Evidence map›Paper›PMID 33168734›Full record

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

Assembly of the peripheral stalk of ATP synthase in human mitochondria.

Jiuya He, Joe Carroll, Shujing Ding, Ian M Fearnley, Martin G Montgomery, John E Walker

Abstract 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 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Cooperative Architecture of Mitochondrial Proteome Homeostasis.medRxiv : the preprint server for health sciences · 2026
    Article
  7. Article
  8. Article
  9. Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. The mitochondrial ATP synthase is a negative regulator of the mitochondrial permeability transition pore.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  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

6 authors.

Jiuya HeMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom.ORCID 0000-0002-8602-1202
Joe CarrollMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom.
Shujing DingMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom.
Ian M FearnleyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom.
Martin G MontgomeryMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom.ORCID 0000-0001-6142-9423
John E WalkerMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, CB2 0XY Cambridge, United Kingdom john.walker@mrc-mbu.cam.ac.uk.ORCID 0000-0001-7929-2162

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 adenosine triphosphate (ATP) synthase in human mitochondria is a membrane bound assembly of 29 proteins of 18 kinds organized into F

Indexed as

Adenosine TriphosphateCell LineHEK293 CellsHumansMitochondriaMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesProtein SubunitsProton-Translocating ATPasesAdenosine TriphosphateMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesProtein SubunitsProton-Translocating ATPasesassemblyATP synthasehuman mitochondriaperipheral stalk

Identifiers

PMID33168734
PMCPMC7703580

What OpenQuestion holds

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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.