메뉴 건너뛰기




Volumn 43, Issue 3, 1999, Pages 521-531

Enzymatic function of nitric oxide synthases

Author keywords

Endothelial factors; Endothelial function; Free radicals; Nitric oxide; Vasoconstriction dilation

Indexed keywords

ANION; ARGININE; CALCIUM ION; CALMODULIN; CITRULLINE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; FREE RADICAL; HEME; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; OXYGENASE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE; TETRAHYDROBIOPTERIN;

EID: 0033567065     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(99)00115-7     Document Type: Review
Times cited : (613)

References (135)
  • 1
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer R.M.J., Ferige A.G., Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature. 327:1987;524-526.
    • (1987) Nature , vol.327 , pp. 524-526
    • Palmer, R.M.J.1    Ferige, A.G.2    Moncada, S.3
  • 2
    • 0025731835 scopus 로고
    • Nitric oxide: An endogenous modulator of leukocyte adhesion
    • Kubes P., Suzuki M., Granger D.N. Nitric oxide: an endogenous modulator of leukocyte adhesion. Proc Natl Acad Sci USA. 88:1991;4651-4655.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4651-4655
    • Kubes, P.1    Suzuki, M.2    Granger, D.N.3
  • 3
    • 0026082745 scopus 로고
    • Modulation of platelet aggregation by an L-arginine-nitric oxide pathway
    • Radomski M.W., Palmer R.M.J., Moncada S. Modulation of platelet aggregation by an L-arginine-nitric oxide pathway. Trends Pharmacol Sci. 12:1991;87-88.
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 87-88
    • Radomski, M.W.1    Palmer, R.M.J.2    Moncada, S.3
  • 4
    • 0027298232 scopus 로고
    • The endothelium as a regulator of vascular smooth muscle proliferation
    • Scott-Burden T., Vanhoutte P.M. The endothelium as a regulator of vascular smooth muscle proliferation. Circulation. 87:(Suppl V):1993;V51-V55.
    • (1993) Circulation , vol.87 , Issue.SUPPL. V
    • Scott-Burden, T.1    Vanhoutte, P.M.2
  • 5
    • 0030694038 scopus 로고    scopus 로고
    • Biosynthesis and action of nitric oxide in mammalian cells
    • Mayer B., Hemmens B. Biosynthesis and action of nitric oxide in mammalian cells. Trends Biochem Sci. 22:1997;477-481.
    • (1997) Trends Biochem Sci , vol.22 , pp. 477-481
    • Mayer, B.1    Hemmens, B.2
  • 7
    • 0030988217 scopus 로고    scopus 로고
    • Structure-function aspects in the nitric oxide synthases
    • Stuehr D.J. Structure-function aspects in the nitric oxide synthases. Annu Rev Pharmacol Toxicol. 37:1997;339-359.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 339-359
    • Stuehr, D.J.1
  • 8
    • 0029914567 scopus 로고    scopus 로고
    • Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells
    • Ayajiki K., Kindermann M., Hecker M., Fleming I., Busse R. Intracellular pH and tyrosine phosphorylation but not calcium determine shear stress-induced nitric oxide production in native endothelial cells. Circ Res. 78:1996;750-758.
    • (1996) Circ Res , vol.78 , pp. 750-758
    • Ayajiki, K.1    Kindermann, M.2    Hecker, M.3    Fleming, I.4    Busse, R.5
  • 9
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith O.W., Stuehr D.J. Nitric oxide synthases: Properties and catalytic mechanism. Annu Rev Physiol. 57:1995;707-736.
    • (1995) Annu Rev Physiol , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 10
    • 0028234359 scopus 로고
    • On the mechanism of the nitric oxide synthase-catalyzed conversion of Nω-hydroxy-L-arginine to citrulline and nitric oxide
    • Korth H.-G., Sustmann R., Thater C., Butler A.R., Ingold K.U. On the mechanism of the nitric oxide synthase-catalyzed conversion of Nω-hydroxy-L-arginine to citrulline and nitric oxide. J Biol Chem. 269:1994;17776-17779.
    • (1994) J Biol Chem , vol.269 , pp. 17776-17779
    • Korth, H.-G.1    Sustmann, R.2    Thater, C.3    Butler, A.R.4    Ingold, K.U.5
  • 11
    • 0027325255 scopus 로고
    • Nitric oxide synthase structure and mechanism
    • Marletta M.A. Nitric oxide synthase structure and mechanism. J Biol Chem. 268:1993;12231-12234.
    • (1993) J Biol Chem , vol.268 , pp. 12231-12234
    • Marletta, M.A.1
  • 12
    • 0030766384 scopus 로고    scopus 로고
    • Analysis of neuronal NO synthase under single-turnover conditions: Conversion of Nω-hydroxyarginine to nitric oxide and citrulline
    • Abu-Soud H.M., Presta A., Mayer B., Stuehr D.J. Analysis of neuronal NO synthase under single-turnover conditions: conversion of Nω-hydroxyarginine to nitric oxide and citrulline. Biochemistry. 36:1997;10811-10816.
    • (1997) Biochemistry , vol.36 , pp. 10811-10816
    • Abu-Soud, H.M.1    Presta, A.2    Mayer, B.3    Stuehr, D.J.4
  • 13
    • 0025848403 scopus 로고
    • Brain nitric oxide synthase is a biopterin- And flavin-containing multi-functional oxido-reductase
    • Mayer B., John M., Heinzel B., et al. Brain nitric oxide synthase is a biopterin- and flavin-containing multi-functional oxido-reductase. FEBS Lett. 288:1991;187-191.
    • (1991) FEBS Lett , vol.288 , pp. 187-191
    • Mayer, B.1    John, M.2    Heinzel, B.3
  • 14
    • 0026584089 scopus 로고
    • 2+/calmodulin-dependent formation of hydrogen peroxide by brain nitric oxide synthase
    • 2+/calmodulin-dependent formation of hydrogen peroxide by brain nitric oxide synthase. Biochem J. 281:1992;627-630.
    • (1992) Biochem J , vol.281 , pp. 627-630
    • Heinzel, B.1    John, M.2    Klatt, P.3    Böhme, E.4    Mayer, B.5
  • 15
    • 0030872552 scopus 로고    scopus 로고
    • L-arginine treatment alters the kinetics of nitric oxide and superoxide release and reduces ischemia/reperfusion injury in skeletal muscle
    • Huk I., Nanobashvili J., Neumayer C., et al. L-arginine treatment alters the kinetics of nitric oxide and superoxide release and reduces ischemia/reperfusion injury in skeletal muscle. Circulation. 96:1997;667-675.
    • (1997) Circulation , vol.96 , pp. 667-675
    • Huk, I.1    Nanobashvili, J.2    Neumayer, C.3
  • 16
    • 0025892441 scopus 로고
    • Nω-Hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-Arginine
    • Stuehr D.J., Kwon N.S., Nathan C.F., et al. Nω-Hydroxy-L-arginine is an intermediate in the biosynthesis of nitric oxide from L-Arginine. J Biol Chem. 266:1991;6259-6263.
    • (1991) J Biol Chem , vol.266 , pp. 6259-6263
    • Stuehr, D.J.1    Kwon, N.S.2    Nathan, C.F.3
  • 17
    • 0028911054 scopus 로고
    • Macrophage NO synthase: Characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction
    • Ghosh D.K., Stuehr D.J. Macrophage NO synthase: Characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction. Biochemistry. 34:1995;801-807.
    • (1995) Biochemistry , vol.34 , pp. 801-807
    • Ghosh, D.K.1    Stuehr, D.J.2
  • 19
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism: Activation of intra- And interdomain electron transfer
    • Abu-Soud H.M., Yoho L.L., Stuehr D.J. Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism: Activation of intra- and interdomain electron transfer. J Biol Chem. 269:1994;32047-32050.
    • (1994) J Biol Chem , vol.269 , pp. 32047-32050
    • Abu-Soud, H.M.1    Yoho, L.L.2    Stuehr, D.J.3
  • 20
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P450 reductase
    • Bredt D.S., Hwang P.M., Glatt C.E., et al. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P450 reductase. Nature. 351:1991;714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3
  • 21
    • 0028097287 scopus 로고
    • Carboxyl terminus of inducible nitric oxide synthase: Contribution to NADPH binding and enzymatic activity
    • Xie Q., Cho H., Kashiwabara Y., et al. Carboxyl terminus of inducible nitric oxide synthase: Contribution to NADPH binding and enzymatic activity. J Biol Chem. 269:1994;28500-28505.
    • (1994) J Biol Chem , vol.269 , pp. 28500-28505
    • Xie, Q.1    Cho, H.2    Kashiwabara, Y.3
  • 22
    • 0030568829 scopus 로고    scopus 로고
    • Reductase domain cysteines 1048 and 1114 are critical for catalytic activity of human endothelial cell nitric oxide synthase as probed by site-directed mutagenesis
    • Zhang J.L., Patel J.M., Li Y.D., Block E.R. Reductase domain cysteines 1048 and 1114 are critical for catalytic activity of human endothelial cell nitric oxide synthase as probed by site-directed mutagenesis. Biochem Biophys Res Commun. 226:1996;293-300.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 293-300
    • Zhang, J.L.1    Patel, J.M.2    Li, Y.D.3    Block, E.R.4
  • 23
    • 0028848093 scopus 로고
    • Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity
    • Chen P.-F., Tsai A.-L., Wu K.K. Cysteine 99 of endothelial nitric oxide synthase (NOS-III) is critical for tetrahydrobiopterin-dependent NOS-III stability and activity. Biochem Biophys Res Commun. 215:1995;1119-1129.
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 1119-1129
    • Chen, P.-F.1    Tsai, A.-L.2    Wu, K.K.3
  • 24
    • 0029558027 scopus 로고
    • Inducible nitric oxide synthase: Identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin
    • Cho H.J., Martin E., Xie Q.W., Sassa S., Nathan C. Inducible nitric oxide synthase: Identification of amino acid residues essential for dimerization and binding of tetrahydrobiopterin. Proc Natl Acad Sci USA. 92:1995;11514-11518.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11514-11518
    • Cho, H.J.1    Martin, E.2    Xie, Q.W.3    Sassa, S.4    Nathan, C.5
  • 25
    • 0029033858 scopus 로고
    • Modular structure of neuronal nitric oxide synthase: Localization of the arginine binding site and modulation by pterin
    • Nishimura J., Martasek P., McMillan K., et al. Modular structure of neuronal nitric oxide synthase: Localization of the arginine binding site and modulation by pterin. Biochem Biophys Res Commun. 210:1995;288-294.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 288-294
    • Nishimura, J.1    Martasek, P.2    McMillan, K.3
  • 26
    • 0030917621 scopus 로고    scopus 로고
    • Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding
    • Gachhui R., Ghosh D.K., Wu C., et al. Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding. Biochemistry. 36:1997;5097-5103.
    • (1997) Biochemistry , vol.36 , pp. 5097-5103
    • Gachhui, R.1    Ghosh, D.K.2    Wu, C.3
  • 27
    • 0030889046 scopus 로고    scopus 로고
    • Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers
    • Chen P.-F., Tsai A.L., Berka V., Wu K.K. Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers. J Biol Chem. 272:1997;6114-6118.
    • (1997) J Biol Chem , vol.272 , pp. 6114-6118
    • Chen, P.-F.1    Tsai, A.L.2    Berka, V.3    Wu, K.K.4
  • 28
    • 0032563106 scopus 로고    scopus 로고
    • Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer
    • Siddhanta U., Presta A., Fan B., et al. Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer. J Biol Chem. 273:1998;18950-18958.
    • (1998) J Biol Chem , vol.273 , pp. 18950-18958
    • Siddhanta, U.1    Presta, A.2    Fan, B.3
  • 29
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane B.R., Arvai A.S., Ghosh D.K., et al. Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. Science. 279:1998;2121-2126.
    • (1998) Science , vol.279 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3
  • 30
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • Raman C.S., Li H., Martásek P., et al. Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center. Cell. 95:1998;939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martásek, P.3
  • 31
    • 0029929385 scopus 로고    scopus 로고
    • Characterisation of heme-deficient neuronal nitric oxide synthase reveals a role for heme in subunit dimerisation and binding of the amino acid substrate and tetrahydrobiopterin
    • Klatt P., Pfeiffer S., List B.M., et al. Characterisation of heme-deficient neuronal nitric oxide synthase reveals a role for heme in subunit dimerisation and binding of the amino acid substrate and tetrahydrobiopterin. J Biol Chem. 271:1996;7336-7342.
    • (1996) J Biol Chem , vol.271 , pp. 7336-7342
    • Klatt, P.1    Pfeiffer, S.2    List, B.M.3
  • 32
    • 0027441142 scopus 로고
    • Macrophage nitric oxide synthase subunits: Purification, characterisation, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme
    • Baek K.J., Thiel B.A., Lucas S., Stuehr D.J. Macrophage nitric oxide synthase subunits: Purification, characterisation, and role of prosthetic groups and substrate in regulating their association into a dimeric enzyme. J Biol Chem. 268:1993;21120-21129.
    • (1993) J Biol Chem , vol.268 , pp. 21120-21129
    • Baek, K.J.1    Thiel, B.A.2    Lucas, S.3    Stuehr, D.J.4
  • 33
    • 0030948345 scopus 로고    scopus 로고
    • Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: Tetrahydrobiopterin binding kinetics and role of haem in dimerization
    • List B.M., Klösch B., Völker C., et al. Characterization of bovine endothelial nitric oxide synthase as a homodimer with down-regulated uncoupled NADPH oxidase activity: tetrahydrobiopterin binding kinetics and role of haem in dimerization. Biochem J. 323:1997;159-165.
    • (1997) Biochem J , vol.323 , pp. 159-165
    • List, B.M.1    Klösch, B.2    Völker, C.3
  • 34
    • 0028043460 scopus 로고
    • Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity
    • Chen P., Tsai A., Wu K.K. Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity. J Biol Chem. 269:1994;25062-25066.
    • (1994) J Biol Chem , vol.269 , pp. 25062-25066
    • Chen, P.1    Tsai, A.2    Wu, K.K.3
  • 35
    • 0030009008 scopus 로고    scopus 로고
    • Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes
    • Xie Q.-W., Leung M., Fuortes M., Sassa S., Nathan C. Complementation analysis of mutants of nitric oxide synthase reveals that the active site requires two hemes. Proc Natl Acad Sci USA. 93:1996;4891-4896.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4891-4896
    • Xie, Q.-W.1    Leung, M.2    Fuortes, M.3    Sassa, S.4    Nathan, C.5
  • 36
    • 0028601409 scopus 로고
    • Characterization of neuronal nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system
    • Richards M.K., Marletta M.A. Characterization of neuronal nitric oxide synthase and a C415H mutant, purified from a baculovirus overexpression system. Biochemistry. 33:1994;14723-14732.
    • (1994) Biochemistry , vol.33 , pp. 14723-14732
    • Richards, M.K.1    Marletta, M.A.2
  • 37
    • 0032103447 scopus 로고    scopus 로고
    • Haem insertion, dimerization and reactivation of haem-free rat neuronal nitric oxide synthase
    • Hemmens B., Gorren A.C.F., Schmidt K., Werner E.R., Mayer B. Haem insertion, dimerization and reactivation of haem-free rat neuronal nitric oxide synthase. Biochem J. 332:1998;337-342.
    • (1998) Biochem J , vol.332 , pp. 337-342
    • Hemmens, B.1    Gorren, A.C.F.2    Schmidt, K.3    Werner, E.R.4    Mayer, B.5
  • 38
    • 0032535511 scopus 로고    scopus 로고
    • Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization
    • Brunner K., Tortschanoff A., Hemmens B., et al. Sensitivity of flavin fluorescence dynamics in neuronal nitric oxide synthase to cofactor-induced conformational changes and dimerization. Biochemistry. 37:1998;17545-17553.
    • (1998) Biochemistry , vol.37 , pp. 17545-17553
    • Brunner, K.1    Tortschanoff, A.2    Hemmens, B.3
  • 39
    • 0027337784 scopus 로고
    • Oxidation of N-hydroxy-L-Arg by nitric oxide synthase: Evidence for involvement of heme in catalysis
    • Pufahl R.A., Marletta M.A. Oxidation of N-hydroxy-L-Arg by nitric oxide synthase: Evidence for involvement of heme in catalysis. Biochem Biophys Res Commun. 193:1993;963-970.
    • (1993) Biochem Biophys Res Commun , vol.193 , pp. 963-970
    • Pufahl, R.A.1    Marletta, M.A.2
  • 40
    • 0031416373 scopus 로고    scopus 로고
    • Substrate binding and calmodulin binding to endothelial nitric oxide synthase co-regulate its enzymatic activity
    • Presta A., Liu J., Sessa W.C., Stuehr D.J. Substrate binding and calmodulin binding to endothelial nitric oxide synthase co-regulate its enzymatic activity. Nitric Oxide. 1:1997;74-87.
    • (1997) Nitric Oxide , vol.1 , pp. 74-87
    • Presta, A.1    Liu, J.2    Sessa, W.C.3    Stuehr, D.J.4
  • 41
    • 0028580205 scopus 로고
    • Electron transfer in the nitric-oxide synthases. Characterization of L-arginine analogs that block heme iron reduction
    • Abu-Soud H.M., Feldman P.L., Clark P., Stuehr D.J. Electron transfer in the nitric-oxide synthases. Characterization of L-arginine analogs that block heme iron reduction. J Biol Chem. 269:1994;32318-32326.
    • (1994) J Biol Chem , vol.269 , pp. 32318-32326
    • Abu-Soud, H.M.1    Feldman, P.L.2    Clark, P.3    Stuehr, D.J.4
  • 42
    • 0029808057 scopus 로고    scopus 로고
    • Binding of intermediate, product, and substrate analogs to neuronal nitric oxide synthase: Ferriheme is sensitive to ligand-specific effects in the L-arginine binding site
    • Salerno J.C., McMillan K., Masters B.S. Binding of intermediate, product, and substrate analogs to neuronal nitric oxide synthase: ferriheme is sensitive to ligand-specific effects in the L-arginine binding site. Biochemistry. 35:1996;11839-11845.
    • (1996) Biochemistry , vol.35 , pp. 11839-11845
    • Salerno, J.C.1    McMillan, K.2    Masters, B.S.3
  • 43
    • 0027442932 scopus 로고
    • Optical difference spectrophotometry as a probe of rat brain nitric oxide synthase heme-substrate interaction
    • McMillan K., Masters B.S.S. Optical difference spectrophotometry as a probe of rat brain nitric oxide synthase heme-substrate interaction. Biochemistry. 32:1993;9875-9880.
    • (1993) Biochemistry , vol.32 , pp. 9875-9880
    • McMillan, K.1    Masters, B.S.S.2
  • 44
    • 0029975203 scopus 로고    scopus 로고
    • Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase
    • Sennequier N., Stuehr D.J. Analysis of substrate-induced electronic, catalytic, and structural changes in inducible NO synthase. Biochemistry. 35:1996;5883-5892.
    • (1996) Biochemistry , vol.35 , pp. 5883-5892
    • Sennequier, N.1    Stuehr, D.J.2
  • 45
    • 0029889353 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation
    • Rodríguez-Crespo I., Gerber N.C., OrtizdeMontellano P.R. Endothelial nitric-oxide synthase. Expression in Escherichia coli, spectroscopic characterization, and role of tetrahydrobiopterin in dimer formation. J Biol Chem. 271:1996;11462-11467.
    • (1996) J Biol Chem , vol.271 , pp. 11462-11467
    • Rodríguez-Crespo, I.1    Gerber, N.C.2    Ortizdemontellano, P.R.3
  • 46
    • 0029892990 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: Binding of ligands at the arginine site induces changes in the heme ligation geometry
    • Salerno J.C., Martasek P., Roman L.J., Masters B.S. Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: binding of ligands at the arginine site induces changes in the heme ligation geometry. Biochemistry. 35:1996;7626-7630.
    • (1996) Biochemistry , vol.35 , pp. 7626-7630
    • Salerno, J.C.1    Martasek, P.2    Roman, L.J.3    Masters, B.S.4
  • 47
    • 0030464496 scopus 로고    scopus 로고
    • Tetrahydrobiopterin-free neuronal nitric oxide synthase: Evidence for two identical highly anticooperative pteridine binding sites
    • Gorren A.C.F., List B.M., Schrammel A., et al. Tetrahydrobiopterin-free neuronal nitric oxide synthase: Evidence for two identical highly anticooperative pteridine binding sites. Biochemistry. 35:1996;16735-16745.
    • (1996) Biochemistry , vol.35 , pp. 16735-16745
    • Gorren, A.C.F.1    List, B.M.2    Schrammel, A.3
  • 48
    • 0031030864 scopus 로고    scopus 로고
    • Subunit interactions of endothelial nitric-oxide synthase: Comparisons to the neuronal and inducible nitric-oxide synthase isoforms
    • Venema R.C., Ju H., Zou R., Ryan J.W., Venema V.J. Subunit interactions of endothelial nitric-oxide synthase: Comparisons to the neuronal and inducible nitric-oxide synthase isoforms. J Biol Chem. 272:1997;1276-1282.
    • (1997) J Biol Chem , vol.272 , pp. 1276-1282
    • Venema, R.C.1    Ju, H.2    Zou, R.3    Ryan, J.W.4    Venema, V.J.5
  • 49
    • 0030585351 scopus 로고    scopus 로고
    • High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin
    • Wu C., Zhang J., Abu-Soud H., Ghosh D.K., Stuehr D.J. High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin. Biochem Biophys Res Commun. 222:1996;439-444.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 439-444
    • Wu, C.1    Zhang, J.2    Abu-Soud, H.3    Ghosh, D.K.4    Stuehr, D.J.5
  • 50
    • 0029125762 scopus 로고
    • Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer
    • Klatt P., Schmidt K., Lehner D., et al. Structural analysis of porcine brain nitric oxide synthase reveals a role for tetrahydrobiopterin and L-arginine in the formation of an SDS-resistant dimer. EMBO J. 14:1995;3687-3695.
    • (1995) EMBO J , vol.14 , pp. 3687-3695
    • Klatt, P.1    Schmidt, K.2    Lehner, D.3
  • 51
    • 0030793667 scopus 로고    scopus 로고
    • Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase: Heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino-tetrahydrobiopterin
    • Mayer B., Wu C., Gorren A.C.F., et al. Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase: heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino-tetrahydrobiopterin. Biochemistry. 36:1997;15091-15095.
    • (1997) Biochemistry , vol.36 , pp. 15091-15095
    • Mayer, B.1    Wu, C.2    Gorren, A.C.F.3
  • 52
    • 0030758321 scopus 로고    scopus 로고
    • Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction
    • Ghosh D.K., Wu C., Pitters E., et al. Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction. Biochemistry. 36:1997;10609-10619.
    • (1997) Biochemistry , vol.36 , pp. 10609-10619
    • Ghosh, D.K.1    Wu, C.2    Pitters, E.3
  • 53
    • 0029827739 scopus 로고    scopus 로고
    • Identification of the 4-amino analogue of tetrahydrobiopterin as a dihydropteridine reductase inhibitor and a potent pteridine antagonist of rat neuronal nitric oxide synthase
    • Werner E.R., Pitters E., Schmidt K., Wachter H., et al. Identification of the 4-amino analogue of tetrahydrobiopterin as a dihydropteridine reductase inhibitor and a potent pteridine antagonist of rat neuronal nitric oxide synthase. Biochem J. 320:1996;193-196.
    • (1996) Biochem J , vol.320 , pp. 193-196
    • Werner, E.R.1    Pitters, E.2    Schmidt, K.3    Wachter, H.4
  • 54
    • 0030687876 scopus 로고    scopus 로고
    • Allosteric modulation of rat brain nitric oxide synthase by the pterin-site enzyme inhibitor 4-aminotetrahydrobiopterin
    • Pfeiffer S., Gorren A.C.F., Pitters E., et al. Allosteric modulation of rat brain nitric oxide synthase by the pterin-site enzyme inhibitor 4-aminotetrahydrobiopterin. Biochem J. 328:1997;349-352.
    • (1997) Biochem J , vol.328 , pp. 349-352
    • Pfeiffer, S.1    Gorren, A.C.F.2    Pitters, E.3
  • 55
    • 0029043644 scopus 로고
    • In search of a function for tetrahydrobiopterin in the biosynthesis of nitric oxide
    • Mayer B., Werner E.R. In search of a function for tetrahydrobiopterin in the biosynthesis of nitric oxide. Naunyn-Schmiedeberg's Arch Pharmacol. 351:1995;453-463.
    • (1995) Naunyn-Schmiedeberg's Arch Pharmacol , vol.351 , pp. 453-463
    • Mayer, B.1    Werner, E.R.2
  • 56
    • 0025826860 scopus 로고
    • Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine
    • Giovanelli J., Campos K.L., Kaufman S. Tetrahydrobiopterin, a cofactor for rat cerebellar nitric oxide synthase, does not function as a reactant in the oxygenation of arginine. Proc Natl Acad Sci USA. 88:1991;7091-7095.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7091-7095
    • Giovanelli, J.1    Campos, K.L.2    Kaufman, S.3
  • 58
    • 0032488596 scopus 로고    scopus 로고
    • Comparative functioning of dihydro- And tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase
    • Presta A., Siddhanta U., Wu C., et al. Comparative functioning of dihydro- and tetrahydropterins in supporting electron transfer, catalysis, and subunit dimerization in inducible nitric oxide synthase. Biochemistry. 37:1998;298-310.
    • (1998) Biochemistry , vol.37 , pp. 298-310
    • Presta, A.1    Siddhanta, U.2    Wu, C.3
  • 59
    • 0030859931 scopus 로고    scopus 로고
    • The ferrous-dioxy complex of neuronal nitric oxide synthase: Divergent effects of L-arginine and tetrahydrobiopterin on its stability
    • Abu-Soud H.M., Gachhui R., Raushel F.M., Stuehr D.J. The ferrous-dioxy complex of neuronal nitric oxide synthase: Divergent effects of L-arginine and tetrahydrobiopterin on its stability. J Biol Chem. 272:1997;17349-17353.
    • (1997) J Biol Chem , vol.272 , pp. 17349-17353
    • Abu-Soud, H.M.1    Gachhui, R.2    Raushel, F.M.3    Stuehr, D.J.4
  • 60
    • 0029983264 scopus 로고    scopus 로고
    • Identification, characterisation, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases
    • Venema R.C., Sayegh H.S., Kent J.D., Harrison D.G. Identification, characterisation, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases. J Biol Chem. 271:1996;6435-6440.
    • (1996) J Biol Chem , vol.271 , pp. 6435-6440
    • Venema, R.C.1    Sayegh, H.S.2    Kent, J.D.3    Harrison, D.G.4
  • 61
    • 0030715301 scopus 로고    scopus 로고
    • An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase
    • Salerno J.C., Harris D.E., Irizarry K., et al. An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase. J Biol Chem. 272:1997;29769-29777.
    • (1997) J Biol Chem , vol.272 , pp. 29769-29777
    • Salerno, J.C.1    Harris, D.E.2    Irizarry, K.3
  • 62
    • 0029003452 scopus 로고
    • Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase
    • Venema R.C., Sayegh H.S., Arnal J.-F., Harrison D.G. Role of the enzyme calmodulin-binding domain in membrane association and phospholipid inhibition of endothelial nitric oxide synthase. J Biol Chem. 270:1995;14705-14711.
    • (1995) J Biol Chem , vol.270 , pp. 14705-14711
    • Venema, R.C.1    Sayegh, H.S.2    Arnal, J.-F.3    Harrison, D.G.4
  • 63
    • 0027525273 scopus 로고
    • Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer
    • Abu-Soud H.M., Stuehr D.J. Nitric oxide synthases reveal a role for calmodulin in controlling electron transfer. Proc Natl Acad Sci USA. 90:1993;10769-10772.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10769-10772
    • Abu-Soud, H.M.1    Stuehr, D.J.2
  • 64
    • 0030894594 scopus 로고    scopus 로고
    • Thiols and neuronal nitric oxide synthase: Complex formation, competitive inhibition, and enzyme stabilization
    • Gorren A.C.F., Schrammel A., Schmidt K., Mayer B. Thiols and neuronal nitric oxide synthase: complex formation, competitive inhibition, and enzyme stabilization. Biochemistry. 36:1997;4360-4366.
    • (1997) Biochemistry , vol.36 , pp. 4360-4366
    • Gorren, A.C.F.1    Schrammel, A.2    Schmidt, K.3    Mayer, B.4
  • 65
    • 0031882260 scopus 로고    scopus 로고
    • Reactive oxygen species as mediators of signal transduction in cardiovascular disease
    • Abe J., Berk B.C. Reactive oxygen species as mediators of signal transduction in cardiovascular disease. Trends Cardiovasc Med. 8:1998;59-64.
    • (1998) Trends Cardiovasc Med , vol.8 , pp. 59-64
    • Abe, J.1    Berk, B.C.2
  • 66
    • 0031041547 scopus 로고    scopus 로고
    • Role of superoxide in angiotensin II-induced but not catecholamine-induced hypertension
    • Laursen J.B., Rajagopalan S., Galis Z., et al. Role of superoxide in angiotensin II-induced but not catecholamine-induced hypertension. Circulation. 95:1997;588-593.
    • (1997) Circulation , vol.95 , pp. 588-593
    • Laursen, J.B.1    Rajagopalan, S.2    Galis, Z.3
  • 67
    • 0025989760 scopus 로고
    • Chronic treatment with polyethylene glycolated superoxide dismutase partially restores endothelium-dependent vascular relaxations in cholesterol-fed rabbits
    • Mügge A., Elwell J.H., Peterson T.E., et al. Chronic treatment with polyethylene glycolated superoxide dismutase partially restores endothelium-dependent vascular relaxations in cholesterol-fed rabbits. Circ Res. 69:1991;1293-1300.
    • (1991) Circ Res , vol.69 , pp. 1293-1300
    • Mügge, A.1    Elwell, J.H.2    Peterson, T.E.3
  • 68
    • 0028078872 scopus 로고
    • Superoxide and peroxynitrite in atherosclerosis
    • White C.R., Brock T.A., Chang L.-Y., et al. Superoxide and peroxynitrite in atherosclerosis. Proc Natl Acad Sci USA. 91:1994;1044-1048.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1044-1048
    • White, C.R.1    Brock, T.A.2    Chang, L.-Y.3
  • 69
    • 0032560966 scopus 로고    scopus 로고
    • Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthases
    • Presta A., Weber-Main A.M., Stankovich M.T., Stuehr D.J. Comparative effects of substrates and pterin cofactor on the heme midpoint potential in inducible and neuronal nitric oxide synthases. J Am Chem Soc. 120:1998;9460-9465.
    • (1998) J Am Chem Soc , vol.120 , pp. 9460-9465
    • Presta, A.1    Weber-Main, A.M.2    Stankovich, M.T.3    Stuehr, D.J.4
  • 70
    • 0032520835 scopus 로고    scopus 로고
    • Manganese superoxide dismutase protects nNOS neurons from NMDA and nitric oxide-mediated neurotoxicity
    • Gonzalez-Zulueta M., Ensz L.M., Mukhina G., et al. Manganese superoxide dismutase protects nNOS neurons from NMDA and nitric oxide-mediated neurotoxicity. J Neurosci. 18:1998;2040-2055.
    • (1998) J Neurosci , vol.18 , pp. 2040-2055
    • Gonzalez-Zulueta, M.1    Ensz, L.M.2    Mukhina, G.3
  • 71
    • 0025329074 scopus 로고
    • Temporal expression of different pathways of L-arginine metabolism in healing wounds
    • Albina J.E., Mills C.D., Henry W.L. Jr., Caldwell M.D. Temporal expression of different pathways of L-arginine metabolism in healing wounds. J Immunol. 144:1990;3877-3880.
    • (1990) J Immunol , vol.144 , pp. 3877-3880
    • Albina, J.E.1    Mills, C.D.2    Henry W.L., Jr.3    Caldwell, M.D.4
  • 72
    • 0032575598 scopus 로고    scopus 로고
    • Inducible nitric-oxide synthase generates superoxide from the reductase domain
    • Xia Y., Roman L.J., Masters B.S., Zweier J.L. Inducible nitric-oxide synthase generates superoxide from the reductase domain. J Biol Chem. 273:1998;22635-22639.
    • (1998) J Biol Chem , vol.273 , pp. 22635-22639
    • Xia, Y.1    Roman, L.J.2    Masters, B.S.3    Zweier, J.L.4
  • 73
    • 0000921940 scopus 로고    scopus 로고
    • Tetrahydrobiopterin alters superoxide and nitric oxide release in prehypertensive rats
    • Cosentino F., Patton S., d́Uscio L.V., et al. Tetrahydrobiopterin alters superoxide and nitric oxide release in prehypertensive rats. J Clin Invest. 101:1998;1530-1537.
    • (1998) J Clin Invest , vol.101 , pp. 1530-1537
    • Cosentino, F.1    Patton, S.2    D́uscio, L.V.3
  • 74
    • 0029133481 scopus 로고
    • Native low-density lipoprotein increases endothelial cell nitric oxide synthase generation of superoxide anion
    • Pritchard K.A., Groszek L., Smalley D.M., et al. Native low-density lipoprotein increases endothelial cell nitric oxide synthase generation of superoxide anion. Circ Res. 77:1995;510-518.
    • (1995) Circ Res , vol.77 , pp. 510-518
    • Pritchard, K.A.1    Groszek, L.2    Smalley, D.M.3
  • 75
    • 0032475865 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent and tetrahydrobiopterin regulatory process
    • 2+/calmodulin-dependent and tetrahydrobiopterin regulatory process. J Biol Chem. 273:1998;25804-25808.
    • (1998) J Biol Chem , vol.273 , pp. 25804-25808
    • Xia, Y.1    Tsai, A.-L.2    Berka, V.3    Zweier, J.L.4
  • 76
    • 0032482975 scopus 로고    scopus 로고
    • Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors
    • Vásquez-Vivar J., Kalyanaraman B., Martásek P., et al. Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors. Proc Natl Acad Sci USA. 95:1998;9220-9225.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9220-9225
    • Vásquez-Vivar, J.1    Kalyanaraman, B.2    Martásek, P.3
  • 77
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and the ugly
    • Beckman J.S., Koppenol W.H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and the ugly. Am J Physiol. 40:1996;C1424-C1437.
    • (1996) Am J Physiol , vol.40
    • Beckman, J.S.1    Koppenol, W.H.2
  • 78
    • 0032488967 scopus 로고    scopus 로고
    • A new pathway of nitric oxide/cyclic GMP signaling involving S-nitrosoglutathione
    • Mayer B., Pfeiffer S., Schrammel A., et al. A new pathway of nitric oxide/cyclic GMP signaling involving S-nitrosoglutathione. J Biol Chem. 273:1998;3264-3270.
    • (1998) J Biol Chem , vol.273 , pp. 3264-3270
    • Mayer, B.1    Pfeiffer, S.2    Schrammel, A.3
  • 79
    • 0027990370 scopus 로고
    • Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group
    • Griscavage J.M., Fukoto J.M., Komori Y., Ignarro L.J. Nitric oxide inhibits neuronal nitric oxide synthase by interacting with the heme prosthetic group. J Biol Chem. 269:1994;21644-21649.
    • (1994) J Biol Chem , vol.269 , pp. 21644-21649
    • Griscavage, J.M.1    Fukoto, J.M.2    Komori, Y.3    Ignarro, L.J.4
  • 80
    • 0029092658 scopus 로고
    • Neuronal nitric oxide synthase self-inactivates by forming a ferrous-nitrosyl complex during aerobic catalysis
    • Abu-Soud H.M., Wang J., Rousseau D.L., et al. Neuronal nitric oxide synthase self-inactivates by forming a ferrous-nitrosyl complex during aerobic catalysis. J Biol Chem. 270:1995;22997-23006.
    • (1995) J Biol Chem , vol.270 , pp. 22997-23006
    • Abu-Soud, H.M.1    Wang, J.2    Rousseau, D.L.3
  • 81
    • 0028924952 scopus 로고
    • Kinetics and mechanism of tetrahydrobiopterin-induced oxidation of nitric oxide
    • Mayer B., Klatt P., Werner E.R., Schmidt K. Kinetics and mechanism of tetrahydrobiopterin-induced oxidation of nitric oxide. J Biol Chem. 270:1995;655-659.
    • (1995) J Biol Chem , vol.270 , pp. 655-659
    • Mayer, B.1    Klatt, P.2    Werner, E.R.3    Schmidt, K.4
  • 82
    • 0025349882 scopus 로고
    • Vasorelaxant properties of the endothelium-derived relaxing factor more closely resemble S-nitrosocysteine than nitric oxide
    • Myers P.R., Minor R.L. Jr., Guerra R. Jr., Bates J.N., Harrison D.G. Vasorelaxant properties of the endothelium-derived relaxing factor more closely resemble S-nitrosocysteine than nitric oxide. Nature. 345:1990;161-163.
    • (1990) Nature , vol.345 , pp. 161-163
    • Myers, P.R.1    Minor R.L., Jr.2    Guerra R., Jr.3    Bates, J.N.4    Harrison, D.G.5
  • 83
    • 0029871586 scopus 로고    scopus 로고
    • Nitrogen dioxide causes pulmonary arterial relaxation via thiol nitrosation and nitric oxide formation
    • Davidson C.A., Kaminski P.M., Wu M., Wolin M.S. Nitrogen dioxide causes pulmonary arterial relaxation via thiol nitrosation and nitric oxide formation. Am J Physiol. 270:1996;H1038-H1043.
    • (1996) Am J Physiol , vol.270
    • Davidson, C.A.1    Kaminski, P.M.2    Wu, M.3    Wolin, M.S.4
  • 84
    • 0028373681 scopus 로고
    • Extensive nitration of protein tyrosines observed in human atherosclerosis detected by immunohistochemistry
    • Beckman J.S., Ye Y.Z., Anderson P., et al. Extensive nitration of protein tyrosines observed in human atherosclerosis detected by immunohistochemistry. Biol Chem Hoppe-Seyler. 375:1994;81-88.
    • (1994) Biol Chem Hoppe-Seyler , vol.375 , pp. 81-88
    • Beckman, J.S.1    Ye, Y.Z.2    Anderson, P.3
  • 85
    • 0032538450 scopus 로고    scopus 로고
    • Lack of tyrosine nitration by peroxynitrite generated at physiological pH
    • Pfeiffer S., Mayer B. Lack of tyrosine nitration by peroxynitrite generated at physiological pH. J Biol Chem. 273:1998;27280-27285.
    • (1998) J Biol Chem , vol.273 , pp. 27280-27285
    • Pfeiffer, S.1    Mayer, B.2
  • 86
    • 0032556905 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
    • Eiserich J.P., Hristova M., Cross C.E., et al. Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature. 391:1998;393-397.
    • (1998) Nature , vol.391 , pp. 393-397
    • Eiserich, J.P.1    Hristova, M.2    Cross, C.E.3
  • 87
    • 0030723041 scopus 로고    scopus 로고
    • Endothelial dysfunction and atherosclerosis
    • Vanhoutte P.M. Endothelial dysfunction and atherosclerosis. Eur Heart J. 18:(Suppl E):1997;E19-E29.
    • (1997) Eur Heart J , vol.18 , Issue.SUPPL. E
    • Vanhoutte, P.M.1
  • 88
    • 0030711684 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of endothelial cell dysfunction
    • Harrison D.G. Cellular and molecular mechanisms of endothelial cell dysfunction. J Clin Invest. 100:1997;2153-2157.
    • (1997) J Clin Invest , vol.100 , pp. 2153-2157
    • Harrison, D.G.1
  • 90
    • 0025866051 scopus 로고
    • Nitric oxide synthesis in cultured endocardial cells of the pig
    • Schulz R., Smith J.A., Lewis M.J., Moncada S. Nitric oxide synthesis in cultured endocardial cells of the pig. Br J Pharmacol. 104:1991;21-24.
    • (1991) Br J Pharmacol , vol.104 , pp. 21-24
    • Schulz, R.1    Smith, J.A.2    Lewis, M.J.3    Moncada, S.4
  • 91
    • 0028825749 scopus 로고
    • Regulation of bovine endothelial constitutive nitric oxide synthase by oxygen
    • Liao J.K., Zulueta J.J., Yu F.-S., et al. Regulation of bovine endothelial constitutive nitric oxide synthase by oxygen. J Clin Invest. 96:1995;2661-2666.
    • (1995) J Clin Invest , vol.96 , pp. 2661-2666
    • Liao, J.K.1    Zulueta, J.J.2    Yu, F.-S.3
  • 92
    • 0028067880 scopus 로고
    • Increased expression of endothelial constitutive nitric oxide synthase in rat aorta during pregnancy
    • Goetz R.M., Morano I., Calovini T., Studer R., Holtz J. Increased expression of endothelial constitutive nitric oxide synthase in rat aorta during pregnancy. Biochem Biophys Res Commun. 205:1994;905-910.
    • (1994) Biochem Biophys Res Commun , vol.205 , pp. 905-910
    • Goetz, R.M.1    Morano, I.2    Calovini, T.3    Studer, R.4    Holtz, J.5
  • 93
    • 0028118896 scopus 로고
    • Chronic exercise in dogs increases coronary vascular nitric oxide production and endothelial cell nitric oxide synthase gene expression
    • Sessa W.C., Pritchard K., Seyedi N., Wang J., Hintze T.H. Chronic exercise in dogs increases coronary vascular nitric oxide production and endothelial cell nitric oxide synthase gene expression. Circ Res. 74:1994;349-353.
    • (1994) Circ Res , vol.74 , pp. 349-353
    • Sessa, W.C.1    Pritchard, K.2    Seyedi, N.3    Wang, J.4    Hintze, T.H.5
  • 94
    • 0001599370 scopus 로고
    • Role of endothelium-derived nitric oxide in the regulation of blood pressure
    • Rees D.D., Palmer R.M., Moncada S. Role of endothelium-derived nitric oxide in the regulation of blood pressure. Proc Natl Acad Sci USA. 86:1989;3375-3378.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3375-3378
    • Rees, D.D.1    Palmer, R.M.2    Moncada, S.3
  • 95
    • 0030962682 scopus 로고    scopus 로고
    • G proteins and endothelium-dependent relaxations
    • Boulanger C.M., Vanhoutte P.M. G proteins and endothelium-dependent relaxations. J Vasc Res. 34:1997;175-185.
    • (1997) J Vasc Res , vol.34 , pp. 175-185
    • Boulanger, C.M.1    Vanhoutte, P.M.2
  • 96
    • 0026497997 scopus 로고
    • Molecular cloning and characterisation of the constitutive bovine aortic endothelial cell nitric oxide synthase
    • Nishida K., Harrison D.G., Navas J.P., et al. Molecular cloning and characterisation of the constitutive bovine aortic endothelial cell nitric oxide synthase. J Clin Invest. 90:1992;2092-2096.
    • (1992) J Clin Invest , vol.90 , pp. 2092-2096
    • Nishida, K.1    Harrison, D.G.2    Navas, J.P.3
  • 97
    • 0029122777 scopus 로고
    • Cyclic strain upregulates nitric oxide synthase in cultured bovine aortic endothelial cells
    • Awolesi M.A., Sessa W.C., Sumpio B.E. Cyclic strain upregulates nitric oxide synthase in cultured bovine aortic endothelial cells. J Clin Invest. 96:1995;1449-1454.
    • (1995) J Clin Invest , vol.96 , pp. 1449-1454
    • Awolesi, M.A.1    Sessa, W.C.2    Sumpio, B.E.3
  • 98
    • 0027267272 scopus 로고
    • Shear stress elevates endothelial cGMP. Role of a potassium channel and G protein coupling
    • Ohno M., Gibbons G.H., Dzau V.J., Cooke J.P. Shear stress elevates endothelial cGMP. Role of a potassium channel and G protein coupling. Circulation. 88:1993;193-197.
    • (1993) Circulation , vol.88 , pp. 193-197
    • Ohno, M.1    Gibbons, G.H.2    Dzau, V.J.3    Cooke, J.P.4
  • 99
    • 0029664995 scopus 로고    scopus 로고
    • Acylation targets endothelial nitric-oxide synthase to plasmalemmal caveolae
    • Shaul P.W., Smart E.J., Robinson L.J., et al. Acylation targets endothelial nitric-oxide synthase to plasmalemmal caveolae. J Biol Chem. 271:1996;6518-6522.
    • (1996) J Biol Chem , vol.271 , pp. 6518-6522
    • Shaul, P.W.1    Smart, E.J.2    Robinson, L.J.3
  • 100
    • 0039397709 scopus 로고    scopus 로고
    • Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo
    • García-Cardeña G., Martásek P., Masters B.S.S., et al. Dissecting the interaction between nitric oxide synthase (NOS) and caveolin: Functional significance of the NOS caveolin binding domain in vivo. J Biol Chem. 272:1997;25437-25440.
    • (1997) J Biol Chem , vol.272 , pp. 25437-25440
    • García-Cardeña, G.1    Martásek, P.2    Masters, B.S.S.3
  • 101
    • 0032575496 scopus 로고    scopus 로고
    • Interaction between caveolin-1 and the reductase domain of endothelial nitric-oxide synthase. Consequences for catalysis
    • Ghosh S., Gachhui R., Crooks C., Wu C., Lisanti M., Stuehr D.J. Interaction between caveolin-1 and the reductase domain of endothelial nitric-oxide synthase. Consequences for catalysis. J Biol Chem. 273:1998;22267-22271.
    • (1998) J Biol Chem , vol.273 , pp. 22267-22271
    • Ghosh, S.1    Gachhui, R.2    Crooks, C.3    Wu, C.4    Lisanti, M.5    Stuehr, D.J.6
  • 102
    • 0032508575 scopus 로고    scopus 로고
    • Inhibitory interactions of the bradykinin B2 receptor with endothelial nitric-oxide synthase
    • Ju H., Venema V.J., Marrero M.B., Venema R.C. Inhibitory interactions of the bradykinin B2 receptor with endothelial nitric-oxide synthase. J Biol Chem. 273:1998;24025-24029.
    • (1998) J Biol Chem , vol.273 , pp. 24025-24029
    • Ju, H.1    Venema, V.J.2    Marrero, M.B.3    Venema, R.C.4
  • 103
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins
    • Couet J., Li S., Okamoto T., Ikezu T., Lisanti M.P. Identification of peptide and protein ligands for the caveolin-scaffolding domain. Implications for the interaction of caveolin with caveolae-associated proteins. J Biol Chem. 272:1997;6525-6533.
    • (1997) J Biol Chem , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 104
    • 0028876766 scopus 로고
    • Agonist-modulated palmitoylation of endothelial nitric oxide synthase
    • Robinson L.J., Busconi L., Michel T. Agonist-modulated palmitoylation of endothelial nitric oxide synthase. J Biol Chem. 270:1995;995-998.
    • (1995) J Biol Chem , vol.270 , pp. 995-998
    • Robinson, L.J.1    Busconi, L.2    Michel, T.3
  • 105
    • 0032488594 scopus 로고    scopus 로고
    • Dynamic regulation of endothelial nitric oxide synthase: Complementary roles of dual acylation and caveolin interactions
    • Feron O., Michel J.B., Sase K., Michel T. Dynamic regulation of endothelial nitric oxide synthase: Complementary roles of dual acylation and caveolin interactions. Biochemistry. 37:1998;193-200.
    • (1998) Biochemistry , vol.37 , pp. 193-200
    • Feron, O.1    Michel, J.B.2    Sase, K.3    Michel, T.4
  • 106
    • 0025081992 scopus 로고
    • Nitric oxide and cyclic GMP formation upon electrical field stimulation cause relaxation of corpus cavernosum smooth muscle
    • Ignarro L.J., Bush P.A., Buga G.M., et al. Nitric oxide and cyclic GMP formation upon electrical field stimulation cause relaxation of corpus cavernosum smooth muscle. Biochem Biophys Res Commun. 170:1990;843-850.
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 843-850
    • Ignarro, L.J.1    Bush, P.A.2    Buga, G.M.3
  • 107
    • 0028915434 scopus 로고
    • Nitric oxide as a neurotransmitter in peripheral nerves: Nature of transmitter and mechanism of transmission
    • Rand M.J., Li C.G. Nitric oxide as a neurotransmitter in peripheral nerves: Nature of transmitter and mechanism of transmission. Annu Rev Physiol. 57:1995;659-682.
    • (1995) Annu Rev Physiol , vol.57 , pp. 659-682
    • Rand, M.J.1    Li, C.G.2
  • 108
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy M.B. Origin of PDZ (DHR, GLGF) domains. Trends Biochem Sci. 20:1995;350.
    • (1995) Trends Biochem Sci , vol.20 , pp. 350
    • Kennedy, M.B.1
  • 109
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman J.E., Chao D.S., Xia H.H., Aldape K., Bredt D.S. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell. 82:1995;743-752.
    • (1995) Cell , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.H.3    Aldape, K.4    Bredt, D.S.5
  • 110
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha 1-syntrophin mediated by PDZ domains
    • Brenman J.E., Chao D.S., Gee S.H., et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha 1-syntrophin mediated by PDZ domains. Cell. 84:1996;757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3
  • 111
    • 0030895195 scopus 로고    scopus 로고
    • PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences
    • Stricker N.L., Christopherson K.S., Yi B.A., et al. PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences. Nat Biotechnol. 15:1997;336-342.
    • (1997) Nat Biotechnol , vol.15 , pp. 336-342
    • Stricker, N.L.1    Christopherson, K.S.2    Yi, B.A.3
  • 112
    • 0030662249 scopus 로고    scopus 로고
    • Interaction of neuronal nitric-oxide synthase with caveolin-3 in skeletal muscle. Identification of a novel caveolin scaffolding/inhibitory domain
    • Venema V.J., Ju H., Zou R., Venema R.C. Interaction of neuronal nitric-oxide synthase with caveolin-3 in skeletal muscle. Identification of a novel caveolin scaffolding/inhibitory domain. J Biol Chem. 272:1997;28187-28190.
    • (1997) J Biol Chem , vol.272 , pp. 28187-28190
    • Venema, V.J.1    Ju, H.2    Zou, R.3    Venema, R.C.4
  • 113
    • 0027945658 scopus 로고
    • Effects of cerebral ischemia in mice deficient in neuronal nitric oxide synthase
    • Huang Z.H., Huang P.L., Panahian N., et al. Effects of cerebral ischemia in mice deficient in neuronal nitric oxide synthase. Science. 265:1994;1883-1885.
    • (1994) Science , vol.265 , pp. 1883-1885
    • Huang, Z.H.1    Huang, P.L.2    Panahian, N.3
  • 114
    • 0028999596 scopus 로고
    • Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase
    • MacMicking J.D., Nathan C., Hom G., et al. Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase. Cell. 81:1995;641-650.
    • (1995) Cell , vol.81 , pp. 641-650
    • MacMicking, J.D.1    Nathan, C.2    Hom, G.3
  • 115
    • 0025943425 scopus 로고
    • Cytokine-activated endothelial cells express an isotype of nitric oxide synthase which is tetrahydrobiopterin-dependent, calmodulin-independent, and inhibited by arginine analogues
    • Gross S.S., Jaffe E.A., Levi R., Kilbourn R.G. Cytokine-activated endothelial cells express an isotype of nitric oxide synthase which is tetrahydrobiopterin-dependent, calmodulin-independent, and inhibited by arginine analogues. Biochem Biophys Res Commun. 178:1991;823-829.
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 823-829
    • Gross, S.S.1    Jaffe, E.A.2    Levi, R.3    Kilbourn, R.G.4
  • 116
    • 0028135094 scopus 로고
    • Cytokine-inducible nitric oxide synthase (iNOS) expression in cardiac myocytes
    • Balligand J.-L., Ungureanu-Longrois D., Simmons W.W., et al. Cytokine-inducible nitric oxide synthase (iNOS) expression in cardiac myocytes. J Biol Chem. 269:1994;27580-27588.
    • (1994) J Biol Chem , vol.269 , pp. 27580-27588
    • Balligand, J.-L.1    Ungureanu-Longrois, D.2    Simmons, W.W.3
  • 117
    • 0027538176 scopus 로고
    • Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes
    • Geller D.A., Lowenstein C.J., Shapiro R.A., et al. Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci USA. 90:1993;3491-3495.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3491-3495
    • Geller, D.A.1    Lowenstein, C.J.2    Shapiro, R.A.3
  • 118
    • 0029895815 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase is present within human atherosclerotic lesions and promotes the formation and activity of peroxynitrite
    • Buttery L.D.K., Springall D.R., Chester A.H., et al. Inducible nitric oxide synthase is present within human atherosclerotic lesions and promotes the formation and activity of peroxynitrite. Lab Invest. 75:1996;77-85.
    • (1996) Lab Invest , vol.75 , pp. 77-85
    • Buttery, L.D.K.1    Springall, D.R.2    Chester, A.H.3
  • 119
    • 0030800726 scopus 로고    scopus 로고
    • Inhibition of inducible nitric oxide synthase restores endothelium-dependent relaxations in proinflammatory mediator-induced blood vessels
    • Kessler P., Bauersachs J., Busse R., Schini-Kerth V.B. Inhibition of inducible nitric oxide synthase restores endothelium-dependent relaxations in proinflammatory mediator-induced blood vessels. Arterioscler Thromb Vasc Biol. 17:1997;1746-1755.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 1746-1755
    • Kessler, P.1    Bauersachs, J.2    Busse, R.3    Schini-Kerth, V.B.4
  • 120
    • 0030727904 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase suppresses the development of allograft arteriosclerosis
    • Shears L.L. II, Kawaharada N., Tzeng E., et al. Inducible nitric oxide synthase suppresses the development of allograft arteriosclerosis. J Clin Invest. 100:1997;2035-2042.
    • (1997) J Clin Invest , vol.100 , pp. 2035-2042
    • Shears L.L. II1    Kawaharada, N.2    Tzeng, E.3
  • 122
    • 0028940960 scopus 로고
    • Vesicle membrane association of nitric oxide synthase in primary mouse macrophages
    • Vodovotz Y., Russell D., Xie Q.-W., Bogdan C., Nathan C. Vesicle membrane association of nitric oxide synthase in primary mouse macrophages. J Immunol. 154:1995;2914-2925.
    • (1995) J Immunol , vol.154 , pp. 2914-2925
    • Vodovotz, Y.1    Russell, D.2    Xie, Q.-W.3    Bogdan, C.4    Nathan, C.5
  • 123
    • 0027066985 scopus 로고
    • Regulation and subcellular location of nitrogen oxide synthases in RAW264.7 macrophages
    • Schmidt H.H.H.W., Warner T.D., Nakane M., Förstermann U., Murad F. Regulation and subcellular location of nitrogen oxide synthases in RAW264.7 macrophages. Mol Pharmacol. 41:1992;615-624.
    • (1992) Mol Pharmacol , vol.41 , pp. 615-624
    • Schmidt, H.H.H.W.1    Warner, T.D.2    Nakane, M.3    Förstermann, U.4    Murad, F.5
  • 124
    • 0032521624 scopus 로고    scopus 로고
    • Atherogenic concentrations of native low-density lipoproteins down-regulate nitric-oxide-synthase mRNA and protein levels in endothelial cells
    • Vidal F., Colomé C., Martínez-González J., Badimon L. Atherogenic concentrations of native low-density lipoproteins down-regulate nitric-oxide-synthase mRNA and protein levels in endothelial cells. Eur J Biochem. 252:1998;378-384.
    • (1998) Eur J Biochem , vol.252 , pp. 378-384
    • Vidal, F.1    Colomé, C.2    Martínez-González, J.3    Badimon, L.4
  • 125
    • 0026560972 scopus 로고
    • L-Arginine transport is increased in macrophages generating nitric oxide
    • Bogle R.G., Baydoun A.R., Pearson J.D., Moncada S., Mann G.E. L. L-Arginine transport is increased in macrophages generating nitric oxide. Biochem J. 284:1992;15-18.
    • (1992) Biochem J , vol.284 , pp. 15-18
    • Bogle, R.G.1    Baydoun, A.R.2    Pearson, J.D.3    Moncada, S.4    Mann G.E., L.5
  • 126
    • 0028084722 scopus 로고
    • Coinduction of nitric oxide synthase and argininosuccinate synthetase in a murine macrophage cell line: Implications for regulation of nitric oxide production
    • Nüssler A.K., Billiar T.R., Liu Z.-Z., Morris S.M. Jr. Coinduction of nitric oxide synthase and argininosuccinate synthetase in a murine macrophage cell line: implications for regulation of nitric oxide production. J Biol Chem. 269:1994;1257-1261.
    • (1994) J Biol Chem , vol.269 , pp. 1257-1261
    • Nüssler, A.K.1    Billiar, T.R.2    Liu, Z.-Z.3    Morris S.M., Jr.4
  • 127
    • 0028919209 scopus 로고
    • Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages
    • Corraliza I.M., Soler G., Eichmann K., Modolell M. Arginase induction by suppressors of nitric oxide synthesis (IL-4, IL-10 and PGE2) in murine bone-marrow-derived macrophages. Biochem Biophys Res Commun. 206:1995;667-673.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 667-673
    • Corraliza, I.M.1    Soler, G.2    Eichmann, K.3    Modolell, M.4
  • 129
    • 0025018196 scopus 로고
    • The metabolism of L-arginine and its significance for the biosynthesis of endothelium-derived relaxing factor: Cultured human endothelial cells recycle L-citrulline to L-arginine
    • Hecker M., Sessa W.C., Harris H.J., Anggard E.E., Vane J.R. The metabolism of L-arginine and its significance for the biosynthesis of endothelium-derived relaxing factor: Cultured human endothelial cells recycle L-citrulline to L-arginine. Proc Natl Acad Sci USA. 87:1990;8612-8616.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8612-8616
    • Hecker, M.1    Sessa, W.C.2    Harris, H.J.3    Anggard, E.E.4    Vane, J.R.5
  • 130
    • 0029070801 scopus 로고
    • Interactions between L-arginine and L-glutamine change endothelial NO production: An effect independent of NO synthase substrate availability
    • Arnal J.F., Münzel T., Venema R.C., et al. Interactions between L-arginine and L-glutamine change endothelial NO production: An effect independent of NO synthase substrate availability. J Clin Invest. 95:1995;2565-2572.
    • (1995) J Clin Invest , vol.95 , pp. 2565-2572
    • Arnal, J.F.1    Münzel, T.2    Venema, R.C.3
  • 131
    • 0025750850 scopus 로고
    • Purification and characterisation of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells
    • Pollock J.S., Förstermann U., Mitchell J.A., et al. Purification and characterisation of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. Proc Natl Acad Sci USA. 88:1991;10480-10484.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10480-10484
    • Pollock, J.S.1    Förstermann, U.2    Mitchell, J.A.3
  • 132
    • 0031458090 scopus 로고    scopus 로고
    • Adhesiveness of mononuclear cells in hypercholesterolemic humans is normalized by dietary L-arginine
    • Theilmeier G., Chan J.R., Zalpour C., et al. Adhesiveness of mononuclear cells in hypercholesterolemic humans is normalized by dietary L-arginine. Arterioscler Thromb Vasc Biol. 17:1997;3557-3564.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 3557-3564
    • Theilmeier, G.1    Chan, J.R.2    Zalpour, C.3
  • 133
    • 0029670349 scopus 로고    scopus 로고
    • Elevated L-arginine/dimethylarginine ratio contributes to enhanced systemic NO production by dietary L-arginine in hypercholesterolemic rabbits
    • Bode-Boger S.M., Boger R.H., Kienke S., Junker W., Frohlich J.C. Elevated L-arginine/dimethylarginine ratio contributes to enhanced systemic NO production by dietary L-arginine in hypercholesterolemic rabbits. Biochem Biophys Res Commun. 219:1996;598-603.
    • (1996) Biochem Biophys Res Commun , vol.219 , pp. 598-603
    • Bode-Boger, S.M.1    Boger, R.H.2    Kienke, S.3    Junker, W.4    Frohlich, J.C.5
  • 134
    • 0030867403 scopus 로고    scopus 로고
    • The vascular effects of L-arginine in humans. The role of endogenous insulin
    • Giugliano D., Marfella R., Verrazzo G., et al. The vascular effects of L-arginine in humans. The role of endogenous insulin. J Clin Invest. 99:1997;433-438.
    • (1997) J Clin Invest , vol.99 , pp. 433-438
    • Giugliano, D.1    Marfella, R.2    Verrazzo, G.3
  • 135
    • 0029086629 scopus 로고
    • Vascular and hormonal responses to arginine: Provision of substrate for nitric oxide or non-specific effect?
    • MacAllister R.J., Calver A.L., Collier J., et al. Vascular and hormonal responses to arginine: provision of substrate for nitric oxide or non-specific effect? Clin Sci Colch. 89:1995;183-190.
    • (1995) Clin Sci Colch , vol.89 , pp. 183-190
    • MacAllister, R.J.1    Calver, A.L.2    Collier, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.