All Outputs (5)

Fragment-Based Discovery of Subtype-Selective Adenosine Receptor Ligands from Homology Models (2015)
Journal Article
Ranganathan, A., Stoddart, L. A., Hill, S. J., & Carlsson, J. (2015). Fragment-Based Discovery of Subtype-Selective Adenosine Receptor Ligands from Homology Models. Journal of Medicinal Chemistry, 58(24), 9578-9590. https://doi.org/10.1021/acs.jmedchem.5b01120

Fragment-based lead discovery (FBLD) holds great promise for drug discovery, but applications to G protein-coupled receptors (GPCRs) have been limited by a lack of sensitive screening techniques and scarce structural information. If virtual screening... Read More about Fragment-Based Discovery of Subtype-Selective Adenosine Receptor Ligands from Homology Models.

Application of BRET to monitor ligand binding to GPCRs (2015)
Journal Article
Stoddart, L. A., Johnstone, E. K., Wheal, A. J., Goulding, J., Robers, M. B., Machleidt, T., …Pfleger, K. D. (in press). Application of BRET to monitor ligand binding to GPCRs. Nature Methods, 12, https://doi.org/10.1038/nmeth.3398

Bioluminescence resonance energy transfer (BRET) is a well-established method for investigating protein-protein interactions. Here we present a BRET approach to monitor ligand binding to G protein–coupled receptors (GPCRs) on the surface of living ce... Read More about Application of BRET to monitor ligand binding to GPCRs.

Direct visualisation of internalization of the adenosine A3 receptor and localization with arrestin3 using a fluorescent agonist (2015)
Journal Article
Stoddart, L. A., Vernall, A. J., Briddon, S. J., Kellam, B., & Hill, S. J. (2015). Direct visualisation of internalization of the adenosine A3 receptor and localization with arrestin3 using a fluorescent agonist. Neuropharmacology, 98, 68-77. https://doi.org/10.1016/j.neuropharm.2015.04.013

Fluorescence based probes provide a novel way to study the dynamic internalization process of G protein-coupled receptors (GPCRs). Recent advances in the rational design of fluorescent ligands for GPCRs have been used here to generate new fluorescent... Read More about Direct visualisation of internalization of the adenosine A3 receptor and localization with arrestin3 using a fluorescent agonist.

Negative cooperativity across ?1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ?1-adrenoceptor binding conformation (2015)
Journal Article
Gherbi, K., May, L. T., Baker, J. G., Briddon, S. J., & Hill, S. J. (2015). Negative cooperativity across ?1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ?1-adrenoceptor binding conformation. FASEB Journal, 29(7), 2859-2871. https://doi.org/10.1096/fj.14-265199

At the β1-adrenoceptor, CGP 12177 potently antagonizes agonist responses at the primary high-affinity catecholamine conformation while also exerting agonist effects of its own through a secondary low-affinity conformation. A recent mutagenesis study... Read More about Negative cooperativity across ?1-adrenoceptor homodimers provides insights into the nature of the secondary low-affinity CGP 12177 ?1-adrenoceptor binding conformation.

Effects of receptor tyrosine kinase inhibitors on VEGF165a- and VEGF165b-stimulated gene transcription in HEK-293 cells expressing human VEGFR2 (2015)
Journal Article
Carter, J. J., Wheal, A. J., Hill, S. J., & Woolard, J. (2015). Effects of receptor tyrosine kinase inhibitors on VEGF165a- and VEGF165b-stimulated gene transcription in HEK-293 cells expressing human VEGFR2. British Journal of Pharmacology, 172(12), https://doi.org/10.1111/bph.13116

BACKGROUND AND PURPOSE: Receptor tyrosine kinase inhibitors (RTKIs) targeted at VEGF receptor 2 (VEGFR2) have proved to be attractive approaches to cancer therapy based on their ability to reduce angiogenesis. Here we have undertaken a quantitative... Read More about Effects of receptor tyrosine kinase inhibitors on VEGF165a- and VEGF165b-stimulated gene transcription in HEK-293 cells expressing human VEGFR2.