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Graeme Milligan

Researcher at University of Glasgow

Publications -  570
Citations -  32250

Graeme Milligan is an academic researcher from University of Glasgow. The author has contributed to research in topics: Receptor & G protein. The author has an hindex of 88, co-authored 556 publications receiving 30032 citations. Previous affiliations of Graeme Milligan include University of Leicester & Autonomous University of Barcelona.

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Real time visualization of agonist-mediated redistribution and internalization of a green fluorescent protein-tagged form of the thyrotropin-releasing hormone receptor.

TL;DR: Results demonstrate the G protein-coupling capacity and provide real time visualization of the processes of internalization of a TRH-receptor-GFP construct in response to agonist.
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Differential effects of suramin on the coupling of receptors to individual species of pertussis-toxin-sensitive guanine-nucleotide-binding proteins.

TL;DR: The anti-helminthic drug suramin inhibited the basal high-affinity GTPase activity of both C6 BU1glioma and NG 108-15 neuroblastoma x glioma hybrid-cell membranes with an IC50 value close to 30 micrograms/ml and provides the first evidence for a selective effect of a drug on the functions of different G-proteins.
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Insulin activates glycerol-3-phosphate acyltransferase (de novo phosphatidic acid synthesis) through a phospholipid-derived mediator. Apparent involvement of Gi alpha and activation of a phospholipase C.

TL;DR: The mechanism whereby insulin activates de novo phosphatidic acid synthesis in BC3H-1 myocytes is studied to suggest involvement of a PLC in insulin-induced activation of G3PAT.
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The Molecular Basis of Ligand Interaction at Free Fatty Acid Receptor 4 (FFA4/GPR120)

TL;DR: Examination of the detailed mode of binding of both long-chain fatty acid and synthetic agonist ligands at FFA4 by integrating molecular modeling, receptor mutagenesis, and ligand structure-activity relationship approaches in an iterative format yields a well validated model of the mode of ligand-FFA4 interaction.