Evidence map›Paper›PMID 36038502›Full record

ArticleChemistry, an Asian journal2022

Investigation of α-Synuclein and Amyloid-β(42)-E22Δ Oligomers Using SiN Nanopore Functionalized with L-Dopa.

Imad Abrao-Nemeir, Jeremy Bentin, Nathan Meyer, Jean-Marc Janot, Joan Torrent, Fabien Picaud, Sebastien Balme

Open access · hybridAbstract read
In one paragraph

Article in Chemistry, an Asian journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025
    Review
  6. Review
  7. Secondary Nucleation of Aβ Revealed by Single-Molecule and Computational Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Article
  9. Article
  10. Article
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

7 authors at 1 institution in 1 country.

Imad Abrao-NemeirEuropean Institute of Membranes, UMR5635, University of Montpelier, ENCSM CNRS, Place Eugène Bataillon, 34095, Montpellier cedex 5, France.
Jeremy BentinLaboratory of Nanomedicin, Imagery and Therapeutics, EA4662, University hospital center of Besançon, University of Bourgogne-Franche-Comté (UFR Sciences et Techniques), 16 route de Gray, 25030, Besançon, France.
Nathan MeyerEuropean Institute of Membranes, UMR5635, University of Montpelier, ENCSM CNRS, Place Eugène Bataillon, 34095, Montpellier cedex 5, France.
Jean-Marc JanotEuropean Institute of Membranes, UMR5635, University of Montpelier, ENCSM CNRS, Place Eugène Bataillon, 34095, Montpellier cedex 5, France.
Joan TorrentNeurological institute of Montpellier, University of Montpellier, INSERM CNRS, Place Eugène Bataillon, 34095, Montpellier cedex 5, France.
Fabien PicaudLaboratory of Nanomedicin, Imagery and Therapeutics, EA4662, University hospital center of Besançon, University of Bourgogne-Franche-Comté (UFR Sciences et Techniques), 16 route de Gray, 25030, Besançon, France.
Sebastien BalmeEuropean Institute of Membranes, UMR5635, University of Montpelier, ENCSM CNRS, Place Eugène Bataillon, 34095, Montpellier cedex 5, France.ORCID http://orcid.org/0000-0001-8631-5334
Centre National de la Recherche Scientifique · FR

Funding

Agence Nationale de la Recherche ANR-19-CE42-0006GENCIUniversity of Franche-Comté 2021 - DARIA0110913048
6 · The paper itself

Abstract

Solid-state nanopores are an emerging technology used as a high-throughput, label-free analytical method for the characterization of protein aggregation in an aqueous solution. In this work, we used Levodopamine to coat a silicon nitride nanopore surface that was fabricated through a dielectric breakdown in order to reduce the unspecific adsorption. The coating of inner nanopore wall by investigation of the translocation of heparin. The functionalized nanopore was used to investigate the aggregation of amyloid-β and α-synuclein, two biomarkers of degenerative diseases. In the first application, we demonstrate that the α-synuclein WT is more prone to form dimers than the variant A53T. In the second one, we show for the Aβ(42)-E22Δ (Osaka mutant) that the addition of Aβ(42)-WT monomers increases the polymorphism of oligomers, while the incubation with Aβ(42)-WT fibrils generates larger aggregates.

Indexed as

alpha-SynucleinNanoporesAmyloidAmyloid beta-PeptidesHeparinLevodopaProtein Aggregatesalpha-SynucleinAmyloidAmyloid beta-PeptidesHeparinLevodopaProtein Aggregatesaggregationamyloid-βnanoporesingle moleculeα-synuclein

Identifiers

PMID36038502
PMCPMC9826174
OpenAlexW4293778428

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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 OpenQuestion graph.