Disease variants of FGFR3 reveal molecular basis for the recognition and new roles for Cdc37 in Hsp90 chaperone system

Bunney, TD, Inglis, AJ, Sanfelice, D et al. (9 more authors) (2018) Disease variants of FGFR3 reveal molecular basis for the recognition and new roles for Cdc37 in Hsp90 chaperone system. Structure, 26 (3). pp. 446-458. ISSN 0969-2126

Metadata

Authors/Creators:
Copyright, Publisher and Additional Information: (c) 2018 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0
Keywords: Cdc37 cochaperone; Hsp90 chaperone; client kinases; fibroblast growth factor receptors; cancer; disease-linked mutations; structural and mechanistic insights; protein folding
Dates:
  • Accepted: 5 January 2018
  • Published (online): 22 February 2018
  • Published: 6 March 2018
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > NMR (Leeds)
Funding Information:
FunderGrant number
Wellcome Trust109155/Z/15/Z
Depositing User: Symplectic Publications
Date Deposited: 30 Jan 2018 15:33
Last Modified: 25 Jun 2023 21:13
Status: Published
Publisher: Elsevier
Identification Number: https://doi.org/10.1016/j.str.2018.01.016

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