Evidence map›Paper›PMID 19801635›Full record

ArticleThe Journal of biological chemistry2009

Cyclophilin D modulates mitochondrial F0F1-ATP synthase by interacting with the lateral stalk of the complex.

Valentina Giorgio, Elena Bisetto, Maria Eugenia Soriano, Federica Dabbeni-Sala, Emy Basso, Valeria Petronilli, Michael A Forte, Paolo Bernardi, Giovanna Lippe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 173 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
173citing papers in PubMed, 2 pooled it
3.8field-weighted citation impact, top 6% 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

173 citing papers in PubMed, 2 syntheses or guidelines pooled it, 297 citations in OpenAlex.

  1. Pooled it
  2. FMolecular biology reports · 2023
    Pooled it
  3. Trial
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  5. Review
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  15. Mitochondrial DNA signals driving immune responses: Why, How, Where?Cell communication and signaling : CCS · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

113 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 3 institutions in 2 countries.

Valentina GiorgioDepartment of Biomedical Sciences and the Consiglio Nazionale delle Ricerche Institute of Neuroscience, University of Padova, I-35121 Padova, Italy.
Elena Bisetto
Maria Eugenia Soriano
Federica Dabbeni-Sala
Emy Basso
Valeria Petronilli
Michael A Forte
Paolo Bernardi
Giovanna Lippe
University of Udine · ITUniversity of Padua · ITVollum Institute · US

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 GM69883NIGMS NIH HHS R01 GM069883
6 · The paper itself

Abstract

Blue native gel electrophoresis purification and immunoprecipitation of F(0)F(1)-ATP synthase from bovine heart mitochondria revealed that cyclophilin (CyP) D associates to the complex. Treatment of intact mitochondria with the membrane-permeable bifunctional reagent dimethyl 3,3-dithiobis-propionimidate (DTBP) cross-linked CyPD with the lateral stalk of ATP synthase, whereas no interactions with F(1) sector subunits, the ATP synthase natural inhibitor protein IF1, and the ATP/ADP carrier were observed. The ATP synthase-CyPD interactions have functional consequences on enzyme catalysis and are modulated by phosphate (increased CyPD binding and decreased enzyme activity) and cyclosporin (Cs) A (decreased CyPD binding and increased enzyme activity). Treatment of MgATP submitochondrial particles or intact mitochondria with CsA displaced CyPD from membranes and activated both hydrolysis and synthesis of ATP sustained by the enzyme. No effect of CsA was detected in CyPD-null mitochondria, which displayed a higher specific activity of the ATP synthase than wild-type mitochondria. Modulation by CyPD binding appears to be independent of IF1, whose association to ATP synthase was not affected by CsA treatment. These findings demonstrate that CyPD association to the lateral stalk of ATP synthase modulates the activity of the complex.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesCattleCyclohexanesCyclophilinsHeartImmunoprecipitationMiceMitochondria, HeartMitochondria, LiverMitochondrial Proton-Translocating ATPasesModels, BiologicalPeptidyl-Prolyl Isomerase FProtein BindingAdenosine TriphosphatasesAdenosine TriphosphateCyclohexanesCyclophilinsdi-tert-butylperoxy-3,3,5-trimethylcyclohexane peroxideMitochondrial Proton-Translocating ATPasesPeptidyl-Prolyl Isomerase FPPIF protein, mouse

Identifiers

PMID19801635
PMCPMC2797168
OpenAlexW2066200217

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.