(Q28201157)

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Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3

scientific article (publication date: 15 June 2001)

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Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3 (English)

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apoptotic process

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Gabriela Paroni

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G Paroni

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author name string

C Henderson

2

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C Schneider

3

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C Brancolini

4

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language of work or name

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publication date

15 June 2001

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Journal of Biological Chemistry

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276

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24

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21907-15

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Caspases: enemies within

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https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Caspases: the executioners of apoptosis

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Caspases: intracellular signaling by proteolysis

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

1 reference

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Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9

1 reference

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Differential requirement for caspase 9 in apoptotic pathways in vivo.

1 reference

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Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally.

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Defects in regulation of apoptosis in caspase-2-deficient mice

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Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogen-mediated apoptosis

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RAIDD is a new 'death' adaptor molecule

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Activation of caspase-2 in apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

1 reference

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Proteolytic processing of the adherens junctions components beta-catenin and gamma-catenin/plakoglobin during apoptosis

1 reference

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Oncogene-dependent apoptosis is mediated by caspase-9.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis

1 reference

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Caspases disrupt the nuclear-cytoplasmic barrier

1 reference

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

1 reference

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Caspases: their intracellular localization and translocation during apoptosis.

1 reference

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

1 reference

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of p53-induced apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Apoptotic pathways: paper wraps stone blunts scissors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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BH3-Only proteins-essential initiators of apoptotic cell death

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Apoptosis control by death and decoy receptors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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The proteolytic procaspase activation network: an in vitro analysis

1 reference

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21 January 2018

The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Caspase-9 can be activated without proteolytic processing

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

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Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

Mitochondrial release of caspase-2 and -9 during the apoptotic process

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M011565200

21 January 2018

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10.1074/JBC.M011565200

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