Closing in on the Hsp90 chaperone-client relationship

Klaus Richter; Johannes Buchner

doi:10.1016/j.str.2011.03.007

Closing in on the Hsp90 chaperone-client relationship

Klaus Richter, Johannes Buchner

Publikation: Beitrag in Fachzeitschrift › Kurzer Abriss › Begutachtung

11 Zitate (Scopus)

Abstract

The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

Originalsprache	Englisch
Seiten (von - bis)	445-446
Seitenumfang	2
Fachzeitschrift	Structure
Jahrgang	19
Ausgabenummer	4
DOIs	https://doi.org/10.1016/j.str.2011.03.007
Publikationsstatus	Veröffentlicht - 13 Apr. 2011

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10.1016/j.str.2011.03.007

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abstract = "The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.",

author = "Klaus Richter and Johannes Buchner",

note = "Funding Information: Work in the authors' labs was supported by grants from the DFG, the BMBF, and the Fonds der chemischen Industrie. The authors thank Jing Li for help with the artwork, and Marco Retzlaff for stimulating discussions.",

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PY - 2011/4/13

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AB - The molecular chaperone Hsp90 regulates the activity and stability of a set of client proteins. Despite progress in understanding its mechanism, the interaction of Hsp90 with clients has remained enigmatic. Now, in a recent issue of Molecular Cell, Street and coworkers present results that integrate the client in the Hsp90 chaperone cycle.

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Closing in on the Hsp90 chaperone-client relationship

Abstract

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