Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques.
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Low levels of copper disrupt brain amyloid-β homeostasis by altering its production and clearanceMetals and amyloid-beta in Alzheimer's diseaseMulti-Target Directed Donepezil-Like Ligands for Alzheimer's DiseaseTransient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseRole of environmental contaminants in the etiology of Alzheimer's disease: a reviewNumerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesBinding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide.The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Metals and cholesterol: two sides of the same coin in Alzheimer's disease pathology.The native copper- and zinc-binding protein metallothionein blocks copper-mediated Abeta aggregation and toxicity in rat cortical neurons.ESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-βPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.The amyloid-beta peptide of Alzheimer's disease binds Cu(I) in a linear bis-his coordination environment: insight into a possible neuroprotective mechanism for the amyloid-beta peptideElectrochemical and homogeneous electron transfers to the Alzheimer amyloid-beta copper complex follow a preorganization mechanism.Modulation of amyloid-β aggregation by histidine-coordinating Cobalt(III) Schiff base complexes.Correlation of copper interaction, copper-driven aggregation, and copper-driven h(2)o(2) formation with aβ40 conformationDistinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationEffects of oxidation on copper-binding properties of Aβ1-16 peptide: a pulse radiolysis study.On the role of electrostatics in protein-protein interactions.Substantial 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.Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity.Cu(II)-Zn(II) Cross-Modulation in Amyloid-Beta Peptide Binding: An X-ray Absorption Spectroscopy Study.Promotion of oxidative lipid membrane damage by amyloid beta proteinsThe elevated copper binding strength of amyloid-β aggregates allows the sequestration of copper from albumin: a pathway to accumulation of copper in senile plaquesNanoprobing of the effect of Cu(2+) cations on misfolding, interaction and aggregation of amyloid β peptide.The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease.The structure of the amyloid-beta peptide high-affinity copper II binding site in Alzheimer disease.Local structure and global patterning of Cu2+ binding in fibrillar amyloid-β [Aβ(1-40)] proteinInhibition of human high-affinity copper importer Ctr1 orthologous in the nervous system of Drosophila ameliorates Aβ42-induced Alzheimer's disease-like symptomsZn(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.Amyloid plaques in PSAPP mice bind less metal than plaques in human Alzheimer's disease.Ternary complexes of iron, amyloid-beta, and nitrilotriacetic acid: binding affinities, redox properties, and relevance to iron-induced oxidative stress in Alzheimer's disease.Copper(II)-bis-histidine coordination structure in a fibrillar amyloid β-peptide fragment and model complexes revealed by electron spin echo envelope modulation spectroscopyBioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.A central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease.Mapping brain metals to evaluate therapies for neurodegenerative disease.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.Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity.
P2860
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P2860
Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@en
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@nl
type
label
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@en
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@nl
prefLabel
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@en
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@nl
P2093
P2860
P356
P1476
Copper binding to the amyloid- ...... tary spectroscopic techniques.
@en
P2093
Christopher D Syme
John H Viles
Rebecca C Nadal
Stephen E J Rigby
P2860
P304
18169-18177
P356
10.1074/JBC.M313572200
P407
P577
2004-02-20T00:00:00Z