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- W2022754948 abstract "The existence of drug resistance caused by mutations in the break-point cluster region-Abelson (BCR-ABL) tyrosine kinase domain remains a clinical challenge due to limited treatment options for effective CML therapies. Here, we report a series of flavone-based common inhibitors equipotent for the wild type and the most drug-resistant T315I mutant of BCR-ABL. The original hit 1 was extensively modified through a structure-based drug design strategy, especially by varying the C7 acetamide appendage of the scaffold to exploit extended interactions with P-loop residues. Structural features relevant to the stabilization of the newly identified inhibitors in the ATP-binding site of ABL are discussed in detail." @default.
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- W2022754948 date "2013-08-01" @default.
- W2022754948 modified "2023-10-16" @default.
- W2022754948 title "Structure-based design of flavone-based inhibitors of wild-type and T315I mutant of ABL" @default.
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- W2022754948 doi "https://doi.org/10.1016/j.bmcl.2013.05.095" @default.
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