Conformational equilibria in allosteric control of Hsp70 chaperones-Reference-Cited by-同舟云学术

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Conformational equilibria in allosteric control of Hsp70 chaperones

Published:2021-10 Issue:19 Volume:81 Page:3919-3933.e7
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Wang Wei,Liu Qinglian,Liu Qun,Hendrickson Wayne A.

Funder

Argonne National Laboratory

Columbia University

Virginia Commonwealth University

National Institutes of Health

American Heart Association

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference68 articles.

1. PHENIX: a comprehensive Python-based system for macromolecular structure solution;Adams;Acta Crystallogr. D Biol. Crystallogr.,2010

2. Principles that govern the folding of protein chains;Anfinsen;Science,1973

3. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate;Bertelsen;Proc. Natl. Acad. Sci. USA,2009

4. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication;Buchberger;J. Biol. Chem.,1995

5. Mutations in the C-terminal fragment of DnaK affecting peptide binding;Burkholder;Proc. Natl. Acad. Sci. USA,1996

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