Evidence map›Paper›PMID 32929284›Full record

ArticleNature structural & molecular biology2020

Cryo-EM structure of the entire mammalian F-type ATP synthase.

Gergely Pinke, Long Zhou, Leonid A Sazanov

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

107 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
  2. Pooled it
  3. Beyond Bioenergetics: Moonlighting Functions of FMedicinal research reviews · 2026
    Review
  4. Article
  5. Article
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  7. ATP synthase subunits e and g are essential for CaCell death and differentiation · 2026
    Article
  8. Review
  9. Review
  10. Article
  11. A planar dimer of bovine ATP synthase.Cell death and differentiation · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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47 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.

Gergely PinkeInstitute of Science and Technology Austria, Klosterneuburg, Austria.
Long ZhouInstitute of Science and Technology Austria, Klosterneuburg, Austria.
Leonid A SazanovInstitute of Science and Technology Austria, Klosterneuburg, Austria. sazanov@ist.ac.at.ORCID http://orcid.org/0000-0002-0977-7989

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine.

Indexed as

Protein MultimerizationAnimalsCryoelectron MicroscopyMitochondrial Proton-Translocating ATPasesModels, MolecularProtein ConformationProtein DomainsProtein SubunitsSheepF1F0-ATP synthaseMitochondrial Proton-Translocating ATPasesProtein Subunits

Identifiers

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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.