Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Martínez-Lumbreras, S., Krysztofinska, E.M., Thapaliya, A. et al. (10 more authors) (2018) Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. BMC Biology, 16. 76. ISSN 1741-7007

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Item Type: Article
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© Isaacson et al. 2018. This is an open access article under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited.

Keywords: Hydrophobic Substrates; Endoplasmic Reticulum-associated Degradation; Protein Quality Control Mechanisms; BCL2-associated Athanogene (BAG6); Double Electron–electron Resonance (DEER)
Dates:
  • Published: 11 July 2018
  • Accepted: 20 June 2018
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 15 Jan 2024 13:08
Last Modified: 15 Jan 2024 13:08
Published Version: http://dx.doi.org/10.1186/s12915-018-0542-3
Status: Published
Publisher: BMC
Identification Number: 10.1186/s12915-018-0542-3
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