Prodromou, C. (2009) Strategies for Stalling Malignancy: Targeting Cancer's Addiction to Hsp90. CURRENT TOPICS IN MEDICINAL CHEMISTRY, 9 (15). pp. 1352-1368. ISSN 1568-0266

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Abstract

Hsp90 is involved in the maturation and activation of client proteins. Often these are key proteins involved in signal transduction and regulatory pathways that in a mutated and/or deregulated form sustain an oncogenic cellular state. Consequently, the malignancy is maintained with the aid of Hsp90 upon which the mutated proteins have become particularly dependent for their activity. The requirement for the Hsp90 chaperone machine to drive the malignancy makes Hsp90 a prime anticancer target, an `axle in a wheel' that when disrupted has been shown to be effective in killing cancerous cells. This review aims to identify potential drug targets, based on the current structural knowledge of the Hsp90-chaperone machine, that could be targeted with the aim of disrupting its functioning and promoting an anti-cancer activity.

Item Type:	Review Article
Authors (ICR Faculty only):	Prodromou, Chris
All Authors:	Prodromou, C.
Uncontrolled Keywords:	Heat shock protein; Hsp90; co-chaperones; cancer; drug design;HEAT-SHOCK-PROTEIN; ESCHERICHIA-COLI HSP90; N-TERMINAL DOMAIN; PHASE-II TRIAL; MOLECULAR CHAPERONE; CRYSTAL-STRUCTURE; ATPASE CYCLE; STEROID-RECEPTOR; ANTICANCER AGENT; STRUCTURAL BASIS
Research teams:	Closed research groups > Other closed groups
Depositing User:	Users 10 not found.
Date Deposited:	04 Jan 2010 10:52
Last Modified:	19 Aug 2011 09:42
URI:	http://publications.icr.ac.uk/id/eprint/9157

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