Evidence map›Paper›PMID 23675351›Full record

ArticleFrontiers in physiology2013

The mitochondrial permeability transition pore: a mystery solved?

Paolo Bernardi

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 165 papers.

0numbers the graph read from it
0cells of the map it votes in
165citing papers in PubMed
24.7field-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

165 citing papers in PubMed, 329 citations in OpenAlex.

  1. Review
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105 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

1 author at 1 institution in 1 country.

Paolo BernardiDepartment of Biomedical Sciences, University of Padova Padova, Italy.
Neuroscience 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
Small Molecules Targeting the Mitochondrial Permeability TransitionR03DA033978 · NIDA · OREGON HEALTH & SCIENCE UNIVERSITY · PI BOURDETTE, DENNIS NEIL, FORTE, MICHAEL A · 2012 to 2013
$62k
NIDA NIH HHS R03 DA033978NIGMS NIH HHS R01 GM069883Telethon GGP11082
6 · The paper itself

Abstract

The permeability transition (PT) denotes an increase of the mitochondrial inner membrane permeability to solutes with molecular masses up to about 1500 Da. It is presumed to be mediated by opening of a channel, the permeability transition pore (PTP), whose molecular nature remains a mystery. Here I briefly review the history of the PTP, discuss existing models, and present our new results indicating that reconstituted dimers of the FOF1 ATP synthase form a channel with properties identical to those of the mitochondrial megachannel (MMC), the electrophysiological equivalent of the PTP. Open questions remain, but there is now promise that the PTP can be studied by genetic methods to solve the large number of outstanding problems.

Indexed as

calciumFOF1 ATP synthasemitochondriapermeability transition

Identifiers

PMID23675351
PMCPMC3650560
OpenAlexW2030618370

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.