Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.
about
Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyModulating self-assembly of amyloidogenic proteins as a therapeutic approach for neurodegenerative diseases: strategies and mechanismsFlexibility and binding affinity in protein-ligand, protein-protein and multi-component protein interactions: limitations of current computational approaches.Modulation of Amyloid β-Protein (Aβ) Assembly by Homologous C-Terminal Fragments as a Strategy for Inhibiting Aβ Toxicity.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Minimal model of self-assembly: emergence of diversity and complexity.Aβ(39-42) modulates Aβ oligomerization but not fibril formationFolding of pig gastric mucin non-glycosylated domains: a discrete molecular dynamics study.Stabilizing Off-pathway Oligomers by Polyphenol Nanoassemblies for IAPP Aggregation InhibitionDiscrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.Computational approaches to understanding protein aggregation in neurodegeneration.Membrane and surface interactions of Alzheimer's Aβ peptide--insights into the mechanism of cytotoxicity.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseBiophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Plant-based vaccines for Alzheimer's disease: an overview.High-Resolution Structures of the Amyloid-β 1-42 Dimers from the Comparison of Four Atomistic Force Fields.C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Capping of aβ42 oligomers by small molecule inhibitors.Melatonin ameliorates Aβ1-42 -induced Alzheimer's cognitive deficits in mouse model.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates.
P2860
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P2860
Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
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
name
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@ast
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@en
type
label
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@ast
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@en
prefLabel
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@ast
Structural basis for Aβ1–42 to ...... rete molecular dynamics study.
@en
P2093
P2860
P1476
Structural basis for Aβ1–42 to ...... crete molecular dynamics study
@en
P2093
P2860
P304
P356
10.1016/J.JMB.2011.05.021
P407
P577
2011-05-23T00:00:00Z