메뉴 건너뛰기




Volumn , Issue , 2007, Pages 201-221

S-nitrosated proteins: Formation, metabolism, and function

Author keywords

[No Author keywords available]

Indexed keywords


EID: 40949105490     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-044452236-8/50010-1     Document Type: Chapter
Times cited : (8)

References (199)
  • 1
    • 33645326657 scopus 로고
    • Action of mercaptans on acid chlorides. I. Oxalychloride; the mono-and dithioxalates
    • Tasker HS, Jones HO Action of mercaptans on acid chlorides. I. Oxalychloride; the mono-and dithioxalates. J Chem.Soc. 1909, 95:1904-1909.
    • (1909) J Chem.Soc. , vol.95 , pp. 1904-1909
    • Tasker, H.S.1    Jones, H.O.2
  • 2
    • 0023518452 scopus 로고
    • Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical
    • Ignarro LJ, Byrns RE, Buga GM, Wood KS Endothelium-derived relaxing factor from pulmonary artery and vein possesses pharmacologic and chemical properties identical to those of nitric oxide radical. Circ.Res. 1987, 61:866-879.
    • (1987) Circ.Res. , vol.61 , pp. 866-879
    • Ignarro, L.J.1    Byrns, R.E.2    Buga, G.M.3    Wood, K.S.4
  • 3
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott RF, Zawadzki JV The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature 1980, 288:373-376.
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 4
    • 0019322058 scopus 로고
    • Possible involvement of S-nitrosothiols in the activation of guanylate cyclase by nitroso compounds
    • Ignarro LJ, Edwards JC, Gruetter DY, Barry BK, Gruetter CA Possible involvement of S-nitrosothiols in the activation of guanylate cyclase by nitroso compounds. FEBS Lett. 1980, 110:275-278.
    • (1980) FEBS Lett. , vol.110 , pp. 275-278
    • Ignarro, L.J.1    Edwards, J.C.2    Gruetter, D.Y.3    Barry, B.K.4    Gruetter, C.A.5
  • 5
    • 0019313372 scopus 로고
    • Requirement of thiols for activation of coronary arterial guanylate cyclase by glyceryl trinitrate sodium nitrite: possible involvement of S-nitrosothiols
    • Ignarro LJ, Gruetter CA Requirement of thiols for activation of coronary arterial guanylate cyclase by glyceryl trinitrate sodium nitrite: possible involvement of S-nitrosothiols. Biochim Biophys.Acta 1980, 631:221-231.
    • (1980) Biochim Biophys.Acta , vol.631 , pp. 221-231
    • Ignarro, L.J.1    Gruetter, C.A.2
  • 7
    • 0025078860 scopus 로고
    • Flow stimulates endothelial cells to release a nitrovasodilator that is potentiated by reduced thiol
    • Cooke JP, Stamler J, Andon N, Davies PF, McKinley G, Loscalzo J Flow stimulates endothelial cells to release a nitrovasodilator that is potentiated by reduced thiol. Am J.Physiol. 1990, 259:H804-H812.
    • (1990) Am J.Physiol. , vol.259
    • Cooke, J.P.1    Stamler, J.2    Andon, N.3    Davies, P.F.4    McKinley, G.5    Loscalzo, J.6
  • 13
    • 1842852208 scopus 로고    scopus 로고
    • Vasorelaxation by red blood cells and impairment in diabetes: reduced nitric oxide and oxygen delivery by glycated hemoglobin
    • James PE, Lang D, Tufnell-Barret T, Milsom AB, Frenneaux MP Vasorelaxation by red blood cells and impairment in diabetes: reduced nitric oxide and oxygen delivery by glycated hemoglobin. Circ.Res. 2004, 94:976-983.
    • (2004) Circ.Res. , vol.94 , pp. 976-983
    • James, P.E.1    Lang, D.2    Tufnell-Barret, T.3    Milsom, A.B.4    Frenneaux, M.P.5
  • 17
    • 33751280703 scopus 로고    scopus 로고
    • Hemodynamic effects of L-and D-S-nitroso-betabeta-dimethylcysteine in rats
    • Travis MD, Davisson RL, Bates JN, Lewis SJ Hemodynamic effects of L-and D-S-nitroso-betabeta-dimethylcysteine in rats. Am J.Physiol. 1997, 273:H1493-H1501.
    • (1997) Am J.Physiol. , vol.273
    • Travis, M.D.1    Davisson, R.L.2    Bates, J.N.3    Lewis, S.J.4
  • 18
    • 0030055889 scopus 로고    scopus 로고
    • Hemodynamic effects of L-and D-S-nitrosocysteine in the rat. Stereoselective S-nitrosothiol recognition sites
    • Davisson RL, Travis MD, Bates JN, Lewis SJ Hemodynamic effects of L-and D-S-nitrosocysteine in the rat. Stereoselective S-nitrosothiol recognition sites. Circ.Res. 1996, 79:256-262.
    • (1996) Circ.Res. , vol.79 , pp. 256-262
    • Davisson, R.L.1    Travis, M.D.2    Bates, J.N.3    Lewis, S.J.4
  • 19
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation regulates intracellular transfer of nitric oxide
    • Zai A, Rudd MA, Scribner AW, Loscalzo J Cell-surface protein disulfide isomerase catalyzes transnitrosation regulates intracellular transfer of nitric oxide. J Clin.Invest. 1999, 103:393-399.
    • (1999) J Clin.Invest. , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, M.A.2    Scribner, A.W.3    Loscalzo, J.4
  • 20
    • 0035859858 scopus 로고    scopus 로고
    • Mechanism of transfer of NO from extracel-lular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase
    • Ramachandran N, Root P, Jiang XM, Hogg PJ, Mutus B Mechanism of transfer of NO from extracel-lular S-nitrosothiols into the cytosol by cell-surface protein disulfide isomerase. Proc. Natl. Acad Sci.USA 2001, 98:9539-9544.
    • (2001) Proc. Natl. Acad Sci.USA , vol.98 , pp. 9539-9544
    • Ramachandran, N.1    Root, P.2    Jiang, X.M.3    Hogg, P.J.4    Mutus, B.5
  • 21
    • 0034326826 scopus 로고    scopus 로고
    • Effect of S-nitrosothiols on cellular glutathione reactive protein sulfhydryls
    • Mallis RJ, Thomas JA Effect of S-nitrosothiols on cellular glutathione reactive protein sulfhydryls. Arch Biochem.Biophys. 2000, 383:60-69.
    • (2000) Arch Biochem.Biophys. , vol.383 , pp. 60-69
    • Mallis, R.J.1    Thomas, J.A.2
  • 22
    • 2542516981 scopus 로고    scopus 로고
    • The mechanism of transmembrane S-nitrosothiol transport
    • Zhang Y, Hogg N The mechanism of transmembrane S-nitrosothiol transport. Proc. Natl. Acad Sci.USA 2004, 101:7891-7896.
    • (2004) Proc. Natl. Acad Sci.USA , vol.101 , pp. 7891-7896
    • Zhang, Y.1    Hogg, N.2
  • 23
    • 14644401128 scopus 로고    scopus 로고
    • S-Nitrosothiols: cellular formation transport
    • Zhang Y, Hogg N S-Nitrosothiols: cellular formation transport. Free Radic Biol.Med. 2005, 38:831-838.
    • (2005) Free Radic Biol.Med. , vol.38 , pp. 831-838
    • Zhang, Y.1    Hogg, N.2
  • 24
    • 0030827923 scopus 로고    scopus 로고
    • Involvement of L-type-like amino acid transporters in S-nitrosocysteine-stimulated noradrenaline release in the rat hippocampus
    • Satoh S, Kimura T, Toda M, Maekawa M, Ono S, Narita H, Miyazaki H, Murayama T, Nomura Y Involvement of L-type-like amino acid transporters in S-nitrosocysteine-stimulated noradrenaline release in the rat hippocampus. J.Neurochem. 1997, 69:2197-2205.
    • (1997) J.Neurochem. , vol.69 , pp. 2197-2205
    • Satoh, S.1    Kimura, T.2    Toda, M.3    Maekawa, M.4    Ono, S.5    Narita, H.6    Miyazaki, H.7    Murayama, T.8    Nomura, Y.9
  • 25
    • 11844295419 scopus 로고    scopus 로고
    • S-nitrosoprotein formation localization in endothelial cells
    • Yang Y, Loscalzo J S-nitrosoprotein formation localization in endothelial cells. Proc. Natl. Acad Sci.USA 2005, 102:117-122.
    • (2005) Proc. Natl. Acad Sci.USA , vol.102 , pp. 117-122
    • Yang, Y.1    Loscalzo, J.2
  • 26
    • 0346458616 scopus 로고    scopus 로고
    • Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes heat shock proteins
    • Ramachandran A, Ceaser E, Darley-Usmar VM Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes heat shock proteins. Proc. Natl.Acad Sci.USA 2004, 101:384-389.
    • (2004) Proc. Natl.Acad Sci.USA , vol.101 , pp. 384-389
    • Ramachandran, A.1    Ceaser, E.2    Darley-Usmar, V.M.3
  • 27
  • 29
    • 0030781227 scopus 로고    scopus 로고
    • Formation properties of peroxynitrite as studied by laser flash photolysis high-pressure stopped-flow technique and pulse radiolysis
    • Kissner R, Nauser T, Bugnon P, Lye PG, Koppenol WH Formation properties of peroxynitrite as studied by laser flash photolysis high-pressure stopped-flow technique and pulse radiolysis. Chem Res.Toxicol. 1997, 10:1285-1292.
    • (1997) Chem Res.Toxicol. , vol.10 , pp. 1285-1292
    • Kissner, R.1    Nauser, T.2    Bugnon, P.3    Lye, P.G.4    Koppenol, W.H.5
  • 31
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1 alpha protein as a target for S-nitrosation
    • Sumbayev VV, Budde A, Zhou J, Brune B HIF-1 alpha protein as a target for S-nitrosation. FEBS Lett. 2003, 535:106-112.
    • (2003) FEBS Lett. , vol.535 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brune, B.4
  • 32
    • 0037143608 scopus 로고    scopus 로고
    • Focusing of nitric oxide mediated nitrosation oxidative nitrosylation as a consequence of reaction with superoxide
    • Espey MG, Thomas DD, Miranda KM, Wink DA Focusing of nitric oxide mediated nitrosation oxidative nitrosylation as a consequence of reaction with superoxide. Proc. Natl. Acad Sci.USA 2002, 99:11127-11132.
    • (2002) Proc. Natl. Acad Sci.USA , vol.99 , pp. 11127-11132
    • Espey, M.G.1    Thomas, D.D.2    Miranda, K.M.3    Wink, D.A.4
  • 33
    • 0031417313 scopus 로고    scopus 로고
    • Iron catalyzes both decomposition and synthesis of S-nitrosothiols: optical and electron paramagnetic resonance studies
    • Vanin AF, Malenkova IV, Serezhenkov VA Iron catalyzes both decomposition and synthesis of S-nitrosothiols: optical and electron paramagnetic resonance studies. Nitric Oxide 1997, 1:191-203.
    • (1997) Nitric Oxide , vol.1 , pp. 191-203
    • Vanin, A.F.1    Malenkova, I.V.2    Serezhenkov, V.A.3
  • 35
    • 0028803686 scopus 로고
    • Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen
    • Kharitonov VG, Sundquist AR, Sharma VS Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen. J Biol.Chem. 1995, 270:28158-28164.
    • (1995) J Biol.Chem. , vol.270 , pp. 28158-28164
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 36
    • 0037465761 scopus 로고    scopus 로고
    • Mechanism of S-nitrosation of recombinant human brain calbindin D28K
    • Tao L, English AM Mechanism of S-nitrosation of recombinant human brain calbindin D28K. Biochemistry 2003, 42:3326-3334.
    • (2003) Biochemistry , vol.42 , pp. 3326-3334
    • Tao, L.1    English, A.M.2
  • 37
    • 0027104253 scopus 로고
    • Biochemistry of nitric oxide and its redox-activated forms
    • Stamler JS, Singel DJ, Loscalzo J Biochemistry of nitric oxide and its redox-activated forms. Science 1992, 258:1898-1902.
    • (1992) Science , vol.258 , pp. 1898-1902
    • Stamler, J.S.1    Singel, D.J.2    Loscalzo, J.3
  • 38
    • 0033214985 scopus 로고    scopus 로고
    • Mechanism of S-nitrosothiol formation degradation mediated by copper ions
    • Stubauer G, Giuffre A, Sarti P Mechanism of S-nitrosothiol formation degradation mediated by copper ions. J Biol.Chem. 1999, 274:28128-28133.
    • (1999) J Biol.Chem. , vol.274 , pp. 28128-28133
    • Stubauer, G.1    Giuffre, A.2    Sarti, P.3
  • 39
    • 0345306295 scopus 로고    scopus 로고
    • Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein
    • Romeo AA, Capobianco JA, English AM Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein. J. Am Chem.Soc. 2003, 125:14370-14378.
    • (2003) J. Am Chem.Soc. , vol.125 , pp. 14370-14378
    • Romeo, A.A.1    Capobianco, J.A.2    English, A.M.3
  • 42
    • 0032113092 scopus 로고    scopus 로고
    • NO-synthase and nitrite-reductase components of nitric oxide cycle
    • Reutov VP, Sorokina EG NO-synthase and nitrite-reductase components of nitric oxide cycle. Biochemistry (Mosc.) 1998, 63:874-884.
    • (1998) Biochemistry (Mosc.) , vol.63 , pp. 874-884
    • Reutov, V.P.1    Sorokina, E.G.2
  • 44
    • 20444451649 scopus 로고    scopus 로고
    • Xanthine oxidase catalyzes anaerobic transformation of organic nitrates to nitric oxide nitrosothiols: characterization of this mechanism and the link between nitrate and guanylyl cyclase activation
    • Li H, Cui H, Liu X, Zweier JL Xanthine oxidase catalyzes anaerobic transformation of organic nitrates to nitric oxide nitrosothiols: characterization of this mechanism and the link between nitrate and guanylyl cyclase activation. J Biol.Chem. 2005, 280:16594-16600.
    • (2005) J Biol.Chem. , vol.280 , pp. 16594-16600
    • Li, H.1    Cui, H.2    Liu, X.3    Zweier, J.L.4
  • 45
    • 0035826695 scopus 로고    scopus 로고
    • Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein
    • Yang Y, Maret W, Vallee BL Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein. Proc. Natl.Acad Sci.USA 2001, 98:5556-5559.
    • (2001) Proc. Natl.Acad Sci.USA , vol.98 , pp. 5556-5559
    • Yang, Y.1    Maret, W.2    Vallee, B.L.3
  • 47
    • 0001301709 scopus 로고
    • Photochemistry of the S-nitroso derivatives of hexane-1-thiol and hexane-1,6-dithiol
    • Barrett J, Fitzgibbons LJ, Glauser J, Still RH, Young PNW Photochemistry of the S-nitroso derivatives of hexane-1-thiol and hexane-1,6-dithiol. Nature 1966, 211:848.
    • (1966) Nature , vol.211 , pp. 848
    • Barrett, J.1    Fitzgibbons, L.J.2    Glauser, J.3    Still, R.H.4    Young, P.N.W.5
  • 48
    • 0000887557 scopus 로고
    • The photoactivated relaxation of smooth muscle of rabbit aorta
    • Furchgott RF, Ehrreich SJ, Greenblatt E The photoactivated relaxation of smooth muscle of rabbit aorta. J Gen.Physiol. 1961, 44:499-519.
    • (1961) J Gen.Physiol. , vol.44 , pp. 499-519
    • Furchgott, R.F.1    Ehrreich, S.J.2    Greenblatt, E.3
  • 49
    • 0024542671 scopus 로고
    • Interactions of light sodium nitrite in producing relaxation of rabbit aorta
    • Matsunaga K, Furchgott RF Interactions of light sodium nitrite in producing relaxation of rabbit aorta. J.Pharmacol Exp.Ther. 1989, 248:687-695.
    • (1989) J.Pharmacol Exp.Ther. , vol.248 , pp. 687-695
    • Matsunaga, K.1    Furchgott, R.F.2
  • 50
    • 0033859018 scopus 로고    scopus 로고
    • Selective modifiers of glutathione biosynthesis 'repriming' of vascular smooth muscle photorelaxation
    • Megson IL, Holmes SA, Magid KS, Pritchard RJ, Flitney FW Selective modifiers of glutathione biosynthesis 'repriming' of vascular smooth muscle photorelaxation. Br J.Pharmacol. 2000, 130:1575-1580.
    • (2000) Br J.Pharmacol. , vol.130 , pp. 1575-1580
    • Megson, I.L.1    Holmes, S.A.2    Magid, K.S.3    Pritchard, R.J.4    Flitney, F.W.5
  • 51
    • 1642578898 scopus 로고    scopus 로고
    • Neocuproine inhibits the decomposition of endogenous S-nitrosothiol by ultraviolet irradiation in the mouse gastric fundus
    • Ogulener N, Ergun Y Neocuproine inhibits the decomposition of endogenous S-nitrosothiol by ultraviolet irradiation in the mouse gastric fundus. Eur J.Pharmacol. 2004, 485:269-274.
    • (2004) Eur J.Pharmacol. , vol.485 , pp. 269-274
    • Ogulener, N.1    Ergun, Y.2
  • 52
    • 0037199702 scopus 로고    scopus 로고
    • Putative role for S-nitrosoglutathione as the source of nitric oxide in photorelaxation of the mouse gastric fundus
    • Ogulener N, Ergun YA putative role for S-nitrosoglutathione as the source of nitric oxide in photorelaxation of the mouse gastric fundus. Eur J.Pharmacol. 2002, 450:267-275.
    • (2002) Eur J.Pharmacol. , vol.450 , pp. 267-275
    • Ogulener, N.1    Ergun, Y.A.2
  • 53
    • 0034831382 scopus 로고    scopus 로고
    • Decomposition of S-nitrosothiols: unimolecular versus autocatalytic mechanism
    • Grossi L, Montevecchi PC, Strazzari S Decomposition of S-nitrosothiols: unimolecular versus autocatalytic mechanism. J.Am Chem.Soc. 2001, 123:4853-4854.
    • (2001) J.Am Chem.Soc. , vol.123 , pp. 4853-4854
    • Grossi, L.1    Montevecchi, P.C.2    Strazzari, S.3
  • 55
    • 0031019667 scopus 로고    scopus 로고
    • Role of ascorbate protein thiols in the release of nitric oxide from S-nitroso-albumin and S-nitroso-glutathione in human plasma
    • Scorza G, Pietraforte D, Minetti M Role of ascorbate protein thiols in the release of nitric oxide from S-nitroso-albumin and S-nitroso-glutathione in human plasma. Free Radic Biol.Med. 1997, 22:633-642.
    • (1997) Free Radic Biol.Med. , vol.22 , pp. 633-642
    • Scorza, G.1    Pietraforte, D.2    Minetti, M.3
  • 58
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu L, Hausladen A, Zeng M, Que L, Heitman J, Stamler JS A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 2001, 410:490-494.
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 60
    • 0032513115 scopus 로고    scopus 로고
    • Superoxide-mediated decomposition of biological S-nitrosothiols
    • Aleryani S, Milo E, Rose Y, Kostka P Superoxide-mediated decomposition of biological S-nitrosothiols. J Biol.Chem. 1998, 273:6041-6045.
    • (1998) J Biol.Chem. , vol.273 , pp. 6041-6045
    • Aleryani, S.1    Milo, E.2    Rose, Y.3    Kostka, P.4
  • 62
    • 0036430357 scopus 로고    scopus 로고
    • Evidence that intrinsic iron but not intrinsic copper determines S-nitrosocysteine decomposition in buffer solution
    • Vanin AF, Muller B, Alencar JL, Lobysheva II, Nepveu F, Stoclet JC Evidence that intrinsic iron but not intrinsic copper determines S-nitrosocysteine decomposition in buffer solution. Nitric Oxide 2002, 7:194-209.
    • (2002) Nitric Oxide , vol.7 , pp. 194-209
    • Vanin, A.F.1    Muller, B.2    Alencar, J.L.3    Lobysheva, I.I.4    Nepveu, F.5    Stoclet, J.C.6
  • 63
    • 0033927212 scopus 로고    scopus 로고
    • Role of redox-active iron ions in the decom-position of S-nitrosocysteine in subcellular fractions of porcine aorta
    • Sorenson E, Skiles EH, Xu B, Aleryani S, Kostka P Role of redox-active iron ions in the decom-position of S-nitrosocysteine in subcellular fractions of porcine aorta. Eur J.Biochem. 2000, 267:4593-4599.
    • (2000) Eur J.Biochem. , vol.267 , pp. 4593-4599
    • Sorenson, E.1    Skiles, E.H.2    Xu, B.3    Aleryani, S.4    Kostka, P.5
  • 64
    • 0029780524 scopus 로고    scopus 로고
    • Mechanism of nitric oxide release from S-nitrosothiols
    • Singh RJ, Hogg N, Joseph J, Kalyanaraman B Mechanism of nitric oxide release from S-nitrosothiols. J Biol.Chem. 1996, 271:18596-18603.
    • (1996) J Biol.Chem. , vol.271 , pp. 18596-18603
    • Singh, R.J.1    Hogg, N.2    Joseph, J.3    Kalyanaraman, B.4
  • 65
    • 0030010784 scopus 로고    scopus 로고
    • Decomposition of S-nitrosoglutathione in the presence of copper ions glutathione
    • Gorren AC, Schrammel A, Schmidt K, Mayer B Decomposition of S-nitrosoglutathione in the presence of copper ions glutathione. Arch Biochem.Biophys. 1996, 330:219-228.
    • (1996) Arch Biochem.Biophys. , vol.330 , pp. 219-228
    • Gorren, A.C.1    Schrammel, A.2    Schmidt, K.3    Mayer, B.4
  • 67
    • 0036441366 scopus 로고    scopus 로고
    • Reactions of S-nitrosothiols with L-ascorbic acid in aqueous solution
    • Dasgupta TP, Smith JN Reactions of S-nitrosothiols with L-ascorbic acid in aqueous solution. Methods Enzymol. 2002, 359:219-229.
    • (2002) Methods Enzymol. , vol.359 , pp. 219-229
    • Dasgupta, T.P.1    Smith, J.N.2
  • 68
    • 1242293702 scopus 로고    scopus 로고
    • Dynamics of interaction of vitamin C with some potent nitrovasodilators S-nitroso-N-acetyl-dl-penicillamine (SNAP) S-nitrosocaptopril (SNOCap) in aqueous solu
    • Aquart DV, Dasgupta TP Dynamics of interaction of vitamin C with some potent nitrovasodilators S-nitroso-N-acetyl-dl-penicillamine (SNAP) S-nitrosocaptopril (SNOCap) in aqueous solu. Biophys.Chem. 2004, 107:117-131.
    • (2004) Biophys.Chem. , vol.107 , pp. 117-131
    • Aquart, D.V.1    Dasgupta, T.P.2
  • 69
    • 0033874466 scopus 로고    scopus 로고
    • Ascorbic acid and glutathione modulate the biological activity of S-nitrosoglutathione
    • Xu A, Vita JA, Keaney JF Ascorbic acid and glutathione modulate the biological activity of S-nitrosoglutathione. Hypertension 2000, 36:291-295.
    • (2000) Hypertension , vol.36 , pp. 291-295
    • Xu, A.1    Vita, J.A.2    Keaney, J.F.3
  • 70
    • 0035849715 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • Jaffrey SR, Snyder SH The biotin switch method for the detection of S-nitrosylated proteins. Sci.STKE. 2001, 2001:PL1.
    • (2001) Sci.STKE. , vol.2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 71
    • 29344465714 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase binds S-nitrosylates and activates cyclooxygenase-2
    • Kim SF, Huri DA, Snyder SH Inducible nitric oxide synthase binds S-nitrosylates and activates cyclooxygenase-2. Science 2005, 310:1966-1970.
    • (2005) Science , vol.310 , pp. 1966-1970
    • Kim, S.F.1    Huri, D.A.2    Snyder, S.H.3
  • 72
    • 0344012010 scopus 로고    scopus 로고
    • Nitric oxide induces apoptosis via hydrogen peroxide but necrosis via energy thiol depletion
    • Borutaite V, Brown GC Nitric oxide induces apoptosis via hydrogen peroxide but necrosis via energy thiol depletion. Free Radic Biol.Med. 2003, 35:1457-1468.
    • (2003) Free Radic Biol.Med. , vol.35 , pp. 1457-1468
    • Borutaite, V.1    Brown, G.C.2
  • 75
    • 0030945376 scopus 로고    scopus 로고
    • S-Nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase
    • Pt 2
    • Hogg N, Singh RJ, Konorev E, Joseph J, Kalyanaraman B S-Nitrosoglutathione as a substrate for gamma-glutamyl transpeptidase. J.Biochem. 1997, 323:477-481. Pt 2.
    • (1997) J.Biochem. , vol.323 , pp. 477-481
    • Hogg, N.1    Singh, R.J.2    Konorev, E.3    Joseph, J.4    Kalyanaraman, B.5
  • 76
    • 0032522535 scopus 로고    scopus 로고
    • S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme
    • Pt 2
    • Jensen DE, Belka GK, Du Bois GC S-Nitrosoglutathione is a substrate for rat alcohol dehydrogenase class III isoenzyme. J.Biochem. 1998, 331:659-668. Pt 2.
    • (1998) J.Biochem. , vol.331 , pp. 659-668
    • Jensen, D.E.1    Belka, G.K.2    Du, B.G.C.3
  • 78
    • 0344034360 scopus 로고    scopus 로고
    • Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells Mol
    • Kahlos K, Zhang J, Block ER, Patel JM Thioredoxin restores nitric oxide-induced inhibition of protein kinase C activity in lung endothelial cells Mol. Cell Biochem. 2003, 254:47-54.
    • (2003) Cell Biochem. , vol.254 , pp. 47-54
    • Kahlos, K.1    Zhang, J.2    Block, E.R.3    Patel, J.M.4
  • 79
    • 0035849714 scopus 로고    scopus 로고
    • S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation
    • Lane P, Hao G, Gross SS S-nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation. Sci.STKE. 2001, 2001:RE1.
    • (2001) Sci.STKE. , vol.2001
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 81
    • 0034620508 scopus 로고    scopus 로고
    • An apoptotic model for nitrosative stress
    • Eu JP, Liu L, Zeng M, Stamler JS An apoptotic model for nitrosative stress. Biochemistry 2000, 39:1040-1047.
    • (2000) Biochemistry , vol.39 , pp. 1040-1047
    • Eu, J.P.1    Liu, L.2    Zeng, M.3    Stamler, J.S.4
  • 83
    • 9644290748 scopus 로고    scopus 로고
    • In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation
    • Ckless K, Reynaert NL, Taatjes DJ, Lounsbury KM, van der Vliet A, Janssen-Heininger Y In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation. Nitric Oxide 2004, 11:216-227.
    • (2004) Nitric Oxide , vol.11 , pp. 216-227
    • Ckless, K.1    Reynaert, N.L.2    Taatjes, D.J.3    Lounsbury, K.M.4    van der Vliet, A.5    Janssen-Heininger, Y.6
  • 84
    • 20444409884 scopus 로고    scopus 로고
    • Receptor-regulated dynamic S-nitrosylation of endothelial nitric-oxide synthase in vascular endothelial cells
    • Erwin PA, Lin AJ, Golan DE, Michel T Receptor-regulated dynamic S-nitrosylation of endothelial nitric-oxide synthase in vascular endothelial cells. J Biol.Chem. 2005, 280:19888-19894.
    • (2005) J Biol.Chem. , vol.280 , pp. 19888-19894
    • Erwin, P.A.1    Lin, A.J.2    Golan, D.E.3    Michel, T.4
  • 85
    • 33644864135 scopus 로고    scopus 로고
    • Subcellular targeting differential S-nitrosylation of endothelial nitric-oxide synthase
    • Erwin PA, Mitchell DA, Sartoretto J, Marletta MA, Michel T Subcellular targeting differential S-nitrosylation of endothelial nitric-oxide synthase. J Biol.Chem. 2006, 281:151-157.
    • (2006) J Biol.Chem. , vol.281 , pp. 151-157
    • Erwin, P.A.1    Mitchell, D.A.2    Sartoretto, J.3    Marletta, M.A.4    Michel, T.5
  • 88
    • 0036890053 scopus 로고    scopus 로고
    • Concomitant presence of N-nitroso S-nitroso proteins in human plasma
    • Rassaf T, Bryan NS, Kelm M, Feelisch M Concomitant presence of N-nitroso S-nitroso proteins in human plasma. Free Radic Biol.Med. 2002, 33:1590-1596.
    • (2002) Free Radic Biol.Med. , vol.33 , pp. 1590-1596
    • Rassaf, T.1    Bryan, N.S.2    Kelm, M.3    Feelisch, M.4
  • 90
    • 1242351238 scopus 로고    scopus 로고
    • Circulating NO pool: assessment of nitrite nitroso species in blood and tissues
    • Rassaf T, Feelisch M, Kelm M Circulating NO pool: assessment of nitrite nitroso species in blood and tissues. Free Radic Biol.Med. 2004, 36:413-422.
    • (2004) Free Radic Biol.Med. , vol.36 , pp. 413-422
    • Rassaf, T.1    Feelisch, M.2    Kelm, M.3
  • 93
    • 0141961564 scopus 로고    scopus 로고
    • Measurement of physiological S-nitrosothiols: a problem child and a challenge
    • Tsikas D Measurement of physiological S-nitrosothiols: a problem child and a challenge. Nitric Oxide 2003, 9:53-55.
    • (2003) Nitric Oxide , vol.9 , pp. 53-55
    • Tsikas, D.1
  • 95
    • 0033988226 scopus 로고    scopus 로고
    • A chemiluminescense-based assay for S-nitrosoalbumin other plasma S-nitrosothiols
    • Marley R, Feelisch M, Holt S, Moore K A chemiluminescense-based assay for S-nitrosoalbumin other plasma S-nitrosothiols. Free Radic.Res. 2000, 32:1-9.
    • (2000) Free Radic.Res. , vol.32 , pp. 1-9
    • Marley, R.1    Feelisch, M.2    Holt, S.3    Moore, K.4
  • 96
    • 0037251861 scopus 로고    scopus 로고
    • Methodologies for the sensitive specific mea-surement of S-nitrosothiols iron-nitrosyls and nitrite in biological samples
    • Yang BK, Vivas EX, Reiter CD, Gladwin MT Methodologies for the sensitive specific mea-surement of S-nitrosothiols iron-nitrosyls and nitrite in biological samples. Free Radic.Res. 2003, 37:1-10.
    • (2003) Free Radic.Res. , vol.37 , pp. 1-10
    • Yang, B.K.1    Vivas, E.X.2    Reiter, C.D.3    Gladwin, M.T.4
  • 97
    • 0032080124 scopus 로고    scopus 로고
    • Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols
    • Samouilov A, Zweier JL Development of chemiluminescence-based methods for specific quantitation of nitrosylated thiols. Anal.Biochem. 1998, 258:322-330.
    • (1998) Anal.Biochem. , vol.258 , pp. 322-330
    • Samouilov, A.1    Zweier, J.L.2
  • 98
    • 0031795787 scopus 로고    scopus 로고
    • Fluorometric detection of S-nitrosothiols
    • Kostka P, Park JK Fluorometric detection of S-nitrosothiols. Methods Enzymol. 1999, 301:227-235.
    • (1999) Methods Enzymol. , vol.301 , pp. 227-235
    • Kostka, P.1    Park, J.K.2
  • 100
    • 0029160379 scopus 로고
    • Monitoring reactions of nitric oxide with peptides proteins by electrospray ionization-mass spectrometry
    • Mirza UA, Chait BT, Lander HM Monitoring reactions of nitric oxide with peptides proteins by electrospray ionization-mass spectrometry. J Biol.Chem. 1995, 270:17185-17188.
    • (1995) J Biol.Chem. , vol.270 , pp. 17185-17188
    • Mirza, U.A.1    Chait, B.T.2    Lander, H.M.3
  • 101
    • 0033597924 scopus 로고    scopus 로고
    • Mass spectrometric analysis of nitric oxide-modified caspase-3
    • Zech B, Wilm M, van Eldik R, Brune B Mass spectrometric analysis of nitric oxide-modified caspase-3. J Biol.Chem. 1999, 274:20931-20936.
    • (1999) J Biol.Chem. , vol.274 , pp. 20931-20936
    • Zech, B.1    Wilm, M.2    van Eldik, R.3    Brune, B.4
  • 104
    • 14644423288 scopus 로고    scopus 로고
    • Characterization application of the biotin-switch assay for the identification of S-nitrosated proteins
    • Zhang Y, Keszler A, Broniowska KA, Hogg N Characterization application of the biotin-switch assay for the identification of S-nitrosated proteins. Free Radic Biol.Med. 2005, 38:874-881.
    • (2005) Free Radic Biol.Med. , vol.38 , pp. 874-881
    • Zhang, Y.1    Keszler, A.2    Broniowska, K.A.3    Hogg, N.4
  • 105
    • 1042267391 scopus 로고    scopus 로고
    • Detection proteomic identification of S-nitrosylated proteins in endothelial cells
    • Martinez-Ruiz A, Lamas S Detection proteomic identification of S-nitrosylated proteins in endothelial cells. Arch Biochem.Biophys. 2004, 423:192-199.
    • (2004) Arch Biochem.Biophys. , vol.423 , pp. 192-199
    • Martinez-Ruiz, A.1    Lamas, S.2
  • 107
    • 0017144598 scopus 로고
    • Spectroscopic studies of actin-metal-nucleotide complexes
    • Loscalzo J, Reed GH Spectroscopic studies of actin-metal-nucleotide complexes. Biochemistry 1976, 15:5407-5413.
    • (1976) Biochemistry , vol.15 , pp. 5407-5413
    • Loscalzo, J.1    Reed, G.H.2
  • 109
    • 0029743817 scopus 로고    scopus 로고
    • Redox modulation of L-type calcium channels in ferret ventric-ular myocytes. Dual mechanism regulation by nitric oxide S-nitrosothiols
    • Campbell DL, Stamler JS, Strauss HC Redox modulation of L-type calcium channels in ferret ventric-ular myocytes. Dual mechanism regulation by nitric oxide S-nitrosothiols. J Gen.Physiol. 1996, 108:277-293.
    • (1996) J Gen.Physiol. , vol.108 , pp. 277-293
    • Campbell, D.L.1    Stamler, J.S.2    Strauss, H.C.3
  • 111
    • 0030662226 scopus 로고    scopus 로고
    • Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms
    • Kim YM, Talanian RV, Billiar TR Nitric oxide inhibits apoptosis by preventing increases in caspase-3-like activity via two distinct mechanisms. J Biol.Chem. 1997, 272:31138-31148.
    • (1997) J Biol.Chem. , vol.272 , pp. 31138-31148
    • Kim, Y.M.1    Talanian, R.V.2    Billiar, T.R.3
  • 112
    • 0019331580 scopus 로고
    • Determination of interactive thiol ionizations in bovine serum albumin glutathione and other thiols by potentiometric difference titration
    • Lewis SD, Misra DC, Shafer JA Determination of interactive thiol ionizations in bovine serum albumin glutathione and other thiols by potentiometric difference titration. Biochemistry 1980, 19:6129-6137.
    • (1980) Biochemistry , vol.19 , pp. 6129-6137
    • Lewis, S.D.1    Misra, D.C.2    Shafer, J.A.3
  • 116
    • 12244293660 scopus 로고    scopus 로고
    • S-nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense
    • Rhee KY, Erdjument-Bromage H, Tempst P, Nathan CF S-nitroso proteome of Mycobacterium tuberculosis: Enzymes of intermediary metabolism and antioxidant defense. Proc. Natl. Acad Sci.USA 2005, 102:467-472.
    • (2005) Proc. Natl. Acad Sci.USA , vol.102 , pp. 467-472
    • Rhee, K.Y.1    Erdjument-Bromage, H.2    Tempst, P.3    Nathan, C.F.4
  • 119
    • 0036176869 scopus 로고    scopus 로고
    • Potential therapeutic uses for S-nitrosothiols
    • Richardson G, Benjamin N Potential therapeutic uses for S-nitrosothiols. Clin Sci.(Lond.) 2002, 102:99-105.
    • (2002) Clin Sci.(Lond.) , vol.102 , pp. 99-105
    • Richardson, G.1    Benjamin, N.2
  • 121
    • 0034617146 scopus 로고    scopus 로고
    • Inhibition of papain by S-nitrosothiols. Formation of mixed disulfides
    • Xian M, Chen X, Liu Z, Wang K, Wang PG Inhibition of papain by S-nitrosothiols. Formation of mixed disulfides. J Biol.Chem. 2000, 275:20467-20473.
    • (2000) J Biol.Chem. , vol.275 , pp. 20467-20473
    • Xian, M.1    Chen, X.2    Liu, Z.3    Wang, K.4    Wang, P.G.5
  • 122
    • 0034663637 scopus 로고    scopus 로고
    • Reversal of nitric oxide-peroxynitrite-and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light thiols
    • Borutaite V, Budriunaite A, Brown GC Reversal of nitric oxide-peroxynitrite-and S-nitrosothiol-induced inhibition of mitochondrial respiration or complex I activity by light thiols. Biochim Biophys.Acta 2000, 1459:405-412.
    • (2000) Biochim Biophys.Acta , vol.1459 , pp. 405-412
    • Borutaite, V.1    Budriunaite, A.2    Brown, G.C.3
  • 123
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E, Brown GC, Feelisch M, Moncada S Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad Sci.USA 1998, 95:7631-7636.
    • (1998) Proc. Natl. Acad Sci.USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 124
    • 0034057120 scopus 로고    scopus 로고
    • Oxidative stress S-nitrosylation of proteins in cells
    • Beltran B, Orsi A, Clementi E, Moncada S Oxidative stress S-nitrosylation of proteins in cells. Br J.Pharmacol. 2000, 129:953-960.
    • (2000) Br J.Pharmacol. , vol.129 , pp. 953-960
    • Beltran, B.1    Orsi, A.2    Clementi, E.3    Moncada, S.4
  • 126
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase the terminal enzyme of the mitochondrial respiratory chain by nitric oxide. Implications for neurodegenerative d
    • Cleeter MW, Cooper JM, Darley-Usmar VM, Moncada S, Schapira AH Reversible inhibition of cytochrome c oxidase the terminal enzyme of the mitochondrial respiratory chain by nitric oxide. Implications for neurodegenerative d. FEBS Lett. 1994, 345:50-54.
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 127
    • 15444372431 scopus 로고    scopus 로고
    • Nitric oxide-induced persistent inhibition nitrosylation of active site cysteine residues of mitochondrial cytochrome-c oxidase in lung endothelial cells
    • Zhang J, Jin B, Li L, Block ER, Patel JM Nitric oxide-induced persistent inhibition nitrosylation of active site cysteine residues of mitochondrial cytochrome-c oxidase in lung endothelial cells. Am.J Physiol.Cell Physiol. 2005, 288:C840-C849.
    • (2005) Am.J Physiol.Cell Physiol. , vol.288
    • Zhang, J.1    Jin, B.2    Li, L.3    Block, E.R.4    Patel, J.M.5
  • 128
    • 0029875840 scopus 로고    scopus 로고
    • S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control
    • Jia L, Bonaventura C, Bonaventura J, Stamler JS S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature 1996, 380:221-226.
    • (1996) Nature , vol.380 , pp. 221-226
    • Jia, L.1    Bonaventura, C.2    Bonaventura, J.3    Stamler, J.S.4
  • 129
    • 0037008720 scopus 로고    scopus 로고
    • S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment lacks O2/NO-linked allosteric function
    • Gladwin MT, Wang X, Reiter CD, Yang BK, Vivas EX, Bonaventura C, Schechter AN S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment lacks O2/NO-linked allosteric function. J Biol.Chem. 2002, 277:27818-27828.
    • (2002) J Biol.Chem. , vol.277 , pp. 27818-27828
    • Gladwin, M.T.1    Wang, X.2    Reiter, C.D.3    Yang, B.K.4    Vivas, E.X.5    Bonaventura, C.6    Schechter, A.N.7
  • 132
    • 29644432729 scopus 로고    scopus 로고
    • Nitric oxide negatively regulates Fas CD95-induced apoptosis through inhibition of ubiquitin-proteasome-mediated degradation of FLICE inhibitory protein
    • Chanvorachote P, Nimmannit U, Wang L, Stehlik C, Lu B, Azad N, Rojanasakul Y Nitric oxide negatively regulates Fas CD95-induced apoptosis through inhibition of ubiquitin-proteasome-mediated degradation of FLICE inhibitory protein. J Biol.Chem. 2005, 280:42044-42050.
    • (2005) J Biol.Chem. , vol.280 , pp. 42044-42050
    • Chanvorachote, P.1    Nimmannit, U.2    Wang, L.3    Stehlik, C.4    Lu, B.5    Azad, N.6    Rojanasakul, Y.7
  • 133
    • 0347624596 scopus 로고    scopus 로고
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • Kim S, Wing SS, Ponka P S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway. Mol.Cell Biol. 2004, 24:330-337.
    • (2004) Mol.Cell Biol. , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 135
    • 0033673457 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redox-dependent effect of nitrogen oxides
    • Palmer LA, Gaston B, Johns RA Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redox-dependent effect of nitrogen oxides. Mol.Pharmacol. 2000, 58:1197-1203.
    • (2000) Mol.Pharmacol. , vol.58 , pp. 1197-1203
    • Palmer, L.A.1    Gaston, B.2    Johns, R.A.3
  • 136
    • 0035864361 scopus 로고    scopus 로고
    • Accumulation of HIF-1alpha under the influence of nitric oxide
    • Sandau KB, Fandrey J, Brune B Accumulation of HIF-1alpha under the influence of nitric oxide. Blood 2001, 97:1009-1015.
    • (2001) Blood , vol.97 , pp. 1009-1015
    • Sandau, K.B.1    Fandrey, J.2    Brune, B.3
  • 137
    • 0030808955 scopus 로고    scopus 로고
    • Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein
    • Calmels S, Hainaut P, Ohshima H Nitric oxide induces conformational and functional modifications of wild-type p53 tumor suppressor protein. Cancer Res. 1997, 57:3365-3369.
    • (1997) Cancer Res. , vol.57 , pp. 3365-3369
    • Calmels, S.1    Hainaut, P.2    Ohshima, H.3
  • 138
    • 0034899785 scopus 로고    scopus 로고
    • Transcription factors p53 and HIF-1alpha as targets of nitric oxide
    • Brune B, von Knethen A, Sandau KB Transcription factors p53 and HIF-1alpha as targets of nitric oxide. Cell Signal 2001, 13:525-533.
    • (2001) Cell Signal , vol.13 , pp. 525-533
    • Brune, B.1    von Knethen, A.2    Sandau, K.B.3
  • 139
    • 0031037180 scopus 로고    scopus 로고
    • Suppression of apoptosis by nitric oxide via inhi-bition of interleukin-1beta-converting enzyme (ICE) -like cysteine protease protein (CPP) -32-like proteases
    • Dimmeler S, Haendeler J, Nehls M, Zeiher AM Suppression of apoptosis by nitric oxide via inhi-bition of interleukin-1beta-converting enzyme (ICE) -like cysteine protease protein (CPP) -32-like proteases. J Exp.Med. 1997, 185:601-607.
    • (1997) J Exp.Med. , vol.185 , pp. 601-607
    • Dimmeler, S.1    Haendeler, J.2    Nehls, M.3    Zeiher, A.M.4
  • 141
    • 0030706098 scopus 로고    scopus 로고
    • Suppression of neuronal apoptosis by S-nitrosylation of caspases
    • Tenneti L, D'Emilia DM, Lipton SA Suppression of neuronal apoptosis by S-nitrosylation of caspases. Neurosci.Lett. 1997, 236:139-142.
    • (1997) Neurosci.Lett. , vol.236 , pp. 139-142
    • Tenneti, L.1    D'Emilia, D.M.2    Lipton, S.A.3
  • 143
    • 1642280954 scopus 로고    scopus 로고
    • S-Nitrosation regulates the activation of endogenous procaspase-9 in HT-29 human colon carcinoma cells
    • Kim JE, Tannenbaum SR S-Nitrosation regulates the activation of endogenous procaspase-9 in HT-29 human colon carcinoma cells. J Biol.Chem. 2004, 279:9758-9764.
    • (2004) J Biol.Chem. , vol.279 , pp. 9758-9764
    • Kim, J.E.1    Tannenbaum, S.R.2
  • 144
    • 33644818614 scopus 로고    scopus 로고
    • Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine
    • Mitchell DA, Marletta MA Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine. Nat Chem.Biol. 2005, 1:154-158.
    • (2005) Nat Chem.Biol. , vol.1 , pp. 154-158
    • Mitchell, D.A.1    Marletta, M.A.2
  • 145
    • 0037907637 scopus 로고    scopus 로고
    • Nitric oxide donors inhibit formation of the Apaf-1/caspase-9 apoptosome and activation of caspases
    • Zech B, Kohl R, von Knethen A, Brune B Nitric oxide donors inhibit formation of the Apaf-1/caspase-9 apoptosome and activation of caspases. Biochem.J. 2003, 371:1055-1064.
    • (2003) Biochem.J. , vol.371 , pp. 1055-1064
    • Zech, B.1    Kohl, R.2    von Knethen, A.3    Brune, B.4
  • 146
    • 0032549511 scopus 로고    scopus 로고
    • Nitric oxide (NO) disrupts specific DNA binding of the transcription factor c-Myb in vitro
    • Brendeford EM, Andersson KB, Gabrielsen OS Nitric oxide (NO) disrupts specific DNA binding of the transcription factor c-Myb in vitro. FEBS Lett. 1998, 425:52-56.
    • (1998) FEBS Lett. , vol.425 , pp. 52-56
    • Brendeford, E.M.1    Andersson, K.B.2    Gabrielsen, O.S.3
  • 147
    • 0028146764 scopus 로고
    • Modulation of AP-1 activity by nitric oxide (NO) in vitro: NO-mediated modulation of AP-1
    • Tabuchi A, Sano K, Oh E, Tsuchiya T, Tsuda M Modulation of AP-1 activity by nitric oxide (NO) in vitro: NO-mediated modulation of AP-1. FEBS Lett. 1994, 351:123-127.
    • (1994) FEBS Lett. , vol.351 , pp. 123-127
    • Tabuchi, A.1    Sano, K.2    Oh, E.3    Tsuchiya, T.4    Tsuda, M.5
  • 148
    • 1642483507 scopus 로고    scopus 로고
    • S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages
    • Gao C, Guo H, Wei J, Mi Z, Wai P, Kuo PC S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages. J Biol.Chem. 2004, 279:11236-11243.
    • (2004) J Biol.Chem. , vol.279 , pp. 11236-11243
    • Gao, C.1    Guo, H.2    Wei, J.3    Mi, Z.4    Wai, P.5    Kuo, P.C.6
  • 150
    • 14044276372 scopus 로고    scopus 로고
    • Rapid nitric oxide-mediated S-nitrosylation of estrogen receptor: regulation of estrogen-dependent gene transcription
    • Garban HJ, Marquez-Garban DC, Pietras RJ, Ignarro LJ Rapid nitric oxide-mediated S-nitrosylation of estrogen receptor: regulation of estrogen-dependent gene transcription. Proc. Natl. Acad Sci.USA 2005, 102:2632-2636.
    • (2005) Proc. Natl. Acad Sci.USA , vol.102 , pp. 2632-2636
    • Garban, H.J.1    Marquez-Garban, D.C.2    Pietras, R.J.3    Ignarro, L.J.4
  • 151
    • 0033053615 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor binding by nitric oxide
    • Galigniana MD, Piwien-Pilipuk G, Assreuy J Inhibition of glucocorticoid receptor binding by nitric oxide. Mol.Pharmacol. 1999, 55:317-323.
    • (1999) Mol.Pharmacol. , vol.55 , pp. 317-323
    • Galigniana, M.D.1    Piwien-Pilipuk, G.2    Assreuy, J.3
  • 153
    • 15444379675 scopus 로고    scopus 로고
    • S-Nitrosation and regulation of inducible nitric oxide synthase
    • Mitchell DA, Erwin PA, Michel T, Marletta MA S-Nitrosation and regulation of inducible nitric oxide synthase. Biochemistry 2005, 44:4636-4647.
    • (2005) Biochemistry , vol.44 , pp. 4636-4647
    • Mitchell, D.A.1    Erwin, P.A.2    Michel, T.3    Marletta, M.A.4
  • 155
    • 0030456218 scopus 로고    scopus 로고
    • Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc
    • Gergel D, Cederbaum AI Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S nitrosylation and the release of zinc. Biochemistry 1996, 35:16186-16194.
    • (1996) Biochemistry , vol.35 , pp. 16186-16194
    • Gergel, D.1    Cederbaum, A.I.2
  • 156
    • 1442330336 scopus 로고    scopus 로고
    • S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization decreased enzyme activity
    • Ravi K, Brennan LA, Levic S, Ross PA, Black SM S-nitrosylation of endothelial nitric oxide synthase is associated with monomerization decreased enzyme activity. Proc. Natl. Acad Sci.USA 2004, 101:2619-2624.
    • (2004) Proc. Natl. Acad Sci.USA , vol.101 , pp. 2619-2624
    • Ravi, K.1    Brennan, L.A.2    Levic, S.3    Ross, P.A.4    Black, S.M.5
  • 157
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator
    • Ding H, Demple B Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator. Proc. Natl.Acad Sci.USA 2000, 97:5146-5150.
    • (2000) Proc. Natl.Acad Sci.USA , vol.97 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 158
    • 0011759783 scopus 로고    scopus 로고
    • Endotoxin-mediated S-nitrosylation of p50 alters NF-kappa B-dependent gene transcription in ANA-1 murine macrophages
    • DelaTorre A, Schroeder RA, Punzalan C, Kuo PC Endotoxin-mediated S-nitrosylation of p50 alters NF-kappa B-dependent gene transcription in ANA-1 murine macrophages. J.Immunol. 1999, 162:4101-4108.
    • (1999) J.Immunol. , vol.162 , pp. 4101-4108
    • DelaTorre, A.1    Schroeder, R.A.2    Punzalan, C.3    Kuo, P.C.4
  • 159
    • 0031059681 scopus 로고    scopus 로고
    • Nitric oxide regulates nitric oxide synthase-2 gene expression by inhibiting NF-kappaB binding to DNA
    • Pt 2
    • Park SK, Lin HL, Murphy S Nitric oxide regulates nitric oxide synthase-2 gene expression by inhibiting NF-kappaB binding to DNA. Biochem.J. 1997, 322:609-613. Pt 2.
    • (1997) Biochem.J. , vol.322 , pp. 609-613
    • Park, S.K.1    Lin, H.L.2    Murphy, S.3
  • 160
    • 0031590264 scopus 로고    scopus 로고
    • Alteration of NF-kappa B p50 DNA binding kinetics by S-nitrosylation
    • DelaTorre A, Schroeder RA, Kuo PC Alteration of NF-kappa B p50 DNA binding kinetics by S-nitrosylation. Biochem.Biophys Res.Commun. 1997, 238:703-706.
    • (1997) Biochem.Biophys Res.Commun. , vol.238 , pp. 703-706
    • DelaTorre, A.1    Schroeder, R.A.2    Kuo, P.C.3
  • 162
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B by S-nitrosylation
    • Marshall HE, Stamler JS Inhibition of NF-kappa B by S-nitrosylation. Biochemistry 2001, 40:1688-1693.
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 163
    • 0030608668 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB DNA binding nitric oxide induction in human T cells and lung adenocarcinoma cells by selenite treatment
    • Kim IY, Stadtman TC Inhibition of NF-kappaB DNA binding nitric oxide induction in human T cells and lung adenocarcinoma cells by selenite treatment. Proc. Natl.Acad Sci.USA 1997, 94:12904-12907.
    • (1997) Proc. Natl.Acad Sci.USA , vol.94 , pp. 12904-12907
    • Kim, I.Y.1    Stadtman, T.C.2
  • 165
    • 0029011129 scopus 로고
    • Induction stabilization of I kappa B alpha by nitric oxide mediates inhibition of NF-kappa B
    • Peng HB, Libby P, Liao JK Induction stabilization of I kappa B alpha by nitric oxide mediates inhibition of NF-kappa B. J Biol.Chem. 1995, 270:14214-14219.
    • (1995) J Biol.Chem. , vol.270 , pp. 14214-14219
    • Peng, H.B.1    Libby, P.2    Liao, J.K.3
  • 166
    • 0037072883 scopus 로고    scopus 로고
    • Nitrosative stress-induced apoptosis through inhibition of NF-kappa B
    • Marshall HE, Stamler JS Nitrosative stress-induced apoptosis through inhibition of NF-kappa B. J Biol.Chem. 2002, 277:34223-34228.
    • (2002) J Biol.Chem. , vol.277 , pp. 34223-34228
    • Marshall, H.E.1    Stamler, J.S.2
  • 168
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases
    • Metzen E, Zhou J, Jelkmann W, Fandrey J, Brune B Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases. Mol Biol.Cell 2003, 14:3470-3481.
    • (2003) Mol Biol.Cell , vol.14 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 169
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity
    • Yasinska IM, Sumbayev VV S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett. 2003, 549:105-109.
    • (2003) FEBS Lett. , vol.549 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 170
    • 0028786601 scopus 로고
    • A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter
    • Melillo G, Musso T, Sica A, Taylor LS, Cox GW, Varesio L A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter. J Exp.Med. 1995, 182:1683-1693.
    • (1995) J Exp.Med. , vol.182 , pp. 1683-1693
    • Melillo, G.1    Musso, T.2    Sica, A.3    Taylor, L.S.4    Cox, G.W.5    Varesio, L.6
  • 171
    • 0031888729 scopus 로고    scopus 로고
    • Hypoxia induces type II NOS gene expression in pulmonary artery endothelial cells via HIF-1
    • Palmer LA, Semenza GL, Stoler MH, Johns RA Hypoxia induces type II NOS gene expression in pulmonary artery endothelial cells via HIF-1. Am J.Physiol. 1998, 274:L212-L219.
    • (1998) Am J.Physiol. , vol.274
    • Palmer, L.A.1    Semenza, G.L.2    Stoler, M.H.3    Johns, R.A.4
  • 172
    • 0030986262 scopus 로고    scopus 로고
    • Interactive effects of nitric oxide and the p53 tumor suppressor gene in carcinogenesis and tumor progression
    • Ambs S, Hussain SP, Harris CC Interactive effects of nitric oxide and the p53 tumor suppressor gene in carcinogenesis and tumor progression. Faseb J. 1997, 11:443-448.
    • (1997) Faseb J. , vol.11 , pp. 443-448
    • Ambs, S.1    Hussain, S.P.2    Harris, C.C.3
  • 173
    • 0347683478 scopus 로고    scopus 로고
    • Shear stress regulates endothelial nitric-oxide synthase promoter activity through nuclear factor kappaB binding
    • Davis ME, Grumbach IM, Fukai T, Cutchins A, Harrison DG Shear stress regulates endothelial nitric-oxide synthase promoter activity through nuclear factor kappaB binding. J Biol.Chem. 2004, 279:163-168.
    • (2004) J Biol.Chem. , vol.279 , pp. 163-168
    • Davis, M.E.1    Grumbach, I.M.2    Fukai, T.3    Cutchins, A.4    Harrison, D.G.5
  • 175
  • 178
    • 0033574565 scopus 로고    scopus 로고
    • S-nitrosation ameliorates homocysteine-induced neurotoxicity and calcium responses in primary culture of rat cortical neurons
    • Kim WK S-nitrosation ameliorates homocysteine-induced neurotoxicity and calcium responses in primary culture of rat cortical neurons. Neurosci.Lett. 1999, 265:99-102.
    • (1999) Neurosci.Lett. , vol.265 , pp. 99-102
    • Kim, W.K.1
  • 181
    • 0034685883 scopus 로고    scopus 로고
    • A single intracellular cysteine residue is responsible for the activation of the olfactory cyclic nucleotide-gated channel by NO
    • Broillet MC A single intracellular cysteine residue is responsible for the activation of the olfactory cyclic nucleotide-gated channel by NO. J Biol.Chem. 2000, 275:15135-15141.
    • (2000) J Biol.Chem. , vol.275 , pp. 15135-15141
    • Broillet, M.C.1
  • 182
    • 2442717744 scopus 로고    scopus 로고
    • NO stimulation of ATP-sensitive potassium channels: Involvement of Ras/mitogen-activated protein kinase pathway contribution to neuroprotection
    • Lin YF, Raab-Graham K, Jan YN, Jan LY NO stimulation of ATP-sensitive potassium channels: Involvement of Ras/mitogen-activated protein kinase pathway contribution to neuroprotection. Proc. Natl. Acad Sci.USA 2004, 101:7799-7804.
    • (2004) Proc. Natl. Acad Sci.USA , vol.101 , pp. 7799-7804
    • Lin, Y.F.1    Raab-Graham, K.2    Jan, Y.N.3    Jan, L.Y.4
  • 185
    • 0032498185 scopus 로고    scopus 로고
    • Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation
    • Xu L, Eu JP, Meissner G, Stamler JS Activation of the cardiac calcium release channel (ryanodine receptor) by poly-S-nitrosylation. Science 1998, 279:234-237.
    • (1998) Science , vol.279 , pp. 234-237
    • Xu, L.1    Eu, J.P.2    Meissner, G.3    Stamler, J.S.4
  • 186
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J, Xin C, Eu JP, Stamler JS, Meissner G Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc. Natl.Acad Sci.USA 2001, 98:11158-11162.
    • (2001) Proc. Natl.Acad Sci.USA , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 187
    • 0037424471 scopus 로고    scopus 로고
    • Nitric oxide NOC-12 S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric functi in S-nitrosylation of the channel
    • Sun J, Xu L, Eu JP, Stamler JS, Meissner G Nitric oxide NOC-12 S-nitrosoglutathione modulate the skeletal muscle calcium release channel/ryanodine receptor by different mechanisms. An allosteric functi in S-nitrosylation of the channel. J Biol.Chem. 2003, 278:8184-8189.
    • (2003) J Biol.Chem. , vol.278 , pp. 8184-8189
    • Sun, J.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 189
    • 0035844120 scopus 로고    scopus 로고
    • Classes of thiols that influence the activity of the skeletal muscle calcium release channel
    • Sun J, Xu L, Eu JP, Stamler JS, Meissner G Classes of thiols that influence the activity of the skeletal muscle calcium release channel. J Biol.Chem. 2001, 276:15625-15630.
    • (2001) J Biol.Chem. , vol.276 , pp. 15625-15630
    • Sun, J.1    Xu, L.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 192
    • 0034687778 scopus 로고    scopus 로고
    • Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated protein kinase by means of S-nitrosylation
    • Park HS, Huh SH, Kim MS, Lee SH, Choi EJ Nitric oxide negatively regulates c-Jun N-terminal kinase/stress-activated protein kinase by means of S-nitrosylation. Proc. Natl. Acad Sci.USA 2000, 97:14382-14387.
    • (2000) Proc. Natl. Acad Sci.USA , vol.97 , pp. 14382-14387
    • Park, H.S.1    Huh, S.H.2    Kim, M.S.3    Lee, S.H.4    Choi, E.J.5
  • 193
    • 0030870368 scopus 로고    scopus 로고
    • Nitric oxide reversibly inhibits the epidermal growth factor receptor tyrosine kinase
    • Pt 2
    • Estrada C, Gomez C, Martin-Nieto J, De Frutos T, Jimenez A, Villalobo A Nitric oxide reversibly inhibits the epidermal growth factor receptor tyrosine kinase. Biochem.J. 1997, 326:369-376. Pt 2.
    • (1997) Biochem.J. , vol.326 , pp. 369-376
    • Estrada, C.1    Gomez, C.2    Martin-Nieto, J.3    De Frutos, T.4    Jimenez, A.5    Villalobo, A.6
  • 194
    • 1542320091 scopus 로고    scopus 로고
    • Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism
    • Park HS, Yu JW, Cho JH, Kim MS, Huh SH, Ryoo K, Choi EJ Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism. J Biol.Chem. 2004, 279:7584-7590.
    • (2004) J Biol.Chem. , vol.279 , pp. 7584-7590
    • Park, H.S.1    Yu, J.W.2    Cho, J.H.3    Kim, M.S.4    Huh, S.H.5    Ryoo, K.6    Choi, E.J.7
  • 195
    • 0038511319 scopus 로고    scopus 로고
    • S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1
    • Sumbayev VV S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1. Arch Biochem.Biophys. 2003, 415:133-136.
    • (2003) Arch Biochem.Biophys. , vol.415 , pp. 133-136
    • Sumbayev, V.V.1
  • 196
    • 0033520310 scopus 로고    scopus 로고
    • Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent Tyr-416-linked mechanism
    • Akhand AA, Pu M, Senga T, Kato M, Suzuki H, Miyata T, Hamaguchi M, Nakashima I Nitric oxide controls src kinase activity through a sulfhydryl group modification-mediated Tyr-527-independent Tyr-416-linked mechanism. J Biol.Chem. 1999, 274:25821-25826.
    • (1999) J Biol.Chem. , vol.274 , pp. 25821-25826
    • Akhand, A.A.1    Pu, M.2    Senga, T.3    Kato, M.4    Suzuki, H.5    Miyata, T.6    Hamaguchi, M.7    Nakashima, I.8
  • 197
    • 0028866021 scopus 로고
    • In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide
    • Caselli A, Chiarugi P, Camici G, Manao G, Ramponi G In vivo inactivation of phosphotyrosine protein phosphatases by nitric oxide. FEBS Lett. 1995, 374:249-252.
    • (1995) FEBS Lett. , vol.374 , pp. 249-252
    • Caselli, A.1    Chiarugi, P.2    Camici, G.3    Manao, G.4    Ramponi, G.5
  • 198
    • 0033046078 scopus 로고    scopus 로고
    • Nitric oxide superoxide inhibit platelet-derived growth factor receptor phosphotyrosine phosphatases
    • Callsen D, Sandau KB, Brune B. Nitric oxide superoxide inhibit platelet-derived growth factor receptor phosphotyrosine phosphatases. Free Radic Biol.Med. 1999, 26:1544-1553.
    • (1999) Free Radic Biol.Med. , vol.26 , pp. 1544-1553
    • Callsen, D.1    Sandau, K.B.2    Brune, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.