The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant.
about
Structure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrilsInduced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibitionEffect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates.Structural determination of Abeta25-35 micelles by molecular dynamics simulations.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Hydration effects on the HET-s prion and amyloid-beta fibrillous aggregates, studied with three-dimensional molecular theory of solvationPolymorphism of Alzheimer's Abeta17-42 (p3) oligomers: the importance of the turn location and its conformationTauroursodeoxycholic acid prevents E22Q Alzheimer's Abeta toxicity in human cerebral endothelial cells.Lipid-induced conformational transition of the amyloid core fragment Abeta(28-35) and its A30G and A30I mutants.Modulating protein amyloid aggregation with nanomaterials.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Hierarchy and the mechanism of fibril formation in ADan peptides.Conformational features of the Aβ42 peptide monomer and its interaction with the surrounding solvent.Dynamics of the conformational transitions during the dimerization of an intrinsically disordered peptide: a case study on the human islet amyloid polypeptide fragment.Structural and Material Properties of Amyloid Aβ40/42 Fibrils.Single molecule study of initial structural features on the amyloidosis process.Global fitting without a global model: regularization based on the continuity of the evolution of parameter distributions.
P2860
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P2860
The stability of monomeric intermediates controls amyloid formation: Abeta25-35 and its N27Q mutant.
description
2006 nî lūn-bûn
@nan
2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@ast
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@en
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@nl
type
label
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@ast
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@en
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@nl
prefLabel
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@ast
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@en
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@nl
P2860
P1433
P1476
The stability of monomeric int ...... beta25-35 and its N27Q mutant.
@en
P2860
P304
P356
10.1529/BIOPHYSJ.105.075309
P407
P577
2006-02-24T00:00:00Z