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Volumn 11, Issue 5, 2006, Pages 194-206

NO• chemistry: A diversity of targets in the cell

Author keywords

Modification; Nitric oxide; Reactive nitrogen species

Indexed keywords

ARGININE; BIOLOGICAL MARKER; CYSTEINE; DOUBLE STRANDED DNA; HISTIDINE; IRON REGULATORY PROTEIN 1; LYSINE; METHIONINE; MITOCHONDRIAL DNA; NITRIC OXIDE; PHENYLALANINE; REACTIVE NITROGEN SPECIES; RNA BINDING PROTEIN; SELENOCYSTEINE; SINGLE STRANDED DNA; TRYPTOPHAN; TYROSINE;

EID: 33750967378     PISSN: 13510002     EISSN: 13510002     Source Type: Journal    
DOI: 10.1179/135100006X116718     Document Type: Review
Times cited : (37)

References (173)
  • 1
    • 0000220064 scopus 로고
    • The basic chemistry of nitric oxide and its possible biological reactions
    • Fontecave MP, Pierre JL. The basic chemistry of nitric oxide and its possible biological reactions. Bull Soc Chim Fr 1994; 131: 620-631.
    • (1994) Bull Soc Chim Fr , vol.131 , pp. 620-631
    • Fontecave, M.P.1    Pierre, J.L.2
  • 2
    • 1042298162 scopus 로고    scopus 로고
    • Reactive nitrogen species in the chemical biology of inflammation
    • Dedon PC, Tannenbaum SR. Reactive nitrogen species in the chemical biology of inflammation. Arch Biochem Biophys 2004; 423: 12-22.
    • (2004) Arch Biochem Biophys , vol.423 , pp. 12-22
    • Dedon, P.C.1    Tannenbaum, S.R.2
  • 3
    • 0001373384 scopus 로고
    • Kinetics of N-nitrosation in oxygenated nitric oxide solutions at physiological pH: Role of nitrous anhydride and effects of phosphate and chloride
    • Lewis RS, Tannenbaum SR, Deen WM. Kinetics of N-nitrosation in oxygenated nitric oxide solutions at physiological pH: role of nitrous anhydride and effects of phosphate and chloride. J Am Chem Soc 1995; 117: 3933-3939.
    • (1995) J Am Chem Soc , vol.117 , pp. 3933-3939
    • Lewis, R.S.1    Tannenbaum, S.R.2    Deen, W.M.3
  • 4
    • 0028070186 scopus 로고
    • Kinetics of the reaction of nitric oxide with oxygen in aqueous solutions
    • Lewis RS, Deen WM. Kinetics of the reaction of nitric oxide with oxygen in aqueous solutions. Chem Res Toxicol 1994; 7: 568-574.
    • (1994) Chem Res Toxicol , vol.7 , pp. 568-574
    • Lewis, R.S.1    Deen, W.M.2
  • 5
    • 0035839611 scopus 로고    scopus 로고
    • Distinction between nitrosating mechanisms within human cells and aqueous solution
    • Espey MG, Miranda KM, Thomas DD, Wink DA. Distinction between nitrosating mechanisms within human cells and aqueous solution. J Biol Chem 2001; 276: 30085-30091.
    • (2001) J Biol Chem , vol.276 , pp. 30085-30091
    • Espey, M.G.1    Miranda, K.M.2    Thomas, D.D.3    Wink, D.A.4
  • 6
    • 0036273095 scopus 로고    scopus 로고
    • A chemical perspective on the interplay between NO, reactive oxygen species, and reactive nitrogen species
    • Espey MG, Miranda KM, Thomas DD et al. A chemical perspective on the interplay between NO, reactive oxygen species, and reactive nitrogen species. Ann NY Acad Sci 2002; 962: 195-206.
    • (2002) Ann NY Acad Sci , vol.962 , pp. 195-206
    • Espey, M.G.1    Miranda, K.M.2    Thomas, D.D.3
  • 8
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J Biol Chem 1991; 266: 4244-4250.
    • (1991) J Biol Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 12
    • 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
  • 13
    • 0033534725 scopus 로고    scopus 로고
    • Kinetics of peroxynitrite reaction with amino acids and human serum albumin
    • Alvarez B, Ferrer-Sueta G, Freeman BA, Radi R. Kinetics of peroxynitrite reaction with amino acids and human serum albumin. J Biol Chem 1999; 274: 842-848.
    • (1999) J Biol Chem , vol.274 , pp. 842-848
    • Alvarez, B.1    Ferrer-Sueta, G.2    Freeman, B.A.3    Radi, R.4
  • 14
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC. Nitrosylation: the prototypic: redox-based signaling mechanism. Cell 2001; 106: 675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 15
    • 0030956929 scopus 로고    scopus 로고
    • (S)NO signals: Translocation, regulation, and a consensus motif
    • Stamler JS, Toone EJ, Lipton SA, Sucher NJ. (S)NO signals: translocation, regulation, and a consensus motif. Neuron 1997; 18: 691-696.
    • (1997) Neuron , vol.18 , pp. 691-696
    • Stamler, J.S.1    Toone, E.J.2    Lipton, S.A.3    Sucher, N.J.4
  • 16
    • 33646580362 scopus 로고    scopus 로고
    • Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells
    • Greco TM, Hodara. R, Parastatidis I et al. Identification of S-nitrosylation motifs by site-specific mapping of the S-nitrosocysteine proteome in human vascular smooth muscle cells. Proc Natl Acad Sci USA 2006; 103: 7420-7425.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7420-7425
    • Greco, T.M.1    Hodara, R.2    Parastatidis, I.3
  • 18
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxiredoxins
    • Bryk R, Griffin P, Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 2000; 407: 211-215.
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 19
    • 0042974241 scopus 로고    scopus 로고
    • Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite
    • Carballal S, Radi R, Kirk MC, Barnes S, Freeman BA, Alvarez B. Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry 2003; 42: 9906-9914.
    • (2003) Biochemistry , vol.42 , pp. 9906-9914
    • Carballal, S.1    Radi, R.2    Kirk, M.C.3    Barnes, S.4    Freeman, B.A.5    Alvarez, B.6
  • 20
    • 0035971225 scopus 로고    scopus 로고
    • Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
    • Bonini MG, Augusto O. Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite. J Biol Chem 2001; 276: 9749-9754.
    • (2001) J Biol Chem , vol.276 , pp. 9749-9754
    • Bonini, M.G.1    Augusto, O.2
  • 21
    • 0033610904 scopus 로고    scopus 로고
    • S-nitroglutathione, a product of the reaction between peroxynitrite and glutathione that generates nitric oxide
    • Balazy M, Kaminski PM, Mao K, Tan J, Wolin MS. S-nitroglutathione, a product of the reaction between peroxynitrite and glutathione that generates nitric oxide. J Biol Chem 1998; 273: 32009-32015.
    • (1998) J Biol Chem , vol.273 , pp. 32009-32015
    • Balazy, M.1    Kaminski, P.M.2    Mao, K.3    Tan, J.4    Wolin, M.S.5
  • 22
    • 0027974136 scopus 로고
    • One and two-electron oxidations of methionine by peroxynitrite
    • Pryor WA, Jin X, Squadrito GL. One and two-electron oxidations of methionine by peroxynitrite. Proc Natl Acad Sci USA 1994; 91: 11173-11177.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11173-11177
    • Pryor, W.A.1    Jin, X.2    Squadrito, G.L.3
  • 23
    • 0034657371 scopus 로고    scopus 로고
    • The quantitative oxidation of methionine to methionine sulfoxide by peroxynitrite
    • Perrin D, Koppenol WH. The quantitative oxidation of methionine to methionine sulfoxide by peroxynitrite. Arch Biochem Biophys 2000; 377:266-272.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 266-272
    • Perrin, D.1    Koppenol, W.H.2
  • 24
    • 0032539899 scopus 로고    scopus 로고
    • Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: Both modifications mimic effects of adenylylation
    • Berlett BS, Levine RL, Stadtman ER. Carbon dioxide stimulates peroxynitrite-mediated nitration of tyrosine residues and inhibits oxidation of methionine residues of glutamine synthetase: both modifications mimic effects of adenylylation. Proc Natl Acad Sci USA 1998; 95:2784-2789.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2784-2789
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 25
    • 0032411442 scopus 로고    scopus 로고
    • Kinetic study of the reaction of glutathione peroxidase with peroxynitrite
    • Briviba K, Kissner R, Koppenol WH, Sies H. Kinetic study of the reaction of glutathione peroxidase with peroxynitrite. Chem Res Toxicol 1998; 11: 1398-1401.
    • (1998) Chem Res Toxicol , vol.11 , pp. 1398-1401
    • Briviba, K.1    Kissner, R.2    Koppenol, W.H.3    Sies, H.4
  • 26
    • 0030834975 scopus 로고    scopus 로고
    • Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase
    • Sies H, Sharov VS, Klotz LO, Briviba K. Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase. J Biol Chem 1997; 272: 27812-27817.
    • (1997) J Biol Chem , vol.272 , pp. 27812-27817
    • Sies, H.1    Sharov, V.S.2    Klotz, L.O.3    Briviba, K.4
  • 27
    • 33744965588 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of selenoprotein glutathione peroxidase: A computational study
    • Prabhakar R, Morokuma K, Musaev DG. Peroxynitrite reductase activity of selenoprotein glutathione peroxidase: a computational study. Biochemistry 2006; 45: 6967-6977.
    • (2006) Biochemistry , vol.45 , pp. 6967-6977
    • Prabhakar, R.1    Morokuma, K.2    Musaev, D.G.3
  • 28
    • 0037124020 scopus 로고    scopus 로고
    • A tale of two controversies: Defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species
    • Brennan ML, Wu W, Fu X et al. A tale of two controversies: defining both the role of peroxidases in nitrotyrosine formation in vivo using eosinophil peroxidase and myeloperoxidase-deficient mice, and the nature of peroxidase-generated reactive nitrogen species. J Biol Chem 2002; 277: 17415-17427.
    • (2002) J Biol Chem , vol.277 , pp. 17415-17427
    • Brennan, M.L.1    Wu, W.2    Fu, X.3
  • 29
    • 0032147208 scopus 로고    scopus 로고
    • Biological tyrosine nitration: A pathophysiological function of nitric oxide and reactive oxygen species
    • Ischiropoulos H. Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive oxygen species. Arch Biochem Biophys 1998; 356: 1-11.
    • (1998) Arch Biochem Biophys , vol.356 , pp. 1-11
    • Ischiropoulos, H.1
  • 30
    • 0038731081 scopus 로고    scopus 로고
    • Molecular basis for the selectivity of protein tyrosine nitration in vivo
    • Ischiropoulos H. Molecular basis for the selectivity of protein tyrosine nitration in vivo. Biochem Biophys Res Commun 2003; 305: 776-783.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 31
    • 0344196903 scopus 로고    scopus 로고
    • NO-dependent protein nitration: A cell signaling event or an oxidative inflammatory response?
    • Schopfer FJ, Baker PR, Freeman BA. NO-dependent protein nitration: a cell signaling event or an oxidative inflammatory response? Trends Biochem Sci 2003; 28: 646-654.
    • (2003) Trends Biochem Sci , vol.28 , pp. 646-654
    • Schopfer, F.J.1    Baker, P.R.2    Freeman, B.A.3
  • 32
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: Localization, quantification, consequences for protein function and signal transduction
    • Greenacre SA, Ischiropoulos H. Tyrosine nitration: localization, quantification, consequences for protein function and signal transduction. Free Radic Res 2001; 34: 541-581.
    • (2001) Free Radic Res , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 33
    • 33645961872 scopus 로고    scopus 로고
    • Nitrotyrosine proteome survey in asthma identifies oxidative mechanism of catalase inactivation
    • Ghosh S, Janocha AJ, Aronica MA et al. Nitrotyrosine proteome survey in asthma identifies oxidative mechanism of catalase inactivation. J Immunol 2006; 176: 5587-5597.
    • (2006) J Immunol , vol.176 , pp. 5587-5597
    • Ghosh, S.1    Janocha, A.J.2    Aronica, M.A.3
  • 35
    • 0035832914 scopus 로고    scopus 로고
    • Modification of a single tryptophan residue in human Cu,Zn-superoxide dismutase by peroxynitrite in the presence of bicarbonate
    • Yamakura F, Matsumoto T, Fujimara T et al. Modification of a single tryptophan residue in human Cu,Zn-superoxide dismutase by peroxynitrite in the presence of bicarbonate. Biochim Biophys Acta 2001; 1548: 38-46.
    • (2001) Biochim Biophys Acta , vol.1548 , pp. 38-46
    • Yamakura, F.1    Matsumoto, T.2    Fujimara, T.3
  • 36
    • 0036877403 scopus 로고    scopus 로고
    • Structural features of proteins responsible for resistance to tryptophan residues to nitrosylation
    • Suntsova TP, Beva NV, Nedospasov AA. Structural features of proteins responsible for resistance to tryptophan residues to nitrosylation. IUBMB Life 2002; 54: 281-292.
    • (2002) IUBMB Life , vol.54 , pp. 281-292
    • Suntsova, T.P.1    Beva, N.V.2    Nedospasov, A.A.3
  • 37
    • 0031045787 scopus 로고    scopus 로고
    • One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: Evidence for the formation of protein tryptophan-centred radicals
    • Pietraforte D, Minetti M. One-electron oxidation pathway of peroxynitrite decomposition in human blood plasma: evidence for the formation of protein tryptophan-centred radicals. Biochem J 1997; 321: 743-750.
    • (1997) Biochem J , vol.321 , pp. 743-750
    • Pietraforte, D.1    Minetti, M.2
  • 38
    • 0028207642 scopus 로고
    • Aromatic hydroxylation and nitration of phenylalanine and tyrosine by peroxynitrite. Evidence for hydroxyl radical production from peroxynitrite
    • Van der Vliet A, O'Neill CA, Halliwell B, Cross CE, Kaur H. Aromatic hydroxylation and nitration of phenylalanine and tyrosine by peroxynitrite. Evidence for hydroxyl radical production from peroxynitrite. FEBS Lett 1994; 339: 89-92.
    • (1994) FEBS Lett , vol.339 , pp. 89-92
    • Van der Vliet, A.1    O'Neill, C.A.2    Halliwell, B.3    Cross, C.E.4    Kaur, H.5
  • 39
    • 0034904122 scopus 로고    scopus 로고
    • 6-Hydroxydopamine increases the hydroxylation and nitration of phenylalanine in vivo: Implication of peroxynitrite formation
    • Ferger B, Themann C, Rose S, Halliwell B, Jenner P. 6-Hydroxydopamine increases the hydroxylation and nitration of phenylalanine in vivo: implication of peroxynitrite formation. J Neurochem 2001; 78: 509-514.
    • (2001) J Neurochem , vol.78 , pp. 509-514
    • Ferger, B.1    Themann, C.2    Rose, S.3    Halliwell, B.4    Jenner, P.5
  • 40
    • 15444380683 scopus 로고    scopus 로고
    • N-nitrosations of basic amino acid residues in polypeptide
    • Kuo WN, Ivy D, Guruvadoo L, White A, Graham L. N-nitrosations of basic amino acid residues in polypeptide. Front Biosci 2004; 9: 3163-3166.
    • (2004) Front Biosci , vol.9 , pp. 3163-3166
    • Kuo, W.N.1    Ivy, D.2    Guruvadoo, L.3    White, A.4    Graham, L.5
  • 41
    • 2542496880 scopus 로고    scopus 로고
    • N-nitrosation and denitrosation on lysine residues of histories
    • Kuo WN, Ivy D, Robinson MJ. N-nitrosation and denitrosation on lysine residues of histories. Front Biosci 2004; 9: 187-191.
    • (2004) Front Biosci , vol.9 , pp. 187-191
    • Kuo, W.N.1    Ivy, D.2    Robinson, M.J.3
  • 42
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B, Radi R. Peroxynitrite reactivity with amino acids and proteins. Amino Acids 2003; 25: 295-311.
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 43
    • 4043159127 scopus 로고    scopus 로고
    • Inactivation of human Cu,Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical
    • Alvarez B, Demicheli V, Duran R et al. Inactivation of human Cu,Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical. Free Radic Biol Med 2004; 37: 813-822.
    • (2004) Free Radic Biol Med , vol.37 , pp. 813-822
    • Alvarez, B.1    Demicheli, V.2    Duran, R.3
  • 44
    • 0034891783 scopus 로고    scopus 로고
    • Oxidative modification of proteins during aging
    • Levine RL, Stadtman ER. Oxidative modification of proteins during aging. Exp Gerontol 2001; 36: 1495-1502.
    • (2001) Exp Gerontol , vol.36 , pp. 1495-1502
    • Levine, R.L.1    Stadtman, E.R.2
  • 45
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean RT, Shanlin FU, Stocker R, Davies MJ. Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 1997; 324: 1-18.
    • (1997) Biochem J , vol.324 , pp. 1-18
    • Dean, R.T.1    Shanlin, F.U.2    Stocker, R.3    Davies, M.J.4
  • 46
    • 0033529262 scopus 로고    scopus 로고
    • Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concentration: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation
    • Tien M, Berlett BS, Levine RL, Chock PB, Stadtman ER. Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concentration: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation. Proc Natl Acad Sci USA 1999; 96: 7809-7814.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7809-7814
    • Tien, M.1    Berlett, B.S.2    Levine, R.L.3    Chock, P.B.4    Stadtman, E.R.5
  • 47
    • 15244350287 scopus 로고    scopus 로고
    • Nitric oxide-related species-induced protein oxidation: Reversible, irreversible, and protective effects on enzyme function of papain
    • Vaananen AJ, Kankuri E, Rauhala P. Nitric oxide-related species-induced protein oxidation: reversible, irreversible, and protective effects on enzyme function of papain. Free Radic Biol Med 2005; 38: 1102-1111.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1102-1111
    • Vaananen, A.J.1    Kankuri, E.2    Rauhala, P.3
  • 48
    • 0020485917 scopus 로고
    • Activation of purified guanylate cyclase by nitric oxide requires heme. Comparison of heme-deficient, heme-reconstituted and hemecontaining forms of soluble enzyme from bovine lung
    • Ignarro L, Degnan JN, Baricos WH, Kadowitz PJ, Wolin MS. Activation of purified guanylate cyclase by nitric oxide requires heme. Comparison of heme-deficient, heme-reconstituted and hemecontaining forms of soluble enzyme from bovine lung. Biochim Biophys Acta 1982; 718: 49-59.
    • (1982) Biochim Biophys Acta , vol.718 , pp. 49-59
    • Ignarro, L.1    Degnan, J.N.2    Baricos, W.H.3    Kadowitz, P.J.4    Wolin, M.S.5
  • 49
    • 0032951905 scopus 로고    scopus 로고
    • Nitric oxide and iron proteins
    • Cooper CE. Nitric oxide and iron proteins. Biochim Biophys Acta 1999; 1411: 290-309.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 290-309
    • Cooper, C.E.1
  • 50
    • 0030197587 scopus 로고    scopus 로고
    • Modulation by nitric oxide of metalloprotein regulatory effects
    • Drapier JC, Bouton C. Modulation by nitric oxide of metalloprotein regulatory effects. Bioessays 1996; 18: 549-556.
    • (1996) Bioessays , vol.18 , pp. 549-556
    • Drapier, J.C.1    Bouton, C.2
  • 51
    • 0032899131 scopus 로고    scopus 로고
    • The reactions of copper proteins with nitric oxide
    • Torres J, Wilson MT. The reactions of copper proteins with nitric oxide. Biochim Biophys Acta 1999; 1411: 310-322.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 310-322
    • Torres, J.1    Wilson, M.T.2
  • 52
    • 0036083783 scopus 로고    scopus 로고
    • NO running on MT: Regulation of zinc homeostasis by interaction of nitric oxide with metallothionein
    • Gow A, Ischiropoulos H. NO running on MT: regulation of zinc homeostasis by interaction of nitric oxide with metallothionein. Am J Physiol 2002; 282: L183-L184.
    • (2002) Am J Physiol , vol.282
    • Gow, A.1    Ischiropoulos, H.2
  • 53
    • 0034859653 scopus 로고    scopus 로고
    • Zinc finger proteins as molecular targets for nitric oxide-mediated gene regulation
    • Kroncke KD. Zinc finger proteins as molecular targets for nitric oxide-mediated gene regulation. Antioxid Redox Signal 2001; 3: 565-575.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 565-575
    • Kroncke, K.D.1
  • 54
    • 0032769550 scopus 로고    scopus 로고
    • Interactions of nitric oxide with hemoproteins: Roles of nitric oxide in mitochondria
    • Henry Y, Guissani A. Interactions of nitric oxide with hemoproteins: roles of nitric oxide in mitochondria. Cell Mol Life Sci 1999; 55: 1003-1014.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1003-1014
    • Henry, Y.1    Guissani, A.2
  • 55
    • 0032902722 scopus 로고    scopus 로고
    • Guanylate cyclase and the NO/cGMP signaling pathway
    • Denninger JW, Marletta MA. Guanylate cyclase and the NO/cGMP signaling pathway. Biochim Biophys Acta 1999; 1411: 334-350.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 334-350
    • Denninger, J.W.1    Marletta, M.A.2
  • 57
    • 0029739154 scopus 로고    scopus 로고
    • Inhibition of cytochrome P450 enzymes by nitric oxide
    • Stadler J, Schmalix WA, Doehmer J. Inhibition of cytochrome P450 enzymes by nitric oxide. Adv Exp Med Biol 1996; 387: 187-193.
    • (1996) Adv Exp Med Biol , vol.387 , pp. 187-193
    • Stadler, J.1    Schmalix, W.A.2    Doehmer, J.3
  • 58
    • 0032483454 scopus 로고    scopus 로고
    • Heme and the endothelium: Effects of nitric oxide on catalytic iron and heme degradation by heme oxygenase
    • Juckett M, Zheng Y, Yuan H et al. Heme and the endothelium: effects of nitric oxide on catalytic iron and heme degradation by heme oxygenase. J Biol Chem 1998; 273: 23388-23397.
    • (1998) J Biol Chem , vol.273 , pp. 23388-23397
    • Juckett, M.1    Zheng, Y.2    Yuan, H.3
  • 59
    • 0028058917 scopus 로고
    • Cytokine-induced expression of nitric oxide synthase results in nitrosylation of heme and nonheme iron proteins in vascular smooth muscle cells
    • Geng YJ, Petersson AS, Wennmalm A, Hansson GK. Cytokine-induced expression of nitric oxide synthase results in nitrosylation of heme and nonheme iron proteins in vascular smooth muscle cells. Exp Cell Res 1994; 214: 418-428.
    • (1994) Exp Cell Res , vol.214 , pp. 418-428
    • Geng, Y.J.1    Petersson, A.S.2    Wennmalm, A.3    Hansson, G.K.4
  • 60
    • 0034098690 scopus 로고    scopus 로고
    • The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex
    • Ueno Y, Yoshimura T. The physiological activity and in vivo distribution of dinitrosyl dithiolato iron complex. Jpn J Pharmacol 2000;82:95-101.
    • (2000) Jpn J Pharmacol , vol.82 , pp. 95-101
    • Ueno, Y.1    Yoshimura, T.2
  • 63
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols
    • Brown GC, Borutaite V. Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols. Biochim Biophys Acta 2004; 1658: 44-49.
    • (2004) Biochim Biophys Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 64
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina A, Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch Biochem Biophys 1996; 328: 309-316.
    • (1996) Arch Biochem Biophys , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 65
    • 0032807550 scopus 로고    scopus 로고
    • Nitrosative and oxidative modulation of iron regulatory proteins
    • Bouton C. Nitrosative and oxidative modulation of iron regulatory proteins. Cell Mol Life Sci 1999; 55: 1043-1053.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1043-1053
    • Bouton, C.1
  • 66
    • 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
  • 67
    • 0025695636 scopus 로고
    • Nitric oxide mediates iron release from ferritin
    • Reif DW, Simmons RD. Nitric oxide mediates iron release from ferritin. Arch Biochem Biophys 1990; 283: 537-541.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 537-541
    • Reif, D.W.1    Simmons, R.D.2
  • 68
    • 0029131712 scopus 로고
    • Reaction of NO with the reduced R2 protein of ribonucleotide reductase from Escherichia coli
    • Haskin CJ, Ravi N, Lynch JB, Munck E, Que Jr L. Reaction of NO with the reduced R2 protein of ribonucleotide reductase from Escherichia coli. Biochemistry 1995; 34: 11090-11098.
    • (1995) Biochemistry , vol.34 , pp. 11090-11098
    • Haskin, C.J.1    Ravi, N.2    Lynch, J.B.3    Munck, E.4    Que Jr., L.5
  • 69
    • 0033528744 scopus 로고    scopus 로고
    • Reactions of nitric oxide with the reduced non-heme di-iron center of the soluble methane monooxygenase hydroxylase
    • Coufal D, Tavares P, Pereira AS, Hyunh BH, Lippard SJ. Reactions of nitric oxide with the reduced non-heme di-iron center of the soluble methane monooxygenase hydroxylase. Biochemistry 1999; 38: 4504-4513.
    • (1999) Biochemistry , vol.38 , pp. 4504-4513
    • Coufal, D.1    Tavares, P.2    Pereira, A.S.3    Hyunh, B.H.4    Lippard, S.J.5
  • 70
    • 0032502730 scopus 로고    scopus 로고
    • A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase
    • Torres J, Cooper CE, Wilson MT. A common mechanism for the interaction of nitric oxide with the oxidized binuclear centre and oxygen intermediates of cytochrome c oxidase. J Biol Chem 1998; 273:8756-8766.
    • (1998) J Biol Chem , vol.273 , pp. 8756-8766
    • Torres, J.1    Cooper, C.E.2    Wilson, M.T.3
  • 71
    • 0028346793 scopus 로고
    • Peroxynitrite releases copper from caeruloplasmin: Implications for atherosclerosis
    • Swain JA, Darley-Usmar V, Gutteridge JM. Peroxynitrite releases copper from caeruloplasmin: implications for atherosclerosis. FEBS Lett 1994; 342: 49-52.
    • (1994) FEBS Lett , vol.342 , pp. 49-52
    • Swain, J.A.1    Darley-Usmar, V.2    Gutteridge, J.M.3
  • 72
    • 0028351149 scopus 로고
    • Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription factor LAC9
    • Kroncke KD, Fehsel K, Schmidt T et al. Nitric oxide destroys zinc-sulfur clusters inducing zinc release from metallothionein and inhibition of the zinc finger-type yeast transcription factor LAC9. Biochem Biophys Res Commun 1994; 200: 1105-1110.
    • (1994) Biochem Biophys Res Commun , vol.200 , pp. 1105-1110
    • Kroncke, K.D.1    Fehsel, K.2    Schmidt, T.3
  • 73
    • 0035696440 scopus 로고    scopus 로고
    • Zinc and disease of the brain
    • Koh JY. Zinc and disease of the brain. Mol Neurobiol 2001; 24: 99-106.
    • (2001) Mol Neurobiol , vol.24 , pp. 99-106
    • Koh, J.Y.1
  • 74
    • 0029836493 scopus 로고    scopus 로고
    • Detection of nitric oxide interaction with zinc finger proteins
    • Kroncke KD, Kolb-Bachofen V. Detection of nitric oxide interaction with zinc finger proteins. Methods Enzymol 1996; 269: 279-284.
    • (1996) Methods Enzymol , vol.269 , pp. 279-284
    • Kroncke, K.D.1    Kolb-Bachofen, V.2
  • 75
    • 0037954792 scopus 로고    scopus 로고
    • Inactivation of zinc finger transcription factors provides a mechanism for a gene regulatory role of nitric oxide
    • Kroncke KD, Carlberg C. Inactivation of zinc finger transcription factors provides a mechanism for a gene regulatory role of nitric oxide. FASEB J 2000; 14: 166-173.
    • (2000) FASEB J , vol.14 , pp. 166-173
    • Kroncke, K.D.1    Carlberg, C.2
  • 76
    • 0032899132 scopus 로고    scopus 로고
    • Nitric oxide and lipid peroxidation
    • Hogg N, Kalyanaraman B. Nitric oxide and lipid peroxidation. Biochim Biophys Acta 1999; 1411:378-384.
    • (1999) Biochim Biophys Acta , vol.1411 , pp. 378-384
    • Hogg, N.1    Kalyanaraman, B.2
  • 78
    • 0035910611 scopus 로고    scopus 로고
    • Interactions between nitric oxide and lipid oxidation pathways
    • O'Donnell VB, Freeman BA. Interactions between nitric oxide and lipid oxidation pathways. Circ Res 2001; 88: 12-21.
    • (2001) Circ Res , vol.88 , pp. 12-21
    • O'Donnell, V.B.1    Freeman, B.A.2
  • 79
    • 0033913195 scopus 로고    scopus 로고
    • Nitric oxide regulation of free radical-and enzyme-mediated lipid and lipoprotein oxidation
    • Bloodsworth A, O'Donnell VB, Freeman BA. Nitric oxide regulation of free radical-and enzyme-mediated lipid and lipoprotein oxidation. Arterioscler Thromb Vasc Biol 2000; 20: 1707-1715.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1707-1715
    • Bloodsworth, A.1    O'Donnell, V.B.2    Freeman, B.A.3
  • 80
    • 0027228294 scopus 로고
    • The reaction of nitric oxide with organic peroxyl radicals
    • Padmaja S, Huie RE. The reaction of nitric oxide with organic peroxyl radicals. Biochem Biophys Res Commun 1993; 195: 539-544.
    • (1993) Biochem Biophys Res Commun , vol.195 , pp. 539-544
    • Padmaja, S.1    Huie, R.E.2
  • 81
    • 0030781227 scopus 로고    scopus 로고
    • Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse
    • Kissner R, Nauser T, Bugnon P, Lye PG, Koppenol WH. Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse. 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
  • 83
    • 0032478104 scopus 로고    scopus 로고
    • Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes
    • Liu X, Miller MJ, Joshi MS, Thomas DD, Lancaster Jr JR. Accelerated reaction of nitric oxide with O2 within the hydrophobic interior of biological membranes. Proc Natl Acad Sci USA 1998; 95: 2175-2179.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2175-2179
    • Liu, X.1    Miller, M.J.2    Joshi, M.S.3    Thomas, D.D.4    Lancaster Jr., J.R.5
  • 84
    • 0030700237 scopus 로고    scopus 로고
    • Nitric oxide inhibition of lipid peroxidation: Kinetics of reaction with lipid peroxyl radicals and comparison with alpha-tocopherol
    • O'Donnell VB, Chumley PH, Hogg N, Bloodsworth A, Darley-Usmar VM, Freeman BA. Nitric oxide inhibition of lipid peroxidation: kinetics of reaction with lipid peroxyl radicals and comparison with alpha-tocopherol. Biochemistry 1997; 36: 15216-15223.
    • (1997) Biochemistry , vol.36 , pp. 15216-15223
    • O'Donnell, V.B.1    Chumley, P.H.2    Hogg, N.3    Bloodsworth, A.4    Darley-Usmar, V.M.5    Freeman, B.A.6
  • 85
    • 0029024408 scopus 로고
    • The antioxidant effect of spermine NONOate in human low-density lipoprotein
    • Goss SP, Hogg N, Kalyanaraman B. The antioxidant effect of spermine NONOate in human low-density lipoprotein. Chem Res Toxicol 1995; 8: 800-806.
    • (1995) Chem Res Toxicol , vol.8 , pp. 800-806
    • Goss, S.P.1    Hogg, N.2    Kalyanaraman, B.3
  • 86
    • 0029119766 scopus 로고
    • Inhibition of macrophage-dependent low density lipoprotein oxidation by nitric-oxide donors
    • Hogg N, Struck A, Goss SP et al. Inhibition of macrophage-dependent low density lipoprotein oxidation by nitric-oxide donors. J Lipid Res 1995; 36: 1756-1762.
    • (1995) J Lipid Res , vol.36 , pp. 1756-1762
    • Hogg, N.1    Struck, A.2    Goss, S.P.3
  • 87
    • 0027952991 scopus 로고
    • Nitric oxide donor GEA 3162 inhibits endothelial cell-mediated oxidation of low density lipoprotein
    • Malo-Ranta U, Yla-Herttuala S, Metsa-Ketela T et al. Nitric oxide donor GEA 3162 inhibits endothelial cell-mediated oxidation of low density lipoprotein. FEBS Lett 1994; 337: 179-183.
    • (1994) FEBS Lett , vol.337 , pp. 179-183
    • Malo-Ranta, U.1    Yla-Herttuala, S.2    Metsa-Ketela, T.3
  • 88
    • 0029118058 scopus 로고
    • Action of nitric oxide as an antioxidant against oxidation of soybean phosphatidylcholine liposomal membranes
    • Hayashi K, Noguchi N, Niki E. Action of nitric oxide as an antioxidant against oxidation of soybean phosphatidylcholine liposomal membranes. FEBS Lett 1995; 370: 37-40.
    • (1995) FEBS Lett , vol.370 , pp. 37-40
    • Hayashi, K.1    Noguchi, N.2    Niki, E.3
  • 89
    • 0034643867 scopus 로고    scopus 로고
    • Nitric oxide inhibition of free radical-mediated cholesterol peroxidation in liposomal membranes
    • Korytowski W, Zareba M, Girotti AW. Nitric oxide inhibition of free radical-mediated cholesterol peroxidation in liposomal membranes. Biochemistry 2000; 39: 6918-6928.
    • (2000) Biochemistry , vol.39 , pp. 6918-6928
    • Korytowski, W.1    Zareba, M.2    Girotti, A.W.3
  • 91
    • 0034078645 scopus 로고    scopus 로고
    • Interactions of nitric oxide with lipid peroxidation products under aerobic conditions: Inhibitory effects on the formation of malondialdehyde and related thiobarbituric acid-reactive substances
    • d'Ischia M, Palumbo A, Buzzo F. Interactions of nitric oxide with lipid peroxidation products under aerobic conditions: inhibitory effects on the formation of malondialdehyde and related thiobarbituric acid-reactive substances. Nitric Oxide 2000; 4: 4-14.
    • (2000) Nitric Oxide , vol.4 , pp. 4-14
    • d'Ischia, M.1    Palumbo, A.2    Buzzo, F.3
  • 92
  • 94
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Radi R, Trujillo M et al. Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives. J Biol Chem 1994; 269: 26066-26075.
    • (1994) J Biol Chem , vol.269 , pp. 26066-26075
    • Rubbo, H.1    Radi, R.2    Trujillo, M.3
  • 95
    • 0028793450 scopus 로고
    • Nitric oxide inhibition of lipoxygenase-dependent liposome and low-density lipoprotein oxidation: Termination of radical chain propagation reactions and formation of nitrogen-containing oxidized lipid derivatives
    • Rubbo H, Parthasarathy S, Barnes S, Kirk M, Kalyanaraman B, Freeman BA. Nitric oxide inhibition of lipoxygenase-dependent liposome and low-density lipoprotein oxidation: termination of radical chain propagation reactions and formation of nitrogen-containing oxidized lipid derivatives. Arch Biochem Biophys 1995; 324: 15-25.
    • (1995) Arch Biochem Biophys , vol.324 , pp. 15-25
    • Rubbo, H.1    Parthasarathy, S.2    Barnes, S.3    Kirk, M.4    Kalyanaraman, B.5    Freeman, B.A.6
  • 96
    • 0015111756 scopus 로고
    • Oxidation of unsaturated fatty acids by ozone and nitrogen dioxide. A common mechanism of action
    • Roehnm JN, Hadley JG, Menzel DB. Oxidation of unsaturated fatty acids by ozone and nitrogen dioxide. A common mechanism of action. Arch Environ Health 1971; 23: 142-148.
    • (1971) Arch Environ Health , vol.23 , pp. 142-148
    • Roehnm, J.N.1    Hadley, J.G.2    Menzel, D.B.3
  • 97
    • 0027408024 scopus 로고
    • The identification of the allylic nitrite and nitro derivatives of methyl linoleate and methyl linolenate by negative chemical ionization mass spectrometry
    • Gallon AA, Pryor WA. The identification of the allylic nitrite and nitro derivatives of methyl linoleate and methyl linolenate by negative chemical ionization mass spectrometry. Lipids 1993; 28: 125-133.
    • (1993) Lipids , vol.28 , pp. 125-133
    • Gallon, A.A.1    Pryor, W.A.2
  • 98
    • 0032914526 scopus 로고    scopus 로고
    • Nitration of unsaturated fatty acids by nitric oxide-derived reactive nitrogen species peroxynitrite, nitrous acid, nitrogen dioxide, and nitronium ion
    • O'Donnell VB, Eiserich JP, Chumley PH et al. Nitration of unsaturated fatty acids by nitric oxide-derived reactive nitrogen species peroxynitrite, nitrous acid, nitrogen dioxide, and nitronium ion. Chem Res Toxicol 1999; 12: 83-92.
    • (1999) Chem Res Toxicol , vol.12 , pp. 83-92
    • O'Donnell, V.B.1    Eiserich, J.P.2    Chumley, P.H.3
  • 99
    • 0034637496 scopus 로고    scopus 로고
    • Acid-promoted reactions of ethyl linoleate with nitrite ions: Formation and structural characterization of isomeric nitroalkene, nitrohydroxy, and novel 3-nitro-1, 5-hexadiene and 1,5-dinitro-1,3-pentadiene products
    • Napolitano A, Camera E, Picardo M, d'Ischia M. Acid-promoted reactions of ethyl linoleate with nitrite ions: formation and structural characterization of isomeric nitroalkene, nitrohydroxy, and novel 3-nitro-1, 5-hexadiene and 1,5-dinitro-1,3-pentadiene products. J Org Chem 2000; 65: 4853-4860.
    • (2000) J Org Chem , vol.65 , pp. 4853-4860
    • Napolitano, A.1    Camera, E.2    Picardo, M.3    d'Ischia, M.4
  • 100
    • 0028205948 scopus 로고
    • The reaction of low levels of nitrogen dioxide with methyl linoleate in the presence and absence of oxygen
    • Gallon AA, Pryor WA. The reaction of low levels of nitrogen dioxide with methyl linoleate in the presence and absence of oxygen. Lipids 1994; 29: 171-176.
    • (1994) Lipids , vol.29 , pp. 171-176
    • Gallon, A.A.1    Pryor, W.A.2
  • 102
    • 0028938521 scopus 로고
    • Uptake by macrophages of low-density lipoprotein damaged by nitrogen dioxide in air
    • Kikugawa K, Beppu U, Okamoto Y. Uptake by macrophages of low-density lipoprotein damaged by nitrogen dioxide in air. Lipids 1995; 30: 313-320.
    • (1995) Lipids , vol.30 , pp. 313-320
    • Kikugawa, K.1    Beppu, U.2    Okamoto, Y.3
  • 103
    • 0014400436 scopus 로고
    • Lipoperoxidation of lung lipids in rats exposed to nitrogen dioxide
    • Thomas HV, Mueller PK, Lyman RL. Lipoperoxidation of lung lipids in rats exposed to nitrogen dioxide. Science 1968; 159: 532-534.
    • (1968) Science , vol.159 , pp. 532-534
    • Thomas, H.V.1    Mueller, P.K.2    Lyman, R.L.3
  • 104
    • 0032464635 scopus 로고    scopus 로고
    • Pathophysiology of nitric oxide and related species: Free radical reactions and modification of biomolecules
    • Eiserich JP, Patel RP, O'Donnell VB. Pathophysiology of nitric oxide and related species: free radical reactions and modification of biomolecules. Mol Aspects Med 1998; 19: 221-357:
    • (1998) Mol Aspects Med , vol.19 , pp. 221-357
    • Eiserich, J.P.1    Patel, R.P.2    O'Donnell, V.B.3
  • 105
    • 0034700236 scopus 로고    scopus 로고
    • Permeation of phospholipid membranes by peroxynitnte
    • Khairutdinov RF, Coddington JW, Hurst JK. Permeation of phospholipid membranes by peroxynitnte. Biochemistty 2000; 39: 14238-14249.
    • (2000) Biochemistty , vol.39 , pp. 14238-14249
    • Khairutdinov, R.F.1    Coddington, J.W.2    Hurst, J.K.3
  • 106
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch Biochem Biophys 1991; 288: 481-487.
    • (1991) Arch Biochem Biophys , vol.288 , pp. 481-487
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 107
    • 23844477179 scopus 로고    scopus 로고
    • Chemiluminescence evaluation of oxidative damage to biomolecules induced by singlet oxygen and the protective effects of antioxidants
    • Wenli Y, Yaping Z. Chemiluminescence evaluation of oxidative damage to biomolecules induced by singlet oxygen and the protective effects of antioxidants. Biochim Biophys Acta 2005; 1725: 30-34.
    • (2005) Biochim Biophys Acta , vol.1725 , pp. 30-34
    • Wenli, Y.1    Yaping, Z.2
  • 108
    • 0028105887 scopus 로고
    • Interactions of peroxynitrite with human plasma and its constituents: Oxidative damage and antioxidant depletion
    • Van der Vliet A, Smith D, O'Neill CA et al. Interactions of peroxynitrite with human plasma and its constituents: oxidative damage and antioxidant depletion. Biochem J 1994; 303: 295-301.
    • (1994) Biochem J , vol.303 , pp. 295-301
    • Van der Vliet, A.1    Smith, D.2    O'Neill, C.A.3
  • 109
    • 0347287708 scopus 로고    scopus 로고
    • The effects of peroxynitrite on pig platelet lipid peroxidation and the secretory process induced by thrombin
    • Nowak P, Wachowicz B. The effects of peroxynitrite on pig platelet lipid peroxidation and the secretory process induced by thrombin. Cytobios 2001; 106: 179-187.
    • (2001) Cytobios , vol.106 , pp. 179-187
    • Nowak, P.1    Wachowicz, B.2
  • 110
    • 0033590983 scopus 로고    scopus 로고
    • Formation of phospholipid hydroperoxides and its inhibition by alpha-tocopherol in rat brain synaptosomes induced by peroxynitrite
    • Shi H, Noguchi N, Xu Y, Niki E. Formation of phospholipid hydroperoxides and its inhibition by alpha-tocopherol in rat brain synaptosomes induced by peroxynitrite. Biochem Biophys Res Commun 1999; 257: 651-656.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 651-656
    • Shi, H.1    Noguchi, N.2    Xu, Y.3    Niki, E.4
  • 111
    • 18544375472 scopus 로고    scopus 로고
    • Lipid peroxidation and cell death mechanisms in pulmonary epithelial cells induced by peroxynitrite and nitric oxide
    • Ho YS, Liou HB, Lin JK et al. Lipid peroxidation and cell death mechanisms in pulmonary epithelial cells induced by peroxynitrite and nitric oxide. Arch Toxicol 2002; 76: 484-493.
    • (2002) Arch Toxicol , vol.76 , pp. 484-493
    • Ho, Y.S.1    Liou, H.B.2    Lin, J.K.3
  • 112
    • 0026676388 scopus 로고
    • The simultaneous generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein
    • Darley-Usmar VM, Hogg N, O'Leary VJ, Wilson MT, Moncada, S. The simultaneous generation of superoxide and nitric oxide can initiate lipid peroxidation in human low density lipoprotein. Free Radic Res Commun 1992; 17: 9-20.
    • (1992) Free Radic Res Commun , vol.17 , pp. 9-20
    • Darley-Usmar, V.M.1    Hogg, N.2    O'Leary, V.J.3    Wilson, M.T.4    Moncada, S.5
  • 114
    • 0035890228 scopus 로고    scopus 로고
    • Formation of lipid-protein adducts in low-density lipoprotein by fluxes of peroxynitrite and its inhibition by nitric oxide
    • Trostchansky A, Batthyany C, Botti H, Radi R, Denicola A, Rubbo H. Formation of lipid-protein adducts in low-density lipoprotein by fluxes of peroxynitrite and its inhibition by nitric oxide. Arch Biochem Biophys 2001; 395: 225-232.
    • (2001) Arch Biochem Biophys , vol.395 , pp. 225-232
    • Trostchansky, A.1    Batthyany, C.2    Botti, H.3    Radi, R.4    Denicola, A.5    Rubbo, H.6
  • 115
    • 0030454202 scopus 로고    scopus 로고
    • Formation of oxysterols during oxidation of low density lipoprotein by peroxynitrite, myoglobin, and copper
    • Patel RP, Diczfalusy U, Dzeletovic S, Wilson MT, Darley-Usmar VM. Formation of oxysterols during oxidation of low density lipoprotein by peroxynitrite, myoglobin, and copper. J Lipid Res 1996; 37:2361-2371.
    • (1996) J Lipid Res , vol.37 , pp. 2361-2371
    • Patel, R.P.1    Diczfalusy, U.2    Dzeletovic, S.3    Wilson, M.T.4    Darley-Usmar, V.M.5
  • 116
    • 30044439773 scopus 로고    scopus 로고
    • Interaction with phospholipids modulates alpha-synuclein nitration and lipid-protein adduct formation
    • Trostchansky A, Lind S, Hodara R et al. Interaction with phospholipids modulates alpha-synuclein nitration and lipid-protein adduct formation. Biochem J 2006; 393: 343-349.
    • (2006) Biochem J , vol.393 , pp. 343-349
    • Trostchansky, A.1    Lind, S.2    Hodara, R.3
  • 117
    • 0028807047 scopus 로고
    • Kinetic analysis of the fate of nitric oxide synthesized by macrophages in vitro
    • Lewis CT, Tamir S, Tannenbaum SR, Deen WM. Kinetic analysis of the fate of nitric oxide synthesized by macrophages in vitro. J Biol Chem 1995; 270: 29350-29355.
    • (1995) J Biol Chem , vol.270 , pp. 29350-29355
    • Lewis, C.T.1    Tamir, S.2    Tannenbaum, S.R.3    Deen, W.M.4
  • 118
    • 19744377792 scopus 로고    scopus 로고
    • Cytosine catalysis of nitrosative guanine deamination and interstrand cross-link formation
    • Glaser R, Wu H, Lewis M. Cytosine catalysis of nitrosative guanine deamination and interstrand cross-link formation. J Am Chem Soc 2005; 127: 7346-7358.
    • (2005) J Am Chem Soc , vol.127 , pp. 7346-7358
    • Glaser, R.1    Wu, H.2    Lewis, M.3
  • 119
    • 0141848395 scopus 로고    scopus 로고
    • Absence of 2′-deoxyoxanosine and presence of abasic sites in DNA exposed to nitric oxide at controlled physiological concentrations
    • Dong M, Wang C, Deen WM, Dedon PC. Absence of 2′-deoxyoxanosine and presence of abasic sites in DNA exposed to nitric oxide at controlled physiological concentrations. Chem Res Toxicol 2003; 16: 1044-1055.
    • (2003) Chem Res Toxicol , vol.16 , pp. 1044-1055
    • Dong, M.1    Wang, C.2    Deen, W.M.3    Dedon, P.C.4
  • 120
    • 31844444034 scopus 로고    scopus 로고
    • Relatively small increases in the steady-state levels of nucleobase deamination products in DNA from human TK6 cells exposed to toxic levels of nitric oxide
    • Dong M, Dedon PC. Relatively small increases in the steady-state levels of nucleobase deamination products in DNA from human TK6 cells exposed to toxic levels of nitric oxide. Chem Res Toxicol 2006; 19: 50-57.
    • (2006) Chem Res Toxicol , vol.19 , pp. 50-57
    • Dong, M.1    Dedon, P.C.2
  • 122
    • 0015504253 scopus 로고
    • Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid
    • Lindahl PA, Andersson A. Rate of chain breakage at apurinic sites in double-stranded deoxyribonucleic acid. Biochemistry 1972; 11: 3618-3623.
    • (1972) Biochemistry , vol.11 , pp. 3618-3623
    • Lindahl, P.A.1    Andersson, A.2
  • 123
    • 0017767390 scopus 로고
    • Isolation and identification of cross-linked nucleosides from nitrous acid treated deoxyribonucleic acid
    • Shapiro R, Dubelman S, Feinberg AM, Crain PF, McCloskey JA. Isolation and identification of cross-linked nucleosides from nitrous acid treated deoxyribonucleic acid. J Am Chem Soc 1977; 99: 302-303.
    • (1977) J Am Chem Soc , vol.99 , pp. 302-303
    • Shapiro, R.1    Dubelman, S.2    Feinberg, A.M.3    Crain, P.F.4    McCloskey, J.A.5
  • 124
    • 0025823709 scopus 로고
    • Nitrous acid cross-links duplex DNA fragments through deoxyguanosine residues at the sequence 5′-CG
    • Kirchner JJ, Hopkins PB. Nitrous acid cross-links duplex DNA fragments through deoxyguanosine residues at the sequence 5′-CG. J Am Chem Soc 1991; 113: 4681-4682.
    • (1991) J Am Chem Soc , vol.113 , pp. 4681-4682
    • Kirchner, J.J.1    Hopkins, P.B.2
  • 127
    • 0035341318 scopus 로고    scopus 로고
    • Gaseous nitric oxide-induced 8-nitroguanine formation in human lung fibroblast cells and cell-free DNA
    • Hsieh YS, Wang HC, Tseng TH, Chang WC, Wang CJ. Gaseous nitric oxide-induced 8-nitroguanine formation in human lung fibroblast cells and cell-free DNA. Toxicol Appl Pharmacol 2001; 172: 210-216.
    • (2001) Toxicol Appl Pharmacol , vol.172 , pp. 210-216
    • Hsieh, Y.S.1    Wang, H.C.2    Tseng, T.H.3    Chang, W.C.4    Wang, C.J.5
  • 128
    • 0030940178 scopus 로고    scopus 로고
    • Oxygen-dependent fragmentation of cellular DNA by nitric oxide
    • Yabuki M, Inai Y, Yoshioka T et al. Oxygen-dependent fragmentation of cellular DNA by nitric oxide. Free Radic Res 1997; 26: 245-255.
    • (1997) Free Radic Res , vol.26 , pp. 245-255
    • Yabuki, M.1    Inai, Y.2    Yoshioka, T.3
  • 130
    • 0036807332 scopus 로고    scopus 로고
    • DNA damage profiling in motor neurons: A single-cell analysis by comet assay
    • Martin LJ. DNA damage profiling in motor neurons: a single-cell analysis by comet assay. Neurochem Res 2002; 27: 1093-1104.
    • (2002) Neurochem Res , vol.27 , pp. 1093-1104
    • Martin, L.J.1
  • 132
    • 0033533565 scopus 로고    scopus 로고
    • Effects of exogenous nitric oxide and hyperoxia on lung fibroblast viability and DNA fragmentation
    • Raghuram N, Fortenberry JD, Owens ML, Brown LA. Effects of exogenous nitric oxide and hyperoxia on lung fibroblast viability and DNA fragmentation. Biochem Biophys Res Commun 1999; 262: 685-691.
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 685-691
    • Raghuram, N.1    Fortenberry, J.D.2    Owens, M.L.3    Brown, L.A.4
  • 133
    • 0026321495 scopus 로고
    • DNA deaminating ability and genotoxicity of nitric oxide and its progenitors
    • Wink DA, Kasprzak KS, Maragos CM et al. DNA deaminating ability and genotoxicity of nitric oxide and its progenitors. Science 1991; 254: 1001-1003.
    • (1991) Science , vol.254 , pp. 1001-1003
    • Wink, D.A.1    Kasprzak, K.S.2    Maragos, C.M.3
  • 135
    • 0025124336 scopus 로고
    • Nitrogen dioxide induces DNA single-strand breaks in cultured Chinese hamster cells
    • Gorsdorf S, Appel KE, Engeholm C, Obe G. Nitrogen dioxide induces DNA single-strand breaks in cultured Chinese hamster cells. Carcinogenesis 1990; 11: 37-41.
    • (1990) Carcinogenesis , vol.11 , pp. 37-41
    • Gorsdorf, S.1    Appel, K.E.2    Engeholm, C.3    Obe, G.4
  • 136
    • 0023146207 scopus 로고
    • Nitrous acid induced damage in T7 DNA and phage
    • Scearce LM, Masker WE. Nitrous acid induced damage in T7 DNA and phage. Mutat Res 1987; 190: 1-6.
    • (1987) Mutat Res , vol.190 , pp. 1-6
    • Scearce, L.M.1    Masker, W.E.2
  • 137
    • 0034646034 scopus 로고    scopus 로고
    • Peroxynitrite-induced DNA damage in the supF gene: Correlation with the mutational spectrum
    • Tretyakova NY, Burney S, Pamir B et al. Peroxynitrite-induced DNA damage in the supF gene: correlation with the mutational spectrum. Mutat Res 2000; 447: 287-303.
    • (2000) Mutat Res , vol.447 , pp. 287-303
    • Tretyakova, N.Y.1    Burney, S.2    Pamir, B.3
  • 138
    • 0028785105 scopus 로고
    • Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination
    • Yermilov V, Rubio J, Ohshima H. Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination. FEBS Lett 1995; 376: 207-210.
    • (1995) FEBS Lett , vol.376 , pp. 207-210
    • Yermilov, V.1    Rubio, J.2    Ohshima, H.3
  • 139
    • 0029979758 scopus 로고    scopus 로고
    • Base modification and strand breakage in isolated calf thymus DNA and in DNA from human skin epidermal keratinocytes exposed to peroxynitrite or 3-morpholinosydnonimine
    • Spencer JP, Wong J, Jenner A, Aruoma OI, Cross CE, Halliwell B. Base modification and strand breakage in isolated calf thymus DNA and in DNA from human skin epidermal keratinocytes exposed to peroxynitrite or 3-morpholinosydnonimine. Chem Res Toxicol 1996; 9: 1152-1158.
    • (1996) Chem Res Toxicol , vol.9 , pp. 1152-1158
    • Spencer, J.P.1    Wong, J.2    Jenner, A.3    Aruoma, O.I.4    Cross, C.E.5    Halliwell, B.6
  • 140
    • 29644444127 scopus 로고    scopus 로고
    • Quantification of four guanine oxidation products from reaction of DNA with varying doses of peroxynitrite
    • Yu H, Venkatarangan L, Wishnok JS, Tannenbaum SR. Quantification of four guanine oxidation products from reaction of DNA with varying doses of peroxynitrite. Chem Res Toxicol 2005; 18: 1849-1857.
    • (2005) Chem Res Toxicol , vol.18 , pp. 1849-1857
    • Yu, H.1    Venkatarangan, L.2    Wishnok, J.S.3    Tannenbaum, S.R.4
  • 143
    • 0033024623 scopus 로고    scopus 로고
    • DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite
    • Burney S, Niles JC, Dedon PC, Tannenbaum SR. DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite. Chem Res Toxicol 1999; 12: 513-520.
    • (1999) Chem Res Toxicol , vol.12 , pp. 513-520
    • Burney, S.1    Niles, J.C.2    Dedon, P.C.3    Tannenbaum, S.R.4
  • 145
    • 0030010723 scopus 로고    scopus 로고
    • Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA
    • Douki T, Cadet J. Peroxynitrite mediated oxidation of purine bases of nucleosides and isolated DNA. Free Radic Res 1996; 24: 369-380.
    • (1996) Free Radic Res , vol.24 , pp. 369-380
    • Douki, T.1    Cadet, J.2
  • 147
    • 0029111530 scopus 로고
    • Oxidative DNA damage induced by simultaneous generation of nitric oxide and superoxide
    • Inoue S, Kawanishi S. Oxidative DNA damage induced by simultaneous generation of nitric oxide and superoxide. FEBS Lett 1995; 371: 86-88.
    • (1995) FEBS Lett , vol.371 , pp. 86-88
    • Inoue, S.1    Kawanishi, S.2
  • 148
    • 0029862775 scopus 로고    scopus 로고
    • DNA damage by peroxynitrite characterized with DNA repair enzymes
    • Epe B, Ballmaier D, Roussyn I, Briviba K, Sies H. DNA damage by peroxynitrite characterized with DNA repair enzymes. Nucleic Acids Res 1996; 24: 4105-4110.
    • (1996) Nucleic Acids Res , vol.24 , pp. 4105-4110
    • Epe, B.1    Ballmaier, D.2    Roussyn, I.3    Briviba, K.4    Sies, H.5
  • 149
    • 0037062625 scopus 로고    scopus 로고
    • Peroxynitrite-induced reactions of synthetic oligo 2′-deoxynucleotides and DNA containing guanine: Formation and stability of a 5-guanidino-4-nitroimidazole lesion
    • Gu F, Stillwell WG, Wishnok JS, Shallop AJ, Jones RA, Tannenbaum SR. Peroxynitrite-induced reactions of synthetic oligo 2′-deoxynucleotides and DNA containing guanine: formation and stability of a 5-guanidino-4-nitroimidazole lesion. Biochemistry 2002; 41: 7508-7518.
    • (2002) Biochemistry , vol.41 , pp. 7508-7518
    • Gu, F.1    Stillwell, W.G.2    Wishnok, J.S.3    Shallop, A.J.4    Jones, R.A.5    Tannenbaum, S.R.6
  • 150
    • 0030034846 scopus 로고    scopus 로고
    • An adduct between peroxynitrite and 2′-deoxyguanosine: 4,5-dihydro-5-hydroxy-4-(nitrosooxy)-2′-deoxyguanosine
    • Douki T, Cadet J, Ames BN. An adduct between peroxynitrite and 2′-deoxyguanosine: 4,5-dihydro-5-hydroxy-4-(nitrosooxy)-2′-deoxyguanosine. Chem Res Toxicol 1996; 9: 3-7.
    • (1996) Chem Res Toxicol , vol.9 , pp. 3-7
    • Douki, T.1    Cadet, J.2    Ames, B.N.3
  • 151
    • 0035852024 scopus 로고    scopus 로고
    • A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-guanosine
    • Niles JC, Wishnok JS, Tannenbaum SR. A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-guanosine. J Am Chem Soc 2001; 123: 12147-12151.
    • (2001) J Am Chem Soc , vol.123 , pp. 12147-12151
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 152
    • 0029783851 scopus 로고    scopus 로고
    • Competitive reactions of peroxynitrite with 2′-deoxyguanosine and 7,8-dihydro-8-oxo-2′-deoxyguanosine (8-oxodG): Relevance to the formation of 8-oxo-dG in DNA exposed to peroxynitrite
    • Uppu RM, Cueto R, Squadrito GL, Salgo MG, Pryor WA. Competitive reactions of peroxynitrite with 2′-deoxyguanosine and 7,8-dihydro-8-oxo-2′-deoxyguanosine (8-oxodG): relevance to the formation of 8-oxo-dG in DNA exposed to peroxynitrite. Free Radic Biol Med 1996; 21: 407-411.
    • (1996) Free Radic Biol Med , vol.21 , pp. 407-411
    • Uppu, R.M.1    Cueto, R.2    Squadrito, G.L.3    Salgo, M.G.4    Pryor, W.A.5
  • 154
    • 0034079273 scopus 로고    scopus 로고
    • A novel nitration product formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-7,8-dihydro-8-oxoguanosine: N-nitro-N'-[1-(2,3,5-tri-O-acetyl-β-D-erythro-pentofuranosyl) -2,4-dioxoimidazolidin-5-ylidene]guanidine
    • Niles JC, Wishnok JS, Tannenbaum SR. A novel nitration product formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-7,8-dihydro-8-oxoguanosine: N-nitro-N'-[1-(2,3,5-tri-O-acetyl-β-D-erythro-pentofuranosyl) -2,4-dioxoimidazolidin-5-ylidene]guanidine. Chem Res Toxicol 2000; 13: 390-396.
    • (2000) Chem Res Toxicol , vol.13 , pp. 390-396
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 155
    • 0032742691 scopus 로고    scopus 로고
    • Peroxy-nitrite reaction products of 3′,5′-di-O-acetyl-8-oxo-7,8-dihydro-2′-deoxyguanosine
    • Niles JC, Burney S, Singh SP, Wishnok JS, Tannenbaum SR. Peroxy-nitrite reaction products of 3′,5′-di-O-acetyl-8-oxo-7,8-dihydro-2′-deoxyguanosine. Proc Natl Acad Sci USA 1999; 96: 11729-11734.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11729-11734
    • Niles, J.C.1    Burney, S.2    Singh, S.P.3    Wishnok, J.S.4    Tannenbaum, S.R.5
  • 156
    • 0030042984 scopus 로고    scopus 로고
    • Peroxynitrite-induced mutation spectra of pSP189 following replication in bacteria and in human cells
    • Juedes MJ, Wogan GN. Peroxynitrite-induced mutation spectra of pSP189 following replication in bacteria and in human cells. Mutat Res l996; 349: 51-61.
    • (1996) Mutat Res , vol.349 , pp. 51-61
    • Juedes, M.J.1    Wogan, G.N.2
  • 157
    • 12144256259 scopus 로고    scopus 로고
    • Effects of peroxynitrite dose and dose rate on DNA damage and mutation in the supF shuttle vector
    • Kim MY, Dong M, Dedon PC, Wogan GN. Effects of peroxynitrite dose and dose rate on DNA damage and mutation in the supF shuttle vector. Chem Res Toxicol 2005; 18: 76-86.
    • (2005) Chem Res Toxicol , vol.18 , pp. 76-86
    • Kim, M.Y.1    Dong, M.2    Dedon, P.C.3    Wogan, G.N.4
  • 159
    • 17244366814 scopus 로고    scopus 로고
    • Oxidatively induced DNA-protein cross-linking between single-stranded binding protein and oligodeoxynucleotides containing 8-oxo-7, 8-dihydro-2′-deoxyguanosine
    • Johansen ME, Muller JG, Xu X, Burrows CJ. Oxidatively induced DNA-protein cross-linking between single-stranded binding protein and oligodeoxynucleotides containing 8-oxo-7, 8-dihydro-2′-deoxyguanosine. Biochemistry 2005; 44: 5660-5671.
    • (2005) Biochemistry , vol.44 , pp. 5660-5671
    • Johansen, M.E.1    Muller, J.G.2    Xu, X.3    Burrows, C.J.4
  • 160
    • 21844432111 scopus 로고    scopus 로고
    • Chemical and biological evidence for base propenols as the major source of the endogenous M1dG adduct in cellular DNA
    • Zhou X, Taghizadeh K, Dedon PC. Chemical and biological evidence for base propenols as the major source of the endogenous M1dG adduct in cellular DNA. J Biol Chem 2005; 280: 25377-25382.
    • (2005) J Biol Chem , vol.280 , pp. 25377-25382
    • Zhou, X.1    Taghizadeh, K.2    Dedon, P.C.3
  • 162
    • 0035341542 scopus 로고    scopus 로고
    • Hepatocellular oxidative DNA injury induced by macrophage-derived nitric oxide
    • Watanabe N, Miura S, Zeki S, Ishii H. Hepatocellular oxidative DNA injury induced by macrophage-derived nitric oxide. Free Radic Biol Med 2001; 30: 1019-1028.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1019-1028
    • Watanabe, N.1    Miura, S.2    Zeki, S.3    Ishii, H.4
  • 163
    • 0032421755 scopus 로고    scopus 로고
    • Etheno adducts in spleen DNA of SJL mice stimulated to overproduce nitric oxide
    • Nair J, Gal A, Tamir S, Tannenbaum SR, Wogan GN, Bartsch H. Etheno adducts in spleen DNA of SJL mice stimulated to overproduce nitric oxide. Carcinogenesis 1998; 19: 2081-2084.
    • (1998) Carcinogenesis , vol.19 , pp. 2081-2084
    • Nair, J.1    Gal, A.2    Tamir, S.3    Tannenbaum, S.R.4    Wogan, G.N.5    Bartsch, H.6
  • 164
    • 0035367510 scopus 로고    scopus 로고
    • Intracellular ascorbic acid enhances the DNA single-strand breakage and toxicity induced by peroxynitrite in U937 cells
    • Guidarelli A, De Sanctis R, Cellini B, Fiorani M, Dacha M, Cantoni O. Intracellular ascorbic acid enhances the DNA single-strand breakage and toxicity induced by peroxynitrite in U937 cells. Biochem J 2001; 356: 509-513.
    • (2001) Biochem J , vol.356 , pp. 509-513
    • Guidarelli, A.1    De Sanctis, R.2    Cellini, B.3    Fiorani, M.4    Dacha, M.5    Cantoni, O.6
  • 165
    • 0036231450 scopus 로고    scopus 로고
    • Genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells exposed to peroxynitrite generated from SIN-1
    • Li CQ, Trudel LJ, Wogan GN. Genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells exposed to peroxynitrite generated from SIN-1. Chem Res Toxicol 2002; 15: 527-535.
    • (2002) Chem Res Toxicol , vol.15 , pp. 527-535
    • Li, C.Q.1    Trudel, L.J.2    Wogan, G.N.3
  • 166
    • 0030000690 scopus 로고    scopus 로고
    • DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite
    • Szabo C, Zingarelli B, O'Conner M, Salzman AL. DNA strand breakage, activation of poly (ADP-ribose) synthetase, and cellular energy depletion are involved in the cytotoxicity of macrophages and smooth muscle cells exposed to peroxynitrite. Proc Natl Acad Sci USA 1996; 93: 1753-1758.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1753-1758
    • Szabo, C.1    Zingarelli, B.2    O'Conner, M.3    Salzman, A.L.4
  • 167
    • 0343580474 scopus 로고    scopus 로고
    • Peroxynitrite-mediated decarboxylation of pyruvate to both carbon dioxide and carbon dioxide radical anion
    • Vasquez-Vivar J, Denicola A, Radi R, Augusto O. Peroxynitrite-mediated decarboxylation of pyruvate to both carbon dioxide and carbon dioxide radical anion. Chem Res Toxicol 1997; 10: 786-794.
    • (1997) Chem Res Toxicol , vol.10 , pp. 786-794
    • Vasquez-Vivar, J.1    Denicola, A.2    Radi, R.3    Augusto, O.4
  • 169
    • 0037138481 scopus 로고    scopus 로고
    • Formation of 8-nitroguanosine in cellular RNA as a biomarker of exposure to reactive nitrogen species
    • Masuda M, Nishino H, Ohshima H. Formation of 8-nitroguanosine in cellular RNA as a biomarker of exposure to reactive nitrogen species. Chem Biol Interact 2002; 139: 187-197.
    • (2002) Chem Biol Interact , vol.139 , pp. 187-197
    • Masuda, M.1    Nishino, H.2    Ohshima, H.3
  • 170
    • 0034640248 scopus 로고    scopus 로고
    • Hydrogen peroxide- and peroxynitrite-induced mitochondrial DNA damage and dysfunction in vascular endothelial and smooth muscle cells
    • Ballinger SW, Patterson C, Yan CN et al. Hydrogen peroxide- and peroxynitrite-induced mitochondrial DNA damage and dysfunction in vascular endothelial and smooth muscle cells. Circ Res 2000; 86: 915-916.
    • (2000) Circ Res , vol.86 , pp. 915-916
    • Ballinger, S.W.1    Patterson, C.2    Yan, C.N.3
  • 171
    • 33644661625 scopus 로고    scopus 로고
    • Role of nitric oxide-induced mtDNA damage in mitochondrial dysfunction and apoptosis
    • Rachek LI, Grishko VI, LeDoux SP, Wilson GL. Role of nitric oxide-induced mtDNA damage in mitochondrial dysfunction and apoptosis. Free Radic Biol Med 2006; 40: 754-762.
    • (2006) Free Radic Biol Med , vol.40 , pp. 754-762
    • Rachek, L.I.1    Grishko, V.I.2    LeDoux, S.P.3    Wilson, G.L.4
  • 172
    • 0030839198 scopus 로고    scopus 로고
    • Mitochondrial DNA in beta-cells is a sensitive target for damage by nitric oxide
    • Wilson GL, Patton NJ, LeDoux SP. Mitochondrial DNA in beta-cells is a sensitive target for damage by nitric oxide. Diabetes 1997; 46: 1291-1295.
    • (1997) Diabetes , vol.46 , pp. 1291-1295
    • Wilson, G.L.1    Patton, N.J.2    LeDoux, S.P.3


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