All Outputs (4)

Unravelling intrinsic efficacy and ligand bias at G protein coupled receptors: A practical guide to assessing functional data (2015)
Journal Article
Stott, L. A., Hall, D. A., & Holliday, N. D. (2016). Unravelling intrinsic efficacy and ligand bias at G protein coupled receptors: A practical guide to assessing functional data. Biochemical Pharmacology, 101, 1-12. https://doi.org/10.1016/j.bcp.2015.10.011

© 2015 Elsevier Inc. All rights reserved. Stephenson's empirical definition of an agonist, as a ligand with binding affinity and intrinsic efficacy (the ability to activate the receptor once bound), underpins classical receptor pharmacology. Quantify... Read More about Unravelling intrinsic efficacy and ligand bias at G protein coupled receptors: A practical guide to assessing functional data.

Plasma membrane dynamics and tetrameric organisation of ABCG2 transporters in mammalian cells revealed by single particle imaging techniques (2015)
Journal Article
Wong, K., Briddon, S. J., Holliday, N. D., & Kerr, I. D. (2016). Plasma membrane dynamics and tetrameric organisation of ABCG2 transporters in mammalian cells revealed by single particle imaging techniques. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1863(1), 19-29. https://doi.org/10.1016/j.bbamcr.2015.10.002

ABCG2 is one of three human ATP binding cassette (ABC) transporters involved in the export from cells of a chemically and structurally diverse range of compounds. This multidrug efflux capability, together with a broad tissue distribution in the body... Read More about Plasma membrane dynamics and tetrameric organisation of ABCG2 transporters in mammalian cells revealed by single particle imaging techniques.

Biased Gs versus Gq proteins and ?-arrestin signaling in the NK1 receptor determined by interactions in the water hydrogen bond network (2015)
Journal Article
Valentin-Hansen, L., Frimurer, T. M., Mokrosinski, J., Holliday, N. D., & Schwartz, T. W. (2015). Biased Gs versus Gq proteins and ?-arrestin signaling in the NK1 receptor determined by interactions in the water hydrogen bond network. Journal of Biological Chemistry, 290(40), 24495-24508. https://doi.org/10.1074/jbc.m115.641944

X-ray structures, molecular dynamics simulations, and mutational analysis have previously indicated that an extended water hydrogen bond network between trans-membranes I-III, VI, and VII constitutes an allosteric interface essential for stabilizing... Read More about Biased Gs versus Gq proteins and ?-arrestin signaling in the NK1 receptor determined by interactions in the water hydrogen bond network.

A G protein-coupled receptor dimer imaging assay reveals selectively modified pharmacology of neuropeptide Y Y1/Y5 receptor heterodimers (2015)
Journal Article
Kilpatrick, L. E., Humphrys, L. J., & Holliday, N. D. (in press). A G protein-coupled receptor dimer imaging assay reveals selectively modified pharmacology of neuropeptide Y Y1/Y5 receptor heterodimers. Molecular Pharmacology, 87(4), https://doi.org/10.1124/mol.114.095356

The ability of G protein-coupled receptors (GPCRs) to form dimers, and particularly heterodimers, offers potential for targeted therapeutics with improved selectivity. However, studying dimer pharmacology is challenging, because of signaling cross-ta... Read More about A G protein-coupled receptor dimer imaging assay reveals selectively modified pharmacology of neuropeptide Y Y1/Y5 receptor heterodimers.