Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.
about
Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wiresThe centriolar protein CPAP G-box: an amyloid fibril in a single domainHigh-Resolution Structure of a Self-Assembly-Competent Form of a Hydrophobic Peptide Captured in a Soluble β-Sheet ScaffoldMinimalist design of water-soluble cross-beta architecture.A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35Atomic structures of peptide self-assembly mimicsNanomaterials design and tests for neural tissue engineering.Free cholesterol induces higher β-sheet content in Aβ peptide oligomers by aromatic interaction with Phe19.Modeling the Alzheimer Abeta17-42 fibril architecture: tight intermolecular sheet-sheet association and intramolecular hydrated cavitiesPolyglutamine variation in a flowering time protein correlates with island age in a Hawaiian plant radiationFormation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentThermodynamic selection of steric zipper patterns in the amyloid cross-beta spineAtomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRRole of intermolecular forces in defining material properties of protein nanofibrils.Conformational stability of fibrillar amyloid-beta oligomers via protofilament pair formation - a systematic computational studyRole of hydration force in the self-assembly of collagens and amyloid steric zipper filamentsInterplay of sequence, topology and termini charge in determining the stability of the aggregates of GNNQQNY mutants: a molecular dynamics study.Structural complexity of a composite amyloid fibril.Spontaneous formation of twisted Aβ(16-22) fibrils in large-scale molecular-dynamics simulations.Molecular dynamics simulations on the oligomer-formation process of the GNNQQNY peptide from yeast prion protein Sup35.All-atom computer simulations of amyloid fibrils disaggregation.Computational simulations of the early steps of protein aggregation.Aggregation of amyloids in a cellular context: modelling and experiment.The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Unique example of amyloid aggregates stabilized by main chain H-bond instead of the steric zipper: molecular dynamics study of the amyloidogenic segment of amylin wild-type and mutants.GNNQQNY--investigation of early steps during amyloid formation.Investigating the mechanism of peptide aggregation: insights from mixed monte carlo-molecular dynamics simulations.Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses.Effect of dehydration on the aggregation kinetics of two amyloid peptides.Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations.Thermodynamic description of polymorphism in Q- and N-rich peptide aggregates revealed by atomistic simulation.Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.Molecular modeling to investigate the binding of Congo red toward GNNQQNY protofibril and in silico virtual screening for the identification of new aggregation inhibitors.Simulation studies on the stabilities of aggregates formed by fibril-forming segments of alpha-Synuclein.Thermodynamic analysis of structural transitions during GNNQQNY aggregation.Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.Characterizing Structural Stability of Amyloid Motif Fibrils Mediated by Water Molecules.Structural and Material Properties of Amyloid Aβ40/42 Fibrils.
P2860
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P2860
Molecular dynamics analyses of cross-beta-spine steric zipper models: beta-sheet twisting and aggregation.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
name
Molecular dynamics analyses of ...... heet twisting and aggregation.
@ast
Molecular dynamics analyses of ...... heet twisting and aggregation.
@en
Molecular dynamics analyses of ...... heet twisting and aggregation.
@nl
type
label
Molecular dynamics analyses of ...... heet twisting and aggregation.
@ast
Molecular dynamics analyses of ...... heet twisting and aggregation.
@en
Molecular dynamics analyses of ...... heet twisting and aggregation.
@nl
prefLabel
Molecular dynamics analyses of ...... heet twisting and aggregation.
@ast
Molecular dynamics analyses of ...... heet twisting and aggregation.
@en
Molecular dynamics analyses of ...... heet twisting and aggregation.
@nl
P2093
P2860
P356
P1476
Molecular dynamics analyses of ...... heet twisting and aggregation.
@en
P2093
Carlo Pedone
Luciana Esposito
Luigi Vitagliano
P2860
P304
11533-11538
P356
10.1073/PNAS.0602345103
P407
P577
2006-07-24T00:00:00Z