Phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca(2+) concentrations required for calmodulin to bind and activate the enzyme.
Tran, Quang-Kim
Phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca(2+) concentrations required for calmodulin to bind and activate the enzyme. [electronic resource] - Biochemistry Jul 2008 - 7557-66 p. digital
Publication Type: Journal Article
1520-4995
10.1021/bi8003186 doi
Animals
Binding Sites
Calcium--metabolism
Calmodulin--metabolism
Cattle
Cloning, Molecular
DNA Primers
Kinetics
Mutagenesis
Nitric Oxide Synthase Type III--antagonists & inhibitors
Phosphoproteins--metabolism
Phosphorylation
Protein Binding
Recombinant Proteins--metabolism
Phosphorylation within an autoinhibitory domain in endothelial nitric oxide synthase reduces the Ca(2+) concentrations required for calmodulin to bind and activate the enzyme. [electronic resource] - Biochemistry Jul 2008 - 7557-66 p. digital
Publication Type: Journal Article
1520-4995
10.1021/bi8003186 doi
Animals
Binding Sites
Calcium--metabolism
Calmodulin--metabolism
Cattle
Cloning, Molecular
DNA Primers
Kinetics
Mutagenesis
Nitric Oxide Synthase Type III--antagonists & inhibitors
Phosphoproteins--metabolism
Phosphorylation
Protein Binding
Recombinant Proteins--metabolism