Probing the mechanisms of fibril formation using lattice models
about
A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.Influence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationβ-sheet propensity controls the kinetic pathways and morphologies of seeded peptide aggregation.Effect of beta-sheet propensity on peptide aggregation.Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer's peptides.Nanomaterials design and tests for neural tissue engineering.Principles governing oligomer formation in amyloidogenic peptides.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsThermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.Impact of sequence on the molecular assembly of short amyloid peptides.Connecting macroscopic observables and microscopic assembly events in amyloid formation using coarse grained simulationsConformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational studyRelative stability of de novo four-helix bundle proteins: insights from coarse grained molecular simulations.Role of water in protein aggregation and amyloid polymorphism.Spontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Influence of temperature on formation of perfect tau fragment fibrils using PRIME20/DMD simulationsDynamics of locking of peptides onto growing amyloid fibrils.Multiscale modeling of macromolecular biosystems.Statistical mechanical treatments of protein amyloid formation.A simple lattice model that captures protein folding, aggregation and amyloid formation.Accounting for protein-solvent contacts facilitates design of nonaggregating lattice proteins.Frozen in beta.A Simple Model of Protein Domain Swapping in Crowded Cellular Environments.Diversity of kinetic pathways in amyloid fibril formation.Thermodynamics of amyloid formation and the role of intersheet interactions.New method for determining size of critical nucleus of fibril formation of polypeptide chains.Dual effect of crowders on fibrillation kinetics of polypeptide chains revealed by lattice models.Relationship between population of the fibril-prone conformation in the monomeric state and oligomer formation times of peptides: insights from all-atom simulations.Preformed template fluctuations promote fibril formation: insights from lattice and all-atom models.Factors Governing Fibrillogenesis of Polypeptide Chains Revealed by Lattice Models
P2860
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P2860
Probing the mechanisms of fibril formation using lattice models
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Probing the mechanisms of fibril formation using lattice models
@en
Probing the mechanisms of fibril formation using lattice models.
@nl
type
label
Probing the mechanisms of fibril formation using lattice models
@en
Probing the mechanisms of fibril formation using lattice models.
@nl
prefLabel
Probing the mechanisms of fibril formation using lattice models
@en
Probing the mechanisms of fibril formation using lattice models.
@nl
P2093
P2860
P356
P1476
Probing the mechanisms of fibril formation using lattice models
@en
P2093
D K Klimov
D Thirumalai
J E Straub
P2860
P304
P356
10.1063/1.2989981
P407
P50
P577
2008-11-01T00:00:00Z