Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides.
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Amyloid-beta (Aβ) D7H mutation increases oligomeric Aβ42 and alters properties of Aβ-zinc/copper assembliesNumerical Simulations Reveal Randomness of Cu(II) Induced Aβ Peptide Dimerization under Conditions Present in Glutamatergic SynapsesEffect of metals on kinetic pathways of amyloid-β aggregationA necessary condition for coexistence of autocatalytic replicators in a prebiotic environmentCu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.Effect of Copper and Zinc on the Single Molecule Self-Affinity of Alzheimer's Amyloid-β Peptides.Amyloid-β and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.Unique effect of Cu(II) in the metal-induced amyloid formation of β-2-microglobulinThe role of metal ions in amyloid formation: general principles from model peptides.Biophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.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.The effect of Cu(2+) and Zn(2+) on the Aβ42 peptide aggregation and cellular toxicityRecent Progress in Alzheimer's Disease Research, Part 1: Pathology.Cellular polyamines promote amyloid-beta (Aβ) peptide fibrillation and modulate the aggregation pathways.Small angle X-ray scattering analysis of Cu(2+)-induced oligomers of the Alzheimer's amyloid β peptide.Kinetics of the Interactions between Copper and Amyloid-β with FAD Mutations and Phosphorylation at the N terminus.Kinetic Analysis Reveals the Identity of Aβ-Metal Complex Responsible for the Initial Aggregation of Aβ in the Synapse.Aggregation pathways of the amyloid β(1-42) peptide depend on its colloidal stability and ordered β-sheet stackingCu(II) promotes amyloid pore formation.Copper(II) directs formation of toxic amorphous aggregates resulting in inhibition of hen egg white lysozyme fibrillation under alkaline salt-mediated conditions.Aggregation-Prone Amyloid-β⋅Cu(II) Species Formed on the Millisecond Timescale under Mildly Acidic Conditions.The Pathogenic A2V Mutant Exhibits Distinct Aggregation Kinetics, Metal Site Structure, and Metal Exchange of the Cu2+ -Aβ Complex.Inhibition of Cu-amyloid-β by using bifunctional peptides with β-sheet breaker and chelator moieties.Cu²⁺ accentuates distinct misfolding of Aβ₁₋₄₀ and Aβ₁₋₄₂ peptides, and potentiates membrane disruption.Copper in Alzheimer’s disease: Implications in amyloid aggregation and neurotoxicity
P2860
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P2860
Cu(II) mediates kinetically distinct, non-amyloidogenic aggregation of amyloid-beta peptides.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Cu(II) mediates kinetically di ...... tion of amyloid-beta peptides.
@en
type
label
Cu(II) mediates kinetically di ...... tion of amyloid-beta peptides.
@en
prefLabel
Cu(II) mediates kinetically di ...... tion of amyloid-beta peptides.
@en
P2093
P2860
P356
P1476
Cu(II) mediates kinetically di ...... tion of amyloid-beta peptides.
@en
P2093
Jeppe T Pedersen
Niels H H Heegaard
Noemi Rozlosnik
P2860
P304
26952-26963
P356
10.1074/JBC.M111.220863
P407
P577
2011-06-03T00:00:00Z