ArticleBiophysical journal2013
Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Somatostatin: Linking Cognition and Alzheimer Disease to Therapeutic Targeting.Pharmacological reviews · 2024Review
- Predictive network analysis identifies JMJD6 and other potential key drivers in Alzheimer's disease.Communications biology · 2023Article
- Calcium inhibits penetration of Alzheimer's AβProteins · 2022Article
- The Positive Side of the Alzheimer's Disease Amyloid Cross-Interactions: The Case of the Aβ 1-42 Peptide with Tau, TTR, CysC, and ApoA1.Molecules (Basel, Switzerland) · 2020Review
- How Fluorescent Tags Modify Oligomer Size Distributions of the Alzheimer Peptide.Biophysical journal · 2019Article
- Stability analysis of a steady state of a model describing Alzheimer's disease and interactions with prion proteins.Journal of mathematical biology · 2019Article
- Single-molecule photobleaching: Instrumentation and applications.Journal of biosciences · 2018Article
- Alzheimer's disease: amyloid-based pathogenesis and potential therapies.Cell stress · 2018Article
- 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.International journal of molecular sciences · 2018Review
- Amyloid-β(1-42) Aggregation Initiates Its Cellular Uptake and Cytotoxicity.The Journal of biological chemistry · 2016Article
- Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.Scientific reports · 2016Article
- The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy.EBioMedicine · 2016Review
- First effects of rising amyloid-β in transgenic mouse brain: synaptic transmission and gene expression.Brain : a journal of neurology · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
- Monitoring of single vesicle cytochrome-c release illuminates BAK as a novel target of Aβ oligomers.Biophysical journal · 2014Article
- Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease.Cellular and molecular life sciences : CMLS · 2014Review
- Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs).Chemical reviews · 2014Review
- Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies.Protein science : a publication of the Protein Society · 2014Review
- Targeting the proper amyloid-beta neuronal toxins: a path forward for Alzheimer's disease immunotherapeutics.Alzheimer's research & therapy · 2014Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Soluble oligomers of the amyloid-β peptide have been implicated as proximal neurotoxins in Alzheimer's disease. However, the identity of the neurotoxic aggregate(s) and the mechanisms by which these species induce neuronal dysfunction remain uncertain. Physiologically relevant experimentation is hindered by the low endogenous concentrations of the peptide, the metastability of Aβ oligomers, and the wide range of observed interactions between Aβ and biological membranes. Single-molecule microscopy represents one avenue for overcoming these challenges. Using this technique, we find that Aβ binds to primary rat hippocampal neurons at physiological concentrations. Although amyloid-β(1-40) as well as amyloid-β(1-42) initially form larger oligomers on neurites than on glass slides, a 1:1 mix of the two peptides result in smaller neurite-bound oligomers than those detected on-slide or for either peptide alone. With 1 nM peptide in solution, Aβ40 oligomers do not grow over the course of 48 h, Aβ42 oligomers grow slightly, and oligomers of a 1:1 mix grow substantially. Evidently, small Aβ oligomers are capable of binding to neurons at physiological concentrations and grow at rates dependent on local Aβ42:Aβ40 ratios. These results are intriguing in light of the increased Aβ42:Aβ40 ratios shown to correlate with familial Alzheimer's disease mutations.
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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.