Mitochondria, AIF and caspases--rivaling for cell death execution. (Q53718758)

18 May 2018

title

Mitochondria, AIF and caspases--rivaling for cell death execution. (English)

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18 May 2018

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1

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18 May 2018

Guido Kroemer

series ordinal

2

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18 May 2018

publication date

1 February 2003

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18 May 2018

published in

Nature Cell Biology

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18 May 2018

volume

5

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18 May 2018

issue

2

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18 May 2018

page(s)

97-99

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18 May 2018

https://scigraph.springernature.com/pub.10.1038/ncb0203-97

exact match

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cites work

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Apoptosis-inducing factor (AIF): key to the conserved caspase-independent pathways of cell death?

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Mitochondrial endonuclease G is important for apoptosis in C. elegans.

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Endonuclease G is an apoptotic DNase when released from mitochondria

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Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans

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Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli

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The harlequin mouse mutation downregulates apoptosis-inducing factor

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Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor

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On the evolutionary conservation of the cell death pathway: mitochondrial release of an apoptosis-inducing factor during Dictyostelium discoideum cell death

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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

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Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization

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Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

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Apoptotic protease activating factor 1 (Apaf-1)-independent cell death suppression by Bcl-2.

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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

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Life-or-death decisions by the Bcl-2 protein family.

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Identifiers

DOI

10.1038/NCB0203-97

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18 May 2018

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18 May 2018