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- W2336691225 abstract "Myeloid cell leukemia 1 (Mcl-1), a potent anti-apoptotic protein of the BCL2 family, has been studied as a key resistance factor in human cancers. Restoring apoptotic signals by inactivating Mcl-1 protein interactions with small molecule inhibitors has been intensively pursued as targets for cancer therapeutics. We herein describe our effort towards the structure-based design, synthesis and evaluation of first potent, covalent binders of Mcl-1. The resulting inhibitors specifically modified a non-catalytic lysine residue with high level of Mcl-1 potency in biochemical and cell based assays. Our covalent inhibitors could provide potent probes to interrogate Mcl-1 dependent cancer biology. Citation Format: Qibin Su, Gizem Akcay, Neil Grimster, Matthew Belmonte, Philip Rawlins, Michelle Lamb, Alexander Hird, Brian Aquila. Inhibition of Mcl-1 through covalent modification of a non-catalytic lysine side chain. [abstract]. In: Proceedings of the AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics; 2015 Nov 5-9; Boston, MA. Philadelphia (PA): AACR; Mol Cancer Ther 2015;14(12 Suppl 2):Abstract nr C40." @default.
- W2336691225 created "2016-06-24" @default.
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- W2336691225 date "2015-12-01" @default.
- W2336691225 modified "2023-10-14" @default.
- W2336691225 title "Abstract C40: Inhibition of Mcl-1 through covalent modification of a non-catalytic lysine side chain" @default.
- W2336691225 doi "https://doi.org/10.1158/1535-7163.targ-15-c40" @default.
- W2336691225 hasPublicationYear "2015" @default.
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