The Hsp90 chaperone machinery: from structure to drug development

Volume: 42, Issue: 10, Pages: 623 - 630
Published: Oct 31, 2009
Abstract
Hsp90, an evolutionarily conserved molecular chaperone, is involved in the folding, stabilization, activation, and assembly of a wide range of 'client' proteins, thus playing a central role in many biological processes. Especially, several oncoproteins act as Hsp90 client proteins and tumor cells require higher Hsp90 activity than normal cells to maintain their malignancy. For this reason, Hsp90 has emerged as a promising target for anti-cancer...
Paper Details
Title
The Hsp90 chaperone machinery: from structure to drug development
Published Date
Oct 31, 2009
Volume
42
Issue
10
Pages
623 - 630
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