(Q24290124)

extrinsic apoptotic signaling pathway via death domain receptors

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

S M Srinivasula

1

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P Datta

2

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X J Fan

3

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T Fernandes-Alnemri

4

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Z Huang

5

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E S Alnemri

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

17 November 2000

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published in

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volume

275

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page(s)

36152-7

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issue

46

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cites work

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

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

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Caspases: intracellular signaling by proteolysis

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

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

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The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID.

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

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Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis

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The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant

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Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome

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Negative regulation of the Apaf-1 apoptosome by Hsp70

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Structural and biochemical basis of apoptotic activation by Smac/DIABLO

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X-linked IAP is a direct inhibitor of cell-death proteases

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