Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

The in vivo function of the heat shock protein 90 (Hsp90) molecular chaperone is dependent on the binding and hydrolysis of ATP, and on interactions with a variety of co-chaperones containing tetratricopeptide repeat (TPR) domains. We have now analysed the interaction of the yeast TPR-domain co-chap...

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Bibliographic Details
Main Authors:	Prodromou, C, Siligardi, G, O'Brien, R, Woolfson, D N, Regan, L, Panaretou, B, Ladbury, J E, Piper, P W, Pearl, L H
Format:	Artigo
Language:	Inglês
Published:	1999
Subjects:	Research Article
Online Access:	https://ncbi.nlm.nih.gov/pmc/articles/PMC1171168/ https://ncbi.nlm.nih.gov/pubmed/9927435 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/18.3.754
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Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones.

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