Monte Carlo Study of the Formation and Conformational Properties of Dimers of Aβ42 Variants
about
β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptidesThe toxicity of amyloid β oligomersDimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyFlexibility and binding affinity in protein-ligand, protein-protein and multi-component protein interactions: limitations of current computational approaches.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Binding of apolipoprotein E inhibits the oligomer growth of amyloid-β peptide in solution as determined by fluorescence cross-correlation spectroscopy.Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationImpact of chemical heterogeneity on protein self-assembly in water.Study of structural stability and damaging effect on membrane for four Aβ42 dimers.Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.Structure of ring-shaped Aβ₄₂ oligomers determined by conformational selection.Kinesin-1 inhibits the aggregation of amyloid-β peptide as detected by fluorescence cross-correlation spectroscopy.Energetic contributions of residues to the formation of early amyloid-β oligomers.Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.Molecular mechanism of misfolding and aggregation of Aβ(13-23).A β-hairpin-binding protein for three different disease-related amyloidogenic proteins.Atomic and dynamic insights into the beneficial effect of the 1,4-naphthoquinon-2-yl-L-tryptophan inhibitor on Alzheimer's Aβ1-42 dimer in terms of aggregation and toxicity.Mechanical resistance in unstructured proteins.Effect of the English familial disease mutation (H6R) on the monomers and dimers of Aβ40 and Aβ42Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.Distinct phases of free α-synuclein--a Monte Carlo study.Self-assembly of the full-length amyloid Aβ42 protein in dimers.Accelerating atomic-level protein simulations by flat-histogram techniques.
P2860
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P2860
Monte Carlo Study of the Formation and Conformational Properties of Dimers of Aβ42 Variants
description
im Juli 2011 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в липні 2011
@uk
name
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@en
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@nl
type
label
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@en
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@nl
prefLabel
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@en
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@nl
P50
P1476
Monte Carlo Study of the Forma ...... ies of Dimers of Aβ42 Variants
@en
P2093
Iskra Staneva
P304
P356
10.1016/J.JMB.2011.05.014
P407
P577
2011-07-01T00:00:00Z