Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance-Reference-Cited by-同舟云学术

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Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance

Published:2017-05 Issue:21 Volume:292 Page:8773-8785
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Lai Alex L.,Clerico Eugenia M.,Blackburn Mandy E.,Patel Nisha A.,Robinson Carol V.,Borbat Peter P.,Freed Jack H.,Gierasch Lila M.

Funder

National Institute of General Medical Sciences

Wellcome Trust

European Research Council

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference54 articles.

1. The changing landscape of protein allostery;Swain;Curr. Opin. Struct. Biol,2006

2. In vivo aspects of protein folding and quality control;Balchin;Science,2016

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

4. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein;Flaherty;Nature,1990

5. Structural analysis of substrate binding by the molecular chaperone DnaK;Zhu;Science,1996

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