The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.

Hsp90 is a dimeric ATPase responsible for the activation or maturation of a specific set of substrate proteins termed 'clients'. This molecular chaperone acts in the context of a structurally dynamic and highly regulated cycle involving ATP, co-chaperone proteins and clients. Co-chaperone...

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Bibliographic Details

Published in:	PLoS ONE
Main Authors:	Heather Armstrong, Annemarie Wolmarans, Rebecca Mercier, BaoChan Mai, Paul LaPointe
Format:	Article
Language:	English
Published:	Public Library of Science (PLoS) 2012-01-01
Online Access:	http://europepmc.org/articles/PMC3498168?pdf=render