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Cell Membrane Permeability
Mitochondrial Membrane Transport Proteins
tBid elicits a conformational alteration in membrane-bound Bcl-2 such that it inhibits Bax pore formation.
The cytosolic domain of Bcl-2 forms small pores in model mitochondrial outer membrane after acidic pH-induced membrane association.
The Bax BH3 peptide H2-H3 promotes apoptosis by inhibiting Bcl-2's pore-forming and anti-Bax activities in the membrane.
Hyaluronan synthase mediates dye translocation across liposomal membranes.
Auto-activation of the apoptosis protein Bax increases mitochondrial membrane permeability and is inhibited by Bcl-2.
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.
Membrane topography and topogenesis of prenylated Rab acceptor (PRA1).
The cytosolic domain of Bcl-2 oligomerizes to form pores in model mitochondrial outer membrane at acidic pH.
Photocrosslinking Approach to Investigate Protein Interactions in the BCL-2 Family.
Oligomerization of membrane-bound Bcl-2 is involved in its pore formation induced by tBid.
BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes.
Structure-Function of Bcl-2 Related Apoptosis Regulators in Membranes
Cysteine-based crosslinking approach for characterization of oligomeric pore-forming proteins in the mitochondrial membranes.