ArticleBiophysical journal2010
Measurement of the attachment and assembly of small amyloid-β oligomers on live cell membranes at physiological concentrations using single-molecule tools.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 65 citations in OpenAlex.
- Calcium inhibits penetration of Alzheimer's AβProteins · 2022Article
- Determining the Stoichiometry of Amyloid Oligomers by Single-Molecule Photobleaching.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- De novo aggregation of Alzheimer's Aβ25-35 peptides in a lipid bilayer.Scientific reports · 2019Article
- Methionine Oxidation Changes the Mechanism of Aβ Peptide Binding to the DMPC Bilayer.Scientific reports · 2019Article
- Single-molecule photobleaching: Instrumentation and applications.Journal of biosciences · 2018Article
- Glucose directs amyloid-beta into membrane-active oligomers.Physical chemistry chemical physics : PCCP · 2017Article
- Is the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?PLoS computational biology · 2017Article
- Individual aggregates of amyloid beta induce temporary calcium influx through the cell membrane of neuronal cells.Scientific reports · 2016Article
- Calcium enhances binding of Aβ monomer to DMPC lipid bilayer.Biophysical journal · 2015Article
- Effects of Low Amyloid-β (Aβ) Concentration on Aβ1-42 Oligomers Binding and GluN2B Membrane Expression.Journal of Alzheimer's disease : JAD · 2015Article
- Cellular membrane fluidity in amyloid precursor protein processing.Molecular neurobiology · 2014Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Aggregation distributions on cells determined by photobleaching image correlation spectroscopy.Biophysical journal · 2013Article
- Binding to the lipid monolayer induces conformational transition in Aβ monomer.Journal of molecular modeling · 2013Article
- Synergistic interactions between Alzheimer's Aβ40 and Aβ42 on the surface of primary neurons revealed by single molecule microscopy.PloS one · 2013Article
- Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Frontiers in physiology · 2013Article
- Quantitative fluorescence loss in photobleaching for analysis of protein transport and aggregation.BMC bioinformatics · 2012Article
- Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay.The Journal of biological chemistry · 2012Article
- Weak glycolipid binding of a microdomain-tracer peptide correlates with aggregation and slow diffusion on cell membranes.PloS one · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is thought that the pathological cascade in Alzheimer's disease is initiated by the formation of amyloid-β (Aβ) peptide complexes on cell membranes. However, there is considerable debate about the nature of these complexes and the type of solution-phase Aβ aggregates that may contribute to their formation. Also, it is yet to be shown that Aβ attaches strongly to living cell membranes, and that this can happen at low, physiologically relevant Aβ concentrations. Here, we simultaneously measure the aggregate size and fluorescence lifetime of fluorescently labeled Aβ(1-40) on and above the membrane of cultured PC12 cells at near-physiological concentrations. We find that at 350 nM Aβ concentration, large (>>10 nm average hydrodynamic radius) assemblies of codiffusing, membrane-attached Aβ molecules appear on the cell membrane together with a near-monomeric species. When the extracellular concentration is 150 nM, the membrane contains only the smaller species, but with a similar degree of attachment. At both concentrations, the extracellular solution contains only small (∼2.3 nm average hydrodynamic radius) Aβ oligomers or monomers. We conclude that at near-physiological concentrations only the small oligomeric Aβ species are relevant, they are capable of attaching to the cell membrane, and they assemble in situ to form much larger complexes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.