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Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
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instance of
scholarly article
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title
Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
(English)
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author name string
S M Srinivasula
series ordinal
1
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M Ahmad
series ordinal
2
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T Fernandes-Alnemri
series ordinal
3
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E S Alnemri
series ordinal
4
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language of work or name
English
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publication date
June 1998
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published in
Molecular Cell
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volume
1
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issue
7
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page(s)
949-57
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cites work
Human ICE/CED-3 protease nomenclature
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Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
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A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
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Role of CED-4 in the activation of CED-3.
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Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death
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FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
1 reference
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Caspases: the executioners of apoptosis
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IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
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X-linked IAP is a direct inhibitor of cell-death proteases
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RAIDD is a new 'death' adaptor molecule
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In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
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A license to kill
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Interleukin-1 beta converting enzyme requires oligomerization for activity of processed forms in vivo
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ICE family proteases: mediators of all apoptotic cell death?
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The CARD domain: a new apoptotic signalling motif
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CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9.
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Cell-specific induction of apoptosis by microinjection of cytochrome c. Bcl-xL has activity independent of cytochrome c release
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Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
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Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL
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Protease activation during apoptosis: death by a thousand cuts?
1 reference
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FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex
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An induced proximity model for caspase-8 activation.
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Apoptosis by death factor
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Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex
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Death substrates come alive
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Caspases: intracellular signaling by proteolysis
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Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis
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Interaction between the C. elegans cell-death regulators CED-9 and CED-4.
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Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases
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FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis
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The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32
1 reference
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Interaction and regulation of subcellular localization of CED-4 by CED-9
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Autoproteolytic activation of pro-caspases by oligomerization.
1 reference
stated in
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7 January 2021
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Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
1 reference
stated in
Crossref
reference URL
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Identifiers
DOI
10.1016/S1097-2765(00)80095-7
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605758
OpenCitations bibliographic resource ID
605758
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605758
PubMed ID
9651578
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
605758
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