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Volumn 25, Issue 3-4, 2003, Pages 375-396

Protein oxidation at the air-lung interface

Author keywords

tocopherol; Air pollution; Ascorbic acid; Glutathione; Lung; Protein carbonyl; Respiratory tract lining fluid

Indexed keywords

ALPHA TOCOPHEROL; ASCORBIC ACID; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 0346731071     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-003-0024-x     Document Type: Review
Times cited : (95)

References (269)
  • 3
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: A hypothesis
    • Ames BN, Cathcart R, Schwiers E, Hochstein P (1981) Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. Proc Natl Acad Sci USA 78: 6858-6862
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 6
    • 0033773687 scopus 로고    scopus 로고
    • Ozone, but not nitrogen dioxide, exposure decreases glutathione peroxidases in epithelial lining fluid of human lung
    • Avissar NE, Reed CK, Cox C, Frampton MW, Finkelstein JN (2000) Ozone, but not nitrogen dioxide, exposure decreases glutathione peroxidases in epithelial lining fluid of human lung. Am J Respir Crit Care Med 162: 1342-1347
    • (2000) Am J Respir Crit Care Med , vol.162 , pp. 1342-1347
    • Avissar, N.E.1    Reed, C.K.2    Cox, C.3    Frampton, M.W.4    Finkelstein, J.N.5
  • 7
    • 0032584017 scopus 로고    scopus 로고
    • Protein oxidation biomarkers in hyperoxic lung injury in rats: Effects of U-74389
    • Awasthi S, Gyurasics A, Knight SA, Welty SE, Smith CV (1998) Protein oxidation biomarkers in hyperoxic lung injury in rats: effects of U-74389. Toxicol Lett 95: 47-61
    • (1998) Toxicol Lett , vol.95 , pp. 47-61
    • Awasthi, S.1    Gyurasics, A.2    Knight, S.A.3    Welty, S.E.4    Smith, C.V.5
  • 8
    • 0034725724 scopus 로고    scopus 로고
    • Phagocytes and oxidative stress
    • Babior BM (2000) Phagocytes and oxidative stress. Am J Med 109: 33-44
    • (2000) Am J Med , vol.109 , pp. 33-44
    • Babior, B.M.1
  • 10
    • 0035010171 scopus 로고    scopus 로고
    • Increased nitric oxide metabolites in exhaled breath condensate after exposure to tobacco smoke
    • Balint B, Donnelly LE, Hanazawa T, Kharitonov SA, Barnes PJ (2001) Increased nitric oxide metabolites in exhaled breath condensate after exposure to tobacco smoke. Thorax 56: 456-461
    • (2001) Thorax , vol.56 , pp. 456-461
    • Balint, B.1    Donnelly, L.E.2    Hanazawa, T.3    Kharitonov, S.A.4    Barnes, P.J.5
  • 12
    • 0027160479 scopus 로고
    • Towards the physiological function of uric acid
    • Becker BF (1993) Towards the physiological function of uric acid. Free Radic Biol Med 14: 615-631
    • (1993) Free Radic Biol Med , vol.14 , pp. 615-631
    • Becker, B.F.1
  • 13
    • 0028881049 scopus 로고
    • Inhibition of human glutathione reductase by S-nitrosoglutathione
    • Becker K, Gui M, Schirmer RH (1995) Inhibition of human glutathione reductase by S-nitrosoglutathione. Eur J Biochem 234: 472-478
    • (1995) Eur J Biochem , vol.234 , pp. 472-478
    • Becker, K.1    Gui, M.2    Schirmer, R.H.3
  • 15
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman JS, Koppenol WH (1996) Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 271: C1424-C1437
    • (1996) Am J Physiol , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 16
    • 0025189864 scopus 로고
    • Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide
    • Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman BA (1990) Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc Natl Acad Sci USA 87: 1620-1624
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1620-1624
    • Beckman, J.S.1    Beckman, T.W.2    Chen, J.3    Marshall, P.A.4    Freeman, B.A.5
  • 18
    • 0034657351 scopus 로고    scopus 로고
    • Evidence for oxidative stress in bronchiolitis obliterans syndrome after lung and heart-lung transplantation
    • The Munich Lung Transplant Group
    • Behr J, Maier K, Braun B, Schwaiblmair M, Vogelmeier C (2000) Evidence for oxidative stress in bronchiolitis obliterans syndrome after lung and heart-lung transplantation. The Munich Lung Transplant Group. Transplantation 69: 1856-1860
    • (2000) Transplantation , vol.69 , pp. 1856-1860
    • Behr, J.1    Maier, K.2    Braun, B.3    Schwaiblmair, M.4    Vogelmeier, C.5
  • 20
    • 0019404355 scopus 로고
    • Plasma proteins of the bronchoalveolar surface of the lungs of smokers and nonsmokers
    • Bell DY, Haseman JA, Spock A, McLennan G, Hook GE (1981) Plasma proteins of the bronchoalveolar surface of the lungs of smokers and nonsmokers. Am Rev Respir Dis 124: 72-79
    • (1981) Am Rev Respir Dis , vol.124 , pp. 72-79
    • Bell, D.Y.1    Haseman, J.A.2    Spock, A.3    McLennan, G.4    Hook, G.E.5
  • 21
    • 0030070186 scopus 로고    scopus 로고
    • Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin
    • Berlett BS, Levine RL, Stadtman ER (1996) Comparison of the effects of ozone on the modification of amino acid residues in glutamine synthetase and bovine serum albumin. J Biol Chem 271: 4177-4182
    • (1996) J Biol Chem , vol.271 , pp. 4177-4182
    • Berlett, B.S.1    Levine, R.L.2    Stadtman, E.R.3
  • 23
    • 0028220671 scopus 로고
    • Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle
    • Bolotina VM, Najibi S, Palacino JJ, Pagano PJ, Cohen RA (1994) Nitric oxide directly activates calcium-dependent potassium channels in vascular smooth muscle. Nature 368: 850-853
    • (1994) Nature , vol.368 , pp. 850-853
    • Bolotina, V.M.1    Najibi, S.2    Palacino, J.J.3    Pagano, P.J.4    Cohen, R.A.5
  • 24
    • 0037054861 scopus 로고    scopus 로고
    • Responses of normal and sickle cell hemoglobin to S-nitroscysteine: Implications for therapeutic applications of NO in treatment of sickle cell disease
    • Bonaventura C, Godette G, Ferruzzi G, Tesh S, Stevens RD, Henkens R (2002) Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease. Biophys Chem 98: 165-181
    • (2002) Biophys Chem , vol.98 , pp. 165-181
    • Bonaventura, C.1    Godette, G.2    Ferruzzi, G.3    Tesh, S.4    Stevens, R.D.5    Henkens, R.6
  • 25
    • 0028064657 scopus 로고
    • Oxidized mucus proteinase inhibitor: A fairly potent neutrophil elastase inhibitor
    • Boudier C, Bieth JG (1994) Oxidized mucus proteinase inhibitor: a fairly potent neutrophil elastase inhibitor. Biochem J 303 (Pt 1): 61-68
    • (1994) Biochem J , vol.303 , Issue.1 PART , pp. 61-68
    • Boudier, C.1    Bieth, J.G.2
  • 26
    • 0036127848 scopus 로고    scopus 로고
    • From pollutant gas to biological messenger: The diverse actions of nitric oxide in cancer
    • Brennan PA, Moncada S (2002) From pollutant gas to biological messenger: the diverse actions of nitric oxide in cancer. Ann R Coll Surg Engl 84: 75-78
    • (2002) Ann R Coll Surg Engl , vol.84 , pp. 75-78
    • Brennan, P.A.1    Moncada, S.2
  • 27
    • 0020582583 scopus 로고
    • Biochemistry and physiological role of methionine sulfoxide residues in proteins
    • Brot N, Weissbach H (1983) Biochemistry and physiological role of methionine sulfoxide residues in proteins. Arch Biochem Biophys 223: 271-281
    • (1983) Arch Biochem Biophys , vol.223 , pp. 271-281
    • Brot, N.1    Weissbach, H.2
  • 28
    • 0033963933 scopus 로고    scopus 로고
    • Depletion of glutathione and ascorbate in lung lining fluid by respirable fibres
    • Brown DM, Beswick PH, Bell KS, Donaldson K (2000) Depletion of glutathione and ascorbate in lung lining fluid by respirable fibres. Ann Occup Hyg 44: 101-108
    • (2000) Ann Occup Hyg , vol.44 , pp. 101-108
    • Brown, D.M.1    Beswick, P.H.2    Bell, K.S.3    Donaldson, K.4
  • 29
    • 0027469054 scopus 로고
    • Ascorbate free radical as a marker of oxidative stress: An EPR study
    • Buettner GR, Jurkiewicz BA (1993) Ascorbate free radical as a marker of oxidative stress: an EPR study. Free Radic Biol Med 14: 49-55
    • (1993) Free Radic Biol Med , vol.14 , pp. 49-55
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 30
    • 0029939394 scopus 로고    scopus 로고
    • Catalytic metals, ascorbate and free radicals: Combinations to avoid
    • Buettner GR, Jurkiewicz BA (1996) Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat Res 145: 532-541
    • (1996) Radiat Res , vol.145 , pp. 532-541
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 31
    • 0027331598 scopus 로고
    • Oxidized glutathione is increased in the alveolar fluid of patients with the adult respiratory distress syndrome
    • Bunnell E, Pacht ER (1993) Oxidized glutathione is increased in the alveolar fluid of patients with the adult respiratory distress syndrome. Am Rev Respir Dis 148: 1174-1178
    • (1993) Am Rev Respir Dis , vol.148 , pp. 1174-1178
    • Bunnell, E.1    Pacht, E.R.2
  • 32
    • 0019750550 scopus 로고
    • An improved procedure for the isolation of ghost membranes from human red blood cells
    • Burton GW, Ingold KU, Thompson KE (1981) An improved procedure for the isolation of ghost membranes from human red blood cells. Lipids 16: 946-947
    • (1981) Lipids , vol.16 , pp. 946-947
    • Burton, G.W.1    Ingold, K.U.2    Thompson, K.E.3
  • 34
    • 0034062242 scopus 로고    scopus 로고
    • Elevated protein carbonyls and lipid peroxidation products correlating with myeloperoxidase in tracheal aspirates from premature infants
    • Buss IH, Darlow BA, Winterbourn CC (2000) Elevated protein carbonyls and lipid peroxidation products correlating with myeloperoxidase in tracheal aspirates from premature infants. Pediatr Res 47: 640-645
    • (2000) Pediatr Res , vol.47 , pp. 640-645
    • Buss, I.H.1    Darlow, B.A.2    Winterbourn, C.C.3
  • 35
    • 0023263523 scopus 로고
    • Normal alveolar epithelial lining fluid contains high levels of glutathione
    • Cantin AM, North SL, Hubbard RC, Crystal RG (1987) Normal alveolar epithelial lining fluid contains high levels of glutathione. J Appl Physiol 63: 152-157
    • (1987) J Appl Physiol , vol.63 , pp. 152-157
    • Cantin, A.M.1    North, S.L.2    Hubbard, R.C.3    Crystal, R.G.4
  • 36
    • 0024578662 scopus 로고
    • Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis
    • Cantin AM, Hubbard RC, Crystal RG (1989) Glutathione deficiency in the epithelial lining fluid of the lower respiratory tract in idiopathic pulmonary fibrosis. Am Rev Respir Dis 139: 370-372
    • (1989) Am Rev Respir Dis , vol.139 , pp. 370-372
    • Cantin, A.M.1    Hubbard, R.C.2    Crystal, R.G.3
  • 38
    • 0021942070 scopus 로고
    • Human eosinophil peroxidase: Purification and characterization
    • Carlson MG, Peterson CG, Venge P (1985) Human eosinophil peroxidase: purification and characterization. J Immunol 134: 1875-1879
    • (1985) J Immunol , vol.134 , pp. 1875-1879
    • Carlson, M.G.1    Peterson, C.G.2    Venge, P.3
  • 39
    • 0020622108 scopus 로고
    • Human methionine sulfoxide-peptide reductase, an enzyme capable of reactivating oxidized alpha-1-proteinase inhibitor in vitro
    • Carp H, Janoff A, Abrams W, Weinbaum G, Drew RT, Weissbach H, Brot N (1983) Human methionine sulfoxide-peptide reductase, an enzyme capable of reactivating oxidized alpha-1-proteinase inhibitor in vitro. Am Rev Respir Dis 127: 301-305
    • (1983) Am Rev Respir Dis , vol.127 , pp. 301-305
    • Carp, H.1    Janoff, A.2    Abrams, W.3    Weinbaum, G.4    Drew, R.T.5    Weissbach, H.6    Brot, N.7
  • 41
    • 0028355875 scopus 로고
    • Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils
    • Chai YC, Hendrich S, Thomas JA (1994) Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch Biochem Biophys 310: 264-272
    • (1994) Arch Biochem Biophys , vol.310 , pp. 264-272
    • Chai, Y.C.1    Hendrich, S.2    Thomas, J.A.3
  • 43
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • Chao CC, Ma YS, Stadtman ER (1997) Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc Natl Acad Sci USA 94: 2969-2974
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2969-2974
    • Chao, C.C.1    Ma, Y.S.2    Stadtman, E.R.3
  • 44
    • 0034685015 scopus 로고    scopus 로고
    • Nitric oxide nitrates tyrosine residues of tumor-suppressor p53 protein in MCF-7 cells
    • Chazotte-Aubert L, Hainaut P, Ohshima H (2000) Nitric oxide nitrates tyrosine residues of tumor-suppressor p53 protein in MCF-7 cells. Biochem Biophys Res Commun 267: 609-613
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 609-613
    • Chazotte-Aubert, L.1    Hainaut, P.2    Ohshima, H.3
  • 45
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne A, Miller H, Parsonage D, Ross RP (1993) Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. Faseb J 7: 1483-1490
    • (1993) Faseb J , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 47
    • 0024286643 scopus 로고
    • The Meisenheimer complex of glutathione and trinitrobenzene. A potent inhibitor of the glutathione S-transferase from Galleria mellonella
    • Clark AG, Sinclair M (1988) The Meisenheimer complex of glutathione and trinitrobenzene. A potent inhibitor of the glutathione S-transferase from Galleria mellonella. Biochem Pharmacol 37: 259-263
    • (1988) Biochem Pharmacol , vol.37 , pp. 259-263
    • Clark, A.G.1    Sinclair, M.2
  • 48
    • 0032993093 scopus 로고    scopus 로고
    • Increased glutathione and glutathione peroxidase in lungs of individuals with chronic beryllium disease
    • Comhair SA, Lewis MJ, Bhathena PR, Hammel JP, Erzurum SC (1999) Increased glutathione and glutathione peroxidase in lungs of individuals with chronic beryllium disease. Am J Respir Crit Care Med 159: 1824-1829
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 1824-1829
    • Comhair, S.A.1    Lewis, M.J.2    Bhathena, P.R.3    Hammel, J.P.4    Erzurum, S.C.5
  • 49
    • 0343920015 scopus 로고    scopus 로고
    • Rapid loss of superoxide dismutase activity during antigen-induced asthmatic response
    • Comhair SA, Bhathena PR, Dweik RA, Kavuru M, Erzurum SC (2000) Rapid loss of superoxide dismutase activity during antigen-induced asthmatic response. Lancet 355: 624-625
    • (2000) Lancet , vol.355 , pp. 624-625
    • Comhair, S.A.1    Bhathena, P.R.2    Dweik, R.A.3    Kavuru, M.4    Erzurum, S.C.5
  • 50
    • 9044240863 scopus 로고    scopus 로고
    • Health effects of outdoor air pollution
    • Committee of the Environmental and Occupational Health Assembly of the American Thoracic Society (1996) Health effects of outdoor air pollution. Am J Respir Crit Care Med 153: 3-50
    • (1996) Am J Respir Crit Care Med , vol.153 , pp. 3-50
  • 51
    • 0030130524 scopus 로고    scopus 로고
    • Inflammation, free radicals, and antioxidants
    • Conner EM, Grisham MB (1996) Inflammation, free radicals, and antioxidants. Nutrition 12: 274-277
    • (1996) Nutrition , vol.12 , pp. 274-277
    • Conner, E.M.1    Grisham, M.B.2
  • 54
    • 0017912973 scopus 로고
    • Constituents of mucus and their separation
    • Creeth JM (1978) Constituents of mucus and their separation. Br Med Bull 34: 17-24
    • (1978) Br Med Bull , vol.34 , pp. 17-24
    • Creeth, J.M.1
  • 57
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies MJ, Fu S, Wang H, Dean RT (1999) Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radic Biol Med 27 1151-1163
    • (1999) Free Radic Biol Med , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3    Dean, R.T.4
  • 59
    • 0027482738 scopus 로고
    • Reactive species and their accumulation on radical-damaged proteins
    • Dean RT, Gieseg S, Davies MJ (1993) Reactive species and their accumulation on radical-damaged proteins. Trends Biochem Sci 18: 437-441
    • (1993) Trends Biochem Sci , vol.18 , pp. 437-441
    • Dean, R.T.1    Gieseg, S.2    Davies, M.J.3
  • 61
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi M, Shringarpure R, Davies KJ (2001) Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch Biochem Biophys 389: 254-263
    • (2001) Arch Biochem Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.3
  • 62
    • 0026509071 scopus 로고
    • The ultrastructural immunolocalization of gamma-glutamyltranspeptidase in rat lung: Correlation with the histochemical demonstration of enzyme activity
    • Dinsdale D, Green JA, Manson MM, Lee MJ (1992) The ultrastructural immunolocalization of gamma-glutamyltranspeptidase in rat lung: correlation with the histochemical demonstration of enzyme activity. Histochem J 24: 144-152
    • (1992) Histochem J , vol.24 , pp. 144-152
    • Dinsdale, D.1    Green, J.A.2    Manson, M.M.3    Lee, M.J.4
  • 64
    • 0030881017 scopus 로고    scopus 로고
    • Estimation of thickness of airway surface liquid in ferret trachea in vitro
    • Duneclift S, Wells U, Widdicombe J (1997) Estimation of thickness of airway surface liquid in ferret trachea in vitro. J Appl Physiol 83: 761-767
    • (1997) J Appl Physiol , vol.83 , pp. 761-767
    • Duneclift, S.1    Wells, U.2    Widdicombe, J.3
  • 65
    • 0034939772 scopus 로고    scopus 로고
    • Lipid hydroperoxide modification of proteins during myocardial ischaemia
    • Eaton P, Hearse DJ, Shattock MJ (2001) Lipid hydroperoxide modification of proteins during myocardial ischaemia. Cardiovasc Res 51: 294-303
    • (2001) Cardiovasc Res , vol.51 , pp. 294-303
    • Eaton, P.1    Hearse, D.J.2    Shattock, M.J.3
  • 66
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • Eaton P, Byers HL, Leeds N, Ward MA, Shattock MJ (2002) Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277: 9806-9811
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 68
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: A nitric oxide-dependent mechanism of cellular injury
    • Eiserich JP, Estevez AG, Bamberg TV, Ye YZ, Chumley PH, Beckman JS, Freeman BA (1999) Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc Natl Acad Sci USA 96: 6365-6370
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1    Estevez, A.G.2    Bamberg, T.V.3    Ye, Y.Z.4    Chumley, P.H.5    Beckman, J.S.6    Freeman, B.A.7
  • 69
    • 0029788914 scopus 로고    scopus 로고
    • Human eotaxin represents a potent activator of the respiratory burst of human eosinophils
    • Elsner J, Hochstetter R, Kimmig D, Kapp A (1996) Human eotaxin represents a potent activator of the respiratory burst of human eosinophils. Eur J Immunol 26: 1919-1925
    • (1996) Eur J Immunol , vol.26 , pp. 1919-1925
    • Elsner, J.1    Hochstetter, R.2    Kimmig, D.3    Kapp, A.4
  • 70
    • 0034124568 scopus 로고    scopus 로고
    • New aspects of degranulation and fates of airway mucosal eosinophils
    • Erjefalt JS, Persson CG (2000) New aspects of degranulation and fates of airway mucosal eosinophils. Am J Respir Crit Care Med 161: 2074-2085
    • (2000) Am J Respir Crit Care Med , vol.161 , pp. 2074-2085
    • Erjefalt, J.S.1    Persson, C.G.2
  • 71
    • 0032557581 scopus 로고    scopus 로고
    • Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells
    • Figueiredo-Pereira ME, Yakushin S, Cohen G (1998) Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells. J Biol Chem 273: 12703-12709
    • (1998) J Biol Chem , vol.273 , pp. 12703-12709
    • Figueiredo-Pereira, M.E.1    Yakushin, S.2    Cohen, G.3
  • 72
    • 0020702109 scopus 로고
    • Assessment of chlorination by human neutrophils
    • Foote CS, Goyne TE, Lehrer RI (1983) Assessment of chlorination by human neutrophils. Nature 301: 715-716
    • (1983) Nature , vol.301 , pp. 715-716
    • Foote, C.S.1    Goyne, T.E.2    Lehrer, R.I.3
  • 73
    • 0032964497 scopus 로고    scopus 로고
    • Role of the eosinophil in protein oxidation in asthma: Possible effects on proteinase/antiproteinase balance
    • Foreman RC, Mercer PF, Kroegel C, Warner JA (1999) Role of the eosinophil in protein oxidation in asthma: possible effects on proteinase/antiproteinase balance. Int Arch Allergy Immunol 118: 183-186
    • (1999) Int Arch Allergy Immunol , vol.118 , pp. 183-186
    • Foreman, R.C.1    Mercer, P.F.2    Kroegel, C.3    Warner, J.A.4
  • 74
    • 0032732641 scopus 로고    scopus 로고
    • Antioxidant transport modulates peripheral airway reactivity and inflammation during ozone exposure
    • Freed AN, Cueto R, Pryor WA (1999) Antioxidant transport modulates peripheral airway reactivity and inflammation during ozone exposure. J Appl Physiol 87: 1595-1603
    • (1999) J Appl Physiol , vol.87 , pp. 1595-1603
    • Freed, A.N.1    Cueto, R.2    Pryor, W.A.3
  • 75
    • 0001218860 scopus 로고
    • Ascorbate is an outstanding antioxidant in human blood plasma
    • Frei B, England L, Ames BN (1989) Ascorbate is an outstanding antioxidant in human blood plasma. Proc Natl Acad Sci USA 86: 6377-6381
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6377-6381
    • Frei, B.1    England, L.2    Ames, B.N.3
  • 77
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • Gardner PR, Raineri J, Epstein LB, White CW (1995) Superoxide radical and iron modulate aconitase activity in mammalian cells. J Biol Chem 270: 13399-13405
    • (1995) J Biol Chem , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, J.2    Epstein, L.B.3    White, C.W.4
  • 79
    • 0024495466 scopus 로고
    • Inactivation of alpha 2-antiplasmin by limited reaction with cis-dichlorodiammineplatinum (II)
    • Geary WA, Gonias SL (1989) Inactivation of alpha 2-antiplasmin by limited reaction with cis-dichlorodiammineplatinum (II). Biochim Biophys Acta 994: 1-6
    • (1989) Biochim Biophys Acta , vol.994 , pp. 1-6
    • Geary, W.A.1    Gonias, S.L.2
  • 80
    • 0035881065 scopus 로고    scopus 로고
    • Inflammatory lung injury after bronchial instillation of air pollution particles
    • Ghio AJ, Devlin RB (2001) Inflammatory lung injury after bronchial instillation of air pollution particles. Am J Respir Crit Care Med 164: 704-708
    • (2001) Am J Respir Crit Care Med , vol.164 , pp. 704-708
    • Ghio, A.J.1    Devlin, R.B.2
  • 82
    • 0027319565 scopus 로고
    • Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins
    • Gieseg SP, Simpson JA, Charlton TS, Duncan MW, Dean RT (1993) Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry 32: 4780-4786
    • (1993) Biochemistry , vol.32 , pp. 4780-4786
    • Gieseg, S.P.1    Simpson, J.A.2    Charlton, T.S.3    Duncan, M.W.4    Dean, R.T.5
  • 83
    • 0028283298 scopus 로고
    • Dityrosine: A marker for oxidatively modified proteins and selective proteolysis
    • Giulivi C, Davies KJ (1994) Dityrosine: a marker for oxidatively modified proteins and selective proteolysis. Methods Enzymol 233: 363-371
    • (1994) Methods Enzymol , vol.233 , pp. 363-371
    • Giulivi, C.1    Davies, K.J.2
  • 85
    • 0035131144 scopus 로고    scopus 로고
    • Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions
    • Grant CM (2001) Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions. Mol Microbiol 39: 533-541
    • (2001) Mol Microbiol , vol.39 , pp. 533-541
    • Grant, C.M.1
  • 86
    • 0030758774 scopus 로고    scopus 로고
    • Nitric oxide trapping of the tyrosyl radical of prostaglandin H synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation
    • Gunther MR, Hsi LC, Curtis JF, Gierse JK, Marnett LJ, Eling TE, Mason RP (1997) Nitric oxide trapping of the tyrosyl radical of prostaglandin H synthase-2 leads to tyrosine iminoxyl radical and nitrotyrosine formation. J Biol Chem 272: 17086-17090
    • (1997) J Biol Chem , vol.272 , pp. 17086-17090
    • Gunther, M.R.1    Hsi, L.C.2    Curtis, J.F.3    Gierse, J.K.4    Marnett, L.J.5    Eling, T.E.6    Mason, R.P.7
  • 87
    • 0029893572 scopus 로고    scopus 로고
    • Prooxidant iron is present in human pulmonary epithelial lining fluid: Implications for oxidative stress in the lung
    • Gutteridge JM, Mumby S, Quinlan GJ, Chung KF, Evans TW (1996) Prooxidant iron is present in human pulmonary epithelial lining fluid: implications for oxidative stress in the lung. Biochem Biophys Res Commun 220: 1024-1027
    • (1996) Biochem Biophys Res Commun , vol.220 , pp. 1024-1027
    • Gutteridge, J.M.1    Mumby, S.2    Quinlan, G.J.3    Chung, K.F.4    Evans, T.W.5
  • 89
    • 0028007172 scopus 로고
    • Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury
    • Haddad IY, Pataki G, Hu P, Galliani C, Beckman JS, Matalon S (1994) Quantitation of nitrotyrosine levels in lung sections of patients and animals with acute lung injury. J Clin Invest 94: 2407-2413
    • (1994) J Clin Invest , vol.94 , pp. 2407-2413
    • Haddad, I.Y.1    Pataki, G.2    Hu, P.3    Galliani, C.4    Beckman, J.S.5    Matalon, S.6
  • 90
    • 0029995083 scopus 로고    scopus 로고
    • Nitration of surfactant protein A results in decreased ability to aggregate lipids
    • Haddad IY, Zhu S, Ischiropoulos H, Matalon S (1996) Nitration of surfactant protein A results in decreased ability to aggregate lipids. Am J Physiol 270: L281-288
    • (1996) Am J Physiol , vol.270
    • Haddad, I.Y.1    Zhu, S.2    Ischiropoulos, H.3    Matalon, S.4
  • 91
    • 0032715834 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: A personal view of recent controversies
    • Halliwell B, Zhao K, Whiteman M (1999) Nitric oxide and peroxynitrite. The ugly, the uglier and the not so good: a personal view of recent controversies. Free Radic Res 31: 651-669
    • (1999) Free Radic Res , vol.31 , pp. 651-669
    • Halliwell, B.1    Zhao, K.2    Whiteman, M.3
  • 93
    • 0033582342 scopus 로고    scopus 로고
    • Thiolation of the gammaB-crystallins in intact bovine lens exposed to hydrogen peroxide
    • Hanson SR, Chen AA, Smith JB, Lou MF (1999) Thiolation of the gammaB-crystallins in intact bovine lens exposed to hydrogen peroxide. J Biol Chem 274: 4735-4742
    • (1999) J Biol Chem , vol.274 , pp. 4735-4742
    • Hanson, S.R.1    Chen, A.A.2    Smith, J.B.3    Lou, M.F.4
  • 94
    • 0036479238 scopus 로고    scopus 로고
    • Selective nitration of histone tyrosine residues in vivo in mutatect tumors
    • Haqqani AS, Kelly JF, Birnboim HC (2002) Selective nitration of histone tyrosine residues in vivo in mutatect tumors. J Biol Chem 277: 3614-3621
    • (2002) J Biol Chem , vol.277 , pp. 3614-3621
    • Haqqani, A.S.1    Kelly, J.F.2    Birnboim, H.C.3
  • 95
    • 0028141628 scopus 로고
    • Iron release from ferritin and its sensitivity to superoxide ions differs among vertebrates
    • Harris LR, Cake MH, Macey DJ (1994) Iron release from ferritin and its sensitivity to superoxide ions differs among vertebrates. Biochem J 301 (Pt 2): 385-389
    • (1994) Biochem J , vol.301 , Issue.2 PART , pp. 385-389
    • Harris, L.R.1    Cake, M.H.2    Macey, D.J.3
  • 96
    • 0032824515 scopus 로고    scopus 로고
    • Report of ERS Task Force: Guidelines for measurement of acellular components and standardization of BAL
    • Haslam PL, Baughman RP (1999) Report of ERS Task Force: guidelines for measurement of acellular components and standardization of BAL. Eur Respir J 14: 245-248
    • (1999) Eur Respir J , vol.14 , pp. 245-248
    • Haslam, P.L.1    Baughman, R.P.2
  • 97
    • 0000906101 scopus 로고
    • Comparative biochemistry of airway lining fluid
    • Parent R (ed). CRC Press, Baton Rouge, Louisiana
    • Hatch G (1992) Comparative biochemistry of airway lining fluid. In: Parent R (ed) Treatise on pulmonary toxicology. Comparative biology of the normal lung. VoI 1. CRC Press, Baton Rouge, Louisiana, pp 617-632
    • (1992) Treatise on Pulmonary Toxicology. Comparative Biology of the Normal Lung , vol.1 , pp. 617-632
    • Hatch, G.1
  • 98
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen A, Fridovich I (1994) Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J Biol Chem 269: 29405-29408
    • (1994) J Biol Chem , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 99
    • 0024421581 scopus 로고
    • Pulmonary strategies of antioxidant defense
    • Heffner JE, Repine JE (1989) Pulmonary strategies of antioxidant defense. Am Rev Respir Dis 140: 531-554
    • (1989) Am Rev Respir Dis , vol.140 , pp. 531-554
    • Heffner, J.E.1    Repine, J.E.2
  • 100
    • 0030708895 scopus 로고    scopus 로고
    • Pathways for oxidation of low density lipoprotein by myeloperoxidase: Tyrosyl radical, reactive aldehydes, hypochlorous acid and molecular chlorine
    • Heinecke JW (1997) Pathways for oxidation of low density lipoprotein by myeloperoxidase: tyrosyl radical, reactive aldehydes, hypochlorous acid and molecular chlorine. Biofactors 6: 145-155
    • (1997) Biofactors , vol.6 , pp. 145-155
    • Heinecke, J.W.1
  • 101
    • 0022988477 scopus 로고
    • The ubiquitin pathway for the degradation of intracellular proteins
    • Hershko A, Ciechanover A (1986) The ubiquitin pathway for the degradation of intracellular proteins. Prog Nucleic Acid Res Mol Biol 33: 19-56
    • (1986) Prog Nucleic Acid Res Mol Biol , vol.33 , pp. 19-56
    • Hershko, A.1    Ciechanover, A.2
  • 103
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N (2002) The biochemistry and physiology of S-nitrosothiols. Annu Rev Pharmacol Toxicol 42: 585-600
    • (2002) Annu Rev Pharmacol Toxicol , vol.42 , pp. 585-600
    • Hogg, N.1
  • 104
    • 0023117404 scopus 로고
    • Glutathione biosynthesis from sulfur-containing amino acids in enriched populations of Clara and type II cells and macrophages freshly isolated from rabbit lung
    • Horton JK, Meredith MJ, Bend JR (1987) Glutathione biosynthesis from sulfur-containing amino acids in enriched populations of Clara and type II cells and macrophages freshly isolated from rabbit lung. J Pharmacol Exp Ther 240: 376-380
    • (1987) J Pharmacol Exp Ther , vol.240 , pp. 376-380
    • Horton, J.K.1    Meredith, M.J.2    Bend, J.R.3
  • 105
    • 0025600464 scopus 로고
    • Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload
    • Houglum K, Filip M, Witztum JL, Chojkier M (1990) Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload. J Clin Invest 86: 1991-1998
    • (1990) J Clin Invest , vol.86 , pp. 1991-1998
    • Houglum, K.1    Filip, M.2    Witztum, J.L.3    Chojkier, M.4
  • 107
    • 0029744078 scopus 로고    scopus 로고
    • Gender difference in the concentration of the antioxidant uric acid in human nasal lavage
    • Housley DG, Eccles R, Richards RJ (1996) Gender difference in the concentration of the antioxidant uric acid in human nasal lavage. Acta Otolaryngol 116: 751-754
    • (1996) Acta Otolaryngol , vol.116 , pp. 751-754
    • Housley, D.G.1    Eccles, R.2    Richards, R.J.3
  • 108
    • 0028201059 scopus 로고
    • Peroxynitrite inhibition of oxygen consumption and sodium transport in alveolar type II cells
    • Hu P, Ischiropoulos H, Beckman JS, Matalon S (1994) Peroxynitrite inhibition of oxygen consumption and sodium transport in alveolar type II cells. Am J Physiol 266: L628-L634
    • (1994) Am J Physiol , vol.266
    • Hu, P.1    Ischiropoulos, H.2    Beckman, J.S.3    Matalon, S.4
  • 109
    • 0027180882 scopus 로고
    • Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation
    • Huggins TG, Wells-Knecht MC, Detorie NA, Baynes JW, Thorpe SR (1993) Formation of o-tyrosine and dityrosine in proteins during radiolytic and metal-catalyzed oxidation. J Biol Chem 268: 12341-12347
    • (1993) J Biol Chem , vol.268 , pp. 12341-12347
    • Huggins, T.G.1    Wells-Knecht, M.C.2    Detorie, N.A.3    Baynes, J.W.4    Thorpe, S.R.5
  • 111
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • Ischiropoulos H, Zhu L, Beckman JS (1992) Peroxynitrite formation from macrophage-derived nitric oxide. Arch Biochem Biophys 298: 446-451
    • (1992) Arch Biochem Biophys , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 112
    • 0029129972 scopus 로고
    • Reactive species in ischemic rat lung injury: Contribution of peroxynitrite
    • Ischiropoulos H, al-Mehdi AB, Fisher AB (1995) Reactive species in ischemic rat lung injury: contribution of peroxynitrite. Am J Physiol 269: L158-L164
    • (1995) Am J Physiol , vol.269
    • Ischiropoulos, H.1    Al-Mehdi, A.B.2    Fisher, A.B.3
  • 113
    • 0018800894 scopus 로고
    • The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center
    • Johnson D, Travis J (1979) The oxidative inactivation of human alpha-1-proteinase inhibitor. Further evidence for methionine at the reactive center. J Biol Chem 254: 4022-4026
    • (1979) J Biol Chem , vol.254 , pp. 4022-4026
    • Johnson, D.1    Travis, J.2
  • 114
    • 0035482240 scopus 로고    scopus 로고
    • The tolerability, safety, and success of sputum induction and combined hypertonic saline challenge in children
    • Jones PD, Hankin R, Simpson J, Gibson PG, Henry RL (2001) The tolerability, safety, and success of sputum induction and combined hypertonic saline challenge in children. AmJ Respir Crit Care Med 164: 1146-1149
    • (2001) AmJ Respir Crit Care Med , vol.164 , pp. 1146-1149
    • Jones, P.D.1    Hankin, R.2    Simpson, J.3    Gibson, P.G.4    Henry, R.L.5
  • 115
    • 0018869987 scopus 로고
    • Bactericidal activity of eosinophil peroxidase
    • Jong EC, Henderson WR, Klebanoff SJ (1980) Bactericidal activity of eosinophil peroxidase. J Immunol 124: 1378-1382
    • (1980) J Immunol , vol.124 , pp. 1378-1382
    • Jong, E.C.1    Henderson, W.R.2    Klebanoff, S.J.3
  • 116
    • 0014429904 scopus 로고
    • Selective and reversible photo-oxidation of the methionyl residues in lysozyme
    • Jori G, Galiazzo G, Marzotto A, Scoffone E (1968) Selective and reversible photo-oxidation of the methionyl residues in lysozyme. J Biol Chem 243: 4272-4278
    • (1968) J Biol Chem , vol.243 , pp. 4272-4278
    • Jori, G.1    Galiazzo, G.2    Marzotto, A.3    Scoffone, E.4
  • 118
    • 0029438532 scopus 로고
    • Thiyl radicals in biological systems: Significant or trivial?
    • Kalyanaraman B (1995) Thiyl radicals in biological systems: significant or trivial? Biochem Soc Symp 61: 55-63
    • (1995) Biochem Soc Symp , vol.61 , pp. 55-63
    • Kalyanaraman, B.1
  • 121
    • 0029875931 scopus 로고    scopus 로고
    • The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins
    • Keck RG (1996) The use of t-butyl hydroperoxide as a probe for methionine oxidation in proteins. Anal Biochem 236: 56-62
    • (1996) Anal Biochem , vol.236 , pp. 56-62
    • Keck, R.G.1
  • 122
    • 0030479466 scopus 로고    scopus 로고
    • Antioxidant kinetics in lung lavage fluid following exposure of humans to nitrogen dioxide
    • Kelly FJ, Blomberg A, Frew A, Holgate ST, Sandstrom T (1996) Antioxidant kinetics in lung lavage fluid following exposure of humans to nitrogen dioxide. Am J Respir Crit Care Med 154: 1700-1705
    • (1996) Am J Respir Crit Care Med , vol.154 , pp. 1700-1705
    • Kelly, F.J.1    Blomberg, A.2    Frew, A.3    Holgate, S.T.4    Sandstrom, T.5
  • 123
    • 0030801588 scopus 로고    scopus 로고
    • Nitrogen dioxide depletes uric acid and ascorbic acid but not glutathione from lung lining fluid
    • Kelly FJ, Tetley TD (1997) Nitrogen dioxide depletes uric acid and ascorbic acid but not glutathione from lung lining fluid. Biochem J 325 (Pt 1): 95-99
    • (1997) Biochem J , vol.325 , Issue.1 PART , pp. 95-99
    • Kelly, F.J.1    Tetley, T.D.2
  • 124
    • 0030046117 scopus 로고    scopus 로고
    • Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
    • Kettle AJ (1996) Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett 379: 103-106
    • (1996) FEBS Lett , vol.379 , pp. 103-106
    • Kettle, A.J.1
  • 125
    • 0028240904 scopus 로고
    • Superoxide-dependent hydroxylation by myeloperoxidase
    • Kettle AJ, Winterbourn CC (1994) Superoxide-dependent hydroxylation by myeloperoxidase. J Biol Chem 269: 17146-17151
    • (1994) J Biol Chem , vol.269 , pp. 17146-17151
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 126
    • 0033768818 scopus 로고    scopus 로고
    • Clinical aspects of exhaled nitric oxide
    • Kharitonov SA, Barnes PJ (2000) Clinical aspects of exhaled nitric oxide. Eur Respir J 16: 781-792
    • (2000) Eur Respir J , vol.16 , pp. 781-792
    • Kharitonov, S.A.1    Barnes, P.J.2
  • 128
    • 0036146786 scopus 로고    scopus 로고
    • Biomarkers of some pulmonary diseases in exhaled breath
    • Kharitonov SA, Barnes PJ (2002) Biomarkers of some pulmonary diseases in exhaled breath. Biomarkers 7: 1-32
    • (2002) Biomarkers , vol.7 , pp. 1-32
    • Kharitonov, S.A.1    Barnes, P.J.2
  • 129
    • 0028803686 scopus 로고
    • Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen
    • Kharitonov VG, Sundquist AR, Sharma VS (1995) Kinetics of nitrosation of thiols by nitric oxide in the presence of oxygen. J Biol Chem 270: 28158-28164
    • (1995) J Biol Chem , vol.270 , pp. 28158-28164
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 130
    • 0031017415 scopus 로고    scopus 로고
    • Nasal nitric oxide is increased in patients with asthma and allergic rhinitis and may be modulated by nasal glucocorticoids
    • Kharitonov SA, Rajakulasingam K, O'Connor B, Durham SR, Barnes PJ (1997) Nasal nitric oxide is increased in patients with asthma and allergic rhinitis and may be modulated by nasal glucocorticoids. J Allergy Clin Immunol 99: 58-64
    • (1997) J Allergy Clin Immunol , vol.99 , pp. 58-64
    • Kharitonov, S.A.1    Rajakulasingam, K.2    O'Connor, B.3    Durham, S.R.4    Barnes, P.J.5
  • 132
    • 0033869092 scopus 로고    scopus 로고
    • Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress
    • Klatt P, Lamas S (2000) Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur J Biochem 267: 4928-4944
    • (2000) Eur J Biochem , vol.267 , pp. 4928-4944
    • Klatt, P.1    Lamas, S.2
  • 136
    • 0032880537 scopus 로고    scopus 로고
    • Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: Evidence for neutrophil-mediated hydroxylation, nitration, and chlorination
    • Lamb NJ, Gutteridge JM, Baker C, Evans TW, Quinlan GJ (1999) Oxidative damage to proteins of bronchoalveolar lavage fluid in patients with acute respiratory distress syndrome: evidence for neutrophil-mediated hydroxylation, nitration, and chlorination. Crit Care Med 27: 1738-1744
    • (1999) Crit Care Med , vol.27 , pp. 1738-1744
    • Lamb, N.J.1    Gutteridge, J.M.2    Baker, C.3    Evans, T.W.4    Quinlan, G.J.5
  • 137
    • 0028982274 scopus 로고
    • p21ras as a common signaling target of reactive free radicals and cellular redox stress
    • Lander HM, Ogiste JS, Teng KK, Novogrodsky A (1995) p21ras as a common signaling target of reactive free radicals and cellular redox stress. J Biol Chem 270 :21195-21198
    • (1995) J Biol Chem , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4
  • 138
    • 0029045103 scopus 로고
    • Ozone-reactive absorption by pulmonary epithelial lining fluid constituents
    • Langford SD, Bidani A, Postlethwait EM (1995) Ozone-reactive absorption by pulmonary epithelial lining fluid constituents. Toxicol Appl Pharmacol 132: 122-130
    • (1995) Toxicol Appl Pharmacol , vol.132 , pp. 122-130
    • Langford, S.D.1    Bidani, A.2    Postlethwait, E.M.3
  • 139
    • 0028181674 scopus 로고
    • Inhibition by nitric oxide of the repair protein, O6-methylguanine-DNA- methyltransferase
    • Laval F, Wink DA (1994) Inhibition by nitric oxide of the repair protein, O6-methylguanine-DNA-methyltransferase. Carcinogenesis 15: 443-447
    • (1994) Carcinogenesis , vol.15 , pp. 443-447
    • Laval, F.1    Wink, D.A.2
  • 140
    • 0027410677 scopus 로고
    • Bronchoalveolar lavage fluid proteins in human lung disease: Analysis by two-dimensional electrophoresis
    • Lenz AG, Meyer B, Costabel U, Maier K (1993) Bronchoalveolar lavage fluid proteins in human lung disease: analysis by two-dimensional electrophoresis. Electrophoresis 14: 242-244
    • (1993) Electrophoresis , vol.14 , pp. 242-244
    • Lenz, A.G.1    Meyer, B.2    Costabel, U.3    Maier, K.4
  • 141
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine RL, Moskovitz J, Stadtman ER (2000) Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 50: 301-307
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 142
    • 0029130138 scopus 로고
    • Two-dimensional gel electrophoresis of nasal and bronchoalveolar lavage fluids after occupational exposure
    • Lindahl M, Stahlbom B, Tagesson C (1995) Two-dimensional gel electrophoresis of nasal and bronchoalveolar lavage fluids after occupational exposure. Electrophoresis 16: 1199-1204
    • (1995) Electrophoresis , vol.16 , pp. 1199-1204
    • Lindahl, M.1    Stahlbom, B.2    Tagesson, C.3
  • 143
    • 0029804716 scopus 로고    scopus 로고
    • Two dimensional protein patterns of bronchoalveolar lavage fluid from non-smokers, smokers, and subjects exposed to asbestos
    • Lindahl M, Ekstrom T, Sorensen J, Tagesson C (1996) Two dimensional protein patterns of bronchoalveolar lavage fluid from non-smokers, smokers, and subjects exposed to asbestos. Thorax 51: 1028-1235
    • (1996) Thorax , vol.51 , pp. 1028-1235
    • Lindahl, M.1    Ekstrom, T.2    Sorensen, J.3    Tagesson, C.4
  • 144
    • 0032428443 scopus 로고    scopus 로고
    • Protein patterns of human nasal and bronchoalveolar lavage fluids analyzed with two-dimensional gel electrophoresis
    • Lindahl M, Stahlbom B, Svartz J, Tagesson C (1998) Protein patterns of human nasal and bronchoalveolar lavage fluids analyzed with two-dimensional gel electrophoresis. Electrophoresis 19: 3222-3229
    • (1998) Electrophoresis , vol.19 , pp. 3222-3229
    • Lindahl, M.1    Stahlbom, B.2    Svartz, J.3    Tagesson, C.4
  • 145
    • 0343049118 scopus 로고    scopus 로고
    • Newly identified proteins in human nasal and bronchoalveolar lavage fluids: Potential biomedical and clinical applications
    • Lindahl M, Stahlbom B, Tagesson C (1999a) Newly identified proteins in human nasal and bronchoalveolar lavage fluids: potential biomedical and clinical applications. Electrophoresis 20: 3670-3676
    • (1999) Electrophoresis , vol.20 , pp. 3670-3676
    • Lindahl, M.1    Stahlbom, B.2    Tagesson, C.3
  • 146
    • 0032900311 scopus 로고    scopus 로고
    • Demonstration of different forms of the anti-inflammatory proteins lipocortin-1 and Clara cell protein-16 in human nasal and bronchoalveolar lavage fluids
    • Lindahl M, Svartz J, Tagesson C (1999b) Demonstration of different forms of the anti-inflammatory proteins lipocortin-1 and Clara cell protein-16 in human nasal and bronchoalveolar lavage fluids. Electrophoresis 20: 881-890
    • (1999) Electrophoresis , vol.20 , pp. 881-890
    • Lindahl, M.1    Svartz, J.2    Tagesson, C.3
  • 147
  • 148
    • 0032780007 scopus 로고    scopus 로고
    • 4-Hydroxynonenal triggers an epidermal growth factor receptor-linked signal pathway for growth inhibition
    • Liu W, Akhand AA, Kato M, Yokoyama I, Miyata T, Kurokawa K, Uchida K, Nakashima I (1999) 4-hydroxynonenal triggers an epidermal growth factor receptor-linked signal pathway for growth inhibition. J Cell Sci 112 (Pt 14): 2409-2417
    • (1999) J Cell Sci , vol.112 , Issue.14 PART , pp. 2409-2417
    • Liu, W.1    Akhand, A.A.2    Kato, M.3    Yokoyama, I.4    Miyata, T.5    Kurokawa, K.6    Uchida, K.7    Nakashima, I.8
  • 149
    • 0033057535 scopus 로고    scopus 로고
    • Correlation of nuclear color and opalescence with protein S-thiolation in human lenses
    • Lou MF, Dickerson JE Jr, Tung WH, Wolfe JK, Chylack LT Jr (1999) Correlation of nuclear color and opalescence with protein S-thiolation in human lenses. Exp Eye Res 68: 547-552
    • (1999) Exp Eye Res , vol.68 , pp. 547-552
    • Lou, M.F.1    Dickerson Jr., J.E.2    Tung, W.H.3    Wolfe, J.K.4    Chylack Jr., L.T.5
  • 150
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • MacMillan-Crow LA, Crow JP, Kerby JD, Beckman JS, Thompson JA (1996) Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc Natl Acad Sci USA 93: 11853-11858
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 151
    • 0035340289 scopus 로고    scopus 로고
    • Eosinophils are a major source of nitric oxide-derived oxidants in severe asthma: Characterization of pathways available to eosinophils for generating reactive nitrogen species
    • MacPherson JC, Comhair SA, Erzurum SC, Klein DF, Lipscomb MF, Kavuru MS, Samoszuk MK, Hazen SL (2001) Eosinophils are a major source of nitric oxide-derived oxidants in severe asthma: characterization of pathways available to eosinophils for generating reactive nitrogen species. J Immunol 166: 5763-5772
    • (2001) J Immunol , vol.166 , pp. 5763-5772
    • MacPherson, J.C.1    Comhair, S.A.2    Erzurum, S.C.3    Klein, D.F.4    Lipscomb, M.F.5    Kavuru, M.S.6    Samoszuk, M.K.7    Hazen, S.L.8
  • 152
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K, Zilbering A, Zhu L, Goldstein BJ (2001) Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J Biol Chem 276: 21938-21942
    • (2001) J Biol Chem , vol.276 , pp. 21938-21942
    • Mahadev, K.1    Zilbering, A.2    Zhu, L.3    Goldstein, B.J.4
  • 153
    • 0026650664 scopus 로고
    • Increased oxidized methionine residues in BAL fluid proteins in acute or chronic bronchitis
    • Maier KL, Leuschel L, Costabel U (1992) Increased oxidized methionine residues in BAL fluid proteins in acute or chronic bronchitis. Eur Respir J 5: 651-658
    • (1992) Eur Respir J , vol.5 , pp. 651-658
    • Maier, K.L.1    Leuschel, L.2    Costabel, U.3
  • 154
    • 0035310359 scopus 로고    scopus 로고
    • Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines
    • Mallis RJ, Buss JE, Thomas JA (2001) Oxidative modification of H-ras: S-thiolation and S-nitrosylation of reactive cysteines. Biochem J 355: 145-153
    • (2001) Biochem J , vol.355 , pp. 145-153
    • Mallis, R.J.1    Buss, J.E.2    Thomas, J.A.3
  • 155
    • 0037072883 scopus 로고    scopus 로고
    • Nitrosative Stress-induced Apoptosis through Inhibition of NF-kappa B
    • Marshall HE, Stamler JS (2002) Nitrosative Stress-induced Apoptosis through Inhibition of NF-kappa B. J Biol Chem 277: 34223-34228
    • (2002) J Biol Chem , vol.277 , pp. 34223-34228
    • Marshall, H.E.1    Stamler, J.S.2
  • 156
    • 0033880888 scopus 로고    scopus 로고
    • Nitrated proteins in bronchoalveolar lavage fluid of patients at risk of ventilator-associated bronchopneumonia
    • Mathy-Hartert M, Damas P, Nys M, Deby-Dupont G, Canivet JL, Ledoux D, Lamy M (2000) Nitrated proteins in bronchoalveolar lavage fluid of patients at risk of ventilator-associated bronchopneumonia. Eur Respir J 16: 296-301
    • (2000) Eur Respir J , vol.16 , pp. 296-301
    • Mathy-Hartert, M.1    Damas, P.2    Nys, M.3    Deby-Dupont, G.4    Canivet, J.L.5    Ledoux, D.6    Lamy, M.7
  • 157
    • 0030611083 scopus 로고    scopus 로고
    • Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase
    • May JM, Mendiratta S, Hill KE, Burk RF (1997) Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. J Biol Chem 272: 22607-22610
    • (1997) J Biol Chem , vol.272 , pp. 22607-22610
    • May, J.M.1    Mendiratta, S.2    Hill, K.E.3    Burk, R.F.4
  • 158
    • 0021776272 scopus 로고
    • Vitamin E: Interactions with free radicals and ascorbate
    • McCay PB (1985) Vitamin E: interactions with free radicals and ascorbate. Annu Rev Nutr 5: 323-340
    • (1985) Annu Rev Nutr , vol.5 , pp. 323-340
    • McCay, P.B.1
  • 159
    • 0030796175 scopus 로고    scopus 로고
    • Immunohistochemical localization of nitric oxide synthase and the oxidant peroxynitrite in lung transplant recipients with obliterative bronchiolitis
    • McDermott CD, Gavita SM, Shennib H, Giaid A (1997) Immunohistochemical localization of nitric oxide synthase and the oxidant peroxynitrite in lung transplant recipients with obliterative bronchiolitis. Transplantation 64: 270-274
    • (1997) Transplantation , vol.64 , pp. 270-274
    • McDermott, C.D.1    Gavita, S.M.2    Shennib, H.3    Giaid, A.4
  • 161
    • 0024515755 scopus 로고
    • Studies of ascorbate-dependent, iron-catalyzed lipid peroxidation
    • Miller DM, Aust SD (1989) Studies of ascorbate-dependent, iron-catalyzed lipid peroxidation. Arch Biochem Biophys 271: 113-119
    • (1989) Arch Biochem Biophys , vol.271 , pp. 113-119
    • Miller, D.M.1    Aust, S.D.2
  • 162
    • 0030028219 scopus 로고    scopus 로고
    • Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment
    • Mohr S, Stamler JS, Brune B (1996) Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment. J Biol Chem 271: 4209-4214
    • (1996) J Biol Chem , vol.271 , pp. 4209-4214
    • Mohr, S.1    Stamler, J.S.2    Brune, B.3
  • 163
    • 0033515479 scopus 로고    scopus 로고
    • Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
    • Mohr S, Hallak H, de Boitte A, Lapetina EG, Brune B (1999) Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3- phosphate dehydrogenase. J Biol Chem 274: 9427-9430
    • (1999) J Biol Chem , vol.274 , pp. 9427-9430
    • Mohr, S.1    Hallak, H.2    De Boitte, A.3    Lapetina, E.G.4    Brune, B.5
  • 164
    • 0033230421 scopus 로고    scopus 로고
    • Oxidative stress and pulmonary inflammation: Pharmacological intervention with antioxidants
    • Morcillo EJ, Estrela J, Cortijo J (1999) Oxidative stress and pulmonary inflammation: pharmacological intervention with antioxidants. Pharmacol Res 40: 393-404
    • (1999) Pharmacol Res , vol.40 , pp. 393-404
    • Morcillo, E.J.1    Estrela, J.2    Cortijo, J.3
  • 165
    • 0032791062 scopus 로고    scopus 로고
    • Antioxidant consumption and repletion kinetics in nasal lavage fluid following exposure of healthy human volunteers to ozone
    • Mudway IS, Blomberg A, Frew AJ, Holgate ST, Sandstrom T, Kelly FJ (1999) Antioxidant consumption and repletion kinetics in nasal lavage fluid following exposure of healthy human volunteers to ozone. Eur Respir J 13: 1429-1438
    • (1999) Eur Respir J , vol.13 , pp. 1429-1438
    • Mudway, I.S.1    Blomberg, A.2    Frew, A.J.3    Holgate, S.T.4    Sandstrom, T.5    Kelly, F.J.6
  • 166
    • 0031905748 scopus 로고    scopus 로고
    • Modeling the interactions of ozone with pulmonary epithelial lining fluid antioxidants
    • Mudway IS, Kelly FJ (1998) Modeling the interactions of ozone with pulmonary epithelial lining fluid antioxidants. Toxicol Appl Pharmacol 148: 91-100
    • (1998) Toxicol Appl Pharmacol , vol.148 , pp. 91-100
    • Mudway, I.S.1    Kelly, F.J.2
  • 168
    • 0035887713 scopus 로고    scopus 로고
    • Differences in basal airway antioxidant concentrations are not predictive of individual responsiveness to ozone: A comparison of healthy and mild asthmatic subjects
    • Mudway IS, Stenfors N, Blomberg A, Helleday R, Dunster C, Marklund SL, Frew AJ, Sandstrom T, Kelly FJ (2001) Differences in basal airway antioxidant concentrations are not predictive of individual responsiveness to ozone: a comparison of healthy and mild asthmatic subjects. Free Radic Biol Med 31: 962-974
    • (2001) Free Radic Biol Med , vol.31 , pp. 962-974
    • Mudway, I.S.1    Stenfors, N.2    Blomberg, A.3    Helleday, R.4    Dunster, C.5    Marklund, S.L.6    Frew, A.J.7    Sandstrom, T.8    Kelly, F.J.9
  • 169
    • 0026691581 scopus 로고
    • Activation of human macrophages for the killing of intracellular Trypanosoma cruzi by TNE-alpha and IFN-gamma through a nitric oxide-dependent mechanism
    • Munoz-Fernandez MA, Fernandez MA, Fresno M (1992) Activation of human macrophages for the killing of intracellular Trypanosoma cruzi by TNE-alpha and IFN-gamma through a nitric oxide-dependent mechanism. Immunol Lett 33: 35-40
    • (1992) Immunol Lett , vol.33 , pp. 35-40
    • Munoz-Fernandez, M.A.1    Fernandez, M.A.2    Fresno, M.3
  • 170
    • 0029940140 scopus 로고    scopus 로고
    • Regional variation in iron and iron-binding proteins within the lungs of smokers
    • Nelson ME, O'Brien-Ladner AR, Wesselius LJ (1996) Regional variation in iron and iron-binding proteins within the lungs of smokers. Am J Respir Crit Care Med 153: 1353-1358
    • (1996) Am J Respir Crit Care Med , vol.153 , pp. 1353-1358
    • Nelson, M.E.1    O'Brien-Ladner, A.R.2    Wesselius, L.J.3
  • 171
    • 0032730236 scopus 로고    scopus 로고
    • Effect of inhaled ozone on exhaled nitric oxide, pulmonary function, and induced sputum in normal and asthmatic subjects
    • Nightingale JA, Rogers DF, Barnes PJ (1999) Effect of inhaled ozone on exhaled nitric oxide, pulmonary function, and induced sputum in normal and asthmatic subjects. Thorax 54: 1061-1069
    • (1999) Thorax , vol.54 , pp. 1061-1069
    • Nightingale, J.A.1    Rogers, D.F.2    Barnes, P.J.3
  • 176
    • 0025612247 scopus 로고
    • Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins
    • Ohshima H, Friesen M, Brouet I, Bartsch H (1990) Nitrotyrosine as a new marker for endogenous nitrosation and nitration of proteins. Food Chem Toxicol 28: 647-652
    • (1990) Food Chem Toxicol , vol.28 , pp. 647-652
    • Ohshima, H.1    Friesen, M.2    Brouet, I.3    Bartsch, H.4
  • 177
    • 0023144962 scopus 로고
    • Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils
    • Oliver CN (1987) Inactivation of enzymes and oxidative modification of proteins by stimulated neutrophils. Arch Biochem Biophys 253: 62-72
    • (1987) Arch Biochem Biophys , vol.253 , pp. 62-72
    • Oliver, C.N.1
  • 178
    • 0023923526 scopus 로고
    • Role of transferrin and ceruloplasmin in antioxidant activity of lung epithelial lining fluid
    • Pacht ER, Davis WB (1988) Role of transferrin and ceruloplasmin in antioxidant activity of lung epithelial lining fluid. J Appl Physiol 64: 2092-2099
    • (1988) J Appl Physiol , vol.64 , pp. 2092-2099
    • Pacht, E.R.1    Davis, W.B.2
  • 179
    • 0030747167 scopus 로고    scopus 로고
    • Alveolar fluid glutathione decreases in asymptomatic HIV-seropositive subjects over time
    • Pacht ER, Diaz P, Clanton T, Hart J, Gadek JE (1997) Alveolar fluid glutathione decreases in asymptomatic HIV-seropositive subjects over time. Chest 112: 785-788
    • (1997) Chest , vol.112 , pp. 785-788
    • Pacht, E.R.1    Diaz, P.2    Clanton, T.3    Hart, J.4    Gadek, J.E.5
  • 180
    • 0032532084 scopus 로고    scopus 로고
    • Cellular responses to nitric oxide: Role of protein S-thiolation/ dethiolation
    • Padgett CM, Whorton AR (1998) Cellular responses to nitric oxide: role of protein S-thiolation/dethiolation. Arch Biochem Biophys 358: 232-242
    • (1998) Arch Biochem Biophys , vol.358 , pp. 232-242
    • Padgett, C.M.1    Whorton, A.R.2
  • 181
    • 0032125191 scopus 로고    scopus 로고
    • Oxidative damage in tissues of rats exposed to cigarette smoke
    • Park EM, Park YM, Gwak YS (1998) Oxidative damage in tissues of rats exposed to cigarette smoke. Free Radic Biol Med 25: 79-86
    • (1998) Free Radic Biol Med , vol.25 , pp. 79-86
    • Park, E.M.1    Park, Y.M.2    Gwak, Y.S.3
  • 182
    • 0019475753 scopus 로고
    • Nitrogen-13-labeled nitrite and nitrate: Distribution and metabolism after intratracheal administration
    • Parks NJ, Krohn KJ, Mathis CA, Chasko JH, Geiger KR, Gregor ME, Peek NF (1981) Nitrogen-13-labeled nitrite and nitrate: distribution and metabolism after intratracheal administration. Science 212: 58-60
    • (1981) Science , vol.212 , pp. 58-60
    • Parks, N.J.1    Krohn, K.J.2    Mathis, C.A.3    Chasko, J.H.4    Geiger, K.R.5    Gregor, M.E.6    Peek, N.F.7
  • 186
    • 0033550050 scopus 로고    scopus 로고
    • Inhibition of cathepsin K by nitric oxide donors: Evidence for the formation of mixed disulfides and a sulfenic acid
    • Percival MD, Ouellet M, Campagnolo C, Claveau D, Li C (1999) Inhibition of cathepsin K by nitric oxide donors: evidence for the formation of mixed disulfides and a sulfenic acid. Biochemistry 38: 13574-13583
    • (1999) Biochemistry , vol.38 , pp. 13574-13583
    • Percival, M.D.1    Ouellet, M.2    Campagnolo, C.3    Claveau, D.4    Li, C.5
  • 187
    • 0034659164 scopus 로고    scopus 로고
    • Myeloperoxidase-generated oxidants and atherosclerosis
    • Podrez EA, Abu-Soud HM, Hazen SL (2000) Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic Biol Med 28: 1717-1725
    • (2000) Free Radic Biol Med , vol.28 , pp. 1717-1725
    • Podrez, E.A.1    Abu-Soud, H.M.2    Hazen, S.L.3
  • 188
    • 0026006720 scopus 로고
    • Interfacial transfer kinetics of NO2 into pulmonary epithelial lining fluid
    • Postlethwait EM, Langford SD, Bidani A (1991) Interfacial transfer kinetics of NO2 into pulmonary epithelial lining fluid. J Appl Physiol 71: 1502-1510
    • (1991) J Appl Physiol , vol.71 , pp. 1502-1510
    • Postlethwait, E.M.1    Langford, S.D.2    Bidani, A.3
  • 191
    • 0026776404 scopus 로고
    • Catalytic reduction of Fe(III)-cytochrome-c involving stable radiolysis products derived from disulphides, proteins and thiols
    • Prutz WA (1992) Catalytic reduction of Fe(III)-cytochrome-c involving stable radiolysis products derived from disulphides, proteins and thiols. Int J Radiat Biol 61: 593-602
    • (1992) Int J Radiat Biol , vol.61 , pp. 593-602
    • Prutz, W.A.1
  • 192
    • 0027454498 scopus 로고
    • Ozone in all its reactive splendor
    • Pryor WA (1993) Ozone in all its reactive splendor. J Lab Clin Med 122: 483-486
    • (1993) J Lab Clin Med , vol.122 , pp. 483-486
    • Pryor, W.A.1
  • 193
    • 0028080284 scopus 로고
    • Mechanisms of radical formation from reactions of ozone with target molecules in the lung
    • Pryor WA (1994) Mechanisms of radical formation from reactions of ozone with target molecules in the lung. Free Radic Biol Med 17: 451-465
    • (1994) Free Radic Biol Med , vol.17 , pp. 451-465
    • Pryor, W.A.1
  • 194
    • 0029037495 scopus 로고
    • The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
    • Pryor WA, Squadrito GL (1995) The chemistry of peroxynitrite: a product from the reaction of nitric oxide with superoxide. Am J Physiol 268: L699-L722
    • (1995) Am J Physiol , vol.268
    • Pryor, W.A.1    Squadrito, G.L.2
  • 195
    • 0028840467 scopus 로고
    • The cascade mechanism to explain ozone toxicity: The role of lipid ozonation products
    • Pryor WA, Squadrito GL, Friedman M (1995a) The cascade mechanism to explain ozone toxicity: the role of lipid ozonation products. Free Radic Biol Med 19: 935-941
    • (1995) Free Radic Biol Med , vol.19 , pp. 935-941
    • Pryor, W.A.1    Squadrito, G.L.2    Friedman, M.3
  • 196
  • 197
    • 0035933821 scopus 로고    scopus 로고
    • Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide
    • Pullar JM, Vissers MC, Winterbourn CC (2001) Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfide. J Biol Chem 276: 22120-22125
    • (2001) J Biol Chem , vol.276 , pp. 22120-22125
    • Pullar, J.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 198
    • 0028426899 scopus 로고
    • Oxidative damage to plasma proteins in adult respiratory distress syndrome
    • Quinlan GJ, Evans TW, Gutteridge JM (1994) Oxidative damage to plasma proteins in adult respiratory distress syndrome. Free Radic Res 20: 289-298
    • (1994) Free Radic Res , vol.20 , pp. 289-298
    • Quinlan, G.J.1    Evans, T.W.2    Gutteridge, J.M.3
  • 199
    • 0018704394 scopus 로고
    • Composition and control of secretions from tracheal bronchial submucosal glands
    • Quinton PM (1979) Composition and control of secretions from tracheal bronchial submucosal glands. Nature 279: 551-552
    • (1979) Nature , vol.279 , pp. 551-552
    • Quinton, P.M.1
  • 200
    • 0033806242 scopus 로고    scopus 로고
    • Oxidative stress and regulation of glutathione in lung inflammation
    • Rahman I, MacNee W (2000) Oxidative stress and regulation of glutathione in lung inflammation. Eur Respir J 16: 534-554
    • (2000) Eur Respir J , vol.16 , pp. 534-554
    • Rahman, I.1    MacNee, W.2
  • 202
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran V, Seres T, Moriguchi T, Thomas JA, Johnston RB Jr (1994) S-thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. J Biol Chem 269: 25010-25015
    • (1994) J Biol Chem , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston Jr., R.B.5
  • 204
    • 0034693038 scopus 로고    scopus 로고
    • Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite
    • Reiter CD, Teng RJ, Beckman JS (2000) Superoxide reacts with nitric oxide to nitrate tyrosine at physiological pH via peroxynitrite. J Biol Chem 275: 32460-32466
    • (2000) J Biol Chem , vol.275 , pp. 32460-32466
    • Reiter, C.D.1    Teng, R.J.2    Beckman, J.S.3
  • 206
    • 0030752487 scopus 로고    scopus 로고
    • Oxidative stress in chronic obstructive pulmonary disease
    • Oxidative Stress Study Group
    • Repine JE, Bast A, Lankhorst I (1997) Oxidative stress in chronic obstructive pulmonary disease. Oxidative Stress Study Group. Am J Respir Crit Care Med 156: 341-357
    • (1997) Am J Respir Crit Care Med , vol.156 , pp. 341-357
    • Repine, J.E.1    Bast, A.2    Lankhorst, I.3
  • 207
    • 0033554654 scopus 로고    scopus 로고
    • Conversion of lysine to N(epsilon)-(carboxymethyl)lysine increases susceptibility of proteins to metal-catalyzed oxidation
    • Requena JR, Stadtman ER (1999) Conversion of lysine to N(epsilon)-(carboxymethyl)lysine increases susceptibility of proteins to metal-catalyzed oxidation. Biochem Biophys Res Commun 264: 207-211
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 207-211
    • Requena, J.R.1    Stadtman, E.R.2
  • 210
    • 0037192175 scopus 로고    scopus 로고
    • Nitration of annexin II tetramer
    • Rowan WH, 3rd, Sun P, Liu L (2002) Nitration of annexin II tetramer. Biochemistry 41: 1409-1420
    • (2002) Biochemistry , vol.41 , pp. 1409-1420
    • Rowan III, W.H.1    Sun, P.2    Liu, L.3
  • 211
    • 0027198468 scopus 로고
    • Type II pneumocytes secrete vitamin e together with surfactant lipids
    • Rustow B, Haupt R, Stevens PA, Kunze D (1993) Type II pneumocytes secrete vitamin E together with surfactant lipids. Am J Physiol 265: L133-139
    • (1993) Am J Physiol , vol.265
    • Rustow, B.1    Haupt, R.2    Stevens, P.A.3    Kunze, D.4
  • 212
    • 70449626815 scopus 로고    scopus 로고
    • Detection and identification of human bronchoalveolar lavage proteins using narrow-range immobilized pH gradient DryStrip and the paper bridge sample application method
    • Sabounchi-Schutt F, Astrom J, Eklund A, Grunewald J, Bjellqvist B (2001) Detection and identification of human bronchoalveolar lavage proteins using narrow-range immobilized pH gradient DryStrip and the paper bridge sample application method. Electrophoresis 22: 1851-1860
    • (2001) Electrophoresis , vol.22 , pp. 1851-1860
    • Sabounchi-Schutt, F.1    Astrom, J.2    Eklund, A.3    Grunewald, J.4    Bjellqvist, B.5
  • 213
    • 0030915094 scopus 로고    scopus 로고
    • Increased production of the potent oxidant peroxynitrite in the lungs of patients with idiopathic pulmonary fibrosis
    • Saleh D, Barnes PJ, Giaid A (1997) Increased production of the potent oxidant peroxynitrite in the lungs of patients with idiopathic pulmonary fibrosis. Am J Respir Crit Care Med 155: 1763-1769
    • (1997) Am J Respir Crit Care Med , vol.155 , pp. 1763-1769
    • Saleh, D.1    Barnes, P.J.2    Giaid, A.3
  • 214
    • 0031857283 scopus 로고    scopus 로고
    • Increased formation of the potent oxidant peroxynitrite in the airways of asthmatic patients is associated with induction of nitric oxide synthase: Effect of inhaled glucocorticoid
    • Saleh D, Ernst P, Lim S, Barnes PJ, Giaid A (1998) Increased formation of the potent oxidant peroxynitrite in the airways of asthmatic patients is associated with induction of nitric oxide synthase: effect of inhaled glucocorticoid. FASEB J 12: 929-937
    • (1998) FASEB J , vol.12 , pp. 929-937
    • Saleh, D.1    Ernst, P.2    Lim, S.3    Barnes, P.J.4    Giaid, A.5
  • 215
    • 0032778825 scopus 로고    scopus 로고
    • Effects of reactive oxygen and nitrogen metabolites on RANTES- and IL-5-induced eosinophil chemotactic activity in vitro
    • Sato E, Simpson KL, Grisham MB, Koyama S, Robbins RA (1999) Effects of reactive oxygen and nitrogen metabolites on RANTES- and IL-5-induced eosinophil chemotactic activity in vitro. Am J Pathol 155: 591-598
    • (1999) Am J Pathol , vol.155 , pp. 591-598
    • Sato, E.1    Simpson, K.L.2    Grisham, M.B.3    Koyama, S.4    Robbins, R.A.5
  • 216
    • 0020546431 scopus 로고
    • Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen. Effect of superoxide dismutase
    • Scarpa M, Stevanato R, Viglino P, Rigo A (1983) Superoxide ion as active intermediate in the autoxidation of ascorbate by molecular oxygen. Effect of superoxide dismutase. J Biol Chem 258: 6695-6697
    • (1983) J Biol Chem , vol.258 , pp. 6695-6697
    • Scarpa, M.1    Stevanato, R.2    Viglino, P.3    Rigo, A.4
  • 217
    • 0030003486 scopus 로고    scopus 로고
    • Amino acid sequence of chicken Cu, Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues
    • Schinina ME, Carlini P, Polticelli F, Zappacosta F, Bossa F, Calabrese L (1996) Amino acid sequence of chicken Cu, Zn-containing superoxide dismutase and identification of glutathionyl adducts at exposed cysteine residues. Eur J Biochem 237: 433-439
    • (1996) Eur J Biochem , vol.237 , pp. 433-439
    • Schinina, M.E.1    Carlini, P.2    Polticelli, F.3    Zappacosta, F.4    Bossa, F.5    Calabrese, L.6
  • 219
    • 0030057750 scopus 로고    scopus 로고
    • Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress
    • Seres T, Ravichandran V, Moriguchi T, Rokutan K, Thomas JA, Johnston RB Jr (1996) Protein S-thiolation and dethiolation during the respiratory burst in human monocytes. A reversible post-translational modification with potential for buffering the effects of oxidant stress. J Immunol 156: 1973-1980
    • (1996) J Immunol , vol.156 , pp. 1973-1980
    • Seres, T.1    Ravichandran, V.2    Moriguchi, T.3    Rokutan, K.4    Thomas, J.A.5    Johnston Jr., R.B.6
  • 220
    • 0027198602 scopus 로고
    • Measurement of Na(+)-K+ pump current in isolated rabbit ventricular myocytes using the whole-cell voltage-clamp technique. Inhibition of the pump by oxidant stress
    • Shattock MJ, Matsuura H (1993) Measurement of Na(+)-K+ pump current in isolated rabbit ventricular myocytes using the whole-cell voltage-clamp technique. Inhibition of the pump by oxidant stress. Circ Res 72: 91-101
    • (1993) Circ Res , vol.72 , pp. 91-101
    • Shattock, M.J.1    Matsuura, H.2
  • 221
    • 0026010936 scopus 로고
    • Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: A model for eosinophilic endocarditis
    • Slungaard A, Mahoney JR Jr (1991) Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis. J Exp Med 173: 117-126
    • (1991) J Exp Med , vol.173 , pp. 117-126
    • Slungaard, A.1    Mahoney Jr., J.R.2
  • 222
    • 0027315107 scopus 로고
    • Increased levels of glutathione in bronchoalveolar lavage fluid from patients with asthma
    • Smith LJ, Houston M, Anderson J (1993) Increased levels of glutathione in bronchoalveolar lavage fluid from patients with asthma. Am Rev Respir Dis 147: 1461-1464
    • (1993) Am Rev Respir Dis , vol.147 , pp. 1461-1464
    • Smith, L.J.1    Houston, M.2    Anderson, J.3
  • 223
    • 0032535514 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite
    • Souza JM, Radi R (1998) Glyceraldehyde-3-phosphate dehydrogenase inactivation by peroxynitrite. Arch Biochem Biophys 360: 187-194
    • (1998) Arch Biochem Biophys , vol.360 , pp. 187-194
    • Souza, J.M.1    Radi, R.2
  • 224
    • 0035500449 scopus 로고    scopus 로고
    • Quinoid redox cycling as a mechanism for sustained free radical generation by inhaled airborne particulate matter
    • Squadrito GL, Cueto R, Dellinger B, Pryor WA (2001) Quinoid redox cycling as a mechanism for sustained free radical generation by inhaled airborne particulate matter. Free Radic Biol Med 31: 1132-1138
    • (2001) Free Radic Biol Med , vol.31 , pp. 1132-1138
    • Squadrito, G.L.1    Cueto, R.2    Dellinger, B.3    Pryor, W.A.4
  • 226
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman ER, Oliver CN (1991) Metal-catalyzed oxidation of proteins. Physiological consequences. J Biol Chem 266: 2005-2008
    • (1991) J Biol Chem , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 228
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation, the prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC (2001) Nitrosylation, the prototypic redox-based signaling mechanism. Cell 106: 675-683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 229
    • 0032499878 scopus 로고    scopus 로고
    • Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord
    • Strong MJ, Sopper MM, Crow JP, Strong WL, Beckman JS (1998) Nitration of the low molecular weight neurofilament is equivalent in sporadic amyotrophic lateral sclerosis and control cervical spinal cord. Biochem Biophys Res Commun 248: 157-164
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 157-164
    • Strong, M.J.1    Sopper, M.M.2    Crow, J.P.3    Strong, W.L.4    Beckman, J.S.5
  • 230
    • 0035949671 scopus 로고    scopus 로고
    • Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO
    • Sun J, Xin C, Eu JP, Stamler JS, Meissner G (2001) Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO. Proc Natl Acad Sci USA 98: 11158-11162
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11158-11162
    • Sun, J.1    Xin, C.2    Eu, J.P.3    Stamler, J.S.4    Meissner, G.5
  • 231
    • 0034282683 scopus 로고    scopus 로고
    • Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity
    • Taggart C, Cervantes-Laurean D, Kim G, McElvaney NG, Wehr N, Moss J, Levine RL (2000) Oxidation of either methionine 351 or methionine 358 in alpha 1-antitrypsin causes loss of anti-neutrophil elastase activity. J Biol Chem 275: 27258-27265
    • (2000) J Biol Chem , vol.275 , pp. 27258-27265
    • Taggart, C.1    Cervantes-Laurean, D.2    Kim, G.3    McElvaney, N.G.4    Wehr, N.5    Moss, J.6    Levine, R.L.7
  • 232
    • 0033568723 scopus 로고    scopus 로고
    • Rapid and irreversible inactivation of protein tyrosine phosphatases PTP1B, CD45, and LAR by peroxynitrite
    • Takakura K, Beckman JS, MacMillan-Crow LA, Crow JP (1999) Rapid and irreversible inactivation of protein tyrosine phosphatases PTP1B, CD45, and LAR by peroxynitrite. Arch Biochem Biophys 369: 197-207
    • (1999) Arch Biochem Biophys , vol.369 , pp. 197-207
    • Takakura, K.1    Beckman, J.S.2    MacMillan-Crow, L.A.3    Crow, J.P.4
  • 233
    • 0032528181 scopus 로고    scopus 로고
    • Asbestos inhalation induces reactive nitrogen species and nitrotyrosine formation in the lungs and pleura of the rat
    • Tanaka S, Choe N, Hemenway DR, Zhu S, Matalon S, Kagan E (1998) Asbestos inhalation induces reactive nitrogen species and nitrotyrosine formation in the lungs and pleura of the rat. J Clin Invest 102: 445-454
    • (1998) J Clin Invest , vol.102 , pp. 445-454
    • Tanaka, S.1    Choe, N.2    Hemenway, D.R.3    Zhu, S.4    Matalon, S.5    Kagan, E.6
  • 234
    • 0037076518 scopus 로고    scopus 로고
    • S-nitrosation of Ca(2+)-loaded and Ca(26+)-free recombinant calbindin D(28K) from human brain
    • Tao L, Murphy ME, English AM (2002) S-nitrosation of Ca(2+)-loaded and Ca(26+)-free recombinant calbindin D(28K) from human brain. Biochemistry 41: 6185-6192
    • (2002) Biochemistry , vol.41 , pp. 6185-6192
    • Tao, L.1    Murphy, M.E.2    English, A.M.3
  • 235
    • 0035734002 scopus 로고    scopus 로고
    • Oxidative targets in the stratum corneum. A new basis for antioxidative strategies
    • Thiele JJ (2001) Oxidative targets in the stratum corneum. A new basis for antioxidative strategies. Skin Pharmacol Appl Skin Physiol 14 Suppl 1: 87-91
    • (2001) Skin Pharmacol Appl Skin Physiol , vol.14 , Issue.1 SUPPL. , pp. 87-91
    • Thiele, J.J.1
  • 236
    • 0020573713 scopus 로고
    • Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils
    • Thomas EL, Grisham MB, Jefferson MM (1983) Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils. J Clin Invest 72: 441-454
    • (1983) J Clin Invest , vol.72 , pp. 441-454
    • Thomas, E.L.1    Grisham, M.B.2    Jefferson, M.M.3
  • 237
    • 0028801505 scopus 로고
    • Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines
    • Thomas EL, Bozeman PM, Jefferson MM, King CC (1995a) Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines. J Biol Chem 270: 2906-2913
    • (1995) J Biol Chem , vol.270 , pp. 2906-2913
    • Thomas, E.L.1    Bozeman, P.M.2    Jefferson, M.M.3    King, C.C.4
  • 238
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas JA, Poland B, Honzatko R (1995b) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch Biochem Biophys 319: 1-9
    • (1995) Arch Biochem Biophys , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 239
    • 0025255103 scopus 로고
    • Lower respiratory tract lactoferrin and lysozyme arise primarily in the airways and are elevated in association with chronic bronchitis
    • Thompson AB, Bohling T, Payvandi F, Rennard ST (1990) Lower respiratory tract lactoferrin and lysozyme arise primarily in the airways and are elevated in association with chronic bronchitis. J Lab Clin Med 115: 148-158
    • (1990) J Lab Clin Med , vol.115 , pp. 148-158
    • Thompson, A.B.1    Bohling, T.2    Payvandi, F.3    Rennard, S.T.4
  • 240
    • 0033529262 scopus 로고    scopus 로고
    • Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concentration: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation
    • Tien M, Berlett BS, Levine RL, Chock PB, Stadtman ER (1999) Peroxynitrite-mediated modification of proteins at physiological carbon dioxide concentration: pH dependence of carbonyl formation, tyrosine nitration, and methionine oxidation. Proc Natl Acad Sci USA 96: 7809-7814
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7809-7814
    • Tien, M.1    Berlett, B.S.2    Levine, R.L.3    Chock, P.B.4    Stadtman, E.R.5
  • 243
    • 0027368195 scopus 로고
    • 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins
    • Uchida K, Kawakishi S (1993) 2-Oxo-histidine as a novel biological marker for oxidatively modified proteins. FEBS Lett 332: 208-210
    • (1993) FEBS Lett , vol.332 , pp. 208-210
    • Uchida, K.1    Kawakishi, S.2
  • 244
    • 0035736649 scopus 로고    scopus 로고
    • Innate antioxidant defense systems in the respiratory tract
    • van der Vliet A, Cross CE (2001) Innate antioxidant defense systems in the respiratory tract. Biofactors 15: 83-86
    • (2001) Biofactors , vol.15 , pp. 83-86
    • Van Der Vliet, A.1    Cross, C.E.2
  • 245
    • 0028105887 scopus 로고
    • Interactions of peroxynitrite with human plasma and its constituents: Oxidative damage and antioxidant depletion
    • van der Vliet A, Smith D, O'Neill CA, Kaur H, Darley-Usmar V, Cross CE, Halliwell B (1994) Interactions of peroxynitrite with human plasma and its constituents: oxidative damage and antioxidant depletion. Biochem J 303 (Pt 1): 295-301
    • (1994) Biochem J , vol.303 , Issue.1 PART , pp. 295-301
    • Van Der Vliet, A.1    Smith, D.2    O'Neill, C.A.3    Kaur, H.4    Darley-Usmar, V.5    Cross, C.E.6    Halliwell, B.7
  • 249
    • 0029915016 scopus 로고    scopus 로고
    • The oxidative inactivation of sarcoplasmic reticulum Ca(2+)-ATPase by peroxynitrite
    • Viner RI, Huhmer AF, Bigelow DJ, Schoneich C (1996) The oxidative inactivation of sarcoplasmic reticulum Ca(2+)-ATPase by peroxynitrite. Free Radic Res 24: 243-259
    • (1996) Free Radic Res , vol.24 , pp. 243-259
    • Viner, R.I.1    Huhmer, A.F.2    Bigelow, D.J.3    Schoneich, C.4
  • 250
    • 0028940342 scopus 로고
    • Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid
    • Vissers MC, Winterbourn CC (1995) Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid. Biochem J 307 (Pt 1): 57-62
    • (1995) Biochem J , vol.307 , Issue.1 PART , pp. 57-62
    • Vissers, M.C.1    Winterbourn, C.C.2
  • 252
    • 0035916938 scopus 로고    scopus 로고
    • Stimulation of topoisomerase II-mediated DNA damage via a mechanism involving protein thiolation
    • Wang H, Mao Y, Chen AY, Zhou N, La Voie EJ, Liu LF (2001) Stimulation of topoisomerase II-mediated DNA damage via a mechanism involving protein thiolation. Biochemistry 40: 3316-3323
    • (2001) Biochemistry , vol.40 , pp. 3316-3323
    • Wang, H.1    Mao, Y.2    Chen, A.Y.3    Zhou, N.4    La Voie, E.J.5    Liu, L.F.6
  • 255
    • 0033551198 scopus 로고    scopus 로고
    • Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase
    • Washburn MP, Wells WW (1999) Identification of the dehydroascorbic acid reductase and thioltransferase (Glutaredoxin) activities of bovine erythrocyte glutathione peroxidase. Biochem Biophys Res Commun 257: 567-571
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 567-571
    • Washburn, M.P.1    Wells, W.W.2
  • 256
    • 0033000140 scopus 로고    scopus 로고
    • Human bronchoalveolar lavage fluid: Two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins
    • Wattiez R, Hermans C, Bernard A, Lesur O, Falmagne P (1999) Human bronchoalveolar lavage fluid: two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins. Electrophoresis 20: 1634-1645
    • (1999) Electrophoresis , vol.20 , pp. 1634-1645
    • Wattiez, R.1    Hermans, C.2    Bernard, A.3    Lesur, O.4    Falmagne, P.5
  • 257
    • 0031451793 scopus 로고    scopus 로고
    • Regulation of depth and composition of airway surface liquid
    • Widdicombe JH, Bastacky SJ, Wu DX, Lee CY (1997) Regulation of depth and composition of airway surface liquid. Eur Respir J 10: 2892-2897
    • (1997) Eur Respir J , vol.10 , pp. 2892-2897
    • Widdicombe, J.H.1    Bastacky, S.J.2    Wu, D.X.3    Lee, C.Y.4
  • 258
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective
    • Winkler BS, Orselli SM, Rex TS (1994) The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective. Free Radic Biol Med 17: 333-349
    • (1994) Free Radic Biol Med , vol.17 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Rex, T.S.3
  • 259
    • 0026331377 scopus 로고
    • Free radical-induced carbonyl content in protein of estrogen-treated hamsters assayed by sodium boro[3H]hydride reduction
    • Winter ML, Liehr JG (1991) Free radical-induced carbonyl content in protein of estrogen-treated hamsters assayed by sodium boro[3H]hydride reduction. J Biol Chem 266: 14446-14450
    • (1991) J Biol Chem , vol.266 , pp. 14446-14450
    • Winter, M.L.1    Liehr, J.G.2
  • 260
    • 0021807129 scopus 로고
    • Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite
    • Winterbourn CC (1985) Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 840: 204-210
    • (1985) Biochim Biophys Acta , vol.840 , pp. 204-210
    • Winterbourn, C.C.1
  • 261
  • 262
    • 0027931153 scopus 로고
    • Effects of acute endotoxemia on production of cytokines and nitric oxide by pulmonary alveolar and interstitial macrophages
    • Wizemann TM, Laskin DL (1994) Effects of acute endotoxemia on production of cytokines and nitric oxide by pulmonary alveolar and interstitial macrophages. Ann NY Acad Sci 730: 336-337
    • (1994) Ann NY Acad Sci , vol.730 , pp. 336-337
    • Wizemann, T.M.1    Laskin, D.L.2
  • 263
    • 0033520499 scopus 로고    scopus 로고
    • Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders
    • Wu W, Chen Y, Hazen SL (1999) Eosinophil peroxidase nitrates protein tyrosyl residues. Implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J Biol Chem 274: 25933-25944
    • (1999) J Biol Chem , vol.274 , pp. 25933-25944
    • Wu, W.1    Chen, Y.2    Hazen, S.L.3
  • 265
    • 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 (1998) 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) J Biol Chem , vol.273 , pp. 14085-14089
    • Yamakura, F.1    Taka, H.2    Fujimura, T.3    Murayama, K.4
  • 266
    • 0035877211 scopus 로고    scopus 로고
    • Surfactant protein D regulates NF-kappa B and matrix metalloproteinase production in alveolar macrophages via oxidant-sensitive pathways
    • Yoshida M, Korfhagen TR, Whitsett JA (2001) Surfactant protein D regulates NF-kappa B and matrix metalloproteinase production in alveolar macrophages via oxidant-sensitive pathways. J Immunol 166: 7514-7519
    • (2001) J Immunol , vol.166 , pp. 7514-7519
    • Yoshida, M.1    Korfhagen, T.R.2    Whitsett, J.A.3
  • 267
    • 0030248709 scopus 로고    scopus 로고
    • Nitration of surfactant protein A (SP-A) tyrosine residues results in decreased mannose binding ability
    • Zhu S, Haddad IY, Matalon S (1996) Nitration of surfactant protein A (SP-A) tyrosine residues results in decreased mannose binding ability. Arch Biochem Biophys 333: 282-290
    • (1996) Arch Biochem Biophys , vol.333 , pp. 282-290
    • Zhu, S.1    Haddad, I.Y.2    Matalon, S.3
  • 268
    • 0034079281 scopus 로고    scopus 로고
    • Carbon dioxide enhances nitration of surfactant protein A by activated alveolar macrophages
    • Zhu S, Basiouny KF, Crow JP, Matalon S (2000) Carbon dioxide enhances nitration of surfactant protein A by activated alveolar macrophages. Am J Physiol Lung Cell Mol Physiol 278: L1025-L1031
    • (2000) Am J Physiol Lung Cell Mol Physiol , vol.278
    • Zhu, S.1    Basiouny, K.F.2    Crow, J.P.3    Matalon, S.4
  • 269
    • 0030877284 scopus 로고    scopus 로고
    • Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite
    • Zou M, Martin C, Ullrich V (1997) Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite. Biol Chem 378: 707-713
    • (1997) Biol Chem , vol.378 , pp. 707-713
    • Zou, M.1    Martin, C.2    Ullrich, V.3


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