Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1â16 Amyloid-Î² Peptide: A Key Role of the First Two N-Terminus Residues-Reference-Cited by-同舟云学术

Pulse EPR Spectroscopy Reveals the Coordination Sphere of Copper(II) Ions in the 1â16 Amyloid-Î² Peptide: A Key Role of the First Two N-Terminus Residues

Published:2009-11-23 Issue:49 Volume:48 Page:9273-9276
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angew. Chem. Int. Ed.

Author:

Dorlet Pierre,Gambarelli Serge,Faller Peter,Hureau Christelle

Publisher

Wiley

Subject

General Chemistry,Catalysis

Reference22 articles.

1. The metallobiology of Alzheimer's disease

2. Aβ-mediated ROS production by Cu ions: Structural insights, mechanisms and relevance to Alzheimer's disease

3. Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

4. N-Terminal Deletions Modify the Cu2+ Binding Site in Amyloid-β

5. Role of Aspartate-1 in Cu(II) Binding to the Amyloid-β Peptide of Alzheimer's Disease

Cited by 173 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Cu(II) Specifically Disassembles Insulin Amyloid Nanostructures via Direct Interaction with Cross-β Fibrils;Nano Letters;2024-07-11

2. The green cupredoxin CopI is a multicopper protein able to oxidize Cu(I);Journal of Inorganic Biochemistry;2024-05

3. Evaluation of Copper(II) Transfer between Amyloid‐beta Peptides by Relaxation‐Induced Dipolar Modulation Enhancement (RIDME);ChemPhysChem;2024-02-14

4. Copper(II) Can Kinetically Trap Arctic and Italian Amyloid-β₄₀ as Toxic Oligomers, Mimicking Cu(II) Binding to Wild-Type Amyloid-β₄₂: Implications for Familial Alzheimer’s Disease;JACS Au;2024-02-06

5. Rationally Designed Cu(I) Ligand to Prevent CuAβ-Generated ROS Production in the Alzheimer’s Disease Context;Inorganic Chemistry;2024-01-20