BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis (Q28189945)

4

object named as

R A Flavell

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author name string

E H Cheng

1

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M C Wei

2

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S Weiler

3

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T W Mak

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T Lindsten

The Bcl-2 protein family: arbiters of cell survival

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language of work or name

English

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publication date

September 2001

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published in

Molecular Cell

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volume

8

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issue

3

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page(s)

705-11

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cites work

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Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane

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Mitochondria and apoptosis

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

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Pro-apoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x(L).

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Activation of C. elegans cell death protein CED-9 by an amino-acid substitution in a domain conserved in Bcl-2.

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Nonionic detergents induce dimerization among members of the Bcl-2 family

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BH3-Only proteins-essential initiators of apoptotic cell death

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Bcl-2-family proteins: the role of the BH3 domain in apoptosis

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The pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol

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Bcl-2 and Bax function independently to regulate cell death

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

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

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Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

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

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

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A reversible component of mitochondrial respiratory dysfunction in apoptosis can be rescued by exogenous cytochrome c.

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Bim: a novel member of the Bcl-2 family that promotes apoptosis

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

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

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BAX-dependent transport of cytochrome c reconstituted in pure liposomes

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Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

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Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

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Structure of Bax: coregulation of dimer formation and intracellular localization

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Cell death regulation in Drosophila: conservation of mechanism and unique insights

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BID: a novel BH3 domain-only death agonist

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Movement of Bax from the cytosol to mitochondria during apoptosis

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Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death

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BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax.

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Apaf1 is required for mitochondrial pathways of apoptosis and brain development

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Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11583631

1 reference

Consolidated OpenCitations Corpus – April 2017