Evidence map›Paper›PMID 24790105›Full record

ArticleThe Journal of biological chemistry2014

Channel formation by yeast F-ATP synthase and the role of dimerization in the mitochondrial permeability transition.

Michela Carraro, Valentina Giorgio, Justina Šileikytė, Geppo Sartori, Michael Forte, Giovanna Lippe, Mario Zoratti, Ildikò Szabò, Paolo Bernardi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
10.4field-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

93 citing papers in PubMed, 153 citations in OpenAlex.

  1. ATP synthase subunits e and g are essential for CaCell death and differentiation · 2026
    Article
  2. Review
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  4. 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
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  9. Review
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  11. 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
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  13. Review
  14. Review
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  16. Article
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  20. Review

33 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

9 authors at 2 institutions in 1 country.

Michela CarraroFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Valentina GiorgioFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Justina ŠileikytėFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Geppo SartoriFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Michael Fortethe Vollum Institute, Oregon Health and Sciences University, Portland, Oregon 97239-3098, and.
Giovanna Lippethe Department of Food Science, University of Udine, 33100 Udine, Italy.
Mario ZorattiFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and.
Ildikò Szabòthe Department of Biology, University of Padova, I-35121 Padova, Italy.
Paolo BernardiFrom the Consiglio Nazionale delle Ricerche Neuroscience Institute and Department of Biomedical Sciences and bernardi@bio.unipd.it.
University of Padua · ITNeuroscience Institute · IT

Funding

Molecular Structure and Regulation of the Permeability Transition PoreR01GM069883 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI FORTE, MICHAEL A · 2004 to 2016
$3.3M
NIGMS NIH HHS 1R01GM069883NIGMS NIH HHS R01 GM069883
6 · The paper itself

Abstract

Purified F-ATP synthase dimers of yeast mitochondria display Ca(2+)-dependent channel activity with properties resembling those of the permeability transition pore (PTP) of mammals. After treatment with the Ca(2+) ionophore ETH129, which allows electrophoretic Ca(2+) uptake, isolated yeast mitochondria undergo inner membrane permeabilization due to PTP opening. Yeast mutant strains ΔTIM11 and ΔATP20 (lacking the e and g F-ATP synthase subunits, respectively, which are necessary for dimer formation) display a striking resistance to PTP opening. These results show that the yeast PTP originates from F-ATP synthase and indicate that dimerization is required for pore formation in situ.

Indexed as

Blotting, WesternDimerizationElectrophoresis, Polyacrylamide GelMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesSaccharomyces cerevisiaeMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesCalciumF1FO-ATPaseIon ChannelMitochondriaMitochondrial Permeability Transition (MPT)Oxidative StressYeast

Identifiers

PMID24790105
PMCPMC4047373
OpenAlexW2092514471

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.