Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
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Dimer formation enhances structural differences between amyloid β-protein (1-40) and (1-42): an explicit-solvent molecular dynamics studyModulation of p53 binding to MDM2: computational studies reveal important roles of Tyr100Computational backbone mutagenesis of Abeta peptides: probing the role of backbone hydrogen bonds in aggregation.Molecular dynamics simulations of anti-aggregation effect of ibuprofen.Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Globular state in the oligomers formed by Abeta peptides.Mapping conformational ensembles of aβ oligomers in molecular dynamics simulationsNonsteroidal anti-inflammatory drug naproxen destabilizes Aβ amyloid fibrils: a molecular dynamics investigation.The unique Alzheimer's β-amyloid triangular fibril has a cavity along the fibril axis under physiological conditions.Binding of nonsteroidal anti-inflammatory drugs to Abeta fibrilNaproxen interferes with the assembly of Aβ oligomers implicated in Alzheimer's disease.Alzheimer's protective A2T mutation changes the conformational landscape of the Aβ₁₋₄₂ monomer differently than does the A2V mutation.Does amino acid sequence determine the properties of Aβ dimer?Amyloid β-Protein Assembly: Differential Effects of the Protective A2T Mutation and Recessive A2V Familial Alzheimer's Disease Mutation.Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.In silico cross seeding of Aβ and amylin fibril-like oligomers.Molecular dynamics simulations of Ibuprofen binding to Abeta peptidesSide chain interactions can impede amyloid fibril growth: replica exchange simulations of Abeta peptide mutant.Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Modulation in the conformational and stability attributes of the Alzheimer's disease associated amyloid-beta mutants and their favorable stabilization by curcumin: molecular dynamics simulation analysis.Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.Molecular interactions of Alzheimer's biomarker FDDNP with Aβ peptide.
P2860
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P2860
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
description
2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@ast
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@en
type
label
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@ast
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@en
prefLabel
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@ast
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@en
P2860
P356
P1476
Probing the effect of amino-terminal truncation for Abeta1-40 peptides.
@en
P2093
Dmitri K Klimov
Takako Takeda
P2860
P304
P356
10.1021/JP9016773
P407
P577
2009-05-01T00:00:00Z