메뉴 건너뛰기




Volumn 392, Issue 6678, 1998, Pages 821-824

Dynamic activation of endothelial nitric oxide synthase by Hsp90

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 90; NITRIC OXIDE SYNTHASE;

EID: 0009621605     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/33934     Document Type: Article
Times cited : (888)

References (30)
  • 1
    • 0028618296 scopus 로고
    • Protein folding and the regulation of signaling pathways
    • Rutherford, S. L. & Zucker, C. S. Protein folding and the regulation of signaling pathways. Cell 79, 1129-1132 (1994).
    • (1994) Cell , vol.79 , pp. 1129-1132
    • Rutherford, S.L.1    Zucker, C.S.2
  • 2
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J. L. & Craig, E. A. Protein folding in vivo: unraveling complex pathways. Cell 90, 201-204 (1997).
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 3
    • 0030982641 scopus 로고    scopus 로고
    • The role of the Hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase
    • Pratt, W. B. The role of the Hsp90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase. Annu. Rev. Pharmacol. Toxicol. 37, 297-326 (1997).
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 297-326
    • Pratt, W.B.1
  • 4
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W. B. & Toft, D. O. Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocrinol Rev. 18, 306-360 (1997).
    • (1997) Endocrinol Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 5
    • 0028999582 scopus 로고
    • Hold'em and fold'm: Chaperones and signal transduction
    • Bohen, S. P., Kralli, A. & Yamamoto, K. R. Hold'em and fold'm: chaperones and signal transduction. Science 268, 1303-1304 (1995).
    • (1995) Science , vol.268 , pp. 1303-1304
    • Bohen, S.P.1    Kralli, A.2    Yamamoto, K.R.3
  • 6
    • 0029037110 scopus 로고
    • Mutational analysis of Hsp90 function: Interactions with a steroid receptor and a protein kinase
    • Nathan, D. F. & Lindquist, S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 15, 3917-3925 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3917-3925
    • Nathan, D.F.1    Lindquist, S.2
  • 8
    • 0028363670 scopus 로고
    • Mutations in Hsp83 and cdc37 impair signaling by the Sevenless receptor tyrosine kinase in Drosophila
    • Cutforth, T. & Rubin, G. M. Mutations in Hsp83 and cdc37 impair signaling by the Sevenless receptor tyrosine kinase in Drosophila. Cell 77, 1027-1036 (1994).
    • (1994) Cell , vol.77 , pp. 1027-1036
    • Cutforth, T.1    Rubin, G.M.2
  • 9
    • 0027193228 scopus 로고
    • Torso, a receptor tyrosine kinase required for embryonic pattern formation, shares substrates with the Sevenless and EGF-R pathways in Drosophila
    • Doyle, H. J. & Bishop, J. M. Torso, a receptor tyrosine kinase required for embryonic pattern formation, shares substrates with the Sevenless and EGF-R pathways in Drosophila. Genes Dev. 7, 633-646 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 633-646
    • Doyle, H.J.1    Bishop, J.M.2
  • 10
    • 0030896688 scopus 로고    scopus 로고
    • The heat shock protein 83 (Hsp83) is required for Raf-mediated signaling in Drosophila
    • Van der Straten, A., Rommel, C., Dickson, B. & Hafen, E. The heat shock protein 83 (Hsp83) is required for Raf-mediated signaling in Drosophila. EMBO J. 16, 1961-1969 (1997).
    • (1997) EMBO J. , vol.16 , pp. 1961-1969
    • Van Der Straten, A.1    Rommel, C.2    Dickson, B.3    Hafen, E.4
  • 11
    • 0028092958 scopus 로고
    • Nitric oxide synthases: Roles, tolls, and controls
    • Nathan, C. & Xie, Q.-W. Nitric oxide synthases: roles, tolls, and controls. Cell 78, 915-918 (1994).
    • (1994) Cell , vol.78 , pp. 915-918
    • Nathan, C.1    Xie, Q.-W.2
  • 12
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology and pharmacology
    • Moncada, S., Palmer, R. M. J. & Higgs, E. A. Nitric oxide: physiology, pathophysiology and pharmacology. Pharmacol. Rev. 43, 109-142 (1991).
    • (1991) Pharmacol. Rev. , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.J.2    Higgs, E.A.3
  • 13
    • 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. & Sessa, W. C. 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).
    • (1995) Biochemistry , vol.34 , pp. 12333-12340
    • Liu, J.1    García-Cardeña, G.2    Sessa, W.C.3
  • 14
    • 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. & Sessa, W. C. 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).
    • (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
  • 15
    • 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. & Sessa, W. C. 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).
    • (1997) J. Cell Biol. , vol.137 , pp. 1525-1535
    • Liu, J.1    Hughes, T.E.2    Sessa, W.C.3
  • 16
    • 0029910141 scopus 로고    scopus 로고
    • Endothelial nitric oxide is regulated by tyrosine phosphorylation and interacts with caveolin-1
    • García-Cardeña, G., Fan, R., Stern, D. F., Liu, J. & Sessa, W. C. Endothelial nitric oxide is regulated by tyrosine phosphorylation and interacts with caveolin-1. J. Biol. Chem. 271, 27237-27240 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 27237-27240
    • García-Cardeña, G.1    Fan, R.2    Stern, D.F.3    Liu, J.4    Sessa, W.C.5
  • 17
    • 2642611234 scopus 로고    scopus 로고
    • Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton
    • Venema, V. J., Marrero, M. B. & Venema, R. C. Bradykinin-stimulated protein tyrosine phosphorylation promotes endothelial nitric oxide synthase translocation to the cytoskeleton. Biochem. Biophys. Res. Commun. 155, 801-807 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , vol.155 , pp. 801-807
    • Venema, V.J.1    Marrero, M.B.2    Venema, R.C.3
  • 19
    • 0028240645 scopus 로고
    • The nitric oxide synthase family of proteins
    • Sessa, W. C. The nitric oxide synthase family of proteins. J. Vasc. Res. 31, 131-143 (1994).
    • (1994) J. Vasc. Res. , vol.31 , pp. 131-143
    • Sessa, W.C.1
  • 20
    • 0030042761 scopus 로고    scopus 로고
    • Nitric oxide mediates mitogenic effect of VEGF on coronary venular endothelium
    • Morbidelli, L. et al. Nitric oxide mediates mitogenic effect of VEGF on coronary venular endothelium. Am. J. Physiol. 270, H411-H415 (1996).
    • (1996) Am. J. Physiol. , vol.270
    • Morbidelli, L.1
  • 21
    • 0029072762 scopus 로고
    • Flow-mediated endothelial mechanotransduction
    • Davies, P. F. Flow-mediated endothelial mechanotransduction. Physiol. Rev. 75, 519-560 (1995).
    • (1995) Physiol. Rev. , vol.75 , pp. 519-560
    • Davies, P.F.1
  • 22
    • 0025239467 scopus 로고
    • Spontaneous transformation and immortalization of human endothelial cells in vitro
    • Takahashi, K., Sawasaki, Y., Hata, J.-I., Mukai, K. & Goto, T. Spontaneous transformation and immortalization of human endothelial cells in vitro. Cell. Dev. Biol. 25, 265-274 (1990).
    • (1990) Cell. Dev. Biol. , vol.25 , pp. 265-274
    • Takahashi, K.1    Sawasaki, Y.2    Hata, J.-I.3    Mukai, K.4    Goto, T.5
  • 23
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C. E. et al. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell 89, 239-250 (1997).
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1
  • 24
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert, J. P. et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem. 272, 23843-23850 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 23843-23850
    • Grenert, J.P.1
  • 25
    • 0025011716 scopus 로고
    • Characterization of three inhibitors of endothelial nitric oxide synthase in vitro and in vivo
    • Rees, D. D., Palmer, R. M. J., Schulz, R., Hodson, H. F. & Moncada, S. Characterization of three inhibitors of endothelial nitric oxide synthase in vitro and in vivo. Br. J. Pharmacol. 101, 746-752 (1990).
    • (1990) Br. J. Pharmacol. , vol.101 , pp. 746-752
    • Rees, D.D.1    Palmer, R.M.J.2    Schulz, R.3    Hodson, H.F.4    Moncada, S.5
  • 28
    • 0021972202 scopus 로고
    • Flow effects on prostacyclin production by cultured human endothelial cells
    • Frangos, J. A., Eskin, S. G., McIntire, L. V. & Ives, C. L. Flow effects on prostacyclin production by cultured human endothelial cells. Science 227, 1477-1479 (1985).
    • (1985) Science , vol.227 , pp. 1477-1479
    • Frangos, J.A.1    Eskin, S.G.2    McIntire, L.V.3    Ives, C.L.4
  • 29
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott, R. F. & Zawadzki, J. V. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 288, 373-376 (1980).
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 30
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C. et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75 (1997).
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.