Structural basis of the key residue W320 responsible for Hsp90 conformational change
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK, USA
Funder
NIH
Oklahoma Agricultural Experiment Station at Oklahoma State University
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2022.2146197
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1. PHENIX: a comprehensive Python-based system for macromolecular structure solution
2. Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
3. A Novel Class of Hsp90 C-Terminal Modulators Have Pre-Clinical Efficacy in Prostate Tumor Cells Without Induction of a Heat Shock Response
4. Post-translational modifications of Hsp90 and translating the chaperone code
5. Structure, Function, and Regulation of the Hsp90 Machinery
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