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- W2069908535 abstract "Heat shock protein 90 (Hsp90) is a molecular chaperone that plays an important role in regulating the maturation and stabilization of many oncogenic proteins. In an attempt to discover a new class of Hsp90 inhibitors, a series of 1,3,5-triazine compounds were rationally designed, synthesized, and their biological activities were evaluated. Compound 3b was found to degrade Hsp90's client proteins of Her2, Met and Akt and to induce the expression level of Hsp70. The binding mode of 3b in the ATP-binding site of Hsp90 was predicted by the molecular docking." @default.
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- W2069908535 date "2013-12-01" @default.
- W2069908535 modified "2023-09-26" @default.
- W2069908535 title "Targeting the hydrophobic region of Hsp90’s ATP binding pocket with novel 1,3,5-triazines" @default.
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- W2069908535 doi "https://doi.org/10.1016/j.bmcl.2013.09.050" @default.
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