Evidence map›Paper›PMID 37972066›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Tunable force transduction through the

Daniel P Williams-Jones, Melissa N Webby, Cara E Press, Jan M Gradon, Sophie R Armstrong, Joanna Szczepaniak, Colin Kleanthous

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
6.9field-weighted citation impact, top 3% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Review
  15. Article
  16. Tunable force transduction through theProceedings of the National Academy of Sciences of the United States of America · 2023
    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 at 1 institution in 1 country.

Daniel P Williams-Jones *Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0001-5026-5726
Melissa N Webby *Department of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0001-5721-0381
Cara E PressDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Jan M GradonDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0009-0006-5043-1986
Sophie R ArmstrongDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Joanna SzczepaniakDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0003-2441-6310
Colin KleanthousDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.ORCID 0000-0002-3273-0302
University of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria is not energised and so processes requiring a driving force must connect to energy-transduction systems in the inner membrane (IM). Tol (Tol-Pal) and Ton are related, proton motive force- (PMF-) coupled assemblies that stabilise the OM and import essential nutrients, respectively. Both rely on proton-harvesting IM motor (stator) complexes, which are homologues of the flagellar stator unit Mot, to transduce force to the OM through elongated IM force transducer proteins, TolA and TonB, respectively. How PMF-driven motors in the IM generate mechanical work at the OM via force transducers is unknown. Here, using cryoelectron microscopy, we report the 4.3Å structure of the

Indexed as

Escherichia coliEscherichia coli ProteinsCell MembraneCryoelectron MicroscopyMembrane ProteinsEscherichia coli ProteinsMembrane Proteinscell envelopeforce transductiongram-negative bacteriaouter membrane

Identifiers

PMID37972066
PMCPMC10666116
OpenAlexW4388728287

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.