Evidence map›Paper›PMID 29864148›Full record

ArticlePloS one2018

Xenon-inhibition of the MscL mechano-sensitive channel and the CopB copper ATPase under different conditions suggests direct effects on these proteins.

Evgeny Petrov, Gopalakrishnan Menon, Paul R Rohde, Andrew R Battle, Boris Martinac, Marc Solioz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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  4. Review
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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

6 authors at 4 institutions in 3 countries.

Evgeny PetrovLaboratory of Biochemistry and Molecular Biology, Tomsk State University, Tomsk, Russia.
Gopalakrishnan MenonLaboratory of Biochemistry and Molecular Biology, Tomsk State University, Tomsk, Russia.
Paul R RohdeVictor Chang Cardiac Research Institute, Darlinghurst, Australia.
Andrew R BattleVictor Chang Cardiac Research Institute, Darlinghurst, Australia.
Boris MartinacVictor Chang Cardiac Research Institute, Darlinghurst, Australia.
Marc SoliozLaboratory of Biochemistry and Molecular Biology, Tomsk State University, Tomsk, Russia.ORCID 0000-0002-7989-6721
National Research Tomsk State University · RUVictor Chang Cardiac Research Institute · AUQueensland University of Technology · AUUniversity of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xenon is frequently used as a general anesthetic in humans, but the mechanism remains an issue of debate. While for some membrane proteins, a direct interaction of xenon with the protein has been shown to be the inhibitory mechanism, other membrane protein functions could be affected by changes of membrane properties due to partitioning of the gas into the lipid bilayer. Here, the effect of xenon on a mechanosensitive ion channel and a copper ion-translocating ATPase was compared under different conditions. Xenon inhibited spontaneous gating of the Escherichia coli mechano-sensitive mutant channel MscL-G22E, as shown by patch-clamp recording techniques. Under high hydrostatic pressure, MscL-inhibition was reversed. Similarly, the activity of the Enterococcus hirae CopB copper ATPase, reconstituted into proteoliposomes, was inhibited by xenon. However, the CopB ATPase activity was also inhibited by xenon when CopB was in a solubilized state. These findings suggest that xenon acts by directly interacting with these proteins, rather than via indirect effects by altering membrane properties. Also, inhibition of copper transport may be a novel effect of xenon that contributes to anesthesia.

Indexed as

Adenosine TriphosphatasesCation Transport ProteinsCopper Transport ProteinsEscherichia coli ProteinsIon Channel GatingIon ChannelsMechanotransduction, CellularPatch-Clamp TechniquesXenonAdenosine TriphosphatasesCation Transport ProteinsCopB ATPase, Enterococcus hiraeCopper Transport ProteinsEscherichia coli ProteinsIon ChannelsMscL protein, E coliXenon

Identifiers

PMID29864148
PMCPMC5986136
OpenAlexW2806202712

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.