Molecular mechanisms of direct and indirect interplay between amyloid β42 oligomer and characteristic lipids-Reference-Cited by-同舟云学术

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Molecular mechanisms of direct and indirect interplay between amyloid β42 oligomer and characteristic lipids

Published:2022-10 Issue:4 Volume:1 Page:310-320
ISSN:2772-5715
Container-title:ChemPhysMater
language:en
Short-container-title:ChemPhysMater

Author:

Mei Jinfei,Liu Chengqiang,Yang Huijuan,Ma Xiaohong,Ai Hongqi^ORCID

Publisher

Elsevier BV

Reference65 articles.

1. Compact fibril-like structure of amyloid β-peptide (1–42) monomers;Barz;Chem. Commun.,2021

2. Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Aβ oligomers;Kayed;Mol. Neurodegener.,2010

3. Molecular dynamics simulations of amyloid β-peptide (1-42): Tetramer formation and membrane interactions;Brown;Biophys. J.,2016

4. Highlighting the effect of amyloid beta assemblies on the mechanical properties and conformational stability of cell membrane;Grasso;J. Mol. Graph. Model.,2020

5. Coarse-grained MD simulations reveal beta-amyloid fibrils of various sizes bind to interfacial liquid-ordered and liquid-disordered regions in phase separated lipid rafts with diverse membrane-bound conformational states;Cheng;Biophys. Chem.,2020

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