Sarell, CJ, Stockley, PG and Radford, SE (2013) Assessing the causes and consequences of co-polymerization in amyloid formation. Prion, 7 (5). 359 - 368. ISSN 1933-6896
Abstract
How, and why, different proteins form amyloid fibrils is most often studied in vitro using a single purified protein sequence. However, many amyloid diseases involve co-aggregation of different protein species, including proteins with/without post-translational modifications (e.g., different strains of PrP), proteins of different length (e.g., β2-microglobulin and ΔN6, Aβ40, and Aβ42), sequence variants (e.g., Aβ and AβARC), and proteins from different organisms (e.g., bovine PrP and human PrP). The consequences of coaggregation of different proteins upon the structure, stability, species transmission and toxicity of the resulting amyloid aggregates is discussed here, including the role of co-aggregation in expanding the repertoire of oligomeric and fibrillar structures and how this can affect their biological and biophysical properties.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2013, Sarell, CJ, Stockley, PG and Radford, SE. This is an Open Access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 3.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. |
Keywords: | Amyloid; fibril; heteropolymers; polymorph; seeding; strain |
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) |
Depositing User: | Symplectic Publications |
Date Deposited: | 22 Sep 2014 10:39 |
Last Modified: | 17 Jan 2018 18:09 |
Published Version: | http://dx.doi.org/10.4161/pri.26415 |
Status: | Published |
Publisher: | Landes Bioscience |
Identification Number: | 10.4161/pri.26415 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:80193 |