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33 items found for " heterodimer"
Posts (27)
- G protein coupling and activation of the metabotropic GABAB heterodimer
2022 "Metabotropic γ-aminobutyric acid receptor (GABABR), a class C G protein-coupled receptor (GPCR) heterodimer
- Allosteric ligands control the activation of a class C GPCR heterodimer by acting at the transmembra
They often form homo- and heterodimers with allosteric cross-talk between receptor entities, which contributes positive allosteric modulators (PAMs) that bind at the interface of the transmembrane domains of the heterodimeric possibility of developing allosteric compounds able to specifically modulate the activity of GPCR homo- and heterodimers
- Cell Surface Calcium-Sensing Receptor Heterodimers: Mutant Gene Dosage Affects Ca 2+ Sensing but...
September 2022 Cell Surface Calcium-Sensing Receptor Heterodimers: Mutant Gene Dosage Affects Ca 2+ Sensing and CaSR-GABAB2 chimeras subject to GABAB -dependent endoplasmic reticulum sorting to traffic mutant heterodimers Mutant heterodimers containing one wild-type (WT) and one mutant VFT domain, however, corresponding to WT HH bundle was insufficient for maximal signaling and there was no functional difference between heterodimers
Other Pages (6)
- Chemokine Cxcl1-Cxcl2 heterodimer is a potent neutrophil chemoattractant
< GPCR News < GPCRs in Oncology and Immunology Chemokine Cxcl1-Cxcl2 heterodimer is a potent neutrophil Here, we characterized the role for heterodimer and show that the Cxcl1-Cxcl2 heterodimer is a potent We have now determined heterodimer's Cxcr2 activity using cellular assays and Cxcr2 density in blood and recruited neutrophils in heterodimer-treated mice. We have shown that the heterodimer binds glycosaminoglycans with higher affinity and more efficiently
- Session III | Adhesion GPCR Workshop 2024 | Dr. GPCR Ecosystem
This gap is due to their unique autoproteolytic cleavage in the GAIN domain, creating a heterodimer of
- LPA1-mediated inhibition of CXCR4 attenuates CXCL12-induced signaling and cell migration
In the present study, we investigated in detail the formation of the CXCR4-LPA1 heteromer and characterized the unique molecular features and function of this heteromer. To elucidate the distinctive molecular characteristics and functional implications of the CXCR4-LPA1 heteromer Results: We observed that CXCR4 forms heteromers with LPA1 in recombinant HEK293A cells and the human Conclusions: The presence and impact of CXCR4-LPA1 heteromers on CXCL12-induced signaling and cell migration