Evidence map›Paper›PMID 27021164›Full record

ArticleStructure (London, England : 1993)2016

Molecular Plasticity of the Human Voltage-Dependent Anion Channel Embedded Into a Membrane.

Lin Ge, Saskia Villinger, Stefania A Mari, Karin Giller, Christian Griesinger, Stefan Becker, Daniel J Müller, Markus Zweckstetter

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

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  17. Bcl-2-Protein Family as Modulators of IPCold Spring Harbor perspectives in biology · 2020
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  20. Lipid Internal Dynamics Probed in Nanodiscs.Chemphyschem : a European journal of chemical physics and physical chemistry · 2017
    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

8 authors at 4 institutions in 2 countries.

Lin GeDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zürich, Mattenstrasse 26, 4058 Basel, Switzerland.
Saskia VillingerDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Stefania A MariDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zürich, Mattenstrasse 26, 4058 Basel, Switzerland.
Karin GillerDepartment of NMR-based Structural Biology, 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.
Stefan BeckerDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Daniel J MüllerDepartment of Biosystems Science and Engineering, Eidgenössische Technische Hochschule (ETH) Zürich, Mattenstrasse 26, 4058 Basel, Switzerland. Electronic address: daniel.mueller@bsse.ethz.ch.
Markus ZweckstetterDepartment of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany; Structural Biology in Dementia, German Center for Neurodegenerative Diseases (DZNE), Von-Siebold-Strasse 3a, 37075 Göttingen, Germany; Department of Neurology, University Medical Center Göttingen, University of Göttingen, Am Waldweg 33, 37073 Göttingen, Germany. Electronic address: markus.zweckstetter@dzne.de.
Max Planck Institute for Biophysical Chemistry · DEETH Zurich · CHBoard of the Swiss Federal Institutes of Technology · CHUniversitätsmedizin Göttingen · DE

Funding

European Research Council 282008
6 · The paper itself

Abstract

The voltage-dependent anion channel (VDAC) regulates the flux of metabolites and ions across the outer mitochondrial membrane. Regulation of ion flow involves conformational transitions in VDAC, but the nature of these changes has not been resolved to date. By combining single-molecule force spectroscopy with nuclear magnetic resonance spectroscopy we show that the β barrel of human VDAC embedded into a membrane is highly flexible. Its mechanical flexibility exceeds by up to one order of magnitude that determined for β strands of other membrane proteins and is largest in the N-terminal part of the β barrel. Interaction with Ca(2+), a key regulator of metabolism and apoptosis, considerably decreases the barrel's conformational variability and kinetic free energy in the membrane. The combined data suggest that physiological VDAC function depends on the molecular plasticity of its channel.

Indexed as

CalciumHumansKineticsMitochondrial MembranesModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondarySingle Molecule ImagingVoltage-Dependent Anion Channel 1CalciumVDAC1 protein, humanVoltage-Dependent Anion Channel 1atomic force microscopycalcium dependencyconformational variabilityhuman voltage-dependent anion channelintegral membrane proteinNMR spectroscopysingle-molecule force spectroscopystructural flexibility

Identifiers

PMID27021164
PMCPMC5654509
OpenAlexW2308560469

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.