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• W2893860857 abstract "Cancer cells overexpress a diversity of anti-apoptotic BCL-2 family proteins, such as BCL-2, MCL-1, and BFL-1/A1, to enforce cellular immortality. Thus, intensive drug development efforts have focused on targeting this class of oncogenic proteins to overcome treatment resistance. Whereas a selective BCL-2 inhibitor has been FDA approved and several small molecule inhibitors of MCL-1 have recently entered phase I clinical testing, BFL-1/A1 remains undrugged. Here, we developed a series of stapled peptide design principles to engineer a functionally selective and cell-permeable BFL-1/A1 inhibitor that is specifically cytotoxic to BFL-1/A1-dependent human cancer cells. Because cancers harbor a diversity of resistance mechanisms and typically require multi-agent treatment, we further investigated BFL-1/A1 co-dependencies by mining a genome-scale CRISPR-Cas9 screen. We identified ataxia-telangiectasia-mutated (ATM) kinase as a BFL-1/A1 co-dependency in acute myeloid leukemia (AML), which informed the validation of BFL-1/A1 and ATM inhibitor co-treatment as a synergistic approach to subverting apoptotic resistance in cancer." @default.
• W2893860857 created "2018-10-05" @default.
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• W2893860857 date "2018-09-01" @default.
• W2893860857 modified "2023-10-17" @default.
• W2893860857 title "Precision Targeting of BFL-1/A1 and an ATM Co-dependency in Human Cancer" @default.
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• W2893860857 doi "https://doi.org/10.1016/j.celrep.2018.08.089" @default.
• W2893860857 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6365304" @default.
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