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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.

Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis (2014)
Journal Article
Alqahtani, F. Y. S., Mahdavi, J., Wheldon, L. M., Vassey, M., Pirinccioglu, N., Royer, P., …Ala'Aldeen, D. A. (2014). Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis. Open Biology, 4(10), Article 140053. https://doi.org/10.1098/rsob.140053

The non-integrin laminin receptor (LAMR1/RPSA) and galectin-3 (Gal-3) are multi-functional host molecules with roles in diverse pathological processes, particularly of infectious or oncogenic origins. Using bimolecular fluorescence complementation an... Read More about Deciphering the complex three-way interaction between the non-integrin laminin receptor, galectin-3 and Neisseria meningitidis.

Dimerization of ABCG2 analysed by bimolecular fluorescence complementation (2011)
Journal Article
Haider, A. J., Briggs, D., Self, T. J., Chilvers, H. L., Holliday, N. D., & Kerr, I. D. (2011). Dimerization of ABCG2 analysed by bimolecular fluorescence complementation. PLoS ONE, 6(10), Article e25818. https://doi.org/10.1371/journal.pone.0025818

ABCG2 is one of three human ATP binding cassette transporters that are functionally capable of exporting a diverse range of substrates from cells. The physiological consequence of ABCG2 multidrug transport activity in leukaemia, and some solid tumour... Read More about Dimerization of ABCG2 analysed by bimolecular fluorescence complementation.