Evidence map›Paper›PMID 31952690›Full record

ReviewProgress in molecular biology and translational science2020

Oligomerization of G protein-coupled receptors: Still doubted?

Sergi Ferré, Francisco Ciruela, Vicent Casadó, Leonardo Pardo

Open access · greenAbstract readReview
In one paragraph

Review in Progress in molecular biology and translational science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  9. Development of a highly sensitive platform for protein-protein interaction detection and regulation of T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. The β2-adrenergic receptor associates with CXCR4 multimers in human cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. αPharmacological research · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Heteromerization between αPharmacological research · 2021
    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

4 authors at 4 institutions in 2 countries.

Sergi FerréIntegrative Neurobiology Section, National Institute on Drug Abuse, Intramural Research Program, National Institutes of Health, Baltimore, MD, United States. Electronic address: SFerre@intra.nida.nih.gov.
Francisco CiruelaUnitat de Farmacologia, Departament Patologia i Terapéutica Experimental, Facultat de Medicina, IDIBELL, Institut de Neurociències, Universitat de Barcelona, L'Hospitalet de Llobregat, Spain.
Vicent CasadóDepartment of Biochemistry and Molecular Biomedicine, Faculty of Biology, and Institute of Biomedicine, University of Barcelona, Barcelona, Spain.
Leonardo PardoLaboratori de Medicina Computacional, Unitat de Bioestadística, Facultat de Medicina, Universitat Autònoma de Barcelona, Bellaterra, Spain.
Institut d'Investigació Biomédica de Bellvitge · ESNational Institutes of Health · USUniversitat Autònoma de Barcelona · ESUniversitat de Barcelona · ES

Funding

Neurotransmitter Receptor Heteromers in the Striatal Spine ModuleZIADA000493 · NIDA · NATIONAL INSTITUTE ON DRUG ABUSE · PI FERRE, SERGI · 2009 to 2025
$35.6M
Intramural NIH HHS Z99 DA999999
6 · The paper itself

Abstract

Experimental data accumulated during the last 10 years strongly support the existence and functional significance of oligomerization of G protein-coupled receptors (GPCRs). In this essay, we discuss the unique biochemical properties of GPCR oligomers in the frame of "allosterism" and how these properties can be used to identify GPCR oligomers in artificial systems and in native tissues. We also address how the significant advances in biophysical, computational and crystallization techniques have provided significant structural insights about the mechanisms behind allosterism in GPCRs, giving distinct clues about the mechanisms of allosteric interactions in GPCR homomers and heteromers. Finally, we elaborate on the emerging picture of the role of GPCR oligomers as components of pre-coupled macromolecular complexes that include different G proteins and effectors, such as adenylyl cyclase. Allosteric properties of GPCR oligomers can therefore extend to ligand interactions through the different components of the macromolecular complexes.

Indexed as

Adenylyl CyclasesAllosteric SiteAnimalsBinding SitesGTP-Binding ProteinsHumansLigandsMiceProtein BindingProtein DomainsProtein MultimerizationProtein Structure, SecondaryReceptors, G-Protein-CoupledSignal TransductionAdenylyl CyclasesGTP-Binding ProteinsLigandsReceptors, G-Protein-CoupledAllosterismArtificial systemsG protein-coupled receptorsMacromolecular complexesNative tissuesOligomerizationReceptor heteromersReceptor homomers

Identifiers

PMID31952690
PMCPMC9364906
OpenAlexW3000738780

What OpenQuestion holds

Textmetadata
LicenceTDM
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.