Evidence map›Paper›PMID 34376679›Full record

ArticleNature communications2021

Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase.

Andrea Carrer, Ludovica Tommasin, Justina Šileikytė, Francesco Ciscato, Riccardo Filadi, Andrea Urbani, Michael Forte, Andrea Rasola, Ildikò Szabò, Michela Carraro and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 83 citations in OpenAlex.

  1. ATP synthase subunits e and g are essential for CaCell death and differentiation · 2026
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. CypD Dependent mPTP Opening Is Crucial for Oxidized Mitochondrial DNA Release in Ferroptosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  8. Article
  9. The Ly6gCancer communications (London, England) · 2026
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Tissue-specific differences in CaPhysiological reports · 2024
    Article
  17. Review
  18. Review
  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
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

11 authors at 2 institutions in 2 countries.

Andrea CarrerDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Ludovica TommasinDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Justina ŠileikytėVollum Institute, Oregon Health and Science University, Portland, OR, USA.
Francesco CiscatoDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Riccardo FiladiDepartment of Biomedical Sciences, University of Padova, Padova, Italy.
Andrea UrbaniDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0002-3935-6907
Michael ForteVollum Institute, Oregon Health and Science University, Portland, OR, USA.
Andrea RasolaDepartment of Biomedical Sciences, University of Padova, Padova, Italy.ORCID 0000-0003-4522-3008
Ildikò SzabòConsiglio Nazionale delle Ricerche Neuroscience Institute, Padova, Italy.
Michela CarraroDepartment of Biomedical Sciences, University of Padova, Padova, Italy. carraro.miche@gmail.com.
Paolo BernardiDepartment of Biomedical Sciences, University of Padova, Padova, Italy. bernardi@bio.unipd.it.ORCID 0000-0001-9187-3736
University of Padua · ITOregon Health & Science University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

F-ATP synthase is a leading candidate as the mitochondrial permeability transition pore (PTP) but the mechanism(s) leading to channel formation remain undefined. Here, to shed light on the structural requirements for PTP formation, we test cells ablated for g, OSCP and b subunits, and ρ

Indexed as

CalciumCarbonyl Cyanide p-TrifluoromethoxyphenylhydrazoneCell Line, TumorHeLa CellsHumansMembrane Potential, MitochondrialMitochondriaMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesProtein SubunitsProton IonophoresCalciumCarbonyl Cyanide p-TrifluoromethoxyphenylhydrazoneMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesProtein SubunitsProton Ionophores

Identifiers

PMID34376679
PMCPMC8355262
OpenAlexW3187734245

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.