Evidence map›Paper›PMID 28353339›Full record

ArticleACS nano2017

Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore.

Carsten Wloka, Veerle Van Meervelt, Dewi van Gelder, Natasha Danda, Nienke Jager, Chris P Williams, Giovanni Maglia

Abstract read
In one paragraph

Article in ACS nano, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing 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

50 citing papers in PubMed.

  1. The Ion Permeability of DNA Nanotube Channels.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  2. Review
  3. Review
  4. Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Chemical Tools for Probing the Ub/Ubl Conjugation Cascades.Chembiochem : a European journal of chemical biology · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Ubiquitination detection techniques.Experimental biology and medicine (Maywood, N.J.) · 2023
    Review
  18. Article
  19. Real-time label-free detection of dynamic aptamer-small molecule interactions using a nanopore nucleic acid conformational sensor.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

7 authors.

Carsten WlokaChemical Biology I, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.ORCID 0000-0003-0487-3311
Veerle Van MeerveltDepartment of Chemistry, University of Leuven , 3001 Leuven, Belgium.
Dewi van GelderMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.
Natasha DandaMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.
Nienke JagerChemical Biology I, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.
Chris P WilliamsMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.
Giovanni MagliaChemical Biology I, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen , 9747 AG Groningen, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The covalent addition of ubiquitin to target proteins is a key post-translational modification that is linked to a myriad of biological processes. Here, we report a fast, single-molecule, and label-free method to probe the ubiquitination of proteins employing an engineered Cytolysin A (ClyA) nanopore. We show that ionic currents can be used to recognize mono- and polyubiquitinated forms of native proteins under physiological conditions. Using defined conjugates, we also show that isomeric monoubiquitinated proteins can be discriminated. The nanopore approach allows following the ubiquitination reaction in real time, which will accelerate the understanding of fundamental mechanisms linked to protein ubiquitination.

Indexed as

Biological ProductsMolecular ImagingNanoporesNanotechnologyPerforinProtein Processing, Post-TranslationalProteinsUbiquitinUbiquitinationBiological ProductsPerforinProteinsUbiquitinnanoporenanotechnologyprotein modificationssingle-molecule kineticsubiquitin

Identifiers

PMID28353339
PMCPMC5444049

What Socratic holds

Textmetadata
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.