Evidence map›Paper›PMID 25486353›Full record

ArticleCell cycle (Georgetown, Tex.)2014

Novel insights into the mitochondrial permeability transition.

Massimo Bonora, José Manuel Bravo-San Pedro, Guido Kroemer, Lorenzo Galluzzi, Paolo Pinton

Abstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
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  9. 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

5 authors.

Massimo Bonoraa Section of Pathology , Oncology and Experimental Biology ; Laboratory for Technologies of Advanced Therapies (LTTA); Department of Morphology , Surgery and Experimental Medicine ; University of Ferrara ; Ferrara , Italy.
José Manuel Bravo-San Pedro
Guido Kroemer
Lorenzo Galluzzi
Paolo Pinton

Funding

Telethon GGP11139
6 · The paper itself

Abstract

Alavian and colleagues recently provided further evidence in support of the notion that the c subunit of the mitochondrial F1FO ATP synthase constitutes the long-sought pore-forming unit of the supramolecular complex responsible for the so-called 'mitochondrial permeability transition' (MPT). Besides shedding new light on the molecular mechanisms that underlie the MPT, these findings corroborate the notion that several components of the cell death machinery, including cytochrome c and the F1FO ATP synthase, mediate critical metabolic activities.

Indexed as

AnimalsHumansMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesModels, BiologicalMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreMitochondrial Proton-Translocating ATPasesAIFM1, apoptosis-inducing factor mitochondrion-associated, 1apoptosisATP5G, ATP synthase, H+ transporting, mitochondrial FO complex, subunit CBCL-XLCsA, cyclosporin Acyclophilin Dcyclosporin ACYPD cyclophilin DCYTC holocytochrome cIMM, inner mitochondrial membraneMCU, mitochondrial calcium uniporterMPT, mitochondrial permeability transitionnecrosispermeability transition pore complexPPIF, peptidylprolyl isomerase FPTPC, permeability transition pore complexRCD, regulated cell deathSMV, submitochondrial vesicle.Δψm; mitochondrial transmembrane potential

Identifiers

PMID25486353
PMCPMC4612113

What OpenQuestion holds

Textmetadata
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Registered trials

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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.