Copper Coordination to Native N-Terminally Modified versus Full-Length Amyloid-β: Second-Sphere Effects Determine the Species Present at Physiological pH-Reference-Cited by-同舟云学术

Copper Coordination to Native N-Terminally Modified versus Full-Length Amyloid-β: Second-Sphere Effects Determine the Species Present at Physiological pH

Published:2012-11-14 Issue:23 Volume:51 Page:12988-13000
ISSN:0020-1669
Container-title:Inorganic Chemistry
language:en
Short-container-title:Inorg. Chem.

Author:

Alies Bruno¹²,Bijani Christian¹²,Sayen Stéphanie³,Guillon Emmanuel³,Faller Peter¹²,Hureau Christelle¹²

Affiliation:

1. Laboratoire de Chimie de Coordination (LCC), CNRS, 205 route de Narbonne, F-31077 Toulouse, France

2. UPS, INPT, LCC, Université de Toulouse, F-31077 Toulouse, France

3. Groupe de Chimie de Coordination, Institut de Chimie Moléculaire de Reims (ICMR, CNRS UMR 7312), Université de Reims Champagne-Ardenne, BP 1039, 51687 Reims Cedex 2, France

Publisher

American Chemical Society (ACS)

Subject

Inorganic Chemistry,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ic302097d

Reference72 articles.

1. Amyloid-β Peptide: Dr. Jekyll or Mr. Hyde?

2. The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to Therapeutics

3. Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer’s disease

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

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