Interaction of Aβ1–42 Amyloids with Lipids Promotes “Off-Pathway” Oligomerization and Membrane Damage-Reference-Cited by-同舟云学术

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Interaction of Aβ1–42 Amyloids with Lipids Promotes “Off-Pathway” Oligomerization and Membrane Damage

Published:2015-02-26 Issue:3 Volume:16 Page:944-950
ISSN:1525-7797
Container-title:Biomacromolecules
language:en
Short-container-title:Biomacromolecules

Author:

Henry Sarah¹,Vignaud Hélène²,Bobo Claude²,Decossas Marion¹,Lambert Oliver¹,Harte Etienne¹,Alves Isabel D.¹,Cullin Christophe²,Lecomte Sophie¹

Affiliation:

1. Chimie et Biologie des Membranes et Nanoobjets, CBMN CNRS UMR 5248, Université de Bordeaux, Allée Geoffroy de Saint Hilaire, 33600 Pessac, France

2. Institut de Biochimie et Génétique Cellulaire, IBGC CNRS UMR 5095, Université de Bordeaux, 1 rue Camille Saint Saëns, 33077 Bordeaux cedex, France

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Polymers and Plastics,Biomaterials,Bioengineering

Link

https://pubs.acs.org/doi/pdf/10.1021/bm501837w

Reference42 articles.

1. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

2. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis

3. Toxic fibrillar oligomers of amyloid- have cross- structure

4. ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

5. A Structure-Toxicity Study of Aß42 Reveals a New Anti-Parallel Aggregation Pathway

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