Evidence map›Paper›PMID 34084351›Full record

ArticleChemical science2019

Single-molecule nanopore sensing of actin dynamics and drug binding.

Xiaoyi Wang, Mark D Wilkinson, Xiaoyan Lin, Ren Ren, Keith R Willison, Aleksandar P Ivanov, Jake Baum, Joshua B Edel

Erratum issuedAbstract read
In one paragraph

Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Nanopore Detection Using Supercharged Polypeptide Molecular Carriers.Journal of the American Chemical Society · 2023
    Article
  8. Article
  9. Single-Molecule Binding Assay Using Nanopores and Dimeric NP Conjugates.Advanced materials (Deerfield Beach, Fla.) · 2021
    Article
  10. Article
  11. The Diagnostic Potential of Amyloidogenic Proteins.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Xiaoyi WangDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0002-8346-0808
Mark D WilkinsonDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0003-1109-3727
Xiaoyan LinDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0002-0188-5387
Ren RenDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0001-8288-8012
Keith R WillisonDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0002-1353-1471
Aleksandar P IvanovDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0003-1419-1381
Jake BaumDepartment of Life Sciences, Imperial College London Sir Alexander Fleming Building, Exhibition Road, South Kensington London SW7 2AZ UK jake.baum@imperial.ac.uk.ORCID https://orcid.org/0000-0002-0275-352X
Joshua B EdelDepartment of Chemistry, Imperial College London, Molecular Sciences Research Hub White City Campus, 80 Wood Lane W12 0BZ UK joshua.edel@imperial.ac.uk.ORCID https://orcid.org/0000-0001-5870-8659

Funding

Wellcome Trust
6 · The paper itself

Abstract

Actin is a key protein in the dynamic processes within the eukaryotic cell. To date, methods exploring the molecular state of actin are limited to insights gained from structural approaches, providing a snapshot of protein folding, or methods that require chemical modifications compromising actin monomer thermostability. Nanopore sensing permits label-free investigation of native proteins and is ideally suited to study proteins such as actin that require specialised buffers and cofactors. Using nanopores, we determined the state of actin at the macromolecular level (filamentous or globular) and in its monomeric form bound to inhibitors. We revealed urea-dependent and voltage-dependent transitional states and observed the unfolding process within which sub-populations of transient actin oligomers are visible. We detected, in real-time, filament-growth, and drug-binding at the single-molecule level demonstrating the promise of nanopore sensing for in-depth understanding of protein folding landscapes and for drug discovery.

Identifiers

PMID34084351
PMCPMC8146688

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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.