Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
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Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationStructural and fluctuational difference between two ends of Aβ amyloid fibril: MD simulations predict only one end has open conformations.Globular state in the oligomers formed by Abeta peptides.A molecular dynamics study of the early stages of amyloid-beta(1-42) oligomerization: the role of lipid membranes.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsMechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Replica exchange molecular dynamics of the thermodynamics of fibril growth of Alzheimer's Aβ42 peptide.A study of the α-helical intermediate preceding the aggregation of the amino-terminal fragment of the β amyloid peptide (Aβ(1-28))Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopyPolymorph-specific kinetics and thermodynamics of β-amyloid fibril growth.Design principles for high-pressure force fields: Aqueous TMAO solutions from ambient to kilobar pressures.Structural Properties of Human IAPP Dimer in Membrane Environment Studied by All-Atom Molecular Dynamics Simulations.Elucidating the locking mechanism of peptides onto growing amyloid fibrils through transition path sampling.Unlocking the atomic-level details of amyloid fibril growth through advanced biomolecular simulations.In silico investigation and targeting of amyloid β oligomers of different size.Characterization of the polymorphic states of copper(II)-bound Aβ(1-16) peptides by computational simulations.Thermodynamics of Amyloid-β Fibril Elongation: Atomistic Details of the Transition State.Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.The attachment of α-synuclein to a fiber: A coarse-grain approach.Stability and growth mechanism of self-assembling putative antifreeze cyclic peptides.Phosphorylation at Ser8 as an Intrinsic Regulatory Switch to Regulate the Morphologies and Structures of Alzheimer's 40-residue β-Amyloid (Aβ40) Fibrils.Elucidating Important Sites and the Mechanism for Amyloid Fibril Formation by Coarse-Grained Molecular Dynamics.Seeding and Cross-seeding Fibrillation of N-terminal Prion Protein Peptides PrP(120-144).Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarityRecent Advances by In Silico and In Vitro Studies of Amyloid-β 1-42 Fibril Depicted a S-Shape Conformation
P2860
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P2860
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@ast
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@en
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@nl
type
label
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@ast
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@en
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@nl
prefLabel
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@ast
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@en
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.
@nl
P2093
P2860
P356
P1476
Thermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils
@en
P2093
Bernard R Brooks
D Thirumalai
Edward P O'Brien
John E Straub
P2860
P304
14421-14430
P356
10.1021/JP9050098
P407
P50
P577
2009-10-01T00:00:00Z