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1554202 
Journal Article 
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones 
Li, J; Soroka, J; Buchner, J 
2012 
1 
Biochimica et Biophysica Acta. Molecular Cell Research
ISSN: 0167-4889
EISSN: 1879-2596 
1823 
3 
624-635 
21951723 
WOS:000301628700004 
Hsp90 is a dimeric molecular chaperone required for the
activation and stabilization of numerous client proteins many of which are involved in essential
cellular processes like signal transduction pathways. This activation process is regulated by
ATP-induced large conformational changes, co-chaperones and posttranslational modifications. For
some co-chaperones, a detailed picture on their structures and functions exists, for others their
contributions to the Hsp90 system is still unclear. Recent progress on the conformational
dynamics of Hsp90 and how co-chaperones affect the Hsp90 chaperone cycle significantly increased
our understanding of the gearings of this complex molecular machinery. This article is part of a
Special Issue entitled: Heat Shock Protein 90 (Hsp90). (C) 2011 Elsevier B.V. All rights 
Co-chaperones; Hsp90 clients; Conformational regulation; ATPase; Posttranslational modifications