Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations
about
Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeuticsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesTransnasal delivery of human A-beta peptides elicits impaired learning and memory performance in wild type mice.The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideSingle molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Aβ1-42 monomers or oligomers have different effects on autophagy and apoptosisMultivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicityAnalysis of the native structure, stability and aggregation of biotinylated human lysozyme.Weak glycolipid binding of a microdomain-tracer peptide correlates with aggregation and slow diffusion on cell membranes.Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.Role of membrane biophysics in Alzheimer's-related cell pathways.Single-particle characterization of Aβ oligomers in solution.β-Amyloid (1-40) peptide interactions with supported phospholipid membranes: a single-molecule studySingle-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processesAmyloid-β(1-42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity.Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.The lipid networkAmmonium hydroxide treatment of Aβ produces an aggregate free solution suitable for biophysical and cell culture characterization.Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoformsSingle-cell screening of cytosolic [Ca(2+)] reveals cell-selective action by the Alzheimer's Aβ peptide ion channel.A folding transition underlies the emergence of membrane affinity in amyloid-β.Tip-enhanced Raman spectroscopy of amyloid β at neuronal spines.
P2860
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P2860
Direct observation of single amyloid-β(1-40) oligomers on live cells: binding and growth at physiological concentrations
description
2011 nî lūn-bûn
@nan
2011 թուականին հրատարակուած գիտական յօդուած
@hyw
2011 թվականին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
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name
Direct observation of single a ...... t physiological concentrations
@ast
Direct observation of single a ...... t physiological concentrations
@en
Direct observation of single a ...... t physiological concentrations
@nl
type
label
Direct observation of single a ...... t physiological concentrations
@ast
Direct observation of single a ...... t physiological concentrations
@en
Direct observation of single a ...... t physiological concentrations
@nl
prefLabel
Direct observation of single a ...... t physiological concentrations
@ast
Direct observation of single a ...... t physiological concentrations
@en
Direct observation of single a ...... t physiological concentrations
@nl
P2093
P2860
P3181
P1433
P1476
Direct observation of single a ...... t physiological concentrations
@en
P2093
Duncan G Steel
Joseph A Schauerte
Kathleen C Wisser
Robin D Johnson
P2860
P304
P3181
P356
10.1371/JOURNAL.PONE.0023970
P407
P577
2011-01-01T00:00:00Z