Characterization of the Roles of the 594–645 Region in Human Endothelial Nitric-oxide Synthase in Regulating Calmodulin Binding and Electron Transfer
Open Access
- 1 April 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (17) , 13155-13163
- https://doi.org/10.1074/jbc.275.17.13155
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Endothelial Nitric-oxide SynthasePublished by Elsevier ,1996
- Prokaryotic Expression of the Heme- and Flavin-Binding Domains of Rat Neuronal Nitric Oxide Synthase as Distinct Polypeptides: Identification of the Heme-Binding Proximal Thiolate Ligand as Cysteine-415Biochemistry, 1995
- Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interactionBiochemistry, 1995
- Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer.Proceedings of the National Academy of Sciences, 1993
- Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide.Proceedings of the National Academy of Sciences, 1992
- Cloning and Characterization of Inducible Nitric Oxide Synthase from Mouse MacrophagesScience, 1992
- Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells.Proceedings of the National Academy of Sciences, 1991
- Isoforms of nitric oxide synthase Characterization and purification from different cell typesBiochemical Pharmacology, 1991
- Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductaseNature, 1991
- Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.Proceedings of the National Academy of Sciences, 1990