Evidence map›Paper›PMID 34782468›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Structure of the ATP synthase from

Martin G Montgomery, Jessica Petri, Tobias E Spikes, John E Walker

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  6. Antibiotics (Basel, Switzerland) · 2024
    Review
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  15. Article
  16. FInternational journal of molecular sciences · 2023
    Review
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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

4 authors at 1 institution in 1 country.

Martin G MontgomeryThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0001-6142-9423
Jessica PetriThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
Tobias E SpikesThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-2432-8006
John E WalkerThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, United Kingdom walker@mrc-mbu.cam.ac.uk.ORCID 0000-0001-7929-2162
University of Cambridge · GB

Funding

Medical Research Council MC_EX_MR/M009858/1Medical Research Council MC_UU_00015/8Medical Research Council MR/M009858/1
6 · The paper itself

Abstract

The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from

Indexed as

Adenosine TriphosphateAnimalsAntitubercular AgentsATPase Inhibitory ProteinBacterial ProteinsCattleCryoelectron MicroscopyHydrolysisMitochondrial Proton-Translocating ATPasesModels, MolecularMycobacterium smegmatisProtein ConformationProteinsProtein SubunitsProton-Motive ForceTuberculosisAdenosine TriphosphateAntitubercular AgentsATPase Inhibitory ProteinBacterial ProteinsMitochondrial Proton-Translocating ATPasesProteinsProtein SubunitsATP synthasemycobacteriaregulationrotary mechanismstructure

Identifiers

PMID34782468
PMCPMC8617483
OpenAlexW3213569025

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.