ArticleInternational journal of molecular sciences2022
Functional Characterization of the Venus Flytrap Domain of the Human TAS1R2 Sweet Taste Receptor.
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Targeting sweet taste receptor T1R2/T1R3: a new strategy for metabolic disease regulation and intervention of multiple organ diseases.Food chemistry. Molecular sciences · 2026Review
- Sweet Taste Receptor Genetic VariationNutrients · 2026Article
- Advances in Intestinal Glucose Absorption Regulation for Ruminant Energy Efficiency Improvement.Animals : an open access journal from MDPI · 2026Review
- Glutathione as a taste modulator: molecular mechanisms of interaction with umami and sweet taste receptors.Food chemistry. Molecular sciences · 2025Article
- Molecular Dynamics Insights into TAS1R2 Transmembrane Domain Activation.International journal of molecular sciences · 2025Article
- Inosine-5'-monophosphate interacts with the TAS1R3 subunit to enhance sweet taste detection.Food chemistry. Molecular sciences · 2025Article
- Article
- Article
- Saccharin and aspartame excite rat retinal neurons.Frontiers in ophthalmology · 2023Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The human sweet taste receptor is a heterodimeric receptor composed of two distinct G-protein-coupled receptors (GPCRs), TAS1R2 and TAS1R3. The TAS1R2 and TAS1R3 subunits are members of a small family of class C GPCRs whose members share the same architecture, comprising a Venus Flytrap (VFT) module linked to the seven transmembrane domains (TMDs) by a short cysteine-rich region (CRR). The VFT module of TAS1R2 contains the primary binding site for most of the sweet-tasting compounds, including natural sugars and artificial and natural sweeteners. However, cellular assays, molecular docking and site-directed mutagenesis studies have revealed that the VFT, CRR and TMD of TAS1R3 interact with some sweeteners, including the sweet-tasting protein brazzein. The aim of this study was to better understand the contribution of TAS1R2-VFT in the binding of sweet stimuli. To achieve this, we heterologously expressed human TAS1R2-VFT (hTAS1R2-VFT) in
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Registered trials
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.