Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge.
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Multi-Target Directed Donepezil-Like Ligands for Alzheimer's DiseaseStructural studies of the tethered N-terminus of the Alzheimer's disease amyloid-β peptideNumerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesStructural insights into the interaction of platinum-based inhibitors with the Alzheimer's disease amyloid-β peptide.Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.HH domain of Alzheimer's disease Abeta provides structural basis for neuronal binding in PC12 and mouse cortical/hippocampal neuronsMetals and cholesterol: two sides of the same coin in Alzheimer's disease pathology.The Case for Abandoning Therapeutic Chelation of Copper Ions in Alzheimer's DiseaseA prochelator activated by hydrogen peroxide prevents metal-induced amyloid Beta aggregation.Modulation of amyloid-β aggregation by histidine-coordinating Cobalt(III) Schiff base complexes.Oligomers, fact or artefact? SDS-PAGE induces dimerization of β-amyloid in human brain samples.Distinct effects of Zn2+, Cu2+, Fe3+, and Al3+ on amyloid-beta stability, oligomerization, and aggregation: amyloid-beta destabilization promotes annular protofibril formationMolecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy.Clioquinol promotes the degradation of metal-dependent amyloid-β (Aβ) oligomers to restore endocytosis and ameliorate Aβ toxicity.The 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.Platinum-based inhibitors of amyloid-beta as therapeutic agents for Alzheimer's diseaseAmyloid-β Peptide Aβ3pE-42 Induces Lipid Peroxidation, Membrane Permeabilization, and Calcium Influx in Neurons.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.Revisiting rodent models: Octodon degus as Alzheimer's disease model?Therapeutics for Alzheimer's disease based on the metal hypothesisParadoxical condensation of copper with elevated beta-amyloid in lipid rafts under cellular copper deficiency conditions: implications for Alzheimer diseaseMetallo-complex activation of neuroprotective signalling pathways as a therapeutic treatment for Alzheimer's disease.Membrane-targeted strategies for modulating APP and Abeta-mediated toxicity.Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-beta peptide.A central role for dityrosine crosslinking of Amyloid-β in Alzheimer's disease.Design and synthesis of curcumin analogues for in vivo fluorescence imaging and inhibiting copper-induced cross-linking of amyloid beta species in Alzheimer's diseaseLens Endogenous Peptide αA66-80 Generates Hydrogen Peroxide and Induces Cell Apoptosis.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.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.Aggregation of amyloids in a cellular context: modelling and experiment.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Beta-amyloid oligomers: recent developments.Effects of oxidation on redox and cytotoxic properties of copper complex of Aβ1-16 peptide.Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.Copper inducing Aβ42 rather than Aβ40 nanoscale oligomer formation is the key process for Aβ neurotoxicity.
P2860
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P2860
Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@en
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@nl
type
label
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@en
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@nl
prefLabel
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@en
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@nl
P2093
P2860
P50
P356
P1476
Copper-mediated amyloid-beta t ...... termolecular histidine bridge.
@en
P2093
Danielle G Smith
Deborah J Tew
Giuseppe D Ciccotosto
John F Boas
John R Pilbrow
Kevin J Barnham
Keyla Perez
Tong-Lay Lau
P2860
P304
15145-15154
P356
10.1074/JBC.M600417200
P407
P50
P577
2006-04-04T00:00:00Z