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(Z-LEHD)2-R110 tetrapeptide + H2O
?
-
-
-
-
?
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV-5-[(2'-aminoethyl)-amino]naphthalenesulfonic acid + H2O
4-[[4'-(dimethylamino)phenyl]azo]-benzoic acid-YVADAPV + 5-[(2-aminoethyl)-amino]naphthalenesulfonic acid
-
-
-
?
Ac-LEHD-7-amido-4-methylcoumarin + H2O
Ac-LEHD + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-Trp-Glu-His-Asp-7-amino-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
Ac-YVAD-4-nitroanilide + H2O
Ac-YVAD + 4-nitroaniline
-
-
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
-
-
-
-
?
acetyl-DQMD-4-nitroanilide + H2O
acetyl-DQMD + 4-nitroaniline
-
-
-
-
?
acetyl-L-Leu-L-Glu-L-His-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Leu-L-Glu-L-His-L-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-L-Trp-L-Glu-L-His-L-Asp-7-amido-4-methylcoumarin + H2O
acetyl-L-Trp-L-Glu-L-His-L-Asp + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-LEVD-4-nitroanilide + H2O
acetyl-LEVD + 4-nitroaniline
-
-
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
-
-
-
?
acetyl-VQVD-4-nitroanilide + H2O
acetyl-VQVD + 4-nitroaniline
-
-
-
-
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
acetyl-YEVD-4-nitroanilide + H2O
acetyl-YEVD + 4-nitroaniline
-
-
-
-
?
acetyl-YEVDGW-amide + H2O
?
-
preferred peptide substrate
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
-
-
-
-
?
acetyl-YVAD-7-amido-4-methylcoumarin + H2O
acetyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
?
Assc2 peptide + H2O
?
-
-
-
-
?
ataxin-3 + H2O
?
-
-
-
-
?
Bap31 protein + H2O
?
-
-
-
-
?
calpastatin + H2O
?
-
-
-
-
?
carboxyfluorescein-YVAD-fluoromethylketone + H2O
?
-
-
-
-
?
caspase-1 + H2O
?
-
-
-
-
?
cPLA2 peptide + H2O
?
-
-
-
-
?
cyclin G-associated kinase + H2O
?
-
-
-
-
?
DNA replication licensing factor MCM4 + H2O
?
-
-
-
-
?
elF-4H peptide + H2O
?
-
-
-
-
?
endoplasmin + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
eukaryotic translation initiation factor 3 subunit J + H2O
?
-
-
-
-
?
FLP-1 peptide + H2O
?
-
-
-
-
?
FYN-binding protein + H2O
?
-
-
-
-
?
gamma-actin + H2O
?
-
-
-
-
?
gasdermin D + H2O
?
-
-
-
-
?
GIT2 peptide + H2O
?
-
-
-
-
?
heat shock protein 60 + H2O
?
-
-
-
-
?
histone E3 peptide + H2O
?
-
-
-
-
?
IL-1 beta + H2O
?
-
-
-
-
?
interferon-gamma inducing factor + H2O
?
-
cleavage site: LESD-/-
-
-
?
interleukin-1 + H2O
interleukin-1beta
-
-
-
-
?
interleukin-18 + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
interleukin-1beta + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
ligatin + H2O
?
-
-
-
-
?
LMNA Isoform + H2O
?
-
-
-
-
?
MAP-tau Isoform + H2O
?
-
-
-
-
?
MCM3 peptide + H2O
?
-
-
-
-
?
MyD88 adaptor-like + H2O
?
N-acetyl-Asp-Glu-Val-Asp-7-amido-4-methylcoumarin + H2O
N-acetyl-Asp-Glu-Val-Asp + 7-amino-4-methylcoumarin
-
-
-
?
N-acetyl-DEVD-7-amido-4-methylcoumarin + H2O
N-acetyl-DEVD + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
N-acetyl-IETD-7-amido-4-methylcoumarin + H2O
N-acetyl-IETD + 7-amino-4-methylcoumarin
-
negligible activity
-
-
?
N-acetyl-LEHD-7-amido-4-methylcoumarin + H2O
N-acetyl-LEHD + 7-amino-4-methylcoumarin
-
negligible activity
-
-
?
N-acetyl-WEHD-7-amido-4-trifluoromethylcoumarin + H2O
N-acetyl-WEHD + 7-amino-4-trifluoromethylcoumarin
-
-
-
?
nuclear immunophilin FKBP46 + H2O
?
-
-
-
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
cleavage at Asp87
-
?
periphilin-1 + H2O
?
-
-
-
-
?
PLA2G4A + H2O
?
-
-
-
-
?
poly(ADP-ribose)polymerase + H2O
?
-
-
-
?
PPARgamma + H2O
?
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pre-interleukin-1beta + H2O
interleukin-1beta + ?
PREL-1 peptide + H2O
?
-
-
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
pro-caspase-7 + H2O
caspase-7 + amino-terminal procaspase-7 peptide
-
consensus caspase-7 recognition sequence DEVD, caspase-1 cleaves caspase-7 at the canonical activation sites Asp23 and Asp198, D23A/D198A double caspase-7 mutant is no substrate
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
pro-interleukin-18 + H2O
interleukin-18 propeptide
pro-interleukin-18 + H2O
mature interleukin-18
pro-interleukin-18 + H2O
mature interleukin-18 + ?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pro-interleukin-1beta + H2O
interleukin-1beta + ?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
pro-interleukin-1beta + H2O
mature interleukin-1beta
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
pro-interleukin-33 + H2O
interleukin-33 + ?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
caspase-1 processing at position D20 activates interleukin-37
-
-
?
SMG7 peptide + H2O
?
-
-
-
-
?
sphingosine kinase 2 + H2O
?
-
-
-
-
?
splicing factor U2AF 65-kDa subunit + H2O
?
-
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
succinyl-YVAD-7-amido-4-methylcoumarin + H2O
succinyl-YVAD + 7-amino-4-methylcoumarin
-
-
-
-
?
synapse-associated protein 1 + H2O
?
-
-
-
-
?
target of Myb protein 1 pepitde + H2O
?
-
-
-
-
?
TF AP-2alpha + H2O
?
-
-
-
-
?
TIF1b peptide + H2O
?
-
-
-
-
?
Trp-Glu-His-Asp-p-nitroanilide + H2O
Trp-Glu-His-Asp + p-nitroaniline
-
-
-
-
?
Vsp72 peptide + H2O
?
-
-
-
-
?
additional information
?
-
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-WEHD-7-amido-4-methylcoumarin + H2O
acetyl-WEHD + 7-amino-4-methylcoumarin
-
WEHD is the optimal tetrapeptide recognition motif
-
-
?
beta-actin + H2O
?
-
-
-
-
?
beta-actin + H2O
?
-
-
-
-
?
beta-actin + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
cleavage during apoptosis
-
-
?
MyD88 adaptor-like + H2O
?
-
-
-
-
?
MyD88 adaptor-like + H2O
?
-
NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
-
-
?
MyD88 adaptor-like + H2O
?
-
caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
-
-
?
parkin + H2O
?
-
-
-
-
?
parkin + H2O
?
-
cleavage at Asp126-Ser127
-
-
?
parkin + H2O
?
-
cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinsons disease may play an important role in the degenerative process by initiating a vicious circle that leads to the accumulation of toxic parkin substrates, e.g. alpha-synuclein
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
-
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
cleavage to the mature interleukin-1beta
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
-
?
pre-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
activation
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
interleukin-18 is synthesized as a 24 kDa inactive precursor lacking a signal peptide, which is cleaved after Asp35 by caspase-1 to yield an active 8 kDa molecule
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
active caspase-1 converts inactive pro-interleukin-18 to active interleukin-18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
activation
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
cleavage between Asp116 and Ala117, required for activation of the cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
active caspase-1 converts inactive 31 kDa pro-interleukin-1beta to 18 kDa active interleukin-1beta
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
691461, 707154, 707323, 707393, 708128, 708251, 708272, 708722, 709056, 709153, 709224, 709359, 709953, 710377 -
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
HMG-CoA reductase inhibition induces interleukin-1beta release through Rac1/PI3K/protein kinase B-dependent caspase-1 activation, overview. Caspase-1 is hyperactive in mevalonate kinase deficiency leading secretion of high levels of interleukin-1beta, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37°C conditions
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
caspase-1 effectively cleaves interleukin-1beta to its mature form in both heat shock and 37°C conditions
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
-
-
-
-
?
pro-interleukin-33 + H2O
interleukin-33 + ?
-
activation
-
-
?
pyrin + H2O
?
-
-
-
-
?
pyrin + H2O
?
-
caspase-1 cleaves pyrin at Asp330, Familial Mediterranean fever-associated mutants are cleaved more than wild-type pyrin by caspase-1. Pyrin itself regulates caspase-1 activation and interleukin-1beta production through interaction of its N-terminal PYD motif with the ASC adapterprotein, and also modulates interleukin-1beta production by interaction of its C-terminal B30.2 domain with the catalytic domains of caspase-1
-
-
?
pyrin + H2O
?
-
recombinant substrate expressed in PT67 cells
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
-
-
-
-
?
succinyl-YVAD-4-nitroanilide + H2O
succinyl-YVAD + 4-nitroaniline
-
-
-
?
additional information
?
-
cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
-
-
?
additional information
?
-
-
the enzyme is involved in cytokine activation
-
-
?
additional information
?
-
-
the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
-
-
?
additional information
?
-
-
caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
-
-
?
additional information
?
-
-
caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
-
-
?
additional information
?
-
-
anisomycin-induced activation of preformed pro-interleukin-18 is mediated by a p38 MAPK/caspase-1-dependent mechanism, whereas anisomycin-induced new synthesis of pro-interleukin-18 mRNA is mediated through p38 MAPK-dependent but caspase-1 independent mechanism
-
-
?
additional information
?
-
-
caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is an inflammatory caspase that controls the activation and secretion of the inflammatory cytokines, interleukin-1beta and interleukin-18, active caspase-1 specifically mediates secretion of retinoic acid inducible gene-I, which is not a substrate for proteolytic cleavage by caspase-1, but caspase-1 physically interacts with full length RIG-I, although not with mutant forms lacking either the amino- or carboxyl-terminal domains
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased. Caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
-
-
?
additional information
?
-
-
caspase-1 is the prototype of the inflammatory caspases and is a component of the NALP3 inflammasome, a cytosolic multiprotein complex that mediates the processing of pro-inflammatory caspases and cytokines. The inflammasome represents the first line of defense against cellular stress and is a crucial component of innate immunity. Caspase-1 plays a central role in the mechanisms leading to labor particularly in the context of intrauterine infection/inflammation. Caspase-1 is increased in the amniotic fluid of women with preterm labor in the presence of intra-amniotic infection/inflammation
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, inflammasome regulation system, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta. Infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC
-
-
?
additional information
?
-
-
mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
-
-
?
additional information
?
-
-
Nod-like receptors induce assembling of the inflammasome multiprotein complexes to activate caspase-1 in response to microbial and danger signals, overview. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock, a physiological posttranslational mechanism, overview. Redox-sensitive cysteine residues regulate caspase-1 to identify the redox-sensitive cysteine residues in caspase
-
-
?
additional information
?
-
-
pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
-
-
?
additional information
?
-
-
pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
-
-
?
additional information
?
-
-
the downstream signaling pathway of TLR7 and TLR8 in monocytes and dendritic cells after stimulation with specific ligands included not only the secretion of cytokines, such as TNFalpha and interleukin-1beta, but as well the activation of necessary regulating proteins like caspase-1
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
-
-
?
additional information
?
-
-
caspase-1 and caspase-9 share 100% aspartic acid in the P1 position. The structures in the cleavage sites of most caspase-1 substrates are different from that of caspase-9 substrates in the following three aspects, 1. the amino acid residues with the statistically high frequencies 2. the hydrophobic amino acid occurrence frequencies and 3. the charged amino acid occurrence frequencies, second, the amino acid pairs P1-P1' are different
-
-
?
additional information
?
-
-
phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
-
-
?
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
?
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
?
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
?
additional information
?
-
-
IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
-
-
?
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
?
additional information
?
-
-
caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
-
caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
-
-
?
additional information
?
-
-
caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
?
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
-
-
?
additional information
?
-
-
the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
additional information
?
-
-
peptide substrate screening, the enzyme preferably cleaves after Asp, overview
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
peptide substrate screening, the enzyme preferably cleaves after Asp, overview
-
-
?
additional information
?
-
-
caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
-
-
?
additional information
?
-
-
in brain microvascular endothelial cells and in astrocytes expression and activity of inducible nitric axide synthase exclusively depends on the endogenous availability of bioactive interleukin-1beta as inhibition of ICE activity significantly decreases promoter activity of inducible nitric axide synthase, expression and enzyme activity
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
the enzyme is able to induce apoptosis in Sf9 cells
-
-
?
additional information
?
-
-
the enzyme is able to induce apoptosis in Sf9 cells
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-
?
additional information
?
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-
caspase-1 is involved in this apoptosis
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Bap31 protein + H2O
?
-
-
-
-
?
epidermal growth factor receptor + H2O
?
-
cleavage during apoptosis
-
-
?
interferon-gamma inducing factor + H2O
?
-
cleavage site: LESD-/-
-
-
?
interleukin-1 + H2O
interleukin-1beta
-
-
-
-
?
interleukin-18 + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
interleukin-1beta + H2O
?
-
caspase-1 is required for control of oral infection with wild-type Salmonella in mice, as well as for resistance to septic shock following systemic challenge with live attenuated Salmonella enterica serovar typhimurium. Furthermore host defense against Salmonella enterica serovar typhimurium requires both caspase-1 substrates IL-1beta and IL-18
-
-
?
MyD88 adaptor-like + H2O
?
nuclear immunophilin FKBP46 + H2O
?
-
-
-
?
p35 + H2O
100000 Da fragment + 25000 Da fragment
cleavage at Asp87
-
?
parkin + H2O
?
-
cleavage at Asp126-Ser127. Caspase-1 and caspase-8 dependent parkin cleavage in sporadic Parkinsons disease may play an important role in the degenerative process by initiating a vicious circle that leads to the accumulation of toxic parkin substrates, e.g. alpha-synuclein
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
pro-caspase-7 + H2O
caspase-7 + ?
pro-interleukin-18 + H2O
interleukin-18 + ?
pro-interleukin-18 + H2O
interleukin-18 propeptide
pro-interleukin-18 + H2O
mature interleukin-18
pro-interleukin-18 + H2O
mature interleukin-18 + ?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pro-interleukin-1beta + H2O
interleukin-1beta + ?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
pro-interleukin-1beta + H2O
mature interleukin-1beta
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
pro-interleukin-33 + H2O
interleukin-33 + ?
-
-
-
-
?
pro-interleukin-33 + H2O
mature interleukin-33 + ?
-
recombinant pro-interleukin-33 is cleaved by recombinant caspase-1 in vitro
-
-
?
pro-interleukin-37 + H2O
interleukin-37 propeptide
-
caspase-1 processing at position D20 activates interleukin-37
-
-
?
pyrin + H2O
?
-
caspase-1 cleaves pyrin at Asp330, Familial Mediterranean fever-associated mutants are cleaved more than wild-type pyrin by caspase-1. Pyrin itself regulates caspase-1 activation and interleukin-1beta production through interaction of its N-terminal PYD motif with the ASC adapterprotein, and also modulates interleukin-1beta production by interaction of its C-terminal B30.2 domain with the catalytic domains of caspase-1
-
-
?
sphingosine kinase 2 + H2O
?
-
-
-
-
?
additional information
?
-
MyD88 adaptor-like + H2O
?
-
NF-kappaB activation by the Toll-IL-1 receptor domain protein MyD88 adapter-like is regulated by caspase-1
-
-
?
MyD88 adaptor-like + H2O
?
-
caspase-1 cleaves the TLR adaptor MyD88 adaptor-like at position D198
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pre-interleukin-18 + H2O
interleukin-18 + ?
-
virus infection by influenza A or Sendai virus induces proteolytic processing of IL-18 in human macrophages via caspase-1 and caspase-3 activation
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 mediated maturation and secretion of IL-1beta needs a translocation competent T3SS and flagellin, but not the type III effector proteins ExoS, ExoT and ExoY. ExoS negatively regulates the Pseudomonas aeruginosa induced IL-1beta maturation by a mechanism that is dependent on its ADP ribosyltransferase activity
-
-
?
pre-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1-dependent processing of pro-interleukin-1beta can occur in the cytosol following activation of P2X7-receptor. Structural changes preceding cell death, occurring after caspase-1 activation, promote the cellular release of interleukin-1beta
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
activation
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-caspase-7 + H2O
caspase-7 + ?
-
caspase-1-mediates activation of endogenous caspase-7
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
activation of caspase-1 as a key event resulting in interleukin-18 production, caspase-1 is essential for interleukin-18 production in infected macrophages
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
-
-
-
?
pro-interleukin-18 + H2O
interleukin-18 propeptide
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
-
-
-
?
pro-interleukin-18 + H2O
mature interleukin-18 + ?
-
interleukin-18 is synthesized as inactive cytoplasmic precursor that is processed into biologically activemature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
caspase-1 regulates key steps in inflammation and immunity, by activating the proinflammatory cytokines interleukin-1beta and IL18 or mediating apoptotic processes
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
-
pro-interleukin-1beta cleavage site 1 is FEAD-/-, pro-interleukin-1beta cleavage site II is YVHD-/-
-
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
17000 Da fragment + 28000 Da fragment
pIL-1beta is mainly processed by caspase-1, but also by caspase-3
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
activation
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 activation leads to release of active interleukin-1beta from THP-1 cells, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is the enzyme responsible for the cleavage and activation of interleukin-1beta, which is a potent pro-inflammatory cytokine
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1beta and interleukin 18
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is a caspase recruitment domain, CARD-containing protease required for processing of pro-interleukin-1beta in macrophages. A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide, NOD2 is a NOD-like receptor, i.e. NLR. NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in MDP-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
caspase-1 is essential for interleukin-1beta and interleukin-18 production in the eye in response to muramyl dipeptide. Activation of NOD2 results in IL-1beta production via a caspase-1-dependent mechanism, interleukin-1beta and caspase-1 contribute to muramyl dipeptide-induced ocular inflammation, overview
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta propeptide
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
707323, 707393, 708128, 708251, 708272, 708722, 709056, 709153, 709224, 709359, 709953, 710377 -
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
HMG-CoA reductase inhibition induces interleukin-1beta release through Rac1/PI3K/protein kinase B-dependent caspase-1 activation, overview. Caspase-1 is hyperactive in mevalonate kinase deficiency leading secretion of high levels of interleukin-1beta, regulation, overview
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
interleukin-1beta is synthesized as inactive cytoplasmic precursor that is processed into biologically active mature form in response to various proinflammatory stimuli, including viruses, by the cysteine protease caspase-1
-
-
?
pro-interleukin-1beta + H2O
mature interleukin-1beta + ?
-
-
-
-
?
additional information
?
-
cell death protease essential for development. Loss of zygotic caspase-1 function in Drosophila causes larval lethality and melanotic tumors
-
-
?
additional information
?
-
-
the enzyme is involved in cytokine activation
-
-
?
additional information
?
-
-
the production of the active enzyme induces the activation of an endogenous 32000 Da (CPP32) like caspase
-
-
?
additional information
?
-
-
caspase 1 activated by protease-activating factor acts upstream of mitochondria to cause release of proteins that are known to mediate apoptosis
-
-
?
additional information
?
-
-
caspase-1 is an upstream positive regulator of caspase-6-mediated cell death in primary human neurons
-
-
?
additional information
?
-
-
anisomycin-induced activation of preformed pro-interleukin-18 is mediated by a p38 MAPK/caspase-1-dependent mechanism, whereas anisomycin-induced new synthesis of pro-interleukin-18 mRNA is mediated through p38 MAPK-dependent but caspase-1 independent mechanism
-
-
?
additional information
?
-
-
caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is an inflammatory caspase that controls the activation and secretion of the inflammatory cytokines, interleukin-1beta and interleukin-18, active caspase-1 specifically mediates secretion of retinoic acid inducible gene-I, which is not a substrate for proteolytic cleavage by caspase-1, but caspase-1 physically interacts with full length RIG-I, although not with mutant forms lacking either the amino- or carboxyl-terminal domains
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased. Caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
-
-
?
additional information
?
-
-
caspase-1 is the prototype of the inflammatory caspases and is a component of the NALP3 inflammasome, a cytosolic multiprotein complex that mediates the processing of pro-inflammatory caspases and cytokines. The inflammasome represents the first line of defense against cellular stress and is a crucial component of innate immunity. Caspase-1 plays a central role in the mechanisms leading to labor particularly in the context of intrauterine infection/inflammation. Caspase-1 is increased in the amniotic fluid of women with preterm labor in the presence of intra-amniotic infection/inflammation
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, inflammasome regulation system, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta. Infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC
-
-
?
additional information
?
-
-
mevalonate kinase deficiency patients have overactive caspase-1, causing enhanced interleukin-1beta processing and subsequent inflammation in response to bacterial components
-
-
?
additional information
?
-
-
Nod-like receptors induce assembling of the inflammasome multiprotein complexes to activate caspase-1 in response to microbial and danger signals, overview. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock, a physiological posttranslational mechanism, overview. Redox-sensitive cysteine residues regulate caspase-1 to identify the redox-sensitive cysteine residues in caspase
-
-
?
additional information
?
-
-
pro-inflammatory cytokine interleukin-18 and its activator caspase-1 are involved in acute liver failure and acute-on-chronicliver-failure
-
-
?
additional information
?
-
-
pyrin and caspase-1 interact in their pathway for NF-kappaB activation, mechanism and regulation, overview
-
-
?
additional information
?
-
-
the downstream signaling pathway of TLR7 and TLR8 in monocytes and dendritic cells after stimulation with specific ligands included not only the secretion of cytokines, such as TNFalpha and interleukin-1beta, but as well the activation of necessary regulating proteins like caspase-1
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
caspase-1-cleaved peptides show propensity for hydrophobic residues at P4
-
-
?
additional information
?
-
-
phenotype of aninmals deficient in caspase-1: defective lipopolysaccharide-induced secretion of interleukin-1alpha and interleukin-beta and gamma-interferon, resists endotoxic shock, thymocytes partially resistant to Fas-mediated apoptosis
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
bone marrow derived. Anthrax lethal toxin and Salmonella elicit the common cell death pathway of caspase-1-dependent pyroptosis via distinct mechanisms. Activation of caspase-1 by Bacillus anthracis lethal toxin requires binding, uptake, and endosome acidification to mediate translocation of lethal factor into the host cell cytosol. Catalytically active lethal factor cleaves cytosolic substrates and activates caspase-1 by a mechanism involving proteasome activity and potassium efflux. Lethal toxin activation of caspase-1 requires the inflammasome adapter Nalp1. Salmonella infection activates caspase-1 through an independent pathway requiring the inflammasome adapter Ipaf. These distinct mechanisms of caspase-1 activation converge on a common pathway of caspase-1-dependent cell death featuring DNA cleavage, cytokine activation, and, ultimately, cell lysis resulting from the formation of membrane pores between 1.1 and 2.4 nm in diameter and pathological ion fluxes that can be blocked by glycine
-
-
?
additional information
?
-
-
caspase-1 is critical for IFN-gamma-mediated control of Anaplasma phagocytophilum infection
-
-
?
additional information
?
-
-
caspase-1 is important in the host response to sepsis at least in part via its ability to regulate sepsis-induced splenic cell apoptosis
-
-
?
additional information
?
-
-
caspase-1 is involved in ER/Golgi-independent protein secretion. Caspase-1 activation by the inflammasome is directly linked to IL-1a secretion from activated macrophages and UV-irradiated keratinocytes. Secretion of FGF-2 also depends on caspase-1 expression and activity. Both proteins bind to caspase-1, suggesting a role of the protease as a carrier in an ER/Golgi-independent protein secretion pathway. Secretion of caspase-1 itself requires enzymatic activity, and caspase-1 inhibition therefore prevents secretion of its binding proteins
-
-
?
additional information
?
-
-
caspase-1-mediated macrophage necrosis is the source of the cytokine storm and rapid disease progression in anthrax lethal toxin-treated BALB/c mice
-
-
?
additional information
?
-
-
functional role for caspase-1-mediated myocardial apoptosis contributing to the progression of heart failure
-
-
?
additional information
?
-
-
IRF-2 acts as a transcriptional repressor of Casp1. Absence of IRF-2 renders macrophages more sensitive to apoptotic stimuli in a caspase-1-dependent process
-
-
?
additional information
?
-
-
caspase-1 activation contributes to the development of nitrogen-containing bisphosphonate-associated inflammatory side effects including jaw osteomyelitis, overview
-
-
?
additional information
?
-
-
caspase-1 activation dependent on Nalp1b, an inflammasome component, mediates cell death after pathogen infection, e.g. of dendritic cells after infection by Bacillus anthracis and lethal anthrax toxin, overview. Some dendritic cells of a certain genotype follow a caspase-1-independent way of response to infection by Bacillus anthracis, overview
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
-
caspase-1 mediates cell death and secretion of interleukin-1beta in native macrophages infected with Yersinia enterocolitica and Yersinia pestis, but cell death occurs independently of caspase-1 in Yersinia pestis strain KIM5, while translocation of catalytically active bacterial YopJ into macrophages is required for caspase-1 activation and cell death, regulation, overview
-
-
?
additional information
?
-
-
caspase-1 mediates resistance in murine melioidosis, caused by gram-negative rod Burkholderia pseudomallei, which can induce caspase-1-dependent cell death in macrophages. Caspase-1-dependent rapid cell death might contribute to resistance by reducing the intracellular niche for Birkholderia pseudomallei, but, in addition, caspase-1 might also have a role in controlling intracellular replication of Burkholderia pseudomallei in macrophages
-
-
?
additional information
?
-
-
caspase-1 promotes the maturation of proinflammatory cytokines interleukin-1beta and interleukin-18
-
-
?
additional information
?
-
-
critical involvement of pneumolysin in production of interleukin-1alpha and caspase-1-dependent cytokines in infection with Streptococcus pneumoniae in vitro
-
-
?
additional information
?
-
-
enzyme regulation, mechanisms of ATP-induced and caspase-1-dependent cell death and interleukin-1beta release are both regulated by zinc, overview
-
-
?
additional information
?
-
-
inflammasomes, multiprotein complexes, regulate caspase-1-activation, requiring members of the Nod-like receptor family, including NLRP1, NLRP3 and NLRC4, and the adaptor ASC, and playing a role in regulation of immune responses and disease pathogenesis, recognition mechanisms, overview. Several diseases are associated with dysregulated activation of caspase-1 and secretion of interleukin-1beta
-
-
?
additional information
?
-
-
the enzyme is involved in the cytokine metabolism, cryopyrin and caspase-1 are central to both innate immunity and to moderating lung pathology in influenza pneumonia, absence of cryopyrin and caspase-1, but not Ipaf, is associated with greater mortality, regulation, overview
-
-
?
additional information
?
-
-
the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1. Proteins encoded by the nucleotide-binding domain and leucine-rich repeat, NLR, containing gene family form the central components of inflammasomes and act as intracellular sensors to detect cytosolic microbial components and danger signals, such as ATP and toxins, detailed overview. NLRs consist of three domains, besides others an N-terminal region including protein interaction domains such as the caspase recruitment domain
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
additional information
?
-
the enzyme induces apoptosis in transfected cells
-
-
?
additional information
?
-
-
caspase-1 activation is a key feature of the innate immune response of macrophages elicited by pathogens and a variety of toxins
-
-
?
additional information
?
-
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2
-
-
?
additional information
?
-
-
the inflammasome regulatory proteins, ASC or apoptosis-associated speck-like protein containing a caspase-recruitment domain, and NLRP3 or NLR family, pyrin domain containing 3, are essential for caspase-1 activation, and also for P2X7 receptor-stimulated secretion of MHC class II-containing exosomes requires the ASC/NLRP3 inflammasome, which is, however, independent of caspase-1, overview
-
-
?
additional information
?
-
-
caspase-1 is activated by the inflammasomes and is responsible for the proteolytic maturation of the cytokines interleukin-1beta and interleukin-18 during infection and inflammation
-
-
?
additional information
?
-
-
caspase-1 is a negative regulator of AMPA receptor-mediated long-term potentiation at hippocampal synapses
-
-
?
additional information
?
-
-
in brain microvascular endothelial cells and in astrocytes expression and activity of inducible nitric axide synthase exclusively depends on the endogenous availability of bioactive interleukin-1beta as inhibition of ICE activity significantly decreases promoter activity of inducible nitric axide synthase, expression and enzyme activity
-
-
?
additional information
?
-
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
-
?
additional information
?
-
-
caspase-1 is crucial in mediating neuronal apoptosis and inflammation after mechanical trauma, upregulated caspase-1 in the hours after trauma precedes neuron loss and mRNA and protein levels of interleukin-1beta and interleukin-18 are also increased
-
-
?
additional information
?
-
the enzyme is able to induce apoptosis in Sf9 cells
-
-
?
additional information
?
-
-
the enzyme is able to induce apoptosis in Sf9 cells
-
-
?
additional information
?
-
-
caspase-1 is involved in this apoptosis
-
-
?
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(1S,9S)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepine-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
(3)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-3-((6-[((4-[(6-chloropyrazin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
(3S)-3-((6-[((4-[(6-methylquinoxalin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
(3S)-3-([2-(2-fluorophenyl)-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-([2-ethyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-([6-(([3-methyl-4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)-4-oxobutanoic acid
-
-
(3S)-3-[([(1S,9S)-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepin-1-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-3-[([(3S,6S,9aR)-6-[(isoquinolin-1-ylcarbonyl)amino]-5-oxo-2,3,5,6,9,9a-hexahydro-1H-pyrrolo[1,2-a]azepin-3-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-3-[([(4S,7S,10aS)-7-[(isoquinolin-1-ylcarbonyl)amino]-6-oxo-3,4,6,7,10,10a-hexahydro-1H-[1,4]oxazino[4,3-a]azepin-4-yl]carbonyl)amino]-4-oxobutanoic acid
-
-
(3S)-4-oxo-3-([2-phenyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([4-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)butanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([5-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)pentanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]phenyl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]-2,3-dihydropyrazin-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]furan-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)acetyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-3-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((6-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]pyridin-3-yl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[((trans-4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]cyclohexyl)carbonyl)amino]butanoic acid
-
-
(3S)-4-oxo-3-[(7-oxo-7-([4-(quinoxalin-2-ylamino)phenyl]amino)heptanoyl)amino]butanoic acid
-
-
(S)-2-(4'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-((S)-2-((S)-2-(2-naphthamido)-3-methylbutanamido)-propanamido)-4-(2-hydroxy)benzylaminobutanoic acid
-
-
(S)-3-(2'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(2-naphthalen-1-yl-benzenesulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(3'-acetylamino-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(3'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(6-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
(S)-3-(biphenyl-2-sulfonylamino)-4-oxobutyric acid
-
-
(S)-3-benzenesulfonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
(S)-3-benzenesulfonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
(S)-3-benzyloxycarbonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
(S)-3-benzynesulfonylamino-4-oxo-butyric acid
-
-
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
-
-
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
3-(benzyloxycarbonylamino)-5-((2,3-dihydro-1H-inden-1-yl)methylsulfanylamido)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-4-oxo-9-phenylnonanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([(2-cyclohexylethyl)(dihydroxy)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-naphthalen-1-ylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(3-phenylpropyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(naphthalen-1-yl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(phenyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
3-[[(benzyloxy)carbonyl]amino]-5-[[(2-cyclohexylethyl)sulfonyl]amino]-4-oxopentanoic acid
-
-
4-hydroxy-4,5-dicarboxypentadecanoic acid
-
-
5-([benzyl(dihydroxy)-lambda4-sulfanyl]amino)-3-([(benzyloxy)carbonyl]amino)-4-oxopentanoic acid
-
-
Ac-WEHD-CHO
-
active-site inhibitor
Ac-YVAD-chloromethyl ketone
-
-
Ac-YVAD-chloromethylketone
-
inhibition of caspase-1 with Ac-YVAD-CMK prevents SphK2 cleavage
Ac-YVAD-CHO
-
a caspase-1 inhibitor
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
-
acetyl-L-Leu-L-Glu-L-His-L-Asp-CHO
-
-
acetyl-L-Tyr-L-Val-L-Ala-L-Asp
-
-
acetyl-L-Tyr-L-Val-L-Ala-L-Asp-2,6-dimethylbenzoyloxymethylketone
-
-
acetyl-Tyr-Val-Ala-Asp chloromethyl ketone
-
inhibition of caspase-1 in rat brain reduces spontaneous nonrapid eye movement sleep and nonrapid eye movement sleep enhancement induced by lipopolysaccharide
acetyl-Tyr-Val-Ala-Asp-chloromethylketone
acetyl-Tyr-Val-Ala-Asp-CHO
-
-
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
-
acetyl-YVAD-chloromethylketone
-
-
acetyl-YVAD-CHO
caspase-1 specific inhibitor
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
-
benzyloxycarbonyl-VAD-CHO
-
-
benzyloxycarbonyl-VAD-fluoromethylketone
-
t1/2 at 0.001 mM is 2.5 s
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
benzyloxycarbonyl-YVAD-fluoromethylketone
-
-
butyloxycarbonyl-Asp-chloromethylketone
-
-
butyloxycarbonyl-Asp-fluoromethylketone
-
-
CA-074Me
-
the caspase-1 activation is inhibited by CA-074Me, marked inhibition at 0.05 mM
carbobenzoxy-L-valyl-L-alanyl-L-aspartyl-[O-methyl]-fluoromethylketone
-
caspase-1-specific inhibitor
carbobenzoxy-valylalanyl-aspartyl-fluoromethylketone
-
-
carbobenzyloxy-Asp-Glu-Val-Asp-fluoromethyl ketone
-
specific to suppress the activity of Sf-caspase-1 by blocking amplification of Sfcaspase-1
carbobenzyloxy-Trp-Glu-His-Asp-fluoromethylketone
-
-
carbobenzyloxy-VAD-fluoromethyl ketone
carbobenzyloxy-Val-Ala-Asp-fluoromethyl ketone
-
a broad-spectrum inhibitor of initiator caspase
carbobenzyloxy-WEHD-fluoromethyl ketone
-
caspase-1-specific inhibitor
carboxyfluorescein-YVAD-fluoromethylketone
-
-
Cbz-Val-Asp-fluoromethylketone
-
increase in IL-1beta protein levels in a liver injury mouse model is completely prevented with the pan-caspase inhibitor demonstrating the efficacy of Cbz-Val-Asp-fluoromethylketone to block caspase-1 activity
DEVD-fluoromethylketone
-
-
E-64d
-
the caspase-1 activation is inhibited by E-64d, marked inhibition at 0.05 mM
flightless-I
-
inhibits caspase-1 as a pseudosubstrate. Flightless-I might function as an inhibitor of caspase-1 in living cells through a mechanism similar to that of CrmA
-
geranylgeranyl diphosphate
-
the isoprenyl intermediate of non-sterol isoprenoid biosynthesis blocks activation of caspase-1
L-Tyr-L-Val-L-Ala-L-Asp-chloromethylketone
-
-
L-Tyr-L-Val-L-Ala-L-Asp-CHO
-
caspase-1-specific inhibitor
L-Tyr-L-Val-L-Ala-L-Asp-CN
-
-
N-((S,Z)-1-((R)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
-
N-((S,Z)-1-((S)-1-((3S)-2-ethoxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
good oral bioavailability (more than 50%) when administered as prodrug
N-((S,Z)-1-((S)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
-
N-((S,Z)-1-(2-((3S)-2-ethoxy-5-oxo-tetrahydrofuran-3-ylamino)-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
-
good oral bioavailability (more than 50%) when administered as prodrug
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2R)-1-carboxy-5-phenylpentan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-(benzylamino)-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-(cyclohexylamino)propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-oxopropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-fluorobenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-methoxybenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(4-hydroxybenzyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[methyl(phenyl)amino]propan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(1,3-benzodioxol-5-ylmethyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(4-carbamoylbenzyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[benzyl(methyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
-
N-([4-(quinoxalin-2-ylamino)phenyl]carbonyl)-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide
-
-
N-acetyl-L-tyrosyl-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
N-acetyl-L-tyrosylvalyl-N-[1-(carboxymethyl)-2-oxo-7-phenylheptyl]-L-alaninamide
-
-
N-benzyloxycarbonyl-Tyr-Val-Ala-Asp-fluoromethyl ketone
-
-
N-benzyloxycarbonyl-Val-Ala-Asp(O-Me) fluoromethylketone
-
-
N-carbobenzyloxy-Val-Ala-Asp-fluoromethylketone
-
i.e. Z-VAD-FMK, active-site inhibitor
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-1-benzothiophene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-(trifluoromethyl)benzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-methoxybenzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]isoquinoline-1-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylcarbonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylsulfonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(2-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(3-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(4-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-methyl-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
-
-
N-[(3S)-6-(hydroxymethyl)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
-
-
N-[(3S,5Z)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-1,2,3,4,7,8-hexahydroazocin-3-yl]isoquinoline-1-carboxamide
-
-
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-3-(trifluoromethyl)benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]benzamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
-
good selectivity against the related enzymes caspase-3 and caspase-8
N-[(benzyloxy)carbonyl]-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
N-[(benzyloxy)carbonyl]valyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
NCGC00183434
-
i.e. (S)-3-((S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)pyrrolidine-2-carboxamido)-3-cyanopropanoic acid, competitive inhibition
NCGC00183681
-
i.e. (S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)-N-((S)-1-cyano-2-(1H-tetrazol-5-yl)ethyl)pyrrolidine-2-carboxamide
NCGC00185682
-
i.e. 3-((S)-1-((S)-2-(4-amino-3-chlorobenzamido)-3,3-dimethylbutanoyl)pyrrolidine-2-carboxamido)-3-cyanopropanoate
secospiculisporic acid
-
-
serpin proteinase inhibitor 9
-
endogenous inhibitor of caspase-1 activity in human vascular smooth muscle cells
-
superoxide
-
superoxide production decreases the cellular redox potential and specifically inhibites caspase-1 by reversible oxidation and glutathionylation of the redox-sensitive cysteine residues Cys397 and Cys362
YN-1234
-
i.e. N-2-naphthoyl-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-prolinamide
YVAD-chloromethyl ketone
-
-
YVAD-chloromethylketone
-
-
Z-L-Tyr-L-Val-L-Ala-L-Asp-fluoromethylketone
-
specific inhibitor for caspase-1, complete inhibition at 0.05 mM
Z-L-Val-L-Ala-L-Asp-(O-methyl)-fluoromethylketone
-
-
Z-L-Val-L-Ala-L-Asp-fluoromethylketone
-
broad-spectrum caspase inhibitor
Z-Trp-Glu-His-Asp-fluoromethylketone
-
-
Z-Val-Ala-Asp-fluoromethylketone
Z-WEHD-fluoromethylketone
-
-
Z-YVAD-fluoromethylketone
-
-
acetyl-DEVD-aldehyde
-
-
acetyl-Tyr-Val-Ala-Asp-chloromethylketone
-
-
acetyl-Tyr-Val-Ala-Asp-chloromethylketone
-
-
acetyl-YVAD-aldehyde
-
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
irreversible active site inhibitor
benzyloxycarbonyl-Val-Ala-Asp-fluoromethylketone
-
-
carbobenzyloxy-VAD-fluoromethyl ketone
-
pan-caspase inhibitor
carbobenzyloxy-VAD-fluoromethyl ketone
-
pan-caspase inhibitor
Disulfiram
-
inhibits the enzyme
Disulfiram
-
inhibits the enzyme
Disulfiram
-
inhibits the enzyme
IDN-6556
-
active-site inhibitor that acts through irreversible covalent modification of the catalytic cysteine residue
pralnacasan
-
-
pralnacasan
-
a specific caspase-1 inhibitor
pralnacasan
-
VX-740, active-site inhibitor that acts through reversible covalent modification of the catalytic cysteine residue
pralnacasan
-
potent caspase 1 inhibitor
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
ritonavir
-
blocks caspase-1 activation and inhibits the enzyme
Z-Val-Ala-Asp-fluoromethylketone
-
broad-range caspase inhibitor
Z-Val-Ala-Asp-fluoromethylketone
-
-
Z-Val-Ala-Asp-fluoromethylketone
-
-
additional information
-
a dominant-negative form of the adaptor protein ASC in THP-1 cells blocks LPS-stimulated caspase-1 activation and interleukin-1beta secretion
-
additional information
-
allosteric inhibitors in caspase-1 directly disrupt the hydrogen bond network by preventing the salt bridge between Arg286 and Glu390 from forming
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
additional information
-
hypoxia abrogates caspase-1 inhibition, overview
-
additional information
-
caspase-1 is not inhibited by Asp-Glu-Val-Asp-CHO, Ile-Glu-Thr-Asp-CHO, and Leu-Glu-His-Asp-CHO
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
heat shock inhibits caspase-1 activity while also preventing its Nalp1b or NLRP1b inflammasome-mediated or nigericin-induced activation by anthrax lethal toxin, but once caspase-1 activation is initiated, heat shock is ineffective, time dependence, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
additional information
-
caspase 1 inhibitors share sequence similarity to CASP-1 itself and are all mapped to chr11q22.3, overview
-
additional information
-
caspase inhibition enhances neuronal survivability or protection
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adapter protein Asc
-
is important for caspase-1 activation during Legionella pneumophila infection, mechanism, overview. Activation of caspase-1 through Asc does not require the flagellin-sensing pathway involving the host nucleotide-binding domain and leucine-rich repeat-containing protein Ipaf, NLRC4. Asc-dependent caspase-1 activation is inhibited by high extracellular potassium levels
-
alendronate
-
a nitrogen-containing bisphosphonate, activates caspase-1, activation is inhibited by clodronate. Pretreatment of cells with alendronate augments interleukin-1beta production stimulated by Toll-like receptor ligands, augmentation is inhibited by clodronate
anthrax lethal toxin
-
rapidly activates caspase-1/interleukin-1beta-converting enzyme and induces extracellular release of interleukin-1beta and interleukin-18
-
cathepsin B
-
cathepsin B can effectively cleave and activate pro-caspase-1 in a cell-free system only at an acidic pH and in THP-1 monocytic cells after stimulation with the microbial toxin nigericin
-
chromogranin A
-
chromogranin A can activate pro-caspase-1 in microglia
-
Ipaf
-
i.e. host nucleotide-binding domain and leucine-rich repeatcontaining protein Ipaf or NLRC4, Ipaf-dependent activation is unaffected by potassium treatment
-
Nalp1b
-
an inflammasome component is required for caspase-1 activation, Nalp1b is a member of the NOD-like receptor family, NLR, a family of cytoplasmic proteins involved in the recognition of microbial products or danger signals. Nalp1b has a caspase recruitment domain, CARD, that allows it to interact with caspase-1
-
NOD2
-
NOD2 through its N-terminal caspase recruitment domain directly binds and activates caspase-1 to trigger interleukin-1beta processing and secretion in muramyl dipeptide-stimulated macrophages, whereas the C-terminal leucine-rich repeats of NOD2 prevent caspase-1 activation in nonstimulated cells
-
protease activating factor
-
i.e. Ipaf. Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
-
protease-activating factor
-
activates caspase 1 in p53-dependent apoptosis
-
simvastatin
-
blocks inhibition of caspase-1 activation, simvastatin acts synergistically with lipopolysaccharides and causes an impairment of non-sterol isoprenoid biosynthesis, the isoprenyl intermediate GGPP could block activation of caspase-1 and interleukin-1beta release, overview
thalidomide
-
thalidomide inhibits activation and activity of caspase-1 in cultured cells but not in vitro
additional information
-
activation of the Rac1/PI3K/protein kinase B pathway is required for caspase-1 activation mediating increased interleukin-1beta release
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
-
caspase-1 activation is induced by ATP and lipopolysaccharides
-
additional information
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
additional information
-
caspase-1 activation is stimulated by ATP and 120fold lipopolysaccharides
-
additional information
-
caspase-1 activation pathways and regulation, detailed overview. Many Gram-negative bacteria, such as Salmonella typhimurium, Pseudomonas aeruginosa, Shigella flexneri, and Legionella pneumophila, can induce caspase-1 activation and rapid macrophage cell death, the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1, e.g. besides T3SS and flagellin, the host factor NLRC4 is also required for activation of caspase-1 by Salmonella typhimurium or Pseudomonas aeruginosa. Lipopolysaccharide-stimulated caspase-1 activation. Caspase-1 activation by NLRP1 does not require but is enhanced by adaptor protein ASC
-
additional information
-
caspase-1 is activated and central to neuronal damage in disparate brain injuring events: neonatal exposure to high O2 levels, cold injury, ischemic injury, excitotoxic injury, acceleration injury, the neurotoxic recreational drug methylenedioxymethamphetamine, MDMA, and others
-
additional information
-
infection of macrophages with several Gram-negative bacteria, including Salmonella typhimurium, Legionella pneumophila and Pseudomonas aeruginosa, activates caspase-1 via NLRC4 and ASC, Listeria monocytogenes induces caspase-1 activation through both the NLRC4 and NLRP3 inflammasomes
-
additional information
-
TLR7 and TLR8 ligands and antiphospholipid antibodies show synergistic effects on the induction of IL-1beta and caspase-1 in monocytes and dendritic cells
-
additional information
-
transcription of caspase-1 gene is increased upon lipopolysaccharide and interferon-gamma stimulation
-
additional information
-
Bacillus anthracis poly-gamma-D-glutamic acid capsule activates caspase-1
-
additional information
-
caspase-1 is activated in innate immune complexes called inflammasomes
-
additional information
-
infection of cervical epithelial cells by Chlamydia trachomatis leads to activation of caspase-1, through a process requiring the NOD-like receptor family member NLRP3 and the inflammasome adaptor protein ASC. Elevated levels of reactive oxygen species as a result of K+ efflux are responsible for NLRP3-dependent caspase-1 activation in the infected cells
-
additional information
-
the inflammasome activator ATP can induce the production of reactive oxygen species, which are important for caspase-1 activation
-
additional information
substrate binding increases the dimerization affinity and activity of caspase-1
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
-
activation of caspase-1 in macrophages occurs independently of Nalp3 and proteasome activity
-
additional information
-
activation of caspase-1 is induced in macrophages by Listeria monocytogenes infection depending on cytolysin and listeriolysin O, after evasion from phagosome into the cytoplasm, overview
-
additional information
-
ATP induces caspase-1 expression, P2X7R-deficient macrophages exhibit no caspase-1 activation response to extracellular ATP. ATP-induced caspase-1 inflammasome activation and interleukin-1beta maturation are strictly dependent on lipopolysaccharides priming of dendritic cells before ATP stimulation
-
additional information
-
caspase-1 activation in macrophages infected with Yersinia pestis KIM requires the type III secretion system effector YopJ. Yersinia pestis KIM5 strain displays an unusual ability to activate caspase-1 and kill infected macrophages compared to other Yersinia pestis and Yersinia pseudotuberculosis strains
-
additional information
-
caspase-1 activation induced by MDP and ATP requires pore-forming pannexin-1, for delivery of the inducer MDP into the cell, and cryopyrin but is independent of Nod2 and NF-kappaB and MAPK signaling
-
additional information
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
additional information
-
caspase-1 activation pathways and regulation, detailed overview. Many Gram-negative bacteria, such as Salmonella typhimurium, Pseudomonas aeruginosa, Shigella flexneri, and Legionella pneumophila, can induce caspase-1 activation and rapid macrophage cell death, the inflammasome is a large multiprotein complex whose assembly leads to the activation of caspase-1
-
additional information
-
caspase-1 is activated in macrophages stimulated with recombinant of pneumolysin but not in those stimulated with lipopolysaccharide, and the level of activation is higher in macrophages infected with wild-type Streptococcus pneumoniae serotype 2 strain D39 than in those infected with the DELTAply mutant
-
additional information
-
infection with periodontal pathogenic bacteria, e.g. Porphyromonas gingivalis and Tannerella forsythia, leads to activation of caspase-1 in macrophages, augmented by alendronate
-
additional information
-
nigericin-induces caspase-1 activation. Nalp1b or NLRP1b inflammasome-mediated activation of caspase-1 by anthrax lethal toxin, prevented by heat shock, overview
-
additional information
-
pannexin-1-dependent caspase-1 activation is regulated by zinc and induced by ATP, molecular mechanism
-
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 by caspase-1. Caspase-1 activation involves pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
-
additional information
-
some members of the nucleotide-binding domain and leucine-rich-repeat-containing, NLR, gene family, including ipaf and cryopyrin, induce caspase-1 activation and the release of the interleukin-1beta and interleukin-18 through the assembly of large protein complexes called inflammasomes
-
additional information
-
association of RIP2 with CASP-1 via their homologous CARD domain accelerates the processing of CASP-1 into an active enzyme
-
additional information
-
caspase-1 activation is mediated and regulated by inflammasomes, AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC, i.e. apoptosis-associated speck-like protein containing a caspase activation and recruitment domain. the PYHIN, i.e. pyrin and HIN domain-containing protein acts as a receptor for cytosolic DNA, which regulates caspase-1. The HIN200 domain of AIM2 binds to DNA, whereas the pyrin domain, but not that of the other PYHIN family members, associates with the adaptor molecule ASC to activate both NF-kappaB and caspase-1. Knockdown of Aim2 abrogates caspase-1 activation in response to cytoplasmic double-stranded DNA and the double-stranded DNA vaccinia virus
-
additional information
-
the enzyme and apoptosis in SF-21 cell line are induced by the conditioned medium of the entomopathogenic fungus, Nomuraea rileyi, cell phenotype, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.000054
(3S)-3-((6-[((4-[(6-chloropyrazin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-3-((6-[((4-[(6-methylquinoxalin-2-yl)amino]phenyl)carbonyl)amino]-2-thiophen-2-ylhexanoyl)amino)-4-oxobutanoic acid
-
-
0.000008
(3S)-3-([2-(2-fluorophenyl)-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000016
(3S)-3-([2-ethyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)-4-oxobutanoic acid
-
-
0.000004
(3S)-3-([6-(([3-methyl-4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)-4-oxobutanoic acid
-
-
0.000005
(3S)-4-oxo-3-([2-phenyl-6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.0052
(3S)-4-oxo-3-([4-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)butanoyl]amino)butanoic acid
-
-
0.0028
(3S)-4-oxo-3-([5-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)pentanoyl]amino)butanoic acid
-
-
0.0001
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.037
(3S)-4-oxo-3-([6-(([4-(pyrazin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.00019
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000043 - 0.00032
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
0.0024
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)hexanoyl]amino)butanoic acid
-
-
0.000005 - 0.0026
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
0.0001
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]phenyl)carbonyl)amino]butanoic acid
-
-
0.00026
(3S)-4-oxo-3-[((4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.001
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]-2,3-dihydropyrazin-2-yl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]furan-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)acetyl)amino]butanoic acid
-
-
0.000035
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-2-yl)carbonyl)amino]butanoic acid
-
-
0.00012
(3S)-4-oxo-3-[((5-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]thiophen-3-yl)carbonyl)amino]butanoic acid
-
-
0.000005
(3S)-4-oxo-3-[((6-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]pyridin-3-yl)carbonyl)amino]butanoic acid
-
-
0.00195
(3S)-4-oxo-3-[((trans-4-[(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)methyl]cyclohexyl)carbonyl)amino]butanoic acid
-
-
0.0021
(3S)-4-oxo-3-[(7-oxo-7-([4-(quinoxalin-2-ylamino)phenyl]amino)heptanoyl)amino]butanoic acid
-
-
0.0072
(S)-2-(4'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.000047
(S)-3-((S)-2-((S)-2-(2-naphthamido)-3-methylbutanamido)-propanamido)-4-(2-hydroxy)benzylaminobutanoic acid
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0068
(S)-3-(2'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0069
(S)-3-(2-naphthalen-1-yl-benzenesulfonylamino)-4-oxo-butyric acid
-
-
0.0023
(S)-3-(3'-acetylamino-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0031
(S)-3-(3'-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0019
(S)-3-(6-methyl-biphenyl-2-sulfonylamino)-4-oxo-butyric acid
-
-
0.0016
(S)-3-(biphenyl-2-sulfonylamino)-4-oxobutyric acid
-
-
0.024
(S)-3-benzenesulfonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.024
(S)-3-benzenesulfonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
0.025
(S)-3-benzyloxycarbonylamino-4-oxo-5-(3-phenyl-propylsulfanyl)-pentanoic acid
-
-
0.119
(S)-3-benzyloxycarbonylamino-4-oxo-9-phenyl-nonanoic acid
-
-
0.0094
(S)-3-benzynesulfonylamino-4-oxo-butyric acid
-
-
0.119
3-([(benzyloxy)carbonyl]amino)-4-oxo-9-phenylnonanoic acid
-
-
0.065
3-([(benzyloxy)carbonyl]amino)-5-([(2,3-dihydro-1H-inden-1-ylmethyl)(dihydroxy)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.016
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-naphthalen-1-ylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.011
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.0345
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(3-phenylpropyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.022
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(naphthalen-1-yl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.037
3-([(benzyloxy)carbonyl]amino)-5-([dihydroxy(phenyl)-lambda4-sulfanyl]amino)-4-oxopentanoic acid
-
-
0.033
3-[[(benzyloxy)carbonyl]amino]-5-[[(2-cyclohexylethyl)sulfonyl]amino]-4-oxopentanoic acid
-
-
0.018
5-([benzyl(dihydroxy)-lambda4-sulfanyl]amino)-3-([(benzyloxy)carbonyl]amino)-4-oxopentanoic acid
-
-
0.083
acetyl-Ala-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.000015 - 0.000018
acetyl-DEVD-aldehyde
0.00002
acetyl-DEVS-aldehyde
-
pH 7.5, 37°C
0.000011
acetyl-Tyr-Val-Ala-Asp-CO-(CH2)5-Ph
-
pH 7.5
0.000000056
acetyl-WEHD-aldehyde
-
pH 7.5, 25°C
0.00000076 - 0.000006
acetyl-YVAD-aldehyde
0.03
benzyloxycarbonyl-Pro-Nle-Asp-aldehyde
-
pH 7.5
0.000008
benzyloxycarbonyl-VAD-CHO
-
-
0.00000001
cowpox serpin CrmA
-
pH 7.5, 25°C
-
0.00036
Glu-Val-Asp-aldehyde
pH 7.5
0.3
kaempferol
-
pH not specified in the publication, 30°C, value above
0.118
luteolin
-
pH not specified in the publication, 30°C
0.014
myricetin
-
pH not specified in the publication, 30°C
0.05
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2R)-1-carboxy-5-phenylpentan-2-yl]-L-alaninamide
-
IC50 above 0.05 mM, in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0006
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-(benzylamino)-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000945
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-(cyclohexylamino)propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.0012
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-fluorobenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000965
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(2-methoxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00137
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[(4-hydroxybenzyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000128
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-carboxy-3-[methyl(phenyl)amino]propan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00029
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(1,3-benzodioxol-5-ylmethyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00182
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[(4-carbamoylbenzyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.00189
N-(naphthalen-2-ylcarbonyl)-L-valyl-N-[(2S)-1-[benzyl(methyl)amino]-3-carboxypropan-2-yl]-L-alaninamide
-
in 50 mM HEPES, pH 7.4, 100 mM NaCl, 10 mM dithiothreitol, 1 mM EDTA, 10% (v/v) glycerol, 0.1% (v/v) CHAPS, 1% (v/v) DMSO, at 30°C
0.000004
N-([4-(quinoxalin-2-ylamino)phenyl]carbonyl)-L-valyl-N-[(1S)-2-carboxy-1-formylethyl]-L-alaninamide
-
-
0.000004
N-acetyl-L-tyrosyl-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000014
N-acetyl-L-tyrosylvalyl-N-[1-(carboxymethyl)-2-oxo-7-phenylheptyl]-L-alaninamide
-
-
0.0000239
N-[(benzyloxy)carbonyl]-alpha-glutamyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.000004
N-[(benzyloxy)carbonyl]valyl-N-[1-(carboxymethyl)-3-([dihydroxy(2-phenylethyl)-lambda4-sulfanyl]amino)-2-oxopropyl]-L-alaninamide
-
-
0.0000004
NCGC00183434
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.3
quercetin
-
pH not specified in the publication, 30°C, value above
additional information
additional information
-
the Ki-value for acetyl-IETD-aldehyde is below 6 nM and the Ki-value for acetyl-AEVD-aldehyde is below 12 nM
-
0.000043
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.00032
(3S)-4-oxo-3-([6-(([4-(quinoxalin-2-yloxy)phenyl]carbonyl)amino)-2-thiophen-2-ylhexanoyl]amino)butanoic acid
-
-
0.000005
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
0.0026
(3S)-4-oxo-3-([7-(([4-(quinoxalin-2-ylamino)phenyl]carbonyl)amino)heptanoyl]amino)butanoic acid
-
-
0.000015
acetyl-DEVD-aldehyde
pH 7.5
0.000018
acetyl-DEVD-aldehyde
-
pH 7.5, 25°C
0.00000076
acetyl-YVAD-aldehyde
-
pH 7.5, 25°C
0.000001
acetyl-YVAD-aldehyde
-
pH 7.5, 37°C
0.000006
acetyl-YVAD-aldehyde
pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0000036
(1S,9S)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepine-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000004
(3S)-3-[([(1S,9S)-9-[(isoquinolin-1-ylcarbonyl)amino]-6,10-dioxooctahydro-6H-pyridazino[1,2-a][1,2]diazepin-1-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000004
(3S)-3-[([(3S,6S,9aR)-6-[(isoquinolin-1-ylcarbonyl)amino]-5-oxo-2,3,5,6,9,9a-hexahydro-1H-pyrrolo[1,2-a]azepin-3-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.000003
(3S)-3-[([(4S,7S,10aS)-7-[(isoquinolin-1-ylcarbonyl)amino]-6-oxo-3,4,6,7,10,10a-hexahydro-1H-[1,4]oxazino[4,3-a]azepin-4-yl]carbonyl)amino]-4-oxobutanoic acid
Homo sapiens
-
-
0.0007
1-([2-[(2,6-dimethoxyphenyl)carbonyl]hydrazino]carbonyl)-N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]cyclohexanecarboxamide
Homo sapiens
-
-
0.000007 - 0.000015
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000008 - 0.000029
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
0.000015
acetyl-L-Leu-L-Glu-L-His-L-Asp-CHO
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.1
berkedrimane A
Homo sapiens
-
at 37°C, pH not specified in the publication
0.09
berkedrimane B
Homo sapiens
-
at 37°C, pH not specified in the publication
0.00001
L-Tyr-L-Val-L-Ala-L-Asp-CHO
Homo sapiens
-
-
0.0000216
L-Tyr-L-Val-L-Ala-L-Asp-CN
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000001
N-((S,Z)-1-((R)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.000013
N-((S,Z)-1-((S)-1-((3S)-2-hydroxy-5-oxo-tetrahydrofuran-3-ylamino)-1-oxopropan-2-yl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl)-2-naphthamide
Homo sapiens
-
-
0.00002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
-
0.000011
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
-
0.000053
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]-3-methoxybenzamide
Homo sapiens
-
-
0.000168
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000027
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.000014
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylcarbonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000003
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-6-[[(phenylsulfonyl)amino]methyl]-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000002
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(2-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(3-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000001
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-([[(4-methoxyphenyl)carbonyl]amino]methyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000019
N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-6-methyl-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.0002
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methoxyphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclohexanecarboxamide
Homo sapiens
-
-
0.00049
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)cyclopentanecarboxamide
Homo sapiens
-
-
0.00031
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.0029
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(2-naphthoyl)hydrazino]carbonyl]cyclopropanecarboxamide
Homo sapiens
-
-
0.00026
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methoxybenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(3-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00058
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(4-methylbenzoyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00005
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.0004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00024
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclobutanecarboxamide
Homo sapiens
-
-
0.00009
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclohexanecarboxamide
Homo sapiens
-
-
0.00015
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-1-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]cyclopentanecarboxamide
Homo sapiens
-
-
0.00043
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-([2-[(3-methylphenyl)carbonyl]hydrazino]carbonyl)-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00004
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-1-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.00003
N-[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]-2-[[2-(naphthalen-2-ylcarbonyl)hydrazino]carbonyl]-2,3-dihydro-1H-indene-2-carboxamide
Homo sapiens
-
-
0.000022
N-[(3S)-6-(hydroxymethyl)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]naphthalene-2-carboxamide
Homo sapiens
-
-
0.000077
N-[(3S,5Z)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-1,2,3,4,7,8-hexahydroazocin-3-yl]isoquinoline-1-carboxamide
Homo sapiens
-
-
0.00032
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.0023
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00013
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00015
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-1,1-dioxido-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00008
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-1-benzothiophene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
9
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]-3-(trifluoromethyl)benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00035
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]benzamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00007
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]isoquinoline-1-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.00003
N-[(6R)-4-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-5-oxo-1,4-thiazepan-6-yl]naphthalene-2-carboxamide
Homo sapiens
-
good selectivity against the related enzymes caspase-3 and caspase-8
0.000000023
NCGC00183434
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.00000258
NCGC00183681
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000434
NCGC00185682
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.0000005
p35
Spodoptera frugiperda
IC50: 0.5 nM
-
0.0000036
pralnacasan
Homo sapiens
-
-
0.000000204
VRT-043198
Homo sapiens
-
in 50 mM HEPES, pH 7.4, containing 1 M sodium citrate, 100 mM NaCl, 0.1 mM EDTA, 10 mM dithiothreitol, 0.01% (v/v) CHAPS, 1% (v/v) DMSO, and 0.1 mg/ml bovine serum albumin
0.000024
YN-1234
Homo sapiens
-
-
0.000007
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000015
2,5-dichloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000008
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
0.000029
3-chloro-N-[(3S)-1-(2-[[(3S)-2-hydroxy-5-oxotetrahydrofuran-3-yl]amino]-2-oxoethyl)-2-oxo-2,3,4,7-tetrahydro-1H-azepin-3-yl]benzamide
Homo sapiens
-
-
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C136S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C169S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C244S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C270S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C331S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C362S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C362S/C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C364S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C397S
-
the mutant is hyperactive in normoxic conditions, while the activity of the mutant is similar to that of wild-type caspase-1 in hypoxic conditions
C69S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C72S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
C77S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
D297A
-
site-directed mutagenesis, mutation at the D297 residue abolishes the effect of caspase-1 on RIG-I
D316A
-
site-directed mutagenesis, mutation at the D316 residue does not abolish the effect of caspase-1 on RIG-I
D336A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
E390A
-
site-directed mutagenesis, the mutant shows an about 130fold loss of catalytic efficiency compared to the wild-type enzyme
N337A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
R286A
-
site-directed mutagenesis, the mutant shows an about 230fold loss of catalytic efficiency compared to the wild-type enzyme
R286K
-
site-directed mutagenesis, the mutant shows an about 150fold loss of catalytic efficiency compared to the wild-type enzyme
R286K/E390D
-
site-directed mutagenesis, the mutant shows an about 37fold loss of catalytic efficiency compared to the wild-type enzyme
S332A
-
site-directed mutagenesis, the mutant shows an about 4fold loss of catalytic efficiency compared to the wild-type enzyme
S333A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
S339A
-
site-directed mutagenesis, the mutant shows an about 7fold loss of catalytic efficiency compared to the wild-type enzyme
T334A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
T388A
-
site-directed mutagenesis, the mutant shows an about 2fold loss of catalytic efficiency compared to the wild-type enzyme
A329T
-
a procaspase-1 variant with decreased enzymatic activity
A329T
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
C285A
inactive
C285A
-
a procaspase-1 variant with decreased enzymatic activity showing about 3.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
C285A
active site null mutant
C285S
-
site-directed mutagenesis, in comparison to wild type procaspase-1, expression of the C285S mutant does not alter the cellular levels of the RIG-I protein
C285S
-
the mutant enzyme shows decreased activity compared to the wild-type enzyme
K319R
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.6fold increased nuclear factor-kappaB activation compared to the wild type enzyme
K319R
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
L265S
-
a procaspase-1 variant with decreased enzymatic activity showing about 6.5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
L265S
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
N263S
-
a procaspase-1 variant with decreased enzymatic activity showing about 1.8fold increased nuclear factor-kappaB activation compared to the wild type enzyme
N263S
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
R221C
-
a procaspase-1 variant with decreased enzymatic activity
R221C
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
R240Q
-
a procaspase-1 variant with decreased enzymatic activity showing about 5fold increased nuclear factor-kappaB activation compared to the wild type enzyme
R240Q
the mutant demonstrates decreased enzymatic and interleukin-1beta releasing activity in vitro
T267I
-
a procaspase-1 variant with decreased enzymatic activity
T267I
the mutant demonstrates absent enzymatic and interleukin-1beta releasing activity in vitro
additional information
-
caspase-1-/- bone marrow-derived macrophages exhibit strong caspase-3 expression and reduced cell damage compared to wild-type cells during early Burkholderia pseudomallei infection, indicating classical apoptosis, whereas wild-type bone marrow-derived macrophages show signs of rapid caspase-1-dependent cell death. Caspase-1-/- bone marrow-derived macrophages exhibit impaired bactericidal activity compared to wild-type bone marrow-derived macrophages
additional information
-
caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
additional information
-
caspase-1-deficient mice have unimpaired inflammatory responses to necrotic cells
additional information
-
defective Anthrax-induced interleukin-1beta secretion in Nod2-/- or caspase-1-/- macrophages, not due to decreased pro-interleukin-1beta expression, caspase-1 or NOD2 deficiencies do not exert a major effect on TNF-alpha secretion
additional information
-
genetic disruption of cryopyrin or the adaptor apoptosis associated speck-like protein, ASC, abrogates caspase-1 activation in poly(I:C), dsRNA, or viral RNA-stimulated macrophages
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
additional information
-
secretion of interleukin-1beta following KIM5 infection is reduced in caspase-1-deficient macrophages compared to wild-type macrophages
additional information
-
caspase-1-deficient macrophages show only slightly reduced ATP-triggered MHC-II secretion, overview
-
additional information
-
Salmonella- and lipopolysaccharide-, and ATP-induced activation of caspase-7 is abolished in macrophages deficient in caspase-1, the pattern recognition receptors Ipaf and Cryopyrin, and the inflammasome adaptor ASC
-
additional information
RNAi silencing
additional information
-
RNAi silencing
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