Measurement of the attachment and assembly of small amyloid-β oligomers on live cell membranes at physiological concentrations using single-molecule tools.
about
Quantitative fluorescence loss in photobleaching for analysis of protein transport and aggregation.Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Individual aggregates of amyloid beta induce temporary calcium influx through the cell membrane of neuronal cells.Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrationsWeak glycolipid binding of a microdomain-tracer peptide correlates with aggregation and slow diffusion on cell membranes.Aggregation distributions on cells determined by photobleaching image correlation spectroscopySynergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay.Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?The role of metallobiology and amyloid-β peptides in Alzheimer's disease.Cellular membrane fluidity in amyloid precursor protein processing.Recent applications of fluorescence correlation spectroscopy in live systems.Glucose directs amyloid-beta into membrane-active oligomers.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Calcium enhances binding of Aβ monomer to DMPC lipid bilayer.Nature of the amyloid-beta monomer and the monomer-oligomer equilibrium.Effects of Low Amyloid-β (Aβ) Concentration on Aβ1-42 Oligomers Binding and GluN2B Membrane Expression.Impacts of membrane biophysics in Alzheimer's disease: from amyloid precursor protein processing to aβ Peptide-induced membrane changes.A folding transition underlies the emergence of membrane affinity in amyloid-β.Single-molecule assays for investigating protein misfolding and aggregation.Inclusion of lipopeptides into the DMPC lipid bilayers prevents Aβ peptide insertion.Biofunctionalized Silica Nanoparticles: Standards in Amyloid-β Oligomer-Based Diagnosis of Alzheimer's Disease.
P2860
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P2860
Measurement of the attachment and assembly of small amyloid-β oligomers on live cell membranes at physiological concentrations using single-molecule tools.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Measurement of the attachment ...... s using single-molecule tools.
@en
Measurement of the attachment ...... s using single-molecule tools.
@nl
type
label
Measurement of the attachment ...... s using single-molecule tools.
@en
Measurement of the attachment ...... s using single-molecule tools.
@nl
prefLabel
Measurement of the attachment ...... s using single-molecule tools.
@en
Measurement of the attachment ...... s using single-molecule tools.
@nl
P2860
P1433
P1476
Measurement of the attachment ...... ns using single-molecule tools
@en
P2093
P2860
P304
P356
10.1016/J.BPJ.2010.07.020
P407
P577
2010-09-01T00:00:00Z