Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.
about
My 65 years in protein chemistryStructure and dynamics of amyloid-β segmental polymorphismsβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Coarse-grained force field: general folding theory.Molecular dynamics of protein A and a WW domain with a united-residue model including hydrodynamic interactionPhysical mechanism for biopolymers to aggregate and maintain in non-equilibrium states.A unified coarse-grained model of biological macromolecules based on mean-field multipole-multipole interactions.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsAmyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.The power of coarse graining in biomolecular simulations.Molecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.A study of the α-helical intermediate preceding the aggregation of the amino-terminal fragment of the β amyloid peptide (Aβ(1-28))Phenolic compounds prevent amyloid β-protein oligomerization and synaptic dysfunction by site-specific binding.Coexistence of phases in a protein heterodimerOptimization of a Nucleic Acids united-RESidue 2-Point model (NARES-2P) with a maximum-likelihood approachDissecting two-dimensional ultraviolet spectra of amyloid fibrils into beta-strand and turn contributionsTracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopyExtension of UNRES force field to treat polypeptide chains with D-amino-acid residues.Aggregation of amyloids in a cellular context: modelling and experiment.Molecular mechanism of misfolding and aggregation of Aβ(13-23).Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Unlocking the atomic-level details of amyloid fibril growth through advanced biomolecular simulations.The universality of β-hairpin misfolding indicated by molecular dynamics simulations.Amyloid-β dimers in the absence of plaque pathology impair learning and synaptic plasticity.Thermodynamics of amyloid formation and the role of intersheet interactions.New method for determining size of critical nucleus of fibril formation of polypeptide chains.The attachment of α-synuclein to a fiber: A coarse-grain approach.Elucidating Important Sites and the Mechanism for Amyloid Fibril Formation by Coarse-Grained Molecular Dynamics.Preformed template fluctuations promote fibril formation: insights from lattice and all-atom models.Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarityToward Structure Prediction for Short Peptides Using the Improved SAAP Force Field Parameters
P2860
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P2860
Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Mechanism of fiber assembly: t ...... ed united-residue force field.
@ast
Mechanism of fiber assembly: t ...... ed united-residue force field.
@en
Mechanism of fiber assembly: t ...... ed united-residue force field.
@nl
type
label
Mechanism of fiber assembly: t ...... ed united-residue force field.
@ast
Mechanism of fiber assembly: t ...... ed united-residue force field.
@en
Mechanism of fiber assembly: t ...... ed united-residue force field.
@nl
prefLabel
Mechanism of fiber assembly: t ...... ed united-residue force field.
@ast
Mechanism of fiber assembly: t ...... ed united-residue force field.
@en
Mechanism of fiber assembly: t ...... ed united-residue force field.
@nl
P2860
P1476
Mechanism of fiber assembly: t ...... ed united-residue force field.
@en
P2093
Dana Browne
P2860
P304
P356
10.1016/J.JMB.2010.09.057
P407
P577
2010-10-01T00:00:00Z