Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
about
Structural studies of the tethered N-terminus of the Alzheimer's disease amyloid-β peptideAlzheimer's Aβ peptides with disease-associated N-terminal modifications: influence of isomerisation, truncation and mutation on Cu2+ coordination.Mammalian Metallothionein-3: New Functional and Structural InsightsAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.ESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-βReevaluation of copper(I) affinity for amyloid-β peptides by competition with ferrozine--an unusual copper(I) indicator.Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-beta copper complex follow a preorganization mechanism.Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer's disease.Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.Cu K-edge X-ray absorption spectroscopy reveals differential copper coordination within amyloid-β oligomers compared to amyloid-β monomers.Alzheimer's disease & metals: therapeutic opportunities.Spin hamiltonian parameters for Cu(II)-prion peptide complexes from L-band electron paramagnetic resonance spectroscopySubstantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance.Misfolded proteins in Alzheimer's disease and type II diabetes.The N Terminus of α-Synuclein Forms Cu(II)-Bridged Oligomers.Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.The elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: a pathway to accumulation of copper in senile plaquesLocal structure and global patterning of Cu2+ binding in fibrillar amyloid-β [Aβ(1-40)] proteinZn(II) ions substantially perturb Cu(II) ion coordination in amyloid-β at physiological pH.The tachykinin peptide neurokinin B binds copper forming an unusual [CuII(NKB)2] complex and inhibits copper uptake into 1321N1 astrocytoma cells.Copper(II)-bis-histidine coordination structure in a fibrillar amyloid β-peptide fragment and model complexes revealed by electron spin echo envelope modulation spectroscopyMoving difference (MDIFF) non-adiabatic rapid sweep (NARS) EPR of copper(II).Capturing a reactive state of amyloid aggregates: NMR-based characterization of copper-bound Alzheimer disease amyloid β-fibrils in a redox cycle.Novel drug targets based on metallobiology of Alzheimer's disease.Insights into the thermodynamics of copper association with amyloid-β, α-synuclein and prion proteins.Oxidative stress and cell membranes in the pathogenesis of Alzheimer's disease.Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity.Therapeutic potential of copper chelation with triethylenetetramine in managing diabetes mellitus and Alzheimer's disease.Microwave heating in solid-phase peptide synthesis.The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Werner coordination chemistry and neurodegeneration.The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.Biological metals and metal-targeting compounds in major neurodegenerative diseases.Copper induced spin state change of heme-Aβ associated with Alzheimer's disease.EPR Methods for Biological Cu(II): L-Band CW and NARS.On the involvement of copper binding to the N-terminus of the amyloid Beta Peptide of Alzheimer's disease: a computational study on model systems.In vitro studies of 3-hydroxy-4-pyridinones and their glycosylated derivatives as potential agents for Alzheimer's disease.Reaction rates and mechanism of the ascorbic acid oxidation by molecular oxygen facilitated by Cu(II)-containing amyloid-beta complexes and aggregates.Small angle X-ray scattering analysis of Cu(2+)-induced oligomers of the Alzheimer's amyloid β peptide.
P2860
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P2860
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@ast
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@en
type
label
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@ast
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@en
prefLabel
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@ast
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@en
P2093
P356
P1476
Pleomorphic copper coordination by Alzheimer's disease amyloid-beta peptide.
@en
P2093
Christopher J Noble
Graeme R Hanson
Kevin J Barnham
Simon C Drew
P304
P356
10.1021/JA808073B
P407
P577
2009-01-01T00:00:00Z