Evidence map›Paper›PMID 34281395›Full record

ArticlemBio2021

Chained Structure of Dimeric F

Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Noriyuki Kodera, Tasuku Hamaguchi, Yuhei O Tahara, Toshio Ando, Keiichi Namba, Makoto Miyata

Open access · goldAbstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Dimeric assembly of FScience advances · 2025
    Article
  4. Review
  5. Advances in adhesion-related pathogenesis inFrontiers in microbiology · 2025
    Review
  6. Gliding direction ofBiophysics and physicobiology · 2025
    Article
  7. Internal structure ofBiophysics and physicobiology · 2024
    Article
  8. Reviewing advancement inFrontiers in microbiology · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Detection of Steps and Rotation in the Gliding Motility of Mycoplasma mobile.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. 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

9 authors at 4 institutions in 1 country.

Takuma ToyonagaGraduate School of Science, Osaka City Universitygrid.261445.0, Osaka, Osaka, Japan.
Takayuki KatoInstitute for Protein Research, Osaka Universitygrid.136593.b, Suita, Osaka, Japan.
Akihiro KawamotoInstitute for Protein Research, Osaka Universitygrid.136593.b, Suita, Osaka, Japan.
Noriyuki KoderaNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan.
Tasuku HamaguchiGraduate School of Science, Osaka City Universitygrid.261445.0, Osaka, Osaka, Japan.
Yuhei O TaharaGraduate School of Science, Osaka City Universitygrid.261445.0, Osaka, Osaka, Japan.
Toshio AndoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Ishikawa, Japan.
Keiichi NambaGraduate School of Frontier Biosciences, Osaka Universitygrid.136593.b, Suita, Osaka, Japan.
Makoto MiyataGraduate School of Science, Osaka City Universitygrid.261445.0, Osaka, Osaka, Japan.
Osaka City University · JPKanazawa University · JPProtein Research Foundation · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycoplasma mobile, a fish pathogen, exhibits gliding motility using ATP hydrolysis on solid surfaces, including animal cells. The gliding machinery can be divided into surface and internal structures. The internal structure of the motor is composed of 28 so-called "chains" that are each composed of 17 repeating protein units called "particles." These proteins include homologs of the catalytic α and β subunits of F

Indexed as

Adenosine TriphosphatasesBacterial ProteinsMicroscopy, Atomic ForceMicroscopy, ElectronMovementMycoplasmaProtein ConformationProton-Translocating ATPasesAdenosine TriphosphatasesBacterial ProteinsProton-Translocating ATPasesatomic force microscopybacterial motilityelectron microscopyF1-ATPaseparasitic bacteriarotary motor

Identifiers

PMID34281395
PMCPMC8406192
OpenAlexW3186265826

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.