Structures of the Alzheimer’s Wild-Type Aβ1-40 Dimer from Atomistic Simulations
Author:
Affiliation:
1. Laboratoire de Biochimie Théorique, UPR 9080 CNRS, IBPC, Université Paris Diderot, Sorbonne Paris Cité, 13 Rue Pierre et Marie Curie, 75005 Paris, France
Funder
Pierre Gilles de Gennes Fondation pour la Recherche
European Research Council
Agence Nationale de la Recherche
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5b05593
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1. Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
2. Inhibition of protein aggregation and amyloid formation by small molecules
3. Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration
4. Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
5. Soluble amyloid -protein dimers isolated from Alzheimer cortex directly induce Tau hyperphosphorylation and neuritic degeneration
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