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Lin, Jialing
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Concept Proto-Oncogene Proteins c-bcl-2
Academic Article tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation.
Academic Article The Bax BH3 peptide H2-H3 promotes apoptosis by inhibiting Bcl-2's pore-forming and anti-Bax activities in the membrane.
Academic Article Bcl-2 homodimerization involves two distinct binding surfaces, a topographic arrangement that provides an effective mechanism for Bcl-2 to capture activated Bax.
Academic Article Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2.
Academic Article Bcl-2 and Bax interact via the BH1-3 groove-BH3 motif interface and a novel interface involving the BH4 motif.
Academic Article After embedding in membranes antiapoptotic Bcl-XL protein binds both Bcl-2 homology region 3 and helix 1 of proapoptotic Bax protein to inhibit apoptotic mitochondrial permeabilization.
Academic Article The cytosolic domain of Bcl-2 oligomerizes to form pores in model mitochondrial outer membrane at acidic pH.
Academic Article Photocrosslinking Approach to Investigate Protein Interactions in the BCL-2 Family.
Academic Article Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid.
Academic Article Bax forms an oligomer via separate, yet interdependent, surfaces.
Academic Article A protein bridge to death between the ER and mitochondria.
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  • Proto Oncogene Proteins c bcl 2