Evidence map›Paper›PMID 29311594›Full record

ArticleNature communications2018

Cryo EM structure of intact rotary H

Atsuko Nakanishi, Jun-Ichi Kishikawa, Masatada Tamakoshi, Kaoru Mitsuoka, Ken Yokoyama

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Rotary mechanism of the prokaryotic VNature communications · 2024
    Article
  4. Allosteric activation of VCP, an AAA unfoldase, by small molecule mimicry.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Insight into the acid tolerance mechanism ofFrontiers in microbiology · 2023
    Article
  8. Review
  9. Visualizing Intramolecular Dynamics of Membrane Proteins.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Frontiers in microbiology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Essay on Biomembrane Structure.The Journal of membrane biology · 2019
    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

5 authors at 3 institutions in 1 country.

Atsuko NakanishiDepartment of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, 603-8555, Japan.
Jun-Ichi KishikawaDepartment of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, 603-8555, Japan.
Masatada TamakoshiDepartment of Molecular Biology, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo, 192-0392, Japan.
Kaoru MitsuokaResearch Center for Ultra-High Voltage Electron Microscopy, Osaka University, 7-1, Mihogaoka, Ibaraki, Osaka, 567-0047, Japan. kaorum@uhvem.osaka-u.ac.jp.
Ken YokoyamaDepartment of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, 603-8555, Japan. yokoken@cc.kyoto-su.ac.jp.
Kyoto Sangyo University · JPOsaka University · JPTokyo University of Pharmacy and Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proton translocating rotary ATPases couple ATP hydrolysis/synthesis, which occurs in the soluble domain, with proton flow through the membrane domain via a rotation of the common central rotor complex against the surrounding peripheral stator apparatus. Here, we present a large data set of single particle cryo-electron micrograph images of the V/A type H

Indexed as

Adenosine TriphosphateBacterial ProteinsBiological TransportCryoelectron MicroscopyHydrolysisModels, MolecularProtein ConformationProtein SubunitsProtonsRotationThermus thermophilusVacuolar Proton-Translocating ATPasesAdenosine TriphosphateBacterial ProteinsProtein SubunitsProtonsVacuolar Proton-Translocating ATPases

Identifiers

PMID29311594
PMCPMC5758568
OpenAlexW2781603954

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.