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- W2137402014 abstract "The development of new analytical methods, aimed at profiling G protein-coupled receptor (GPCR) ligands, regardless of the G protein-coupling pattern of their respective receptor, remains a key goal in drug discovery. Considerable evidence has recently revived the central role that could be played by extracellular-signal-regulated kinase (ERK), the cornerstone protein kinase of the first tyrosine kinase receptor-mediated pathway identified, in response to the activation of various types of GPCRs. Here we reveal a conceptual study in which the potential of ERK phosphorylation is evaluated as a generic readout in response to three different receptors activating three main classes of G proteins: Gαs, Gαi and Gα q. GPCR-mediated ERK phosphorylation was compared with different readouts such as GTPγ S, CAMP, or Ca2 +. We propose the measurement of GPCR-activated ERK phosphorylation as an alternative assay to better understand the molecular pharmacology of ligands of promiscuous GPCRs." @default.
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- W2137402014 date "2007-01-01" @default.
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- W2137402014 title "G Protein-Coupled Receptor-Mediated ERK1/2 Phosphorylation: Towards a Generic Sensor of GPCR Activation" @default.
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- W2137402014 doi "https://doi.org/10.1080/10799890601112244" @default.
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