The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function-Reference-Cited by-同舟云学术

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The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function

Published:2014-12-02 Issue:50 Volume:111 Page:17881-17886
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proc Natl Acad Sci USA

Author:

Jahn Markus,Rehn Alexandra,Pelz Benjamin,Hellenkamp Björn,Richter Klaus,Rief Matthias,Buchner Johannes,Hugel Thorsten

Funder

Deutsche Forschungsgemeinschaft (DFG)

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference31 articles.

1. Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery;Pratt;Exp Biol Med (Maywood),2003

2. Navigating the Chaperone Network: An Integrative Map of Physical and Genetic Interactions Mediated by the Hsp90 Chaperone

3. Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition

4. In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis

5. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivo

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