Evidence map›Paper›PMID 29511176›Full record

ArticleNature communications2018

Identification of single amino acid differences in uniformly charged homopolymeric peptides with aerolysin nanopore.

Fabien Piguet, Hadjer Ouldali, Manuela Pastoriza-Gallego, Philippe Manivet, Juan Pelta, Abdelghani Oukhaled

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
–field-weighted citation impact
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

111 citing papers in PubMed.

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  16. Graphene Nanopore Fabrication and Applications.International journal of molecular sciences · 2025
    Review
  17. Review
  18. Review
  19. Article
  20. Article

51 more citing papers are in PubMed but not listed here.

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

6 authors.

Fabien PiguetLAMBE UMR 8587, Université de Cergy-Pontoise, 95300, Pontoise, France. fabien.piguet@u-cergy.fr.
Hadjer OuldaliLAMBE UMR 8587, Université de Cergy-Pontoise, 95300, Pontoise, France.
Manuela Pastoriza-GallegoLAMBE UMR 8587, Université de Cergy-Pontoise, 95300, Pontoise, France.
Philippe ManivetAPHP, Centre de Ressources Biologiques BB-0033-00064, Plateforme de Bio-Pathologie et de Technologies Innovantes en santé, Hôpital Lariboisière, 75010, Paris, France.
Juan PeltaLAMBE UMR 8587, Université d'Evry-Val-d'Essonne, 91000, Evry, France. juan.pelta@univ-evry.fr.
Abdelghani OukhaledLAMBE UMR 8587, Université de Cergy-Pontoise, 95300, Pontoise, France. abdelghani.oukhaled@u-cergy.fr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There are still unmet needs in finding new technologies for biomedical diagnostic and industrial applications. A technology allowing the analysis of size and sequence of short peptide molecules of only few molecular copies is still challenging. The fast, low-cost and label-free single-molecule nanopore technology could be an alternative for addressing these critical issues. Here, we demonstrate that the wild-type aerolysin nanopore enables the size-discrimination of several short uniformly charged homopeptides, mixed in solution, with a single amino acid resolution. Our system is very sensitive, allowing detecting and characterizing a few dozens of peptide impurities in a high purity commercial peptide sample, while conventional analysis techniques fail to do so.

Indexed as

Bacterial ToxinsNanoporesNanotechnologyPeptidesPolymersPore Forming Cytotoxic ProteinsaerolysinBacterial ToxinsPeptidesPolymersPore Forming Cytotoxic Proteins

Identifiers

PMID29511176
PMCPMC5840376

What OpenQuestion holds

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LicenceCC BY
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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 OpenQuestion graph.