Hydrodynamic effects on β-amyloid (16-22) peptide aggregation-Reference-Cited by-同舟云学术

Hydrodynamic effects on β-amyloid (16-22) peptide aggregation

Published:2016-07-21 Issue:3 Volume:145 Page:035102
ISSN:0021-9606
Container-title:The Journal of Chemical Physics
language:en
Short-container-title:The Journal of Chemical Physics

Author:

Chiricotto Mara¹^ORCID,Melchionna Simone²,Derreumaux Philippe¹³,Sterpone Fabio¹

Affiliation:

1. Laboratoire de Biochimie Théorique, IBPC, CNRS UPR9080, University Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005 Paris, France

2. CNR-ISC, Institute for Complex System, Consiglio Nazionale delle Ricerche, Rome, Italy

3. IUF, Institut Universitaire de France, Boulevard Saint Michel, 75005 Paris, France

Funder

European Research Council (ERC)

Agence Nationale de la Recherche (ANR)

Publisher

AIP Publishing

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://aip.scitation.org/doi/pdf/10.1063/1.4958323

Reference93 articles.

1. The physical basis of protein misfolding disorders

2. Inhibition of protein aggregation and amyloid formation by small molecules

3. Peptide dimer structure in an Aβ(1–42) fibril visualized with cryo-EM

4. Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils

5. Polymorphic Fibril Formation by Residues 10–40 of the Alzheimer’s β-Amyloid Peptide

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