The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
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Numerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesThe Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's DiseaseAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Misfolded proteins in Alzheimer's disease and type II diabetes.The antioxidant mechanisms underlying the aged garlic extract- and S-allylcysteine-induced protection.Local structure and global patterning of Cu2+ binding in fibrillar amyloid-β [Aβ(1-40)] proteinCopper(II)-bis-histidine coordination structure in a fibrillar amyloid β-peptide fragment and model complexes revealed by electron spin echo envelope modulation spectroscopyBiophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Metal complexes designed to bind to amyloid-β for the diagnosis and treatment of Alzheimer's disease.Biological metals and metal-targeting compounds in major neurodegenerative diseases.Small angle X-ray scattering analysis of Cu(2+)-induced oligomers of the Alzheimer's amyloid β peptide.An N-heterocyclic amine chelate capable of antioxidant capacity and amyloid disaggregation.Effects of Zn2+ binding on the structural and dynamic properties of amyloid β peptide associated with Alzheimer's disease: Asp1 or Glu11?Identification of key structural features of the elusive Cu-Aβ complex that generates ROS in Alzheimer's disease.Development and Application of a Nonbonded Cu(2+) Model That Includes the Jahn-Teller EffectElucidating the 3D structures of Al(iii)-Aβ complexes: a template free strategy based on the pre-organization hypothesis.Rapid and Label-Free Strategy to Isolate Aptamers for Metal Ions.In silico and in vitro studies to elucidate the role of Cu2+ and galanthamine as the limiting step in the amyloid beta (1-42) fibrillation process.Characterization of the internal dynamics and conformational space of zinc-bound amyloid β peptides by replica-exchange molecular dynamics simulations.Copper-β-amyloid peptides exhibit neither monooxygenase nor superoxide dismutase activities.Mutual interference of Cu and Zn ions in Alzheimer's disease: perspectives at the molecular level.Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Oxidative stress and the amyloid beta peptide in Alzheimer's disease.Resistance of Cu(Aβ4-16) to Copper Capture by Metallothionein-3 Supports a Function for the Aβ4-42 Peptide as a Synaptic Cu(II) Scavenger.Computer-assisted designed "selenoxy-chinolin": a new catalytic mechanism of the GPx-like cycle and inhibition of metal-free and metal-associated Aβ aggregation.Dioxygen activation in the Cu-amyloid β complex.Link between Affinity and Cu(II) Binding Sites to Amyloid-β Peptides Evaluated by a New Water-Soluble UV-Visible Ratiometric Dye with a Moderate Cu(II) Affinity.The Pathogenic A2V Mutant Exhibits Distinct Aggregation Kinetics, Metal Site Structure, and Metal Exchange of the Cu2+ -Aβ Complex.The catalytically active copper-amyloid-Beta state: coordination site responsible for reactive oxygen species production.A Functional Role for Aβ in Metal Homeostasis? N-Truncation and High-Affinity Copper Binding.PtCl2(phen) disrupts the metal ions binding to amyloid-β peptide.Molecular Simulations of Human and Mouse Aβ1-16 at Different pH Values: Structural Characteristics toward Understanding Cu(2+) -Coordinated Amyloid Beta Spheres.34 GHz pulsed ENDOR characterization of the copper coordination of an amyloid β peptide relevant to Alzheimer's disease.Multi-frequency, multi-technique pulsed EPR investigation of the copper binding site of murine amyloid β peptide.Dual-function triazole-pyridine derivatives as inhibitors of metal-induced amyloid-β aggregationCopper–amyloid-β complex may catalyze peroxynitrite production in brain: evidence from molecular modelingA novel hybrid of 6-chlorotacrine and metal–amyloid-β modulator for inhibition of acetylcholinesterase and metal-induced amyloid-β aggregationModeling Cu2+-Aβ complexes from computational approachesCopper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity
P2860
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P2860
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@en
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@nl
type
label
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@en
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@nl
prefLabel
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@en
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide.
@nl
P356
P1476
The heterogeneous nature of Cu2+ interactions with Alzheimer's amyloid-β peptide
@en
P2093
Kevin J Barnham
P304
P356
10.1021/AR200014U
P407
P50
P577
2011-06-29T00:00:00Z