Evidence map›Paper›PMID 33499147›Full record

ArticleInternational journal of molecular sciences2021

Investigation of Receptor Heteromers Using NanoBRET Ligand Binding.

Elizabeth K M Johnstone, Heng B See, Rekhati S Abhayawardana, Angela Song, K Johan Rosengren, Stephen J Hill, Kevin D G Pfleger

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 17 citations in OpenAlex.

  1. Using a NanoBRET-Based Ligand-Binding Assay at the βPharmacology research & perspectives · 2026
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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

7 authors at 3 institutions in 2 countries.

Elizabeth K M JohnstoneMolecular Endocrinology and Pharmacology Group, Harry Perkins Institute of Medical Research, Nedlands, WA 6009, Australia.ORCID 0000-0001-7990-371X
Heng B SeeMolecular Endocrinology and Pharmacology Group, Harry Perkins Institute of Medical Research, Nedlands, WA 6009, Australia.
Rekhati S AbhayawardanaMolecular Endocrinology and Pharmacology Group, Harry Perkins Institute of Medical Research, Nedlands, WA 6009, Australia.
Angela SongSchool of Biomedical Sciences, Faculty of Medicine, The University of Queensland, St Lucia, QLD 4072, Australia.
K Johan RosengrenSchool of Biomedical Sciences, Faculty of Medicine, The University of Queensland, St Lucia, QLD 4072, Australia.ORCID 0000-0002-5007-8434
Stephen J HillMolecular Endocrinology and Pharmacology Group, Harry Perkins Institute of Medical Research, Nedlands, WA 6009, Australia.ORCID 0000-0002-4424-239X
Kevin D G PflegerMolecular Endocrinology and Pharmacology Group, Harry Perkins Institute of Medical Research, Nedlands, WA 6009, Australia.ORCID 0000-0001-8261-9189
Australian Research Council · AUThe University of Queensland · AUUniversity of Nottingham · GB

Funding

Australian Research Council FT130100890Australian Research Council IC170100016Australian Research Council LP130100037Australian Research Council LP160100857National Health and Medical Research Council 1085842
6 · The paper itself

Abstract

Receptor heteromerization is the formation of a complex involving at least two different receptors with pharmacology that is distinct from that exhibited by its constituent receptor units. Detection of these complexes and monitoring their pharmacology is crucial for understanding how receptors function. The Receptor-Heteromer Investigation Technology (Receptor-HIT) utilizes ligand-dependent modulation of interactions between receptors and specific biomolecules for the detection and profiling of heteromer complexes. Previously, the interacting biomolecules used in Receptor-HIT assays have been intracellular proteins, however in this study we have for the first time used bioluminescence resonance energy transfer (BRET) with fluorescently-labeled ligands to investigate heteromerization of receptors on the cell surface. Using the Receptor-HIT ligand binding assay with NanoBRET, we have successfully investigated heteromers between the angiotensin II type 1 (AT

Indexed as

LigandsBinding, CompetitiveBioluminescence Resonance Energy Transfer TechniquesBoron CompoundsCell MembraneCyclic AMPFluorescence Resonance Energy TransferHEK293 CellsHumansKineticsNanotechnologyProtein BindingProtein MultimerizationReceptor, Angiotensin, Type 1Receptor, Angiotensin, Type 2Receptors, Adrenergic, beta-24,4-difluoro-4-bora-3a,4a-diaza-s-indaceneAGTR1 protein, humanAGTR2 protein, humanBoron CompoundsCyclic AMPLigandsReceptor, Angiotensin, Type 1Receptor, Angiotensin, Type 2Receptors, Adrenergic, beta-2Receptors, Angiotensinangiotensin receptorGPCRheteromerligand bindingNanoBRETNlucReceptor-HITβ2 adrenergic receptor

Identifiers

PMID33499147
PMCPMC7866079
OpenAlexW3124694389

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.