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Bcl-XL protein

Ottilie S, Diaz JL, Horne W, Chang J, Wang Y, Wilson G, Chang S, Weeks S, Fritz LC, Oltersdorf T (1997), Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins, J. Biol. Chem. 272 30866-30872. [Pg.177]

Susceptibility to drug-induced apoptosis correlates with differential modulation of Bad, Bcl-2 and Bcl-xL protein levels, Cell Death and Differentiation 7 574-586. [Pg.14]

Examples of anti-apoptotic proteins degraded by caspases are the Bcl-2 and Bcl-xL proteins, which are cleaved by caspase-3 to generate C-terminal fragments that are pro-apoptotic. Caspase-8 cleaves the pro-apoptotic protein Bid (see Section 15.4), generating a C-terminal fragment that induces release of cytochrome c from mitochondria. [Pg.517]

The second kingianin paper also tabulated the activities of the kingianins in an affinity displacement assay with the Bcl-xL protein, a member of the Bel family that is involved in the regulation of apoptosis. Inhibitors of the antiapoptotic Bel proteins are of significant interest in the search for anticancer drugs with new mechanisms of action. ... [Pg.58]

See other pages where Bcl-XL protein is mentioned: [Pg.824]    [Pg.428]    [Pg.443]    [Pg.12]    [Pg.314]    [Pg.122]    [Pg.12]    [Pg.357]    [Pg.523]    [Pg.532]    [Pg.534]    [Pg.824]    [Pg.181]    [Pg.553]    [Pg.554]    [Pg.522]    [Pg.62]    [Pg.929]    [Pg.266]    [Pg.45]    [Pg.437]    [Pg.51]   
See also in sourсe #XX -- [ Pg.6 ]

See also in sourсe #XX -- [ Pg.279 , Pg.292 , Pg.297 ]

See also in sourсe #XX -- [ Pg.53 ]



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