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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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When simple agonism is not enough: emerging modalities of GPCR ligands.

TL;DR: M modes of agonism emerging from the discovery of functional selectivity and allosterism are described and the concept of ago-allosterism, where ligands can initiate signaling by themselves and influence the actions of another ligand at the same receptor is discussed.
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Multiple roles for the C-terminal tail of the chemokine scavenger D6.

TL;DR: It is concluded that the heptahelical body of D 6 on its own can engage the endocytotic machinery of HEK293 cells but that the C terminus is indispensable for scavenging because it prevents initial chemokine engagement of D6 from inhibiting subsequent chemokin uptake.
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betagamma dimers derived from Go and Gi proteins contribute different components of adrenergic inhibition of Ca2+ channels in rat sympathetic neurones.

TL;DR: βγ dimers associated with GαoA and Gαi are identified as mediators of the PTX‐sensitive α2‐adrenoceptor‐mediated inhibition of N‐type Ca2+ channels in sympathetic neurones.
Journal Article

S18616, a highly potent, spiroimidazoline agonist at alpha(2)-adrenoceptors: I. Receptor profile, antinociceptive and hypothermic actions in comparison with dexmedetomidine and clonidine.

TL;DR: In conclusion, S18616 is a novel, selective, and highly potent agonist at alpha(2)-ARs that dose dependently elicited hypothermia and antinociception in rodents and was unaffected by chemically diverse alpha(1)-AR antagonists, ARC239 and prazosin.
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Persistent activation of the alpha subunit of Gs promotes its removal from the plasma membrane.

TL;DR: It is demonstrated that Gs alpha need not remain associated invariantly with the plasma membrane, as assessed by cholera-toxin-catalysed ADP-ribosylation and by immunoblotting with an anti-peptide antiserum raised against the C-terminal decapeptide of forms of Gsalpha.