Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins

Martin, EM, Jackson, MP, Gamerdinger, M et al. (6 more authors) (2018) Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins. Journal of Biological Chemistry, 293 (22). pp. 8554-8568. ISSN 0021-9258

Abstract

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Authors/Creators:
Copyright, Publisher and Additional Information: © 2018 by The American Society for Biochemistry and Molecular Biology, Inc. This is an open access article under the terms of the Creative Commons Attribution License (CC BY 4.0). A copy of the license can be found at: https://creativecommons.org/licenses/by/4.0/
Keywords: NAC; protein folding; molecular chaperone; protein cross-linking; chaperone protein misfolding
Dates:
  • Accepted: 12 April 2018
  • Published (online): 12 April 2018
  • Published: 1 June 2018
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds)
The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 16 Apr 2018 15:35
Last Modified: 06 Jul 2018 22:01
Status: Published
Publisher: American Society for Biochemistry and Molecular Biology
Identification Number: https://doi.org/10.1074/jbc.RA117.001568

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