Evidence map›Paper›PMID 33529977›Full record

ReviewCell calcium2021

VDAC regulation of mitochondrial calcium flux: From channel biophysics to disease.

William M Rosencrans, Megha Rajendran, Sergey M Bezrukov, Tatiana K Rostovtseva

Open access · greenAbstract readReview
In one paragraph

Review in Cell calcium, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
6.1field-weighted citation impact, top 2% 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

82 citing papers in PubMed, 127 citations in OpenAlex.

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  11. Signaling architecture of the glucagon-like peptide-1 receptor.The Journal of clinical investigation · 2026
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  19. Increased Intermembrane Space [CaCirculation research · 2025
    Article
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22 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

4 authors at 1 institution in 1 country.

William M RosencransSection on Molecular Transport, Eunice Kennedy Shriver. National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, United States.
Megha RajendranSection on Molecular Transport, Eunice Kennedy Shriver. National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, United States.
Sergey M BezrukovSection on Molecular Transport, Eunice Kennedy Shriver. National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, United States.
Tatiana K RostovtsevaSection on Molecular Transport, Eunice Kennedy Shriver. National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, United States. Electronic address: rostovtt@mail.nih.gov.
National Institutes of Health · US

Funding

Biophysics of Large Membrane ChannelsZ01HD000072 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BEZRUKOV, SERGEY M · 2004 to 2008
$1.6M
Intramural NIH HHS Z01 HD000072
6 · The paper itself

Abstract

Voltage-dependent anion channel (VDAC), the most abundant mitochondrial outer membrane protein, is important for a variety of mitochondrial functions including metabolite exchange, calcium transport, and apoptosis. While VDAC's role in shuttling metabolites between the cytosol and mitochondria is well established, there is a growing interest in understanding the mechanisms of its regulation of mitochondrial calcium transport. Here we review the current literature on VDAC's role in calcium signaling, its biophysical properties, physiological function, and pathology focusing on its importance in cardiac diseases. We discuss the specific biophysical properties of the three VDAC isoforms in mammalian cells-VDAC 1, 2, and 3-in relationship to calcium transport and their distinct roles in cell physiology and disease. Highlighting the emerging evidence that cytosolic proteins interact with VDAC and regulate its calcium permeability, we advocate for continued investigation into the VDAC interactome at the contact sites between mitochondria and organelles and its role in mitochondrial calcium transport.

Indexed as

Biophysical PhenomenaCalcium SignalingDiseaseAnimalsCalcium ChannelsHumansMitochondriaVoltage-Dependent Anion ChannelsCalcium ChannelsVoltage-Dependent Anion ChannelsCalcium signalingIon selectivityMitochondrial associated membraneMitochondrial outer membraneProtein-protein interactionVoltage-dependent anion channelVoltage gatingα-synuclein

Identifiers

PMID33529977
PMCPMC7914209
OpenAlexW3122198729

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.