Evidence map›Paper›PMID 24627492›Full record

ArticleThe Journal of biological chemistry2014

High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

Johann Schredelseker, Aviv Paz, Carlos J López, Christian Altenbach, Calvin S Leung, Maria K Drexler, Jau-Nian Chen, Wayne L Hubbell, Jeff Abramson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
19.9field-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

86 citing papers in PubMed, 147 citations in OpenAlex.

  1. Article
  2. Review
  3. Membrane protein structure and dynamics probed by MicroED.Biochemical Society transactions · 2026
    Review
  4. VDAC2: an emerging pivotal and multifaceted regulator in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
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  20. Mechanisms of BCL-2 family proteins in mitochondrial apoptosis.Nature reviews. Molecular cell biology · 2023
    Review

26 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

9 authors at 3 institutions in 3 countries.

Johann SchredelsekerFrom the Department of Molecular, Cell and Developmental Biology.
Aviv Paz
Carlos J López
Christian Altenbach
Calvin S Leung
Maria K Drexler
Jau-Nian Chen
Wayne L Hubbell
Jeff Abramson
Ludwig-Maximilians-Universität München · DEDoheny Eye Institute · USTata Institute of Fundamental Research · IN

Funding

Vision Research Core at UCLAP30EY000331 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Gregory Darin Field, DAVID S WILLIAMS · 1985 to 2026
$16.8M
TR&D Project 3P41EB001980 · NIBIB · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2003 to 2017
$16.3M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
Vision Science Training ProgramT32EY007026 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Alapakkam P Sampath · 1985 to 2026
$5.7M
Structures of sodium glucose transporters by cryo electron microscopyR01GM078844 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2006 to 2018
$5.3M
Elucidating the molecular mechanisms regulating embryonic cardiac rhythmicityR01HL096980 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHEN, JAU-NIAN · 2010 to 2013
$1.5M
NEI NIH HHS 2T32EY007026-36A1NEI NIH HHS 5R01 EY005216NEI NIH HHS P30 EY000331NEI NIH HHS R01 EY005216NEI NIH HHS T32 EY007026NHLBI NIH HHS R01 HL096980NIBIB NIH HHS P41 EB001980NIGMS NIH HHS R01 GM078844
6 · The paper itself

Abstract

In recent years, there has been a vast increase in structural and functional understanding of VDAC1, but VDAC2 and -3 have been understudied despite having many unique phenotypes. One reason for the paucity of structural and biochemical characterization of the VDAC2 and -3 isoforms stems from the inability of obtaining purified, functional protein. Here we demonstrate the expression, isolation, and basic characterization of zebrafish VDAC2 (zfVDAC2). Further, we resolved the structure of zfVDAC2 at 2.8 Å resolution, revealing a crystallographic dimer. The dimer orientation was confirmed in solution by double electron-electron resonance spectroscopy and by cross-linking experiments disclosing a dimer population of ∼20% in lauryldimethine amine oxide detergent micelles, whereas in lipidic bicelles a higher population of dimeric and higher order oligomers species were observed. The present study allows for a more accurate structural comparison between VDAC2 and its better-studied counterpart VDAC1.

Indexed as

Protein MultimerizationAmino Acid SequenceAnimalsCrystallography, X-RayCysteineElectric ConductivityElectron Spin Resonance SpectroscopyElectrophoresis, Polyacrylamide GelLipid BilayersModels, MolecularMolecular Sequence DataMutationProtein ConformationProtein Structure, SecondarySequence Homology, Amino AcidStatic ElectricityCysteineLipid BilayersVoltage-Dependent Anion Channel 2Zebrafish ProteinsBiophysicsDEERIon ChannelsMitochondriaVDAC2X-ray CrystallographyZebrafish

Identifiers

PMID24627492
PMCPMC4007448
OpenAlexW1984785146

What OpenQuestion holds

Textmetadata
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.