Sub‐family selective actions in the ability of Erk2 MAP kinase to phosphorylate and regulate the activity of PDE4 cyclic AMP‐specific phosphodiesterases

Expressed in intact cells and in vitro, PDE4B and PDE4C isoenzymes of cyclic nucleotide phosphodiesterase (PDE), in common with PDE4D isoenzymes, are shown to provide substrates for C‐terminal catalytic unit phosphorylation by the extracellular signal‐regulated kinase Erk2 (p42MAPK). In contrast, PD...

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Veröffentlicht in:British journal of pharmacology 2000-10, Vol.131 (4), p.811-819
Hauptverfasser: Baillie, George S, MacKenzie, Simon J, McPhee, Ian, Houslay, Miles D
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Sprache:eng
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