(Q40486900)

21 September 2017

title

Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s). (English)

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Gene Ontology release 2020-05-02

21 September 2017

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Shinji Kamada

1

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21 September 2017

Ushio Kikkawa

series ordinal

2

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21 September 2017

Yoshihide Tsujimoto

series ordinal

3

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21 September 2017

Tony Hunter

series ordinal

4

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21 September 2017

language of work or name

English

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publication date

29 November 2004

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Journal of Biological Chemistry

21 September 2017

number of pages

4

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based on heuristic

inferred from page(s)

published in

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21 September 2017

volume

280

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21 September 2017

issue

2

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21 September 2017

page(s)

857-860

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Human ICE/CED-3 protease nomenclature

21 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.C400538200

21 January 2018

Caspases: enemies within

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Mammalian caspases: structure, activation, substrates, and functions during apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Caspase-3 controls both cytoplasmic and nuclear events associated with Fas-mediated apoptosis in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Determinants of the nuclear localization of the heterodimeric DNA fragmentation factor (ICAD/CAD).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Many cuts to ruin: a comprehensive update of caspase substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Caspases disrupt the nuclear-cytoplasmic barrier

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Efficient selection for high-expression transfectants with a novel eukaryotic vector

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Inhibition of human caspases by peptide-based and macromolecular inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Caspases: their intracellular localization and translocation during apoptosis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Preservation of caspase-3 subunits from degradation contributes to apoptosis evoked by lactacystin: any single lysine or lysine pair of the small subunit is sufficient for ubiquitination

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

Nucleocytoplasmic transport

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.C400538200

21 January 2018

Identifiers

DOI

10.1074/JBC.C400538200

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21 September 2017

1 reference