Evidence map›Paper›PMID 40097683›Full record

ReviewNature biotechnology2025

Toward single-molecule protein sequencing using nanopores.

Chunzhe Lu, Andrea Bonini, Jakob H Viel, Giovanni Maglia

Abstract readReview
In one paragraph

Review in Nature biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Generalizable Direct Protein Sequencing With InstaNexus.Molecular & cellular proteomics : MCP · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Protein Analyte Sensing with an Outer Membrane Protein G (OmpG) Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  16. Article
  17. Purification and Oligomerization of YaxAB Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  18. Article
  19. Fabrication and Characterization of Glass Nanopores.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  20. 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

4 authors.

Chunzhe Lu *University of Groningen, Chemical Biology Department, Groningen Biomolecular Sciences and Biotechnology, Groningen, Netherlands.ORCID http://orcid.org/0000-0002-9453-4550
Andrea Bonini *University of Groningen, Chemical Biology Department, Groningen Biomolecular Sciences and Biotechnology, Groningen, Netherlands.ORCID http://orcid.org/0000-0001-9511-0699
Jakob H Viel *University of Groningen, Chemical Biology Department, Groningen Biomolecular Sciences and Biotechnology, Groningen, Netherlands.
Giovanni Maglia *University of Groningen, Chemical Biology Department, Groningen Biomolecular Sciences and Biotechnology, Groningen, Netherlands. giovanni.maglia@rug.nl.ORCID http://orcid.org/0000-0003-2784-0811

Funding

Designed nanopores for single-molecule protein sequencingR01HG012554 · NHGRI · GRONINGEN UNIVERSITY · PI MAGLIA, GIOVANNI · 2022 to 2024
$1.3M
Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research) 14965NHGRI NIH HHS R01 HG012554U.S. Department of Health & Human Services | NIH | National Human Genome Research Institute (NHGRI) 14965U.S. Department of Health & Human Services | NIH | National Human Genome Research Institute (NHGRI) 1R01HG012554
6 · The paper itself

Abstract

Over the past three decades, biological nanopore sequencing has grown from a research curiosity to a mature technology to sequence nucleic acids at the single-molecule level. Now, recent achievements suggest that nanopores might be able to sequence proteins soon. In this Perspective, we analyze the different approaches that have been proposed to measure proteins and peptides using nanopores. We predict that, more likely than not, nanopores will be capable of identifying full-length proteins at the single-molecule level and with single-amino acid resolution, paving the way to single-molecule protein sequencing. This would allow several applications in proteomics that are at present challenging, including measuring the heterogeneity of post-translational modifications, quantifying low-abundance proteins and characterizing protein splicing.

Indexed as

NanoporesNanopore SequencingProteinsSequence Analysis, ProteinHumansProteomicsProteins

Identifiers

PMID40097683
PMCPMC12006967

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.