Jarosz-Griffiths, HH orcid.org/0000-0001-5154-4815, Noble, E, Rushworth, JV et al. (1 more author) (2016) Amyloid-β Receptors: The Good, the Bad, and the Prion Protein. Journal of Biological Chemistry, 291 (7). pp. 3174-3183. ISSN 0021-9258
Abstract
Several different receptor proteins have been identified that bind monomeric, oligomeric, or fibrillar forms of amyloid-β (Aβ). “Good” receptors internalize Aβ or promote its transcytosis out of the brain, whereas “bad” receptors bind oligomeric forms of Aβ that are largely responsible for the synapticloss, memory impairments, and neurotoxicity that underlie Alzheimer disease. The prion protein both removes Aβ from the brain and transduces the toxic actions of Aβ. The clustering of distinct receptors in cell surface signaling platforms likely underlies the actions of distinct oligomeric species of Aβ. These Aβ receptor-signaling platforms provide opportunities for therapeutic intervention in Alzheimer disease.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license: https://creativecommons.org/licenses/by/4.0/ |
Keywords: | Alzheimer disease; amyloid; oligomer; prion; receptor |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Medicine (Leeds) > Institute of Rheumatology & Musculoskeletal Medicine (LIRMM) (Leeds) > Clinical Musculoskeletal Medicine (LIRMM) (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 09 Jan 2019 15:19 |
Last Modified: | 25 Jun 2023 21:39 |
Status: | Published |
Publisher: | American Society for Biochemistry and Molecular Biology |
Identification Number: | 10.1074/jbc.R115.702704 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:140758 |
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