Tipping, KW, Van Oosten-Hawle, P, Hewitt, EW et al. (1 more author) (2015) Amyloid fibres: inert end-stage aggregates or key players in disease? Trends in Biochemical Sciences, 40 (12). pp. 719-727. ISSN 0968-0004
Abstract
The formation of amyloid fibres is a hallmark of amyloid disorders. Nevertheless, the lack of correlation between fibre load and disease as observed, for example, in Alzheimer's disease, means that fibres are considered secondary contributors to the onset of cellular dysfunction. Instead, soluble intermediates of amyloid assembly are often described as the agents of toxicity. Here, we discuss recent experimental discoveries which suggest that amyloid fibres should be considered as disease-relevant species that can mediate a range of pathological processes. These include disruption of biological membranes, secondary nucleation, amyloid aggregate transmission, and the disruption of protein homeostasis (proteostasis). Thus, a greater understanding of amyloid fibre biology could enhance prospects of developing therapeutic interventions against this devastating class of protein-misfolding disorders.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2015 Elsevier Ltd. All rights reserved. This is an author produced version of a paper published in Trends in Biochemical Sciences. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Amyloid, Fibres, Transmission, Disease |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Funding Information: | Funder Grant number EU - European Union 322408 Wellcome Trust 092896/Z/10/Z |
Depositing User: | Symplectic Publications |
Date Deposited: | 06 Nov 2015 11:01 |
Last Modified: | 04 Nov 2016 01:22 |
Published Version: | http://dx.doi.org/10.1016/j.tibs.2015.10.002 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.tibs.2015.10.002 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:91487 |