메뉴 건너뛰기




Volumn 28, Issue 12, 2003, Pages 646-654

NO-dependent protein nitration: A cell signaling event or an oxidative inflammatory response?

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA TUBULIN; CARBON DIOXIDE; COPPER; HISTONE; NITRIC OXIDE; PEROXIDASE; SUPEROXIDE DISMUTASE; ZINC;

EID: 0344196903     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2003.10.006     Document Type: Review
Times cited : (324)

References (59)
  • 1
    • 0034925593 scopus 로고    scopus 로고
    • Tyrosine nitration: Localisation, quantification, consequences for protein function and signal transduction
    • Greenacre S.A., Ischiropoulos H. Tyrosine nitration: localisation, quantification, consequences for protein function and signal transduction. Free Radic. Res. 34:2001;541-581.
    • (2001) Free Radic. Res. , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 2
    • 0025612247 scopus 로고
    • Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins
    • Ohshima H., et al. Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins. Food Chem. Toxicol. 28:1990;647-652.
    • (1990) Food Chem. Toxicol. , vol.28 , pp. 647-652
    • Ohshima, H.1
  • 3
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman J.S., et al. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. U. S. A. 87:1990;1620-1624.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1620-1624
    • Beckman, J.S.1
  • 4
    • 0022426881 scopus 로고
    • Reactions of nitrogen dioxide in aqueous model systems: Oxidation of tyrosine units in peptides and proteins
    • Prutz W.A., et al. Reactions of nitrogen dioxide in aqueous model systems: oxidation of tyrosine units in peptides and proteins. Arch. Biochem. Biophys. 243:1985;125-134.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 125-134
    • Prutz, W.A.1
  • 5
    • 0030781227 scopus 로고    scopus 로고
    • Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis
    • Kissner R., et al. Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chem. Res. Toxicol. 10:1997;1285-1292.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1285-1292
    • Kissner, R.1
  • 6
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., et al. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266:1991;4244-4250.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1
  • 7
    • 0025874048 scopus 로고
    • Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and nitric oxide
    • Radi R., et al. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch. Biochem. Biophys. 288:1991;481-487.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 481-487
    • Radi, R.1
  • 8
    • 0003092733 scopus 로고    scopus 로고
    • The biological chemistry of peroxynitrite
    • L.J. Ignarro. Academic Press
    • Radi R., et al. The biological chemistry of peroxynitrite. Ignarro L.J. Nitric Oxide Biology and Pathobiology. 2000;57-82 Academic Press.
    • (2000) Nitric Oxide Biology and Pathobiology , pp. 57-82
    • Radi, R.1
  • 9
    • 0031740360 scopus 로고    scopus 로고
    • Peroxynitrite reactions with carbon dioxide-bicarbonate
    • Radi R., et al. Peroxynitrite reactions with carbon dioxide-bicarbonate. Methods Enzymol. 301:1999;353-367.
    • (1999) Methods Enzymol. , vol.301 , pp. 353-367
    • Radi, R.1
  • 10
    • 0033574624 scopus 로고    scopus 로고
    • Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide
    • Bonini M.G., et al. Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide. J. Biol. Chem. 274:1999;10802-10806.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10802-10806
    • Bonini, M.G.1
  • 11
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity
    • van der Vliet A., et al. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J. Biol. Chem. 272:1997;7617-7625.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7617-7625
    • Van Der Vliet, A.1
  • 12
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders
    • Wu W., et al. Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J. Biol. Chem. 274:1999;25933-25944.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25933-25944
    • Wu, W.1
  • 13
    • 0035667004 scopus 로고    scopus 로고
    • Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration
    • Baldus S., et al. Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration. J. Clin. Invest. 108:2001;1759-1770.
    • (2001) J. Clin. Invest. , vol.108 , pp. 1759-1770
    • Baldus, S.1
  • 14
    • 0039173035 scopus 로고    scopus 로고
    • Mechanism of reaction of myeloperoxidase with nitrite
    • Burner U., et al. Mechanism of reaction of myeloperoxidase with nitrite. J. Biol. Chem. 275:2000;20597-20601.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20597-20601
    • Burner, U.1
  • 15
    • 0034830870 scopus 로고    scopus 로고
    • Microperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals
    • Ricoux R., et al. Microperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals. Eur. J. Biochem. 268:2001;3783-3788.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3783-3788
    • Ricoux, R.1
  • 17
    • 0026439963 scopus 로고
    • Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite
    • Beckman J.S., et al. Kinetics of superoxide dismutase- and iron-catalyzed nitration of phenolics by peroxynitrite. Arch. Biochem. Biophys. 298:1992;438-445.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 438-445
    • Beckman, J.S.1
  • 18
    • 0026485192 scopus 로고
    • Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
    • Ischiropoulos H., et al. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch. Biochem. Biophys. 298:1992;431-437.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 431-437
    • Ischiropoulos, H.1
  • 19
    • 0035853685 scopus 로고    scopus 로고
    • Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration
    • Quijano C., et al. Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration. J. Biol. Chem. 276:2001;11631-11638.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11631-11638
    • Quijano, C.1
  • 20
    • 0032486405 scopus 로고    scopus 로고
    • Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine
    • Yamakura F., et al. Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. J. Biol. Chem. 273:1998;14085-14089.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14085-14089
    • Yamakura, F.1
  • 21
    • 0036679808 scopus 로고    scopus 로고
    • Nitric oxide trapping of the tyrosyl radical-chemistry and biochemistry
    • Gunther M.R., et al. Nitric oxide trapping of the tyrosyl radical-chemistry and biochemistry. Toxicology. 177:2002;1-9.
    • (2002) Toxicology , vol.177 , pp. 1-9
    • Gunther, M.R.1
  • 22
    • 0034483934 scopus 로고    scopus 로고
    • Quantification of 3-nitrotyrosine in biological tissues and fluids: Generating valid results by eliminating artifactual formation
    • Yi D., et al. Quantification of 3-nitrotyrosine in biological tissues and fluids: generating valid results by eliminating artifactual formation. J. Am. Soc. Mass Spectrom. 11:2000;578-586.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 578-586
    • Yi, D.1
  • 23
    • 0346218261 scopus 로고    scopus 로고
    • Cytochrome c: A catalyst and target of nitric oxide-dependent protein nitration
    • 10.1016/j.abb.2003.08.033 (
    • Castro L., et al. Cytochrome c: a catalyst and target of nitric oxide-dependent protein nitration. Arch. Biochem. Biophys. 2003;. 10.1016/j.abb.2003.08.033 ( http://www.elsevier.com/locate/issn/0003-9861 ).
    • (2003) Arch. Biochem. Biophys.
    • Castro, L.1
  • 24
    • 0030048479 scopus 로고    scopus 로고
    • Modulation of superoxide-dependent oxidation and hydroxylation reactions by nitric oxide
    • Miles A.M., et al. Modulation of superoxide-dependent oxidation and hydroxylation reactions by nitric oxide. J. Biol. Chem. 271:1996;40-47.
    • (1996) J. Biol. Chem. , vol.271 , pp. 40-47
    • Miles, A.M.1
  • 25
    • 0035800823 scopus 로고    scopus 로고
    • Reaction of superoxide and nitric oxide with peroxynitrite. Implications for peroxynitrite-mediated oxidation reactions in vivo
    • Jourd'heuil D., et al. Reaction of superoxide and nitric oxide with peroxynitrite. Implications for peroxynitrite-mediated oxidation reactions in vivo. J. Biol. Chem. 276:2001;28799-28805.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28799-28805
    • Jourd'Heuil, D.1
  • 26
    • 0028151406 scopus 로고
    • Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo H., et al. Nitric oxide regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives. J. Biol. Chem. 269:1994;26066-26075.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26066-26075
    • Rubbo, H.1
  • 27
    • 0030250041 scopus 로고    scopus 로고
    • Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration
    • Gow A., et al. Carbon dioxide enhancement of peroxynitrite-mediated protein tyrosine nitration. Arch. Biochem. Biophys. 333:1996;42-48.
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 42-48
    • Gow, A.1
  • 28
    • 0031007654 scopus 로고    scopus 로고
    • The catalytic role of carbon dioxide in the decomposition of peroxynitrite
    • Pryor W.A., et al. The catalytic role of carbon dioxide in the decomposition of peroxynitrite. Free Radic. Biol. Med. 23:1997;331-338.
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 331-338
    • Pryor, W.A.1
  • 29
    • 0033714187 scopus 로고    scopus 로고
    • Hypercapnia induces injury to alveolar epithelial cells via a nitric oxide-dependent pathway
    • Lang J.D. Jr, et al. Hypercapnia induces injury to alveolar epithelial cells via a nitric oxide-dependent pathway. Am. J. Physiol. Lung Cell. Mol. Physiol. 279:2000;L994-L1002.
    • (2000) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.279
    • Lang Jr., J.D.1
  • 30
    • 0038731081 scopus 로고    scopus 로고
    • Biological selectivity and functional aspects of protein tyrosine nitration
    • Ischiropoulos H. Biological selectivity and functional aspects of protein tyrosine nitration. Biochem. Biophys. Res. Commun. 305:2003;776-783.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 776-783
    • Ischiropoulos, H.1
  • 31
    • 0033534725 scopus 로고    scopus 로고
    • Kinetics of peroxynitrite reaction with amino acids and human serum albumin
    • Alvarez B., et al. Kinetics of peroxynitrite reaction with amino acids and human serum albumin. J. Biol. Chem. 274:1999;842-848.
    • (1999) J. Biol. Chem. , vol.274 , pp. 842-848
    • Alvarez, B.1
  • 32
    • 0034942993 scopus 로고    scopus 로고
    • Investigation of tyrosine nitration in proteins by mass spectrometry
    • Petersson A.S., et al. Investigation of tyrosine nitration in proteins by mass spectrometry. J. Mass Spectrom. 36:2001;616-625.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 616-625
    • Petersson, A.S.1
  • 33
    • 0035566429 scopus 로고    scopus 로고
    • Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry
    • Sarver A., et al. Analysis of peptides and proteins containing nitrotyrosine by matrix-assisted laser desorption/ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 12:2001;439-448.
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , pp. 439-448
    • Sarver, A.1
  • 34
    • 0035369688 scopus 로고    scopus 로고
    • Site-selective nitration of tyrosine in human serum albumin by peroxynitrite
    • Jiao K., et al. Site-selective nitration of tyrosine in human serum albumin by peroxynitrite. Anal. Biochem. 293:2001;43-52.
    • (2001) Anal. Biochem. , vol.293 , pp. 43-52
    • Jiao, K.1
  • 35
    • 0030004581 scopus 로고    scopus 로고
    • Peroxynitrite-dependent tryptophan nitration
    • Alvarez B., et al. Peroxynitrite-dependent tryptophan nitration. Chem. Res. Toxicol. 9:1996;390-396.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 390-396
    • Alvarez, B.1
  • 36
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson E.K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry. 14:1975;5294-5299.
    • (1975) Biochemistry , vol.14 , pp. 5294-5299
    • Hodgson, E.K.1    Fridovich, I.2
  • 37
    • 0016816805 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Chemiluminescence and peroxidation
    • Hodgson E.K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation. Biochemistry. 14:1975;5299-5303.
    • (1975) Biochemistry , vol.14 , pp. 5299-5303
    • Hodgson, E.K.1    Fridovich, I.2
  • 38
    • 0033214459 scopus 로고    scopus 로고
    • Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical
    • Goss S.P., et al. Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase. Role of carbonate anion radical. J. Biol. Chem. 274:1999;28233-28239.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28233-28239
    • Goss, S.P.1
  • 39
    • 0027066851 scopus 로고
    • Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase
    • Smith C.D., et al. Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase. Arch. Biochem. Biophys. 299:1992;350-355.
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 350-355
    • Smith, C.D.1
  • 40
    • 0030833449 scopus 로고    scopus 로고
    • Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite
    • Crow J.P., et al. Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite. J. Neurochem. 69:1997;1936-1944.
    • (1997) J. Neurochem. , vol.69 , pp. 1936-1944
    • Crow, J.P.1
  • 41
    • 0037330482 scopus 로고    scopus 로고
    • Mutation of tyrosine 190 to alanine eliminates the inactivation of cytochrome P450 2B1 by peroxynitrite
    • Lin H.L., et al. Mutation of tyrosine 190 to alanine eliminates the inactivation of cytochrome P450 2B1 by peroxynitrite. Chem. Res. Toxicol. 16:2003;129-136.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 129-136
    • Lin, H.L.1
  • 42
    • 0036712607 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: Implications for enzymatic activity
    • Lanone S., et al. Inducible nitric oxide synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: implications for enzymatic activity. Biochem. J. 366:2002;399-404.
    • (2002) Biochem. J. , vol.366 , pp. 399-404
    • Lanone, S.1
  • 43
    • 0036479238 scopus 로고    scopus 로고
    • Selective nitration of histone tyrosine residues in vivo in mutatect tumors
    • Haqqani A.S., et al. Selective nitration of histone tyrosine residues in vivo in mutatect tumors. J. Biol. Chem. 277:2002;3614-3621.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3614-3621
    • Haqqani, A.S.1
  • 44
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of α-tubulin: A nitric oxide-dependent mechanism of cellular injury
    • Eiserich J.P., et al. Microtubule dysfunction by posttranslational nitrotyrosination of α-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc. Natl. Acad. Sci. U. S. A. 96:1999;6365-6370.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1
  • 45
    • 0031906885 scopus 로고    scopus 로고
    • Suppression of tubulin tyrosine ligase during tumor growth
    • Lafanechere L., et al. Suppression of tubulin tyrosine ligase during tumor growth. J. Cell Sci. 111:1998;171-181.
    • (1998) J. Cell Sci. , vol.111 , pp. 171-181
    • Lafanechere, L.1
  • 46
    • 0034739245 scopus 로고    scopus 로고
    • Incorporation of nitrotyrosine into α-tubulin by recombinant mammalian tubulin-tyrosine ligase
    • Kalisz H.M., et al. Incorporation of nitrotyrosine into α-tubulin by recombinant mammalian tubulin-tyrosine ligase. Biochim. Biophys. Acta. 1481:2000;131-138.
    • (2000) Biochim. Biophys. Acta , vol.1481 , pp. 131-138
    • Kalisz, H.M.1
  • 47
    • 0036411907 scopus 로고    scopus 로고
    • Incorporation of 3-nitrotyrosine into the C-terminus of α-tubulin is reversible and not detrimental to dividing cells
    • Bisig C.G., et al. Incorporation of 3-nitrotyrosine into the C-terminus of α-tubulin is reversible and not detrimental to dividing cells. Eur. J. Biochem. 269:2002;5037-5045.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5037-5045
    • Bisig, C.G.1
  • 48
    • 0037163058 scopus 로고    scopus 로고
    • Alteration of the C-terminal amino acid of tubulin specifically inhibits myogenic differentiation
    • Chang W., et al. Alteration of the C-terminal amino acid of tubulin specifically inhibits myogenic differentiation. J. Biol. Chem. 277:2002;30690-30698.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30690-30698
    • Chang, W.1
  • 49
    • 0037423394 scopus 로고    scopus 로고
    • Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization
    • Aslan M., et al. Nitric oxide-dependent generation of reactive species in sickle cell disease. Actin tyrosine induces defective cytoskeletal polymerization. J. Biol. Chem. 278:2003;4194-4204.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4194-4204
    • Aslan, M.1
  • 50
    • 0041620467 scopus 로고    scopus 로고
    • Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry
    • Nikov G., et al. Analysis of nitrated proteins by nitrotyrosine-specific affinity probes and mass spectrometry. Anal. Biochem. 320:2003;214-222.
    • (2003) Anal. Biochem. , vol.320 , pp. 214-222
    • Nikov, G.1
  • 51
    • 0034663360 scopus 로고    scopus 로고
    • Proteolytic degradation of tyrosine nitrated proteins
    • Souza J.M., et al. Proteolytic degradation of tyrosine nitrated proteins. Arch. Biochem. Biophys. 380:2000;360-366.
    • (2000) Arch. Biochem. Biophys. , vol.380 , pp. 360-366
    • Souza, J.M.1
  • 52
    • 0141703321 scopus 로고    scopus 로고
    • Nitric oxide inhibits H2O2-induced transferrin receptor-dependent apoptosis in endothelial cells: Role of ubiquitin-proteasome pathway
    • Kotamraju S., et al. Nitric oxide inhibits H2O2-induced transferrin receptor-dependent apoptosis in endothelial cells: role of ubiquitin-proteasome pathway. Proc. Natl. Acad. Sci. U. S. A. 100:2003;10653-10658.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10653-10658
    • Kotamraju, S.1
  • 53
    • 0028834228 scopus 로고
    • Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells
    • Ischiropoulos H., et al. Peroxynitrite-mediated inhibition of DOPA synthesis in PC12 cells. J. Neurochem. 65:1995;2366-2372.
    • (1995) J. Neurochem. , vol.65 , pp. 2366-2372
    • Ischiropoulos, H.1
  • 54
    • 0037948843 scopus 로고    scopus 로고
    • Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins
    • Irie Y., et al. Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins. Proc. Natl. Acad. Sci. U. S. A. 100:2003;5634-5639.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 5634-5639
    • Irie, Y.1
  • 55
    • 0030016003 scopus 로고    scopus 로고
    • Serum concentrations of nitrite in patients with HIV-1 infection
    • Torre D., et al. Serum concentrations of nitrite in patients with HIV-1 infection. J. Clin. Pathol. 49:1996;574-576.
    • (1996) J. Clin. Pathol. , vol.49 , pp. 574-576
    • Torre, D.1
  • 56
    • 0037424429 scopus 로고    scopus 로고
    • Lack of tyrosine nitration by hypochlorous acid in the presence of physiological concentrations of nitrite. Implications for the role of nitryl chloride in tyrosine nitration in vivo
    • Whiteman M., et al. Lack of tyrosine nitration by hypochlorous acid in the presence of physiological concentrations of nitrite. Implications for the role of nitryl chloride in tyrosine nitration in vivo. J. Biol. Chem. 278:2003;8380-8384.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8380-8384
    • Whiteman, M.1
  • 57
    • 0037189377 scopus 로고    scopus 로고
    • Myeloperoxidase, a leukocyte-derived vascular NO oxidase
    • Eiserich J.P., et al. Myeloperoxidase, a leukocyte-derived vascular NO oxidase. Science. 296:2002;2391-2394.
    • (2002) Science , vol.296 , pp. 2391-2394
    • Eiserich, J.P.1
  • 58
    • 0036801357 scopus 로고    scopus 로고
    • Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases
    • Baldus S., et al. Spatial mapping of pulmonary and vascular nitrotyrosine reveals the pivotal role of myeloperoxidase as a catalyst for tyrosine nitration in inflammatory diseases. Free Radic. Biol. Med. 33:2002;1010-1019.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1010-1019
    • Baldus, S.1
  • 59
    • 0037646515 scopus 로고    scopus 로고
    • Transmembrane nitration of hydrophobic tyrosyl peptides. Localization, characterization, mechanism of nitration, and biological implications
    • Zhang H., et al. Transmembrane nitration of hydrophobic tyrosyl peptides. Localization, characterization, mechanism of nitration, and biological implications. J. Biol. Chem. 278:2003;8969-8978.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8969-8978
    • Zhang, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.