Autoactivation of Procaspase-9 by Apaf-1-Mediated Oligomerization (Q28275527)

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29 December 2024

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29 December 2024

author

Srinivasa M Srinivasula

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S. M. Srinivasula

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author name string

M. Ahmad

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T. Fernandes-Alnemri

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E. S. Alnemri

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http://www.cell.com/article/S1097276500800957/pdf

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publication date

June 1998

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language of work or name

English

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work available at URL

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29 December 2024

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https://api.elsevier.com/content/article/PII:S1097276500800957?httpAccept=text/plain

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29 December 2024

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1

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issue

7

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page(s)

949-57

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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

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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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Interleukin-1 beta converting enzyme requires oligomerization for activity of processed forms in vivo

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Blk, a BH3-containing Mouse Protein That Interacts with Bcl-2 and Bcl-xL, Is a Potent Death Agonist

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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?

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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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Caspases: killer proteases

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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

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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

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Interaction and regulation of subcellular localization of CED-4 by CED-9

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7 January 2021

Autoproteolytic Activation of Pro-Caspases by Oligomerization

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7 January 2021

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

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Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor

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The Caenorhabditis elegans cell death gene ced-4 encodes a novel protein and is expressed during the period of extensive programmed cell death

29 December 2024

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https://api.crossref.org/works/10.1016/S1097-2765(00)80095-7

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Identifiers

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017