Evidence map›Paper›PMID 29210357›Full record

ArticleeLife2017

Structural basis of proton translocation and force generation in mitochondrial ATP synthase.

Niklas Klusch, Bonnie J Murphy, Deryck J Mills, Özkan Yildiz, Werner Kühlbrandt

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

38 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Electric Forces and ATP Synthesis.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  5. Article
  6. Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  10. Determinants of Directionality and Efficiency of the ATP Synthase FThe journal of physical chemistry letters · 2022
    Article
  11. Review
  12. Rotational Mechanism of FFrontiers in microbiology · 2022
    Review
  13. Review
  14. ATP Synthase KFunction (Oxford, England) · 2022
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

5 authors at 1 institution in 1 country.

Niklas Klusch *Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Bonnie J Murphy *Department of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0001-6341-9368
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.
Özkan YildizDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0003-3659-2805
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID http://orcid.org/0000-0002-2013-4810
Max Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP synthases produce ATP by rotary catalysis, powered by the electrochemical proton gradient across the membrane. Understanding this fundamental process requires an atomic model of the proton pathway. We determined the structure of an intact mitochondrial ATP synthase dimer by electron cryo-microscopy at near-atomic resolution. Charged and polar residues of the

Indexed as

Proton-Motive ForceCryoelectron MicroscopyMitochondrial Proton-Translocating ATPasesModels, MolecularProtein ConformationProtein MultimerizationVolvocidaMitochondrial Proton-Translocating ATPasesATP synthasebiochemistrybiophysicselectron cryo-microscopyenergy conversionmembrane potentialmembrane protein structuremitochondriastructural biology

Identifiers

PMID29210357
PMCPMC5747523
OpenAlexW2772989510

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.