Evidence map›Paper›PMID 25404294›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Global structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry.

Albert Konijnenberg, Duygu Yilmaz, Helgi I Ingólfsson, Anna Dimitrova, Siewert J Marrink, Zhuolun Li, Catherine Vénien-Bryan, Frank Sobott, Armağan Koçer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed.

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  17. Charge Neutralization Drives the Shape Reconfiguration of DNA Nanotubes.Angewandte Chemie (International ed. in English) · 2018
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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

9 authors.

Albert KonijnenbergBiomolecular & Analytical Mass Spectrometry Group and.
Duygu YilmazDepartment of Biochemistry and.
Helgi I IngólfssonDepartment of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands;
Anna DimitrovaDepartment of Biochemistry and.
Siewert J MarrinkDepartment of Biochemistry and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG, Groningen, The Netherlands;
Zhuolun LiInstitut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France; and.
Catherine Vénien-BryanInstitut de Minéralogie, de Physique des Matériaux et de Cosmochimie, Sorbonne Universités, CNRS UMR 7590, Université Pierre et Marie Curie, 75005 Paris, France; and.
Frank SobottBiomolecular & Analytical Mass Spectrometry Group and UA-VITO Center for Proteomics (CFP-CEPROMA), University of Antwerp, 2020 Antwerp, Belgium; a.kocer@umcg.nl frank.sobott@uantwerpen.be.
Armağan KoçerDepartment of Neuroscience, University of Groningen, University Medical Center Groningen, 9713 AV, Groningen, The Netherlands a.kocer@umcg.nl frank.sobott@uantwerpen.be.

Funding

European Research Council 208814
6 · The paper itself

Abstract

Mechanosensitive ion channels are sensors probing membrane tension in all species; despite their importance and vital role in many cell functions, their gating mechanism remains to be elucidated. Here, we determined the conditions for releasing intact mechanosensitive channel of large conductance (MscL) proteins from their detergents in the gas phase using native ion mobility-mass spectrometry (IM-MS). By using IM-MS, we could detect the native mass of MscL from Escherichia coli, determine various global structural changes during its gating by measuring the rotationally averaged collision cross-sections, and show that it can function in the absence of a lipid bilayer. We could detect global conformational changes during MscL gating as small as 3%. Our findings will allow studying native structure of many other membrane proteins.

Indexed as

DetergentsEscherichia coliEscherichia coli ProteinsIon Channel GatingIon ChannelsMass SpectrometryMechanotransduction, CellularMembrane ProteinsMicroscopy, ElectronMolecular Dynamics SimulationOctoxynolProtein ConformationDetergentsEscherichia coli ProteinsIon ChannelsMembrane ProteinsMscL protein, E coliOctoxynolion channel gatingion mobility mass spectrometrymembrane proteinsMscLstructure function

Identifiers

PMID25404294
PMCPMC4260606

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.