The structure of a β₂-microglobulin fibril suggests a molecular basis for its amyloid polymorphism

Iadanza, MG, Silvers, R, Boardman, J et al. (7 more authors) (2018) The structure of a β₂-microglobulin fibril suggests a molecular basis for its amyloid polymorphism. Nature Communications, 9. 4517. ISSN 2041-1723

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Copyright, Publisher and Additional Information: © 2018, The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Dates:
  • Published: 30 October 2018
  • Accepted: 20 September 2018
  • Published (online): 30 October 2018
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds)
The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Cryo EM, Image Processing (Leeds)
The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds)
Funding Information:
FunderGrant number
Wellcome Trust108466/Z/15/Z
Depositing User: Symplectic Publications
Date Deposited: 26 Sep 2018 12:41
Last Modified: 03 Dec 2018 16:24
Status: Published
Publisher: Nature Research
Identification Number: https://doi.org/10.1038/s41467-018-06761-6

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