ArticleACS nano2012
Single-particle characterization of Aβ oligomers in solution.
Article in ACS nano, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
34 citing papers in PubMed.
- Multispectral photoacoustic microscopy and NIR-II fluorescence imaging of TREM2-positive microglia in Aβ-driven Alzheimer's pathogenesis.Fundamental research · 2026Article
- Selective and Controllable Trapping of Single Proteins in Nanopores Using Reversible Covalent Bonds.ACS nano · 2026Article
- Single-Molecule Techniques for Probing the Conformation, Dynamics and Interactions of Intrinsically Disordered Proteins.Biophysics reviews · 2025Article
- Article
- Cellular and Nuclear Forces: An Overview.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Characterizing Prion-Like Protein Aggregation: Emerging Nanopore-Based Approaches.Small methods · 2024Review
- Accelerated Alzheimer's Aβ-42 secondary nucleation chronologically visualized on fibril surfaces.Science advances · 2024Article
- Secondary Nucleation of Aβ Revealed by Single-Molecule and Computational Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Fluorescence-Based Monitoring of Early-Stage Aggregation of Amyloid-β, Amylin Peptide, Tau, and α-Synuclein Proteins.ACS chemical neuroscience · 2024Article
- Single-Molecule Detection of α-Synuclein Oligomers in Parkinson's Disease Patients Using Nanopores.ACS nano · 2023Article
- Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.ACS nano · 2023Article
- Investigation of α-Synuclein and Amyloid-β(42)-E22Δ Oligomers Using SiN Nanopore Functionalized with L-Dopa.Chemistry, an Asian journal · 2022Article
- Localized Nanopore Fabrication via Controlled Breakdown.Nanomaterials (Basel, Switzerland) · 2022Review
- Fast Decoding of the First Steps of Protein Aggregation Using a Nanopipette.ACS central science · 2022Article
- Real-Time Fast Amyloid Seeding and Translocation of α-Synuclein with a Nanopipette.ACS central science · 2022Article
- The NEOtrap - en route with a new single-molecule technique.iScience · 2021Review
- Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore.Nano letters · 2020Article
- Toward Nanopore Electrospray Mass Spectrometry: Nanopore Effects in the Analysis of Bacteria.ACS central science · 2020Article
- Application of Solid-State Nanopore in Protein Detection.International journal of molecular sciences · 2020Review
- Complete aggregation pathway of amyloid β (1-40) and (1-42) resolved on an atomically clean interface.Science advances · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Determining the pathological role of amyloids in amyloid-associated diseases will require a method for characterizing the dynamic distributions in size and shape of amyloid oligomers with high resolution. Here, we explored the potential of resistive-pulse sensing through lipid bilayer-coated nanopores to measure the size of individual amyloid-β oligomers directly in solution and without chemical modification. This method classified individual amyloid-β aggregates as spherical oligomers, protofibrils, or mature fibers and made it possible to account for the large heterogeneity of amyloid-β aggregate sizes. The approach revealed the distribution of protofibrillar lengths (12- to 155 -mer) as well as the average cross-sectional area of protofibrils and fibers.
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What OpenQuestion holds
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.