(Q28217828)

2

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Anne Druilhe

3

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Teresa Fernandes-Alnemri

4

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Emad S Alnemri

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

19 April 2002

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published in

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volume

277

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issue

16

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page(s)

13430-7

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cites work

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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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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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RAIDD is a new 'death' adaptor molecule

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An induced proximity model for caspase-8 activation.

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Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal

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

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Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked

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

21 January 2018

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Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis

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Bcl-2 and the outer mitochondrial membrane in the inactivation of cytochrome c during Fas-mediated apoptosis

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

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Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization

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

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Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

21 January 2018

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

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Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c.

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The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling

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Mitochondrial release of caspase-2 and -9 during the apoptotic process

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Structural and biochemical basis of apoptotic activation by Smac/DIABLO

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Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway

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Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

21 January 2018

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Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

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Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death

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Identification and molecular cloning of two novel receptors for the cytotoxic ligand TRAIL

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CLAP, a novel caspase recruitment domain-containing protein in the tumor necrosis factor receptor pathway, regulates NF-kappaB activation and apoptosis

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Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

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Role of multiple cellular proteases in the execution of programmed cell death.

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Functional activation of Nedd2/ICH-1 (caspase-2) is an early process in apoptosis

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Serial killers: ordering caspase activation events in apoptosis

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Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis

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Involvement of caspase-2 long isoform in Fas-mediated cell death of human leukemic cells.

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Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3

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Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis

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Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death

21 January 2018

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis

21 January 2018

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Two distinct pathways leading to nuclear apoptosis

21 January 2018

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Bcl-2 family: life-or-death switch

21 January 2018

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Why are mitochondria involved in apoptosis? Permeability transition pores and apoptosis as selective mechanisms to eliminate superoxide-producing mitochondria and cell.

21 January 2018

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

21 January 2018

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The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event

21 January 2018

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Bax-induced cytochrome C release from mitochondria is independent of the permeability transition pore but highly dependent on Mg2+ ions

21 January 2018

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Bax directly induces release of cytochrome c from isolated mitochondria

21 January 2018

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Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M108029200

Bcl-x(L) forms an ion channel in synthetic lipid membranes.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M108029200

Inhibition of Bax channel-forming activity by Bcl-2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M108029200

Ion channel activity of the BH3 only Bcl-2 family member, BID.

21 January 2018

1 reference

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Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane

21 January 2018

1 reference

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Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M108029200

Proapoptotic BH3-only Bcl-2 family members induce cytochrome c release, but not mitochondrial membrane potential loss, and do not directly modulate voltage-dependent anion channel activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M108029200

FLICE Induced Apoptosis in a Cell-free System

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M108029200

21 January 2018

Identifiers

DOI

10.1074/JBC.M108029200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11832478

1 reference

Consolidated OpenCitations Corpus – April 2017