Evidence map›Paper›PMID 33782728›Full record

ReviewEuropean biophysics journal : EBJ2021

Structure, gating and interactions of the voltage-dependent anion channel.

Eszter E Najbauer, Stefan Becker, Karin Giller, Markus Zweckstetter, Adam Lange, Claudia Steinem, Bert L de Groot, Christian Griesinger, Loren B Andreas

Open access · hybridAbstract readReview
In one paragraph

Review in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Review
  3. Novel Drug Targets in Diastolic Heart Disease.International journal of molecular sciences · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Ferroptosis: a potential target for acute lung injury.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Chemical reviews · 2022
    Review
  20. 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

9 authors at 4 institutions in 1 country.

Eszter E NajbauerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Stefan BeckerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Karin GillerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Markus ZweckstetterDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Adam LangeDepartment of Molecular Biophysics, Leibniz-Forschungsinstitut Für Molekulare Pharmakologie, 13125, Berlin, Germany.
Claudia SteinemInstitute of Organic and Biomolecular Chemistry, University of Göttingen, Göttingen, Germany.
Bert L de GrootDepartment of Theoretical and Computational Biophysics, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Christian GriesingerDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.
Loren B AndreasDepartment of NMR-Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany. land@nmr.mpibpc.mpg.de.ORCID http://orcid.org/0000-0003-3216-9065
Max Planck Institute for Biophysical Chemistry · DEGerman Center for Neurodegenerative Diseases · DEHumboldt-Universität zu Berlin · DEMax Planck Institute for Dynamics and Self-Organization · DE

Funding

Deutsche Forschungsgemeinschaft SFB803
6 · The paper itself

Abstract

The voltage-dependent anion channel (VDAC) is one of the most highly abundant proteins found in the outer mitochondrial membrane, and was one of the earliest discovered. Here we review progress in understanding VDAC function with a focus on its structure, discussing various models proposed for voltage gating as well as potential drug targets to modulate the channel's function. In addition, we explore the sensitivity of VDAC structure to variations in the membrane environment, comparing DMPC-only, DMPC with cholesterol, and near-native lipid compositions, and use magic-angle spinning NMR spectroscopy to locate cholesterol on the outside of the β-barrel. We find that the VDAC protein structure remains unchanged in different membrane compositions, including conditions with cholesterol.

Indexed as

Ion Channel GatingVoltage-Dependent Anion ChannelsAnimalsCholesterolHumansProtein BindingCholesterolVoltage-Dependent Anion ChannelsElectrophysiologyMagic-angle spinningMembrane proteinMolecular dynamics simulationsSolid-state NMRVoltage dependent anion channel

Identifiers

PMID33782728
PMCPMC8071794
OpenAlexW3140142583

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.