Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90
Document Type
Article
Publication Date
2-14-2008
Abstract
Heat shock protein 90 (Hsp90) is a molecular chaperone that is responsible for activating many signaling proteins and is a promising target in tumor biology. We have identified small-molecule benzisoxazole derivatives as Hsp90 inhibitors. Crystallographic studies show that these compounds bind in the ATP binding pocket interacting with the Asp93. Structure based optimization led to the identification of potent analogues, such as 13, with good biochemical profiles. © 2008 American Chemical Society.
Publication Title
Journal of Medicinal Chemistry
First Page Number
373
Last Page Number
375
DOI
10.1021/jm701385c
Recommended Citation
Gopalsamy, Ariamala; Shi, Mengxiao; Golas, Jennifer; Vogan, Erik; Jacob, Jaison; Johnson, Mark; Lee, Frederick; Nilakantan, Ramaswamy; Petersen, Roseann; Svenson, Kristin; Chopra, Rajiv; Tam, May S.; Wen, Yingxia; Ellingboe, John; Arndt, Kim; and Boschelli, Frank, "Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90" (2008). Kean Publications. 2486.
https://digitalcommons.kean.edu/keanpublications/2486