Evidence map›Paper›PMID 39805839›Full record

ArticleNature communications2025

Conformational diversity in class C GPCR positive allosteric modulation.

Giuseppe Cannone, Ludovic Berto, Fanny Malhaire, Gavin Ferguson, Aurelien Fouillen, Stéphanie Balor, Joan Font-Ingles, Amadeu Llebaria, Cyril Goudet, Abhay Kotecha and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Unveiling the molecular mechanism of GProtein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Review
  10. 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

12 authors.

Giuseppe Cannone *MRC Laboratory of Molecular Biology, Cambridge, CB2 0QH, UK.
Ludovic Berto *IGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France.
Fanny MalhaireIGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France.
Gavin FergusonIGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France.ORCID http://orcid.org/0000-0003-2551-5994
Aurelien FouillenIGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France.ORCID http://orcid.org/0000-0002-0326-9932
Stéphanie BalorMETi, Centre de Biologie Intégrative, Université de Touluse, CNRS, UPS, 31062, Toulouse, France.
Joan Font-InglesMCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Jordi Girona 18-26, 08034, Barcelona, Spain.
Amadeu LlebariaMCS, Laboratory of Medicinal Chemistry & Synthesis, Department of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Jordi Girona 18-26, 08034, Barcelona, Spain.ORCID http://orcid.org/0000-0002-8200-4827
Cyril GoudetIGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France.ORCID http://orcid.org/0000-0002-8255-3535
Abhay KotechaMaterial and Structure Analysis Division, Thermo Fisher Scientific, Eindhoven, The Netherlands.ORCID http://orcid.org/0000-0002-4480-5439
Vinothkumar K RNational Centre for Biological Sciences, Tata Institute of Fundamental Research, GKVK Post, Bengaluru, 560065, India. vkumar@ncbs.res.in.ORCID http://orcid.org/0000-0002-6746-5684
Guillaume LebonIGF, Université de Montpellier, CNRS, INSERM, 34094, Montpellier, France. guillaume.lebon@igf.cnrs.fr.ORCID http://orcid.org/0000-0003-1162-5148

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-20-CE11-0019
6 · The paper itself

Abstract

The metabotropic glutamate receptors (mGlus) are class C G protein-coupled receptors (GPCR) that form obligate dimers activated by the major excitatory neurotransmitter L-glutamate. The architecture of mGlu receptor comprises an extracellular Venus-Fly Trap domain (VFT) connected to the transmembrane domain (7TM) through a Cysteine-Rich Domain (CRD). The binding of L-glutamate in the VFTs and subsequent conformational change results in the signal being transmitted to the 7TM inducing G protein binding and activation. The mGlu receptors signal transduction can be allosterically potentiated by positive allosteric modulators (PAMs) binding to the 7TMs, which are of therapeutic interest in various neurological disorders. Here, we report the cryoEM structures of metabotropic glutamate receptor 5 (mGlu

Indexed as

Receptor, Metabotropic Glutamate 5Allosteric RegulationAnimalsCryoelectron MicroscopyGlutamic AcidHEK293 CellsHumansModels, MolecularProtein BindingProtein ConformationProtein DomainsSignal TransductionGlutamic AcidReceptor, Metabotropic Glutamate 5

Identifiers

PMID39805839
PMCPMC11730304

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.