Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells. (Q33893102)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10713725%20AND%20SRC:MED&resulttype=core&format=json

4 November 2019

title

Bcl-2 inhibits Bax translocation from cytosol to mitochondria during drug-induced apoptosis of human tumor cells (English)

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4 November 2019

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5

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4 November 2019

author name string

Murphy KM

1

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4 November 2019

Ranganathan V

2

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4 November 2019

Farnsworth ML

3

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4 November 2019

Kavallaris M

4

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4 November 2019

publication date

1 January 2000

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Cell Death & Differentiation

4 November 2019

language of work or name

English

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published in

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4 November 2019

volume

7

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4 November 2019

issue

1

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4 November 2019

page(s)

102-111

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Apoptosis in the pathogenesis and treatment of disease

4 November 2019

cites work

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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death

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Cell-specific induction of apoptosis by microinjection of cytochrome c. Bcl-xL has activity independent of cytochrome c release

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Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis

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Bax in Murine Thymus Is a Soluble Monomeric Protein That Displays Differential Detergent-induced Conformations

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Movement of Bax from the Cytosol to Mitochondria during Apoptosis

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Bax directly induces release of cytochrome c from isolated mitochondria

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Expression of Bcl-2 in human epithelial tumor (HeLa) cells enhances clonogenic survival following exposure to 5-fluoro-2′-deoxyuridine or staurosporine, but not following exposure to etoposide or doxorubicin

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis

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Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2.

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Bax and adenine nucleotide translocator cooperate in the mitochondrial control of apoptosis

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