Evidence map›Paper›PMID 32461058›Full record

ReviewJournal of molecular and cellular cardiology2020

ATP synthase c-subunit ring as the channel of mitochondrial permeability transition: Regulator of metabolism in development and degeneration.

Nelli Mnatsakanyan, Elizabeth Ann Jonas

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
4.7field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 74 citations in OpenAlex.

  1. FMolecular biology reports · 2023
    Pooled it
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  19. A tale of two pathways: Regulation of proteostasis by UPRCurrent opinion in neurobiology · 2023
    Review
  20. 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

2 authors at 1 institution in 1 country.

Nelli MnatsakanyanSection of Endocrinology, Department of Internal Medicine, Yale University, New Haven, CT, USA. Electronic address: nelli.mnatsakanyan@yale.edu.
Elizabeth Ann JonasSection of Endocrinology, Department of Internal Medicine, Yale University, New Haven, CT, USA. Electronic address: elizabeth.jonas@yale.edu.
Yale University · US

Funding

Mitochondrial Ion Channels in Hypoxic NeuronsR37NS045876 · NINDS · YALE UNIVERSITY · PI Elizabeth Ann Jonas · 2014 to 2026
$4.9M
Mitochondrial control of protein translation in Fragile XR01NS112706 · NINDS · YALE UNIVERSITY · PI Elizabeth Ann Jonas, Pawel Licznerski · 2019 to 2026
$3.6M
Mitochondrial ion channels in hypoxic neuronsR01NS045876 · NINDS · YALE UNIVERSITY · PI JONAS, ELIZABETH ANN · 2004 to 2013
$3.3M
Role of DJ1 in mitochondrial biogenergetics and neuronal metabolismR01NS081746 · NINDS · YALE UNIVERSITY · PI JONAS, ELIZABETH ANN · 2014 to 2018
$2.2M
Molecular components of the mitochondrial permeability transition pore and its role in neurodegenerative diseasesK01AG054734 · NIA · YALE UNIVERSITY · PI MNATSAKANYAN, NELLI · 2017 to 2021
$639k
NIA NIH HHS K01 AG054734NINDS NIH HHS R01 NS045876NINDS NIH HHS R01 NS081746NINDS NIH HHS R01 NS112706NINDS NIH HHS R37 NS045876
6 · The paper itself

Abstract

The mitochondrial permeability transition pore (mPTP) or mitochondrial megachannel is arguably one of the most mysterious phenomena in biology today. mPTP has been at the center of ongoing extensive scientific research for the last several decades. In this review we will discuss recent advances in the field that enhance our understanding of the molecular composition of mPTP, its regulatory mechanisms and its pathophysiological role. We will describe our recent findings on the role of ATP synthase c-subunit ring as a central player in mitochondrial permeability transition and as an important metabolic regulator during development and in degenerative diseases.

Indexed as

MitochondriaMitochondrial Proton-Translocating ATPasesProtein SubunitsAnimalsDisease SusceptibilityEnergy MetabolismHumansMitochondrial MembranesModels, MolecularNeuronal PlasticityNeuronsPermeabilityProtein ConformationMitochondrial Proton-Translocating ATPasesProtein SubunitsApoptosisATP synthaseMitochondriaMitochondrial permeability transition pore

Identifiers

PMID32461058
PMCPMC7877492
OpenAlexW3028350492

What OpenQuestion holds

Textmetadata
LicenceTDM
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.