Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein.
about
A comparative analysis of the aggregation behavior of amyloid-β peptide variantsAtomic-level characterization of the ensemble of the Aβ(1-42) monomer in water using unbiased molecular dynamics simulations and spectral algorithmsA condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.Structure and dynamics of amyloid-β segmental polymorphismsLow molecular weight oligomers of amyloid peptides display beta-barrel conformations: a replica exchange molecular dynamics study in explicit solvent.Association thermodynamics and conformational stability of beta-sheet amyloid beta(17-42) oligomers: effects of E22Q (Dutch) mutation and charge neutralizationAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Fibril elongation by Aβ(17-42): kinetic network analysis of hybrid-resolution molecular dynamics simulationsThermodynamic perspective on the dock-lock growth mechanism of amyloid fibrils.Altered synaptic structure in the hippocampus in a mouse model of Alzheimer's disease with soluble amyloid-β oligomers and no plaque pathologyMolecular origin of Gerstmann-Sträussler-Scheinker syndrome: insight from computer simulation of an amyloidogenic prion peptide.Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.Disordered binding of small molecules to Aβ(12-28).β-Amyloid carrying the Dutch mutation has diverse effects on calpain-mediated toxicity in hippocampal neurons.Dynamics of metastable β-hairpin structures in the folding nucleus of amyloid β-protein.Role of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Induced Dipole-Dipole Interactions Influence the Unfolding Pathways of Wild-Type and Mutant Amyloid β-Peptides.Design and Optimization of Anti-amyloid Domain Antibodies Specific for β-Amyloid and Islet Amyloid PolypeptideTemperature and chemical denaturant dependence of forced unfolding of titin I27.Molecular consequences of amyloid precursor protein and presenilin mutations causing autosomal-dominant Alzheimer's diseaseStructural exploration and Förster theory modeling for the interpretation of gas-phase FRET measurements: Chromophore-grafted amyloid-β peptides.Fourier transform infrared spectroscopy on external perturbations inducing secondary structure changes of hemoglobin.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.Introduction of d-Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity.Side-chain hydrophobicity and the stability of Aβ₁₆₋₂₂ aggregates.Phosphorylation as a tool to modulate aggregation propensity and to predict fibril architecture.Comparative fibril formation of analogs corresponding to the (12-24) segment of the β-amyloid peptide.Molecular dynamics simulations and novel drug discovery.Assembly dynamics of two-beta sheets revealed by molecular dynamics simulations.Dimerization and conformation-related free energy landscapes of dye-tagged amyloid-β12-28 linked to FRET experiments.Insights into the Molecular Mechanisms of Alzheimer's and Parkinson's Diseases with Molecular Simulations: Understanding the Roles of Artificial and Pathological Missense Mutations in Intrinsically Disordered Proteins Related to Pathology.Electrochemical probing of the solution pH-induced structural alterations around the heme group in myoglobin
P2860
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P2860
Role of the familial Dutch mutation E22Q in the folding and aggregation of the 15-28 fragment of the Alzheimer amyloid-beta protein.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@ast
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@en
type
label
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@ast
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@en
prefLabel
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@ast
Role of the familial Dutch mut ...... lzheimer amyloid-beta protein.
@en
P2860
P356
P1476
Role of the familial Dutch mut ...... Alzheimer amyloid-beta protein
@en
P2093
Joan-Emma Shea
Mary Griffin Krone
P2860
P304
P356
10.1073/PNAS.0708193105
P407
P50
P577
2008-04-11T00:00:00Z