메뉴 건너뛰기




Volumn 46, Issue 8, 2012, Pages 975-995

Reactions and reactivity of myeloperoxidase-derived oxidants: Differential biological effects of hypochlorous and hypothiocyanous acids

Author keywords

Hypochlorous acid; Hypothiocyanous acid; Myeloperoxidase; Protein oxidation; Thiocyanate

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININE; AROMATIC AMINO ACID; ASPARAGINE; BIOLOGICAL MARKER; CATHEPSIN B; CYANIC ACID DERIVATIVE; CYSTEINE; GLUTAMINE; GLUTATHIONE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HALIDE; HISTIDINE; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; HYPOTHIOCYANOUS ACID; LYSINE; METHIONINE; MYELOPEROXIDASE; OXIDIZING AGENT; SELENIDE; SELENOCYSTEINE; SELENOMETHIONINE; SULFINIC ACID DERIVATIVE; SULFUR DERIVATIVE; THIOCYANATE; TRANSMEMBRANE CONDUCTANCE REGULATOR; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84863890440     PISSN: 10715762     EISSN: 10292470     Source Type: Journal    
DOI: 10.3109/10715762.2012.667566     Document Type: Review
Times cited : (148)

References (261)
  • 1
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant production
    • Kettle AJ, Winterbourn CC. Myeloperoxidase: a key regulator of neutrophil oxidant production. Redox Rep 1997;3:3-15.
    • (1997) Redox Rep , vol.3 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 3
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • Davies MJ, Hawkins CL, Pattison DI, Rees MD. Mammalian heme peroxidases: from molecular mechanisms to health implications. Antioxid Redox Signal 2008;10: 1199-1234.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 4
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff SJ. Myeloperoxidase: friend and foe. J Leukoc Biol 2005;77:598-625.
    • (2005) J Leukoc Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 5
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidasederived oxidants with biological substrates: Gaining chemical insight into human infl ammatory diseases
    • Pattison DI, Davies MJ. Reactions of myeloperoxidasederived oxidants with biological substrates: gaining chemical insight into human infl ammatory diseases. Curr Med Chem 2006;13:3271-3290.
    • (2006) Curr Med Chem , vol.13 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 6
    • 0021807129 scopus 로고
    • Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite
    • Winterbourn CC. Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite. Biochim Biophys Acta 1985;840:204-210.
    • (1985) Biochim Biophys Acta , vol.840 , pp. 204-210
    • Winterbourn, C.C.1
  • 7
    • 0037184780 scopus 로고    scopus 로고
    • Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid
    • Winterbourn CC. Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid. Toxicology 2002;181-182:223-227.
    • (2002) Toxicology , vol.181-182 , pp. 223-227
    • Winterbourn, C.C.1
  • 8
    • 0032742579 scopus 로고    scopus 로고
    • Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid
    • Pullar JM, Winterbourn CC, Vissers MCM. Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid. Am J Physiol 1999;277:H1505-H1512.
    • (1999) Am J Physiol , vol.277
    • Pullar, J.M.1    Winterbourn, C.C.2    Vissers, M.C.M.3
  • 9
    • 0034457129 scopus 로고    scopus 로고
    • Living with a killer: The effects of hypochlorous acid on mammalian cells
    • Pullar JM, Vissers MC, Winterbourn CC. Living with a killer: the effects of hypochlorous acid on mammalian cells. IUBMB Life 2000;50:259-266.
    • (2000) IUBMB Life , vol.50 , pp. 259-266
    • Pullar, J.M.1    Vissers, M.C.2    Winterbourn, C.C.3
  • 11
    • 50949098899 scopus 로고    scopus 로고
    • HOSCN is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than HOCl or HOBr
    • Lloyd MM, Van Reyk DM, Davies MJ, Hawkins CL. HOSCN is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than HOCl or HOBr. Biochem J 2008;414:271-280.
    • (2008) Biochem J , vol.414 , pp. 271-280
    • Lloyd, M.M.1    Van Reyk, D.M.2    Davies, M.J.3    Hawkins, C.L.4
  • 12
    • 19444362449 scopus 로고    scopus 로고
    • Hypochlorous acid-mediated mitochondrial dysfunction and apoptosis in human hepatoma HepG2 and fetal liver cells: Role of mitochondrial permeability transition
    • Whiteman M, Rose P, Siau JL, Cheung NS, Tan GS, Halliwell B, et al. Hypochlorous acid-mediated mitochondrial dysfunction and apoptosis in human hepatoma HepG2 and fetal liver cells: role of mitochondrial permeability transition. Free Radic Biol Med 2005;38:1571-1584.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1571-1584
    • Whiteman, M.1    Rose, P.2    Siau, J.L.3    Cheung, N.S.4    Tan, G.S.5    Halliwell, B.6
  • 13
    • 77955474149 scopus 로고    scopus 로고
    • The myeloperoxidase-derived oxidant hoscn inhibits protein tyrosine phosphatases and modulates cell signalling via the mitogen-activated protein kinase (MAPK) pathway in macrophages
    • Lane AE, Tan JT, Hawkins CL, Heather AK, Davies MJ. The myeloperoxidase-derived oxidant hoscn inhibits protein tyrosine phosphatases and modulates cell signalling via the mitogen-activated protein kinase (MAPK) pathway in macrophages. Biochem J 2010;430:161-169.
    • (2010) Biochem J , vol.430 , pp. 161-169
    • Lane, A.E.1    Tan, J.T.2    Hawkins, C.L.3    Heather, A.K.4    Davies, M.J.5
  • 14
    • 33847053941 scopus 로고    scopus 로고
    • The pro-infl ammatory oxidant hypochlorous acid induces bax-dependent mitochondrial permeabilisation and cell death through AIF-/EndoG-dependent pathways
    • Whiteman M, Chu SH, Siau JL, Rose P, Sabapathy K, Schantz JT, et al. The pro-infl ammatory oxidant hypochlorous acid induces bax-dependent mitochondrial permeabilisation and cell death through AIF-/EndoG-dependent pathways. Cell Signal 2007;19:705-714.
    • (2007) Cell Signal , vol.19 , pp. 705-714
    • Whiteman, M.1    Chu, S.H.2    Siau, J.L.3    Rose, P.4    Sabapathy, K.5    Schantz, J.T.6
  • 15
    • 38349002464 scopus 로고    scopus 로고
    • Do mitochondriotropic antioxidants prevent chlorinative stressinduced mitochondrial and cellular injury?
    • Whiteman M, Spencer JPE, Szeto HH, Armstrong JS. Do mitochondriotropic antioxidants prevent chlorinative stressinduced mitochondrial and cellular injury? Antioxid Redox Signal 2008;10:641-650.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 641-650
    • Whiteman, M.1    Spencer, J.P.E.2    Szeto, H.H.3    Armstrong, J.S.4
  • 16
    • 0033405068 scopus 로고    scopus 로고
    • Hypochlorous acid causes caspase activation and apoptosis or growth arrest in human endothelial cells
    • Vissers MCM, Pullar JM, Hampton MB. Hypochlorous acid causes caspase activation and apoptosis or growth arrest in human endothelial cells. Biochem J 1999;344:443-339.
    • (1999) Biochem J , vol.344 , pp. 443-339
    • Vissers, M.C.M.1    Pullar, J.M.2    Hampton, M.B.3
  • 17
    • 0035861740 scopus 로고    scopus 로고
    • Regulation of apoptosis by vitamin C. Specifi c protection of the apoptotic machinery against exposure to chlorinated oxidants
    • Vissers MC, Lee WG, Hampton MB. Regulation of apoptosis by vitamin C. Specifi c protection of the apoptotic machinery against exposure to chlorinated oxidants. J Biol Chem 2001;276:46835-46840.
    • (2001) J Biol Chem , vol.276 , pp. 46835-46840
    • Vissers, M.C.1    Lee, W.G.2    Hampton, M.B.3
  • 18
    • 0037095623 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced apoptosis of HL-60 human leukemia cells is mediated by the oxidants hypochlorous acid and chloramines
    • Wagner BA, Britigan BE, Reszka KJ, McCormick ML, Burns CP. Hydrogen peroxide-induced apoptosis of HL-60 human leukemia cells is mediated by the oxidants hypochlorous acid and chloramines. Arch Biochem Biophys 2002;401:223-234.
    • (2002) Arch Biochem Biophys , vol.401 , pp. 223-234
    • Wagner, B.A.1    Britigan, B.E.2    Reszka, K.J.3    McCormick, M.L.4    Burns, C.P.5
  • 19
  • 20
    • 0021045723 scopus 로고
    • Lactoperoxidase and thiocyanate protect cultured mammalian cells against hydrogen peroxide toxicity
    • Hanstrom L, Johansson A, Carlsson J. Lactoperoxidase and thiocyanate protect cultured mammalian cells against hydrogen peroxide toxicity. Med Biol 1983;61:268-274.
    • (1983) Med Biol , vol.61 , pp. 268-274
    • Hanstrom, L.1    Johansson, A.2    Carlsson, J.3
  • 21
    • 0021119321 scopus 로고
    • The protective effect of peroxidase and thiocyanate against hydrogen peroxide toxicity assessed by the uptake of [ 3 H]-thymidine by human gingival fi broblasts cultured in vitro
    • Tenovuo J, Larjava H. The protective effect of peroxidase and thiocyanate against hydrogen peroxide toxicity assessed by the uptake of [ 3 H]-thymidine by human gingival fi broblasts cultured in vitro. Arch Oral Biol 1984;29:445-451.
    • (1984) Arch Oral Biol , vol.29 , pp. 445-451
    • Tenovuo, J.1    Larjava, H.2
  • 22
    • 73949105483 scopus 로고    scopus 로고
    • The antioxidant role of thiocyanate in the pathogenesis of cystic fi brosis and other infl ammationrelated diseases
    • Xu Y, Szep S, Lu Z. The antioxidant role of thiocyanate in the pathogenesis of cystic fi brosis and other infl ammationrelated diseases. Proc Natl Acad Sci USA 2009;106: 20515-20519.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 20515-20519
    • Xu, Y.1    Szep, S.2    Lu, Z.3
  • 23
    • 79551607386 scopus 로고    scopus 로고
    • Hypertonic saline increases lung epithelial lining fl uid glutathione and thiocyanate: Two protective CFTR-dependent thiols against oxidative injury
    • Gould NS, Gauthier S, Kariya CT, Min E, Huang J, Brian DJ. Hypertonic saline increases lung epithelial lining fl uid glutathione and thiocyanate: two protective CFTR-dependent thiols against oxidative injury. Respir Res 2010;11:119-128.
    • (2010) Respir Res , vol.11 , pp. 119-128
    • Gould, N.S.1    Gauthier, S.2    Kariya, C.T.3    Min, E.4    Huang, J.5    Brian, D.J.6
  • 24
    • 0025101703 scopus 로고
    • Cytotoxic properties of salivary oxidants
    • Grisham MB, Ryan EM. Cytotoxic properties of salivary oxidants. Am J Physiol 1990;258:C115-C121.
    • (1990) Am J Physiol , vol.258
    • Grisham, M.B.1    Ryan, E.M.2
  • 25
    • 0035808392 scopus 로고    scopus 로고
    • Eosinophil peroxidase oxidation of thiocyanate-characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system
    • Arlandson M, Decker T, Roongta VA, Bonilla L, Mayo KH, MacPherson JC, et al. Eosinophil peroxidase oxidation of thiocyanate-characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. J Biol Chem 2001;276:215-224.
    • (2001) J Biol Chem , vol.276 , pp. 215-224
    • Arlandson, M.1    Decker, T.2    Roongta, V.A.3    Bonilla, L.4    Mayo, K.H.5    MacPherson, J.C.6
  • 26
    • 33845403071 scopus 로고    scopus 로고
    • Thiocyanate-dependent induction of endothelial cell adhesion molecule expression by phagocyte peroxidases: A novel HOSCN-specifi c oxidant mechanism to amplify infl ammation
    • Wang JG, Mahmud SA, Nguyen J, Slungaard A. Thiocyanate-dependent induction of endothelial cell adhesion molecule expression by phagocyte peroxidases: a novel HOSCN-specifi c oxidant mechanism to amplify infl ammation. J Immunol 2006;177:8714-8722.
    • (2006) J Immunol , vol.177 , pp. 8714-8722
    • Wang, J.G.1    Mahmud, S.A.2    Nguyen, J.3    Slungaard, A.4
  • 27
    • 30444436766 scopus 로고    scopus 로고
    • The principal eosinophil peroxidase product, HOSCN, is a uniquely potent phagocyte oxidant inducer of endothelial cell tissue factor activity: A potential mechanism for thrombosis in eosinophilic infl ammatory states
    • Wang JG, Mahmud SA, Thompson JA, Geng JG, Key NS, Slungaard A. The principal eosinophil peroxidase product, HOSCN, is a uniquely potent phagocyte oxidant inducer of endothelial cell tissue factor activity: a potential mechanism for thrombosis in eosinophilic infl ammatory states. Blood 2006;107:558-565.
    • (2006) Blood , vol.107 , pp. 558-565
    • Wang, J.G.1    Mahmud, S.A.2    Thompson, J.A.3    Geng, J.G.4    Key, N.S.5    Slungaard, A.6
  • 28
    • 77955511053 scopus 로고    scopus 로고
    • Hypothiocyanous acid is a potent inhibitor of apoptosis and caspase 3 activation in endothelial cells
    • Bozonet SM, Scott-Thomas AP, Nagy P, Vissers MC. Hypothiocyanous acid is a potent inhibitor of apoptosis and caspase 3 activation in endothelial cells. Free Radic Biol Med 2010;49:1054-1063.
    • (2010) Free Radic Biol Med , vol.49 , pp. 1054-1063
    • Bozonet, S.M.1    Scott-Thomas, A.P.2    Nagy, P.3    Vissers, M.C.4
  • 29
    • 34948834705 scopus 로고    scopus 로고
    • Protein carbamylation links infl ammation, smoking, uremia and atherogenesis
    • Wang Z, Nicholls SJ, Rodriguez ER, Kummu O, Horkko S, Barnard J, et al. Protein carbamylation links infl ammation, smoking, uremia and atherogenesis. Nat Med 2007;13: 1176-1184.
    • (2007) Nat Med , vol.13 , pp. 1176-1184
    • Wang, Z.1    Nicholls, S.J.2    Rodriguez, E.R.3    Kummu, O.4    Horkko, S.5    Barnard, J.6
  • 30
    • 80053586669 scopus 로고    scopus 로고
    • High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase
    • Morgan PE, Pattison DI, Talib J, Summers FA, Harmer JA, Celermajer DS, et al. High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase. Free Radic Biol Med 2011;51:1815-1822.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1815-1822
    • Morgan, P.E.1    Pattison, D.I.2    Talib, J.3    Summers, F.A.4    Harmer, J.A.5    Celermajer, D.S.6
  • 32
    • 0001097874 scopus 로고
    • The respiratory burst oxidase
    • Babior BM. The respiratory burst oxidase. TIBS 1987; 12:241-243.
    • (1987) TIBS , vol.12 , pp. 241-243
    • Babior, B.M.1
  • 35
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound i with chloride, bromide, iodide, and thiocyanate
    • Furtmuller PG, Burner U, Obinger C. Reaction of myeloperoxidase compound i with chloride, bromide, iodide, and thiocyanate. Biochemistry 1998;37:17923-17930.
    • (1998) Biochemistry , vol.37 , pp. 17923-17930
    • Furtmuller, P.G.1    Burner, U.2    Obinger, C.3
  • 36
    • 78650750400 scopus 로고    scopus 로고
    • Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
    • Davies MJ. Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention. J Clin Biochem Nutr 2011;48:8-19.
    • (2011) J Clin Biochem Nutr , vol.48 , pp. 8-19
    • Davies, M.J.1
  • 38
    • 10344256217 scopus 로고    scopus 로고
    • Redox buffering of hypochlorous acid by thiocyanate in physiologic fl uids
    • Ashby MT, Carlson AC, Scott MJ. Redox buffering of hypochlorous acid by thiocyanate in physiologic fl uids. J Am Chem Soc 2004;126:15976-15977.
    • (2004) J Am Chem Soc , vol.126 , pp. 15976-15977
    • Ashby, M.T.1    Carlson, A.C.2    Scott, M.J.3
  • 39
    • 33646078598 scopus 로고    scopus 로고
    • Thiocyanate is an effi cient endogenous scavenger of the phagocytic killing agent hypobromous acid
    • Nagy P, Beal JL, Ashby MT. Thiocyanate is an effi cient endogenous scavenger of the phagocytic killing agent hypobromous acid. Chem Res Toxicol 2006;19:587-593.
    • (2006) Chem Res Toxicol , vol.19 , pp. 587-593
    • Nagy, P.1    Beal, J.L.2    Ashby, M.T.3
  • 40
    • 77749337726 scopus 로고    scopus 로고
    • Small molecular, macromolecular, and cellular chloramines react with thiocyanate to give the human defense factor hypothiocyanite
    • Xulu BA, Ashby MT. Small molecular, macromolecular, and cellular chloramines react with thiocyanate to give the human defense factor hypothiocyanite. Biochemistry 2010; 49:2068-2074.
    • (2010) Biochemistry , vol.49 , pp. 2068-2074
    • Xulu, B.A.1    Ashby, M.T.2
  • 41
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • Winterbourn CC, Hampton MB, Livesey JH, Kettle AJ. Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing. J Biol Chem 2006;281:39860-39869.
    • (2006) J Biol Chem , vol.281 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 42
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil cell proteins during phagocytosis and killing of Staphylococcus aureus
    • Chapman ALP, Hampton MB, Senthilmohan R, Winterbourn CC, Kettle AJ. Chlorination of bacterial and neutrophil cell proteins during phagocytosis and killing of Staphylococcus aureus. J Biol Chem 2002;277:9757-9762.
    • (2002) J Biol Chem , vol.277 , pp. 9757-9762
    • Chapman, A.L.P.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 43
    • 0037163020 scopus 로고    scopus 로고
    • Human neutrophils use the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate but not nitrate bacterial proteins during phagocytosis
    • Rosen H, Crowley JR, Heinecke JW. Human neutrophils use the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate but not nitrate bacterial proteins during phagocytosis. J Biol Chem 2002;34:30463-30468.
    • (2002) J Biol Chem , vol.34 , pp. 30463-30468
    • Rosen, H.1    Crowley, J.R.2    Heinecke, J.W.3
  • 44
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal AW. How neutrophils kill microbes. Ann Rev Immunol 2005;23:197-223.
    • (2005) Ann Rev Immunol , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 45
    • 0018838058 scopus 로고
    • Oxygen metabolism and the toxic properties of phagocytes
    • Klebanoff SJ. Oxygen metabolism and the toxic properties of phagocytes. Ann Int Med 1980;93:480-489.
    • (1980) Ann Int Med , vol.93 , pp. 480-489
    • Klebanoff, S.J.1
  • 46
    • 70449679220 scopus 로고    scopus 로고
    • The role of hypothiocyanous acid (HOSCN) in biological systems
    • Hawkins CL. The role of hypothiocyanous acid (HOSCN) in biological systems. Free Radic Res 2009;43:1147-1158.
    • (2009) Free Radic Res , vol.43 , pp. 1147-1158
    • Hawkins, C.L.1
  • 47
    • 30544452175 scopus 로고    scopus 로고
    • Biosyn thesis processing, and sorting of human myeloperoxidase
    • Hansson M, Olsson I, Nauseef WM. Biosynthesis, processing, and sorting of human myeloperoxidase. Arch Biochem Biophys 2006;445:214-224.
    • (2006) Arch Biochem Biophys , vol.445 , pp. 214-224
    • Hansson, M.1    Olsson, I.2    Nauseef, W.M.3
  • 48
    • 73449143528 scopus 로고    scopus 로고
    • Myeloperoxidase: Molecular mechanisms of action and their relevance to human health and disease
    • van der Veen BS, Winther MPJ, Herringa P. Myeloperoxidase: molecular mechanisms of action and their relevance to human health and disease. Antioxid Redox Signal 2009;11: 2899-2937.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2899-2937
    • Van Der Veen, B.S.1    Winther, M.P.J.2    Herringa, P.3
  • 49
    • 0030979720 scopus 로고    scopus 로고
    • 3-chlorotyrosine, a specifi c marker of myeloperoxidase-catalysed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • Hazen SL, Heinecke JW. 3-chlorotyrosine, a specifi c marker of myeloperoxidase-catalysed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima. J Clin Invest 1997;99:2075-2081.
    • (1997) J Clin Invest , vol.99 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 51
    • 0037372157 scopus 로고    scopus 로고
    • 3-chlorotyrosine as a marker of protein damage by myeloperoxidase in traceal aspirates from preterm infants: Association with adverse respiratory outcome
    • Buss H, Senthilmohan R, Darlow BA, Mogridge N, Kettle AJ, Winterbourn CC. 3-chlorotyrosine as a marker of protein damage by myeloperoxidase in traceal aspirates from preterm infants: association with adverse respiratory outcome. Pediatr Res 2003;53:455-462.
    • (2003) Pediatr Res , vol.53 , pp. 455-462
    • Buss, H.1    Senthilmohan, R.2    Darlow, B.A.3    Mogridge, N.4    Kettle, A.J.5    Winterbourn, C.C.6
  • 53
    • 0034672422 scopus 로고    scopus 로고
    • Elevated levels of protein-bound p-hydroxyphenylacetaldehyde, an amino-acid-derived aldehyde generated by myeloperoxidase, are present in human fatty streaks, intermediate lesions and advanced atherosclerotic lesions
    • Hazen SL, Gaut JP, Crowley JR, Hsu FF, Heinecke JW. Elevated levels of protein-bound p-hydroxyphenylacetaldehyde, an amino-acid-derived aldehyde generated by myeloperoxidase, are present in human fatty streaks, intermediate lesions and advanced atherosclerotic lesions. Biochem J 2000;352:693-699.
    • (2000) Biochem J , vol.352 , pp. 693-699
    • Hazen, S.L.1    Gaut, J.P.2    Crowley, J.R.3    Hsu, F.F.4    Heinecke, J.W.5
  • 54
    • 0031350219 scopus 로고    scopus 로고
    • Modifi cation of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins
    • Carr AC, Vissers MC, Domigan NM, Winterbourn CC. Modifi cation of red cell membrane lipids by hypochlorous acid and haemolysis by preformed lipid chlorohydrins. Redox Rep 1997;3:263-271.
    • (1997) Redox Rep , vol.3 , pp. 263-271
    • Carr, A.C.1    Vissers, M.C.2    Domigan, N.M.3    Winterbourn, C.C.4
  • 56
    • 0348049466 scopus 로고    scopus 로고
    • Identifi cation of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions
    • Thukkani AK, McHowat J, Hsu FF, Brennan ML, Hazen SL, Ford DA. Identifi cation of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions. Circulation 2003;108: 3128-3133.
    • (2003) Circulation , vol.108 , pp. 3128-3133
    • Thukkani, A.K.1    McHowat, J.2    Hsu, F.F.3    Brennan, M.L.4    Hazen, S.L.5    Ford, D.A.6
  • 57
    • 77950566652 scopus 로고    scopus 로고
    • Chemical and immunochemical detection of 8-halogenated deoxyguanosines at early stage infl ammation
    • Asahi T, Kondo H, Masuda M, Nishino H, Aratani Y, Naito Y, et al. Chemical and immunochemical detection of 8-halogenated deoxyguanosines at early stage infl ammation. J Biol Chem 2010;285:9282-9291.
    • (2010) J Biol Chem , vol.285 , pp. 9282-9291
    • Asahi, T.1    Kondo, H.2    Masuda, M.3    Nishino, H.4    Aratani, Y.5    Naito, Y.6
  • 58
    • 0037041274 scopus 로고    scopus 로고
    • DNA damage induced by hypochlorite and hypobromite with reference to infl ammation-associated carcinogenesis
    • Ohnishi S, Murata M, Kawanishi S. DNA damage induced by hypochlorite and hypobromite with reference to infl ammation-associated carcinogenesis. Cancer Lett 2002;178:37-42.
    • (2002) Cancer Lett , vol.178 , pp. 37-42
    • Ohnishi, S.1    Murata, M.2    Kawanishi, S.3
  • 59
    • 0033584939 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxidechloride system of phagocytes produces 5-chlorocytosine in bacterial RNA
    • Henderson JP, Byun J, Heinecke JW. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxidechloride system of phagocytes produces 5-chlorocytosine in bacterial RNA. J Biol Chem 1999;274:33440-33448.
    • (1999) J Biol Chem , vol.274 , pp. 33440-33448
    • Henderson, J.P.1    Byun, J.2    Heinecke, J.W.3
  • 60
    • 0035896545 scopus 로고    scopus 로고
    • Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during infl ammation
    • Henderson JP, Byun J, Williams MV, Mueller DM, McCormick ML, Heinecke JW. Production of brominating intermediates by myeloperoxidase. A transhalogenation pathway for generating mutagenic nucleobases during infl ammation. J Biol Chem 2001;276:7867-7875.
    • (2001) J Biol Chem , vol.276 , pp. 7867-7875
    • Henderson, J.P.1    Byun, J.2    Williams, M.V.3    Mueller, D.M.4    McCormick, M.L.5    Heinecke, J.W.6
  • 61
    • 10944248830 scopus 로고    scopus 로고
    • Endogenous formation of novel halogenated 2 -deoxycytidine. Hypohalous acid-mediated DNA modifi cation at the site of infl ammation
    • Kawai Y, Morinaga H, Kondo H, Miyoshi N, Nakamura Y, Uchida K, et al. Endogenous formation of novel halogenated 2 -deoxycytidine. Hypohalous acid-mediated DNA modifi cation at the site of infl ammation. J Biol Chem 2004;279:51241-51249.
    • (2004) J Biol Chem , vol.279 , pp. 51241-51249
    • Kawai, Y.1    Morinaga, H.2    Kondo, H.3    Miyoshi, N.4    Nakamura, Y.5    Uchida, K.6
  • 63
    • 20344391164 scopus 로고    scopus 로고
    • Expression of human myeloperoxidase by macrophages promotes atherosclerosis in mice
    • McMillen TS, Heinecke JW, LeBoeuf RC. Expression of human myeloperoxidase by macrophages promotes atherosclerosis in mice. Circulation 2005;111:2798-2804.
    • (2005) Circulation , vol.111 , pp. 2798-2804
    • McMillen, T.S.1    Heinecke, J.W.2    Leboeuf, R.C.3
  • 64
    • 0013784519 scopus 로고
    • Reactions of cyanate with functional groups of proteins. III. Reactions with amino and carboxyl groups
    • Stark GR. Reactions of cyanate with functional groups of proteins. III. Reactions with amino and carboxyl groups. Biochemistry 1965;4:1030-1036.
    • (1965) Biochemistry , vol.4 , pp. 1030-1036
    • Stark, G.R.1
  • 65
    • 77957013700 scopus 로고    scopus 로고
    • Modifi cation of proteins with cyanate
    • Stark GR. Modifi cation of proteins with cyanate. Meth Enzymol 1998;25:579-584.
    • (1998) Meth Enzymol , vol.25 , pp. 579-584
    • Stark, G.R.1
  • 66
    • 77249152615 scopus 로고    scopus 로고
    • Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations
    • Koelsch M, Mallak R, Graham GG, Kajer T, Milligan MK, Nguyen LQ, et al. Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations. Biochem Pharmacol 2010;79:1156-1164.
    • (2010) Biochem Pharmacol , vol.79 , pp. 1156-1164
    • Koelsch, M.1    Mallak, R.2    Graham, G.G.3    Kajer, T.4    Milligan, M.K.5    Nguyen, L.Q.6
  • 67
    • 0033515469 scopus 로고    scopus 로고
    • Transient and steady-state kinetics of the oxidation of substituted benzoic acid hydrazides by myeloperoxidase
    • Burner U, Obinger C, Paumann M, Furtmuller PG, Kettle AJ. Transient and steady-state kinetics of the oxidation of substituted benzoic acid hydrazides by myeloperoxidase. J Biol Chem 1999;274:9494-9502.
    • (1999) J Biol Chem , vol.274 , pp. 9494-9502
    • Burner, U.1    Obinger, C.2    Paumann, M.3    Furtmuller, P.G.4    Kettle, A.J.5
  • 68
    • 0033833128 scopus 로고    scopus 로고
    • Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production
    • Kettle AJ, Candaeis LP. Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production. Redox Rep 2000;5: 179-184.
    • (2000) Redox Rep , vol.5 , pp. 179-184
    • Kettle, A.J.1    Candaeis, L.P.2
  • 70
    • 0031029267 scopus 로고    scopus 로고
    • Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic hydrazide
    • Kettle AJ, Geyde CA, Winterbourn CC. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic hydrazide. Biochem J 1997;321:503-508.
    • (1997) Biochem J , vol.321 , pp. 503-508
    • Kettle, A.J.1    Geyde, C.A.2    Winterbourn, C.C.3
  • 72
    • 0026701776 scopus 로고
    • Oxidation of hydroquinone by myeloperoxidase-mechanism of stimulation by benzoquinone
    • Kettle AJ, Winterbourn CC. Oxidation of hydroquinone by myeloperoxidase-mechanism of stimulation by benzoquinone. J Biol Chem 1992;267:8319-8324.
    • (1992) J Biol Chem , vol.267 , pp. 8319-8324
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 74
    • 80054798514 scopus 로고    scopus 로고
    • 2-thioxanthines are mechanism-based inactivators of myeloperoxidase that block oxidative stress during infl ammation
    • Tiden AK, Sjogren T, Svensson M, Bernlind A, Senthilmohan R, Auchere F, et al. 2-thioxanthines are mechanism-based inactivators of myeloperoxidase that block oxidative stress during infl ammation. J Biol Chem 2011;286:37578-37589.
    • (2011) J Biol Chem , vol.286 , pp. 37578-37589
    • Tiden, A.K.1    Sjogren, T.2    Svensson, M.3    Bernlind, A.4    Senthilmohan, R.5    Auchere, F.6
  • 75
    • 0003055993 scopus 로고    scopus 로고
    • Future worldwide health effects of current smoking patterns
    • Koop CE, Pearson CE, Schwartz MR (eds) San Francisco: Jossey-Bass
    • Peto RL. Future worldwide health effects of current smoking patterns. In: Koop CE, Pearson CE, Schwartz MR (eds). Critical issues in global health. San Francisco: Jossey-Bass; 2001.
    • (2001) Critical Issues in Global Health
    • Peto, R.L.1
  • 76
    • 33646700405 scopus 로고    scopus 로고
    • Epidemiology of atherosclerotic vascular disease
    • Lanzer PT, Topel EJ (eds) Berlin: Springer-Verlag
    • O'Donnell CJ, Kannel WB. Epidemiology of atherosclerotic vascular disease. In: Lanzer PT, Topel EJ (eds). Panvascular medicine. Berlin: Springer-Verlag; 2003.
    • (2003) Panvascular Medicine
    • O'Donnell, C.J.1    Kannel, W.B.2
  • 78
    • 56649083647 scopus 로고    scopus 로고
    • Smoking and smoking cessation - The relationship between cardiovascular disease and lipoprotein metabolism: A review
    • Chelland Campbell S, Moffatt RJ, Stamford BA. Smoking and smoking cessation-the relationship between cardiovascular disease and lipoprotein metabolism: a review. Atherosclerosis 2008;201:225-235.
    • (2008) Atherosclerosis , vol.201 , pp. 225-235
    • Chelland Campbell, S.1    Moffatt, R.J.2    Stamford, B.A.3
  • 79
    • 0021018858 scopus 로고
    • Cyanide in human disease: A review of clinical and laboratory evidence
    • Wilson J. Cyanide in human disease: a review of clinical and laboratory evidence. Fundam. Appl Toxicol 1983;3: 397-399.
    • (1983) Fundam. Appl Toxicol , vol.3 , pp. 397-399
    • Wilson, J.1
  • 81
    • 0023734032 scopus 로고
    • Serum thiocyanate levels as an objective measure of smoking habits in epidemiological studies
    • Spagnolo A, Torsello S, Morisi G, Petrozzi E, Antonini R, Ricci G, et al. Serum thiocyanate levels as an objective measure of smoking habits in epidemiological studies. Eur J Epidemiol 1988;4:206-211.
    • (1988) Eur J Epidemiol , vol.4 , pp. 206-211
    • Spagnolo, A.1    Torsello, S.2    Morisi, G.3    Petrozzi, E.4    Antonini, R.5    Ricci, G.6
  • 82
    • 2942541144 scopus 로고    scopus 로고
    • Stable compounds of cigarette smoke induce endothelial superoxide anion production via NADPH oxidase activation
    • Jaimes EA, DeMaster EG, Tian RX, Raij L. Stable compounds of cigarette smoke induce endothelial superoxide anion production via NADPH oxidase activation. Arterioscler. Thromb Vasc Biol 2004;24:1031-1036.
    • (2004) Arterioscler. Thromb Vasc Biol , vol.24 , pp. 1031-1036
    • Jaimes, E.A.1    Demaster, E.G.2    Tian, R.X.3    Raij, L.4
  • 84
    • 0032790745 scopus 로고    scopus 로고
    • Metabolic fates in humans of linamarin in cassava fl our ingested as stiff porridge
    • Carlsson L, Mlingi N, Juma A, Ronquist G, Rosling H. Metabolic fates in humans of linamarin in cassava fl our ingested as stiff porridge. Food Chem Toxicol 1999;37:307-312.
    • (1999) Food Chem Toxicol , vol.37 , pp. 307-312
    • Carlsson, L.1    Mlingi, N.2    Juma, A.3    Ronquist, G.4    Rosling, H.5
  • 85
    • 0036285971 scopus 로고    scopus 로고
    • Occupational and dietary exposures of humans to cyanide poisoning from large-scale cassava processing and ingestion of cassava foods
    • Okafor PN, Okorowkwo CO, Maduagwu EN. Occupational and dietary exposures of humans to cyanide poisoning from large-scale cassava processing and ingestion of cassava foods. Food Chem Toxicol 2002;40:1001-1005.
    • (2002) Food Chem Toxicol , vol.40 , pp. 1001-1005
    • Okafor, P.N.1    Okorowkwo, C.O.2    Maduagwu, E.N.3
  • 86
    • 0033991198 scopus 로고    scopus 로고
    • Plant cyanogenic glycosides
    • Vetter J. Plant cyanogenic glycosides. Toxicon 2000;38: 11-36.
    • (2000) Toxicon , vol.38 , pp. 11-36
    • Vetter, J.1
  • 88
    • 0021917838 scopus 로고
    • Blood cyanide and thiocyanate concentrations produced by long-term therapy with sodium nitroprusside
    • Vesey CJ, Cole PV. Blood cyanide and thiocyanate concentrations produced by long-term therapy with sodium nitroprusside. Br J Anaesth 1985;57:148-155.
    • (1985) Br J Anaesth , vol.57 , pp. 148-155
    • Vesey, C.J.1    Cole, P.V.2
  • 89
    • 0346996439 scopus 로고    scopus 로고
    • Myeloperoxidasecatalyzed oxidation of chloroacetonitrile to cyanide
    • Abdel-Naim AB, Mohamadin AM. Myeloperoxidasecatalyzed oxidation of chloroacetonitrile to cyanide. Toxicol Lett 2004;146:249-257.
    • (2004) Toxicol Lett , vol.146 , pp. 249-257
    • Abdel-Naim, A.B.1    Mohamadin, A.M.2
  • 90
    • 84863908587 scopus 로고    scopus 로고
    • Agency USEP, ed. U.S. Environmental Protection Agency, Washington, DC
    • Agency USEP Toxicological review of acetonitrile (Agency USEP, ed.), U.S. Environmental Protection Agency, Washington, DC; 1999.
    • (1999) Agency USEP Toxicological Review of Acetonitrile
  • 93
    • 37549016050 scopus 로고    scopus 로고
    • Reactions of chlorine with inorganic and organic compounds during water treatmentkinetics and mechanisms: A critical review
    • Deborde M, von Gunten U. Reactions of chlorine with inorganic and organic compounds during water treatmentkinetics and mechanisms: a critical review. Water Res 2008; 42:13-51.
    • (2008) Water Res , vol.42 , pp. 13-51
    • Deborde, M.1    Von Gunten, U.2
  • 94
    • 68749097272 scopus 로고    scopus 로고
    • Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: Absolute rate constants and assessment of biological relevance
    • Skaff O, Pattison DI, Davies MJ. Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance. Biochem J 2009;422:111-117.
    • (2009) Biochem J , vol.422 , pp. 111-117
    • Skaff, O.1    Pattison, D.I.2    Davies, M.J.3
  • 95
    • 81855198483 scopus 로고    scopus 로고
    • Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: Determination of absolute rate constants and implications for biological damage
    • Skaff O, Pattison DI, Morgan PE, Bachana R, Jain VK, Priyadarsin KI, et al. Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage. Biochem J 2012;441:305-316.
    • (2012) Biochem J , vol.441 , pp. 305-316
    • Skaff, O.1    Pattison, D.I.2    Morgan, P.E.3    Bachana, R.4    Jain, V.K.5    Priyadarsin, K.I.6
  • 96
    • 72749119238 scopus 로고    scopus 로고
    • Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione
    • Nagy P, Jameson GN, Winterbourn CC. Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione. Chem Res Toxicol 2009;22:1833-1840.
    • (2009) Chem Res Toxicol , vol.22 , pp. 1833-1840
    • Nagy, P.1    Jameson, G.N.2    Winterbourn, C.C.3
  • 97
    • 67649986506 scopus 로고    scopus 로고
    • What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach
    • Pattison DI, Hawkins CL, Davies MJ. What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach. Chem Res Toxicol 2009;22:807-817.
    • (2009) Chem Res Toxicol , vol.22 , pp. 807-817
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 98
    • 77954221839 scopus 로고    scopus 로고
    • Redox chemistry of biological thiols
    • Fishbein JC (ed) Elsevier
    • Nagy P, Winterbourn CC. Redox chemistry of biological thiols. In: Fishbein JC (ed) Advances in molecular toxicology. Elsevier; 2010. pp. 183-222.
    • (2010) Advances in Molecular Toxicology , pp. 183-222
    • Nagy, P.1    Winterbourn, C.C.2
  • 100
  • 101
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds
    • Pattison DI, Davies MJ. Absolute rate constants for the reaction of hypochlorous acid with protein side-chains and peptide bonds. Chem Res Toxicol 2001;14:1453-1464.
    • (2001) Chem Res Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 102
    • 84980284223 scopus 로고
    • Kinetic study of the formation of N-chloramines
    • Antelo JM, Arce F, Parajo M. Kinetic study of the formation of N-chloramines. Int J Chem Kinet 1995;27:637-647.
    • (1995) Int J Chem Kinet , vol.27 , pp. 637-647
    • Antelo, J.M.1    Arce, F.2    Parajo, M.3
  • 103
    • 0034681349 scopus 로고    scopus 로고
    • First steps in the oxidation of sulfur-containing amino acids by hypohalogenation: Very fast generation of intermediate sulfenyl halides and halosulfonium cations
    • Armesto XL, Canle ML, Fernandez MI, Garcia MV, Santaballa J. First steps in the oxidation of sulfur-containing amino acids by hypohalogenation: very fast generation of intermediate sulfenyl halides and halosulfonium cations. Tetrahedron 2000;56:1103-1109.
    • (2000) Tetrahedron , vol.56 , pp. 1103-1109
    • Armesto, X.L.1    Canle, M.L.2    Fernandez, M.I.3    Garcia, M.V.4    Santaballa, J.5
  • 104
    • 0035283131 scopus 로고    scopus 로고
    • Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate
    • Peskin AV, Winterbourn CC. Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate. Free Radic Biol Med 2001;30: 572-579.
    • (2001) Free Radic Biol Med , vol.30 , pp. 572-579
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 105
    • 0030220396 scopus 로고    scopus 로고
    • Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates
    • Prutz WA. Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates. Arch Biochem Biophys 1996;332:110-120.
    • (1996) Arch Biochem Biophys , vol.332 , pp. 110-120
    • Prutz, W.A.1
  • 106
    • 0242321028 scopus 로고    scopus 로고
    • Histamine chloramine reactivity with thiol compounds, ascorbate and methionine and with intracellular glutathione
    • Peskin AV, Winterbourn CC. Histamine chloramine reactivity with thiol compounds, ascorbate and methionine and with intracellular glutathione. Free Radic Biol Med 2003; 35:1252-1260.
    • (2003) Free Radic Biol Med , vol.35 , pp. 1252-1260
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 107
    • 61549097790 scopus 로고    scopus 로고
    • Selenoproteins
    • Lu J, Holmgren A. Selenoproteins. J Biol Chem 2009; 284:723-727.
    • (2009) J Biol Chem , vol.284 , pp. 723-727
    • Lu, J.1    Holmgren, A.2
  • 108
    • 0002231956 scopus 로고
    • Kinetics of reactions between aqueous chlorine and nitrogen compounds
    • Faust ED, Hunter JV (eds) New York: John Wiley and Sons
    • Morris JC. Kinetics of reactions between aqueous chlorine and nitrogen compounds. In: Faust ED, Hunter JV (eds) Principles and applications of water chemistry. New York: John Wiley and Sons; 1967. pp. 23-53.
    • (1967) Principles and Applications of Water Chemistry , pp. 23-53
    • Morris, J.C.1
  • 109
    • 33745629631 scopus 로고    scopus 로고
    • Evidence for rapid inter-and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: Implications for the prevention of hypochlorous acid mediated damage
    • Pattison DI, Davies MJ. Evidence for rapid inter-and intramolecular chlorine transfer reactions of histamine and carnosine chloramines: implications for the prevention of hypochlorous acid mediated damage. Biochemistry 2006; 45:8152-8162.
    • (2006) Biochemistry , vol.45 , pp. 8152-8162
    • Pattison, D.I.1    Davies, M.J.2
  • 110
    • 0344210992 scopus 로고    scopus 로고
    • Consecutive halogen transfer between various functional groups induced by reaction of hypohalous acids: NADH oxidation by halogenated amide groups
    • Prutz WA. Consecutive halogen transfer between various functional groups induced by reaction of hypohalous acids: NADH oxidation by halogenated amide groups. Arch Biochem Biophys 1999;371:107-114.
    • (1999) Arch Biochem Biophys , vol.371 , pp. 107-114
    • Prutz, W.A.1
  • 111
    • 79952950041 scopus 로고    scopus 로고
    • Kinetics of 3-chlorotyrosine formation and loss due to hypochlorous acid and chloramines
    • Curtis MP, Hicks AJ, Neidigh JW. Kinetics of 3-chlorotyrosine formation and loss due to hypochlorous acid and chloramines. Chem Res Toxicol 2011;24:418-428.
    • (2011) Chem Res Toxicol , vol.24 , pp. 418-428
    • Curtis, M.P.1    Hicks, A.J.2    Neidigh, J.W.3
  • 112
    • 0034282230 scopus 로고    scopus 로고
    • Biomarkers of myeloperoxidasederived hypochlorous acid
    • Winterbourn CC, Kettle AJ. Biomarkers of myeloperoxidasederived hypochlorous acid. Free Radic Biol Med 2000; 29:403-409.
    • (2000) Free Radic Biol Med , vol.29 , pp. 403-409
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 113
    • 0034646718 scopus 로고    scopus 로고
    • Reaction of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues gives dichlorinated and aldehydic products in addition to 3-chlorotyrosine
    • Fu S, Wang H, Davies MJ, Dean RT. Reaction of hypochlorous acid with tyrosine and peptidyl-tyrosyl residues gives dichlorinated and aldehydic products in addition to 3-chlorotyrosine. J Biol Chem 2000;275:10851-10857.
    • (2000) J Biol Chem , vol.275 , pp. 10851-10857
    • Fu, S.1    Wang, H.2    Davies, M.J.3    Dean, R.T.4
  • 114
    • 83055197027 scopus 로고    scopus 로고
    • Mechanism of decomposition of the human defense factor hypothiocyanite near physiological pH
    • Kalmar J, Woldegiorgis KL, Biri B, Ashby MT. Mechanism of decomposition of the human defense factor hypothiocyanite near physiological pH. J Am Chem Soc 2011;133: 19911-19921.
    • (2011) J Am Chem Soc , vol.133 , pp. 19911-19921
    • Kalmar, J.1    Woldegiorgis, K.L.2    Biri, B.3    Ashby, M.T.4
  • 115
    • 4143109074 scopus 로고    scopus 로고
    • Reactive sulfur species: Aqueous chemistry of sulfenyl thiocyanates
    • Ashby MT, Aneetha H. Reactive sulfur species: aqueous chemistry of sulfenyl thiocyanates. J Am Chem Soc 2004; 126:10216-10217.
    • (2004) J Am Chem Soc , vol.126 , pp. 10216-10217
    • Ashby, M.T.1    Aneetha, H.2
  • 117
    • 42149155586 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanism of the equilibrium between cysteine sulfenyl thiocyanate and cysteine thiosulfi nate ester in acidic aqueous solution
    • Lemma K, Ashby MT. Reactive sulfur species: kinetics and mechanism of the equilibrium between cysteine sulfenyl thiocyanate and cysteine thiosulfi nate ester in acidic aqueous solution. J Org Chem 2008;73:3017-3023.
    • (2008) J Org Chem , vol.73 , pp. 3017-3023
    • Lemma, K.1    Ashby, M.T.2
  • 118
    • 33846431983 scopus 로고    scopus 로고
    • Kinetics and mechanism of the comproportionation of hypothiocyanous acid and thiocyanate to give thiocyanogen in acidic aqueous solution
    • Nagy P, Lemma K, Ashby MT. Kinetics and mechanism of the comproportionation of hypothiocyanous acid and thiocyanate to give thiocyanogen in acidic aqueous solution. Inorg Chem 2007;46:285-292.
    • (2007) Inorg Chem , vol.46 , pp. 285-292
    • Nagy, P.1    Lemma, K.2    Ashby, M.T.3
  • 119
    • 35948954266 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the reaction of cysteine thiosulfi nate ester with cysteine to give cysteine sulfenic acid
    • Nagy P, Lemma K, Ashby MT. Reactive sulfur species: kinetics and mechanisms of the reaction of cysteine thiosulfi nate ester with cysteine to give cysteine sulfenic acid. J Org Chem 2007;72:8838-8846.
    • (2007) J Org Chem , vol.72 , pp. 8838-8846
    • Nagy, P.1    Lemma, K.2    Ashby, M.T.3
  • 120
    • 37549025070 scopus 로고    scopus 로고
    • Reactive sulfur species: Hydrolysis of hypothiocyanite to give thiocarbamate-S-oxide
    • Nagy P, Wang X, Lemma K, Ashby MT. Reactive sulfur species: hydrolysis of hypothiocyanite to give thiocarbamate-S-oxide. J Am Chem Soc 2007;129:15756-15757.
    • (2007) J Am Chem Soc , vol.129 , pp. 15756-15757
    • Nagy, P.1    Wang, X.2    Lemma, K.3    Ashby, M.T.4
  • 121
    • 57449098410 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanism of the reaction of thiocarbamate-S-oxide with cysteine
    • Wang XG, Ashby MT. Reactive sulfur species: kinetics and mechanism of the reaction of thiocarbamate-S-oxide with cysteine. Chem Res Toxicol 2008;21:2120-2126.
    • (2008) Chem Res Toxicol , vol.21 , pp. 2120-2126
    • Wang, X.G.1    Ashby, M.T.2
  • 123
    • 84859762951 scopus 로고    scopus 로고
    • Hypothiocyanous acid: Benign or deadly?
    • Barrett TJ, Hawkins CL. Hypothiocyanous acid: benign or deadly? Chem Res Toxicol 2012;25:263-273.
    • (2012) Chem Res Toxicol , vol.25 , pp. 263-273
    • Barrett, T.J.1    Hawkins, C.L.2
  • 124
    • 0030708939 scopus 로고    scopus 로고
    • Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid
    • Carr AC, Winterbourn CC. Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid. Biochem J 1997;327:275-281.
    • (1997) Biochem J , vol.327 , pp. 275-281
    • Carr, A.C.1    Winterbourn, C.C.2
  • 125
    • 0034468846 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of thiols: Formation of thiyl radicals and the role of sulfenyl chlorides as intermediates
    • Davies MJ, Hawkins CL. Hypochlorite-induced oxidation of thiols: formation of thiyl radicals and the role of sulfenyl chlorides as intermediates. Free Radic Res 2000;33: 719-729.
    • (2000) Free Radic Res , vol.33 , pp. 719-729
    • Davies, M.J.1    Hawkins, C.L.2
  • 127
    • 0017709671 scopus 로고
    • Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion
    • Aune TM, Thomas EL. Accumulation of hypothiocyanite ion during peroxidase-catalyzed oxidation of thiocyanate ion. Eur J Biochem 1977;80:209-214.
    • (1977) Eur J Biochem , vol.80 , pp. 209-214
    • Aune, T.M.1    Thomas, E.L.2
  • 128
    • 0017707017 scopus 로고
    • Lactoperoxidasecatalyzed incorporation of thiocyanate ion into a protein substrate
    • Aune TM, Thomas EL, Morrison M. Lactoperoxidasecatalyzed incorporation of thiocyanate ion into a protein substrate. Biochemistry 1977;16:4611-4615.
    • (1977) Biochemistry , vol.16 , pp. 4611-4615
    • Aune, T.M.1    Thomas, E.L.2    Morrison, M.3
  • 129
    • 33749422853 scopus 로고    scopus 로고
    • Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method
    • Harwood DT, Kettle AJ, Winterbourn CC. Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method. Biochem J 2006;399:161-168.
    • (2006) Biochem J , vol.399 , pp. 161-168
    • Harwood, D.T.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 130
    • 0023807461 scopus 로고
    • Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide
    • Drozdz R, Naskalski JW, Sznajd J. Oxidation of amino acids and peptides in reaction with myeloperoxidase, chloride and hydrogen peroxide. Biochim Biophys Acta 1988;957:47-52.
    • (1988) Biochim Biophys Acta , vol.957 , pp. 47-52
    • Drozdz, R.1    Naskalski, J.W.2    Sznajd, J.3
  • 131
    • 0015851676 scopus 로고
    • Chlorination studies. II. The reaction of aqueous hypochlorous acid with α-βmino acids and dipeptides
    • Pereira WE, Hoyano Y, Summons RE, Bacon VA, Duffi eld AM. Chlorination studies. II. The reaction of aqueous hypochlorous acid with α-βmino acids and dipeptides. Biochim Biophys Acta 1973;313:170-180.
    • (1973) Biochim Biophys Acta , vol.313 , pp. 170-180
    • Pereira, W.E.1    Hoyano, Y.2    Summons, R.E.3    Bacon, V.A.4    Duffield, A.M.5
  • 132
    • 0017843636 scopus 로고
    • Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion
    • Aune TM, Thomas EL. Oxidation of protein sulfhydryls by products of peroxidase-catalyzed oxidation of thiocyanate ion. Biochemistry 1978;17:1005-1010.
    • (1978) Biochemistry , vol.17 , pp. 1005-1010
    • Aune, T.M.1    Thomas, E.L.2
  • 133
    • 0344410068 scopus 로고    scopus 로고
    • Hypochlorite-induced oxidation of amino acids, peptides and proteins
    • Hawkins CL, Pattison DI, Davies MJ. Hypochlorite-induced oxidation of amino acids, peptides and proteins. Amino Acids 2003;25:259-274.
    • (2003) Amino Acids , vol.25 , pp. 259-274
    • Hawkins, C.L.1    Pattison, D.I.2    Davies, M.J.3
  • 134
    • 36148995826 scopus 로고    scopus 로고
    • Reactive sulfur species: Kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid
    • Nagy P, Ashby MT. Reactive sulfur species: kinetics and mechanisms of the oxidation of cysteine by hypohalous acid to give cysteine sulfenic acid. J Am Chem Soc 2007; 129:14082-14091.
    • (2007) J Am Chem Soc , vol.129 , pp. 14082-14091
    • Nagy, P.1    Ashby, M.T.2
  • 135
    • 84857232751 scopus 로고    scopus 로고
    • Inactivation of thiol-dependent enzymes by hypothiocyanous acid: Role of sulfenyl thiocyanate and sulfenic acid intermediates
    • Barrett TJ, Pattison DI, Leonard SE, Carroll KS, Davies MJ, Hawkins CL. Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates. Free Radic Biol Med 2012;52: 1075-1085.
    • (2012) Free Radic Biol Med , vol.52 , pp. 1075-1085
    • Barrett, T.J.1    Pattison, D.I.2    Leonard, S.E.3    Carroll, K.S.4    Davies, M.J.5    Hawkins, C.L.6
  • 136
    • 34547206251 scopus 로고    scopus 로고
    • Reactions of cysteine sulfenyl thiocyanate with thiols to give unsymmetrical disulfi des
    • Algunindigue Nimmo SL, Lemma K, Ashby MT. Reactions of cysteine sulfenyl thiocyanate with thiols to give unsymmetrical disulfi des. Heteroatom Chem 2007;18:467-471.
    • (2007) Heteroatom Chem , vol.18 , pp. 467-471
    • Algunindigue Nimmo, S.L.1    Lemma, K.2    Ashby, M.T.3
  • 137
    • 0035933821 scopus 로고    scopus 로고
    • Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfi de
    • Pullar JM, Vissers MCM, Winterbourn CC. Glutathione oxidation by hypochlorous acid in endothelial cells produces glutathione sulfonamide as a major product but not glutathione disulfi de. J Biol Chem 2001;276:22120-22125.
    • (2001) J Biol Chem , vol.276 , pp. 22120-22125
    • Pullar, J.M.1    Vissers, M.C.M.2    Winterbourn, C.C.3
  • 138
    • 47549114277 scopus 로고    scopus 로고
    • Molecular structure and dynamic properties of a sulfonamide derivative of glutathione that is produced under conditions of oxidative stress by hypochlorous acid
    • Harwood DT, Nimmo SL, Kettle AJ, Winterbourn CC, Ashby MT. Molecular structure and dynamic properties of a sulfonamide derivative of glutathione that is produced under conditions of oxidative stress by hypochlorous acid. Chem Res Toxicol 2008;21:1011-1016.
    • (2008) Chem Res Toxicol , vol.21 , pp. 1011-1016
    • Harwood, D.T.1    Nimmo, S.L.2    Kettle, A.J.3    Winterbourn, C.C.4    Ashby, M.T.5
  • 139
    • 78650833245 scopus 로고    scopus 로고
    • Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: Association with bacterial infection
    • Harwood DT, Darlow BA, Cheah FC, McNeill N, Graham P, Winterbourn CC. Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: association with bacterial infection. Pediatr Res 2011;69:28-33.
    • (2011) Pediatr Res , vol.69 , pp. 28-33
    • Harwood, D.T.1    Darlow, B.A.2    Cheah, F.C.3    McNeill, N.4    Graham, P.5    Winterbourn, C.C.6
  • 140
    • 70249098135 scopus 로고    scopus 로고
    • Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fl uids by isotope dilution liquid chromatography-tandem mass spectrometry
    • Harwood DT, Kettle AJ, Brennan S, Winterbourn CC. Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fl uids by isotope dilution liquid chromatography-tandem mass spectrometry. J Chromatogr B 2009; 877:3393-3399.
    • (2009) J Chromatogr B , vol.877 , pp. 3393-3399
    • Harwood, D.T.1    Kettle, A.J.2    Brennan, S.3    Winterbourn, C.C.4
  • 141
    • 70350012762 scopus 로고    scopus 로고
    • Hypochlorous acid converts the gamma-glutamyl group of glutathione disulfi de to 5-hydroxybutyrolactam a potential marker for neutrophil activation
    • Yuan W, Wang Y, Heinecke JW, Fu XY. Hypochlorous acid converts the gamma-glutamyl group of glutathione disulfi de to 5-hydroxybutyrolactam, a potential marker for neutrophil activation. J Biol Chem 2009;284:26908-26917.
    • (2009) J Biol Chem , vol.284 , pp. 26908-26917
    • Yuan, W.1    Wang, Y.2    Heinecke, J.W.3    Fu, X.Y.4
  • 142
    • 58949087905 scopus 로고    scopus 로고
    • Tryptophan residues are targets in hypothiocyanous acidmediated protein oxidation
    • Hawkins CL, Pattison DI, Stanley NR, Davies MJ. Tryptophan residues are targets in hypothiocyanous acidmediated protein oxidation. Biochem J 2008;416:441-452.
    • (2008) Biochem J , vol.416 , pp. 441-452
    • Hawkins, C.L.1    Pattison, D.I.2    Stanley, N.R.3    Davies, M.J.4
  • 143
    • 0002870676 scopus 로고
    • Products of the lactoperoxidase-catalysed oxidation of thiocyanate and halides
    • Pruitt KM, Tenovuo JO (eds) New York: Marcel Dekker, Inc.
    • Thomas EL. Products of the lactoperoxidase-catalysed oxidation of thiocyanate and halides. In: Pruitt KM, Tenovuo JO (eds) The lactoperoxidase system: chemistry and biological signifi cance. New York: Marcel Dekker, Inc.; 1985. pp. 31-53.
    • (1985) The Lactoperoxidase System: Chemistry and Biological Signifi Cance , pp. 31-53
    • Thomas, E.L.1
  • 144
    • 0035823537 scopus 로고    scopus 로고
    • Novel intraand inter-molecular sulfi namide bonds in S100A8 produced by hypochlorite oxidation
    • Raftery MJ, Yang Z, Valenzuela SM, Geczy CL. Novel intraand inter-molecular sulfi namide bonds in S100A8 produced by hypochlorite oxidation. J Biol Chem 2001;276:33 393-33401.
    • (2001) J Biol Chem , vol.276 , pp. 33393-33401
    • Raftery, M.J.1    Yang, Z.2    Valenzuela, S.M.3    Geczy, C.L.4
  • 145
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • Dickinson BC, Chang CJ. Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat Chem Biol 2011;7:504-511.
    • (2011) Nat Chem Biol , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 146
    • 78649268193 scopus 로고    scopus 로고
    • Formation, reactivity, and detection of protein sulfenic acids
    • Kettenhofen NJ, Wood MJ. Formation, reactivity, and detection of protein sulfenic acids. Chem Res Toxicol 2010; 23:1633-1646.
    • (2010) Chem Res Toxicol , vol.23 , pp. 1633-1646
    • Kettenhofen, N.J.1    Wood, M.J.2
  • 148
    • 79959340042 scopus 로고    scopus 로고
    • Protein sulfenic acid formation: From cellular damage to redox regulation
    • Roos G, Messens J. Protein sulfenic acid formation: from cellular damage to redox regulation. Free Radic Biol Med 2011;51:314-326.
    • (2011) Free Radic Biol Med , vol.51 , pp. 314-326
    • Roos, G.1    Messens, J.2
  • 149
    • 10944237769 scopus 로고    scopus 로고
    • Characterization of mammalian sulfi redoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfi nic acid in the active site to cysteine
    • Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. Characterization of mammalian sulfi redoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfi nic acid in the active site to cysteine. J Biol Chem 2004;279:50994-51001.
    • (2004) J Biol Chem , vol.279 , pp. 50994-51001
    • Chang, T.S.1    Jeong, W.2    Woo, H.A.3    Lee, S.M.4    Park, S.5    Rhee, S.G.6
  • 151
    • 77951813369 scopus 로고    scopus 로고
    • Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H 2 O 2 in red blood cells
    • Cho CS, Lee S, Lee GT, Woo HA, Choi EJ, Rhee SG. Irreversible inactivation of glutathione peroxidase 1 and reversible inactivation of peroxiredoxin II by H 2 O 2 in red blood cells. Antioxid Redox Signal 2010;12:1235-1246.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 1235-1246
    • Cho, C.S.1    Lee, S.2    Lee, G.T.3    Woo, H.A.4    Choi, E.J.5    Rhee, S.G.6
  • 152
    • 72649087731 scopus 로고    scopus 로고
    • Functions and evolution of selenoprotein methionine sulfoxide reductases
    • Lee BC, Dikiy A, Kim HY, Gladyshev VN. Functions and evolution of selenoprotein methionine sulfoxide reductases. Biochim Biophys Acta 2009;1790:1471-1477.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 1471-1477
    • Lee, B.C.1    Dikiy, A.2    Kim, H.Y.3    Gladyshev, V.N.4
  • 153
    • 72749112786 scopus 로고    scopus 로고
    • Hypochlorous acid reacts with the N-terminal methionines of proteins to give dehydromethionine, a potential biomarker for neutrophil-induced oxidative stress
    • Beal JL, Foster SB, Ashby MT. Hypochlorous acid reacts with the N-terminal methionines of proteins to give dehydromethionine, a potential biomarker for neutrophil-induced oxidative stress. Biochemistry 2009;48:11142-11148.
    • (2009) Biochemistry , vol.48 , pp. 11142-11148
    • Beal, J.L.1    Foster, S.B.2    Ashby, M.T.3
  • 154
    • 70350222052 scopus 로고    scopus 로고
    • Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils
    • Peskin AV, Turner R, Maghzal GJ, Winterbourn CC, Kettle AJ. Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils. Biochemistry 2009;48:10175-10182.
    • (2009) Biochemistry , vol.48 , pp. 10175-10182
    • Peskin, A.V.1    Turner, R.2    Maghzal, G.J.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 155
    • 0031819753 scopus 로고    scopus 로고
    • Reduction of methionine selenoxide to selenomethionine by glutathione
    • Assmann A, Briviba K, Sies H. Reduction of methionine selenoxide to selenomethionine by glutathione. Arch Biochem Biophys 1998;349:201-203.
    • (1998) Arch Biochem Biophys , vol.349 , pp. 201-203
    • Assmann, A.1    Briviba, K.2    Sies, H.3
  • 156
    • 81855209007 scopus 로고    scopus 로고
    • Catalytic activity of selenomethionine in removing amino acid peptide, and protein hydroperoxides
    • Suryo Rahmanto A, Davies MJ. Catalytic activity of selenomethionine in removing amino acid, peptide, and protein hydroperoxides Free Radic Biol Med 2011;51:2288-2299.
    • (2011) Free Radic Biol Med , vol.51 , pp. 2288-2299
    • Suryo Rahmanto, A.1    Davies, M.J.2
  • 157
  • 158
    • 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. Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromamines. J Biol Chem 1995;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
  • 159
    • 0346613555 scopus 로고    scopus 로고
    • Reaction of hocl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centered radicals
    • Hawkins CL, Davies MJ. Reaction of hocl with amino acids and peptides: EPR evidence for rapid rearrangement and fragmentation reactions of nitrogen-centered radicals. J Chem Soc Perkin Trans 2 1998;1937-1945.
    • (1998) J Chem Soc Perkin Trans , vol.2 , pp. 1937-1945
    • Hawkins, C.L.1    Davies, M.J.2
  • 160
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • Hawkins CL, Davies MJ. Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation. Biochem J 1998;332:617-625.
    • (1998) Biochem J , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 161
    • 5344271785 scopus 로고    scopus 로고
    • Chlorine transfer between glycine, taurine and histamine: Reaction rates and impact on cellular reactivity
    • Peskin AV, Midwinter RG, Harwood DT, Winterbourn CC. Chlorine transfer between glycine, taurine and histamine: reaction rates and impact on cellular reactivity. Free Radic Biol Med 2004;37:1622-1630.
    • (2004) Free Radic Biol Med , vol.37 , pp. 1622-1630
    • Peskin, A.V.1    Midwinter, R.G.2    Harwood, D.T.3    Winterbourn, C.C.4
  • 162
    • 34548206228 scopus 로고    scopus 로고
    • Hypochlorous acidmediated protein oxidation: How important are chloramine transfer reactions and protein tertiary structure?
    • Pattison DI, Hawkins CL, Davies MJ. Hypochlorous acidmediated protein oxidation: how important are chloramine transfer reactions and protein tertiary structure? Biochemistry 2007;46:9853-9864.
    • (2007) Biochemistry , vol.46 , pp. 9853-9864
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 163
    • 0035883949 scopus 로고    scopus 로고
    • Oxidation of nadh by chloramines and chloramides and its activation by iodide and by tertiary amines
    • Prutz WA, Kissner R, Koppenol WH. Oxidation of nadh by chloramines and chloramides and its activation by iodide and by tertiary amines. Arch Biochem Biophys 2001;393:297-307.
    • (2001) Arch Biochem Biophys , vol.393 , pp. 297-307
    • Prutz, W.A.1    Kissner, R.2    Koppenol, W.H.3
  • 164
    • 0019889026 scopus 로고
    • Lactoperoxidase-catalyzed oxidation of thiocyanate: Equilibria between oxidized forms of thiocyanate
    • Thomas EL. Lactoperoxidase-catalyzed oxidation of thiocyanate: equilibria between oxidized forms of thiocyanate. Biochemistry 1981;20:3273-3280.
    • (1981) Biochemistry , vol.20 , pp. 3273-3280
    • Thomas, E.L.1
  • 165
    • 33645449729 scopus 로고    scopus 로고
    • Specifi c sequence motifs direct the oxygenation and chlorination of tryptophan by myeloperoxidase
    • Fu X, Wang Y, Kao J, Irwin A, d'Avignon A, Mecham RP, et al. Specifi c sequence motifs direct the oxygenation and chlorination of tryptophan by myeloperoxidase. Biochemistry 2006;45:3961-3971.
    • (2006) Biochemistry , vol.45 , pp. 3961-3971
    • Fu, X.1    Wang, Y.2    Kao, J.3    Irwin, A.4    D'Avignon, A.5    Mecham, R.P.6
  • 166
    • 1342346608 scopus 로고    scopus 로고
    • Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: Specifi c structural motifs control protein oxidation
    • Fu X, Kao JLF, Bergt C, Kassim SY, Huq NP, d'Avignon A, et al. Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specifi c structural motifs control protein oxidation. J Biol Chem 2004;279:6209-6212.
    • (2004) J Biol Chem , vol.279 , pp. 6209-6212
    • Fu, X.1    Kao, J.L.F.2    Bergt, C.3    Kassim, S.Y.4    Huq, N.P.5    D'Avignon, A.6
  • 167
    • 27144440590 scopus 로고    scopus 로고
    • Inactivation of protease inhibitors and lysozyme by hypochlorous acid: Role of side-chain oxidation and protein unfolding in loss of biological function
    • Hawkins CL, Davies MJ. Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function. Chem Res Toxicol 2005;18:1600-1610.
    • (2005) Chem Res Toxicol , vol.18 , pp. 1600-1610
    • Hawkins, C.L.1    Davies, M.J.2
  • 168
    • 32944455998 scopus 로고    scopus 로고
    • The role of aromatic amino acid oxidation, protein unfolding, and aggregation in the hypobromous acid-induced inactivation of trypsin inhibitor and lysozyme
    • Hawkins CL, Davies MJ. The role of aromatic amino acid oxidation, protein unfolding, and aggregation in the hypobromous acid-induced inactivation of trypsin inhibitor and lysozyme. Chem Res Toxicol 2005;18:1669-1677.
    • (2005) Chem Res Toxicol , vol.18 , pp. 1669-1677
    • Hawkins, C.L.1    Davies, M.J.2
  • 169
    • 55449131962 scopus 로고    scopus 로고
    • Apolipoprotein A-I tryptophan substitution leads to resistance to myeloperoxidase-mediated loss of function
    • Peng DQ, Brubaker G, Wu Z, Zheng L, Willard B, Kinter M, et al. Apolipoprotein A-I tryptophan substitution leads to resistance to myeloperoxidase-mediated loss of function. Arterioscler Thromb Vasc Biol 2008;28:2063-2070.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 2063-2070
    • Peng, D.Q.1    Brubaker, G.2    Wu, Z.3    Zheng, L.4    Willard, B.5    Kinter, M.6
  • 170
    • 0029055476 scopus 로고
    • Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils
    • Domigan NM, Charlton TS, Duncan MW, Winterbourn CC, Kettle AJ. Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J Biol Chem 1995;270:16542-16548.
    • (1995) J Biol Chem , vol.270 , pp. 16542-16548
    • Domigan, N.M.1    Charlton, T.S.2    Duncan, M.W.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 171
    • 1542289811 scopus 로고    scopus 로고
    • Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes HDL
    • Bergt C, Fu X, Huq NP, Kao J, Heinecke JW. Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes HDL. J Biol Chem 2004;279:7856-7866.
    • (2004) J Biol Chem , vol.279 , pp. 7856-7866
    • Bergt, C.1    Fu, X.2    Huq, N.P.3    Kao, J.4    Heinecke, J.W.5
  • 172
    • 12844268120 scopus 로고    scopus 로고
    • Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol effl ux from macrophages
    • Zheng L, Settle M, Brubaker G, Schmitt D, Hazen SL, Smith JD, et al. Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol effl ux from macrophages. J Biol Chem 2005;280:38-47.
    • (2005) J Biol Chem , vol.280 , pp. 38-47
    • Zheng, L.1    Settle, M.2    Brubaker, G.3    Schmitt, D.4    Hazen, S.L.5    Smith, J.D.6
  • 173
    • 14044250955 scopus 로고    scopus 로고
    • Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport
    • Shao B, Bergt C, Fu X, Green P, Voss JC, Oda MN, et al. Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport. J Biol Chem 2005;280:5983-5993.
    • (2005) J Biol Chem , vol.280 , pp. 5983-5993
    • Shao, B.1    Bergt, C.2    Fu, X.3    Green, P.4    Voss, J.C.5    Oda, M.N.6
  • 174
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • Hampton MB, Kettle AJ, Winterbourn CC. Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing. Blood 1998;92:3007-3017.
    • (1998) Blood , vol.92 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 175
    • 16244397401 scopus 로고    scopus 로고
    • Signifi cance of the lactoperoxidase system in the dairy industry and its potential applications: A review
    • Seifu E, Buys EM, Donkin EF. Signifi cance of the lactoperoxidase system in the dairy industry and its potential applications: a review. Trends Food Sci Technol 2005;16: 137-154.
    • (2005) Trends Food Sci Technol , vol.16 , pp. 137-154
    • Seifu, E.1    Buys, E.M.2    Donkin, E.F.3
  • 176
    • 0027143114 scopus 로고
    • Antibacterial activity of the lactoperoxidase system - A review
    • Wolfson LM, Sumner SS. Antibacterial activity of the lactoperoxidase system-a review. J Food Protect 1993;56: 887-892.
    • (1993) J Food Protect , vol.56 , pp. 887-892
    • Wolfson, L.M.1    Sumner, S.S.2
  • 177
    • 0001256839 scopus 로고    scopus 로고
    • Structure, functions and applications of lactoperoxidase in natural antimicrobial systems
    • de Wit JN, van Hooydonk ACM. Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Neth Milk Dairy J 1996;50:227-244.
    • (1996) Neth Milk Dairy J , vol.50 , pp. 227-244
    • De Wit, J.N.1    Van Hooydonk, A.C.M.2
  • 178
    • 0000877556 scopus 로고
    • Lactoperoxidase antibacterial system-natural occurrence, biological functions and practical applications
    • Reiter B, Harnulv G. Lactoperoxidase antibacterial system-natural occurrence, biological functions and practical applications. J Food Protect 1984;47:724-732.
    • (1984) J Food Protect , vol.47 , pp. 724-732
    • Reiter, B.1    Harnulv, G.2
  • 179
    • 0000997859 scopus 로고
    • The lactoperoxidase/thiocyanate/hydrogen peroxide system as a temporary preservative for raw milk in developing countries
    • Bjorck L, Claesson O, Schulthess W. The lactoperoxidase/thiocyanate/ hydrogen peroxide system as a temporary preservative for raw milk in developing countries. Milchwissenschaft 1979;34:726-729.
    • (1979) Milchwissenschaft , vol.34 , pp. 726-729
    • Bjorck, L.1    Claesson, O.2    Schulthess, W.3
  • 180
    • 0007566765 scopus 로고
    • Increasing the keeping quality of raw milk by activation of the lactoperoxidase system Results from Sri Lanka
    • Harnulv BG, Kandasamy C. Increasing the keeping quality of raw milk by activation of the lactoperoxidase system. Results from Sri Lanka. Milchwissenschaft 1982;37:454-457.
    • (1982) Milchwissenschaft , vol.37 , pp. 454-457
    • Harnulv, B.G.1    Kandasamy, C.2
  • 181
    • 0018099284 scopus 로고
    • Lactoperoxidase, peroxide, thiocyanate antimicrobial system: Correlation of sulfhydryl oxidation with antimicrobial action
    • Thomas EL, Aune TM. Lactoperoxidase, peroxide, thiocyanate antimicrobial system: correlation of sulfhydryl oxidation with antimicrobial action. Infect Immun 1978;20:456-463.
    • (1978) Infect Immun , vol.20 , pp. 456-463
    • Thomas, E.L.1    Aune, T.M.2
  • 182
    • 0013936363 scopus 로고
    • The inhibition of Streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide - The oxidation of thiocyanate and the nature of the inhibitory compound
    • Oram JD, Reiter B. The inhibition of Streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide-the oxidation of thiocyanate and the nature of the inhibitory compound. Biochem J 1966;100:382-388.
    • (1966) Biochem J , vol.100 , pp. 382-388
    • Oram, J.D.1    Reiter, B.2
  • 183
    • 0018667916 scopus 로고
    • Antibacterial action of lactoperoxidasethiocyanate-hydrogen peroxide on Streptococcus agalactiae
    • Mickelson MN. Antibacterial action of lactoperoxidasethiocyanate-hydrogen peroxide on Streptococcus agalactiae. Appl Environ Microbiol 1979;38:821-826.
    • (1979) Appl Environ Microbiol , vol.38 , pp. 821-826
    • Mickelson, M.N.1
  • 184
    • 0017356851 scopus 로고
    • Hypothiocyanite ion; The inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. I. Identifi cation of the inhibiting compound
    • Hoogendoorn H, Piessens JP, Scholtes W, Stoddard LA. Hypothiocyanite ion; the inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. I. Identifi cation of the inhibiting compound. Caries Res 1977;11:77-84.
    • (1977) Caries Res , vol.11 , pp. 77-84
    • Hoogendoorn, H.1    Piessens, J.P.2    Scholtes, W.3    Stoddard, L.A.4
  • 185
    • 0020665392 scopus 로고
    • Hydrogen peroxide excretion by oral Streptococci and effect of lactoperoxidase-thiocyanatehydrogen peroxide
    • Carlsson J, Iwami Y, Yamada T. Hydrogen peroxide excretion by oral Streptococci and effect of lactoperoxidase-thiocyanatehydrogen peroxide. Infect Immun 1983;40:70-80.
    • (1983) Infect Immun , vol.40 , pp. 70-80
    • Carlsson, J.1    Iwami, Y.2    Yamada, T.3
  • 186
    • 0002607532 scopus 로고
    • Biochemistry of peroxidase system: Antimicrobial effects
    • Pruitt KM, Tenovuo J (eds) New York: Marcel Dekker
    • Pruitt KM, Reiter B. Biochemistry of peroxidase system: antimicrobial effects. In: Pruitt KM, Tenovuo J (eds) The lactoperoxidase system: chemistry and biological signifi-cance. New York: Marcel Dekker; 1985. pp. 143-178.
    • (1985) The Lactoperoxidase System: Chemistry and Biological Signifi-cance , pp. 143-178
    • Pruitt, K.M.1    Reiter, B.2
  • 187
    • 0035072117 scopus 로고    scopus 로고
    • Inhibition of e scherichia coli respiratory enzymes by the lactoperoxidase-hydrogen peroxide-thiocyanate antimicrobial system
    • Shin K, Hayasawa H, Lonnerdal B. Inhibition of E scherichia coli respiratory enzymes by the lactoperoxidase-hydrogen peroxide-thiocyanate antimicrobial system. J Appl Microbiol 2001;90:489-493.
    • (2001) J Appl Microbiol , vol.90 , pp. 489-493
    • Shin, K.1    Hayasawa, H.2    Lonnerdal, B.3
  • 188
    • 0036179432 scopus 로고    scopus 로고
    • Susceptibility of Helicobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system
    • Shin K, Yamauchi K, Teraguchi S, Hayasawa H, Imoto I. Susceptibility of Helicobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system. J Med Microbiol 2002;51:231-237.
    • (2002) J Med Microbiol , vol.51 , pp. 231-237
    • Shin, K.1    Yamauchi, K.2    Teraguchi, S.3    Hayasawa, H.4    Imoto, I.5
  • 189
    • 0028815793 scopus 로고
    • Thiocyanate a plausible physiological electron-donor of gastric peroxidase
    • Das D, De PK, Banerjee RK. Thiocyanate, a plausible physiological electron-donor of gastric peroxidase. Biochem J 1995;305:59-64.
    • (1995) Biochem J , vol.305 , pp. 59-64
    • Das, D.1    De Pk Banerjee, R.K.2
  • 190
    • 58149214250 scopus 로고    scopus 로고
    • Inorganic chemistry of defensive peroxidases in the human oral cavity
    • Ashby MT. Inorganic chemistry of defensive peroxidases in the human oral cavity. J Dent Res 2008;87:900-914.
    • (2008) J Dent Res , vol.87 , pp. 900-914
    • Ashby, M.T.1
  • 191
    • 0023405416 scopus 로고
    • The salivary peroxidase system: Thermodynamic, kinetic and antibacterial properties
    • Pruitt KM. The salivary peroxidase system: thermodynamic, kinetic and antibacterial properties. J Oral Pathol 1987;16: 417-420.
    • (1987) J Oral Pathol , vol.16 , pp. 417-420
    • Pruitt, K.M.1
  • 192
    • 0024570884 scopus 로고
    • Crevicular fl uid myeloperoxidase at healthy, gingivitis and periodontitis sites
    • Cao CF. Crevicular fl uid myeloperoxidase at healthy, gingivitis and periodontitis sites. J Clin Periodontol 1989;16:17-20.
    • (1989) J Clin Periodontol , vol.16 , pp. 17-20
    • Cao, C.F.1
  • 193
    • 0030586863 scopus 로고    scopus 로고
    • Thiocyanate levels in human saliva-quantifi cation by fourier transform infrared spectroscopy
    • Schultz CP, Ahmed AH, Dawes C, Mantsch HH. Thiocyanate levels in human saliva-quantifi cation by fourier transform infrared spectroscopy. Anal Biochem 1996;240:7-12.
    • (1996) Anal Biochem , vol.240 , pp. 7-12
    • Schultz, C.P.1    Ahmed, A.H.2    Dawes, C.3    Mantsch, H.H.4
  • 195
    • 0020174541 scopus 로고
    • Peroxidase antimicrobial system of human saliva: Hypothiocyanite levels in resting and stimulated saliva
    • Tenovuo J, Pruitt KM, Thomas EL. Peroxidase antimicrobial system of human saliva: hypothiocyanite levels in resting and stimulated saliva. J Dent Res 1982;61:982-985.
    • (1982) J Dent Res , vol.61 , pp. 982-985
    • Tenovuo, J.1    Pruitt, K.M.2    Thomas, E.L.3
  • 196
    • 0013913480 scopus 로고
    • Inhibitory effect of saliva on glutamic acid accumulation by Lactobacillus acidophilus and role of lactoperoxidase-thiocyanate system
    • Clem W, Klebanof S. Inhibitory effect of saliva on glutamic acid accumulation by Lactobacillus acidophilus and role of lactoperoxidase- thiocyanate system. J Bacteriol 1966;91:1848-1853.
    • (1966) J Bacteriol , vol.91 , pp. 1848-1853
    • Clem, W.1    Klebanof, S.2
  • 197
    • 0020446229 scopus 로고
    • Streptococcus mutans S treptococcus mitis, and Actinomyces viscosus in the presence of human saliva
    • Germaine GR, Tellefson LM. Streptococcus mutans, S treptococcus mitis, and Actinomyces viscosus in the presence of human saliva. Infect Immun 1982;38:1060-1067.
    • (1982) Infect Immun , vol.38 , pp. 1060-1067
    • Germaine, G.R.1    Tellefson, L.M.2
  • 198
    • 0019503511 scopus 로고
    • Inhibition of dental plaque acid production by the salivary lactoperoxidase antimicrobial system
    • Tenovuo J, Mansson-Rahemtulla B, Pruitt KM, Arnold R. Inhibition of dental plaque acid production by the salivary lactoperoxidase antimicrobial system. Infect Immun 1981; 34:208-214.
    • (1981) Infect Immun , vol.34 , pp. 208-214
    • Tenovuo, J.1    Mansson-Rahemtulla, B.2    Pruitt, K.M.3    Arnold, R.4
  • 199
    • 0026874841 scopus 로고
    • Antimicrobial factors of saliva in relation to dental caries and salivary levels of mutans Streptococci
    • Tenovuo J, Jentsch H, Soukka T, Karhuvaara L. Antimicrobial factors of saliva in relation to dental caries and salivary levels of mutans Streptococci. J Biol Buccale 1992;20:85-90.
    • (1992) J Biol Buccale , vol.20 , pp. 85-90
    • Tenovuo, J.1    Jentsch, H.2    Soukka, T.3    Karhuvaara, L.4
  • 200
    • 0021274287 scopus 로고
    • Bactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures
    • Carlsson J, Edlund MB, Hanstrom L. Bactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures. Infect Immun 1984;44:581-586.
    • (1984) Infect Immun , vol.44 , pp. 581-586
    • Carlsson, J.1    Edlund, M.B.2    Hanstrom, L.3
  • 201
    • 0006522269 scopus 로고    scopus 로고
    • Effect of peroxidase-generated hypothiocyanite on the survival rate of Porphyromonas gingivalis-NCTC 11834
    • Fadel M, Courtois P. Effect of peroxidase-generated hypothiocyanite on the survival rate of Porphyromonas gingivalis-NCTC 11834. Med Sci Res 1999;27:667-669.
    • (1999) Med Sci Res , vol.27 , pp. 667-669
    • Fadel, M.1    Courtois, P.2
  • 202
    • 0018946559 scopus 로고
    • Bactericidal effect of hydrogen peroxide is prevented by the lactoperoxidase-thiocyanate system under anaerobic conditions
    • Carlsson J. Bactericidal effect of hydrogen peroxide is prevented by the lactoperoxidase-thiocyanate system under anaerobic conditions. Infect Immun 1980;29:1190-1192.
    • (1980) Infect Immun , vol.29 , pp. 1190-1192
    • Carlsson, J.1
  • 203
    • 0020041510 scopus 로고
    • Lactoperoxidase and thiocyanate protect bacteria from hydrogen-peroxide
    • Adamson M, Carlsson J. Lactoperoxidase and thiocyanate protect bacteria from hydrogen-peroxide. Infect Immun 1982;35:20-24.
    • (1982) Infect Immun , vol.35 , pp. 20-24
    • Adamson, M.1    Carlsson, J.2
  • 204
    • 0029989505 scopus 로고    scopus 로고
    • Purifi cation of nadh: Hypothiocyanite oxidoreductase in Streptococcus sanguis
    • Courtois PH, Pourtois M. Purifi cation of nadh: hypothiocyanite oxidoreductase in Streptococcus sanguis. Biochem Mol Med 1996;57:134-138.
    • (1996) Biochem Mol Med , vol.57 , pp. 134-138
    • Courtois, P.H.1    Pourtois, M.2
  • 205
    • 0013935126 scopus 로고
    • The inhibition of Streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide - The effect of the inhibitory system on susceptible and resistant strains of group N Streptococci
    • Oram JD, Reiter B. The inhibition of Streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide-the effect of the inhibitory system on susceptible and resistant strains of group N Streptococci. Biochem J 1966;100:373-381.
    • (1966) Biochem J , vol.100 , pp. 373-381
    • Oram, J.D.1    Reiter, B.2
  • 206
    • 0141451907 scopus 로고    scopus 로고
    • Human salivary peroxidase-catalyzed oxidation of nitrite and nitration of salivary components 4-hydroxyphenylacetic acid and proteins
    • Takahama U, Hirotab S, Nishioka T, Onikia T. Human salivary peroxidase-catalyzed oxidation of nitrite and nitration of salivary components 4-hydroxyphenylacetic acid and proteins. Arch Oral Biol 2003;48:679-690.
    • (2003) Arch Oral Biol , vol.48 , pp. 679-690
    • Takahama, U.1    Hirotab, S.2    Nishioka, T.3    Onikia, T.4
  • 207
    • 0021153060 scopus 로고
    • The distribution and function of peroxidases in the respiratory tract
    • Christensen TG. The distribution and function of peroxidases in the respiratory tract. Surv Synth Pathol Res 1984;3:201-218.
    • (1984) Surv Synth Pathol Res , vol.3 , pp. 201-218
    • Christensen, T.G.1
  • 211
    • 0033898228 scopus 로고    scopus 로고
    • Permeation through the CFTR chloride channel
    • McCarty N. Permeation through the CFTR chloride channel. J Exp Biol 2000;203:1947-1962.
    • (2000) J Exp Biol , vol.203 , pp. 1947-1962
    • McCarty, N.1
  • 213
    • 33846211109 scopus 로고    scopus 로고
    • The lactoperoxidase system links anion transport to host defense in cystic fi brosis
    • Conner GE, Wijkstrom-Frei C, Randell SH, Fernandez VE, Salathe M. The lactoperoxidase system links anion transport to host defense in cystic fi brosis. FEBS Lett 2007; 581:271-278.
    • (2007) FEBS Lett , vol.581 , pp. 271-278
    • Conner, G.E.1    Wijkstrom-Frei, C.2    Randell, S.H.3    Fernandez, V.E.4    Salathe, M.5
  • 214
    • 0032950904 scopus 로고    scopus 로고
    • Anion selectivity of apical membrane conductance of CALU 3 human airway epithelium
    • Illek B, Tam AW, Fischer H, Machen TE. Anion selectivity of apical membrane conductance of CALU 3 human airway epithelium. Eur J Physiol 1999;437:812-822.
    • (1999) Eur J Physiol , vol.437 , pp. 812-822
    • Illek, B.1    Tam, A.W.2    Fischer, H.3    MacHen, T.E.4
  • 218
    • 39449133330 scopus 로고    scopus 로고
    • Airway infl ammation in cystic fi brosis
    • Elizur A, Cannon C, Ferkol T. Airway infl ammation in cystic fi brosis. Chest 2008;133:489-495.
    • (2008) Chest , vol.133 , pp. 489-495
    • Elizur, A.1    Cannon, C.2    Ferkol, T.3
  • 220
    • 0031907675 scopus 로고    scopus 로고
    • Serum eosinophil cationic protein, eosinophil protein X and eosinophil peroxidase in relation to pulmonary function in cystic fi brosis
    • Koller DY, Nilsson M, Enander I, Venge P, Eichler I. Serum eosinophil cationic protein, eosinophil protein X and eosinophil peroxidase in relation to pulmonary function in cystic fi brosis. Clin Exp Allergy 1998;28:241-248.
    • (1998) Clin Exp Allergy , vol.28 , pp. 241-248
    • Koller, D.Y.1    Nilsson, M.2    Enander, I.3    Venge, P.4    Eichler, I.5
  • 221
    • 0028240278 scopus 로고
    • Eosinophilic activation in cystic-fi brosis
    • Koller DY, Gotz M, Eichler I, Urbanek R. Eosinophilic activation in cystic-fi brosis. Thorax 1994;49:496-499.
    • (1994) Thorax , vol.49 , pp. 496-499
    • Koller, D.Y.1    Gotz, M.2    Eichler, I.3    Urbanek, R.4
  • 222
    • 0347361658 scopus 로고    scopus 로고
    • Eosinophil peroxidase catalyzes JNK-mediated membrane blebbing in a Rho kinasedependent manner
    • McElhinney B, Poynter ME, Shrivastava P, Hazen SL, Janssen-Heininger YMW. Eosinophil peroxidase catalyzes JNK-mediated membrane blebbing in a Rho kinasedependent manner. J Leukocyte Biol 2003;74:897-907.
    • (2003) J Leukocyte Biol , vol.74 , pp. 897-907
    • McElhinney, B.1    Poynter, M.E.2    Shrivastava, P.3    Hazen, S.L.4    Ymw, J.5
  • 223
    • 4744374195 scopus 로고    scopus 로고
    • NMR analysis of neutrophil samples from patients with activation in sputum cystic fi brosis
    • Saude EJ, Lacy P, Musat-Marcu S, Mayes DC, Bagu J, Man SFP, et al. NMR analysis of neutrophil samples from patients with activation in sputum cystic fi brosis. Magn Reson Med 2004;52:807-814.
    • (2004) Magn Reson Med , vol.52 , pp. 807-814
    • Saude, E.J.1    Lacy, P.2    Musat-Marcu, S.3    Mayes, D.C.4    Bagu, J.5    Man, S.F.P.6
  • 225
    • 0342902619 scopus 로고    scopus 로고
    • Evidence for more extensive deposits of epitopes of oxidized low density lipoproteins in aortas of young people with elevated serum thiocyanate levels
    • Scanlon CEO, Berger B, Malcom G, Wissler RW. Evidence for more extensive deposits of epitopes of oxidized low density lipoproteins in aortas of young people with elevated serum thiocyanate levels. Atherosclerosis 1996;121:23-33.
    • (1996) Atherosclerosis , vol.121 , pp. 23-33
    • Scanlon, C.E.O.1    Berger, B.2    Malcom, G.3    Wissler, R.W.4
  • 226
    • 0030565016 scopus 로고    scopus 로고
    • A comparison of the quantitation of macrophage foam cell populations and the extent of apolipoprotein e deposition in developing atherosclerotic lesions in young people: High and low serum thiocyanate groups as an indication of smoking
    • Botti TP, Amin H, Hiltscher L, Wissler RW. A comparison of the quantitation of macrophage foam cell populations and the extent of apolipoprotein E deposition in developing atherosclerotic lesions in young people: high and low serum thiocyanate groups as an indication of smoking. Atherosclerosis 1996;124:191-202.
    • (1996) Atherosclerosis , vol.124 , pp. 191-202
    • Botti, T.P.1    Amin, H.2    Hiltscher, L.3    Wissler, R.W.4
  • 227
    • 0036493406 scopus 로고    scopus 로고
    • Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-defi cient subjects: Systematic identifi cation of multiple endogenous diffusible substrates for myeloperoxidase in plasma
    • Zhang R, Shen Z, Nauseef WM, Hazen SL. Defects in leukocyte-mediated initiation of lipid peroxidation in plasma as studied in myeloperoxidase-defi cient subjects: systematic identifi cation of multiple endogenous diffusible substrates for myeloperoxidase in plasma. Blood 2002;99:1802-1810.
    • (2002) Blood , vol.99 , pp. 1802-1810
    • Zhang, R.1    Shen, Z.2    Nauseef, W.M.3    Hazen, S.L.4
  • 229
    • 0026637177 scopus 로고
    • Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN/H 2 O 2
    • Lovaas E. Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN/H 2 O 2. Free Radic Biol Med 1992;13:187-195.
    • (1992) Free Radic Biol Med , vol.13 , pp. 187-195
    • Lovaas, E.1
  • 230
    • 33644582884 scopus 로고    scopus 로고
    • The relationship between plasma levels of oxidized and reduced thiols and early atherosclerosis in healthy adults
    • Ashfaq S, Abramson JL, Jones DP, Rhodes SD, Weintraub WS, Hooper WC, et al. The relationship between plasma levels of oxidized and reduced thiols and early atherosclerosis in healthy adults. J Am Coll Cardiol 2006;47:1005-1011.
    • (2006) J Am Coll Cardiol , vol.47 , pp. 1005-1011
    • Ashfaq, S.1    Abramson, J.L.2    Jones, D.P.3    Rhodes, S.D.4    Weintraub, W.S.5    Hooper, W.C.6
  • 231
    • 0001582001 scopus 로고
    • Reactions of the cyanate present in aqueous urea with amino acids and proteins
    • Stark GR, Stein WH, Moore S. Reactions of the cyanate present in aqueous urea with amino acids and proteins. J Biol Chem 1960;235:3177-3181.
    • (1960) J Biol Chem , vol.235 , pp. 3177-3181
    • Stark, G.R.1    Stein, W.H.2    Moore, S.3
  • 233
    • 0026514620 scopus 로고
    • Carbamylation-induced alterations in low-density-lipoprotein metabolism
    • Horkko S, Savolainen MJ, Kervinen K, Kesaniemi YA. Carbamylation-induced alterations in low-density-lipoprotein metabolism. Kidney Int 1992;41:1175-1181.
    • (1992) Kidney Int , vol.41 , pp. 1175-1181
    • Horkko, S.1    Savolainen, M.J.2    Kervinen, K.3    Kesaniemi, Y.A.4
  • 234
    • 0029081948 scopus 로고
    • Carbamylation of proteins and atherogenesis in renal failure
    • Roxborough HE, Young IS. Carbamylation of proteins and atherogenesis in renal failure. Med Hypoth 1995;45:125-128.
    • (1995) Med Hypoth , vol.45 , pp. 125-128
    • Roxborough, H.E.1    Young, I.S.2
  • 235
    • 24944550971 scopus 로고    scopus 로고
    • Carbamylated low density lipoprotein induces death of endothelial cells: A link to atherosclerosis in patients with kidney disease
    • Ok E, Basnakian AG, Apostolov EO, Barri YM, Shah PK. Carbamylated low density lipoprotein induces death of endothelial cells: a link to atherosclerosis in patients with kidney disease. Kidney Int 2005;68:173-178.
    • (2005) Kidney Int , vol.68 , pp. 173-178
    • Ok, E.1    Basnakian, A.G.2    Apostolov, E.O.3    Barri, Y.M.4    Shah, P.K.5
  • 236
    • 66949165904 scopus 로고    scopus 로고
    • Myeloperoxidase-mediated lipoprotein carbamylation as a mechanistic pathway for atherosclerotic vascular disease
    • Sirpal S. Myeloperoxidase-mediated lipoprotein carbamylation as a mechanistic pathway for atherosclerotic vascular disease. Clin Sci 2009;116:681-695.
    • (2009) Clin Sci , vol.116 , pp. 681-695
    • Sirpal, S.1
  • 238
    • 0037180771 scopus 로고    scopus 로고
    • Infl ammation in atherosclerosis
    • Libby P. Infl ammation in atherosclerosis. Nature 2002;420: 868-874.
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 239
    • 84859772469 scopus 로고    scopus 로고
    • The major phagocyte peroxidase-derived oxidant hoscn stimulates the gene specifi c p38 MAPK-dependent NF-αB mediated activation of tissue factor VCAM-1 and ICAM-1 expression in endothelium
    • Rehani T, Jonas A, Slungaard A. The major phagocyte peroxidase-derived oxidant hoscn stimulates the gene specifi c p38 MAPK-dependent NF-αB mediated activation of tissue factor, VCAM-1 and ICAM-1 expression in endothelium. Blood 2010;116:633.
    • (2010) Blood , vol.116 , pp. 633
    • Rehani, T.1    Jonas, A.2    Slungaard, A.3
  • 240
    • 0035411587 scopus 로고    scopus 로고
    • Role of the NF-αB pathway in the pathogenesis of human disease states
    • Yamamoto Y, Gaynor RB. Role of the NF-αB pathway in the pathogenesis of human disease states. Curr Mol Med 2001;1:287-296.
    • (2001) Curr Mol Med , vol.1 , pp. 287-296
    • Yamamoto, Y.1    Gaynor, R.B.2
  • 242
    • 0031662304 scopus 로고    scopus 로고
    • Apoptosis in the atherosclerotic plaque: Quantitative and qualitative aspects
    • Kockx MM. Apoptosis in the atherosclerotic plaque: quantitative and qualitative aspects. Arterioscler Thromb Vasc Biol 1998;18:1519-1522.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1519-1522
    • Kockx, M.M.1
  • 243
    • 68949204491 scopus 로고    scopus 로고
    • Macrophage apoptosis in atherosclerosis: Consequences on plaque progression and the role of endoplasmic reticulum stress
    • Tabas I. Macrophage apoptosis in atherosclerosis: consequences on plaque progression and the role of endoplasmic reticulum stress. Antioxid Redox Signal 2009;11:2333-2339.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 2333-2339
    • Tabas, I.1
  • 244
    • 0038201864 scopus 로고    scopus 로고
    • Pathology of the thin-cap fi broatheroma: A type of vulnerable plaque
    • Virmani R, Burke AP, Kolodgie FD, Farb A. Pathology of the thin-cap fi broatheroma: a type of vulnerable plaque. J Interv Cardiol 2003;16:267-272.
    • (2003) J Interv Cardiol , vol.16 , pp. 267-272
    • Virmani, R.1    Burke, A.P.2    Kolodgie, F.D.3    Farb, A.4
  • 245
    • 0034116663 scopus 로고    scopus 로고
    • Changing concepts of atherogenesis
    • Libby P. Changing concepts of atherogenesis. J Intern Med 2000;247:349-358.
    • (2000) J Intern Med , vol.247 , pp. 349-358
    • Libby, P.1
  • 247
    • 0033596905 scopus 로고    scopus 로고
    • 3-bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: Potential markers for eosinophil-dependent tissue injury in vivo
    • Wu WJ, Chen YH, d'Avignon A, Hazen SL. 3-bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo. Biochemistry 1999;38:3538-3548.
    • (1999) Biochemistry , vol.38 , pp. 3538-3548
    • Wu, W.J.1    Chen, Y.H.2    D'Avignon, A.3    Hazen, S.L.4
  • 248
    • 30544453606 scopus 로고    scopus 로고
    • Role of eosinophil peroxidase in host defence and disease pathology
    • Wang J, Slungaard A. Role of eosinophil peroxidase in host defence and disease pathology. Arch Biochem Biophys 2006;445:256-260.
    • (2006) Arch Biochem Biophys , vol.445 , pp. 256-260
    • Wang, J.1    Slungaard, A.2
  • 249
    • 3242712276 scopus 로고    scopus 로고
    • Redox signaling: Thiol chemistry defi nes which reactive oxygen and nitrogen species can act as second messengers
    • Forman HJ, Fukuto JM, Torres M. Redox signaling: thiol chemistry defi nes which reactive oxygen and nitrogen species can act as second messengers. Am J Physiol Cell Physiol 2004;287:C246-C256.
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Forman, H.J.1    Fukuto, J.M.2    Torres, M.3
  • 253
    • 0000712070 scopus 로고
    • Non-metal redox kinetics: Hypochlorite and hypochlorous acid reactions with cyanide
    • Gerritsen CM, Margerum DW. Non-metal redox kinetics: hypochlorite and hypochlorous acid reactions with cyanide. Inorg Chem 1990;29:2757-2762.
    • (1990) Inorg Chem , vol.29 , pp. 2757-2762
    • Gerritsen, C.M.1    Margerum, D.W.2
  • 254
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls - The cytotoxic potential of superoxide and nitric-oxide
    • Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite oxidation of sulfhydryls-the cytotoxic potential of superoxide and nitric-oxide. J Biol Chem 1991;266:4244-4250.
    • (1991) J Biol Chem , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 256
    • 0036324618 scopus 로고    scopus 로고
    • Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: New insights into the reaction of peroxynitrite with thiols
    • Trujillo M, Radi R. Peroxynitrite reaction with the reduced and the oxidized forms of lipoic acid: new insights into the reaction of peroxynitrite with thiols. Arch Biochem Biophys 2002;397:91-98.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 91-98
    • Trujillo, M.1    Radi, R.2
  • 257
    • 0034657371 scopus 로고    scopus 로고
    • The quantitative oxidation of methionine to methionine sulfoxide by peroxynitrite
    • Perrin D, Koppenol WH. The quantitative oxidation of methionine to methionine sulfoxide by peroxynitrite. Arch Biochem Biophys 2000;377:266-272.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 266-272
    • Perrin, D.1    Koppenol, W.H.2
  • 258
    • 0027974136 scopus 로고
    • One-electron and 2-electron oxidations of methionine by peroxynitrite
    • Pryor WA, Jin X, Squadrito GL. One-electron and 2-electron oxidations of methionine by peroxynitrite. Proc Natl Acad Sci USA 1994;91:11173-11177.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11173-11177
    • Pryor, W.A.1    Jin, X.2    Squadrito, G.L.3
  • 260
    • 0032865515 scopus 로고    scopus 로고
    • Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide
    • Winterbourn CC, Metodiewa D. Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide. Free Radic Biol Med 1999;27:322-328.
    • (1999) Free Radic Biol Med , vol.27 , pp. 322-328
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 261
    • 0027504460 scopus 로고
    • The kinetics of relaxin oxidation by hydrogen-peroxide
    • Nguyen TH, Burnier J, Meng W. The kinetics of relaxin oxidation by hydrogen-peroxide. Pharmaceut Res 1993;10: 1563-1571.
    • (1993) Pharmaceut Res , vol.10 , pp. 1563-1571
    • Nguyen, T.H.1    Burnier, J.2    Meng, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.