Evidence map›Paper›PMID 28630164›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2017

Single-molecule nanopore enzymology.

Kherim Willems, Veerle Van Meervelt, Carsten Wloka, Giovanni Maglia

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Analysis of Single Biomacromolecules and Viruses: Is It a Myth or Reality?International journal of molecular sciences · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Real-Time and Label-Free Measurement of Deubiquitinase Activity with a MspA Nanopore.Chembiochem : a European journal of chemical biology · 2021
    Article
  13. Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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.

Kherim WillemsDepartment of Chemistry, KU Leuven, Celestijnenlaan 200G, 3001 Leuven, Belgium.
Veerle Van MeerveltDepartment of Chemistry, KU Leuven, Celestijnenlaan 200G, 3001 Leuven, Belgium.
Carsten WlokaGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands.
Giovanni MagliaGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 7, 9747 AG Groningen, The Netherlands g.maglia@rug.nl.ORCID http://orcid.org/0000-0003-2784-0811

Funding

European Research Council 260884
6 · The paper itself

Abstract

Biological nanopores are a class of membrane proteins that open nanoscale water conduits in biological membranes. When they are reconstituted in artificial membranes and a bias voltage is applied across the membrane, the ionic current passing through individual nanopores can be used to monitor chemical reactions, to recognize individual molecules and, of most interest, to sequence DNA. In addition, a more recent nanopore application is the analysis of single proteins and enzymes. Monitoring enzymatic reactions with nanopores, i.e. nanopore enzymology, has the unique advantage that it allows long-timescale observations of native proteins at the single-molecule level. Here, we describe the approaches and challenges in nanopore enzymology.This article is part of the themed issue 'Membrane pores: from structure and assembly, to medicine and technology'.

Indexed as

NanoporesNanotechnologyBiosensing TechniquesEnzymesMembranes, ArtificialProteinsSequence Analysis, DNASingle Molecule ImagingEnzymesMembranes, ArtificialProteinsnanopore enzymologyprotein trappingreviewsingle-molecule

Identifiers

PMID28630164
PMCPMC5483527

What OpenQuestion holds

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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.