Solution structure of BID, an intracellular amplifier of apoptotic signaling (Q27617719)

2

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G S Salvesen

3

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J Yuan

4

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G Wagner

The Bcl-2 protein family: arbiters of cell survival

5

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language of work or name

English

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publication date

5 March 1999

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published in

Cell

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volume

96

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issue

5

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page(s)

615-24

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cites work

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Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

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Conversion of Bcl-2 to a Bax-like death effector by caspases

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Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Apoptotic pathways: the roads to ruin

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NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

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Bax directly induces release of cytochrome c from isolated mitochondria

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Bcl-2 and Bax function independently to regulate cell death

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Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c.

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

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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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Structure of translation factor eIF4E bound to m7GDP and interaction with 4E-binding protein

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Cytoprotection by Bcl-2 requires the pore-forming alpha5 and alpha6 helices

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Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists

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