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- W3037825825 abstract "Significant advances have been made toward discovering allosteric inhibitors for challenging drug targets such as the Ras family of membrane-associated signaling proteins. Malfunction of Ras proteins due to somatic mutations is associated with up to a quarter of all human cancers. Computational techniques have played critical roles in identifying and characterizing allosteric ligand-binding sites on these proteins, and to screen ligand libraries against those sites. These efforts, combined with a wide range of biophysical, structural, biochemical and cell biological experiments, are beginning to yield promising inhibitors to treat malignancies associated with mutated Ras proteins. In this chapter, we discuss some of these developments and how the lessons learned from Ras might be applied to similar other challenging drug targets." @default.
- W3037825825 created "2020-07-02" @default.
- W3037825825 creator A5033192681 @default.
- W3037825825 creator A5087588530 @default.
- W3037825825 date "2020-01-01" @default.
- W3037825825 modified "2023-10-04" @default.
- W3037825825 title "How to make an undruggable enzyme druggable: lessons from ras proteins" @default.
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