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Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides

Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction...

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Detalles Bibliográficos
Autores principales: Rajput, Sunnia, Sani, Marc-Antoine, Keizer, David W., Separovic, Frances
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286822/
https://www.ncbi.nlm.nih.gov/pubmed/34156433
http://dx.doi.org/10.1042/BST20201244
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author Rajput, Sunnia
Sani, Marc-Antoine
Keizer, David W.
Separovic, Frances
author_facet Rajput, Sunnia
Sani, Marc-Antoine
Keizer, David W.
Separovic, Frances
author_sort Rajput, Sunnia
collection PubMed
description Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes.
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spelling pubmed-82868222021-08-02 Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides Rajput, Sunnia Sani, Marc-Antoine Keizer, David W. Separovic, Frances Biochem Soc Trans Review Articles Alzheimer's disease (AD) is a common neurodegenerative condition that involves the extracellular accumulation of amyloid plaques predominantly consisting of Aβ peptide aggregates. The amyloid plaques and soluble oligomeric species of Aβ are believed to be the major cause of synaptic dysfunction in AD brain and their cytotoxic mechanisms have been proposed to involve interactions with cell membranes. In this review, we discuss our solid-state nuclear magnetic resonance (ssNMR) studies of Aβ interactions with model membranes. Portland Press Ltd. 2021-06-30 2021-06-22 /pmc/articles/PMC8286822/ /pubmed/34156433 http://dx.doi.org/10.1042/BST20201244 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . Open access for this article was enabled by the participation of University of Melbourne in an all-inclusive Read & Publish pilot with Portland Press and the Biochemical Society under a transformative agreement with CAUL.
spellingShingle Review Articles
Rajput, Sunnia
Sani, Marc-Antoine
Keizer, David W.
Separovic, Frances
Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title_full Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title_fullStr Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title_full_unstemmed Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title_short Utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
title_sort utilizing magnetic resonance techniques to study membrane interactions of amyloid peptides
topic Review Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8286822/
https://www.ncbi.nlm.nih.gov/pubmed/34156433
http://dx.doi.org/10.1042/BST20201244
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