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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.22.61 - caspase-8

for references in articles please use BRENDA:EC3.4.22.61
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.61 caspase-8
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q14790 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-/-(Gly/Ser/Ala)
Synonyms
caspase-8, caspase 8, casp8, flice, cysteine protease caspase-8, cysteine aspartic acid-specific protease, apoptotic cysteine protease, flice/mach, fadd-like ice, cysteine aspartic acid protease 8, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
apoptotic cysteine protease
-
-
-
-
apoptotic protease Mch-5
-
-
-
-
C14.004
-
-
-
-
CAP4
-
-
-
-
caspase 8
-
-
-
-
FADD-homologous ICE/CED-3-like protease
-
-
-
-
FADD-like ICE
-
-
-
-
FLICE
-
-
-
-
FLICE/MACH
-
-
-
-
ICE-like apoptotic protease 5
-
-
-
-
MACH
-
-
-
-
Mch5
-
-
-
-
MORT1-associated CED-3 homolog
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
179241-78-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ac-IEPD-7-amido-4-methylcoumarin + H2O
Ac-IEPD + 7-amino-4-methylcoumarin
show the reaction diagram
37°C
-
-
?
Ac-IEPD-AMC + H2O
Ac-IEPD + AMC
show the reaction diagram
37°C
-
-
?
acetyl-DEVD-4-nitroanilide + H2O
acetyl-DEVD + 4-nitroaniline
show the reaction diagram
-
-
-
?
acetyl-IETD-4-nitroanilide + H2O
acetyl-IETD + 4-nitroaniline
show the reaction diagram
-
-
-
?
acetyl-IETD-7-amido-4-fluoromethylcoumarin + H2O
acetyl-IETD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
-
-
-
?
acetyl-Ile-Glu-Thr-Asp-7-amino-4-fluoromethylcoumarin + H2O
Ac-IETD + 7-amino-4-fluoromethylcoumarin
show the reaction diagram
37°C, pH 7.4
-
-
?
Atg3 protein + H2O
?
show the reaction diagram
-
-
-
?
BAP31 + H2O
?
show the reaction diagram
cleavage results in a proapoptotic p20 fragment
-
-
?
Bcl-2 protein Bid + H2O
?
show the reaction diagram
cleavage results in a proapoptotic p15 tBid fragment
-
-
?
BH3-only protein Bid + H2O
?
show the reaction diagram
-
-
-
?
Ca2+/calmodulin-dependent protein kinase-like kinase + H2O
?
show the reaction diagram
cleavage generates a 43 kDa C-terminal fragment and a small N-terminal fragment with proapoptotic activity
-
-
?
cellular inhibitor of apoptosis 1 + H2O
?
show the reaction diagram
FLICE2 + H2O
?
show the reaction diagram
-
-
-
?
HER-2 + H2O
?
show the reaction diagram
IETD-4-nitroanilide + H2O
IETD + 4-nitroaniline
show the reaction diagram
-
-
-
?
IETD-7-amido-4-trifluoromethylcoumarin + H2O
IETD + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
LAP3 + H2O
?
show the reaction diagram
-
-
-
?
LAP6 + H2O
?
show the reaction diagram
-
-
-
?
p21-activated kinase 2 + H2O
?
show the reaction diagram
separates the N-terminal regulatory domain from the C-terminal catalytic domain
-
-
?
procaspase-3 + H2O
?
show the reaction diagram
results in a p11 and p20 fragment
-
-
?
receptor-indicating protein + H2O
?
show the reaction diagram
separates the N-terminal kinase from the C-terminal death domain
-
-
?
Tx + H2O
?
show the reaction diagram
-
-
-
?
Yama + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Atg3 protein + H2O
?
show the reaction diagram
-
-
-
?
BH3-only protein Bid + H2O
?
show the reaction diagram
-
-
-
?
cellular inhibitor of apoptosis 1 + H2O
?
show the reaction diagram
i.e. cIAP-1, TRAIL-induced degradation of cIAP-1 requires caspase 8 activity, and it is, at least in part, due to direct cleavage of cIAP-1 by caspase 8
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-IETD-aldehyde
IC50: 50 nM, covalently modifies the active site C360
benzyloxycarbonyl-DEVD-aldehyde
the inhibitor interacts favourably with the enzyme in subsite S4
benzyloxycarbonyl-IETD-fluoromethyl ketone
-
benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
biotin-conjugated valine-alanine-aspartate-fluoromethylketone
-
cowpox serpin CrmA
CrmA, a pox virus-encoded serpin attenuates the ability of FLICE to activate downstrean caspases
-
Fas-associated death domain-like interleukin 1-converting enzyme-inhibitory proteins
FLIPs, natural inhibitor
-
N-acetyl-IETD-aldehyde
-
N-benzyloxycarbonyl-Val-Ala-Asp-fluoromethyl ketone
-
Q-VD-OPH
pan-caspase inhibitor
tert-butyloxycarbonyl-IETD-aldehyde
-
Z-IETD
Z-IETD-fluoromethylketone
caspase 8 inhibitor
Z-VAD
pan-caspase inhibitor
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6'-benzyloxy-4-bromo-2'-hydroxychalcone
compound displays potent cytotoxic properties against human leukaemia cells U-937, HL-60, K-562, NALM-6 and MOLT-3. Application results in significant activation of caspase-8 after 24 h of treatment
Fas-associated death domain protein-like interleukin-1-beta-converting enzyme-like inhibitory protein, long form
FLIP L, results in a heterodimeric enzyme
-
interferon-alpha
increases caspase-8 transcription
-
justicidin A
-
radiation
increases caspase-8 expression and activity
-
Sodium citrate
enhances activity
Tumor necrosis factor alpha
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.066
acetyl-IETD-4-nitroanilide
pH 7.5, 37°C
0.0206 - 0.0552
acetyl-IETD-7-amido-4-fluoromethylcoumarin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 1.25
acetyl-IETD-7-amido-4-fluoromethylcoumarin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000002
benzyloxycarbonyl-DEVD-aldehyde
-
0.000001
tert-butyloxycarbonyl-IETD-aldehyde
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00005
acetyl-IETD-aldehyde
Homo sapiens
IC50: 50 nM, covalently modifies the active site C360
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
no change in activity after irradiation
Manually annotated by BRENDA team
trophoblast cell line
Manually annotated by BRENDA team
the levels of caspase-3 and caspase-8 in plasma are both significantly higher than in sperm
Manually annotated by BRENDA team
OCUM-2M, OCUM-1, OCUM-8, OCUM-9, NUGC3, NIGC4, MKN45, MKN74, FU97, MKN7
Manually annotated by BRENDA team
MCF7 A/Z breast adenocarcinoma cell defective for nuclear factor kappa-B activation
Manually annotated by BRENDA team
caspase-8L is generated by the alternative splicing of human caspase-8
Manually annotated by BRENDA team
increase in caspase-8 transcript levels and activity after irradiation
Manually annotated by BRENDA team
increase in caspase-8 transcript levels and activity after irradiation
Manually annotated by BRENDA team
no change in activity after irradiation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
model of caspase 8 activation. Upon apoptosis induction triggered by interaction of the death ligand to the trimeric death receptor, adaptor FADD (Fas-associated protein with death domain ) is recruited to the death receptor via a death domain DD-DD interaction. FADD recruited at cell surface can recruit caspase-8 via a DED-DED interaction, leading to procaspase-8 proximity to meet another procaspase-8. Closely located FL motif on DED2 causes domain swapping and dimerization of procaspase-8. The dimerization via tandem DED domain swapping causes the proximity-mediated self-activation of caspase-8
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CASP8_HUMAN
479
0
55391
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
alpha2beta2, 2 * 18000 + 2 * 11000, crystallographic data
18000
28000
activated heterodimer, gel filtration
31000
monomer, non-cleavable caspase-8, SDS-PAGE
43000
fragment of caspase-8 resulting from cleavage, SDS-PAGE
54000
monomer, pro-caspase-8, SDS-PAGE
55000
monomer, pro-caspase-8, SDS-PAGE
57000
monomer, full-length unactivated form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
monomer
tetramer
alpha2beta2, 2 * 18000 + 2 * 11000, crystallographic data
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
derived from a single chain proenzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of a complex of the activated caspase-8 proteolytic domain with the irreversible peptidic inhibitor benzyloxycarbonyl-EVD-dichloromethylketone, vapour diffusion method
crystallization of the enzyme covalently modified with acetyl-IETD-aldehyde, hanging- and sitting-drop vapor diffusion
structure of caspase-8 tandem death effector domains (DEDs), reveals domain-swapped dimerization. DEDs exist as dimers in solution. The FL motif on DED2 is critical for caspase-8 dimerization via domain swapping
structure of the N-terminal tandem death effector domains, DEDs and comparison with caspase 8 of Molluscum contagiosum virus subtype 1
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D210A/D216A
cannot be cleaved to release death effector domains, overexpression inhibits the endothelial cell leukocyte adhesion molecule 1 promoter activation induced by Fas-associated death domain and receptor-interacting protein 1
E396A
diminishes TRAF6 binding capacity
E417A
diminishes TRAF6 binding capacity
F122A/I128D
mutations in the N-terminal tandem death effector domains. Mutations markedly reduce the aggregation and improve the solubility
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
expression in Escherichia coli
expression in HEK293T cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
tumor necrosis factor–related apoptosis-inducing ligand, TRAIL, signaling induces caspase 8
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
gastric cancer might be a good target of TRAIL therapy because the majority of tumor cells have intact caspase-8 expression. The anticancer efficacy may be predicted by the degree of caspase-8 activation after TRAIL treatment
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boldin, M.P.; Goncharov, T.M.; Goltsev, Y.V.; Wallach, D.
Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
Cell
85
803-815
1996
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Fernandes-Alnemri, T.; Armstrong, R.C.; Krebs, J.F.; Srinivasula, S.M.; Wang, L.; Bullrich, F.; Fritz, L.C.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri, E.S.
In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
Proc. Natl. Acad. Sci. USA
93
7464-7469
1996
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Himeji, D.; Horiuchi, T.; Tsukamoto, H.; Hayashi, K.; Watanabe, T.; Harada, M.
Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade
Blood
99
4070-4078
2002
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Muzio, M.; Salvesen, G.S.; Dixit, V.M.
FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
J. Biol. Chem.
272
2952-2956
1997
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Ng, F.W.H.; Nguyen, M.; Kwan, T.; Branton, P.E.; Nicholson, D.W.; Cromlish, J.A.; Shore, G.C.
p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum
J. Cell Biol.
139
327-338
1997
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Blanchard, H.; Kodandapani, L.; Mittl, P.R.E.; Di Marco, S.; Krebs, J.F.; Wu, J.C.; Tomaselli, K.J.; Gruetter, M.G.
The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis
Structure
7
1125-1133
1999
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Blanchard, H.; Donepudi, M.; Tschopp, M.; Kodandapani, L.; Wu, J.C.; Grutter, M.G.
Caspase-8 specificity probed at subsite S(4): crystal structure of the caspase-8-Z-DEVD-CHO complex
J. Mol. Biol.
302
9-16
2000
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Watt, W.; Koeplinger, K.A.; Mildner, A.M.; Heinrikson, R.L.; Tomasselli, A.G.; Watenpaugh, K.D.
The atomic-resolution structure of human caspase-8, a key activator of apoptosis
Structure Fold. Des.
7
1135-1143
1999
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Breckenridge, D.G.; Nguyen, M.; Kuppig, S.; Reth, M.; Shore, G.C.
The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
Proc. Natl. Acad. Sci. USA
99
4331-4336
2002
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Boatright, K.M.; Deis, C.; Denault, J.B.; Sutherlin, D.P.; Salvesen, G.S.
Activiation of caspases-8 and -10 by FLIP L
Biochem. J.
382
651-657
2004
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Benoit, V.; Chariot, A.; Delacroix, L.; Deregowski, V.; Jacobs, N.; Merville, M.P.; Bours, V.
Caspase-8-dependent HER-2 cleavage in response to tumor necrosis factor alpha stimulation is counteracted by nuclear factor kappaB through c-FLIP-L expression
Cancer Res.
64
2684-2691
2004
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Afshar, G.; Jelluma, N.; Yang, X.; Basila, D.; Arvold, N.D.; Karlsson, A.; Yount, G.L.; Dansen, T.B.; Koller, E.; Haas-Kogan, D.A.
Radiation-induced caspase-8 mediates p53-independent apoptosis in glioma cells
Cancer Res.
66
4223-4232
2006
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Bidere, N.; Snow, A.L.; Sakai, K.; Zheng, L.; Lenardo, M.J.
Caspase-8 Regulation by Direct Interaction with TRAF6 in T Cell Receptor-Induced NF-kappaB Activation
Curr. Biol.
16
1666-1671
2006
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Su, C.L.; Huang, L.L.; Huang, L.M.; Lee, J.C.; Lin, C.N.; Won, S.J.
Caspase-8 acts as a key upstream executor of mitochondria during justicidin A-induced apoptosis in human hepatoma cells
FEBS Lett.
580
3185-3191
2006
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Jenkins, C.E.; Swiatoniowski, A.; Issekutz, A.C.; Lin, T.J.
Pseudomonas aeruginosa exotoxin A induces human mast cell apoptosis by a caspase-8 and -3-dependent mechanism
J. Biol. Chem.
279
37201-37207
2004
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Liedtke, C.; Groeger, N.; Manns, M.P.; Trautwein, C.
Interferon-alpha enhances TRAIL-mediated apoptosis by up-regulating caspase-8 transcription in human hepatoma cells
J. Hepatol.
44
342-349
2006
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Takahashi, K.; Kawai, T.; Kumar, H.; Sato, S.; Yonehara, S.; Akira, S.
Roles of caspase-8 and caspase-10 in innate immune responses to double-stranded RNA
J. Immunol.
176
4520-4524
2006
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Fischer, U.; Stroh, C.; Schulze-Osthoff, K.
Unique and overlapping substrate specificities of caspase-8 and caspase-10
Oncogene
25
152-159
2006
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Kanehara, I.; Nakata, B.; Hirakawa, K.
Caspase-8 is scarcely silenced and its activity is well correlated with the anticancer effect of tumor necrosis factor-related apoptosis-inducing ligand in gastric cancer cells
Oncol. Rep.
14
1249-1253
2005
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Bidle, K.A.; Haramaty, L.; Baggett, N.; Nannen, J.; Bidle, K.D.
Tantalizing evidence for caspase-like protein expression and activity in the cellular stress response of Archaea
Environ. Microbiol.
12
1161-1172
2010
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Guicciardi, M.E.; Mott, J.L.; Bronk, S.F.; Kurita, S.; Fingas, C.D.; Gores, G.J.
Cellular inhibitor of apoptosis 1 (cIAP-1) degradation by caspase 8 during TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis
Exp. Cell Res.
317
107-116
2011
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Oral, O.; Oz-Arslan, D.; Itah, Z.; Naghavi, A.; Deveci, R.; Karacali, S.; Gozuacik, D.
Cleavage of Atg3 protein by caspase-8 regulates autophagy during receptor-activated cell death
Apoptosis
17
810-820
2012
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Ahmad, K.; Khan, S.; Adil, M.; Saeed, M.; Srivastava, A.K.
Structure based molecular inhibition of Caspase-8 for treatment of multi-neurodegenerative diseases using known natural compounds
Bioinformation
10
191-195
2014
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Shen, C.; Yue, H.; Pei, J.; Guo, X.; Wang, T.; Quan, J.M.
Crystal structure of the death effector domains of caspase-8
Biochem. Biophys. Res. Commun.
463
297-302
2015
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Park, H.H.
Molecular basis of dimerization of initiator caspase was revealed by crystal structure of caspase-8 pro-domain
Cell Death Differ.
26
1213-1220
2019
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Horn, S.; Hughes, M.A.; Schilling, R.; Sticht, C.; Tenev, T.; Ploesser, M.; Meier, P.; Sprick, M.R.; MacFarlane, M.; Leverkus, M.
Caspase-10 negatively regulates caspase-8-mediated cell death, switching the response to CD95L in favor of NF-kappaB activation and cell survival
Cell Rep.
19
785-797
2017
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Saavedra, E.; Del Rosario, H.; Brouard, I.; Quintana, J.; Estevez, F.
6-Benzyloxy-4-bromo-2-hydroxychalcone is cytotoxic against human leukaemia cells and induces caspase-8- and reactive oxygen species-dependent apoptosis
Chem. Biol. Interact.
298
137-145
2019
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Carrillo, I.; Droguett, D.; Castillo, C.; Liempi, A.; Munoz, L.; Maya, J.D.; Galanti, N.; Kemmerling, U.
Caspase-8 activity is part of the BeWo trophoblast cell defense mechanisms against Trypanosoma cruzi infection
Exp. Parasitol.
168
9-15
2016
Homo sapiens (Q14790)
Manually annotated by BRENDA team
Wei, X.; Li, Q.; Han, Z.; Lin, D.; Yu, P.
Differences in caspase-8 and -9 activity and sperm motility in infertile males of Li nationality in China
Int. J. Clin. Exp. Med.
8
4721-4726
2015
Homo sapiens (Q14790), Homo sapiens
Manually annotated by BRENDA team
Huang, K.; Zhang, J.; ONeill, K.L.; Gurumurthy, C.B.; Quadros, R.M.; Tu, Y.; Luo, X.
Cleavage by caspase 8 and mitochondrial membrane association activate the BH3-only protein Bid during TRAIL-induced apoptosis
J. Biol. Chem.
291
11843-11851
2016
Homo sapiens (Q14790)
Manually annotated by BRENDA team