Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. (Q40927226)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10497198%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

title

Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7 (English)

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31 October 2019

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1

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31 October 2019

author name string

E B Affar

2

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31 October 2019

D D'Amours

3

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31 October 2019

V M Dixit

4

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31 October 2019

G S Salvesen

5

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31 October 2019

G G Poirier

6

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31 October 2019

language of work or name

English

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publication date

1 October 1999

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Journal of Biological Chemistry

31 October 2019

published in

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31 October 2019

volume

274

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31 October 2019

page(s)

28379-28384

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31 October 2019

issue

40

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Caspases: killer proteases

31 October 2019

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The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A

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Dual function for poly(ADP-ribose) synthesis in response to DNA strand breakage

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Interaction of poly(ADP-ribose)polymerase with DNA polymerase alpha

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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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Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases.

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Processing/activation of at least four interleukin-1beta converting enzyme-like proteases occurs during the execution phase of apoptosis in human monocytic tumor cells

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An affinity matrix for the purification of poly(ADP-ribose) glycohydrolase

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Complete inhibition of poly(ADP-ribose) polymerase activity prevents the recovery of C3H10T1/2 cells from oxidative stress

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Interactions of poly(ADP-ribose) with nuclear proteins

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Clusters of S1 nuclease-hypersensitive sites induced in vivo by DNA damage

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Possible involvement of poly(ADP-ribosyl) polymerase in triggering stress-induced apoptosis.

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Different basal NAD levels determine opposite effects of poly(ADP-ribosyl)polymerase inhibitors on H2O2-induced apoptosis.

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A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD

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Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis

21 January 2018

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