Co-chaperone Regulation of Conformational Switching in the Hsp90 ATPase Cycle
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Heat-shock protein 90, a chaperone for folding and regulation
2. Structure, function, and mechanism of the Hsp90 molecular chaperone
3. Regulation of Signaling Protein Function and Trafficking by the hsp90/hsp70-Based Chaperone Machinery
4. Structure and Functional Relationships of Hsp90
5. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone invivo
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