Evidence map›Paper›PMID 31936081›Full record

ReviewInternational journal of molecular sciences2020

Structure and Stoichiometry of the Ton Molecular Motor.

Herve Celia, Nicholas Noinaj, Susan K Buchanan

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.1field-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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Structure and Function of Membrane Proteins.International journal of molecular sciences · 2023
    Article
  13. Article
  14. HDX-MS performed on BtuB inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. The Ton Motor.Frontiers in microbiology · 2022
    Review
  17. Article
  18. Article
  19. Article
  20. Ton motor complexes.Current opinion in structural biology · 2021
    Review
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

3 authors at 2 institutions in 1 country.

Herve CeliaNational Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
Nicholas NoinajMarkey Center for Structural Biology, Department of Biological Sciences, and the Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USA.
Susan K BuchananNational Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
National Institute of Diabetes and Digestive and Kidney Diseases · USPurdue University West Lafayette · US

Funding

Structural characterization of outer membrane proteins from Yersinia pestisZIADK011011 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2025
$19.1M
Neisseria gonorrhoeae metal transporters that subvert nutritional immunityR01AI127793 · NIAID · VIRGINIA COMMONWEALTH UNIVERSITY · PI CYNTHIA N CORNELISSEN, Alison K Criss · 2017 to 2026
$6.8M
Structural Characterization of the TOC Protein Translocon MachineryR01GM127896 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2018 to 2022
$1.5M
Unraveling the mechanism by which the BAM complex mediates OMP biogenesisR01GM127884 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2019 to 2022
$1.2M
NIAID NIH HHS R01 AI127793NIGMS NIH HHS R01 GM127884NIGMS NIH HHS R01 GM127896NIH HHS ZIA DK011011-12
6 · The paper itself

Abstract

The Ton complex is a molecular motor that uses the proton gradient at the inner membrane of Gram-negative bacteria to generate force and movement, which are transmitted to transporters at the outer membrane, allowing the entry of nutrients into the periplasmic space. Despite decades of investigation and the recent flurry of structures being reported by X-ray crystallography and cryoEM, the mode of action of the Ton molecular motor has remained elusive, and the precise stoichiometry of its subunits is still a matter of debate. This review summarizes the latest findings on the Ton system by presenting the recently reported structures and related reports on the stoichiometry of the fully assembled complex.

Indexed as

Proton-Motive ForceBacterial ProteinsEscherichia coliEscherichia coli ProteinsGram-Negative BacteriaGram-Negative Bacterial InfectionsHumansMembrane ProteinsModels, MolecularProtein MultimerizationBacterial ProteinsEscherichia coli ProteinsExbB protein, E coliexbD protein, E coliMembrane ProteinstonB protein, Bacteriaenergy-transductionExbBExbDGram-negative bacteriamolecular motorsTonBTon complex

Identifiers

PMID31936081
PMCPMC7014051
OpenAlexW2999679406

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.