ArticleAngewandte Chemie (International ed. in English)2023
Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.
Article in Angewandte Chemie (International ed. in English), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
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.
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Who cites it
8 citing papers in PubMed.
- Fluorescence Characterization of Extracellular Vesicles Using Single-Molecule Confocal Microscopy.Small methods · 2025Article
- A Single-Molecule Liposome Assay for Membrane Permeabilization.Angewandte Chemie (International ed. in English) · 2025Article
- Sequential replacement of PSD95 subunits in postsynaptic supercomplexes is slowest in the cortex.eLife · 2024Article
- α-Synuclein oligomers form by secondary nucleation.Nature communications · 2024Article
- Article
- Two-color coincidence single-molecule pulldown for the specific detection of disease-associated protein aggregates.Science advances · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (International ed. in English) · 2023Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Protein misfolding and aggregation into oligomeric and fibrillar structures is a common feature of many neurogenerative disorders. Single-molecule techniques have enabled characterization of these lowly abundant, highly heterogeneous protein aggregates, previously inaccessible using ensemble averaging techniques. However, they usually rely on the use of recombinantly-expressed labeled protein, or on the addition of amyloid stains that are not protein-specific. To circumvent these challenges, we have made use of a high affinity antibody labeled with orthogonal fluorophores combined with fast-flow microfluidics and single-molecule confocal microscopy to specifically detect α-synuclein, the protein associated with Parkinson's disease. We used this approach to determine the number and size of α-synuclein aggregates down to picomolar concentrations in biologically relevant samples.
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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.