Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis (Q24310597)

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H Zhu

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C J Xu

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J Yuan

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

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language of work or name

English

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publication date

21 August 1998

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published in

Cell

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volume

94

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page(s)

491-501

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issue

4

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cites work

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Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization.

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Conversion of Bcl-2 to a Bax-like death effector by caspases

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Modulation of cell death by Bcl-XL through caspase interaction

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The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9

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Regulation of apoptosis by BH3 domains in a cell-free system

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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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Nonionic detergents induce dimerization among members of the Bcl-2 family

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Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation

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The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4

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Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL.

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The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis

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Bcl-2 and Bax function independently to regulate cell death

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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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Activation of caspase-2 in apoptosis

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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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Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

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Small pool expression screening: identification of genes involved in cell cycle control, apoptosis, and early development

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Bcl-xL acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex.

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Bcl-2 gene family in the nervous system

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Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3

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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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Checkpoints of dueling dimers foil death wishes

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

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Caspases: intracellular signaling by proteolysis

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Two CD95 (APO-1/Fas) signaling pathways

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Bcl-2 prevents apoptotic mitochondrial dysfunction by regulating proton flux

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Bcl-xL functions downstream of caspase-8 to inhibit Fas- and tumor necrosis factor receptor 1-induced apoptosis of MCF7 breast carcinoma cells

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Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria

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BID: a novel BH3 domain-only death agonist

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Movement of Bax from the cytosol to mitochondria during apoptosis

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Caenorhabditis elegans CED-9 protein is a bifunctional cell-death inhibitor.

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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Target protease specificity of the viral serpin CrmA. Analysis of five caspases

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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

1 reference

Consolidated OpenCitations Corpus – April 2017

258974

258974

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference