Evidence map›Paper›PMID 32900941›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Structure of the dimeric ATP synthase from bovine mitochondria.

Tobias E Spikes, Martin G Montgomery, 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, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed, 1 pooled it
11.1field-weighted citation impact, top 1% 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

133 citing papers in PubMed, 1 synthesis or guideline pooled it, 221 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. ATP synthase subunits e and g are essential for CaCell death and differentiation · 2026
    Article
  4. Article
  5. Article
  6. A planar dimer of bovine ATP synthase.Cell death and differentiation · 2026
    Article
  7. Article
  8. Proteolytic processing of the unique FScientific reports · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Cooperative Architecture of Mitochondrial Proteome Homeostasis.medRxiv : the preprint server for health sciences · 2026
    Article
  13. Structural basis for efficient FBiophysical journal · 2026
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. In situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

73 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Tobias E SpikesThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, United Kingdom.ORCID 0000-0002-2432-8006
Martin G MontgomeryThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, United Kingdom.
John E WalkerThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, University of Cambridge, Cambridge CB2 0XY, United Kingdom john.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_U105663150Medical Research Council MC_UU_00015/8Medical Research Council MR/M009858/1Wellcome TrustWellcome Trust 202905/Z/16/ZWellcome Trust 206171/Z/17/Z
6 · The paper itself

Abstract

The structure of the dimeric ATP synthase from bovine mitochondria determined in three rotational states by electron cryo-microscopy provides evidence that the proton uptake from the mitochondrial matrix via the proton inlet half channel proceeds via a Grotthus mechanism, and a similar mechanism may operate in the exit half channel. The structure has given information about the architecture and mechanical constitution and properties of the peripheral stalk, part of the membrane extrinsic region of the stator, and how the action of the peripheral stalk damps the side-to-side rocking motions that occur in the enzyme complex during the catalytic cycle. It also describes wedge structures in the membrane domains of each monomer, where the skeleton of each wedge is provided by three α-helices in the membrane domains of the b-subunit to which the supernumerary subunits e, f, and g and the membrane domain of subunit A6L are bound. Protein voids in the wedge are filled by three specifically bound cardiolipin molecules and two other phospholipids. The external surfaces of the wedges link the monomeric complexes together into the dimeric structures and provide a pivot to allow the monomer-monomer interfaces to change during catalysis and to accommodate other changes not related directly to catalysis in the monomer-monomer interface that occur in mitochondrial cristae. The structure of the bovine dimer also demonstrates that the structures of dimeric ATP synthases in a tetrameric porcine enzyme have been seriously misinterpreted in the membrane domains.

Indexed as

Mitochondrial Proton-Translocating ATPasesAnimalsCattleMitochondriaMitochondrial MembranesModels, MolecularProtein ConformationProtein SubunitsProtonsTorqueMitochondrial Proton-Translocating ATPasesProtein SubunitsProtonsbovine mitochondriadimeric ATP synthaseGrotthus chainstructuretorque generation

Identifiers

PMID32900941
PMCPMC7519299
OpenAlexW3084135130

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.