Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade (Q24311006)

GOA release 2020-03-11

author name string

P Li

1

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D Nijhawan

2

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I Budihardjo

3

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S M Srinivasula

4

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M Ahmad

5

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E S Alnemri

6

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X Wang

Human ICE/CED-3 protease nomenclature

7

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language of work or name

English

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publication date

14 November 1997

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published in

Cell

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volume

91

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page(s)

479-89

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issue

4

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cites work

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Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death

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Intracellular adenosine triphosphate (ATP) concentration: a switch in the decision between apoptosis and necrosis

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

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DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis

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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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Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis

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Affinity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8

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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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