A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone-Reference-Cited by-同舟云学术

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A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone

Published:2020-12 Issue:24 Volume:432 Page:166708
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Siegel Alex,McAvoy Camille Z.,Lam Vinh,Liang Fu-Cheng,Kroon Gerard,Miaou Emily,Griffin Patrick,Wright Peter E.,Shan Shu-ou

Funder

National Institute of General Medical Sciences

Biological and Environmental Research

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference76 articles.

1. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones;Zhuravleva;Proc. Natl. Acad. Sci. USA,2011

2. Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex;Ali;Nature,2006

3. HSP100/Clp proteins: a common mechanism explains diverse functions;Schirmer;Trends Biochem. Sci.,1996

4. Alternative bacterial two-component small heat shock protein systems;Bepperling;Proc. Natl. Acad. Sci. USA,2012

5. Conditional disorder in chaperone action;Bardwell;Trends Biochem. Sci.,2012

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1. EPR Studies of Chaperone Interactions and Dynamics;Biophysics of Molecular Chaperones;2023-11-01

2. Chloroplast SRP43 and SRP54 independently promote thermostability and membrane binding of light‐dependent protochlorophyllide oxidoreductases;The Plant Journal;2023-06-14

3. Intrinsic disorder and allosteric regulation;Structure and Intrinsic Disorder in Enzymology;2023

4. ATP-Independent Chaperones;Annual Review of Biophysics;2022-05-09

5. Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems;Chemical Reviews;2021-09-07

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