Evidence map›Paper›PMID 24786291›Full record

ArticleInternational journal of molecular sciences2014

The oligomycin-sensitivity conferring protein of mitochondrial ATP synthase: emerging new roles in mitochondrial pathophysiology.

Manuela Antoniel, Valentina Giorgio, Federico Fogolari, Gary D Glick, Paolo Bernardi, Giovanna Lippe

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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 3 institutions in 2 countries.

Manuela AntonielDepartment of Biomedical Sciences, University of Padova, via Ugo Bassi 58/B, 35121 Padua, Italy. manuela.antoniel@studenti.unipd.it.
Valentina GiorgioDepartment of Biomedical Sciences, University of Padova, via Ugo Bassi 58/B, 35121 Padua, Italy. vgiorgio@bio.unipd.it.
Federico FogolariDepartment of Biomedical Sciences, University of Udine, p.le Kolbe, 33100 Udine, Italy. federico.fogolari@uniud.it.
Gary D GlickDepartment of Chemistry, Graduate Program in Immunology, University of Michigan, Ann Arbor, MI 48109, USA. gglick@umich.edu.
Paolo BernardiDepartment of Biomedical Sciences, University of Padova, via Ugo Bassi 58/B, 35121 Padua, Italy. bernardi@bio.unipd.it.
Giovanna LippeDepartment of Food Science, University of Udine, via Sondrio 2/A, 33100 Udine, Italy. Giovanna.lippe@uniud.it.
University of Udine · ITUniversity of Padua · ITUniversity of Michigan · US

Funding

Telethon GGP11082
6 · The paper itself

Abstract

The oligomycin-sensitivity conferring protein (OSCP) of the mitochondrial F(O)F1 ATP synthase has long been recognized to be essential for the coupling of proton transport to ATP synthesis. Located on top of the catalytic F1 sector, it makes stable contacts with both F1 and the peripheral stalk, ensuring the structural and functional coupling between F(O) and F1, which is disrupted by the antibiotic, oligomycin. Recent data have established that OSCP is the binding target of cyclophilin (CyP) D, a well-characterized inducer of the mitochondrial permeability transition pore (PTP), whose opening can precipitate cell death. CyPD binding affects ATP synthase activity, and most importantly, it decreases the threshold matrix Ca²⁺ required for PTP opening, in striking analogy with benzodiazepine 423, an apoptosis-inducing agent that also binds OSCP. These findings are consistent with the demonstration that dimers of ATP synthase generate Ca²⁺-dependent currents with features indistinguishable from those of the PTP and suggest that ATP synthase is directly involved in PTP formation, although the underlying mechanism remains to be established. In this scenario, OSCP appears to play a fundamental role, sensing the signal(s) that switches the enzyme of life in a channel able to precipitate cell death.

Indexed as

Adenosine TriphosphatasesAnimalsCarrier ProteinsCyclophilinsHumansMembrane ProteinsMitochondriaMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesModels, MolecularPeptidyl-Prolyl Isomerase FProtein ConformationProtein Processing, Post-TranslationalAdenosine TriphosphatasesCarrier ProteinsCyclophilinsMembrane ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesoligomycin sensitivity-conferring proteinPeptidyl-Prolyl Isomerase F

Identifiers

PMID24786291
PMCPMC4057687
OpenAlexW2060002926

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.