Diversity of kinetic pathways in amyloid fibril formation.
about
Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wiresMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effects of surface interactions on peptide aggregate morphology.Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Factor V activator from Daboia russelli russelli venom destabilizes β-amyloid aggregate, the hallmark of Alzheimer disease.Effect of metals on kinetic pathways of amyloid-β aggregationPrinciples governing oligomer formation in amyloidogenic peptides.Polymorphic structures of Alzheimer's β-amyloid globulomers.Kinetics of amyloid beta monomer-to-oligomer exchange by NMR relaxation.Impact of sequence on the molecular assembly of short amyloid peptides.MetAmyl: a METa-predictor for AMYLoid proteinsMolecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.Spontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Structural transitions and oligomerization along polyalanine fibril formation pathways from computer simulationsComputer simulation study of amyloid fibril formation by palindromic sequences in prion peptidesInfluence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulationsBiomolecular dynamics: order-disorder transitions and energy landscapesInhibition of aggregate formation as therapeutic target in protein misfolding diseases: effect of tetracycline and trehalose.Multiscale modeling of macromolecular biosystems.Force spectroscopy reveals the presence of structurally modified dimers in transthyretin amyloid annular oligomers.Structure-activity relationships in peptide modulators of β-amyloid protein aggregation: variation in α,α-disubstitution results in altered aggregate size and morphologyUsing a reduced dimensionality model to compute the thermodynamic properties of finite polypeptide aggregates.Kinetics of spontaneous filament nucleation via oligomers: Insights from theory and simulation.Effects of mutations in de novo designed synthetic amphiphilic β-sheet peptides on self-assembly of fibrils.Thermodynamic analysis of structural transitions during GNNQQNY aggregation.Lamination and spherulite-like compaction of a hormone's native amyloid-like nanofibrils: spectroscopic insights into key interactions.Hydrodynamic effects on β-amyloid (16-22) peptide aggregation.The attachment of α-synuclein to a fiber: A coarse-grain approach.Multiscale simulations for understanding the evolution and mechanism of hierarchical peptide self-assembly.The Relation between α-Helical Conformation and Amyloidogenicity.β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates.
P2860
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P2860
Diversity of kinetic pathways in amyloid fibril formation.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh-hant
name
Diversity of kinetic pathways in amyloid fibril formation.
@en
Diversity of kinetic pathways in amyloid fibril formation.
@nl
type
label
Diversity of kinetic pathways in amyloid fibril formation.
@en
Diversity of kinetic pathways in amyloid fibril formation.
@nl
prefLabel
Diversity of kinetic pathways in amyloid fibril formation.
@en
Diversity of kinetic pathways in amyloid fibril formation.
@nl
P2860
P356
P1476
Diversity of kinetic pathways in amyloid fibril formation.
@en
P2093
Giovanni Bellesia
Joan-Emma Shea
P2860
P304
P356
10.1063/1.3216103
P407
P577
2009-09-01T00:00:00Z