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- W4213133081 abstract "The BH3-only proteins of the BCL-2 family require multidomain proapoptotic members BAX and BAK to release cytochrome c from mitochondria and kill cells. We find short peptides representing the alpha-helical BH3 domains of BID or BIM are capable of inducing oligomerization of BAK and BAX to release cytochrome c. Another subset characterized by the BH3 peptides from BAD and BIK cannot directly activate BAX, BAK but instead binds antiapoptotic BCL-2, resulting in the displacement of BID-like BH3 domains that initiate mitochondrial dysfunction. Transduced BAD-like and BID-like BH3 peptides also displayed synergy in killing leukemic cells. These data support a two-class model for BH3 domains: BID-like domains that activate BAX, BAK and BAD-like domains that sensitize by occupying the pocket of antiapoptotic members. PMID: 12242151 Funding information This work was supported by: NCI NIH HHS, United States Grant ID: CA 92625" @default.
- W4213133081 created "2022-02-24" @default.
- W4213133081 creator A5066158171 @default.
- W4213133081 date "2002-09-12" @default.
- W4213133081 modified "2023-10-05" @default.
- W4213133081 title "Faculty Opinions recommendation of Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics." @default.
- W4213133081 doi "https://doi.org/10.3410/f.1009339.122058" @default.
- W4213133081 hasPublicationYear "2002" @default.
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