X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death (Q27733156)

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H Liang

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R P Meadows

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J E Harlan

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H S Yoon

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D Nettesheim

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B S Chang

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C B Thompson

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S L Wong

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S L Ng

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S W Fesik

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language of work or name

English

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publication date

23 May 1996

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published in

Nature

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volume

381

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issue

6580

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page(s)

335-41

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cites work

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bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic 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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Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins

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Bax-independent inhibition of apoptosis by Bcl-XL.

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The protein bcl-2 alpha does not require membrane attachment, but two conserved domains to suppress apoptosis

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Structure-function analysis of Bcl-2 protein. Identification of conserved domains important for homodimerization with Bcl-2 and heterodimerization with Bax.

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Multiple Bcl-2 family members demonstrate selective dimerizations with Bax

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

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Evidence that BCL-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+ fluxes

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Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death

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