Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain (Q42826067)

8 November 2017

title

Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain (English)

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8 November 2017

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8 November 2017

Colussi PA

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8 November 2017

Harvey NL

series ordinal

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8 November 2017

Shearwin-Whyatt LM

series ordinal

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8 November 2017

language of work or name

English

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publication date

1 October 1998

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Journal of Biological Chemistry

8 November 2017

published in

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8 November 2017

volume

273

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8 November 2017

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8 November 2017

page(s)

26566-26570

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ICE-like proteases in apoptosis

8 November 2017

cites work

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Caspases: killer proteases

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Portrait of an executioner: the molecular mechanism of FAS/APO-1-induced apoptosis

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

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RAIDD is a new 'death' adaptor molecule

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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

21 January 2018

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Dimerization and autoprocessing of the Nedd2 (caspase-2) precursor requires both the prodomain and the carboxyl-terminal regions

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An induced proximity model for caspase-8 activation.

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Autoproteolytic activation of pro-caspases by oligomerization

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Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme

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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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Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

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Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

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Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain

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Inhibition of the Caenorhabditis elegans cell-death protease CED-3 by a CED-3 cleavage site in baculovirus p35 protein

21 January 2018

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

21 January 2018

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Molecular ordering of the cell death pathway. Bcl-2 and Bcl-xL function upstream of the CED-3-like apoptotic proteases

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Caspase-9, Bcl-XL, and Apaf-1 Form a Ternary Complex

21 January 2018

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

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.41.26566

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8 November 2017

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