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Targeting Dynamic ATP-Binding Site Features Allows Discrimination between Highly Homologous Protein Kinases.
A series of inhibitors that are highly selective for the ATP-binding sites of the Src-family kinases Lyn and Hck are described, and it is shown that sensitivity to this class of selective inhibitors is due to the identity of residues that control the conformational flexibility of helix αC rather than any specific ATP- binding site interactions. Expand
Allosteric Modulation of JNK Docking Site Interactions with ATP-Competitive Inhibitors.
Results demonstrate that there is functional allostery between the ATP-binding sites and DRSs of these kinases, and suggest that ATP-competitive inhibitors can allosterically influence the intracellular binding partners of the JNKs. Expand
Total synthesis of a tetracyclic anti-tumor, UCE6.