PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11281283-1 2000 The role of protein tyrosine phosphorylation during regulation of NO synthase (eNOS) activity in endothelial cells is poorly understood. Tyrosine 20-28 nitric oxide synthase 3 Bos taurus 79-83 8910295-3 1996 Treatment of BAEC with hydrogen peroxide and the protein tyrosine phosphatase inhibitor, sodium orthovanadate, increases eNOS tyrosine phosphorylation. Tyrosine 57-65 nitric oxide synthase 3 Bos taurus 121-125 9223444-0 1997 Caveolin-1 detergent solubility and association with endothelial nitric oxide synthase is modulated by tyrosine phosphorylation. Tyrosine 103-111 nitric oxide synthase 3 Bos taurus 53-86 9223444-7 1997 Agonist-activation of eNOS in endothelial cells thus appears to involve tyrosine phosphorylation-dependent changes in the interaction of eNOS with caveolin-1. Tyrosine 72-80 nitric oxide synthase 3 Bos taurus 22-26 9223444-7 1997 Agonist-activation of eNOS in endothelial cells thus appears to involve tyrosine phosphorylation-dependent changes in the interaction of eNOS with caveolin-1. Tyrosine 72-80 nitric oxide synthase 3 Bos taurus 137-141 8910295-0 1996 Endothelial nitric oxide synthase is regulated by tyrosine phosphorylation and interacts with caveolin-1. Tyrosine 50-58 nitric oxide synthase 3 Bos taurus 0-33 8910295-5 1996 Because eNOS is localized in plasmalemma caveolae, we examined if tyrosine phosphorylated eNOS interacts with caveolin-1, the coat protein of caveolae. Tyrosine 66-74 nitric oxide synthase 3 Bos taurus 90-94 8910295-2 1996 Here, we demonstrate that eNOS is tyrosine-phosphorylated in bovine aortic endothelial cells (BAEC) using 32P metabolic labeling followed by phosphoamino acid analysis and by phosphotyrosine specific Western blotting. Tyrosine 34-42 nitric oxide synthase 3 Bos taurus 26-30 8910295-7 1996 Conversely, immunoprecipitation of caveolin-1 resulted in the co-precipitation of tyrosine-phosphorylated eNOS. Tyrosine 82-90 nitric oxide synthase 3 Bos taurus 106-110 8910295-8 1996 Thus, tyrosine phosphorylation is a novel regulatory mechanism for eNOS and caveolin-1 is the first eNOS-associated protein. Tyrosine 6-14 nitric oxide synthase 3 Bos taurus 67-71 8910295-9 1996 Collectively, these observations provide a novel regulatory mechanism for eNOS and suggest that tyrosine phosphorylation may influence its activity, subcellular trafficking, and interaction with other caveolin-interacting proteins in caveolae. Tyrosine 96-104 nitric oxide synthase 3 Bos taurus 74-78 8831678-0 1996 Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton. Tyrosine 30-38 nitric oxide synthase 3 Bos taurus 64-97 8831678-6 1996 Treatment of BAEC with bradykinin or the tyrosine phosphatase inhibitor, phenylarsine oxide promotes tyrosine phosphorylation of detergent-insoluble, cytoskeletal proteins accompanied by translocation of eNOS to the cytoskeletal subcellular compartment. Tyrosine 41-49 nitric oxide synthase 3 Bos taurus 204-208 17028163-0 2007 TNF-alpha potentiates protein-tyrosine nitration through activation of NADPH oxidase and eNOS localized in membrane rafts and caveolae of bovine aortic endothelial cells. Tyrosine 30-38 nitric oxide synthase 3 Bos taurus 89-93 8831678-8 1996 Tyrosine phosphorylation-dependent association of eNOS with the cytoskeleton may have a role in targeting NO production to specific subcellular locations. Tyrosine 0-8 nitric oxide synthase 3 Bos taurus 50-54 17303569-0 2007 Phosphorylation of tyrosine 801 of vascular endothelial growth factor receptor-2 is necessary for Akt-dependent endothelial nitric-oxide synthase activation and nitric oxide release from endothelial cells. Tyrosine 19-27 nitric oxide synthase 3 Bos taurus 112-145 17303569-2 2007 Herein, we have attempted to determine which autophosphorylated tyrosine residue on the VEGFR-2 is essential for VEGF-mediated endothelial nitric-oxide synthase (eNOS) activation and NO production from endothelial cells. Tyrosine 64-72 nitric oxide synthase 3 Bos taurus 127-160 17303569-2 2007 Herein, we have attempted to determine which autophosphorylated tyrosine residue on the VEGFR-2 is essential for VEGF-mediated endothelial nitric-oxide synthase (eNOS) activation and NO production from endothelial cells. Tyrosine 64-72 nitric oxide synthase 3 Bos taurus 162-166 17303569-10 2007 We thus conclude that autophosphorylation of tyrosine residue 801 of the VEGFR-2 is essential for VEGF-stimulated NO production from endothelial cells, and this is primarily accomplished via the activation of phosphatidylinositol 3-kinase and Akt signaling to eNOS. Tyrosine 45-53 nitric oxide synthase 3 Bos taurus 260-264 16123043-0 2005 Src kinase activates endothelial nitric-oxide synthase by phosphorylating Tyr-83. Tyrosine 74-77 nitric oxide synthase 3 Bos taurus 21-54 16123043-1 2005 The endothelial nitric-oxide synthase (eNOS) is regulated in part by serine/threonine phosphorylation, but eNOS tyrosine phosphorylation is less well understood. Tyrosine 112-120 nitric oxide synthase 3 Bos taurus 107-111 12388315-6 2002 These results indicate that a simultaneous monitoring of [Ca(2+)](i) and intracellular NO production in the intact endothelium is a powerful tool to study Ca(2+)-dependent regulation of endothelial nitric oxide synthase, which provides the first direct evidence for a permissive role of Ca(2+) in tyrosine phosphorylation-induced NO production. Tyrosine 297-305 nitric oxide synthase 3 Bos taurus 186-219 16123043-2 2005 In the present study we have examined the tyrosine phosphorylation of eNOS in bovine aortic endothelial cells (BAECs) exposed to oxidant stress. Tyrosine 42-50 nitric oxide synthase 3 Bos taurus 70-74 16123043-3 2005 Hydrogen peroxide and pervanadate (PV) treatment stimulates eNOS tyrosine phosphorylation in BAECs. Tyrosine 65-73 nitric oxide synthase 3 Bos taurus 60-64 16123043-6 2005 Domain mapping and site-directed mutagenesis studies in COS-7 cells transfected with either eNOS alone and then treated with PV or cotransfected with eNOS and constitutively active v-Src identified Tyr-83 (bovine sequence) as the major eNOS tyrosine phosphorylation site. Tyrosine 198-201 nitric oxide synthase 3 Bos taurus 92-96 16123043-6 2005 Domain mapping and site-directed mutagenesis studies in COS-7 cells transfected with either eNOS alone and then treated with PV or cotransfected with eNOS and constitutively active v-Src identified Tyr-83 (bovine sequence) as the major eNOS tyrosine phosphorylation site. Tyrosine 198-201 nitric oxide synthase 3 Bos taurus 150-154 16123043-6 2005 Domain mapping and site-directed mutagenesis studies in COS-7 cells transfected with either eNOS alone and then treated with PV or cotransfected with eNOS and constitutively active v-Src identified Tyr-83 (bovine sequence) as the major eNOS tyrosine phosphorylation site. Tyrosine 198-201 nitric oxide synthase 3 Bos taurus 150-154 16123043-9 2005 Taken together, these data indicate that Src-mediated tyrosine phosphorylation of eNOS at Tyr-83 modulates eNOS activity in endothelial cells. Tyrosine 54-62 nitric oxide synthase 3 Bos taurus 82-86 16123043-9 2005 Taken together, these data indicate that Src-mediated tyrosine phosphorylation of eNOS at Tyr-83 modulates eNOS activity in endothelial cells. Tyrosine 54-62 nitric oxide synthase 3 Bos taurus 107-111 16123043-9 2005 Taken together, these data indicate that Src-mediated tyrosine phosphorylation of eNOS at Tyr-83 modulates eNOS activity in endothelial cells. Tyrosine 90-93 nitric oxide synthase 3 Bos taurus 82-86 16123043-9 2005 Taken together, these data indicate that Src-mediated tyrosine phosphorylation of eNOS at Tyr-83 modulates eNOS activity in endothelial cells. Tyrosine 90-93 nitric oxide synthase 3 Bos taurus 107-111