Evidence map›Paper›PMID 25399320›Full record

ArticleJournal of biomolecular NMR2015

Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.

Zrinka Gattin, Robert Schneider, Yvonne Laukat, Karin Giller, Elke Maier, Markus Zweckstetter, Christian Griesinger, Roland Benz, Stefan Becker, Adam Lange

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Pharmacological modulation of mitochondrial ion channels.British journal of pharmacology · 2019
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016
    Review
  13. Review
  14. Article
  15. Article
  16. Motifs of VDAC2 required for mitochondrial Bak import and tBid-induced apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. NMR studies of membrane proteins.Journal of biomolecular NMR · 2015
    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

10 authors at 5 institutions in 2 countries.

Zrinka GattinMax Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Robert Schneider
Yvonne Laukat
Karin Giller
Elke Maier
Markus Zweckstetter
Christian Griesinger
Roland Benz
Stefan Becker
Adam Lange
Max Planck Institute for Biophysical Chemistry · DEConstructor University · DEGerman Center for Neurodegenerative Diseases · DELeibniz-Forschungsinstitut für Molekulare Pharmakologie · DEUniversity of Würzburg · DE

Funding

European Research Council 282008
6 · The paper itself

Abstract

The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles.

Indexed as

Amino Acid SequenceElectrophysiological PhenomenaHumansLipid BilayersMitochondriaMolecular ConformationMolecular Dynamics SimulationMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein IsoformsSequence AlignmentVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2Lipid BilayersProtein IsoformsVDAC1 protein, humanVDAC2 protein, humanVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2

Identifiers

PMID25399320
PMCPMC5653203
OpenAlexW2130713922

What OpenQuestion holds

Textmetadata
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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.