Evidence map›Paper›PMID 37327131›Full record

ArticleACS nano2023

Simultaneous Determination of the Size and Shape of Single α-Synuclein Oligomers in Solution.

Saurabh Awasthi, Cuifeng Ying, Jiali Li, Michael Mayer

Open access · hybridAbstract read
In one paragraph

Article in ACS nano, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Carbon-13 Centerband-Only Detection of EXchange with Dynamic Nuclear Polarization.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Recent advances in single-particle analysis with nanopore technology.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
  14. Review
  15. Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Characterizing heterogeneity in amyloid formation processes.Current opinion in structural biology · 2024
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

Saurabh AwasthiAdolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland.ORCID 0000-0002-7243-5578
Cuifeng YingAdolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland.ORCID 0000-0002-7279-1388
Jiali LiUniversity of Arkansas, Fayetteville, Arkansas 72701, United States.ORCID 0000-0002-8198-1132
Michael MayerAdolphe Merkle Institute, University of Fribourg, Chemin des Verdiers 4, CH-1700 Fribourg, Switzerland.ORCID 0000-0002-6148-5756
University of Fribourg · CHUniversity of Arkansas at Fayetteville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Soluble oligomers of amyloid-forming proteins are implicated as toxic species in the context of several neurodegenerative diseases. Since the size and shape of these oligomers influence their toxicity, their biophysical characterization is essential for a better understanding of the structure-toxicity relationship. Amyloid oligomers are difficult to characterize by conventional approaches due to their heterogeneity in size and shape, their dynamic aggregation process, and their low abundance. This work demonstrates that resistive pulse measurements using polymer-coated solid-state nanopores enable single-particle-level characterization of the size and shape of individual αSyn oligomers in solution within minutes. A comparison of the resulting size distribution with single-particle analysis by transmission electron microscopy and mass photometry reveals good agreement with superior resolution by nanopore-based characterization. Moreover, nanopore-based analysis has the capability to combine rapid size analysis with an approximation of the oligomer shape. Applying this shape approximation to putatively toxic oligomeric species that range in size from 18 ± 7 aggregated monomers (10S) to 29 ± 10 aggregated monomers (15S) and in concentration from picomolar to nanomolar revealed oligomer shapes that agree well with previous estimates by cryo-EM with the added advantage that nanopore-based analysis occurs rapidly, in solution, and has the potential to become a widely accessible technique.

Indexed as

alpha-SynucleinParkinson DiseaseAmyloidAmyloidogenic ProteinsHumansMicroscopy, Electron, Transmissionalpha-SynucleinAmyloidAmyloidogenic Proteinsaggregationamyloid oligomersnanoporeresistive pulse sensingα-synuclein

Identifiers

PMID37327131
PMCPMC10339783
OpenAlexW4380988868

What Socratic holds

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Registered trials

None linked

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 Socratic graph.