Disabling a C-terminal autoinhibitory control element in endothelial nitric-oxide synthase by phosphorylation provides a molecular explanation for activation of vascular NO synthesis by diverse physiological stimuli. [electronic resource]
Producer: 20020624Description: 19087-94 p. digitalISSN:- 0021-9258
- Amino Acid Sequence
- Animals
- Base Sequence
- Calcium -- metabolism
- Calmodulin -- metabolism
- Catalysis
- Cattle
- DNA Primers
- Endothelium, Vascular -- enzymology
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Nitric Oxide -- biosynthesis
- Nitric Oxide Synthase -- antagonists & inhibitors
- Nitric Oxide Synthase Type III
- Phosphorylation
- Recombinant Proteins -- antagonists & inhibitors
- Sequence Homology, Amino Acid
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Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
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