Evidence map›Paper›PMID 35365643›Full record

ArticleNature communications2022

Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure.

Alexandre Pozza, François Giraud, Quentin Cece, Marina Casiraghi, Elodie Point, Marjorie Damian, Christel Le Bon, Karine Moncoq, Jean-Louis Banères, Ewen Lescop and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 27 citations in OpenAlex.

  1. Lauric Acid Microemulsions InhibitFoods (Basel, Switzerland) · 2026
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  5. Topological Learning Approach to Characterizing Biological Membranes.Journal of chemical information and modeling · 2024
    Article
  6. Review
  7. Article
  8. Topological Learning Approach to Characterizing Biological Membranes.bioRxiv : the preprint server for biology · 2023
    Article
  9. Review
  10. Review
  11. The complex structure ofScience advances · 2023
    Article
  12. Review
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

11 authors at 1 institution in 2 countries.

Alexandre Pozza *Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
François Giraud *Institut de Chimie des Substances Naturelles (ICSN), CNRS UPR 2301, Université Paris-Saclay, 91198, Gif-sur-Yvette, France.
Quentin CeceLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
Marina CasiraghiLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
Elodie PointLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
Marjorie DamianInstitut des Biomolécules Max Mousseron (IBMM), Université de Montpellier, CNRS, ENSCM, Pôle Chimie Balard Recherche, 34293, Montpellier, cedex 5, France.
Christel Le BonLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
Karine MoncoqLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France.
Jean-Louis BanèresInstitut des Biomolécules Max Mousseron (IBMM), Université de Montpellier, CNRS, ENSCM, Pôle Chimie Balard Recherche, 34293, Montpellier, cedex 5, France.ORCID http://orcid.org/0000-0001-7078-1285
Ewen LescopInstitut de Chimie des Substances Naturelles (ICSN), CNRS UPR 2301, Université Paris-Saclay, 91198, Gif-sur-Yvette, France. ewen.lescop@cnrs.fr.ORCID http://orcid.org/0000-0002-2623-9365
Laurent J CatoireLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, UMR 7099, CNRS/Université de Paris, Institut de Biologie Physico-Chimique (IBPC, FRC 550), 75005, Paris, France. laurent.catoire@ibpc.fr.ORCID http://orcid.org/0000-0001-6839-3312
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell membranes represent a complex and variable medium in time and space of lipids and proteins. Their physico-chemical properties are determined by lipid components which can in turn influence the biological function of membranes. Here, we used hydrostatic pressure to study the close dynamic relationships between lipids and membrane proteins. Experiments on the β-barrel OmpX and the α-helical BLT2 G Protein-Coupled Receptor in nanodiscs of different lipid compositions reveal conformational landscapes intimately linked to pressure and lipids. Pressure can modify the conformational landscape of the membrane protein per se, but also increases the gelation of lipids, both being monitored simultaneously at high atomic resolution by NMR. Our study also clearly shows that a membrane protein can modulate, at least locally, the fluidity of the bilayer. The strategy proposed herein opens new perspectives to scrutinize the dynamic interplay between membrane proteins and their surrounding lipids.

Indexed as

Lipid BilayersMembrane ProteinsCell MembraneHydrostatic PressureMagnetic Resonance SpectroscopyLipid BilayersMembrane Proteins

Identifiers

PMID35365643
PMCPMC8975810
OpenAlexW4220799169

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.