Evidence map›Paper›PMID 28289229›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Persistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase.

Jiuya He, Holly C Ford, Joe Carroll, 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, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
147citing papers in PubMed, 2 pooled it
16.5field-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

147 citing papers in PubMed, 2 syntheses or guidelines pooled it, 243 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Review
  5. Article
  6. Phenotypic CRISPR screens identify NLRX1 as an essential activator of the human mitochondrial permeability transition.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Cooperative Architecture of Mitochondrial Proteome Homeostasis.medRxiv : the preprint server for health sciences · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Transcriptional Signatures of Aerobic Exercise-Induced Muscle Adaptations in Humans.Journal of functional morphology and kinesiology · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Tissue-specific differences in CaPhysiological reports · 2024
    Article
  18. Article
  19. Article
  20. 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

87 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

6 authors at 1 institution in 1 country.

Jiuya HeThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Holly C FordThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Joe CarrollThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Shujing DingThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
Ian M FearnleyThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom.
John E WalkerThe Medical Research Council Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, United Kingdom walker@mrc-mbu.cam.ac.uk.ORCID 0000-0001-7929-2162
MRC Mitochondrial Biology Unit · GB

Funding

Medical Research Council MC_EX_MR/M009858/1Medical Research Council MC_U105663150Medical Research Council MC_U1065663150Medical Research Council MC_UU_00015/7Medical Research Council MC_UU_00015/8Medical Research Council MR/M009858/1
6 · The paper itself

Abstract

The permeability transition in human mitochondria refers to the opening of a nonspecific channel, known as the permeability transition pore (PTP), in the inner membrane. Opening can be triggered by calcium ions, leading to swelling of the organelle, disruption of the inner membrane, and ATP synthesis, followed by cell death. Recent proposals suggest that the pore is associated with the ATP synthase complex and specifically with the ring of c-subunits that constitute the membrane domain of the enzyme's rotor. The c-subunit is produced from three nuclear genes,

Indexed as

Adenosine TriphosphateBiological TransportHumansIsoenzymesMitochondriaMitochondrial Proton-Translocating ATPasesPermeabilityAdenosine TriphosphateIsoenzymesMitochondrial Proton-Translocating ATPasesATP5GATP synthasehuman mitochondriapermeability transition poresubunit c

Identifiers

PMID28289229
PMCPMC5380099
OpenAlexW2596115537

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.