An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity-Reference-Cited by-同舟云学术

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An unexpected second binding site for polypeptide substrates is essential for Hsp70 chaperone activity

Published:2020-01 Issue:2 Volume:295 Page:584-596
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Li Hongtao,Zhu Huanyu,Sarbeng Evans Boateng,Liu Qingdai,Tian Xueli,Yang Ying,Lyons Charles,Zhou Lei,Liu Qinglian

Funder

HHS | NIH | National Institute of General Medical Sciences

Division of Intramural Research, National Institute of Allergy and Infectious Diseases

American Heart Association

Virginia Commonwealth University

Division of Cancer Prevention, National Cancer Institute

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference93 articles.

1. Hsp70 chaperones: cellular functions and molecular mechanism;Mayer;Cell. Mol. Life Sci,2005

2. Converging concepts of protein folding in vitro in vivo;Hartl;Nat. Struct. Mol. Biol,2009

3. Molecular chaperones and protein quality control;Bukau;Cell,2006

4. Getting newly synthesized proteins into shape;Bukau;Cell,2000

5. The Hsp70 and Hsp60 chaperone machines;Bukau;Cell,1998

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2. The Hsp70 and JDP proteins: Structure-function perspective on molecular chaperone activity;History of The Enzymes, Current Topics and Future Perspectives;2023

3. Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress;Journal of Molecular Biology;2022-10

4. Conserved and divergent peptide substrate binding properties of bacterial Hsp70;2022-08-13

5. ThhspA1 is involved in lacA transcriptional regulation of Trametes hirsuta AH28-2 exposed to o-toluidine;Fungal Genetics and Biology;2022-07

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