Evidence map›Paper›PMID 29440398›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Assembly of the membrane domain of ATP synthase in human mitochondria.

Jiuya He, Holly C Ford, Joe Carroll, Corsten Douglas, Evvia Gonzales, Shujing Ding, Ian M Fearnley, John E Walker

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
106citing papers in PubMed, 2 pooled it
9.6field-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

106 citing papers in PubMed, 2 syntheses or guidelines pooled it, 198 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  12. Cooperative Architecture of Mitochondrial Proteome Homeostasis.medRxiv : the preprint server for health sciences · 2026
    Article
  13. Article
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  15. Dystonia: Insights into Mechanisms and Novel Therapeutics.Current neurology and neuroscience reports · 2026
    Review
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  17. Article
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Jiuya HeMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Holly C FordMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Joe CarrollMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Corsten DouglasMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Evvia GonzalesMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Shujing DingMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Ian M FearnleyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
John E WalkerMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge Biomedical Campus, 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_U105663150Medical Research Council MC_UU_00015/7Medical Research Council MC_UU_00015/8
6 · The paper itself

Abstract

The ATP synthase in human mitochondria is a membrane-bound assembly of 29 proteins of 18 kinds. All but two membrane components are encoded in nuclear genes, synthesized on cytoplasmic ribosomes, and imported into the matrix of the organelle, where they are assembled into the complex with ATP6 and ATP8, the products of overlapping genes in mitochondrial DNA. Disruption of individual human genes for the nuclear-encoded subunits in the membrane portion of the enzyme leads to the formation of intermediate vestigial ATPase complexes that provide a description of the pathway of assembly of the membrane domain. The key intermediate complex consists of the F

Indexed as

Cell LineCell ProliferationCRISPR-Cas SystemsGene Expression Regulation, EnzymologicHumansMitochondrial MembranesMitochondrial Proton-Translocating ATPasesModels, MolecularMutationOxygen ConsumptionProtein ConformationProtein SubunitsMitochondrial Proton-Translocating ATPasesProtein SubunitsassemblyATP synthasehuman mitochondriamembrane subunits

Identifiers

PMID29440398
PMCPMC5866602
OpenAlexW2792218846

What OpenQuestion holds

Textmetadata
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.