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Use of a new proximity assay (NanoBRET) to investigate the ligand-binding characteristics of three fluorescent ligands to the human?1-adrenoceptor expressed in HEK-293 cells (2016)
Journal Article
Soave, M., Stoddart, L. A., Brown, A., Woolard, J., & Hill, S. J. (2016). Use of a new proximity assay (NanoBRET) to investigate the ligand-binding characteristics of three fluorescent ligands to the human?1-adrenoceptor expressed in HEK-293 cells. Pharmacology Research and Perspectives, 4(5), Article e00250. https://doi.org/10.1002/prp2.250

Previous research has indicated that allosteric interactions across the dimer interface of β1-adrenoceptors may be responsible for a secondary low affinity binding conformation. Here we have investigated the potential for probe dependence, in the det... Read More about Use of a new proximity assay (NanoBRET) to investigate the ligand-binding characteristics of three fluorescent ligands to the human?1-adrenoceptor expressed in HEK-293 cells.

The use of fluorescence correlation spectroscopy to characterize the molecular mobility of fluorescently labelled G protein-coupled receptors (2016)
Journal Article
Kilpatrick, L. E., & Hill, S. J. (in press). The use of fluorescence correlation spectroscopy to characterize the molecular mobility of fluorescently labelled G protein-coupled receptors. Biochemical Society Transactions, 44(2), https://doi.org/10.1042/BST20150285

The membranes of living cells have been shown to be highly organized into distinct microdomains, which has spatial and temporal consequences for the interaction of membrane bound receptors and their signalling partners as complexes. Fluorescence corr... Read More about The use of fluorescence correlation spectroscopy to characterize the molecular mobility of fluorescently labelled G protein-coupled receptors.