Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
about
Effect of N-homocysteinylation on physicochemical and cytotoxic properties of amyloid β-peptideAmyloid beta-protein monomer folding: free-energy surfaces reveal alloform-specific differencesDisrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsInfluence of preformed Asp23-Lys28 salt bridge on the conformational fluctuations of monomers and dimers of Abeta peptides with implications for rates of fibril formationStructure and dynamics of parallel beta-sheets, hydrophobic core, and loops in Alzheimer's A beta fibrilsProbing protein aggregation using discrete molecular dynamicsStructural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Benchmarking implicit solvent folding simulations of the amyloid beta(10-35) fragmentStructure and dynamics of the Abeta(21-30) peptide from the interplay of NMR experiments and molecular simulations.Association thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralizationTransient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy.Extending the PRIME model for protein aggregation to all 20 amino acids.Solvent and mutation effects on the nucleation of amyloid beta-protein foldingMinimal model of self-assembly: emergence of diversity and complexity.Impact of the mutation A21G (Flemish variant) on Alzheimer's beta-amyloid dimers by molecular dynamics simulations.The peculiar role of the A2V mutation in amyloid-β (Aβ) 1-42 molecular assemblyInvestigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Role of electrostatic interactions in amyloid beta-protein (A beta) oligomer formation: a discrete molecular dynamics studyAn azobenzene photoswitch sheds light on turn nucleation in amyloid-β self-assembly.Familial Alzheimer's disease mutations alter the stability of the amyloid beta-protein monomer folding nucleusDynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.Molecular plasticity regulates oligomerization and cytotoxicity of the multipeptide-length amyloid-β peptide poolRole of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein.The structures of the E22Δ mutant-type amyloid-β alloforms and the impact of E22Δ mutation on the structures of the wild-type amyloid-β alloforms.Ab initio folding of proteins with all-atom discrete molecular dynamics.Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopyStructures and free-energy landscapes of the wild type and mutants of the Abeta(21-30) peptide are determined by an interplay between intrapeptide electrostatic and hydrophobic interactions.Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.Aβ monomers transiently sample oligomer and fibril-like configurations: ensemble characterization using a combined MD/NMR approachStructures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretaseThe use of mass spectrometry to study amyloid-β peptides.Energetic contributions of residues to the formation of early amyloid-β oligomers.Effects of familial Alzheimer's disease mutations on the folding nucleation of the amyloid beta-protein.Structural diversity of Alzheimer's disease amyloid-β dimers and their role in oligomerization and fibril formation.A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.Characterization of the nucleation barriers for protein aggregation and amyloid formation.Gly25-Ser26 amyloid β-protein structural isomorphs produce distinct Aβ42 conformational dynamics and assembly characteristics.Structural dynamics of the amyloid β-protein monomer folding nucleus.On the nucleation of amyloid beta-protein monomer folding.The conformations of the amyloid-beta (21-30) fragment can be described by three families in solution.
P2860
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P2860
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@ast
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@en
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@nl
type
label
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@ast
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@en
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@nl
prefLabel
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@ast
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@en
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@nl
P2860
P50
P356
P1476
Folding events in the 21-30 region of amyloid beta-protein (Abeta) studied in silico
@en
P2093
David B Teplow
P2860
P304
P356
10.1073/PNAS.0502006102
P407
P577
2005-04-26T00:00:00Z