| Literature DB >> 18511277 |
Thomas E Barta1, James M Veal, John W Rice, Jeffrey M Partridge, R Patrick Fadden, Wei Ma, Matthew Jenks, Lifeng Geng, Gunnar J Hanson, Kenneth H Huang, Amy F Barabasz, Briana E Foley, James Otto, Steven E Hall.
Abstract
Hsp90 maintains the conformational stability of multiple proteins implicated in oncogenesis and has emerged as a target for chemotherapy. We report here the discovery of a novel small molecule scaffold that inhibits Hsp90. X-ray data show that the scaffold binds competitively at the ATP site on Hsp90. Cellular proliferation and client assays demonstrate that members of the series are able to inhibit Hsp90 at nanomolar concentrations.Entities:
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Year: 2008 PMID： 18511277 DOI： 10.1016/j.bmcl.2008.05.023
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823