Identification of Regulatory Sites of Phosphorylation of the Bovine Endothelial Nitric-oxide Synthase at Serine 617 and Serine 635
Open Access
- 1 November 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (44) , 42344-42351
- https://doi.org/10.1074/jbc.m205144200
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Insulin-stimulated Activation of eNOS Is Independent of Ca2+ but Requires Phosphorylation by Akt at Ser1179Journal of Biological Chemistry, 2001
- Bradykinin-regulated Interactions of the Mitogen-activated Protein Kinase Pathway with the Endothelial Nitric-oxide SynthaseJournal of Biological Chemistry, 2000
- Enhanced Electron Flux and Reduced Calmodulin Dissociation May Explain “Calcium-independent” eNOS Activation by PhosphorylationJournal of Biological Chemistry, 2000
- The Akt kinase signals directly to endothelial nitric oxide synthaseCurrent Biology, 1999
- AMP‐activated protein kinase phosphorylation of endothelial NO synthaseFEBS Letters, 1999
- Posttranslational Modifications of the 5′-AMP-activated Protein Kinase β1 SubunitJournal of Biological Chemistry, 1997
- Identification, Characterization, and Comparison of the Calmodulin-binding Domains of the Endothelial and Inducible Nitric Oxide SynthasesPublished by Elsevier ,1996
- Wortmannin as a unique probe for an intracellular signalling protein, phosphoinositide 3-kinaseTrends in Biochemical Sciences, 1995
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- K-252 compounds, novel and potent inhibitors of protein kinase C and cyclic nucleotide-dependent protein kinasesBiochemical and Biophysical Research Communications, 1986