; Aguilar, C.; Pelegri, A.; Garcia, J.F.; Palacios, J.
Caspase-3 and caspase-6 in ductal breast carcinoma: a descriptive study
Histol. Histopathol.
21
1321-1329
2006
Homo sapiens
brenda
Nassiri, M.; Woolery-Lloyd, H.; Ramos, S.; Jacob, S.E.; Gugic, D.; Viciana, A.; Romanelli, P.; Elgart, G.; Berman, B.; Vincek, V.
Gene expression profiling reveals alteration of caspase 6 and 14 transcripts in normal skin of keloid-prone patients
Arch. Dermatol. Res.
301
183-188
2009
Homo sapiens
brenda
Klaiman, G.; Champagne, N.; Leblanc, A.C.
Self-activation of Caspase-6 in vitro and in vivo: Caspase-6 activation does not induce cell death in HEK293T cells
Biochim. Biophys. Acta
1793
592-601
2009
Homo sapiens
brenda
Chan, J.Y.; Phoo, M.S.; Clement, M.V.; Pervaiz, S.; Lee, S.C.
Resveratrol displays converse dose-related effects on 5-fluorouracil-evoked colon cancer cell apoptosis: the roles of caspase-6 and p53
Cancer Biol. Ther.
7
1305-1312
2008
Homo sapiens
brenda
Chen, G.G.; Chan, U.P.; Bai, L.C.; Fung, K.Y.; Tessier, A.; To, A.K.; Merchant, J.L.; Lai, P.B.
ZBP-89 reduces the cell death threshold in hepatocellular carcinoma cells by increasing caspase-6 and S phase cell cycle arrest
Cancer Lett.
283
52-58
2009
Homo sapiens
brenda
Eguchi, R.; Tone, S.; Suzuki, A.; Fujimori, Y.; Nakano, T.; Kaji, K.; Ohta, T.
Possible involvement of caspase-6 and -7 but not caspase-3 in the regulation of hypoxia-induced apoptosis in tube-forming endothelial cells
Exp. Cell Res.
315
327-335
2009
Homo sapiens
brenda
Warby, S.C.; Doty, C.N.; Graham, R.K.; Carroll, J.B.; Yang, Y.Z.; Singaraja, R.R.; Overall, C.M.; Hayden, M.R.
Activated caspase-6 and caspase-6-cleaved fragments of huntingtin specifically colocalize in the nucleus
Hum. Mol. Genet.
17
2390-2404
2008
Mus musculus, Mus musculus YAC128
brenda
Rust, C.; Wild, N.; Bernt, C.; Vennegeerts, T.; Wimmer, R.; Beuers, U.
Bile acid-induced apoptosis in hepatocytes is caspase-6-dependent
J. Biol. Chem.
284
2908-2916
2009
Homo sapiens, Rattus norvegicus
brenda
Watanabe, C.; Shu, G.L.; Zheng, T.S.; Flavell, R.A.; Clark, E.A.
Caspase 6 regulates B cell activation and differentiation into plasma cells
J. Immunol.
181
6810-6819
2008
Mus musculus, Mus musculus C57BL/6
brenda
Chu, W.; Rothfuss, J.; Chu, Y.; Zhou, D.; Mach, R.H.
Synthesis and in vitro evaluation of sulfonamide isatin Michael acceptors as small molecule inhibitors of caspase-6
J. Med. Chem.
52
2188-2191
2009
Homo sapiens
brenda
Klaiman, G.; Petzke, T.L.; Hammond, J.; Leblanc, A.C.
Targets of caspase-6 activity in human neurons and Alzheimer disease
Mol. Cell. Proteomics
7
1541-1555
2008
Homo sapiens
brenda
Chan, Y.W.; Chen, Y.; Poon, R.Y.
Generation of an indestructible cyclin B1 by caspase-6-dependent cleavage during mitotic catastrophe
Oncogene
28
170-183
2009
Homo sapiens
brenda
Beretta, F.; Bassani, S.; Binda, E.; Verpelli, C.; Bello, L.; Galli, R.; Passafaro, M.
The GluR2 subunit inhibits proliferation by inactivating Src-MAPK signalling and induces apoptosis by means of caspase 3/6-dependent activation in glioma cells
Eur. J. Neurosci.
30
25-34
2009
Homo sapiens
brenda
Baumgartner, R.; Meder, G.; Briand, C.; Decock, A.; Darcy, A.; Hassiepen, U.; Morse, R.; Renatus, M.
The crystal structure of caspase-6, a selective effector of axonal degeneration
Biochem. J.
423
429-439
2009
Homo sapiens (P55212)
brenda
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
brenda
Lee, A.W.; Champagne, N.; Wang, X.; Su, X.D.; Goodyer, C.; Leblanc, A.C.
Alternatively spliced caspase-6B isoform inhibits the activation of caspase-6A
J. Biol. Chem.
285
31974-31984
2010
Homo sapiens
brenda
Mueller, I.; Lamers, M.B.; Ritchie, A.J.; Park, H.; Dominguez, C.; Munoz-Sanjuan, I.; Maillard, M.; Kiselyov, A.
A new apo-caspase-6 crystal form reveals the active conformation of the apoenzyme
J. Mol. Biol.
410
307-315
2011
Homo sapiens (P55212)
brenda
Mintzer, R.; Ramaswamy, S.; Shah, K.; Hannoush, R.N.; Pozniak, C.D.; Cohen, F.; Zhao, X.; Plise, E.; Lewcock, J.W.; Heise, C.E.
A whole cell assay to measure caspase-6 activity by detecting cleavage of lamin a/c
PLoS ONE
7
e30376
2012
Homo sapiens, Mus musculus, Mus musculus C57BL/6
brenda
Graham, R.K.; Ehrnhoefer, D.E.; Hayden, M.R.
Caspase-6 and neurodegeneration
Trends Neurosci.
34
646-656
2011
Homo sapiens
brenda
Cho, J.H.; Lee, P.Y.; Son, W.C.; Chi, S.W.; Park, B.C.; Kim, J.H.; Park, S.G.
Identification of the novel substrates for caspase-6 in apoptosis using proteomic approaches
BMB Rep.
46
588-593
2013
Homo sapiens (P55212)
brenda
Shahzidi, S.; Brech, A.; Sioud, M.; Li, X.; Suo, Z.; Nesland, J.M.; Peng, Q.
Lamin A/C cleavage by caspase-6 activation is crucial for apoptotic induction by photodynamic therapy with hexaminolevulinate in human B-cell lymphoma cells
Cancer Lett.
339
25-32
2013
Homo sapiens
brenda
van Raam, B.J.; Ehrnhoefer, D.E.; Hayden, M.R.; Salvesen, G.S.
Intrinsic cleavage of receptor-interacting protein kinase-1 by caspase-6
Cell Death Differ.
20
86-96
2013
Homo sapiens
brenda
LeBlanc, A.C.; Ramcharitar, J.; Afonso, V.; Hamel, E.; Bennett, D.A.; Pakavathkumar, P.; Albrecht, S.
Caspase-6 activity in the CA1 region of the hippocampus induces age-dependent memory impairment
Cell Death Differ.
21
696-706
2014
Homo sapiens
brenda
Baburamani, A.A.; Miyakuni, Y.; Vontell, R.; Supramaniam, V.G.; Svedin, P.; Rutherford, M.; Gressens, P.; Mallard, C.; Takeda, S.; Thornton, C.; Hagberg, H.
Does caspase-6 have a role in perinatal brain injury?
Dev. Neurosci.
37
321-337
2015
Homo sapiens, Rattus norvegicus, Mus musculus (Q3TPJ9)
brenda
LeBlanc, A.C.
Caspase-6 as a novel early target in the treatment of Alzheimers disease
Eur. J. Neurosci.
37
2005-2018
2013
Homo sapiens (P55212), Homo sapiens, Mus musculus
brenda
Velazquez-Delgado, E.M.; Hardy, J.A.
Zinc-mediated allosteric inhibition of caspase-6
J. Biol. Chem.
287
36000-36011
2012
Homo sapiens (P55212)
brenda
Lee, P.Y.; Cho, J.H.; Chi, S.W.; Bae, K.H.; Cho, S.; Park, B.C.; Kim, J.H.; Park, S.G.
Expression of the pro-domain-deleted active form of caspase-6 in Escherichia coli
J. Microbiol. Biotechnol.
24
719-723
2014
Homo sapiens (P55212)
brenda
Gafni, J.; Papanikolaou, T.; Degiacomo, F.; Holcomb, J.; Chen, S.; Menalled, L.; Kudwa, A.; Fitzpatrick, J.; Miller, S.; Ramboz, S.; Tuunanen, P.I.; Lehtimaeki, K.K.; Yang, X.W.; Park, L.; Kwak, S.; Howland, D.; Park, H.; Ellerby, L.M.
Caspase-6 activity in a BACHD mouse modulates steady-state levels of mutant huntingtin protein but is not necessary for production of a 586 amino acid proteolytic fragment
J. Neurosci.
32
7454-7465
2012
Mus musculus
brenda
Heise, C.E.; Murray, J.; Augustyn, K.E.; Bravo, B.; Chugha, P.; Cohen, F.; Giannetti, A.M.; Gibbons, P.; Hannoush, R.N.; Hearn, B.R.; Jaishankar, P.; Ly, C.Q.; Shah, K.; Stanger, K.; Steffek, M.; Tang, Y.; Zhao, X.; Lewcock, J.W.; Renslo, A.R.; Flygare, J.; Arkin, M.R.
Mechanistic and structural understanding of uncompetitive inhibitors of caspase-6
PLoS ONE
7
e50864
2012
Homo sapiens (P55212)
brenda
Wang, X.; Cao, Q.; Zhang, Y.; Su, X.
Activation and regulation of caspase-6 and its role in neurodegenerative diseases
Annu. Rev. Pharmacol. Toxicol.
55
553-572
2015
Homo sapiens (P55212)
brenda
Suita, H.; Shinomiya, T.; Nagahara, Y.
Caspase-6 induces 7A6 antigen localization to mitochondria during FAS-induced apoptosis of Jurkat cells
Anticancer Res.
37
1697-1704
2017
Homo sapiens (P55212), Homo sapiens
brenda
Fu, S.; Ding, M.; Yang, Y.; Kong, J.; Li, Y.; Guo, Z.; Wang, A.; Ye, J.
Molecular cloning, characterization and expression analysis of caspase-6 in puffer fish (Takifugu obscurus)
Aquaculture
490
311-320
2018
Takifugu obscurus (H2TDB0)
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brenda
Hogg, M.C.; Mitchem, M.R.; Koenig, H.G.; Prehn, J.H.
Caspase 6 has a protective role in SOD1(G93A) transgenic mice
Biochim. Biophys. Acta
1862
1063-1073
2016
Mus musculus (O08738), Mus musculus
brenda
Yan, A.; Ren, C.; Chen, T.; Huo, D.; Jiang, X.; Sun, H.; Hu, C.
A novel caspase-6 from sea cucumber Holothuria leucospilota Molecular characterization, expression analysis and apoptosis detection
Fish Shellfish Immunol.
80
232-240
2018
Holothuria leucospilota (A0A2I6STS0), Holothuria leucospilota
brenda
Watanabe, C.; Shu, G.L.; Giltiay, N.V.; Clark, E.A.
Regulation of B-lineage cells by caspase 6
Immunol. Cell Biol.
96
1072-1082
2018
Mus musculus (O08738)
brenda
Yao, Y.; Shi, Q.; Chen, B.; Wang, Q.; Li, X.; Li, L.; Huang, Y.; Ji, J.; Shen, P.
Identification of caspase-6 as a new regulator of alternatively activated macrophages
J. Biol. Chem.
291
17450-17466
2016
Mus musculus (O08738)
brenda
MacPherson, D.J.; Mills, C.L.; Ondrechen, M.J.; Hardy, J.A.
Tri-arginine exosite patch of caspase-6 recruits substrates for hydrolysis
J. Biol. Chem.
294
71-88
2019
Homo sapiens (P55212)
brenda
Woo, V.; Cheng, C.; Duraikannu, A.; Chandrasekhar, A.; Purdy, K.; Martinez, J.A.; Zochodne, D.W.
Caspase-6 is a dispensable enabler of adult mammalian axonal degeneration
Neuroscience
371
242-253
2018
Mus musculus (O08738)
brenda
Waldron-Roby, E.; Hoerauf, J.; Arbez, N.; Zhu, S.; Kulcsar, K.; Ross, C.A.
Sox11 reduces caspase-6 cleavage and activity
PLoS ONE
10
e0141439
2015
Homo sapiens (P55212)
brenda
Bartel, A.; Goehler, A.; Hopf, V.; Breitbach, K.
Caspase-6 mediates resistance against Burkholderia pseudomallei infection and influences the expression of detrimental cytokines
PLoS ONE
12
e0180203
2017
Mus musculus (O08738), Mus musculus
brenda
Tubeleviciute-Aydin, A.; Beautrait, A.; Lynham, J.; Sharma, G.; Gorelik, A.; Deny, L.J.; Soya, N.; Lukacs, G.L.; Nagar, B.; Marinier, A.; LeBlanc, A.C.
Identification of allosteric inhibitors against active caspase-6
Sci. Rep.
9
5504
2019
Homo sapiens (P55212), Homo sapiens
brenda