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We show that Ca 2+ /calmodulin(CaM)-dependent protein kinase I (CaMKI) is directly inhibited by its S-glutathionylation at the Cys 179 . In vitro studies demonstrated that treatment of CaMKI with diamide and glutathione results in inactivation of the enzyme, with a concomitant S-glutathionylation of CaMKI at Cys 179 detected by mass spectrometry. Mutagenesis studies confirmed...
We demonstrate here that neuronal nitric-oxide synthase (nNOS) is phosphorylated and inhibited by a constitutively active form of Ca 2+ /calmodulin (CaM)-dependent protein kinase I (CaM-K I1-293). Substitution of Ser 741 to Ala in nNOS blocked the phosphorylation and the inhibitory effect. Mimicking phosphorylation at Ser 741 by Ser to Asp mutation...
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