Amyloid-β peptide structure in aqueous solution varies with fragment size.
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Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein proteinDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyConformational transitions induced by in vitro macromolecular crowding lead to the amyloidogenesis of buffalo heart cystatin.Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Cross dimerization of amyloid-β and αsynuclein proteins in aqueous environment: a molecular dynamics simulations study.Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.Structures and free energy landscapes of the wild-type and A30P mutant-type α-synuclein proteins with dynamics.Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics.Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.Arginine and disordered amyloid-β peptide structures: molecular level insights into the toxicity in Alzheimer's diseaseDivalent copper ion bound amyloid-β(40) and amyloid-β(42) alloforms are less preferred than divalent zinc ion bound amyloid-β(40) and amyloid-β(42) alloforms.Amyloidogenic amyloid-β-peptide variants induce microbial agglutination and exert antimicrobial activity.Molecular Dynamics Simulations of Amyloid β-Peptide (1-42): Tetramer Formation and Membrane InteractionsCharacterization of the internal dynamics and conformational space of zinc-bound amyloid β peptides by replica-exchange molecular dynamics simulations.Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Self-assembly of the full-length amyloid Aβ42 protein in dimers.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.Amyloid-β fibril disruption by C60-molecular guidance for rational drug design.Dual effects of familial Alzheimer's disease mutations (D7H, D7N, and H6R) on amyloid β peptide: correlation dynamics and zinc binding.
P2860
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P2860
Amyloid-β peptide structure in aqueous solution varies with fragment size.
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին 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
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@ast
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@en
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@nl
type
label
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@ast
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@en
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@nl
prefLabel
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@ast
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@en
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@nl
P2093
P2860
P356
P1476
Amyloid-β peptide structure in aqueous solution varies with fragment size.
@en
P2093
Olivia Wise-Scira
Orkid Coskuner
Taizo Kitahara
P2860
P304
P356
10.1063/1.3662490
P407
P50
P577
2011-11-01T00:00:00Z