Evidence map›Paper›PMID 33578201›Full record

ArticleCell calcium2021

α-Synuclein emerges as a potent regulator of VDAC-facilitated calcium transport.

William M Rosencrans, Vicente M Aguilella, Tatiana K Rostovtseva, Sergey M Bezrukov

Open access · greenAbstract read
In one paragraph

Article in Cell calcium, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.1field-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

38 citing papers in PubMed, 54 citations in OpenAlex.

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  9. Mechano-energetic uncoupling in heart failure.Nature reviews. Cardiology · 2025
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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 2 institutions in 2 countries.

William M RosencransSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA.
Vicente M AguilellaLaboratory of Molecular Biophysics, Department of Physics, Universitat Jaume I, Av. Vicent Sos Baynat s/n 12071, Castellón, Spain.
Tatiana K RostovtsevaSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA. Electronic address: rostovtt@mail.nih.gov.
Sergey M BezrukovSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, 20892, USA.
National Institutes of Health · USUniversitat Jaume I · ES

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) is the most ubiquitous channel at the mitochondrial outer membrane, and is believed to be the pathway for calcium entering or leaving the mitochondria. Therefore, understanding the molecular mechanisms of how VDAC regulates calcium influx and efflux from the mitochondria is of particular interest for mitochondrial physiology. When the Parkinson's disease (PD) related neuronal protein, alpha-synuclein (αSyn), is added to the reconstituted VDAC, it reversibly and partially blocks VDAC conductance by its acidic C-terminal tail. Using single-molecule VDAC electrophysiology of reconstituted VDAC we now demonstrate that, at CaCl

Indexed as

alpha-SynucleinAnimalsCalciumHumansMiceMitochondrial Membrane Transport ProteinsRecombinant ProteinsVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2Voltage-Dependent Anion Channelsalpha-SynucleinCalciumMitochondrial Membrane Transport ProteinsRecombinant ProteinsSnca protein, mouseVdac1 protein, mouseVDAC2 protein, humanVDAC3 protein, humanVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2Voltage-Dependent Anion ChannelsCalcium signalingCharge inversionIntrinsically disordered proteinsIon selectivity, beta-barrel channelsSingle-molecule measurementVoltage-dependent anion channel

Identifiers

PMID33578201
PMCPMC7994190
OpenAlexW3126624608

What OpenQuestion holds

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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.