Evidence map›Paper›PMID 35422073›Full record

ArticleCommunications biology2022

High-pressure crystallography shows noble gas intervention into protein-lipid interaction and suggests a model for anaesthetic action.

Igor Melnikov, Philipp Orekhov, Maksim Rulev, Kirill Kovalev, Roman Astashkin, Dmitriy Bratanov, Yury Ryzhykau, Taras Balandin, Sergei Bukhdruker, Ivan Okhrimenko and 8 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. 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

18 authors at 6 institutions in 4 countries.

Igor MelnikovInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany.ORCID 0000-0003-2265-4534
Philipp OrekhovFaculty of Biology, Lomonosov Moscow State University, 119991, Moscow, Russia.ORCID 0000-0003-4078-4762
Maksim RulevInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany.
Kirill KovalevInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, Grenoble, France.
Roman AstashkinInstitut de Biologie Structurale (IBS), Université Grenoble Alpes, CNRS, CEA, Grenoble, France.
Dmitriy BratanovInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany.
Yury RyzhykauResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.ORCID 0000-0003-3719-1464
Taras BalandinInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany.
Sergei BukhdrukerEuropean Synchrotron Radiation Facility, Grenoble, France.ORCID 0000-0002-0157-532X
Ivan OkhrimenkoResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Valentin BorshchevskiyResearch Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
Gleb BourenkovEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Hamburg, Germany.
Christoph Mueller-DieckmannEuropean Synchrotron Radiation Facility, Grenoble, France.
Peter van der LindenPSCM (Partnership for Soft Condensed Matter), ESRF, Grenoble, France.ORCID 0000-0002-3481-0787
Philippe CarpentierEuropean Synchrotron Radiation Facility, Grenoble, France.
Gordon LeonardEuropean Synchrotron Radiation Facility, Grenoble, France.ORCID 0000-0001-5030-0122
Valentin GordeliyInstitute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich GmbH, Jülich, Germany. valentin.gordeliy@ibs.fr.ORCID 0000-0001-5782-5896
Alexander PopovEuropean Synchrotron Radiation Facility, Grenoble, France. alexander.popov@esrf.fr.ORCID 0000-0002-3058-8912
Centre National de la Recherche Scientifique · FREuropean Synchrotron Radiation Facility · FRForschungszentrum Jülich · DEMoscow Institute of Physics and Technology · RUEuropean Molecular Biology Laboratory · DELomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work we examine how small hydrophobic molecules such as inert gases interact with membrane proteins (MPs) at a molecular level. High pressure atmospheres of argon and krypton were used to produce noble gas derivatives of crystals of three well studied MPs (two different proton pumps and a sodium light-driven ion pump). The structures obtained using X-ray crystallography showed that the vast majority of argon and krypton binding sites were located on the outer hydrophobic surface of the MPs - a surface usually accommodating hydrophobic chains of annular lipids (which are known structural and functional determinants for MPs). In conformity with these results, supplementary in silico molecular dynamics (MD) analysis predicted even greater numbers of argon and krypton binding positions on MP surface within the bilayer. These results indicate a potential importance of such interactions, particularly as related to the phenomenon of noble gas-induced anaesthesia.

Indexed as

AnestheticsKryptonArgonCrystallography, X-RayLipidsAnestheticsArgonKryptonLipids

Identifiers

PMID35422073
PMCPMC9010423
OpenAlexW4223926908

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.