Evidence map›Paper›PMID 32454061›Full record

ReviewJournal of molecular and cellular cardiology2020

A 20/20 view of ANT function in mitochondrial biology and necrotic cell death.

Michael J Bround, Donald M Bers, Jeffery D Molkentin

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 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
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  12. Mitochondrial proteomic adaptations to daily torpor in the Djungarian hamster (Phodopus sungorus).Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2025
    Article
  13. Review
  14. Contemporary insights into elamipretide's mitochondrial mechanism of action and therapeutic effects.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2025
    Review
  15. Review
  16. Article
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  18. Targeting CB1R Rewires CaTheranostics · 2025
    Article
  19. Article
  20. Review

1 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

3 authors at 2 institutions in 1 country.

Michael J BroundDepartment of Pediatrics, Cincinnati Children's Hospital Medical Center, University of Cincinnati, Cincinnati, OH 45229, USA.
Donald M BersDepartment of Pharmacology, University of California, Davis, Davis, CA 95616, USA.
Jeffery D MolkentinDepartment of Pediatrics, Cincinnati Children's Hospital Medical Center, University of Cincinnati, Cincinnati, OH 45229, USA; Howard Hughes Medical Institute, Cincinnati Children's Hospital Medical Center, Cincinnati, OH 45229, USA. Electronic address: jeff.molkentin@cchmc.org.
Cincinnati Children's Hospital Medical Center · USUniversity of California, Davis · US

Funding

Molecular examination of mitochondrial calcium controlR01HL132831 · NHLBI · CINCINNATI CHILDRENS HOSP MED CTR · PI BERS, DONALD M, MOLKENTIN, JEFFERY D · 2016 to 2024
$5.9M
IONIC CONTROL OF CARDIAC MUSCLE CONTRACTION: EC COUPLINGR01HL030077 · NHLBI · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI BERS, DONALD M · 1986 to 2018
$3.8M
Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL030077NHLBI NIH HHS R01 HL132831
6 · The paper itself

Abstract

The adenosine nucleotide translocase (ANT) family of proteins are inner mitochondrial membrane proteins involved in energy homeostasis and cell death. The primary function of ANT proteins is to exchange cytosolic ADP with matrix ATP, facilitating the export of newly synthesized ATP to the cell while providing new ADP substrate to the mitochondria. As such, the ANT proteins are central to maintaining energy homeostasis in all eukaryotic cells. Evidence also suggests that the ANTs constitute a pore-forming component of the mitochondrial permeability transition pore (MPTP), a structure that forms in the inner mitochondrial membrane that is thought to underlie regulated necrotic cell death. Additionally, emerging studies suggest that ANT proteins are also critical for mitochondrial uncoupling and for promoting mitophagy. Thus, the ANTs are multifunctional proteins that are poised to participate in several aspects of mitochondrial biology and the greater regulation of cell death, which will be discussed here.

Indexed as

NecroptosisAnimalsGene Expression RegulationHumansMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreModels, BiologicalMultigene FamilyOxidative PhosphorylationMitochondrial ADP, ATP TranslocasesMitochondrial Membrane Transport ProteinsMitochondrial Permeability Transition PoreANTATPHeartMitochondriaNecrotic cell death

Identifiers

PMID32454061
PMCPMC7483807
OpenAlexW3026500698

What OpenQuestion holds

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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.