Evidence map›Paper›PMID 26697057›Full record

ReviewFrontiers in plant science2015

The Permeability Transition in Plant Mitochondria: The Missing Link.

Marco Zancani, Valentino Casolo, Elisa Petrussa, Carlo Peresson, Sonia Patui, Alberto Bertolini, Valentina De Col, Enrico Braidot, Francesco Boscutti, Angelo Vianello

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

12 citing papers in PubMed, 34 citations in OpenAlex.

  1. Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024
    Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Plant Mitochondrial Inner Membrane Protein Insertion.International journal of molecular sciences · 2018
    Review
  11. Article
  12. 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

10 authors at 1 institution in 1 country.

Marco ZancaniPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Valentino CasoloPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Elisa PetrussaPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Carlo PeressonPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Sonia PatuiPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Alberto BertoliniPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Valentina De ColPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Enrico BraidotPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Francesco BoscuttiPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
Angelo VianelloPlant Biology Unit, Department of Agricultural and Environmental Sciences, University of Udine Udine, Italy.
University of Udine · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of ATP in mitochondria is dependent on a low permeability of the inner membrane. Nevertheless, mitochondria can undergo an increased permeability to solutes, named permeability transition (PT) that is mediated by a permeability transition pore (PTP). PTP opening requires matrix Ca(2+) and leads to mitochondrial swelling and release of intramembrane space proteins (e.g., cytochrome c). This feature has been initially observed in mammalian mitochondria and tentatively attributed to some components present either in the outer or inner membrane. Recent works on mammalian mitochondria point to mitochondrial ATP synthase dimers as physical basis for PT, a finding that has been substantiated in yeast and Drosophila mitochondria. In plant mitochondria, swelling and release of proteins have been linked to programmed cell death, but in isolated mitochondria PT has been observed in only a few cases and in plant cell cultures only indirect evidence is available. The possibility that mitochondrial ATP synthase dimers could function as PTP also in plants is discussed here on the basis of the current evidence. Finally, a hypothetical explanation for the origin of PTP is provided in the framework of molecular exaptation.

Indexed as

ATP synthaseenvironmental stressexaptationpermeability transitionplant mitochondria

Identifiers

PMID26697057
PMCPMC4678196
OpenAlexW2235622324

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.