Evidence map›Paper›PMID 35766994›Full record

ArticleNano letters2022

Quantification of Protein Glycosylation Using Nanopores.

Roderick Corstiaan Abraham Versloot, Florian Leonardus Rudolfus Lucas, Liubov Yakovlieva, Matthijs Jonathan Tadema, Yurui Zhang, Thomas M Wood, Nathaniel I Martin, Siewert J Marrink, Marthe T C Walvoort, Giovanni Maglia

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

  1. Automating Model Building for SPM Images of Biomolecules Using MISO.Journal of chemical information and modeling · 2026
    Article
  2. Review
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  5. Protein Analyte Sensing with an Outer Membrane Protein G (OmpG) Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Detection of protein oligomers with nanopores.Nature reviews. Chemistry · 2025
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
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  20. 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

10 authors at 2 institutions in 1 country.

Roderick Corstiaan Abraham VerslootGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0001-6407-9473
Florian Leonardus Rudolfus LucasGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0002-9561-5408
Liubov YakovlievaChemical Biology Division, Stratingh Institute for Chemistry, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0003-2061-4352
Matthijs Jonathan TademaGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.
Yurui ZhangBiological Chemistry Group, Institute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.
Thomas M WoodBiological Chemistry Group, Institute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.
Nathaniel I MartinBiological Chemistry Group, Institute of Biology Leiden, Leiden University, 2333 BE Leiden, The Netherlands.ORCID 0000-0001-8246-3006
Siewert J MarrinkGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0001-8423-5277
Marthe T C WalvoortChemical Biology Division, Stratingh Institute for Chemistry, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0003-1101-2659
Giovanni MagliaGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747AG Groningen, The Netherlands.ORCID 0000-0003-2784-0811
University of Groningen · NLLeiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although nanopores can be used for single-molecule sequencing of nucleic acids using low-cost portable devices, the characterization of proteins and their modifications has yet to be established. Here, we show that hydrophilic or glycosylated peptides translocate too quickly across FraC nanopores to be recognized. However, high ionic strengths (i.e., 3 M LiCl) and low pH (i.e., pH 3) together with using a nanopore with a phenylalanine at its constriction allows the recognition of hydrophilic peptides, and to distinguish between mono- and diglycosylated peptides. Using these conditions, we devise a nanopore method to detect, characterize, and quantify post-translational modifications in generic proteins, which is one of the pressing challenges in proteomic analysis.

Indexed as

NanoporesGlycosylationNanotechnologyPeptidesProteinsProteomicsPeptidesProteinsnanopore spectrometryprotein glycosylationproteomicsrhamnosylationsingle molecule

Identifiers

PMID35766994
PMCPMC9284675
OpenAlexW4283696392

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.