Evidence map›Paper›PMID 31213546›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

Persistence of the permeability transition pore in human mitochondria devoid of an assembled ATP synthase.

Joe Carroll, Jiuya He, 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, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

83 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. 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
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Mitochondria in disease: changes in shapes and dynamics.Trends in biochemical sciences · 2024
    Review
  14. Review
  15. Article
  16. AnPlant signaling & behavior · 2023
    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. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Joe CarrollMedical Research Council Mitochondrial Biology Unit, University of Cambridge, CB2 0XY Cambridge, United Kingdom.
Jiuya HeMedical Research Council Mitochondrial Biology Unit, University of Cambridge, CB2 0XY Cambridge, United Kingdom.
Shujing DingMedical Research Council Mitochondrial Biology Unit, University of Cambridge, CB2 0XY Cambridge, United Kingdom.
Ian M FearnleyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, CB2 0XY Cambridge, United Kingdom.
John E WalkerMedical Research Council Mitochondrial Biology Unit, University of Cambridge, CB2 0XY Cambridge, 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_UU_00015/8
6 · The paper itself

Abstract

The opening of the permeability transition pore, a nonspecific channel in inner mitochondrial membranes, is triggered by an elevated total concentration of calcium ions in the mitochondrial matrix, leading to disruption of the inner membrane and necrotic cell death. Cyclosporin A inhibits pore opening by binding to cyclophilin D, which interacts with the pore. It has been proposed that the pore is associated with the ATP synthase complex. Previously, we confirmed an earlier observation that the pore survives in cells lacking membrane subunits ATP6 and ATP8 of ATP synthase, and in other cells lacking the enzyme's c

Indexed as

Cell LineHumansMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesProtein MultimerizationMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesATP synthasehuman mitochondriapermeability transition

Identifiers

PMID31213546
PMCPMC6601249
OpenAlexW2952677554

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.