Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers

Dawes, S., Hurst, N. orcid.org/0000-0003-3850-6640, Grey, G. et al. (8 more authors) (2024) Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers. Life Science Alliance, 7 (10). e202402702. ISSN 2575-1077

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Item Type: Article
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© 2024 Dawes et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution Licence (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Keywords: Protein Serine-Threonine Kinases; Endoplasmic Reticulum Stress; Endoplasmic Reticulum Chaperone BiP; Protein Binding; Heat-Shock Proteins; Endoribonucleases; Humans; Endoplasmic Reticulum; Unfolded Protein Response; Protein Multimerization; HSP70 Heat-Shock Proteins; Protein Folding; Molecular Chaperones; Protein Domains
Dates:
  • Published: 5 August 2024
  • Published (online): 5 August 2024
  • Accepted: 24 July 2024
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > Department of Chemistry (Sheffield)
Depositing User: Symplectic Sheffield
Date Deposited: 19 Aug 2024 10:26
Last Modified: 19 Aug 2024 10:26
Published Version: http://dx.doi.org/10.26508/lsa.202402702
Status: Published
Publisher: Life Science Alliance, LLC
Refereed: Yes
Identification Number: 10.26508/lsa.202402702
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