Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
about
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.Preventing peptide and protein misbehavior.Specific Binding of Cu(II) Ions to Amyloid-Beta Peptides Bound to Aggregation-Inhibiting Molecules or SDS Micelles Creates Complexes that Generate Radical Oxygen Species.Monomeric Aβ(1-40) and Aβ(1-42) Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil.Amyloid plaques beyond Aβ: a survey of the diverse modulators of amyloid aggregation.Molecular mechanisms of protein aggregation from global fitting of kinetic models.Zinc(II) Binding Site to the Amyloid-β Peptide: Insights from Spectroscopic Studies with a Wide Series of Modified Peptides.Monomer-dependent secondary nucleation in amyloid formation.Kinetic Analysis Reveals the Identity of Aβ-Metal Complex Responsible for the Initial Aggregation of Aβ in the Synapse.Modulation of electrostatic interactions to reveal a reaction network unifying the aggregation behaviour of the Aβ42 peptide and its variantsAlzheimer's disease and cigarette smoke components: effects of nicotine, PAHs, and Cd(II), Cr(III), Pb(II), Pb(IV) ions on amyloid-β peptide aggregation.Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Neurotoxicity of Zinc.Dissecting the behaviour of β-amyloid peptide variants during oligomerization and fibrillation.The Amyloid-β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal IonsNanomechanical Characterization of Amyloid Fibrils Using Single-Molecule Experiments and Computational Simulations
P2860
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P2860
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@ast
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@en
type
label
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@ast
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@en
prefLabel
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@ast
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@en
P2860
P50
P356
P1476
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation.
@en
P2860
P304
P356
10.1073/PNAS.1421961112
P407
P577
2015-03-30T00:00:00Z