ArticleFrontiers in pharmacology2022
A Dynamic Mass Redistribution Assay for the Human Sweet Taste Receptor Uncovers G-Protein Dependent Biased Ligands.
Article in Frontiers in pharmacology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Accelerating GPCR drug discovery through computation and experiment integrated with direct detection of ligand binding events.npj drug discovery · 2026Review
- Steviol rebaudiosides bind to four different sites of the human sweet taste receptor (T1R2/T1R3) complex explaining confusing experiments.Communications chemistry · 2024Article
- Label-free, real-time monitoring of membrane binding events at zeptomolar concentrations using frequency-locked optical microresonators.Nature communications · 2024Article
- Label-free, real-time monitoring of membrane binding events at zeptomolar concentrations using frequency-locked optical microresonators.bioRxiv : the preprint server for biology · 2023Article
- Detecting and measuring of GPCR signaling - comparison of human induced pluripotent stem cells and immortal cell lines.Frontiers in endocrinology · 2023Review
- Fingerprinting heterocellular β-adrenoceptor functional expression in the brain using agonist activity profiles.Frontiers in molecular biosciences · 2023Article
- Investigating the ligand agonism and antagonism at the DScientific reports · 2022Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sweet taste receptor is rather unique, recognizing a diverse repertoire of natural or synthetic ligands, with a surprisingly large structural diversity, and with potencies stretching over more than six orders of magnitude. Yet, it is not clear if different cell-based assays can faithfully report the relative potencies and efficacies of these molecules. Indeed, up to now, sweet taste receptor agonists have been almost exclusively characterized using cell-based assays developed with overexpressed and promiscuous G proteins. This non-physiological coupling has allowed the quantification of receptor activity
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Registered trials
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