Evidence map›Paper›PMID 28584054›Full record

ArticleThe Journal of biological chemistry2017

Conformational biosensors reveal allosteric interactions between heterodimeric AT1 angiotensin and prostaglandin F2α receptors.

Rory Sleno, Dominic Devost, Darlaine Pétrin, Alice Zhang, Kyla Bourque, Yuji Shinjo, Junken Aoki, Asuka Inoue, Terence E Hébert

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Pharmacology of Free Fatty Acid Receptors and Their Allosteric Modulators.International journal of molecular sciences · 2021
    Review
  8. Multiple GPCR Functional Assays Based on Resonance Energy Transfer Sensors.Frontiers in cell and developmental biology · 2021
    Review
  9. Signal profiling of the βScientific reports · 2020
    Article
  10. Review
  11. Review
  12. 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 2 countries.

Rory SlenoDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada.
Dominic DevostDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada.
Darlaine PétrinDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada.
Alice ZhangDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada.
Kyla BourqueDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada.
Yuji ShinjoGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan.
Junken AokiGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan; Japan Agency for Medical Research and Development, Core Research for Evolutional Science and Technology (AMED-CREST), Chiyoda-ku, Tokyo 100-0004, Japan.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan; Japan Science and Technology Agency (JST), Precursory Research for Embryonic Science and Technology (PRESTO), Kawaguchi, Saitama 332-0012, Japan.
Terence E HébertDepartment of Pharmacology and Therapeutics, McGill University, Montréal, Québec H3G 1Y6, Canada. Electronic address: terence.hebert@mcgill.ca.
McGill University · CATohoku University · JP

Funding

CIHR MOP-130309
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are conformationally dynamic proteins transmitting ligand-encoded signals in multiple ways. This transmission is highly complex and achieved through induction of distinct GPCR conformations, which preferentially drive specific receptor-mediated signaling events. This conformational capacity can be further enlarged via allosteric effects between dimers, warranting further study of these effects. Using GPCR conformation-sensitive biosensors, we investigated allosterically induced conformational changes in the recently reported F prostanoid (FP)/angiotensin II type 1 receptor (AT1R) heterodimer. Ligand occupancy of the AT1R induced distinct conformational changes in FP compared with those driven by PGF2α in bioluminescence resonance energy transfer (BRET)-based FP biosensors engineered with

Indexed as

Models, MolecularSignal TransductionAllosteric RegulationBioluminescence Resonance Energy Transfer TechniquesBiosensing TechniquesCell MembraneGTP-Binding Protein alpha Subunits, Gq-G11HEK293 CellsHumansLigandsLuciferases, RenillaOligopeptidesPeptide FragmentsProtein ConformationProtein Interaction Domains and MotifsProtein Kinase CAGTR1 protein, humanFLAG peptideGNAQ protein, humanGTP-Binding Protein alpha Subunits, Gq-G11LigandsLuciferases, RenillaOligopeptidesOXTR protein, humanPeptide Fragmentsprostaglandin F2alpha receptorProtein Kinase CReceptor, Angiotensin, Type 1Receptors, OxytocinReceptors, ProstaglandinRecombinant Fusion ProteinsType C Phospholipasesbioluminescence resonance energy transfer (BRET)cell signalingconformational changedimerizationG protein-coupled receptor (GPCR)

Identifiers

PMID28584054
PMCPMC5519365
OpenAlexW2623838690

What OpenQuestion holds

Textmetadata
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.