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Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis.
scientific article published on 26 March 2012
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scholarly article
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
title
Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 proteolysis
(English)
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
main subject
proteolysis
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based on heuristic
inferred from title
author
Dave Boucher
series ordinal
1
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stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
author name string
Véronique Blais
series ordinal
2
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stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
Jean-Bernard Denault
series ordinal
3
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Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
language of work or name
English
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publication date
26 March 2012
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Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
number of pages
6
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inferred from page(s)
published in
Proceedings of the National Academy of Sciences of the United States of America
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Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
volume
109
1 reference
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Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
issue
15
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stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
page(s)
5669-5674
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
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PubMed Central
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Cutting edge: proteolytic inactivation of poly(ADP-ribose) polymerase 1 by the Nlrp3 and Nlrc4 inflammasomes
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Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation
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Caspase 3 attenuates XIAP (X-linked inhibitor of apoptosis protein)-mediated inhibition of caspase 9
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Activation and caspase-mediated inhibition of PARP: a molecular switch between fibroblast necrosis and apoptosis in death receptor signaling.
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Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing
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Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
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Structural basis for the inhibition of caspase-3 by XIAP
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Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
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The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity
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Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7.
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Granzyme B mimics apical caspases. Description of a unified pathway for trans-activation of executioner caspase-3 and -7.
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Importance of poly(ADP-ribose) polymerase and its cleavage in apoptosis. Lesson from an uncleavable mutant
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Pro-caspase-3 is a major physiologic target of caspase-8.
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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
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ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
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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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Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site
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24 September 2018
Overlapping cleavage motif selectivity of caspases: implications for analysis of apoptotic pathways.
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Engineered hybrid dimers: tracking the activation pathway of caspase-7.
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Human caspase-7 activity and regulation by its N-terminal peptide.
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24 September 2018
Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer.
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24 September 2018
Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis.
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Identifiers
DOI
10.1073/PNAS.1200934109
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
ADS bibcode
2012PNAS..109.5669B
0 references
PMC publication ID
3326497
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
PubMed publication ID
22451931
1 reference
stated in
Europe PubMed Central
PMC publication ID
3326497
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22451931%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
ResearchGate publication ID
221983386
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