Young, LM, Ashcroft, AE and Radford, SE orcid.org/0000-0002-3079-8039 (2017) Small molecule probes of protein aggregation. Current Opinion in Chemical Biology, 39. pp. 90-99. ISSN 1367-5931
Abstract
Understanding the mechanisms of amyloid formation and toxicity remain major challenges. Whilst substantial progress has been made in the development of methods able to identify the species formed during self-assembly and to describe the kinetic mechanisms of aggregation, the structure(s) of non-native species, including potentially toxic oligomers, remain elusive. Moreover, how fibrils contribute to disease remains unclear. Here we review recent advances in the development of small molecules and other reagents that are helping to define the mechanisms of protein aggregation in molecular detail. Such probes form a powerful platform with which to better define the mechanisms of structural conversion into amyloid fibrils and may provide the much-needed stepping stone for future development of successful therapeutic agents.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
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) > Structural Molecular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 14 Jun 2017 09:05 |
Last Modified: | 23 Jun 2023 22:30 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.cbpa.2017.06.008 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:117647 |