메뉴 건너뛰기




Volumn 117, Issue 12, 2004, Pages 2427-2429

eNos at a glance

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; CALMODULIN; CASPASE 3; CASPASE 8; CAVEOLIN 1; COAT PROTEIN; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANYLATE CYCLASE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; NITRIC OXIDE DONOR; NITROUS OXIDE; OXIDOREDUCTASE; OXYGENASE; PHOSPHATIDYLINOSITOL 3 KINASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; VASCULOTROPIN;

EID: 3042730959     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01165     Document Type: Note
Times cited : (485)

References (27)
  • 1
    • 0042388672 scopus 로고    scopus 로고
    • Flow-dependent regulation of endothelial nitric oxide synthase: Role of protein kinases
    • Boo, Y. C. and Jo, H. (2003). Flow-dependent regulation of endothelial nitric oxide synthase: role of protein kinases. Am. J. Physiol. Cell Physiol. 285, C499-C508.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Boo, Y.C.1    Jo, H.2
  • 3
    • 0013578113 scopus 로고    scopus 로고
    • Shear stress stimulates the protein kinase Akt-involvement in the regulation of endothelial nitric oxide synthase
    • Dimmeler, S., Fissthaler, B., Fleming, I., Assmus, B., Hermann, C. and Zeiher, A. (1998). Shear stress stimulates the protein kinase Akt-involvement in the regulation of endothelial nitric oxide synthase. Circulation 98, I-312.
    • (1998) Circulation , vol.98
    • Dimmeler, S.1    Fissthaler, B.2    Fleming, I.3    Assmus, B.4    Hermann, C.5    Zeiher, A.6
  • 4
    • 0242552817 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinases and the cardiovascular system: Insights from genetically modified mice
    • Feil, R., Lohmann, S. M., de Jonge, H., Walter, U. and Hofmann, F. (2003). Cyclic GMP-dependent protein kinases and the cardiovascular system: insights from genetically modified mice. Circ. Res. 93, 907-916.
    • (2003) Circ. Res. , vol.93 , pp. 907-916
    • Feil, R.1    Lohmann, S.M.2    de Jonge, H.3    Walter, U.4    Hofmann, F.5
  • 5
    • 0035827676 scopus 로고    scopus 로고
    • Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity
    • Fleming, I., Fisslthaler, B., Dimmeler, S., Kemp, B. E. and Busse, R. (2001). Phosphorylation of Thr(495) regulates Ca(2+)/calmodulin-dependent endothelial nitric oxide synthase activity. Circ. Res. 88, E68-E75.
    • (2001) Circ. Res. , vol.88
    • Fleming, I.1    Fisslthaler, B.2    Dimmeler, S.3    Kemp, B.E.4    Busse, R.5
  • 7
    • 0035192750 scopus 로고    scopus 로고
    • Post-translational control of endothelial nitric oxide synthase: Why isn't calcium/ calmodulin enough?
    • Fulton, D., Gratton, J. P. and Sessa, W. C. (2001). Post-translational control of endothelial nitric oxide synthase: why isn't calcium/ calmodulin enough? J. Pharmacol. Exp. Ther. 299, 818-24.
    • (2001) J. Pharmacol. Exp. Ther. , vol.299 , pp. 818-824
    • Fulton, D.1    Gratton, J.P.2    Sessa, W.C.3
  • 8
    • 0029901663 scopus 로고    scopus 로고
    • Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling
    • García-Cardeña, G., Oh, P., Liu, J., Schnitzer, J. E. and Sessa, W. C. (1996). Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: Implications for nitric oxide signaling. Proc. Natl. Acad. Sci. USA 93, 6448-6453.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6448-6453
    • García-Cardeña, G.1    Oh, P.2    Liu, J.3    Schnitzer, J.E.4    Sessa, W.C.5
  • 9
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith, O. W. and Stuehr, D. J. (1995). Nitric oxide synthases: properties and catalytic mechanism. Annu. Rev. Physiol. 57, 707-736.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 10
    • 0035844241 scopus 로고    scopus 로고
    • Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation
    • Harris, M. B., Ju, H., Venema, V. J., Liang, H., Zou, R., Michell, B. J., Chen, Z. P., Kemp, B. E. and Venema, R. C. (2001). Reciprocal phosphorylation and regulation of endothelial nitric-oxide synthase in response to bradykinin stimulation. J. Biol. Chem. 276, 16587-16591.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16587-16591
    • Harris, M.B.1    Ju, H.2    Venema, V.J.3    Liang, H.4    Zou, R.5    Michell, B.J.6    Chen, Z.P.7    Kemp, B.E.8    Venema, R.C.9
  • 11
    • 0034644608 scopus 로고    scopus 로고
    • Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells
    • Haynes, M. P., Sinha, D., Russell, K. S., Collinge, M., Fulton, D., Morales-Ruiz, M., Sessa, W. C. and Bender, J. R. (2000). Membrane estrogen receptor engagement activates endothelial nitric oxide synthase via the PI3-kinase-Akt pathway in human endothelial cells. Circ. Res. 87, 677-682.
    • (2000) Circ. Res. , vol.87 , pp. 677-682
    • Haynes, M.P.1    Sinha, D.2    Russell, K.S.3    Collinge, M.4    Fulton, D.5    Morales-Ruiz, M.6    Sessa, W.C.7    Bender, J.R.8
  • 12
    • 0035965242 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate and isoform-specific activation of phosphoinositide 3-kinase beta. Evidence for divergence and convergence of receptor-regulated endothelial nitric-oxide synthase signaling pathways
    • Igarashi, J. and Michel, T. (2001). Sphingosine 1-phosphate and isoform-specific activation of phosphoinositide 3-kinase beta. Evidence for divergence and convergence of receptor-regulated endothelial nitric-oxide synthase signaling pathways. J. Biol. Chem. 276, 36281-36288.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36281-36288
    • Igarashi, J.1    Michel, T.2
  • 13
    • 1542782162 scopus 로고    scopus 로고
    • Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP
    • Jiang, J., Cyr, D., Babbitt, R. W., Sessa, W. C. and Patterson, C. (2003). Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP. J. Biol. Chem. 278, 49332-49341.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49332-49341
    • Jiang, J.1    Cyr, D.2    Babbitt, R.W.3    Sessa, W.C.4    Patterson, C.5
  • 14
    • 0037166321 scopus 로고    scopus 로고
    • 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
    • Lane, P. and Gross, S. S. (2002). 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. J. Biol. Chem. 277, 19087-19094.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19087-19094
    • Lane, P.1    Gross, S.S.2
  • 15
    • 0242666181 scopus 로고    scopus 로고
    • Phosphorylation of threonine 497 in endothelial nitric-oxide synthase coordinates the coupling of L-arginine metabolism to efficient nitric oxide production
    • Lin, M. I., Fulton, D., Babbitt, R., Fleming, I., Busse, R., Pritchard, K. A., Jr and Sessa, W. C. (2003). Phosphorylation of threonine 497 in endothelial nitric-oxide synthase coordinates the coupling of L-arginine metabolism to efficient nitric oxide production. J. Biol. Chem. 278, 44719-44726.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44719-44726
    • Lin, M.I.1    Fulton, D.2    Babbitt, R.3    Fleming, I.4    Busse, R.5    Pritchard Jr., K.A.6    Sessa, W.C.7
  • 16
    • 0028361984 scopus 로고
    • Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase
    • Liu, J. and Sessa, W. C. (1994). Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase. J. Biol. Chem. 269, 11691-11694.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11691-11694
    • Liu, J.1    Sessa, W.C.2
  • 17
    • 0029084761 scopus 로고
    • Biosynthesis and palmitoylation of endothelial nitric oxide synthase: Mutagenesis of palmitoylation sites, cysteines-15 and/or -26, argues against depalmitoylation-induced translocation of the enzyme
    • Liu, J., García-Cardeña, G. and Sessa, W. C. (1995). Biosynthesis and palmitoylation of endothelial nitric oxide synthase: mutagenesis of palmitoylation sites, cysteines-15 and/or -26, argues against depalmitoylation-induced translocation of the enzyme. Biochemistry 34, 12333-12340.
    • (1995) Biochemistry , vol.34 , pp. 12333-12340
    • Liu, J.1    García-Cardeña, G.2    Sessa, W.C.3
  • 18
    • 0030920365 scopus 로고    scopus 로고
    • The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the golgi region of cells: A green fluorescent protein study
    • Liu, J., Hughes, T. E. and Sessa, W. C. (1997). The first 35 amino acids and fatty acylation sites determine the molecular targeting of endothelial nitric oxide synthase into the golgi region of cells: a green fluorescent protein study. J. Cell Biol. 137, 1525-1535.
    • (1997) J. Cell Biol. , vol.137 , pp. 1525-1535
    • Liu, J.1    Hughes, T.E.2    Sessa, W.C.3
  • 19
    • 0034054493 scopus 로고    scopus 로고
    • Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation
    • McCabe, T. J., Fulton, D., Roman, L. J. and Sessa, W. C. (2000). Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation. J. Biol. Chem. 275, 6123-6128.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6123-6128
    • McCabe, T.J.1    Fulton, D.2    Roman, L.J.3    Sessa, W.C.4
  • 20
    • 0036829884 scopus 로고    scopus 로고
    • Identification of regulatory sites of phosphorylation of the bovine endothelial nitric-oxide synthase at serine 617 and serine 635
    • Michell, B. J., Harris, M. B., Chen, Z. P., Ju, H., Venema, V. J., Blackstone, M. A., Huang, W., Venema, R. C. and Kemp, B. E. (2002). Identification of regulatory sites of phosphorylation of the bovine endothelial nitric-oxide synthase at serine 617 and serine 635. J. Biol. Chem. 277, 42344-42351.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42344-42351
    • Michell, B.J.1    Harris, M.B.2    Chen, Z.P.3    Ju, H.4    Venema, V.J.5    Blackstone, M.A.6    Huang, W.7    Venema, R.C.8    Kemp, B.E.9
  • 21
    • 0037245344 scopus 로고    scopus 로고
    • Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS
    • Miranda, K. M., Nims, R. W., Thomas, D. D., Espey, M. G., Citrin, D., Bartberger, M. D., Paolocci, N., Fukuto, J. M., Feelisch, M. and Wink, D. A. (2003). Comparison of the reactivity of nitric oxide and nitroxyl with heme proteins. A chemical discussion of the differential biological effects of these redox related products of NOS. J. Inorg. Biochem. 93, 52-60.
    • (2003) J. Inorg. Biochem. , vol.93 , pp. 52-60
    • Miranda, K.M.1    Nims, R.W.2    Thomas, D.D.3    Espey, M.G.4    Citrin, D.5    Bartberger, M.D.6    Paolocci, N.7    Fukuto, J.M.8    Feelisch, M.9    Wink, D.A.10
  • 22
    • 0035374461 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate activates Akt, nitric oxide production, and chemotaxis through a Gi protein/phosphoinositide 3-kinase pathway in endothelial cells
    • Morales-Ruiz, M., Lee, M. J., Zollner, S., Gratton, J. P., Scotland, R., Shiojima, I., Walsh, K., Hla, T. and Sessa, W. C. (2001). Sphingosine 1-phosphate activates Akt, nitric oxide production, and chemotaxis through a Gi protein/phosphoinositide 3-kinase pathway in endothelial cells. J. Biol. Chem. 276, 19672-19677.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19672-19677
    • Morales-Ruiz, M.1    Lee, M.J.2    Zollner, S.3    Gratton, J.P.4    Scotland, R.5    Shiojima, I.6    Walsh, K.7    Hla, T.8    Sessa, W.C.9
  • 23
    • 0037168483 scopus 로고    scopus 로고
    • There's NO binding like NOS binding: Protein-protein interactions in NO/cGMP signaling
    • Nedvetsky, P. I., Sessa, W. C. and Schmidt, H. H. (2002). There's NO binding like NOS binding: protein-protein interactions in NO/cGMP signaling. Proc. Natl. Acad. Sci. USA 99, 16510-16512.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16510-16512
    • Nedvetsky, P.I.1    Sessa, W.C.2    Schmidt, H.H.3
  • 25
    • 0034727094 scopus 로고    scopus 로고
    • Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase
    • Simoncini, T., Hafezi-Moghadam, A., Brazil, D. P., Ley, K., Chin, W. W. and Liao, J. K. (2000). Interaction of oestrogen receptor with the regulatory subunit of phosphatidylinositol-3-OH kinase. Nature 407, 538-541.
    • (2000) Nature , vol.407 , pp. 538-541
    • Simoncini, T.1    Hafezi-Moghadam, A.2    Brazil, D.P.3    Ley, K.4    Chin, W.W.5    Liao, J.K.6
  • 26
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. the prototypic redox-based signaling mechanism
    • Stamler, J. S., Lamas, S. and Fang, F. C. (2001). Nitrosylation. the prototypic redox-based signaling mechanism. Cell 106, 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.