Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization (Q28275527)

1

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M Ahmad

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T Fernandes-Alnemri

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E S Alnemri

Human ICE/CED-3 protease nomenclature

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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

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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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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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In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains

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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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CED-4 induces chromatin condensation in Schizosaccharomyces pombe and is inhibited by direct physical association with CED-9.

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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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Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex

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Death substrates come alive

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

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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

605758

605758

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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