Evidence map›Paper›PMID 36781912›Full record

ArticleNature communications2023

Illumination of a progressive allosteric mechanism mediating the glycine receptor activation.

Sophie Shi, Solène N Lefebvre, Laurie Peverini, Adrien H Cerdan, Paula Milán Rodríguez, Marc Gielen, Jean-Pierre Changeux, Marco Cecchini, Pierre-Jean Corringer

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

7 citing papers in PubMed, 15 citations in OpenAlex.

  1. Extracellular KNature communications · 2026
    Article
  2. Dynamics and Interplay of the Binding Pockets in the Glycine Receptor.Journal of chemical information and modeling · 2025
    Article
  3. Article
  4. Exploring the Activation Process of the Glycine Receptor.Journal of the American Chemical Society · 2024
    Article
  5. Review
  6. Article
  7. 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

9 authors at 2 institutions in 1 country.

Sophie Shi *Institut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France.
Solène N Lefebvre *Institut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France.ORCID 0000-0002-1333-2042
Laurie PeveriniInstitut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France.ORCID 0000-0002-7992-1245
Adrien H CerdanInstitut de Chimie de Strasbourg, UMR7177, CNRS, Université de Strasbourg, F-67083, Strasbourg, Cedex, France.ORCID 0000-0001-6953-8325
Paula Milán RodríguezInstitut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France.ORCID 0000-0002-2724-0747
Marc GielenInstitut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France.ORCID 0000-0003-0941-4325
Jean-Pierre ChangeuxNeuroscience Department, Institut Pasteur, Collège de France, Paris, France.
Marco CecchiniInstitut de Chimie de Strasbourg, UMR7177, CNRS, Université de Strasbourg, F-67083, Strasbourg, Cedex, France. mcecchini@unistra.fr.ORCID 0000-0003-2671-1583
Pierre-Jean CorringerInstitut Pasteur, Université Paris Cité, CNRS UMR 3571, Channel-Receptors Unit, Paris, France. pierre-jean.corringer@pasteur.fr.
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pentameric ligand-gated ion channel mediate signal transduction at chemical synapses by transiting between resting and open states upon neurotransmitter binding. Here, we investigate the gating mechanism of the glycine receptor fluorescently labeled at the extracellular-transmembrane interface by voltage-clamp fluorometry (VCF). Fluorescence reports a glycine-elicited conformational change that precedes pore opening. Low concentrations of glycine, partial agonists or specific mixtures of glycine and strychnine trigger the full fluorescence signal while weakly activating the channel. Molecular dynamic simulations of a partial agonist bound-closed Cryo-EM structure show a highly dynamic nature: a marked structural flexibility at both the extracellular-transmembrane interface and the orthosteric site, generating docking properties that recapitulate VCF data. This work illuminates a progressive propagating transition towards channel opening, highlighting structural plasticity within the mechanism of action of allosteric effectors.

Indexed as

GlycineReceptors, GlycineLightingMolecular Dynamics SimulationSignal TransductionGlycineReceptors, Glycine

Identifiers

PMID36781912
PMCPMC9925812
OpenAlexW4320491310

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.