Evidence map›Paper›PMID 30717191›Full record

ReviewMolecules (Basel, Switzerland)2019

Bioluminescence Resonance Energy Transfer as a Method to Study Protein-Protein Interactions: Application to G Protein Coupled Receptor Biology.

Chayma El Khamlichi, Flora Reverchon-Assadi, Nadège Hervouet-Coste, Lauren Blot, Eric Reiter, Séverine Morisset-Lopez

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

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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

6 authors.

Chayma El KhamlichiCentre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, 45071 Orléans, France. chayma.el-khamlichi@cnrs-orleans.fr.
Flora Reverchon-AssadiCentre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, 45071 Orléans, France. flora.reverchon@cnrs-orleans.fr.
Nadège Hervouet-CosteCentre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, 45071 Orléans, France. nadege.hervouet@cnrs-orleans.fr.
Lauren BlotCentre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, 45071 Orléans, France. lauren.blot@cnrs-orleans.fr.
Eric ReiterPRC, INRA, CNRS, Université François Rabelais-Tours, 37380 Nouzilly, France. eric.reiter@inra.fr.
Séverine Morisset-LopezCentre de Biophysique Moléculaire, CNRS, UPR 4301, University of Orléans and INSERM, 45071 Orléans, France. severine.morisset-lopez@cnrs-orleans.fr.ORCID 0000-0002-9930-7824

Funding

Association pour la Recherche sur la Sclérose Latérale Amyotrophique et autres Maladies du Motoneurone ARSLA_LINGOConseil Régional du Centre-Val de Loire APR IR LINGOConseil Régional du Centre-Val de Loire APR IR PAINConseil Régional du Centre-Val de Loire ARD2020 BiomedicamentsFondation pour la Recherche Médicale FRM SPF201809006912Labex LabExMabImprove
6 · The paper itself

Abstract

The bioluminescence resonance energy transfer (BRET) approach involves resonance energy transfer between a light-emitting enzyme and fluorescent acceptors. The major advantage of this technique over biochemical methods is that protein-protein interactions (PPI) can be monitored without disrupting the natural environment, frequently altered by detergents and membrane preparations. Thus, it is considered as one of the most versatile technique for studying molecular interactions in living cells at "physiological" expression levels. BRET analysis has been applied to study many transmembrane receptor classes including G-protein coupled receptors (GPCR). It is well established that these receptors may function as dimeric/oligomeric forms and interact with multiple effectors to transduce the signal. Therefore, they are considered as attractive targets to identify PPI modulators. In this review, we present an overview of the different BRET systems developed up to now and their relevance to identify inhibitors/modulators of protein⁻protein interaction. Then, we introduce the different classes of agents that have been recently developed to target PPI, and provide some examples illustrating the use of BRET-based assays to identify and characterize innovative PPI modulators in the field of GPCRs biology. Finally, we discuss the main advantages and the limits of BRET approach to characterize PPI modulators.

Indexed as

Bioluminescence Resonance Energy Transfer TechniquesHigh-Throughput Screening AssaysAntibodiesAptamers, NucleotideBacterial ProteinsCarbocyaninesGenes, ReporterGreen Fluorescent ProteinsHumansLuciferasesLuminescent ProteinsPeptidomimeticsProtein Interaction Domains and MotifsProtein MultimerizationQuantum DotsReceptors, G-Protein-CoupledAntibodiesAptamers, NucleotideBacterial ProteinsCarbocyaninesfluorescent protein 583Green Fluorescent ProteinsLuciferasesLuminescent ProteinsPeptidomimeticsReceptors, G-Protein-CoupledRed Fluorescent ProteinSmall Molecule Librariesyellow fluorescent protein, BacteriaBRETdrug discoveryGPCR-interacting proteinsGPCR signalingG protein-coupled receptorsreceptor-protein interactionsscreening

Identifiers

PMID30717191
PMCPMC6384791

What OpenQuestion holds

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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.