Spontaneous beta-barrel formation: an all-atom Monte Carlo study of Abeta16-22 oligomerization
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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesA multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Low molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Effect of beta-sheet propensity on peptide aggregation.PHAISTOS: a framework for Markov chain Monte Carlo simulation and inference of protein structure.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Carbon nanotube inhibits the formation of β-sheet-rich oligomers of the Alzheimer's amyloid-β(16-22) peptide.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationComputational validation of protein nanotubesReduced atomic pair-interaction design (RAPID) model for simulations of proteins.Dynamics of locking of peptides onto growing amyloid fibrils.Aggregation of amyloids in a cellular context: modelling and experiment.Amyloid scaffolds as alternative chlorosomes.An effective all-atom potential for proteinsComputer simulations of the growth of synthetic peptide fibres.Diversity of kinetic pathways in amyloid fibril formation.Thermodynamics of amyloid formation and the role of intersheet interactions.Assemblies of amyloid-β30-36 hexamer and its G33V/L34T mutants by replica-exchange molecular dynamics simulation.Accelerating atomic-level protein simulations by flat-histogram techniques.Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation.Monte Carlo simulations of protein amyloid formation reveal origin of sigmoidal aggregation kinetics.β-barrel Oligomers as Common Intermediates of Peptides Self-Assembling into Cross-β Aggregates.The interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide
P2860
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P2860
Spontaneous beta-barrel formation: an all-atom Monte Carlo study of Abeta16-22 oligomerization
description
im April 2008 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2008
@uk
name
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@en
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@nl
type
label
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@en
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@nl
prefLabel
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@en
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@nl
P356
P1433
P1476
Spontaneous beta-barrel format ...... of Abeta16-22 oligomerization
@en
P304
P356
10.1002/PROT.21682
P407
P577
2008-04-01T00:00:00Z