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Volumn 6, Issue 8, 2007, Pages 662-680

Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; CABERGOLINE; DEFEROXAMINE; DIHYDROLIPOATE; EBSELEN; HYDRALAZINE; METALLOPORPHYRIN; NEBIVOLOL; NITRATE; NITRIC OXIDE; NITRITE; NITROXIDE; NORPHENAZONE; PARACETAMOL; PENICILLAMINE; PEROXYNITRITE; PINDOLOL; PROPOFOL; RASAGILINE; SCAVENGER; SELEGILINE; SELENIUM DERIVATIVE; SIMVASTATIN; SUPEROXIDE; TELLURIUM DERIVATIVE; TEMPOL; THIOL DERIVATIVE; UNINDEXED DRUG; URIC ACID; ZILEUTON;

EID: 34547673497     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd2222     Document Type: Review
Times cited : (1766)

References (310)
  • 1
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implication for endothelial injury from NO and superoxide
    • Beckman, J. S. et al. Apparent hydroxyl radical production by peroxynitrite: Implication for endothelial injury from NO and superoxide. Proc. Natl Acad. Sci. USA 87, 1620-1624 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1620-1624
    • Beckman, J.S.1
  • 2
    • 0022640297 scopus 로고
    • Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor
    • Gryglewski, R. J., Palmer, R. M. & Moncada, S. Superoxide anion is involved in the breakdown of endothelium-derived vascular relaxing factor. Nature 320, 454-456 (1986).
    • (1986) Nature , vol.320 , pp. 454-456
    • Gryglewski, R.J.1    Palmer, R.M.2    Moncada, S.3
  • 3
    • 0035282582 scopus 로고    scopus 로고
    • Unraveling peroxynitrite formation in biological systems
    • Radi, R. et al. Unraveling peroxynitrite formation in biological systems. Free Radic. Biol. Med. 30, 463-488 (2001).
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 463-488
    • Radi, R.1
  • 4
    • 7944228943 scopus 로고    scopus 로고
    • Macrophage-derived peroxynitrite diffusion and toxicity to Trypanosoma cruzi
    • Alvarez, M. N., Piacenza, L., Irigoin, F., Peluffo, G. & Radi, R. Macrophage-derived peroxynitrite diffusion and toxicity to Trypanosoma cruzi. Arch. Biochem. Biophys. 432, 222-232 (2004).
    • (2004) Arch. Biochem. Biophys , vol.432 , pp. 222-232
    • Alvarez, M.N.1    Piacenza, L.2    Irigoin, F.3    Peluffo, G.4    Radi, R.5
  • 5
    • 15344349691 scopus 로고    scopus 로고
    • oxygen, and superoxide formation and consumption in macrophage cultures
    • Nalwaya, N. & Deen, W. M. NO, oxygen, and superoxide formation and consumption in macrophage cultures. Chem. Res. Toxicol. 18, 486-493 (2005).
    • (2005) Chem. Res. Toxicol , vol.18 , pp. 486-493
    • Nalwaya, N.1    Deen, W.M.N.2
  • 6
    • 23744461597 scopus 로고    scopus 로고
    • Tyrosine nitration by superoxide and NO fluxes in biological systems: Modeling the impact of superoxide dismutase and NO diffusion
    • Quijano, C., Romero, N. & Radi, R. Tyrosine nitration by superoxide and NO fluxes in biological systems: Modeling the impact of superoxide dismutase and NO diffusion. Free Radic. Biol. Med. 39, 728-741 (2005).
    • (2005) Free Radic. Biol. Med , vol.39 , pp. 728-741
    • Quijano, C.1    Romero, N.2    Radi, R.3
  • 7
    • 0031460696 scopus 로고    scopus 로고
    • Peroxynitrite rapidly permeates phospholipid membranes
    • Maria, S. S., Lee, J. & Groves, J. T. Peroxynitrite rapidly permeates phospholipid membranes. Proc. Natl Acad. Sci. USA 94, 14243-14248 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14243-14248
    • Maria, S.S.1    Lee, J.2    Groves, J.T.3
  • 8
    • 0032584141 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite across erythrocyte membranes
    • Denicola, A., Souza, J. M. & Radi, R. Diffusion of peroxynitrite across erythrocyte membranes. Proc. Natl Acad. Sci. USA 95, 3566-3571 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3566-3571
    • Denicola, A.1    Souza, J.M.2    Radi, R.3
  • 9
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls: The cytotoxic potential of superoxide and nitric oxide
    • Radi, R., Beckman, J. S., Bush, K. M. & Freeman, B. A. Peroxynitrite oxidation of sulfhydryls: The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266, 4244-4250 (1991).
    • (1991) J. Biol. Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 10
    • 33744959547 scopus 로고    scopus 로고
    • Mechanistic studies of peroxynitrite-mediated tyrosine nitration in membranes using the hydrophobic probe N-t-BOC-L-tyrosine tert-butyl ester
    • Bartesaghi, S. et al. Mechanistic studies of peroxynitrite-mediated tyrosine nitration in membranes using the hydrophobic probe N-t-BOC-L-tyrosine tert-butyl ester. Biochemistry 45, 6813-6825 (2006).
    • (2006) Biochemistry , vol.45 , pp. 6813-6825
    • Bartesaghi, S.1
  • 11
    • 0031045544 scopus 로고    scopus 로고
    • Pathways of peroxynitrite oxidation of thiol groups
    • Ouijano, C., Alvarez, B., Gatti, R., Augusto, O. & Radi, R. Pathways of peroxynitrite oxidation of thiol groups. Biochem. J. 322, 167-173 (1997).
    • (1997) Biochem. J , vol.322 , pp. 167-173
    • Ouijano, C.1    Alvarez, B.2    Gatti, R.3    Augusto, O.4    Radi, R.5
  • 12
    • 0042974241 scopus 로고    scopus 로고
    • Sulfenic acid formation in human serum albumin
    • Carballal, S. et al. Sulfenic acid formation in human serum albumin. Biochemistry 42, 9906-9914 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9906-9914
    • Carballal, S.1
  • 13
    • 0031875938 scopus 로고    scopus 로고
    • Radical nature of peroxynitrite reactivity
    • Lymar, S. V. & Hurst, J. K. Radical nature of peroxynitrite reactivity. Chem. Res. Toxicol. 11, 714-715 (1998).
    • (1998) Chem. Res. Toxicol , vol.11 , pp. 714-715
    • Lymar, S.V.1    Hurst, J.K.2
  • 14
    • 21944443058 scopus 로고    scopus 로고
    • Chemistry of peroxynitrites as compared to peroxynitrates
    • Goldstein, S., Lind, J. & Merenyi, G. Chemistry of peroxynitrites as compared to peroxynitrates. Chem. Rev. 105, 2457-2470 (2005).
    • (2005) Chem. Rev , vol.105 , pp. 2457-2470
    • Goldstein, S.1    Lind, J.2    Merenyi, G.3
  • 15
    • 0242666822 scopus 로고    scopus 로고
    • Reaction of human hemoglobin with peroxynitrite: Isomerization to nitrate and secondary formation of protein radicals
    • Romero, N. et al. Reaction of human hemoglobin with peroxynitrite: isomerization to nitrate and secondary formation of protein radicals. J. Biol. Chem. 278, 44049-44057 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 44049-44057
    • Romero, N.1
  • 16
    • 1642570319 scopus 로고    scopus 로고
    • Radi, R. NO, oxidants, and protein tyrosine nitration. Proc. Natl Acad. Sci. USA 101, 4003-4008 (2004).
    • Radi, R. NO, oxidants, and protein tyrosine nitration. Proc. Natl Acad. Sci. USA 101, 4003-4008 (2004).
  • 17
    • 0035971225 scopus 로고    scopus 로고
    • Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite
    • Bonini, M. G. & Augusto, O. Carbon dioxide stimulates the production of thiyl, sulfinyl, and disulfide radical anion from thiol oxidation by peroxynitrite. J. Biol. Chem. 276, 9749-54 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 9749-9754
    • Bonini, M.G.1    Augusto, O.2
  • 18
    • 0029145358 scopus 로고
    • Peroxynitrite causes DNA damage and oxidation of thiols in rat thymocytes
    • Salgo, M. G., Bermudez, E., Squadrito, G. L. & Pryor, W. A. Peroxynitrite causes DNA damage and oxidation of thiols in rat thymocytes. Arch. Biochem. Biophys. 322, 500-505 (1995).
    • (1995) Arch. Biochem. Biophys , vol.322 , pp. 500-505
    • Salgo, M.G.1    Bermudez, E.2    Squadrito, G.L.3    Pryor, W.A.4
  • 19
    • 0031423789 scopus 로고    scopus 로고
    • DNA damage induced by peroxynitrite: Subsequent biological effects
    • Szabó, C. & Ohshima, H. DNA damage induced by peroxynitrite: subsequent biological effects. Nitric Oxide 1, 373-385 (1997).
    • (1997) Nitric Oxide , vol.1 , pp. 373-385
    • Szabó, C.1    Ohshima, H.2
  • 20
    • 0033024623 scopus 로고    scopus 로고
    • DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite
    • Burney, S., Niles, J. C., Dedon, P. C. & Tannenbaum, S. R. DNA damage in deoxynucleosides and oligonucleotides treated with peroxynitrite. Chem. Res. Toxicol. 12, 513-520 (1999).
    • (1999) Chem. Res. Toxicol , vol.12 , pp. 513-520
    • Burney, S.1    Niles, J.C.2    Dedon, P.C.3    Tannenbaum, S.R.4
  • 21
    • 31544432817 scopus 로고    scopus 로고
    • Peroxynitrite-induced oxidation and nitration products of guanine and 8-oxoguanine: Structures and mechanisms of product formation
    • Niles, J. C., Wishnok, J. S. & Tannenbaum, S. R. Peroxynitrite-induced oxidation and nitration products of guanine and 8-oxoguanine: Structures and mechanisms of product formation. Nitric Oxide 14, 109-121 (2006).
    • (2006) Nitric Oxide , vol.14 , pp. 109-121
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 23
    • 0028670471 scopus 로고
    • Peroxynitrite induces both vasodilatation and impaired vascular relaxation in the isolated perfused rat heart
    • Villa, L. M., Salas, E., Darley-Usmar, V. M., Radomski, M. W. & Moncada, S. Peroxynitrite induces both vasodilatation and impaired vascular relaxation in the isolated perfused rat heart. Proc. Natl Acad. Sci. USA 91, 12383-12387 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12383-12387
    • Villa, L.M.1    Salas, E.2    Darley-Usmar, V.M.3    Radomski, M.W.4    Moncada, S.5
  • 24
    • 0028151406 scopus 로고
    • NO regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives
    • Rubbo, H. et al. NO regulation of superoxide and peroxynitrite-dependent lipid peroxidation. Formation of novel nitrogen-containing oxidized lipid derivatives. J. Biol. Chem. 269, 26066-26075 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 26066-26075
    • Rubbo, H.1
  • 26
    • 0028990886 scopus 로고
    • 2-isoprostanes during oxidation of human low-density lipoprotein and plasma by peroxynitrite
    • 2-isoprostanes during oxidation of human low-density lipoprotein and plasma by peroxynitrite. Circ. Res. 77, 335-341 (1995).
    • (1995) Circ. Res , vol.77 , pp. 335-341
    • Moore, K.P.1    Darley-Usmar, V.2    Morrow, J.3    Roberts, L.J.4
  • 27
    • 33746000445 scopus 로고    scopus 로고
    • Reversible post-translational modification of proteins by nitrated fatty acids in vivo
    • Batthyany C, et al. Reversible post-translational modification of proteins by nitrated fatty acids in vivo. J. Biol. Chem. 281 20450-20463 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 20450-20463
    • Batthyany, C.1
  • 28
    • 33645238897 scopus 로고    scopus 로고
    • Fatty acid transduction of NO signaling: Nitrolinoleic acid potently activates endothelial heme oxygenase 1 expression
    • Wright, M. M. et al. Fatty acid transduction of NO signaling: nitrolinoleic acid potently activates endothelial heme oxygenase 1 expression. Proc. Natl Acad. Sci. USA 103, 4299-4304 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 4299-4304
    • Wright, M.M.1
  • 29
    • 0033527413 scopus 로고    scopus 로고
    • Oxidation of tetrahydrobiopterin by peroxynitrite: Implications for vascular endothelial function
    • Milstien, S. & Katusic, Z. Oxidation of tetrahydrobiopterin by peroxynitrite: Implications for vascular endothelial function. Biochem. Biophys. Res. Commun. 263, 681-684 (1999).
    • (1999) Biochem. Biophys. Res. Commun , vol.263 , pp. 681-684
    • Milstien, S.1    Katusic, Z.2
  • 30
    • 0038604446 scopus 로고    scopus 로고
    • Interactions of peroxynitrite, tetrahydrobiopterin, ascorbic acid, and thiols: Implications for uncoupling endothelial nitric-oxide synthase
    • Kuzkaya, N., Weissmann, N., Harrison, D. G. & Dikalov, S. Interactions of peroxynitrite, tetrahydrobiopterin, ascorbic acid, and thiols: implications for uncoupling endothelial nitric-oxide synthase. J. Biol. Chem. 278, 22546-22554 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 22546-22554
    • Kuzkaya, N.1    Weissmann, N.2    Harrison, D.G.3    Dikalov, S.4
  • 31
    • 33645780634 scopus 로고    scopus 로고
    • Endothelial NO synthase in vascular disease: From marvel to menace
    • Forstermann, U. & Munzel, T. Endothelial NO synthase in vascular disease: From marvel to menace. Circulation 113, 1708-1714 (2006).
    • (2006) Circulation , vol.113 , pp. 1708-1714
    • Forstermann, U.1    Munzel, T.2
  • 32
    • 0033609921 scopus 로고    scopus 로고
    • Reaction of peroxynitrite with reduced nicotinamide nucleotides, the formation of hydrogen peroxide
    • Kirsch, M. & de Groot, H. Reaction of peroxynitrite with reduced nicotinamide nucleotides, the formation of hydrogen peroxide. J. Biol. Chem. 274, 24664-24670 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 24664-24670
    • Kirsch, M.1    de Groot, H.2
  • 33
    • 0033845751 scopus 로고    scopus 로고
    • Reactivity of peroxynitrite versus simultaneous generation of (*)NO and O(2)(*) (-) toward NADH
    • Goldstein, S. & Czapski, G. Reactivity of peroxynitrite versus simultaneous generation of (*)NO and O(2)(*) (-) toward NADH. Chem. Res. Toxicol. 13, 736-741 (2000).
    • (2000) Chem. Res. Toxicol , vol.13 , pp. 736-741
    • Goldstein, S.1    Czapski, G.2
  • 34
    • 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. 298 431-437 (1992).
    • (1992) Arch. Biochem. Biophys , vol.298 , pp. 431-437
    • Ischiropoulos, H.1
  • 35
    • 0032501998 scopus 로고    scopus 로고
    • Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and Oxidation of critical tyrosine residues
    • MacMillan-Crow, L. A., Crow, J. P. & Thompson, J. A. Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and Oxidation of critical tyrosine residues. Biochemistry 37, 1613-1622 (1998).
    • (1998) Biochemistry , vol.37 , pp. 1613-1622
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Thompson, J.A.3
  • 36
    • 4043159127 scopus 로고    scopus 로고
    • Inactivation of human Cu, Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical
    • Alvarez, B. et al. Inactivation of human Cu, Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical. Free Radic. Biol. Med. 37, 813-822 (2004).
    • (2004) Free Radic. Biol. Med , vol.37 , pp. 813-822
    • Alvarez, B.1
  • 37
    • 0002770493 scopus 로고    scopus 로고
    • Superoxide dismutase and the death of motoneurons in ALS
    • Beckman, J. S., Estevez, A. G., Crow, J. P. & Barbeito, L. Superoxide dismutase and the death of motoneurons in ALS. Trends Neurosci. 24 (Suppl. 11), 15-20 (2001).
    • (2001) Trends Neurosci , vol.24 , Issue.SUPPL. 11 , pp. 15-20
    • Beckman, J.S.1    Estevez, A.G.2    Crow, J.P.3    Barbeito, L.4
  • 38
    • 0037169547 scopus 로고    scopus 로고
    • Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite
    • Savvides, S. N. et al. Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite. J. Biol. Chem. 277, 2779-2784 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 2779-2784
    • Savvides, S.N.1
  • 40
    • 0027158630 scopus 로고    scopus 로고
    • Hogg, N., Darley-Usmar, V. M., Wilson, M. T. & Moncada, S. The oxidation of α-tocopherol in human low-density lipoprotein by the simultaneous generation of superoxide and NO FEBS Lett. 326, 199-203 (1993).
    • Hogg, N., Darley-Usmar, V. M., Wilson, M. T. & Moncada, S. The oxidation of α-tocopherol in human low-density lipoprotein by the simultaneous generation of superoxide and NO FEBS Lett. 326, 199-203 (1993).
  • 41
    • 0028105887 scopus 로고
    • Interactions of peroxynitrite with human plasma and its constituents: Oxidative damage and antioxidant depletion
    • Van der Vliet, A. et al. Interactions of peroxynitrite with human plasma and its constituents: Oxidative damage and antioxidant depletion. Biochem. J. 303, 295-301 (1994).
    • (1994) Biochem. J , vol.303 , pp. 295-301
    • Van der Vliet, A.1
  • 42
    • 1542274276 scopus 로고    scopus 로고
    • Oxidation of vitamin E and vitamin C and inhibition of brain mitochondrial oxidative phosphorylation by peroxynitrite
    • Vatassery, G. T., Lai, J. C., DeMaster, E. G., Smith, W. E. & Quach, H. T. Oxidation of vitamin E and vitamin C and inhibition of brain mitochondrial oxidative phosphorylation by peroxynitrite. J. Neurosci. Res. 75, 845-853 (2004).
    • (2004) J. Neurosci. Res , vol.75 , pp. 845-853
    • Vatassery, G.T.1    Lai, J.C.2    DeMaster, E.G.3    Smith, W.E.4    Quach, H.T.5
  • 43
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but NO does not
    • Hausladen, A. & Fridovich, I. Superoxide and peroxynitrite inactivate aconitases, but NO does not. J. Biol. Chem. 269, 29405-29408 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 44
    • 0028937652 scopus 로고
    • Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite
    • Crow, J. P., Beckman, J. S. & McCord, J. M. Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite. Biochemistry 34, 3544-3552 (1995).
    • (1995) Biochemistry , vol.34 , pp. 3544-3552
    • Crow, J.P.1    Beckman, J.S.2    McCord, J.M.3
  • 45
    • 0028175539 scopus 로고
    • Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by NO, peroxynitrite and related nitrosating agents
    • Mohr, S., Stamler, J. S. & Brune, B. Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by NO, peroxynitrite and related nitrosating agents. FEBS Lett. 348, 223-227 (1994).
    • (1994) FEBS Lett , vol.348 , pp. 223-227
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 46
    • 0032496422 scopus 로고    scopus 로고
    • Rapid and irreversible inhibition of creatine kinase by peroxynitrite
    • Konorev, E. A., Hogg, N. & Kalyanaraman, B. Rapid and irreversible inhibition of creatine kinase by peroxynitrite. FEBS Lett. 427 171-174 (1998).
    • (1998) FEBS Lett , vol.427 , pp. 171-174
    • Konorev, E.A.1    Hogg, N.2    Kalyanaraman, B.3
  • 47
    • 0035110310 scopus 로고    scopus 로고
    • Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure
    • Mihm, M. J. et al. Peroxynitrite induced nitration and inactivation of myofibrillar creatine kinase in experimental heart failure. Cardiovasc. Res. 49, 798-807 (2001).
    • (2001) Cardiovasc. Res , vol.49 , pp. 798-807
    • Mihm, M.J.1
  • 48
    • 0035824528 scopus 로고    scopus 로고
    • Nitration and inactivation of tyrosine hydroxylase by peroxynitrite
    • Blanchard-Fillion, B. et al. Nitration and inactivation of tyrosine hydroxylase by peroxynitrite. J. Biol. Chem. 276, 46017-46023 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 46017-46023
    • Blanchard-Fillion, B.1
  • 49
    • 0035887860 scopus 로고    scopus 로고
    • Induction of α-synuclein aggregation by intracellular nitrative insult
    • Paxinou, E. et al. Induction of α-synuclein aggregation by intracellular nitrative insult. J. Neurosci. 21, 8053-8061 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 8053-8061
    • Paxinou, E.1
  • 50
    • 33645546784 scopus 로고    scopus 로고
    • Peroxynitrite-mediated tau modifications stabilize preformed filaments and destabilize microtubules through distinct mechanisms
    • Reynolds, M. R., Lukas, T. J., Berry, R. W. & Binder, L. I. Peroxynitrite-mediated tau modifications stabilize preformed filaments and destabilize microtubules through distinct mechanisms. Biochemistry 45, 4314-4326 (2006).
    • (2006) Biochemistry , vol.45 , pp. 4314-4326
    • Reynolds, M.R.1    Lukas, T.J.2    Berry, R.W.3    Binder, L.I.4
  • 51
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto, T. et al. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J. Biol. Chem. 276, 29596-29602 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 29596-29602
    • Okamoto, T.1
  • 52
    • 20444409184 scopus 로고    scopus 로고
    • Peroxynitrite-mediated matrix metalloproteinase-2 activation in human hepatic stellate cells
    • Migita, K. et al. Peroxynitrite-mediated matrix metalloproteinase-2 activation in human hepatic stellate cells. FEBS Lett. 579, 3119-3125 (2005).
    • (2005) FEBS Lett , vol.579 , pp. 3119-3125
    • Migita, K.1
  • 53
    • 33644850478 scopus 로고    scopus 로고
    • Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite
    • Ji, Y., Neverova, I., Van Eyk, J. E. & Bennett, B. M. Nitration of tyrosine 92 mediates the activation of rat microsomal glutathione S-transferase by peroxynitrite. J. Biol. Chem. 281, 986-991 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 986-991
    • Ji, Y.1    Neverova, I.2    Van Eyk, J.E.3    Bennett, B.M.4
  • 54
    • 33646573080 scopus 로고    scopus 로고
    • Activation of protein kinase C zeta by peroxynitrite regulates LKB 1-dependent AMP-activated protein kinase in cultured endothelial cells
    • Xie, Z. et al. Activation of protein kinase C zeta by peroxynitrite regulates LKB 1-dependent AMP-activated protein kinase in cultured endothelial cells. J. Biol. Chem. 281, 6366-6375 (2005).
    • (2005) J. Biol. Chem , vol.281 , pp. 6366-6375
    • Xie, Z.1
  • 55
    • 27944453616 scopus 로고    scopus 로고
    • Biochemical properties of cytochrome c nitrated by peroxynitrite
    • Jang, B. & Han, S. Biochemical properties of cytochrome c nitrated by peroxynitrite. Biochimie 88, 53-58 (2006).
    • (2006) Biochimie , vol.88 , pp. 53-58
    • Jang, B.1    Han, S.2
  • 57
    • 0028201059 scopus 로고
    • Peroxynitrite inhibition of oxygen consumption and sodium transport in alveolar type II cells
    • Hu, P., Ischiropoulos, H., Beckman, J. S. & Matalon, S. Peroxynitrite inhibition of oxygen consumption and sodium transport in alveolar type II cells. Am. J. Physiol. 266, L628-L634 (1994).
    • (1994) Am. J. Physiol , vol.266
    • Hu, P.1    Ischiropoulos, H.2    Beckman, J.S.3    Matalon, S.4
  • 58
    • 0032488809 scopus 로고    scopus 로고
    • 2+-ATPase in low-frequency stimulated rabbit muscle
    • 2+-ATPase in low-frequency stimulated rabbit muscle. FEBS Lett. 422, 381-384 (1998).
    • (1998) FEBS Lett , vol.422 , pp. 381-384
    • Klebl, B.M.1    Ayoub, A.T.2    Pette, D.3
  • 59
    • 0034665152 scopus 로고    scopus 로고
    • NO-dependent modification of the sarcoplasmic reticulum Ca-ATPase: Localization of cysteine target sites
    • Viner, R. I., Williams. T. D., Schoneich, C. NO-dependent modification of the sarcoplasmic reticulum Ca-ATPase: Localization of cysteine target sites. Free Radic. Biol. Med. 29, 489-496 (2000).
    • (2000) Free Radic. Biol. Med , vol.29 , pp. 489-496
    • Viner, R.I.1    Williams, T.D.2    Schoneich, C.3
  • 61
    • 1542328249 scopus 로고    scopus 로고
    • 2+ exchanger by peroxynitrite in microsomes of pulmonary smooth muscle: Role of matrix metalloproteinase-2
    • 2+ exchanger by peroxynitrite in microsomes of pulmonary smooth muscle: Role of matrix metalloproteinase-2. Biochim. Biophys. Acta 1671, 70-78 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1671 , pp. 70-78
    • Chakraborti, S.1    Mandel, A.2    Das, S.3    Chakraborti, T.4
  • 62
    • 13644256731 scopus 로고    scopus 로고
    • 2+ channels to extracellular oxidative/nitrosative stress in cerebellar granule cells
    • 2+ channels to extracellular oxidative/nitrosative stress in cerebellar granule cells. J. Neurochem. 92, 973-989 (2005).
    • (2005) J. Neurochem , vol.92 , pp. 973-989
    • Gutierrez-Martin, Y.1
  • 63
    • 0032925359 scopus 로고    scopus 로고
    • Peroxynitrite inactivates prostacyclin synthase by heme-thiolate-catalyzed tyrosine nitration
    • Zou, M., Yesilkaya, A. & Ullrich, V. Peroxynitrite inactivates prostacyclin synthase by heme-thiolate-catalyzed tyrosine nitration. Drug Metab. Rev. 31, 343-349 (1999).
    • (1999) Drug Metab. Rev , vol.31 , pp. 343-349
    • Zou, M.1    Yesilkaya, A.2    Ullrich, V.3
  • 64
    • 0142164964 scopus 로고    scopus 로고
    • Peroxynitrite modulates acidic fibroblast growth factor (FGF-1) activity
    • Bagnasco, P. et al. Peroxynitrite modulates acidic fibroblast growth factor (FGF-1) activity. Arch. Biochem. Biophys. 419, 178-189 (2003).
    • (2003) Arch. Biochem. Biophys , vol.419 , pp. 178-189
    • Bagnasco, P.1
  • 65
    • 0037108520 scopus 로고    scopus 로고
    • Enhanced activity of human IL-10 after nitration in reducing human IL-1 production by stimulated peripheral blood mononuclear cells
    • Freels, J. L. et al. Enhanced activity of human IL-10 after nitration in reducing human IL-1 production by stimulated peripheral blood mononuclear cells. J. Immunol. 169, 4568-4571 (2002).
    • (2002) J. Immunol , vol.169 , pp. 4568-4571
    • Freels, J.L.1
  • 66
    • 0033610890 scopus 로고    scopus 로고
    • Peroxynitrite induces covalent dimerization of epidermal growth factor receptors in A431 epidermoid carcinoma cells
    • van der Vliet, A, Hristova, M., Cross, C. E., Eiserich, J. P. & Goldkorn, T. Peroxynitrite induces covalent dimerization of epidermal growth factor receptors in A431 epidermoid carcinoma cells. J. Biol. Chem. 273, 31860-31866 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 31860-31866
    • van der Vliet, A.1    Hristova, M.2    Cross, C.E.3    Eiserich, J.P.4    Goldkorn, T.5
  • 67
    • 23644439601 scopus 로고    scopus 로고
    • Potential role of nitration and oxidation reactions in the effects of peroxynitrite on the function of β-adrenoceptor sub-types in the rat
    • Lewis, S. J., Hoque, A., Walton, T. M. & Kooy, N. W. Potential role of nitration and oxidation reactions in the effects of peroxynitrite on the function of β-adrenoceptor sub-types in the rat. Eur. J. Pharmacol. 518, 187-194 (2005).
    • (2005) Eur. J. Pharmacol , vol.518 , pp. 187-194
    • Lewis, S.J.1    Hoque, A.2    Walton, T.M.3    Kooy, N.W.4
  • 68
    • 0037077383 scopus 로고    scopus 로고
    • Nitration of PPARγ inhibits ligand-dependent translocation into the nucleus in a macrophage-like cell line, RAW 264
    • Shibuya, A. et al. Nitration of PPARγ inhibits ligand-dependent translocation into the nucleus in a macrophage-like cell line, RAW 264. FEBS Lett. 525, 43-47 (2002).
    • (2002) FEBS Lett , vol.525 , pp. 43-47
    • Shibuya, A.1
  • 69
  • 70
    • 3042841983 scopus 로고    scopus 로고
    • Reduction of insulin-stimulated glucose uptake by peroxynitrite is concurrent with tyrosine nitration of insulin receptor substrate-1
    • Nomiyama, T. et al. Reduction of insulin-stimulated glucose uptake by peroxynitrite is concurrent with tyrosine nitration of insulin receptor substrate-1. Biochem. Biophys. Res. Commun. 320, 639-647 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.320 , pp. 639-647
    • Nomiyama, T.1
  • 71
    • 33645806282 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite of R21 ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • Clavreul, N. et al. S-glutathiolation by peroxynitrite of R21 ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J. 20, 518-520 (2006).
    • (2006) FASEB J , vol.20 , pp. 518-520
    • Clavreul, N.1
  • 72
    • 0036392047 scopus 로고    scopus 로고
    • Nitration of PECAM-1 ITIM tyrosines abrogates phosphorylation and SHP-2 binding
    • Newman, D. K. et al. Nitration of PECAM-1 ITIM tyrosines abrogates phosphorylation and SHP-2 binding. Biochem. Biophys. Res. Commun. 296, 1171-1179 (2002).
    • (2002) Biochem. Biophys. Res. Commun , vol.296 , pp. 1171-1179
    • Newman, D.K.1
  • 73
    • 33646703558 scopus 로고    scopus 로고
    • Peroxynitrite induces an alternative NF-κB activation pathway in 18 rat myoblasts
    • Bar-Shai, M. & Reznick, A Z. Peroxynitrite induces an alternative NF-κB activation pathway in 18 rat myoblasts. Antioxid. Redox Signal. 8, 639-652 (2006).
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 639-652
    • Bar-Shai, M.1    Reznick, A.Z.2
  • 74
    • 0343831476 scopus 로고    scopus 로고
    • Peroxynitrite mediates cytokine-induced IL-8 gene expression and production by human leukocytes
    • Zouki, C., Jozsef, L., Ouellet, S., Paquette, Y. & Filep, J. G. Peroxynitrite mediates cytokine-induced IL-8 gene expression and production by human leukocytes. J. Leukoc. Biol. 69, 815-824 (2001).
    • (2001) J. Leukoc. Biol , vol.69 , pp. 815-824
    • Zouki, C.1    Jozsef, L.2    Ouellet, S.3    Paquette, Y.4    Filep, J.G.5
  • 75
    • 0037127223 scopus 로고    scopus 로고
    • Peroxynitrite is an essential component of cytokine production mechanism in human monocytes through modulation of NFκB DNA-binding activity
    • Matata, B. M. & Galinanes, M. Peroxynitrite is an essential component of cytokine production mechanism in human monocytes through modulation of NFκB DNA-binding activity. J. Biol. Chem. 277, 2330-2335 (2001).
    • (2001) J. Biol. Chem , vol.277 , pp. 2330-2335
    • Matata, B.M.1    Galinanes, M.2
  • 76
    • 27144547642 scopus 로고    scopus 로고
    • Peroxynitrite is a potent inhibitor of NFkκB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines
    • Levrand, S. et al. Peroxynitrite is a potent inhibitor of NFkκB activation triggered by inflammatory stimuli in cardiac and endothelial cell lines. J. Biol. Chem. 280, 4878-4887 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 4878-4887
    • Levrand, S.1
  • 77
  • 78
    • 0035875772 scopus 로고    scopus 로고
    • Peroxynitrite activates mitogen-activated protein kinase (MAPK) via a MEK-independent pathway: A role for protein kinase C
    • Bapat, S., Verkleij, A. & Post, J. A Peroxynitrite activates mitogen-activated protein kinase (MAPK) via a MEK-independent pathway: A role for protein kinase C. FEBS Lett. 499, 21-26 (2001).
    • (2001) FEBS Lett , vol.499 , pp. 21-26
    • Bapat, S.1    Verkleij, A.2    Post, J.A.3
  • 79
    • 0035902957 scopus 로고    scopus 로고
    • Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn
    • Mallozzi, C., Di Stasi, A. M. & Minetti, M. Nitrotyrosine mimics phosphotyrosine binding to the SH2 domain of the src family tyrosine kinase lyn. FEBS Lett. 503, 189-195 (2001).
    • (2001) FEBS Lett , vol.503 , pp. 189-195
    • Mallozzi, C.1    Di Stasi, A.M.2    Minetti, M.3
  • 80
    • 0035873825 scopus 로고    scopus 로고
    • Peroxynitrite-dependent activation of src tyrosine kinases lyn and hck in erythrocytes is under mechanistically different pathways of redox control
    • Mallozzi, C., Di Stasi, M. A & Minetti, M. Peroxynitrite-dependent activation of src tyrosine kinases lyn and hck in erythrocytes is under mechanistically different pathways of redox control. Free Radic. Biol. Med. 30, 1108-1117 (2001).
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 1108-1117
    • Mallozzi, C.1    Di Stasi, M.A.2    Minetti, M.3
  • 81
    • 0034626916 scopus 로고    scopus 로고
    • NO activation of TrkB through peroxynitrite
    • Yuen, E. C., Gunther, E. C. & Bothwell, M. NO activation of TrkB through peroxynitrite. Neuroreport 11, 3593-3597 (2000).
    • (2000) Neuroreport , vol.11 , pp. 3593-3597
    • Yuen, E.C.1    Gunther, E.C.2    Bothwell, M.3
  • 82
    • 27544500281 scopus 로고    scopus 로고
    • Peroxynitrite increases VEGF expression in vascular endothelial cells via STAT3
    • Platt, D. H. et al. Peroxynitrite increases VEGF expression in vascular endothelial cells via STAT3. Free Radic. Biol. Med. 39 1353-1361 (2005).
    • (2005) Free Radic. Biol. Med , vol.39 , pp. 1353-1361
    • Platt, D.H.1
  • 83
    • 0034668930 scopus 로고    scopus 로고
    • Peroxynitrite activates the phosphoinositide 3-kinase/ Akt pathway in human skin primary fibroblasts
    • Klotz, L. O., Schieke, S. M., Sies, H. & Holbrook, N. J. Peroxynitrite activates the phosphoinositide 3-kinase/ Akt pathway in human skin primary fibroblasts. Biochem. J. 352, 219-225 (2000).
    • (2000) Biochem. J , vol.352 , pp. 219-225
    • Klotz, L.O.1    Schieke, S.M.2    Sies, H.3    Holbrook, N.J.4
  • 84
    • 33746379949 scopus 로고    scopus 로고
    • Two distinct signaling pathways regulate peroxynitrite-induced apoptosis in PC 12 cells
    • Shacka, J. J. et al. Two distinct signaling pathways regulate peroxynitrite-induced apoptosis in PC 12 cells. Cell Death Differ. 13, 1506-1514 (2006).
    • (2006) Cell Death Differ , vol.13 , pp. 1506-1514
    • Shacka, J.J.1
  • 85
    • 0032514225 scopus 로고    scopus 로고
    • Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury
    • Zingarelli, B., Salzman, A. L. & Szabó, C. Genetic disruption of poly (ADP-ribose) synthetase inhibits the expression of P-selectin and intercellular adhesion molecule-1 in myocardial ischemia/reperfusion injury. Circ. Res. 83, 85-94 (1998).
    • (1998) Circ. Res , vol.83 , pp. 85-94
    • Zingarelli, B.1    Salzman, A.L.2    Szabó, C.3
  • 86
    • 0028003280 scopus 로고
    • Concurrent generation of NO and superoxide damages surfactant protein
    • Haddad, I. Y. et al. Concurrent generation of NO and superoxide damages surfactant protein Am. J. Physiol. 267, L242-L249 (1994).
    • (1994) Am. J. Physiol , vol.267
    • Haddad, I.Y.1
  • 87
    • 0025874048 scopus 로고    scopus 로고
    • Radi, R., Beckman, J. S., Bush, K. M. & Freeman, B. A. Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and NO. Arch. Biochem. Biophys. 288, 481-487 (1991).
    • Radi, R., Beckman, J. S., Bush, K. M. & Freeman, B. A. Peroxynitrite-induced membrane lipid peroxidation: The cytotoxic potential of superoxide and NO. Arch. Biochem. Biophys. 288, 481-487 (1991).
  • 89
    • 0030000690 scopus 로고    scopus 로고
    • DNA strand breakage, activation of poly-ADP ribosyl synthetase, and cellular energy depletion are involved in the cytotoxicity in macrophages and smooth muscle cells exposed to peroxynitrite
    • Szabó, C., Zingarelli, B., O'Connor, M. & Salzman, A. L. DNA strand breakage, activation of poly-ADP ribosyl synthetase, and cellular energy depletion are involved in the cytotoxicity in macrophages and smooth muscle cells exposed to peroxynitrite. Proc. Natl Acad. Sci. USA 93, 1753-1758 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1753-1758
    • Szabó, C.1    Zingarelli, B.2    O'Connor, M.3    Salzman, A.L.4
  • 90
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by NO, peroxynitrite and S-nitrosothiols
    • Brown, G. C. & Borutaite, V. Inhibition of mitochondrial respiratory complex I by NO, peroxynitrite and S-nitrosothiols. Biochim. Biophys. Acta 1658, 44-49 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 91
    • 11344250253 scopus 로고    scopus 로고
    • Nitroxia: The pathological consequence of dysfunction in the NO-cytochrome c oxidase signaling pathway
    • Shiva, S. et al. Nitroxia: The pathological consequence of dysfunction in the NO-cytochrome c oxidase signaling pathway. Free Radic. Biol. Med. 38, 297-306 (2005).
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 297-306
    • Shiva, S.1
  • 92
    • 0037432615 scopus 로고    scopus 로고
    • Multiple pathways of peroxynitrite cytotoxicity
    • Szabó C. Multiple pathways of peroxynitrite cytotoxicity. Toxicol. Lett. 140-141, 105-112 (2003).
    • (2003) Toxicol. Lett , vol.140-141 , pp. 105-112
    • Szabó, C.1
  • 94
    • 34547707096 scopus 로고    scopus 로고
    • Quijano, C., Cassina, A., Castro, L., Rodriguez, M. & Raid, R. in Nitric Oxide, Cell Signaling and Gene Expression (eds Lamas, S. & Cadenas, E.) (CRC, Boca Raton, 2005).
    • Quijano, C., Cassina, A., Castro, L., Rodriguez, M. & Raid, R. in Nitric Oxide, Cell Signaling and Gene Expression (eds Lamas, S. & Cadenas, E.) (CRC, Boca Raton, 2005).
  • 96
    • 31544458671 scopus 로고    scopus 로고
    • Mitochondrial NO and reactive nitrogen species production: Does mtNOS exist?
    • Lacza, Z. et al. Mitochondrial NO and reactive nitrogen species production: Does mtNOS exist? Nitric Oxide 14, 162-168 (2006).
    • (2006) Nitric Oxide , vol.14 , pp. 162-168
    • Lacza, Z.1
  • 97
    • 33644783713 scopus 로고    scopus 로고
    • Mitochondrial produce reactive nitrogen species via an arginine-independent pathway
    • Lacza, Z. et al. Mitochondrial produce reactive nitrogen species via an arginine-independent pathway. Free Radic. Res. 40, 369-378 (2006).
    • (2006) Free Radic. Res , vol.40 , pp. 369-378
    • Lacza, Z.1
  • 98
    • 0028275459 scopus 로고
    • Inhibition of mitochondrial electron transport by peroxynitrite
    • Radi, R., Rodriguez, M., Castro, L. & Telleri, R. Inhibition of mitochondrial electron transport by peroxynitrite. Arch. Biochem. Biophys. 308, 89-95 (1994).
    • (1994) Arch. Biochem. Biophys , vol.308 , pp. 89-95
    • Radi, R.1    Rodriguez, M.2    Castro, L.3    Telleri, R.4
  • 99
    • 0035477926 scopus 로고    scopus 로고
    • NO inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation
    • Riobo, N. A. et al. NO inhibits mitochondrial NADH: Ubiquinone reductase activity through peroxynitrite formation. Biochem. J. 359, 139-145 (2001).
    • (2001) Biochem. J , vol.359 , pp. 139-145
    • Riobo, N.A.1
  • 100
    • 0035101487 scopus 로고    scopus 로고
    • Peroxynitrite-mediated mitochondrial dysfunction
    • Boczkowski, J. et al. Peroxynitrite-mediated mitochondrial dysfunction. Biol. Signals Recept. 10, 66-80 (2001).
    • (2001) Biol. Signals Recept , vol.10 , pp. 66-80
    • Boczkowski, J.1
  • 101
    • 0034647729 scopus 로고    scopus 로고
    • Cytochrome c nitration by peroxynitrite
    • Cassina, A. M. et al. Cytochrome c nitration by peroxynitrite. J. Biol. Chem. 275, 21409-21415 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 21409-21415
    • Cassina, A.M.1
  • 102
    • 20144370272 scopus 로고    scopus 로고
    • Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite
    • Batthyany, C. et al. Time course and site(s) of cytochrome c tyrosine nitration by peroxynitrite. Biochemistry 44, 8038-8046 (2005).
    • (2005) Biochemistry , vol.44 , pp. 8038-8046
    • Batthyany, C.1
  • 103
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • Giulivi, C., Poderoso, J. J. & Boveris, A. Production of nitric oxide by mitochondria. J. Biol. Chem. 273, 11038-11043 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 104
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • MacMillan-Crow, L. A. et al. Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc. Natl Acad. Sci. USA, 93, 11853-11858 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1
  • 105
    • 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., Taka, H., Fujimura, T. & Murayama, K. Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. J. Biol. Chem. 273, 14085-14089 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 14085-14089
    • Yamakura, F.1    Taka, H.2    Fujimura, T.3    Murayama, K.4
  • 106
    • 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, 11631-11638 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 11631-11638
    • Quijano, C.1
  • 107
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • Virag, L. & Szabó. C. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 54, 375-429 (2002).
    • (2002) Pharmacol. Rev , vol.54 , pp. 375-429
    • Virag, L.1    Szabó, C.2
  • 108
    • 18944390248 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
    • Jagtap, P. & Szabó, C. Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors. Nature Rev. Drug Discov. 4, 421-440 (2005).
    • (2005) Nature Rev. Drug Discov , vol.4 , pp. 421-440
    • Jagtap, P.1    Szabó, C.2
  • 109
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos, J. P., Heales. S. J., Land, J. M. & Clark, J. B. Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64, 1965-1972 (1995).
    • (1995) J. Neurochem , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.2    Land, J.M.3    Clark, J.B.4
  • 110
    • 0028988038 scopus 로고
    • Endogenous peroxynitrite is involved in the inhibition of cellular respiration in immuno-stimulated J774.2 macrophages
    • Szabó, C. & Salzman, A. L. Endogenous peroxynitrite is involved in the inhibition of cellular respiration in immuno-stimulated J774.2 macrophages. Biochem. Biophys. Res. Comm. 209, 739-743 (1995).
    • (1995) Biochem. Biophys. Res. Comm , vol.209 , pp. 739-743
    • Szabó, C.1    Salzman, A.L.2
  • 111
    • 0029934194 scopus 로고    scopus 로고
    • Role of poly-ADP ribosyltransferase activation in the vascular contractile and energetic failure elicited by exogenous and endogenous NO and peroxynitrite
    • Szabó, C., Zingarelli, B. & Salzman, A. L. Role of poly-ADP ribosyltransferase activation in the vascular contractile and energetic failure elicited by exogenous and endogenous NO and peroxynitrite. Circ. Res. 78, 1051-1063 (1996).
    • (1996) Circ. Res , vol.78 , pp. 1051-1063
    • Szabó, C.1    Zingarelli, B.2    Salzman, A.L.3
  • 112
    • 22844446527 scopus 로고    scopus 로고
    • + ATPase activity is inhibited in cultured intestinal epithelial cells by endotoxin or
    • + ATPase activity is inhibited in cultured intestinal epithelial cells by endotoxin or NO. Int. J. Mol. Med. 15, 871-877 (2005).
    • (2005) Int. J. Mol. Med , vol.15 , pp. 871-877
    • Suzuki, Y.1
  • 113
    • 33745611162 scopus 로고    scopus 로고
    • Endogenously nitrated proteins in mouse brain: Links to neurodegenerative disease
    • Sacksteder C. A. et al. Endogenously nitrated proteins in mouse brain: Links to neurodegenerative disease. Biochemistry 45, 8009-8022 (2006).
    • (2006) Biochemistry , vol.45 , pp. 8009-8022
    • Sacksteder, C.A.1
  • 114
    • 19944431482 scopus 로고    scopus 로고
    • Septic diaphragmatic dysfunction is prevented by Mn(III)porphyrin therapy and inducible NO synthase inhibition
    • Nin, N. et al. Septic diaphragmatic dysfunction is prevented by Mn(III)porphyrin therapy and inducible NO synthase inhibition. Int. Care Med. 30, 2271-2278 (2004).
    • (2004) Int. Care Med , vol.30 , pp. 2271-2278
    • Nin, N.1
  • 115
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher, P. Beckman, J. S. & Liaudet, L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87, 315-424 (2007).
    • (2007) Physiol. Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 116
    • 0037177860 scopus 로고    scopus 로고
    • Nitric oxide (NO) induces nitration of protein kinase C epsilon (PKCε), facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: A novel mechanism of no-triggered activation of PKCε
    • Balafanova, Z. et al. Nitric oxide (NO) induces nitration of protein kinase C epsilon (PKCε), facilitating PKCε translocation via enhanced PKCε-RACK2 interactions: A novel mechanism of no-triggered activation of PKCε. J Biol. Chem. 277, 15021-15027 (2002).
    • (2002) J Biol. Chem , vol.277 , pp. 15021-15027
    • Balafanova, Z.1
  • 117
    • 33750361150 scopus 로고    scopus 로고
    • Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons
    • Pehar, M. et al. Peroxynitrite transforms nerve growth factor into an apoptotic factor for motor neurons, Free Radic. Biol. Med. 41, 1632-1644 (2006).
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 1632-1644
    • Pehar, M.1
  • 118
    • 0036712607 scopus 로고    scopus 로고
    • Inducible NO synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: Implications for enzymic activity
    • Lanone, S. et al. Inducible NO synthase (NOS2) expressed in septic patients is nitrated on selected tyrosine residues: Implications for enzymic activity. Biochem. J. 366, 399-404 (2002).
    • (2002) Biochem. J , vol.366 , pp. 399-404
    • Lanone, S.1
  • 119
    • 0035221276 scopus 로고    scopus 로고
    • Peroxynitrite induces integirin-dependent adhesion of human neutrophils to endotheliall cells via activation of the Raf-1/MEK/Erk pathway
    • Zouki, C., Zhang, S. L., Chan, J. S. & Filep, J. G. Peroxynitrite induces integirin-dependent adhesion of human neutrophils to endotheliall cells via activation of the Raf-1/MEK/Erk pathway. FASEB J. 15, 25-27 (2001).
    • (2001) FASEB J , vol.15 , pp. 25-27
    • Zouki, C.1    Zhang, S.L.2    Chan, J.S.3    Filep, J.G.4
  • 120
    • 0030475604 scopus 로고    scopus 로고
    • Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis
    • Landino, L. M., Crews, B. C., Timmons, M. D., Morrow, J. D. & Marnett. L. J. Peroxynitrite, the coupling product of nitric oxide and superoxide, activates prostaglandin biosynthesis. Proc. Natl Acad. Sci. USA 93, 15069-15074 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 15069-15074
    • Landino, L.M.1    Crews, B.C.2    Timmons, M.D.3    Morrow, J.D.4    Marnett, L.J.5
  • 121
    • 33847649954 scopus 로고    scopus 로고
    • Interactions between nitric oxide and peroxynitrite during prostaglandin endoperoxide H synthase-1 catalysis: A free radical mechanism of inactivation
    • Trostchansky, A. et al. Interactions between nitric oxide and peroxynitrite during prostaglandin endoperoxide H synthase-1 catalysis: a free radical mechanism of inactivation. Free Radic. Biol. Med. 42, 1029-1038 (2007).
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 1029-1038
    • Trostchansky, A.1
  • 122
    • 0842308109 scopus 로고    scopus 로고
    • Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: Role of tyrosine nitration
    • Ito, K., Hanazawa, T., Tomita, K., Barnes, P. J. & Adcock, I. M. Oxidative stress reduces histone deacetylase 2 activity and enhances IL-8 gene expression: Role of tyrosine nitration. Biochem. Biophys. Res. Commun. 315, 240-245 (2004).
    • (2004) Biochem. Biophys. Res. Commun , vol.315 , pp. 240-245
    • Ito, K.1    Hanazawa, T.2    Tomita, K.3    Barnes, P.J.4    Adcock, I.M.5
  • 123
    • 0035021429 scopus 로고    scopus 로고
    • Mechanisms of cell signaling by NO and peroxynitrite: From mitochondria to MAP kinases
    • Levonen, A. L. et al. Mechanisms of cell signaling by NO and peroxynitrite: From mitochondria to MAP kinases. Antioxid. Redox Signal. 3, 215-229 (2001).
    • (2001) Antioxid. Redox Signal , vol.3 , pp. 215-229
    • Levonen, A.L.1
  • 124
    • 0345505248 scopus 로고    scopus 로고
    • Crucial role of local peroxynitrite formation in neutrophil-induced endothelial cell activation
    • Sohn, H. Y. et al. Crucial role of local peroxynitrite formation in neutrophil-induced endothelial cell activation. Cardiovasc. Res. 57, 804-815 (2003).
    • (2003) Cardiovasc. Res , vol.57 , pp. 804-815
    • Sohn, H.Y.1
  • 125
    • 0032561404 scopus 로고    scopus 로고
    • Peroxynitrite oxidises catechols to o-quinones
    • Kerry, N. & Rice-Evans, C. Peroxynitrite oxidises catechols to o-quinones. FEBS Lett 437, 167-171 (1998).
    • (1998) FEBS Lett , vol.437 , pp. 167-171
    • Kerry, N.1    Rice-Evans, C.2
  • 126
    • 0034662864 scopus 로고    scopus 로고
    • Inactivation of catecholamines by superoxide gives new insights on the pathogenesis of septic shock
    • Macarthur, H., Westfall, T. C., Riley, D. P., Misko, T. P. & Salvemini, D. Inactivation of catecholamines by superoxide gives new insights on the pathogenesis of septic shock. Proc. Natl Acad. Sci. USA 97 9753-9758 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9753-9758
    • Macarthur, H.1    Westfall, T.C.2    Riley, D.P.3    Misko, T.P.4    Salvemini, D.5
  • 127
    • 33646589634 scopus 로고    scopus 로고
    • Subcellular localization of tyrosine-nitrated proteins is dictated by reactive oxygen species generating enzymes and by proximity to nitric oxide synthase
    • Heijnen, H. F. G. et al. Subcellular localization of tyrosine-nitrated proteins is dictated by reactive oxygen species generating enzymes and by proximity to nitric oxide synthase. Free Radic. Biol. Med. 40, 1903-1913 (2006).
    • (2006) Free Radic. Biol. Med , vol.40 , pp. 1903-1913
    • Heijnen, H.F.G.1
  • 128
    • 0038265141 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase and intracellular protein tyrosine nitration in vascular smooth muscle cells: Role of reactive oxygen species
    • Fries, D. M. et al. Expression of inducible nitric oxide synthase and intracellular protein tyrosine nitration in vascular smooth muscle cells: Role of reactive oxygen species. J. Biol. Chem. 278, 22901-22907 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 22901-22907
    • Fries, D.M.1
  • 129
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective α-synuclein nitration in synucleinopathy lesions
    • Giasson, B. I. et al., Oxidative damage linked to neurodegeneration by selective α-synuclein nitration in synucleinopathy lesions, Science 290, 985-989 (2000).
    • (2000) Science , vol.290 , pp. 985-989
    • Giasson, B.I.1
  • 130
    • 0038107581 scopus 로고    scopus 로고
    • MHC class II-restricted peptides containing the inflammation-associated marker 3-nitrotyrosine evade central tolerance and elicit a robust cell-mediated immune response
    • Bimboim, H. C., Lemay, A. M., Lam, D. K., Goldstein, R. & Webb. J. R. MHC class II-restricted peptides containing the inflammation-associated marker 3-nitrotyrosine evade central tolerance and elicit a robust cell-mediated immune response. J. Immunol. 171, 528-532 (2003).
    • (2003) J. Immunol , vol.171 , pp. 528-532
    • Bimboim, H.C.1    Lemay, A.M.2    Lam, D.K.3    Goldstein, R.4    Webb, J.R.5
  • 131
    • 20344391931 scopus 로고    scopus 로고
    • Activated antigen-presenting cells select and present chemically modified peptides recognized by unique CD4 T cells
    • Herzog, J., Maekawa, Y., Cirrito, T. P., Illian, B. S. & Unanue, E. R. Activated antigen-presenting cells select and present chemically modified peptides recognized by unique CD4 T cells. Proc. Natl Acad. Sci. USA 102, 7928-7933 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 7928-7933
    • Herzog, J.1    Maekawa, Y.2    Cirrito, T.P.3    Illian, B.S.4    Unanue, E.R.5
  • 132
    • 33751288381 scopus 로고    scopus 로고
    • Superoxide, peroxynitrite and oxidative/nitrative stress in inflammation
    • Salvemini, D., Doyle, T. M. & Cuzzocrea, S. Superoxide, peroxynitrite and oxidative/nitrative stress in inflammation. Biochem. Soc. Trans. 34, 965-970 (2006).
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 965-970
    • Salvemini, D.1    Doyle, T.M.2    Cuzzocrea, S.3
  • 133
    • 33745074718 scopus 로고    scopus 로고
    • Biological time-dependent difference in effect of peroxynitrite demonstrated by the mouse hot plate pain model
    • Altug, S. et al. Biological time-dependent difference in effect of peroxynitrite demonstrated by the mouse hot plate pain model. Chronobiol. Int. 23, 583-591 (2006).
    • (2006) Chronobiol. Int , vol.23 , pp. 583-591
    • Altug, S.1
  • 134
    • 33748704531 scopus 로고    scopus 로고
    • Tempol, a membrane-permeable radical scavenger, attenuates peroxynitrite- and superoxide anion-enhanced carrageenan-induced paw edema and hyperalgesia: A key role for superoxide anion
    • Khattab, M. M. Tempol, a membrane-permeable radical scavenger, attenuates peroxynitrite- and superoxide anion-enhanced carrageenan-induced paw edema and hyperalgesia: A key role for superoxide anion. Eur. J. Pharmacol. 548, 167-173 (2006).
    • (2006) Eur. J. Pharmacol , vol.548 , pp. 167-173
    • Khattab, M.M.1
  • 135
    • 33846131993 scopus 로고    scopus 로고
    • Neutrophils-derived peroxynitrite contributes to acute hyperalgesia and cell influx in zymosan arthritis
    • Bezerra, M. M. et al. Neutrophils-derived peroxynitrite contributes to acute hyperalgesia and cell influx in zymosan arthritis. Nounyn Schmiedebergs Arch. Pharmacol. 374, 265-273 (2007).
    • (2007) Nounyn Schmiedebergs Arch. Pharmacol , vol.374 , pp. 265-273
    • Bezerra, M.M.1
  • 136
    • 2442648975 scopus 로고    scopus 로고
    • A newly identified role for superoxide in inflammatory pain
    • Wang, Z. Q. et al. A newly identified role for superoxide in inflammatory pain. J. Pharmacol. Exp. Ther. 309, 869-878 (2004).
    • (2004) J. Pharmacol. Exp. Ther , vol.309 , pp. 869-878
    • Wang, Z.Q.1
  • 137
    • 0035884848 scopus 로고    scopus 로고
    • The central nervous system inflammatory response to neurotropic virus infection is peroxynitrite dependent
    • Hooper, D. C. et al. The central nervous system inflammatory response to neurotropic virus infection is peroxynitrite dependent. J. Immunol. 167, 3470-3477 (2001).
    • (2001) J. Immunol , vol.167 , pp. 3470-3477
    • Hooper, D.C.1
  • 138
    • 4143085003 scopus 로고    scopus 로고
    • Peroxynitrite inhibition of Coxsackievirus infection by prevention of viral RNA entry
    • Padalko, E. Peroxynitrite inhibition of Coxsackievirus infection by prevention of viral RNA entry. Proc. Natl Acad. Sci. USA 101 11731-11736 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11731-11736
    • Padalko, E.1
  • 139
    • 0344643456 scopus 로고    scopus 로고
    • Peroxynitrite-induced cytotoxicity: Mechanism and opportunities for intervention
    • Virag, L, Szabó, E., Gergely, P. & Szabó, C. Peroxynitrite-induced cytotoxicity: Mechanism and opportunities for intervention. Toxicol. Lett. 140-141, 113-124 (2003).
    • (2003) Toxicol. Lett , vol.140-141 , pp. 113-124
    • Virag, L.1    Szabó, E.2    Gergely, P.3    Szabó, C.4
  • 140
    • 0032403857 scopus 로고    scopus 로고
    • Crucial role of apopain in the peroxynitrite-induced apoptotic DNA fragmentation
    • Virag, L, Marmer, D. J. & Szabó, C. Crucial role of apopain in the peroxynitrite-induced apoptotic DNA fragmentation. Free Radic. Biol. Med. 25, 1075-1082 (1998).
    • (1998) Free Radic. Biol. Med , vol.25 , pp. 1075-1082
    • Virag, L.1    Marmer, D.J.2    Szabó, C.3
  • 141
    • 0033852205 scopus 로고    scopus 로고
    • Peroxynitrite-induced apoptosis involves activation of multiple caspases in HL-60 cells
    • Zhuang, S. & Simon, G. Peroxynitrite-induced apoptosis involves activation of multiple caspases in HL-60 cells. Am. J. Physiol. Cell Physiol. 279, C341-C351 (2000).
    • (2000) Am. J. Physiol. Cell Physiol , vol.279
    • Zhuang, S.1    Simon, G.2
  • 142
    • 33745769721 scopus 로고    scopus 로고
    • NO and peroxynitrite induce cellular death in bovine chromaffin cells: Evidence for a mixed necrotic and apoptotic mechanism with caspases activation
    • Vicente, S. et al. NO and peroxynitrite induce cellular death in bovine chromaffin cells: Evidence for a mixed necrotic and apoptotic mechanism with caspases activation. J. Neurosci. Res. 84, 78-96 (2006).
    • (2006) J. Neurosci. Res , vol.84 , pp. 78-96
    • Vicente, S.1
  • 143
    • 0032929052 scopus 로고    scopus 로고
    • 2+ and peroxynitrite and is responsible for Ca(2 +)-induced inhibition of substrate oxidation
    • 2+ and peroxynitrite and is responsible for Ca(2 +)-induced inhibition of substrate oxidation. Biochim. Biophys. Acta 1453, 41-48 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1453 , pp. 41-48
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 144
    • 0031740461 scopus 로고    scopus 로고
    • Richter, C., Schweizer, M. & Ghafourifar P. Mitochondria, NO, and peroxynitrite. Methods Enzymol. 301. 381-393 (1999).
    • Richter, C., Schweizer, M. & Ghafourifar P. Mitochondria, NO, and peroxynitrite. Methods Enzymol. 301. 381-393 (1999).
  • 145
    • 0031890108 scopus 로고    scopus 로고
    • Nitric oxide and superoxide contribute to motor neuron apoptosis induced by trophic factor deprivation
    • Estevez, E. et al. Nitric oxide and superoxide contribute to motor neuron apoptosis induced by trophic factor deprivation. J. Neurosci. 18, 923-931 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 923-931
    • Estevez, E.1
  • 146
    • 0032833924 scopus 로고    scopus 로고
    • Requirement of intracellular calcium mobilization for peroxynitrite-induced poly(ADP-ribose) synthetase activation and cytotoxicity
    • Virag, L. et al. Requirement of intracellular calcium mobilization for peroxynitrite-induced poly(ADP-ribose) synthetase activation and cytotoxicity. Mol. Pharmacol. 56, 824-833 (1999).
    • (1999) Mol. Pharmacol , vol.56 , pp. 824-833
    • Virag, L.1
  • 147
    • 33644790277 scopus 로고    scopus 로고
    • Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: Implications in atherogenesis
    • Dickhout, J. G. et al. Peroxynitrite causes endoplasmic reticulum stress and apoptosis in human vascular endothelium: Implications in atherogenesis. Arterioscler. Thromb. Vasc. Biol. 25, 2623-2629 (2005).
    • (2005) Arterioscler. Thromb. Vasc. Biol , vol.25 , pp. 2623-2629
    • Dickhout, J.G.1
  • 148
    • 20744456318 scopus 로고    scopus 로고
    • 2+ mobilization and aggregation in platelets from type 2 diabetic patients
    • 2+ mobilization and aggregation in platelets from type 2 diabetic patients. Biochem. Biophys. Res. Commun. 333, 794-802 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.333 , pp. 794-802
    • Redondo, P.C.1
  • 149
    • 9444275970 scopus 로고    scopus 로고
    • Peroxynitrite mediates calcium-dependent mitochondrial dysfunction and cell death via activation of calpains
    • Whiteman, M. et al. Peroxynitrite mediates calcium-dependent mitochondrial dysfunction and cell death via activation of calpains. FASEB J. 18, 1395-1397 (2004).
    • (2004) FASEB J , vol.18 , pp. 1395-1397
    • Whiteman, M.1
  • 150
    • 26644452758 scopus 로고    scopus 로고
    • Survival pathways triggered by peroxynitrite in cells belonging to the monocyte/macrophage lineage
    • Cantoni, O. et al. Survival pathways triggered by peroxynitrite in cells belonging to the monocyte/macrophage lineage. Comp. Biochem. Physiol. A. Mol. Integr. Physiol. 14, 118-123 (2005).
    • (2005) Comp. Biochem. Physiol. A. Mol. Integr. Physiol , vol.14 , pp. 118-123
    • Cantoni, O.1
  • 151
    • 20244364788 scopus 로고    scopus 로고
    • Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite
    • Zhang, X. et al. Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite. J. Neurochem. 82, 181-191 (2002).
    • (2002) J. Neurochem , vol.82 , pp. 181-191
    • Zhang, X.1
  • 152
    • 10244241834 scopus 로고    scopus 로고
    • Deadly conversations: Nuclear-mitochondrial cross-talk
    • Dawson, V. L. & Dawson, T. M. Deadly conversations: nuclear-mitochondrial cross-talk. J. Bioenerg. Biomembr. 36, 287-294 (2004).
    • (2004) J. Bioenerg. Biomembr , vol.36 , pp. 287-294
    • Dawson, V.L.1    Dawson, T.M.2
  • 153
    • 33645730486 scopus 로고    scopus 로고
    • Activation of the peroxynitrite-poly[adenosine diphosphate-ribose] polymerase pathway during neointima proliferation: A new target to prevent restenosis after endarterectomy
    • Beller, C. J. et al. Activation of the peroxynitrite-poly[adenosine diphosphate-ribose] polymerase pathway during neointima proliferation: A new target to prevent restenosis after endarterectomy. J. Vasc. Surg. 43, 824-830 (2006).
    • (2006) J. Vasc. Surg , vol.43 , pp. 824-830
    • Beller, C.J.1
  • 154
    • 33749035991 scopus 로고    scopus 로고
    • Nitrative inactivation of thioredoxin-1 and its role in postischemic myocardial apoptosis
    • Tao, L. et al. Nitrative inactivation of thioredoxin-1 and its role in postischemic myocardial apoptosis. Circulation 114, 1395-1402 (2006).
    • (2006) Circulation , vol.114 , pp. 1395-1402
    • Tao, L.1
  • 155
    • 0036724929 scopus 로고    scopus 로고
    • HMGB1 B box increases the permeability of Caco-2 enterocytic monolayers and impairs intestinal barrier function in mice
    • Sappington, P. L. et al. HMGB1 B box increases the permeability of Caco-2 enterocytic monolayers and impairs intestinal barrier function in mice. Gastroenterology 123, 790-802 (2002).
    • (2002) Gastroenterology , vol.123 , pp. 790-802
    • Sappington, P.L.1
  • 156
    • 33745461107 scopus 로고    scopus 로고
    • High-mobility group box 1 (HMGB 1) protein: Friend and foe
    • Ulloa, L. & Messmer, D. High-mobility group box 1 (HMGB 1) protein: friend and foe. Cytokine Growth Factor Rev. 17, 189-201 (2006).
    • (2006) Cytokine Growth Factor Rev , vol.17 , pp. 189-201
    • Ulloa, L.1    Messmer, D.2
  • 157
    • 24344446907 scopus 로고    scopus 로고
    • Immunological studies on peroxynitrite modified human DNA
    • Dixit, K. & Moinuddin, A. A. Immunological studies on peroxynitrite modified human DNA. Life Sci. 77, 2626-2642 (2005).
    • (2005) Life Sci , vol.77 , pp. 2626-2642
    • Dixit, K.1    Moinuddin, A.A.2
  • 158
    • 18944404651 scopus 로고    scopus 로고
    • Immunogenicity of an inflammation-associated product, tyrosine nitrated self-proteins
    • Ohmori, H. & Kanayama, N. Immunogenicity of an inflammation-associated product, tyrosine nitrated self-proteins. Autoimmun. Rev. 4, 224-229 (2005).
    • (2005) Autoimmun. Rev , vol.4 , pp. 224-229
    • Ohmori, H.1    Kanayama, N.2
  • 160
    • 0034648827 scopus 로고    scopus 로고
    • Peroxynitrite reductase activity of bacterial peroxinedoxins
    • Bryk, R., Griffin, P. & Nathan, C. Peroxynitrite reductase activity of bacterial peroxinedoxins. Nature 407, 211-215 (2000).
    • (2000) Nature , vol.407 , pp. 211-215
    • Bryk, R.1    Griffin, P.2    Nathan, C.3
  • 161
    • 4544264011 scopus 로고    scopus 로고
    • Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols
    • Trujilo, M. et al. Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. J. Biol. Chem. 279, 34175-34182 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 34175-34182
    • Trujilo, M.1
  • 162
    • 3342976149 scopus 로고    scopus 로고
    • Human peroxiredoxin 5 is a peroxynitrite reductase
    • Dubuisson, M. et al. Human peroxiredoxin 5 is a peroxynitrite reductase. FEBS Lett. 571, 161-165 (2004).
    • (2004) FEBS Lett , vol.571 , pp. 161-165
    • Dubuisson, M.1
  • 163
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee, S. G., Chae, H. Z. & Kim, K. Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38, 1543-1552 (2005).
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 165
    • 0036268393 scopus 로고    scopus 로고
    • A reassessment of the peroxynitrite scavenging activity of uric acid
    • Whiteman, M., Ketsawatsakul, U. & Halliwell, B. A reassessment of the peroxynitrite scavenging activity of uric acid. Ann. N. Y. Acad. Sci. 962, 242-259 (2002).
    • (2002) Ann. N. Y. Acad. Sci , vol.962 , pp. 242-259
    • Whiteman, M.1    Ketsawatsakul, U.2    Halliwell, B.3
  • 166
    • 0037058925 scopus 로고    scopus 로고
    • Therapeutic intervention in experimental allergic encephalomyelitis by administration of uric acid precursors
    • Scott, G. S. et al. Therapeutic intervention in experimental allergic encephalomyelitis by administration of uric acid precursors. Proc. Natl Acad. Sci. USA 99, 16303-16308 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16303-16308
    • Scott, G.S.1
  • 167
    • 1042290474 scopus 로고    scopus 로고
    • Triuret: A novel product of peroxynitrite-mediated oxidation of urate
    • Robinson, K. M., Morre, J. T. & Beckman, J. S. Triuret: A novel product of peroxynitrite-mediated oxidation of urate. Arch. Biochem. Biophys. 423, 213-217 (2004).
    • (2004) Arch. Biochem. Biophys , vol.423 , pp. 213-217
    • Robinson, K.M.1    Morre, J.T.2    Beckman, J.S.3
  • 168
    • 14744272784 scopus 로고    scopus 로고
    • Uric acid protects against secondary damage after spinal cord injury
    • Scott, G. S. et al. Uric acid protects against secondary damage after spinal cord injury. Proc. Natl Acad. Sci. USA 102, 3483-3488 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 3483-3488
    • Scott, G.S.1
  • 169
    • 0030938584 scopus 로고    scopus 로고
    • Mercaptoethylguanidine and guanidine inhibitors of nitric-oxide synthase react with peroxynitrite and protect against peroxynitrite-induced oxidative damage
    • Szabó, C. et al. Mercaptoethylguanidine and guanidine inhibitors of nitric-oxide synthase react with peroxynitrite and protect against peroxynitrite-induced oxidative damage. J. Biol. Chem. 272, 9030-9036 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 9030-9036
    • Szabó, C.1
  • 170
    • 0030689044 scopus 로고    scopus 로고
    • Amelioration by mercaptoethylguanidine of the vascular and energetic failure in haemorrhagic shock in the anesthetised rat
    • Zingarelli, B., Ischiropoulos, H., Salzman, A. L. & Szabö, C. Amelioration by mercaptoethylguanidine of the vascular and energetic failure in haemorrhagic shock in the anesthetised rat. Eur. J. Pharmacol. 338, 55-65 (1997).
    • (1997) Eur. J. Pharmacol , vol.338 , pp. 55-65
    • Zingarelli, B.1    Ischiropoulos, H.2    Salzman, A.L.3    Szabö, C.4
  • 171
    • 27844585186 scopus 로고    scopus 로고
    • Mercaptoethylguanidine inhibition of inducible NO synthase and cyclooxygenase-2 expressions induced in rats after fluid-percussion brain injury
    • Moochhala, S.M. et al. Mercaptoethylguanidine inhibition of inducible NO synthase and cyclooxygenase-2 expressions induced in rats after fluid-percussion brain injury. J. Trauma 59, 450-457 (2005).
    • (2005) J. Trauma , vol.59 , pp. 450-457
    • Moochhala, S.M.1
  • 172
    • 0035433378 scopus 로고    scopus 로고
    • Effects of combined selective iNOS inhibition and peroxynitrite blockade during endotoxemia in pigs
    • Ploner, F. et al. Effects of combined selective iNOS inhibition and peroxynitrite blockade during endotoxemia in pigs. Shock 16 130-136 (2001).
    • (2001) Shock , vol.16 , pp. 130-136
    • Ploner, F.1
  • 173
    • 2942601560 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalysts prevent myocardial dysfunction and inflammation in endotoxemic rats
    • Lancel, S. et al. Peroxynitrite decomposition catalysts prevent myocardial dysfunction and inflammation in endotoxemic rats. J. Am. Coll. Cardiol. 43, 2348-2358 (2004).
    • (2004) J. Am. Coll. Cardiol , vol.43 , pp. 2348-2358
    • Lancel, S.1
  • 174
    • 18244415707 scopus 로고    scopus 로고
    • Defenses against peroxynitrite: Selenocompounds and flavonoids
    • Klotz, L. O. & Sies, H. Defenses against peroxynitrite: Selenocompounds and flavonoids. Toxicol. Lett. 140-141, 125-132 (2003).
    • (2003) Toxicol. Lett , vol.140-141 , pp. 125-132
    • Klotz, L.O.1    Sies, H.2
  • 175
    • 0032788469 scopus 로고    scopus 로고
    • Role of peroxynitrite in airway microvascular hyperpermeability during late allergic phase in guinea pigs
    • Sugiura, H. et al. Role of peroxynitrite in airway microvascular hyperpermeability during late allergic phase in guinea pigs. Am. J. Respir. Crit. Care Med. 160, 663-671 (1999).
    • (1999) Am. J. Respir. Crit. Care Med , vol.160 , pp. 663-671
    • Sugiura, H.1
  • 176
    • 0033990512 scopus 로고    scopus 로고
    • Ebselen as a peroxynitrite scavenger in vitro and ex vivo
    • Daiber, A., Zou, M. H., Bachschmid, M. & Ullrich, V. Ebselen as a peroxynitrite scavenger in vitro and ex vivo. Biochem. Pharmacol. 59. 153-160 (2000).
    • (2000) Biochem. Pharmacol , vol.59 , pp. 153-160
    • Daiber, A.1    Zou, M.H.2    Bachschmid, M.3    Ullrich, V.4
  • 177
    • 0035203602 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress in acute renal ischemia
    • Noiri, E. et al. Oxidative and nitrosative stress in acute renal ischemia. Am. J. Physiol. Renol Physiol. 281, F948-F957 (2001).
    • (2001) Am. J. Physiol. Renol Physiol , vol.281
    • Noiri, E.1
  • 178
    • 21644467118 scopus 로고    scopus 로고
    • Endothelial dysfunction as a modifier of angiogenic response in Zucker diabetic fat rat: Amelioration with ebselen
    • Gealekman, O. et al. Endothelial dysfunction as a modifier of angiogenic response in Zucker diabetic fat rat: Amelioration with ebselen. Kidney Int. 66, 2337-2347 (2004).
    • (2004) Kidney Int , vol.66 , pp. 2337-2347
    • Gealekman, O.1
  • 179
    • 0032980390 scopus 로고    scopus 로고
    • Protection against peroxynitrite
    • Arteel, G. E., Briviba, K. & Sies, H. Protection against peroxynitrite. FEBS Lett. 445, 226-230 (1999).
    • (1999) FEBS Lett , vol.445 , pp. 226-230
    • Arteel, G.E.1    Briviba, K.2    Sies, H.3
  • 180
    • 0033994250 scopus 로고    scopus 로고
    • Ebselen: Prospective therapy for cerebral ischaemia
    • Parnham, M. & Sies, H. Ebselen: Prospective therapy for cerebral ischaemia. Expert Opin. Investig. Drugs. 9, 607-619 (2000).
    • (2000) Expert Opin. Investig. Drugs , vol.9 , pp. 607-619
    • Parnham, M.1    Sies, H.2
  • 181
    • 0030834975 scopus 로고    scopus 로고
    • Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase
    • Sies, H., Sharov, V. S., Klotz, L. O. & Briviba, K. Glutathione peroxidase protects against peroxynitrite-mediated oxidations. A new function for selenoproteins as peroxynitrite reductase. J. Biol. Chem. 272. 27812-24817 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 27812-24817
    • Sies, H.1    Sharov, V.S.2    Klotz, L.O.3    Briviba, K.4
  • 182
    • 0031667276 scopus 로고    scopus 로고
    • Protection by selenoprotein P in human plasma against peroxynitrite-mediated oxidation and nitration
    • Arteel, G. E., Mostert, V., Oubrahim, H., Briviba, K., Abel, J. & Sies, H. Protection by selenoprotein P in human plasma against peroxynitrite-mediated oxidation and nitration. Biol. Chem. 379 1201-1205 (1998).
    • (1998) Biol. Chem , vol.379 , pp. 1201-1205
    • Arteel, G.E.1    Mostert, V.2    Oubrahim, H.3    Briviba, K.4    Abel, J.5    Sies, H.6
  • 183
    • 0029809946 scopus 로고    scopus 로고
    • Attenuation of oxidation and nitration reactions of peroxynitrite by selenomethionine, selenocystine and ebselen
    • Briviba, K., Roussyn, I., Sharov, V. S. & Sies, H. Attenuation of oxidation and nitration reactions of peroxynitrite by selenomethionine, selenocystine and ebselen. Biochem. J. 319, 13-15 (1996).
    • (1996) Biochem. J , vol.319 , pp. 13-15
    • Briviba, K.1    Roussyn, I.2    Sharov, V.S.3    Sies, H.4
  • 185
    • 10644266861 scopus 로고    scopus 로고
    • Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation
    • Fernandes, D. C., Medinas, D. B., Alves, M. J. & Augusta, O. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free Radic. Biol. Med. 38, 189-200 (2005).
    • (2005) Free Radic. Biol. Med , vol.38 , pp. 189-200
    • Fernandes, D.C.1    Medinas, D.B.2    Alves, M.J.3    Augusta, O.4
  • 186
    • 0036223560 scopus 로고    scopus 로고
    • Bonini, M. G., Mason, R. P. & Augusto, O. The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperide-1 oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chem. Res. Toxicol. 15. 506-511 (2002).
    • Bonini, M. G., Mason, R. P. & Augusto, O. The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperide-1 oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chem. Res. Toxicol. 15. 506-511 (2002).
  • 187
    • 0035146373 scopus 로고    scopus 로고
    • The stable nitroxide, tempol, attenuates the effects of peroxynitrite and oxygen-derived free radicals
    • Thiemermann, C., McDonald, M. C. & Cuzzocrea, S. The stable nitroxide, tempol, attenuates the effects of peroxynitrite and oxygen-derived free radicals. Crit. Care Med. 29. 223-224 (2001).
    • (2001) Crit. Care Med , vol.29 , pp. 223-224
    • Thiemermann, C.1    McDonald, M.C.2    Cuzzocrea, S.3
  • 188
    • 0034284555 scopus 로고    scopus 로고
    • Effects of tempol, a membrane-permeable radical scavenger, in a gerbil model of brain injury
    • Cuzzocrea, S. et al. Effects of tempol, a membrane-permeable radical scavenger, in a gerbil model of brain injury. Brain Res. 875. 96-106 (2000).
    • (2000) Brain Res , vol.875 , pp. 96-106
    • Cuzzocrea, S.1
  • 189
    • 2942674742 scopus 로고    scopus 로고
    • Tempol, an intracelullar free radical scavenger, reduces liver injury in hepatic ischemia-reperfusion in the rat
    • Sepodes, B. et al. Tempol, an intracelullar free radical scavenger, reduces liver injury in hepatic ischemia-reperfusion in the rat. Transplant Proc. 36, 849-853 (2004).
    • (2004) Transplant Proc , vol.36 , pp. 849-853
    • Sepodes, B.1
  • 190
    • 33646021307 scopus 로고    scopus 로고
    • Cabergoline scavenges peroxynitrite enhanced by L-DOPA therapy in patients with Parkinson's disease
    • Isobe, C. et al. Cabergoline scavenges peroxynitrite enhanced by L-DOPA therapy in patients with Parkinson's disease. Eur. J. Neurol. 13, 346-350 (2006).
    • (2006) Eur. J. Neurol , vol.13 , pp. 346-350
    • Isobe, C.1
  • 191
    • 33645064567 scopus 로고    scopus 로고
    • Acetaminophen attenuates peroxynitrite-activated matrix metalloproteinase-2-mediated troponin I cleavage in the isolated guinea pig myocardium
    • Rork, T. H., Hadzimichalis, N. M., Kappil, M. A & Merrill, G. F. Acetaminophen attenuates peroxynitrite-activated matrix metalloproteinase-2-mediated troponin I cleavage in the isolated guinea pig myocardium. J. Mol. Cell. Cardiol. 40, 553-561 (2006).
    • (2006) J. Mol. Cell. Cardiol , vol.40 , pp. 553-561
    • Rork, T.H.1    Hadzimichalis, N.M.2    Kappil, M.A.3    Merrill, G.F.4
  • 192
    • 33644875667 scopus 로고    scopus 로고
    • Nebivolol reduces nitroxidative stress and restores NO bioavailability in endothelium of black Americans
    • Mason, R. P. Kalinowski, L., Jacob, R. F., Jacoby, A. M. & Malinski, T. Nebivolol reduces nitroxidative stress and restores NO bioavailability in endothelium of black Americans. Circulation 112, 3795-3801 (2005).
    • (2005) Circulation , vol.112 , pp. 3795-3801
    • Mason, R.P.1    Kalinowski, L.2    Jacob, R.F.3    Jacoby, A.M.4    Malinski, T.5
  • 193
    • 27844580204 scopus 로고    scopus 로고
    • Hydralazine is a powerful inhibitor of peroxynitrite formation as a possible explanation for its beneficial effects on prognosis in patients with congestive heart failure
    • Dalber, A. et al. Hydralazine is a powerful inhibitor of peroxynitrite formation as a possible explanation for its beneficial effects on prognosis in patients with congestive heart failure. Biochem. Biophys. Res. Commun. 338, 1865-1874 (2005).
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 1865-1874
    • Dalber, A.1
  • 194
    • 23144466673 scopus 로고    scopus 로고
    • Pindolol is a potent scavenger of reactive nitrogen species
    • Fernandes, E., Gomes, A., Costa, D. & Lima, J. L. Pindolol is a potent scavenger of reactive nitrogen species. Life Sci. 77, 1983-1992 (2005).
    • (2005) Life Sci , vol.77 , pp. 1983-1992
    • Fernandes, E.1    Gomes, A.2    Costa, D.3    Lima, J.L.4
  • 195
    • 0034802381 scopus 로고    scopus 로고
    • Peroxynitrite-induced nitrotyrosination of proteins is blocked by direct 5-lipoxygenase inhibitor zileuton
    • Coffey, M. J., Phare, S. M. & Peters-Golden, M. Peroxynitrite-induced nitrotyrosination of proteins is blocked by direct 5-lipoxygenase inhibitor zileuton. J. Pharmacol. Exp. Ther. 299. 198-203 (2001).
    • (2001) J. Pharmacol. Exp. Ther , vol.299 , pp. 198-203
    • Coffey, M.J.1    Phare, S.M.2    Peters-Golden, M.3
  • 196
    • 0034955224 scopus 로고    scopus 로고
    • Effects of chronic N-acetylcysteine treatment on the actions of peroxynitrite on aortic vascular reactivity in hypertensive rats
    • Cabassi, A. et al. Effects of chronic N-acetylcysteine treatment on the actions of peroxynitrite on aortic vascular reactivity in hypertensive rats. J. Hypertens. 19, 1233-1244 (2001).
    • (2001) J. Hypertens , vol.19 , pp. 1233-1244
    • Cabassi, A.1
  • 197
    • 0028178450 scopus 로고
    • Structure activity relationships of peroxynitrite scavengers an approach to NO neurotoxicity
    • Althaus, J. S. et al. Structure activity relationships of peroxynitrite scavengers an approach to NO neurotoxicity. Res Commun. Chem. Pathol. Pharmacol. 83, 243-254 (1994).
    • (1994) Res Commun. Chem. Pathol. Pharmacol , vol.83 , pp. 243-254
    • Althaus, J.S.1
  • 198
    • 14944350244 scopus 로고    scopus 로고
    • Selley, M. L. Simvastatin prevents 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced striatal dopamine depletion and protein tyrosine nitration in mice. Brain Res. 1037, 1-6 (2005).
    • Selley, M. L. Simvastatin prevents 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced striatal dopamine depletion and protein tyrosine nitration in mice. Brain Res. 1037, 1-6 (2005).
  • 199
    • 13444292146 scopus 로고    scopus 로고
    • The radical scavenger edaravone prevents oxidative neurotoxicity induced by peroxynitrite and activated microglia
    • Banno, M. et al. The radical scavenger edaravone prevents oxidative neurotoxicity induced by peroxynitrite and activated microglia. Neuropharmacology 48, 283-290 (2005).
    • (2005) Neuropharmacology , vol.48 , pp. 283-290
    • Banno, M.1
  • 200
    • 9444297877 scopus 로고    scopus 로고
    • Propofol attenuates peroxynitrite-mediated DNA damage and apoptosis in cultured astrocytes: An alternative protective mechanism
    • Acquaviva, R. et al. Propofol attenuates peroxynitrite-mediated DNA damage and apoptosis in cultured astrocytes: An alternative protective mechanism. Anesthesiology 101, 1363-1371 (2004).
    • (2004) Anesthesiology , vol.101 , pp. 1363-1371
    • Acquaviva, R.1
  • 201
    • 20444456654 scopus 로고    scopus 로고
    • Peroxynitrite-derived carbonate and nitrogen dioxide radicals readily react with lipoic and dihydrolipoic acid
    • Trujillo, M. et al. Peroxynitrite-derived carbonate and nitrogen dioxide radicals readily react with lipoic and dihydrolipoic acid. Free Radic. Biol. Med. 39, 279-288 (2005).
    • (2005) Free Radic. Biol. Med , vol.39 , pp. 279-288
    • Trujillo, M.1
  • 202
    • 0036203428 scopus 로고    scopus 로고
    • Effect of R-(-)-deprenyl and harmaline on dopamine- and peroxynitrite-induced membrane permeability transition in brain mitochondria
    • Lee, C. S. et al. Effect of R-(-)-deprenyl and harmaline on dopamine- and peroxynitrite-induced membrane permeability transition in brain mitochondria. Neurochem. Res. 27, 215-224 (2002).
    • (2002) Neurochem. Res , vol.27 , pp. 215-224
    • Lee, C.S.1
  • 203
    • 0036206323 scopus 로고    scopus 로고
    • The anti-Parkinson drug, rasagiline, prevents apoptotic DNA damage induced by peroxynitrite in human dopaminergic neuroblastoma SH-SY5Y cells
    • Maruyama, W., Takahashi, T., Youdim, M. & Naoi, M. The anti-Parkinson drug, rasagiline, prevents apoptotic DNA damage induced by peroxynitrite in human dopaminergic neuroblastoma SH-SY5Y cells. J. Neurol Transm. 109, 467-481 (2002).
    • (2002) J. Neurol Transm , vol.109 , pp. 467-481
    • Maruyama, W.1    Takahashi, T.2    Youdim, M.3    Naoi, M.4
  • 204
    • 6344282164 scopus 로고    scopus 로고
    • Reactivity of 1,4-dihydropyridines toward SIN-1-derived peroxynitrite
    • Lopez-Alarcon, C. et al. Reactivity of 1,4-dihydropyridines toward SIN-1-derived peroxynitrite. Pharm. Res. 21, 1750-1757 (2004).
    • (2004) Pharm. Res , vol.21 , pp. 1750-1757
    • Lopez-Alarcon, C.1
  • 205
    • 1242306194 scopus 로고    scopus 로고
    • Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals
    • Bartesaghi, S. et al. Reactions of desferrioxamine with peroxynitrite-derived carbonate and nitrogen dioxide radicals. Free Radic. Biol. Med. 36, 471-483 (2004).
    • (2004) Free Radic. Biol. Med , vol.36 , pp. 471-483
    • Bartesaghi, S.1
  • 206
    • 0027180218 scopus 로고    scopus 로고
    • Oury, T D. et al., Cold-induced brain edema in mice. Involvement of extracellular superoxide dismutase and NO. J. Biol. Chem. 268, 15394-15398 (1993).
    • Oury, T D. et al., Cold-induced brain edema in mice. Involvement of extracellular superoxide dismutase and NO. J. Biol. Chem. 268, 15394-15398 (1993).
  • 207
    • 34250314563 scopus 로고    scopus 로고
    • Prevention of peroxynitrite-induced apoptosis of motor neurons and pc 12 cells by tyrosine-containing peptides
    • Ye, Y. et al. Prevention of peroxynitrite-induced apoptosis of motor neurons and pc 12 cells by tyrosine-containing peptides. J. Biol. Chem. 282, 6324-6337 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 6324-6337
    • Ye, Y.1
  • 208
    • 0033979990 scopus 로고    scopus 로고
    • Interaction of peroxynitrite with carotenoids in human low density lipoproteins
    • Panasenko, O. M., Sharov, V. S., Briviba. K. & Sies, H. Interaction of peroxynitrite with carotenoids in human low density lipoproteins. Arch. Biochem. Biophys. 373, 302-305 (2000).
    • (2000) Arch. Biochem. Biophys , vol.373 , pp. 302-305
    • Panasenko, O.M.1    Sharov, V.S.2    Briviba, K.3    Sies, H.4
  • 209
    • 0032740359 scopus 로고    scopus 로고
    • Protection against peroxynitrite by cocoa polyphenol oligomers
    • Arteel, G. E. & Sies, H. Protection against peroxynitrite by cocoa polyphenol oligomers. FEBS Lett. 462, 167-170 (1999).
    • (1999) FEBS Lett , vol.462 , pp. 167-170
    • Arteel, G.E.1    Sies, H.2
  • 210
    • 0038387937 scopus 로고    scopus 로고
    • Amphiphilic properties of (-)-epicatechin and their significance for protection of cells against peroxynitrite
    • Schroeder, P., Klotz, L. O. & Sies, H. Amphiphilic properties of (-)-epicatechin and their significance for protection of cells against peroxynitrite. Biochem. Biophys. Res. Commun. 307, 69-73 (2003).
    • (2003) Biochem. Biophys. Res. Commun , vol.307 , pp. 69-73
    • Schroeder, P.1    Klotz, L.O.2    Sies, H.3
  • 211
    • 0036122570 scopus 로고    scopus 로고
    • Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite
    • Ferrer-Sueta, G., Quijano, C. Alvarez, B. & Radi, R. Reactions of manganese porphyrins and manganese-superoxide dismutase with peroxynitrite. Methods Enzymol. 349, 23-37 (2002).
    • (2002) Methods Enzymol , vol.349 , pp. 23-37
    • Ferrer-Sueta, G.1    Quijano, C.2    Alvarez, B.3    Radi, R.4
  • 212
    • 0029797982 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalysts
    • Stern, M. K., Jensen, M. P. & Kramer, K. Peroxynitrite decomposition catalysts. J. Am. Chem. Soc. 118, 8735-8736 (1996).
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 8735-8736
    • Stern, M.K.1    Jensen, M.P.2    Kramer, K.3
  • 213
    • 0037047957 scopus 로고    scopus 로고
    • Peroxynitrite decomposition activity of iron porphyrin complexes
    • Jensen, M. P. & Riley, D. P. Peroxynitrite decomposition activity of iron porphyrin complexes. Inorg. Chem. 41, 4788-4797 (2002).
    • (2002) Inorg. Chem , vol.41 , pp. 4788-4797
    • Jensen, M.P.1    Riley, D.P.2
  • 214
    • 0035866568 scopus 로고    scopus 로고
    • Mechanisms of peroxynitrite decomposition catalyzed by FeTMPS, a bioactive sulfonated iron porphyrin
    • Shimanovich, R. & Groves, J. T. Mechanisms of peroxynitrite decomposition catalyzed by FeTMPS, a bioactive sulfonated iron porphyrin. Arch. Biochem. Biophys. 387, 307-317 (2001).
    • (2001) Arch. Biochem. Biophys , vol.387 , pp. 307-317
    • Shimanovich, R.1    Groves, J.T.2
  • 215
    • 0029952391 scopus 로고    scopus 로고
    • Evidence of peroxynitrite involvement in the carrageenan-induced rat paw edema
    • Salvemini, D. et al. Evidence of peroxynitrite involvement in the carrageenan-induced rat paw edema. Eur. J. Pharmocol. 303, 217-220 (1996).
    • (1996) Eur. J. Pharmocol , vol.303 , pp. 217-220
    • Salvemini, D.1
  • 216
    • 0032478182 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalysts: Therapeutics for peroxynitrite-mediated pathology
    • Salvemini, D., Wang, Z. Q., Stern, M. K., Currie, M. G. & Misko, T. P. Peroxynitrite decomposition catalysts: Therapeutics for peroxynitrite-mediated pathology. Proc. Natl. Acad. Sci. USA 95 2659-2663 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2659-2663
    • Salvemini, D.1    Wang, Z.Q.2    Stern, M.K.3    Currie, M.G.4    Misko, T.P.5
  • 217
    • 0034632225 scopus 로고    scopus 로고
    • A catalyst of peroxynitrite decomposition inhibits murine experimental autoimmune encephalomyelitis
    • Cross, A. H. et al. A catalyst of peroxynitrite decomposition inhibits murine experimental autoimmune encephalomyelitis. J. Neuroimmunol. 107, 21-28 (2001).
    • (2001) J. Neuroimmunol , vol.107 , pp. 21-28
    • Cross, A.H.1
  • 218
    • 0037120631 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalyst prevents apoptotic cell death in a human astrocytoma cell line incubated with supernatants of HIV-infected macrophages
    • Muscoli, C. et al. Peroxynitrite decomposition catalyst prevents apoptotic cell death in a human astrocytoma cell line incubated with supernatants of HIV-infected macrophages. BMC Neurosci. 3, 13 (2002).
    • (2002) BMC Neurosci , vol.3 , pp. 13
    • Muscoli, C.1
  • 219
    • 0034043548 scopus 로고    scopus 로고
    • Beneficial effects of peroxynitrite decomposition catalyst in a rat model of splanchnic artery occlusion and reperfuslon
    • Cuzzocrea, S. et al. Beneficial effects of peroxynitrite decomposition catalyst in a rat model of splanchnic artery occlusion and reperfuslon. FASEB J. 14, 1061-1072 (2000).
    • (2000) FASEB J , vol.14 , pp. 1061-1072
    • Cuzzocrea, S.1
  • 220
    • 3242892582 scopus 로고    scopus 로고
    • Neuroprotective efficacy and therapeutic time window of peroxynitrite decomposition catalysts in focal cerebral ischemia in rats
    • Thiyagarajan, M., Kaul, C. L. & Sharma, S. S. Neuroprotective efficacy and therapeutic time window of peroxynitrite decomposition catalysts in focal cerebral ischemia in rats. Br. J. Pharmacol. 142, 899-911 (2004).
    • (2004) Br. J. Pharmacol , vol.142 , pp. 899-911
    • Thiyagarajan, M.1    Kaul, C.L.2    Sharma, S.S.3
  • 221
    • 7944224937 scopus 로고    scopus 로고
    • Neuroprotective effect of peroxynitrite decomposition catalyst and poly(adenosine diphosphate-ribose) polymerase inhibitor alone and in combination in rats with focal cerebral ischemia
    • Sharma, S. S., Munusamy, S., Thiyagarajan, M. & Kaul, C. L. Neuroprotective effect of peroxynitrite decomposition catalyst and poly(adenosine diphosphate-ribose) polymerase inhibitor alone and in combination in rats with focal cerebral ischemia. J. Neurosurg. 101, 669-675 (2004).
    • (2004) J. Neurosurg , vol.101 , pp. 669-675
    • Sharma, S.S.1    Munusamy, S.2    Thiyagarajan, M.3    Kaul, C.L.4
  • 222
    • 0036584232 scopus 로고    scopus 로고
    • 1-42- and lipopolysaccharide-activated microglia
    • 1-42- and lipopolysaccharide-activated microglia. J. Neurosci. 22, 3484-3492 (2002).
    • (2002) J. Neurosci , vol.22 , pp. 3484-3492
    • Xie, Z.1
  • 223
    • 27344458546 scopus 로고    scopus 로고
    • Activation of microglial NADPH oxidase is synergistic with glial iNOS expression in inducing neuronal death: A dual-key mechanism of inflammatory neurodegeneration
    • Mander, P. & Brown, G. C. Activation of microglial NADPH oxidase is synergistic with glial iNOS expression in inducing neuronal death: A dual-key mechanism of inflammatory neurodegeneration. J. Neuroinflammation 22, 20 (2005).
    • (2005) J. Neuroinflammation , vol.22 , pp. 20
    • Mander, P.1    Brown, G.C.2
  • 224
    • 1542348201 scopus 로고    scopus 로고
    • Peroxynitrite mediates NO-induced blood-brain barrier damage
    • Tan, K. H., Harrington, S., Purcell, W. M. & Hurst, R. D. Peroxynitrite mediates NO-induced blood-brain barrier damage. Neurochem. Res. 29, 579-587 (2004).
    • (2004) Neurochem. Res , vol.29 , pp. 579-587
    • Tan, K.H.1    Harrington, S.2    Purcell, W.M.3    Hurst, R.D.4
  • 225
    • 0033900011 scopus 로고    scopus 로고
    • Peroxynitrite is a major contributor to cytokine-induced myocardial contractile failure
    • Ferdinandy, P., Danial, H. Ambrus, I., Rothery, R. A. & Schulz, R. Peroxynitrite is a major contributor to cytokine-induced myocardial contractile failure. Circ. Res. 87, 241-247 (2000).
    • (2000) Circ. Res , vol.87 , pp. 241-247
    • Ferdinandy, P.1    Danial, H.2    Ambrus, I.3    Rothery, R.A.4    Schulz, R.5
  • 226
    • 21344452296 scopus 로고    scopus 로고
    • Peroxynitrite modulates release of inflammatory mediators from guinea pig lung mast cells activated by antigen-antibody reaction
    • Kim, J. Y., Lee, K. H., Lee, B. K. & Ro, J. Y. Peroxynitrite modulates release of inflammatory mediators from guinea pig lung mast cells activated by antigen-antibody reaction. Int. Arch. Allergy Immunol. 137, 104-114 (2005).
    • (2005) Int. Arch. Allergy Immunol , vol.137 , pp. 104-114
    • Kim, J.Y.1    Lee, K.H.2    Lee, B.K.3    Ro, J.Y.4
  • 227
    • 7444239689 scopus 로고    scopus 로고
    • Redox-dependent effects of NO on microvascular integrity in oxygen-induced retinopathy
    • Beauchamp, M. H. et al. Redox-dependent effects of NO on microvascular integrity in oxygen-induced retinopathy. Free Radic. Biol. Med. 37, 1885-1894 (2004).
    • (2004) Free Radic. Biol. Med , vol.37 , pp. 1885-1894
    • Beauchamp, M.H.1
  • 228
    • 12944261922 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalyst ameliorates renal damage and protein nitration in cisplatin-induced nephrotoxicity in rats
    • Chirino, Y. I., Hernandez-Pando, R. & Pedraza-Chaverri, J. Peroxynitrite decomposition catalyst ameliorates renal damage and protein nitration in cisplatin-induced nephrotoxicity in rats. BMC Pharmacol. 4, 20 (2004).
    • (2004) BMC Pharmacol , vol.4 , pp. 20
    • Chirino, Y.I.1    Hernandez-Pando, R.2    Pedraza-Chaverri, J.3
  • 229
    • 4744353904 scopus 로고    scopus 로고
    • Effects of the peroxynitrite decomposition catalyst, FeTMPyP, on function of corpus cavernosum from diabetic mice
    • Nangle, M. R., Cotter, M. A. & Cameron. N. E. Effects of the peroxynitrite decomposition catalyst, FeTMPyP, on function of corpus cavernosum from diabetic mice. Eur. J. Pharmacol. 502, 143-148 (2004).
    • (2004) Eur. J. Pharmacol , vol.502 , pp. 143-148
    • Nangle, M.R.1    Cotter, M.A.2    Cameron, N.E.3
  • 230
    • 33748990922 scopus 로고    scopus 로고
    • A role for NO-mediated peroxynitrite formation in a model of endotoxin induced shock
    • Cuzzocrea, S. et al. A role for NO-mediated peroxynitrite formation in a model of endotoxin induced shock. J. Pharmacol. Exp. Ther. 319, 73-81 (2006).
    • (2006) J. Pharmacol. Exp. Ther , vol.319 , pp. 73-81
    • Cuzzocrea, S.1
  • 231
    • 0036821898 scopus 로고    scopus 로고
    • Pathogenetic role of peroxynitrite in the development of diabetes and diabetic vascular complications: Studies with FP15, a novel potent peroxynitrite decomposition catalyst
    • Szabó, C. et al. Pathogenetic role of peroxynitrite in the development of diabetes and diabetic vascular complications: Studies with FP15, a novel potent peroxynitrite decomposition catalyst. Mol. Med. 8, 571-580 (2002).
    • (2002) Mol. Med , vol.8 , pp. 571-580
    • Szabó, C.1
  • 232
    • 33646541061 scopus 로고    scopus 로고
    • Competing approaches to excitotoxic neuroprotection by inert and catalytic andoxidant porphyrins
    • Tauskela, J. S. et al. Competing approaches to excitotoxic neuroprotection by inert and catalytic andoxidant porphyrins. Neurosci. Lett. 401, 236-241 (2006).
    • (2006) Neurosci. Lett , vol.401 , pp. 236-241
    • Tauskela, J.S.1
  • 233
    • 14644405532 scopus 로고    scopus 로고
    • Role for nitrosative stress in diabetic neuropathy: Evidence from studies with-a peroxynitrite decomposition catalyst
    • Obrosava, I. G. et al. Role for nitrosative stress in diabetic neuropathy: Evidence from studies with-a peroxynitrite decomposition catalyst. FASEB J. 19, 401-403 (2005).
    • (2005) FASEB J , vol.19 , pp. 401-403
    • Obrosava, I.G.1
  • 234
    • 6344293916 scopus 로고    scopus 로고
    • Peroxynitrite decomposition catalyst, FP 15, and poly(ADP-ribose) polymerase inhibitor, PJ34, inhibit leukocyte entrapment in the retinal microcirculation of diabetic rats
    • Sugawara, R. et al. Peroxynitrite decomposition catalyst, FP 15, and poly(ADP-ribose) polymerase inhibitor, PJ34, inhibit leukocyte entrapment in the retinal microcirculation of diabetic rats. Curr. Eye Res. 29, 11-16 (2004).
    • (2004) Curr. Eye Res , vol.29 , pp. 11-16
    • Sugawara, R.1
  • 235
    • 0036797558 scopus 로고    scopus 로고
    • A novel peroxynitrite decomposer catalyst (FP-15) reduces myocardial infarct size in an in vivo peroxynitrite decomposer and acute ischemia-reperfusion in pigs
    • Bianchi, C. et al. A novel peroxynitrite decomposer catalyst (FP-15) reduces myocardial infarct size in an in vivo peroxynitrite decomposer and acute ischemia-reperfusion in pigs. Ann. Thorac. Surg. 74, 1201-1207 (2002).
    • (2002) Ann. Thorac. Surg , vol.74 , pp. 1201-1207
    • Bianchi, C.1
  • 236
    • 0037448784 scopus 로고    scopus 로고
    • Potent metalloporphyrin peroxynitrite decomposition catalyst protects against the development of doxorubicin-induced cardiac dysfunction
    • Pacher, P. et al. Potent metalloporphyrin peroxynitrite decomposition catalyst protects against the development of doxorubicin-induced cardiac dysfunction. Circulation 107, 896-904 (2003).
    • (2003) Circulation , vol.107 , pp. 896-904
    • Pacher, P.1
  • 237
    • 0038693336 scopus 로고    scopus 로고
    • Enhanced peroxynitrite decomposition protects against experimental obliterative bronchiolitis
    • Naidu, B. V. et al. Enhanced peroxynitrite decomposition protects against experimental obliterative bronchiolitis. Exp. Mol. Pathol. 75, 12-17 (2003).
    • (2003) Exp. Mol. Pathol , vol.75 , pp. 12-17
    • Naidu, B.V.1
  • 238
    • 0141941746 scopus 로고    scopus 로고
    • PARP inhibition improves the effectiveness of neural stem cell transplantation in experimental brain trauma
    • Lacza, Z. et al. PARP inhibition improves the effectiveness of neural stem cell transplantation in experimental brain trauma. Int. J. Mol. Med. 12, 153-159 (2003).
    • (2003) Int. J. Mol. Med , vol.12 , pp. 153-159
    • Lacza, Z.1
  • 239
    • 0037489515 scopus 로고    scopus 로고
    • Critical role of reactive nitrogen species in lung ischemia-reperfusion injury
    • Naidu, B. V. et al. Critical role of reactive nitrogen species in lung ischemia-reperfusion injury. J. Heart Lung Transplant. 22 784-793 (2003).
    • (2003) J. Heart Lung Transplant , vol.22 , pp. 784-793
    • Naidu, B.V.1
  • 240
    • 1842614095 scopus 로고    scopus 로고
    • Suppression of intestinal polyposis in Apcmin/ + mice by targeting the NO or poly(ADP-ribose) pathways
    • Mabley, J. G. et al. Suppression of intestinal polyposis in Apcmin/ + mice by targeting the NO or poly(ADP-ribose) pathways. Mutat. Res. 548, 107-116 (2004).
    • (2004) Mutat. Res , vol.548 , pp. 107-116
    • Mabley, J.G.1
  • 241
    • 0036821907 scopus 로고    scopus 로고
    • Beneficial effects of the peroxynitrite decomposition catalyst FP 15 in murine models of arthritis and colitis
    • Mabley, J. G. et al. Beneficial effects of the peroxynitrite decomposition catalyst FP 15 in murine models of arthritis and colitis. Mol. Med. 8, 581-590 (2002).
    • (2002) Mol. Med , vol.8 , pp. 581-590
    • Mabley, J.G.1
  • 242
    • 23044479642 scopus 로고    scopus 로고
    • Protective mechanisms of a metalloporphyrinic peroxynitrite decomposition catalyst, MW85, in rat cardiac transplants
    • Pieper, G. M. et al. Protective mechanisms of a metalloporphyrinic peroxynitrite decomposition catalyst, MW85, in rat cardiac transplants. J. Pharmocol. Exp. Ther. 314, 53-60 (2005).
    • (2005) J. Pharmocol. Exp. Ther , vol.314 , pp. 53-60
    • Pieper, G.M.1
  • 243
    • 29144471851 scopus 로고    scopus 로고
    • Role of peroxynitrite anion in renal hypothermic preservation injury
    • Mangino, M. J. et al. Role of peroxynitrite anion in renal hypothermic preservation injury. Transplantation 80, 1455-1460 (2005).
    • (2005) Transplantation , vol.80 , pp. 1455-1460
    • Mangino, M.J.1
  • 244
    • 0029922989 scopus 로고    scopus 로고
    • Evaluation of the relative contribution of NO and peroxynitrite to the suppression of mitochondrial respiration in immunostimulated macrophages using a manganese mesoporphyrin superoxide dismutase mimetic and peroxynitrite scavenger
    • Szabó, C., Day, B. J. & Salzman, A. L. Evaluation of the relative contribution of NO and peroxynitrite to the suppression of mitochondrial respiration in immunostimulated macrophages using a manganese mesoporphyrin superoxide dismutase mimetic and peroxynitrite scavenger. FEBS Lett. 381, 82-86 (1996).
    • (1996) FEBS Lett , vol.381 , pp. 82-86
    • Szabó, C.1    Day, B.J.2    Salzman, A.L.3
  • 245
    • 0031033903 scopus 로고    scopus 로고
    • The potential role of peroxynitrite in the vascular contractile and cellular energetic failure in endotoxic shock
    • Zingarelli, B., Day, B. J., Crapo, J. D., Salzman, A. L. & Szabó, C. The potential role of peroxynitrite in the vascular contractile and cellular energetic failure in endotoxic shock. Br. J. Pharmocol. 120, 259-267 (1997).
    • (1997) Br. J. Pharmocol , vol.120 , pp. 259-267
    • Zingarelli, B.1    Day, B.J.2    Crapo, J.D.3    Salzman, A.L.4    Szabó, C.5
  • 246
    • 0345196633 scopus 로고    scopus 로고
    • Beneficial effects of Mn(III)tetrakis (4-benzoic acid) porphyrin (MnTBAP), a superoxide dismutase mimetic, in carrageenan-induced pleurisy
    • Cuzzocrea, S., Zingarelli, B., Costantino, G. & Caputi, A. P. Beneficial effects of Mn(III)tetrakis (4-benzoic acid) porphyrin (MnTBAP), a superoxide dismutase mimetic, in carrageenan-induced pleurisy. Free Radic. Biol. Med. 26, 25-33 (1999).
    • (1999) Free Radic. Biol. Med , vol.26 , pp. 25-33
    • Cuzzocrea, S.1    Zingarelli, B.2    Costantino, G.3    Caputi, A.P.4
  • 247
    • 0037008268 scopus 로고    scopus 로고
    • Pneumococcal meningitis in the rat: Evaluation of peroxynitrite scavengers for adjunctive therapy
    • Kastenbauer, S., Koedel, U., Becker, B. F. & Pfister, H. W. Pneumococcal meningitis in the rat: Evaluation of peroxynitrite scavengers for adjunctive therapy. Eur. J. Pharmacol. 449, 177-181 (2002).
    • (2002) Eur. J. Pharmacol , vol.449 , pp. 177-181
    • Kastenbauer, S.1    Koedel, U.2    Becker, B.F.3    Pfister, H.W.4
  • 248
    • 27444435011 scopus 로고    scopus 로고
    • Peroxynitrite generated at the level produced by spinal cord injury induces peroxidation of membrane phospholipids in normal rat cord: Reduction by a metalloporphyrin
    • Liu, D., Bao, F., Prough, D. S. & Dewitt, D. S. Peroxynitrite generated at the level produced by spinal cord injury induces peroxidation of membrane phospholipids in normal rat cord: Reduction by a metalloporphyrin. J. Neurotrauma. 22, 1123-1133 (2005).
    • (2005) J. Neurotrauma , vol.22 , pp. 1123-1133
    • Liu, D.1    Bao, F.2    Prough, D.S.3    Dewitt, D.S.4
  • 249
    • 0042848453 scopus 로고    scopus 로고
    • Reactions of manganese porphyrins with peroxynitrite and carbonate radical anion
    • Ferrer-Sueta, G. et al. Reactions of manganese porphyrins with peroxynitrite and carbonate radical anion. J. Biol. Chem. 278 27432-27438 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 27432-27438
    • Ferrer-Sueta, G.1
  • 250
    • 0242321029 scopus 로고    scopus 로고
    • Peroxynitrite flux-mediated LDL oxidation is inhibited by manganese porphyrins in the presence of uric acid
    • Trostchansky, A. et al. Peroxynitrite flux-mediated LDL oxidation is inhibited by manganese porphyrins in the presence of uric acid. Free Radic. Biol. Med. 35, 1293-1300 (2003).
    • (2003) Free Radic. Biol. Med , vol.35 , pp. 1293-1300
    • Trostchansky, A.1
  • 251
    • 0034656837 scopus 로고    scopus 로고
    • Peroxynitrite scavenging by metalloporphyrins and thiolates
    • Crow, J. P. Peroxynitrite scavenging by metalloporphyrins and thiolates. Free Radic. Biol. Med. 28, 1487-1494 (2000).
    • (2000) Free Radic. Biol. Med , vol.28 , pp. 1487-1494
    • Crow, J.P.1
  • 252
    • 33745829019 scopus 로고    scopus 로고
    • Reduction of manganese porphyrins by flavoenzymes and submitochondrial particles: A catalytic cycle for the reduction of peroxynitrite
    • Ferrer-Sueta, G., Hannibal, L., Batinic-Haberle, I. & Radi, R. Reduction of manganese porphyrins by flavoenzymes and submitochondrial particles: a catalytic cycle for the reduction of peroxynitrite. Free Radic. Biol. Med. 41, 503-512 (2006).
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 503-512
    • Ferrer-Sueta, G.1    Hannibal, L.2    Batinic-Haberle, I.3    Radi, R.4
  • 253
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner, K. M., Liochev, S. I. & Fridovich, I. Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo. J. Biol. Chem. 269, 23471-23476 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 254
    • 33947304812 scopus 로고    scopus 로고
    • +, targets mouse heart mitochondria
    • +, targets mouse heart mitochondria. Free Radic. Biol. Med. 42, 1193-1200 (2007).
    • (2007) Free Radic. Biol. Med , vol.42 , pp. 1193-1200
    • Spasojevic, I.1
  • 255
    • 0032544579 scopus 로고    scopus 로고
    • The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium-2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic
    • Batinic-Haberle, I., Benov, L., Spasojevic, I. & Fridovich, I. The ortho effect makes manganese(III) meso-tetrakis(N-methylpyridinium-2-yl)porphyrin a powerful and potentially useful superoxide dismutase mimic. J. Biol. Chem. 273, 24521-24528 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 24521-24528
    • Batinic-Haberle, I.1    Benov, L.2    Spasojevic, I.3    Fridovich, I.4
  • 256
    • 0035399884 scopus 로고    scopus 로고
    • Neuroprotection from delayed postischemic administration of a metalloporphyrin catalytic antioxidant
    • Mackensen, G. B. et al. Neuroprotection from delayed postischemic administration of a metalloporphyrin catalytic antioxidant. J. Neurosci. 21, 4582-4592 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 4582-4592
    • Mackensen, G.B.1
  • 257
    • 2942713709 scopus 로고    scopus 로고
    • A small molecular weight catalytic metalloporphyrin antioxidant with superoxide dismutase (SOD) mimetic properties protects lungs from radiation-induced injury
    • Vujaskovic, Z. et al. A small molecular weight catalytic metalloporphyrin antioxidant with superoxide dismutase (SOD) mimetic properties protects lungs from radiation-induced injury. Free Radic. Biol. Med. 33, 857-863 (2002).
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 857-863
    • Vujaskovic, Z.1
  • 258
    • 24944488889 scopus 로고    scopus 로고
    • A manganese porphyrin superoxide dismutase mimetic enhances tumor radioresponsiveness
    • Moeller, B. J. et al. A manganese porphyrin superoxide dismutase mimetic enhances tumor radioresponsiveness. Int. J. Radiat. Oncol. Biol. Phys. 63, 545-552 (2005).
    • (2005) Int. J. Radiat. Oncol. Biol. Phys , vol.63 , pp. 545-552
    • Moeller, B.J.1
  • 260
    • 18644383755 scopus 로고    scopus 로고
    • Effects of metalloporphyrin catalytic antioxidants in experimental brain ischemia
    • Sheng, H. et al. Effects of metalloporphyrin catalytic antioxidants in experimental brain ischemia. Free Radic. Biol. Med. 33, 947-961 (2002).
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 947-961
    • Sheng, H.1
  • 261
    • 3242755872 scopus 로고    scopus 로고
    • Mouse spinal cord compression injury is ameliorated by intrathecall cationic manganese(III) porphyrin catalytic antioxidant therapy
    • Sheng, H., Spasojevic, I., Warner, D. S. & Batinic-Haberle, I. Mouse spinal cord compression injury is ameliorated by intrathecall cationic manganese(III) porphyrin catalytic antioxidant therapy. Neurosci. Lett. 366, 220-225 (2004).
    • (2004) Neurosci. Lett , vol.366 , pp. 220-225
    • Sheng, H.1    Spasojevic, I.2    Warner, D.S.3    Batinic-Haberle, I.4
  • 262
    • 23244439603 scopus 로고    scopus 로고
    • Manganese porphyrin given at symptom onset markedly extends survival of ALS mice
    • Crow, J. P., Calingasan, N. Y., Chen, J., Hill, J. L. & Beal, M. F. Manganese porphyrin given at symptom onset markedly extends survival of ALS mice. Ann. Neurol. 58, 258-265 (2005).
    • (2005) Ann. Neurol , vol.58 , pp. 258-265
    • Crow, J.P.1    Calingasan, N.Y.2    Chen, J.3    Hill, J.L.4    Beal, M.F.5
  • 263
    • 0034827921 scopus 로고    scopus 로고
    • Mn(II)-texaphyrin as a catalyst for the decomposition of peroxynitrite
    • Shimanovich, R. et al. Mn(II)-texaphyrin as a catalyst for the decomposition of peroxynitrite. J. Am. Chem. Soc. 123, 3613-3614 (2001).
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 3613-3614
    • Shimanovich, R.1
  • 264
    • 0037103792 scopus 로고    scopus 로고
    • Oxidation of nitric oxide by oxomanganese-salen complexes: A new mechanism for cellular protection by superoxide dismutase/catalase mimetics
    • Sharpe, M. A., Ollosson, R., Stewart, V. C. & Clark, J. B. Oxidation of nitric oxide by oxomanganese-salen complexes: A new mechanism for cellular protection by superoxide dismutase/catalase mimetics. Biochem. J. 366, 97-107 (2002).
    • (2002) Biochem. J , vol.366 , pp. 97-107
    • Sharpe, M.A.1    Ollosson, R.2    Stewart, V.C.3    Clark, J.B.4
  • 265
    • 33745753533 scopus 로고    scopus 로고
    • Decomposition of reactive oxygen species by copper(II) bis(1-pyrazolyl)methane complexes
    • Schepetkin, I. et al. Decomposition of reactive oxygen species by copper(II) bis(1-pyrazolyl)methane complexes. J. Biol. Inorg. Chem. 11, 499-513 (2006).
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 499-513
    • Schepetkin, I.1
  • 266
    • 33748460635 scopus 로고    scopus 로고
    • Design of manganese porphyrin modified with mitochondrial signal peptide for a new antioxidant
    • Asayama, S., Kawamura, E., Nagaoka, S. & Kawakami, H. Design of manganese porphyrin modified with mitochondrial signal peptide for a new antioxidant. Mol. Pharm. 3, 468-470 (2006).
    • (2006) Mol. Pharm , vol.3 , pp. 468-470
    • Asayama, S.1    Kawamura, E.2    Nagaoka, S.3    Kawakami, H.4
  • 267
    • 0028967728 scopus 로고
    • Endotoxin triggers the expression of an inducible isoform of NO synthase and the formation of peroxynitrite in the rat aorta in vivo
    • Szabó, C., Salzman, A. L. & Ischiropoulos, H. Endotoxin triggers the expression of an inducible isoform of NO synthase and the formation of peroxynitrite in the rat aorta in vivo. FEBS Lett. 363, 235-238 (1995).
    • (1995) FEBS Lett , vol.363 , pp. 235-238
    • Szabó, C.1    Salzman, A.L.2    Ischiropoulos, H.3
  • 268
    • 0029148018 scopus 로고
    • Peroxynitrite-mediated oxidation of dihydrorhodamine 123 occurs in early stages of endotoxic and hemorrhagic shock and ischemia-reperfusion injury
    • Szabó, C., Salzman, A. L. & Ischiropoulos, H. Peroxynitrite-mediated oxidation of dihydrorhodamine 123 occurs in early stages of endotoxic and hemorrhagic shock and ischemia-reperfusion injury. FEBS Lett. 372, 229-232 (1995).
    • (1995) FEBS Lett , vol.372 , pp. 229-232
    • Szabó, C.1    Salzman, A.L.2    Ischiropoulos, H.3
  • 269
    • 0031028998 scopus 로고    scopus 로고
    • Clinical evidence of peroxynitrite formation in chronic renal failure patients with septic shock
    • Fukuyama, N. et al. Clinical evidence of peroxynitrite formation in chronic renal failure patients with septic shock. Free Radic. Biol. Med. 22, 771-774 (1997).
    • (1997) Free Radic. Biol. Med , vol.22 , pp. 771-774
    • Fukuyama, N.1
  • 270
    • 0037381114 scopus 로고    scopus 로고
    • Deactivation of norepinephrine by peroxynitrite as a new pathogenesis in the hypotension of septic shock
    • Takakura, K, Xiaohong, W., Takeuchi, K. Yasuda, Y. & Fukuda, S. Deactivation of norepinephrine by peroxynitrite as a new pathogenesis in the hypotension of septic shock. Anesthesiology 98, 928-934 (2003).
    • (2003) Anesthesiology , vol.98 , pp. 928-934
    • Takakura, K.1    Xiaohong, W.2    Takeuchi, K.3    Yasuda, Y.4    Fukuda, S.5
  • 271
    • 0030573997 scopus 로고    scopus 로고
    • Sensitivity of human pancreatic islets to peroxynitrite-induced cell dysfunction and death
    • Delaney, C. A. et al. Sensitivity of human pancreatic islets to peroxynitrite-induced cell dysfunction and death. FEBS Lett. 394, 300-306 (1996).
    • (1996) FEBS Lett , vol.394 , pp. 300-306
    • Delaney, C.A.1
  • 272
    • 0030987135 scopus 로고    scopus 로고
    • Development of autoimmune diabetes in NOD mice is associated with the formation of peroxynitrite in pancreatic islet β-cells
    • Suarez-Pinzon, W. L, Szabé, C. & Rabinovitch, A. Development of autoimmune diabetes in NOD mice is associated with the formation of peroxynitrite in pancreatic islet β-cells. Diabetes 46, 907-911 (1997).
    • (1997) Diabetes , vol.46 , pp. 907-911
    • Suarez-Pinzon, W.L.1    Szabé, C.2    Rabinovitch, A.3
  • 273
    • 0034949349 scopus 로고    scopus 로고
    • An inhibitor of inducible NO synthase and scavenger of peroxynitrite prevents diabetes development in NOD mice
    • Suarez-Pinzon, W. L et al. An inhibitor of inducible NO synthase and scavenger of peroxynitrite prevents diabetes development in NOD mice. J. Autoimmun. 16, 449-455 (2001).
    • (2001) J. Autoimmun , vol.16 , pp. 449-455
    • Suarez-Pinzon, W.L.1
  • 274
    • 0036328572 scopus 로고    scopus 로고
    • Preservation of human islet cell functional mass by anti-oxidative action of a novel SOD mimic compound
    • Bottino, R. et al. Preservation of human islet cell functional mass by anti-oxidative action of a novel SOD mimic compound. Diabetes 51, 2561-2567 (2002).
    • (2002) Diabetes , vol.51 , pp. 2561-2567
    • Bottino, R.1
  • 275
    • 0036061614 scopus 로고    scopus 로고
    • A metalloporphyrin-based superoxide dismutase mimic inhibits adoptive transfer of autoimmune diabetes by a diabetogenic T-cell clone
    • Piganelli, J. D. et al. A metalloporphyrin-based superoxide dismutase mimic inhibits adoptive transfer of autoimmune diabetes by a diabetogenic T-cell clone. Diabetes 51, 347-355 (2002).
    • (2002) Diabetes , vol.51 , pp. 347-355
    • Piganelli, J.D.1
  • 276
    • 4644325195 scopus 로고    scopus 로고
    • A salen-manganese catalytic free radical scavenger inhibits type 1 diabetes and islet allograft rejection
    • Olcott, A. P. et al. A salen-manganese catalytic free radical scavenger inhibits type 1 diabetes and islet allograft rejection. Diabetes 53, 2574-2580 (2004).
    • (2004) Diabetes , vol.53 , pp. 2574-2580
    • Olcott, A.P.1
  • 277
    • 20044390365 scopus 로고    scopus 로고
    • Functional and molecular defects of pancreatic islets in human type 2 diabetes
    • Del Guerra. S. et al. Functional and molecular defects of pancreatic islets in human type 2 diabetes. Diabetes 54, 727-735 (2005).
    • (2005) Diabetes , vol.54 , pp. 727-735
    • Del Guerra, S.1
  • 278
    • 0034078563 scopus 로고    scopus 로고
    • Increased nitrotyrosine staining in kidneys from patients with diabetic nephropathy
    • Thuraisingham, R. C., Nott, C. A., Dodd, S. M. & Yaqoob, M. M. Increased nitrotyrosine staining in kidneys from patients with diabetic nephropathy. Kidney Int. 57, 1968-1972 (2000).
    • (2000) Kidney Int , vol.57 , pp. 1968-1972
    • Thuraisingham, R.C.1    Nott, C.A.2    Dodd, S.M.3    Yaqoob, M.M.4
  • 279
    • 0037137287 scopus 로고    scopus 로고
    • Poly(ADP-Ribose) polymerase is activated in subjects at risk of developing type 2 diabetes and is associated with impaired vascular reactivity
    • Szabó, C. et al. Poly(ADP-Ribose) polymerase is activated in subjects at risk of developing type 2 diabetes and is associated with impaired vascular reactivity. Circulation 106, 2680-2686 (2002).
    • (2002) Circulation , vol.106 , pp. 2680-2686
    • Szabó, C.1
  • 280
    • 0035136240 scopus 로고    scopus 로고
    • Diabetic endothelial dysfunction: The role of poly(ADP-ribose) polymerase activation
    • Garcia Soriano, F. et al. Diabetic endothelial dysfunction: The role of poly(ADP-ribose) polymerase activation. Nature Med. 7 108-113 (2001).
    • (2001) Nature Med , vol.7 , pp. 108-113
    • Garcia Soriano, F.1
  • 281
    • 33644756809 scopus 로고    scopus 로고
    • Increased monocytic activity and biomarkers of inflammation in patients with type 1 diabetes
    • Devaraj, S. et al. Increased monocytic activity and biomarkers of inflammation in patients with type 1 diabetes. Diabetes 55, 774-779 (2006).
    • (2006) Diabetes , vol.55 , pp. 774-779
    • Devaraj, S.1
  • 282
    • 19544392527 scopus 로고    scopus 로고
    • Nitrosative stress and pharmacological modulation of heart failure
    • Pacher, P., Schulz, R., Liaudet, L. & Szabó, C. Nitrosative stress and pharmacological modulation of heart failure. Trends Pharmacol. Sci. 26, 302-310 (2005).
    • (2005) Trends Pharmacol. Sci , vol.26 , pp. 302-310
    • Pacher, P.1    Schulz, R.2    Liaudet, L.3    Szabó, C.4
  • 283
    • 0033558704 scopus 로고    scopus 로고
    • Effects of endotoxin on human myocardial contractility involvement of NO and peroxynitrite
    • Flesch, M. et al. Effects of endotoxin on human myocardial contractility involvement of NO and peroxynitrite. J. Am. Coll. Cordial. 33, 1062-1070 (1996).
    • (1996) J. Am. Coll. Cordial , vol.33 , pp. 1062-1070
    • Flesch, M.1
  • 284
    • 14844361721 scopus 로고    scopus 로고
    • 2+-ATPase in human heart failure
    • 2+-ATPase in human heart failure. Circulation 111, 988-995 (2005).
    • (2005) Circulation , vol.111 , pp. 988-995
    • Lokuta, A.J.1
  • 285
    • 20244361944 scopus 로고    scopus 로고
    • Antioxidative effects of exercise training in patients with chronic heart failure: Increase in radical scavenger enzyme activity in skeletal muscle
    • Linke, A. et al. Antioxidative effects of exercise training in patients with chronic heart failure: Increase in radical scavenger enzyme activity in skeletal muscle. Circulation 111, 1763-1770 (2005).
    • (2005) Circulation , vol.111 , pp. 1763-1770
    • Linke, A.1
  • 286
    • 0036070546 scopus 로고    scopus 로고
    • Induction of oxidative stress and disintegrin metalloproteinase in human heart endstage failure
    • Hunt, M. J. et al. Induction of oxidative stress and disintegrin metalloproteinase in human heart endstage failure. Am. J. Physiol. Lung Cell. Mol. Physiol. 283. L239-L245 (2002).
    • (2002) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.283
    • Hunt, M.J.1
  • 287
    • 0037303479 scopus 로고    scopus 로고
    • NO-induced mitochondrial dysfunction: Implications for neurodegeneration
    • Stewart, V. C. & Heales, S. J. NO-induced mitochondrial dysfunction: implications for neurodegeneration. Free Radic. Biol. Med. 34 287-303(2003).
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 287-303
    • Stewart, V.C.1    Heales, S.J.2
  • 288
    • 0030868480 scopus 로고    scopus 로고
    • The role of mitochondrial dysfunction and neuronal NO in animal models of neurodegenerative diseases
    • Schulz, J. B., Matthews, R. T., Klockgether, T., Dichgans, J. & Beal, M. F. The role of mitochondrial dysfunction and neuronal NO in animal models of neurodegenerative diseases. Mol. Cell. Biochem. 174 193-197 (1997).
    • (1997) Mol. Cell. Biochem , vol.174 , pp. 193-197
    • Schulz, J.B.1    Matthews, R.T.2    Klockgether, T.3    Dichgans, J.4    Beal, M.F.5
  • 290
    • 0034965383 scopus 로고    scopus 로고
    • Expression of inducible NO synthase and nitrotyrosine in multiple sclerosis lesions
    • Liu, J. S., Zhao, M. L, Brosnan, C. F & Lee, S. C. Expression of inducible NO synthase and nitrotyrosine in multiple sclerosis lesions. Am. J. Pathol. 158, 2057-2066 (2001).
    • (2001) Am. J. Pathol , vol.158 , pp. 2057-2066
    • Liu, J.S.1    Zhao, M.L.2    Brosnan, C.F.3    Lee, S.C.4
  • 291
    • 0034939015 scopus 로고    scopus 로고
    • Localization of 3-nitrotyrosine to rheumatoid and normal synovium
    • Mapp. P. I. et al. Localization of 3-nitrotyrosine to rheumatoid and normal synovium. Arthritis Rheum. 44, 1534-1539 (2001).
    • (2001) Arthritis Rheum , vol.44 , pp. 1534-1539
    • Mapp, P.I.1
  • 292
    • 7144253803 scopus 로고    scopus 로고
    • increased expression of an inducible isoform of NO synthase and the formation of peroxynitrite in colonic mucosa of patients with active ulcerative colitis
    • Kimura, H. et al. increased expression of an inducible isoform of NO synthase and the formation of peroxynitrite in colonic mucosa of patients with active ulcerative colitis. Gut 42, 180-187 (1998).
    • (1998) Gut , vol.42 , pp. 180-187
    • Kimura, H.1
  • 293
    • 0033014055 scopus 로고    scopus 로고
    • Inducible NO synthase expression in human cerebral infarcts
    • Forster, C., Clark, H. B., Ross, M. E. & Iadecola, C. Inducible NO synthase expression in human cerebral infarcts. Acta Neuropathol. 97, 215-220 (1999).
    • (1999) Acta Neuropathol , vol.97 , pp. 215-220
    • Forster, C.1    Clark, H.B.2    Ross, M.E.3    Iadecola, C.4
  • 294
    • 0036736045 scopus 로고    scopus 로고
    • Immunocytochemical evidence for inducible NO synthase and cyclooxygenase-2 expression with nitrotyrosine formation in human hibernating myocardium
    • Baker, C. S. et al. Immunocytochemical evidence for inducible NO synthase and cyclooxygenase-2 expression with nitrotyrosine formation in human hibernating myocardium. Basic Res. Cardiol. 97, 409-415 (2002).
    • (2002) Basic Res. Cardiol , vol.97 , pp. 409-415
    • Baker, C.S.1
  • 295
    • 33747598024 scopus 로고    scopus 로고
    • Peroxynitrite is a major trigger of cardiomyocyte apoptosis in vitro and in vivo
    • Levirand, S. et al. Peroxynitrite is a major trigger of cardiomyocyte apoptosis in vitro and in vivo. Free Radic. Biol. Med. 41, 886-895 (2006).
    • (2006) Free Radic. Biol. Med , vol.41 , pp. 886-895
    • Levirand, S.1
  • 296
    • 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, 541-581 (2001).
    • (2001) Free Radic. Res , vol.34 , pp. 541-581
    • Greenacre, S.A.1    Ischiropoulos, H.2
  • 297
    • 0037380924 scopus 로고    scopus 로고
    • Iron porphyrin treatment extends survival in a transgenic animal model of amyotrophic lateral sclerosis
    • Wu, A. S. et al. Iron porphyrin treatment extends survival in a transgenic animal model of amyotrophic lateral sclerosis. J. Neurochem. 85, 142-150 (2003).
    • (2003) J. Neurochem , vol.85 , pp. 142-150
    • Wu, A.S.1
  • 298
    • 0033019478 scopus 로고    scopus 로고
    • Peroxynitrite formation during rat hepatic allograft rejection
    • Yamaguchi. Y. et al. Peroxynitrite formation during rat hepatic allograft rejection. Hepatology 29, 777-784 (1999).
    • (1999) Hepatology , vol.29 , pp. 777-784
    • Yamaguchi, Y.1
  • 299
    • 0033572882 scopus 로고    scopus 로고
    • Quantitative analysis of cardiac 3-L-nitrotyrosine during acute allograft rejection in an experimental heart transplantation
    • Sakurai, M. et al. Quantitative analysis of cardiac 3-L-nitrotyrosine during acute allograft rejection in an experimental heart transplantation. Transplantation 68, 1818-1822 (1999).
    • (1999) Transplantation , vol.68 , pp. 1818-1822
    • Sakurai, M.1
  • 300
    • 0034684652 scopus 로고    scopus 로고
    • Enhanced peroxynitrite formation is associated with vascular aging
    • Van der Loo. B. et al. Enhanced peroxynitrite formation is associated with vascular aging. J. Exp Med. 192, 1731-1744 (2000).
    • (2000) J. Exp Med , vol.192 , pp. 1731-1744
    • Van der Loo, B.1
  • 301
    • 33744937888 scopus 로고    scopus 로고
    • Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging
    • Xu, S. et al. Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging. Am. J. Physiol. Heart Circ. Physiol. 290, H2220-H2226 (2006).
    • (2006) Am. J. Physiol. Heart Circ. Physiol , vol.290
    • Xu, S.1
  • 302
    • 33646697132 scopus 로고    scopus 로고
    • Hepatic oxidative stress during aging: Effects of 8% long-term calorie restriction and lifelong exercise
    • Seo, A. Y. et al. Hepatic oxidative stress during aging: Effects of 8% long-term calorie restriction and lifelong exercise. Antioxid. Redox Signal. 8, 529-538 (2006).
    • (2006) Antioxid. Redox Signal , vol.8 , pp. 529-538
    • Seo, A.Y.1
  • 303
    • 33846250408 scopus 로고    scopus 로고
    • The peroxynitrite decomposition catalyst FP15 improves ageing-associated cardiac and vascular dysfunction
    • Radovits, T. et al. The peroxynitrite decomposition catalyst FP15 improves ageing-associated cardiac and vascular dysfunction. Mech. Ageing Dev. 128, 173-181 (2007).
    • (2007) Mech. Ageing Dev , vol.128 , pp. 173-181
    • Radovits, T.1
  • 304
    • 10744226883 scopus 로고    scopus 로고
    • Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species
    • Vadseth, C. et al. Pro-thrombotic state induced by post-translational modification of fibrinogen by reactive nitrogen species. J. Biol. Chem. 279, 8820-8826 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 8820-8826
    • Vadseth, C.1
  • 305
    • 0035912714 scopus 로고    scopus 로고
    • Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration
    • Marrondes, S., Turko, I. V. & Murad, F. Nitration of succinyl-CoA:3-oxoacid CoA-transferase in rats after endotoxin administration. Proc. Natl Acad. Sci. USA 98, 7146-7151 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7146-7151
    • Marrondes, S.1    Turko, I.V.2    Murad, F.3
  • 306
    • 0035668056 scopus 로고    scopus 로고
    • Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase
    • Turko, I. V., Marcondes, S. & Murad, F. Diabetes-associated nitration of tyrosine and inactivation of succinyl-CoA:3-oxoacid CoA-transferase. Am. J. Physiol. Heart Circ. Physiol. 281, H2289-H2294 (2001).
    • (2001) Am. J. Physiol. Heart Circ. Physiol , vol.281
    • Turko, I.V.1    Marcondes, S.2    Murad, F.3
  • 307
    • 32144453826 scopus 로고    scopus 로고
    • Stroke-Acute Ischemic NXY Treatment (SAINT I) Trial Investigators. NXY-059 for acute ischemic stroke
    • Lees, K. R.et al. Stroke-Acute Ischemic NXY Treatment (SAINT I) Trial Investigators. NXY-059 for acute ischemic stroke. N. Engl. J. Med. 354, 588-600 (2006).
    • (2006) N. Engl. J. Med , vol.354 , pp. 588-600
    • Lees, K.R.1
  • 308
    • 0031059207 scopus 로고    scopus 로고
    • Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: Evidence against a stress-mediated response
    • Cable, E. E., Gildemeister, O. S., Pepe, J. A., Lambrecht, R. W. & Bonkovsky, H. L. Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: Evidence against a stress-mediated response. Mol. Cell. Biochem. 169, 13-20 (1997).
    • (1997) Mol. Cell. Biochem , vol.169 , pp. 13-20
    • Cable, E.E.1    Gildemeister, O.S.2    Pepe, J.A.3    Lambrecht, R.W.4    Bonkovsky, H.L.5
  • 309
    • 0037108119 scopus 로고    scopus 로고
    • A catalytic antioxidant (AEOL 10150) attenuates expression of inflammatory genes in stroke
    • Bowler, R. P. et al. A catalytic antioxidant (AEOL 10150) attenuates expression of inflammatory genes in stroke. Free Radic. Rial. Med. 33, 1141-1152 (2002).
    • (2002) Free Radic. Rial. Med , vol.33 , pp. 1141-1152
    • Bowler, R.P.1
  • 310
    • 33846974038 scopus 로고    scopus 로고
    • MnTBAP. a synthetic metalloporphyrin, inhibits production of tumor necrosis factor-α in lipopolysaccharide-stimulated RAW 264.7 macrophages cells via inhibiting oxidative stress-mediating p38 and SAPK/JNK signaling
    • Tumurkhuu, G. et al. MnTBAP. a synthetic metalloporphyrin, inhibits production of tumor necrosis factor-α in lipopolysaccharide-stimulated RAW 264.7 macrophages cells via inhibiting oxidative stress-mediating p38 and SAPK/JNK signaling. FEMS Immunol. Med. Microbiol. 49, 304-311 (2007).
    • (2007) FEMS Immunol. Med. Microbiol , vol.49 , pp. 304-311
    • Tumurkhuu, G.1


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