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Volumn 1840, Issue 2, 2014, Pages 781-793

Measuring chlorine bleach in biology and medicine

Author keywords

Hypochlorous acid; Inflammation; Myeloperoxidase; Neutrophil; Peroxidase; Reactive oxygen species

Indexed keywords

3 CHLOROTYROSINE; ASCORBIC ACID; BIOLOGICAL MARKER; CHLORAMINE DERIVATIVE; CHLORINE; FLUORESCENT DYE; GLUTATHIONE SULFONAMIDE; HYDROGEN PEROXIDE; HYPOCHLOROUS ACID; METHIONINE; METHIONINE SULFOXIDE; MYELOPEROXIDASE; PEROXIDASE; PLASMALOGEN; REACTIVE OXYGEN METABOLITE; SULFONAMIDE; TAURINE; TOSYLCHLORAMIDE SODIUM; UNCLASSIFIED DRUG; GLUTATHIONE;

EID: 84890130268     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2013.07.004     Document Type: Review
Times cited : (102)

References (173)
  • 1
    • 61849104559 scopus 로고    scopus 로고
    • Air and fire - Carl Wilhelm Scheele, Torbern Bergman, the Royal Society of Sciences and the discovery of oxygen in Uppsala in the year 1772
    • L.O. Sundelof Air and fire - Carl Wilhelm Scheele, Torbern Bergman, the Royal Society of Sciences and the discovery of oxygen in Uppsala in the year 1772 Adv. Exp. Med. Biol. 645 2009 1 6
    • (2009) Adv. Exp. Med. Biol. , vol.645 , pp. 1-6
    • Sundelof, L.O.1
  • 3
    • 84965230905 scopus 로고
    • On the use of certain antiseptic substances in the treatment of infected wounds
    • H.D. Dakin On the use of certain antiseptic substances in the treatment of infected wounds Br. Med. J. 2 1915 318 320
    • (1915) Br. Med. J. , vol.2 , pp. 318-320
    • Dakin, H.D.1
  • 4
    • 85047684347 scopus 로고    scopus 로고
    • Chemical warfare and medical response during World War I
    • DOI 10.2105/AJPH.2007.11930
    • G.J. Fitzgerald Chemical warfare and medical response during World War I Am. J. Public Health 98 2008 611 625 (Pubitemid 351576317)
    • (2008) American Journal of Public Health , vol.98 , Issue.4 , pp. 611-625
    • Fitzgerald, G.J.1
  • 5
    • 0001645466 scopus 로고
    • A peroxidase-mediated antimicrobial system in leukocytes
    • S.J. Klebanoff A peroxidase-mediated antimicrobial system in leukocytes J. Clin. Invest. 46 1967 1078
    • (1967) J. Clin. Invest. , vol.46 , pp. 1078
    • Klebanoff, S.J.1
  • 6
    • 84872476329 scopus 로고    scopus 로고
    • Redox reactions and microbial killing in the neutrophil phagosome
    • C.C. Winterbourn, and A.J. Kettle Redox reactions and microbial killing in the neutrophil phagosome Antioxid. Redox Signal. 18 2013 642 660
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 642-660
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 8
    • 34247496337 scopus 로고    scopus 로고
    • Reactions of superoxide with myeloperoxidase
    • DOI 10.1021/bi602587k
    • A.J. Kettle, R.F. Anderson, M.B. Hampton, and C.C. Winterbourn Reactions of superoxide with myeloperoxidase Biochemistry 46 2007 4888 4897 (Pubitemid 46651210)
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4888-4897
    • Kettle, A.J.1    Anderson, R.F.2    Hampton, M.B.3    Winterbourn, C.C.4
  • 9
    • 84863430573 scopus 로고    scopus 로고
    • What really happens in the neutrophil phagosome?
    • J.K. Hurst What really happens in the neutrophil phagosome? Free Radic. Biol. Med. 53 2012 508 520
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 508-520
    • Hurst, J.K.1
  • 10
    • 0021874027 scopus 로고
    • Neutrophils adherent to a nonphagocytosable surface (glomerular basement membrane) produce oxidants only at the site of attachment
    • M.C.M. Vissers, A.W. Day, and C.C. Winterbourn Neutrophils adherent to a non-phagocytosable surface (glomerular basement membrane) produce oxidants only at the site of attachment Blood 66 1985 161 166 (Pubitemid 15004799)
    • (1985) Blood , vol.66 , Issue.1 , pp. 161-166
    • Vissers, M.C.M.1    Day, W.A.2    Winterbourn, C.C.3
  • 11
    • 43049173503 scopus 로고    scopus 로고
    • Mammalian heme peroxidases: From molecular mechanisms to health implications
    • DOI 10.1089/ars.2007.1927
    • M.J. Davies, C.L. Hawkins, D.I. Pattison, and M.D. Rees Mammalian heme peroxidases: from molecular mechanisms to health implications Antioxid. Redox Signal. 10 2008 1199 1234 (Pubitemid 351634397)
    • (2008) Antioxidants and Redox Signaling , vol.10 , Issue.7 , pp. 1199-1234
    • Davies, M.J.1    Hawkins, C.L.2    Pattison, D.I.3    Rees, M.D.4
  • 13
    • 84868544160 scopus 로고    scopus 로고
    • Vascular peroxidase 1 catalyzes the formation of hypohalous acids: Characterization of its substrate specificity and enzymatic properties
    • H. Li, Z. Cao, G. Zhang, V.J. Thannickal, and G. Cheng Vascular peroxidase 1 catalyzes the formation of hypohalous acids: characterization of its substrate specificity and enzymatic properties Free Radic. Biol. Med. 53 2012 1954 1959
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 1954-1959
    • Li, H.1    Cao, Z.2    Zhang, G.3    Thannickal, V.J.4    Cheng, G.5
  • 14
    • 84865318544 scopus 로고    scopus 로고
    • Peroxidasin: Tying the collagen-sulfilimine knot
    • S.J. Weiss Peroxidasin: tying the collagen-sulfilimine knot Nat. Chem. Biol. 8 2012 740 741
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 740-741
    • Weiss, S.J.1
  • 15
    • 84874350662 scopus 로고    scopus 로고
    • VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids
    • Y. Yang, Z. Cao, L. Tian, W.T. Garvey, and G. Cheng VPO1 mediates ApoE oxidation and impairs the clearance of plasma lipids PLoS One 8 2013 e57571
    • (2013) PLoS One , vol.8 , pp. 57571
    • Yang, Y.1    Cao, Z.2    Tian, L.3    Garvey, W.T.4    Cheng, G.5
  • 16
    • 0030915481 scopus 로고    scopus 로고
    • Myeloperoxidase: A key regulator of neutrophil oxidant product
    • A.J. Kettle, and C.C. Winterbourn Myeloperoxidase: a key regulator of neutrophil oxidant production Redox Rep. 3 1997 3 15 (Pubitemid 27199160)
    • (1997) Redox Report , vol.3 , Issue.1 , pp. 3-15
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 17
    • 0034792757 scopus 로고    scopus 로고
    • Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase
    • DOI 10.1046/j.0014-2956.2001.02449.x
    • J. Arnhold, P.G. Furtmuller, G. Regelsberger, and C. Obinger Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase Eur. J. Biochem. 268 2001 5142 5148 (Pubitemid 32955566)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.19 , pp. 5142-5148
    • Arnhold, J.1    Furtmuller, P.G.2    Regelsberger, G.3    Obinger, C.4
  • 19
    • 0017240322 scopus 로고
    • Studies on the chlorinating activity of myeloperoxidase
    • J.E. Harrison, and J. Shultz Studies on the chlorinating activity of myeloperoxidase J. Biol. Chem. 251 1976 1371 1374
    • (1976) J. Biol. Chem. , vol.251 , pp. 1371-1374
    • Harrison, J.E.1    Shultz, J.2
  • 21
    • 0001526854 scopus 로고
    • Kinetics of reversible chlorine hydrolysis - Temperature-dependence and general acid base-assisted mechanisms
    • T.X. Wang, and D.W. Margerum Kinetics of reversible chlorine hydrolysis - temperature-dependence and general acid base-assisted mechanisms Inorg. Chem. 33 1994 1050 1055
    • (1994) Inorg. Chem. , vol.33 , pp. 1050-1055
    • Wang, T.X.1    Margerum, D.W.2
  • 22
    • 8544251150 scopus 로고
    • The acid ionization constant of HOCl from 5 to 35
    • J.C. Morris The acid ionization constant of HOCl from 5 to 35 J. Phys. Chem. 70 1966 3798 3805
    • (1966) J. Phys. Chem. , vol.70 , pp. 3798-3805
    • Morris, J.C.1
  • 23
    • 37549066891 scopus 로고    scopus 로고
    • Antioxidants as potential therapeutics for lung fibrosis
    • B.J. Day Antioxidants as potential therapeutics for lung fibrosis Antioxid. Redox Signal. 10 2008 355 370
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 355-370
    • Day, B.J.1
  • 24
    • 0019480640 scopus 로고
    • The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
    • DOI 10.1038/290406a0
    • A.W. Segal, M. Geisow, R. Garcia, A. Harper, and R. Miller The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH Nature 290 1981 406 409 (Pubitemid 11158485)
    • (1981) Nature , vol.290 , Issue.5805 , pp. 406-409
    • Segal, A.W.1    Geisow, M.2    Garcia, R.3
  • 25
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • DOI 10.1038/nchembio.85, PII NCHEMBIO85
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286 (Pubitemid 351550893)
    • (2008) Nature Chemical Biology , vol.4 , Issue.5 , pp. 278-286
    • Winterbourn, C.C.1
  • 26
    • 37549016050 scopus 로고    scopus 로고
    • Reactions of chlorine with inorganic and organic compounds during water treatment - Kinetics and mechanisms: A critical review
    • M. Deborde, and U. von Gunten Reactions of chlorine with inorganic and organic compounds during water treatment - kinetics and mechanisms: a critical review Water Res. 42 2008 13 51
    • (2008) Water Res. , vol.42 , pp. 13-51
    • Deborde, M.1    Von Gunten, U.2
  • 27
    • 77956655731 scopus 로고    scopus 로고
    • Elucidating mechanisms of chlorine toxicity: Reaction kinetics, thermodynamics, and physiological implications
    • G.L. Squadrito, E.M. Postlethwait, and S. Matalon Elucidating mechanisms of chlorine toxicity: reaction kinetics, thermodynamics, and physiological implications Am. J. Physiol. 299 2010 L289 300
    • (2010) Am. J. Physiol. , vol.299 , pp. 289-300
    • Squadrito, G.L.1    Postlethwait, E.M.2    Matalon, S.3
  • 28
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • DOI 10.1021/tx0155451
    • D.I. Pattison, and M.J. Davies Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds Chem. Res. Toxicol. 14 2001 1453 1464 (Pubitemid 32983270)
    • (2001) Chemical Research in Toxicology , vol.14 , Issue.10 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 30
    • 0242321028 scopus 로고    scopus 로고
    • Histamine chloramine reactivity with thiol compounds, ascorbate, and methionine and with intracellular glutathione
    • DOI 10.1016/S0891-5849(03)00502-1
    • A.V. Peskin, and C.C. Winterbourn Histamine chloramine reactivity with thiol compounds, ascorbate, and methionine and with intracellular glutathione Free Radic. Biol. Med. 35 2003 1252 1260 (Pubitemid 37357250)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.10 , pp. 1252-1260
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 31
    • 28744458907 scopus 로고    scopus 로고
    • Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3- phosphate dehydrogenase
    • DOI 10.1016/j.freeradbiomed.2005.08.019, PII S0891584905004570
    • A.V. Peskin, and C.C. Winterbourn Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase Free Radic. Biol. Med. 40 2006 45 53 (Pubitemid 41759402)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.1 , pp. 45-53
    • Peskin, A.V.1    Winterbourn, C.C.2
  • 32
    • 58149095815 scopus 로고    scopus 로고
    • Pathways for the decay of organic dichloramines and liberation of antimicrobial chloramine gases
    • M.S.A. Coker, W. Hu, S.T. Senthilmohan, and A.J. Kettle Pathways for the decay of organic dichloramines and liberation of antimicrobial chloramine gases Chem. Res. Toxicol. 21 2008 2334 2343
    • (2008) Chem. Res. Toxicol. , vol.21 , pp. 2334-2343
    • Coker, M.S.A.1    Hu, W.2    Senthilmohan, S.T.3    Kettle, A.J.4
  • 33
    • 1942502782 scopus 로고    scopus 로고
    • Kinetic Analysis of the Reactions of Hypobromous Acid with Protein Components: Implications for Cellular Damage and Use of 3-Bromotyrosine as a Marker of Oxidative Stress
    • DOI 10.1021/bi035946a
    • D.I. Pattison, and M.J. Davies Kinetic analysis of the reactions of hypobromous acid with protein components: implications for cellular damage and use of 3-bromotyrosine as a marker of oxidative stress Biochemistry 43 2004 4799 4809 (Pubitemid 38509101)
    • (2004) Biochemistry , vol.43 , Issue.16 , pp. 4799-4809
    • Pattison, D.I.1    Davies, M.J.2
  • 34
    • 70449679220 scopus 로고    scopus 로고
    • The role of hypothiocyanous acid (HOSCN) in biological systems
    • C.L. Hawkins The role of hypothiocyanous acid (HOSCN) in biological systems Free Radic. Res. 43 2009 1147 1158
    • (2009) Free Radic. Res. , vol.43 , pp. 1147-1158
    • Hawkins, C.L.1
  • 35
    • 84857719465 scopus 로고    scopus 로고
    • Assessing the reactivity of free chlorine constituents Cl-2, Cl2O, and HOCl toward aromatic ethers
    • J.D. Sivey, and A.L. Roberts Assessing the reactivity of free chlorine constituents Cl-2, Cl2O, and HOCl toward aromatic ethers Environ. Sci. Technol. 46 2012 2141 2147
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 2141-2147
    • Sivey, J.D.1    Roberts, A.L.2
  • 36
    • 37049125270 scopus 로고
    • Kinetics and mechanisms of additions to olefinic substances. 12. Kinetics of addition initiated by chlorine acetate
    • P.B.D. Delamare, J. Oconnor, and M.A. Wilson Kinetics and mechanisms of additions to olefinic substances. 12. Kinetics of addition initiated by chlorine acetate J. Chem. Soc. Perkin Trans. 2 1975 1150 1155
    • (1975) J. Chem. Soc. Perkin Trans. , vol.2 , pp. 1150-1155
    • Delamare, P.B.D.1    Oconnor, J.2    Wilson, M.A.3
  • 37
    • 0001663194 scopus 로고
    • Mechanisms of chlorination by hypochlorous acid - Last of chlorinium ion, L +
    • C.G. Swain, and D.R. Crist Mechanisms of chlorination by hypochlorous acid - last of chlorinium ion, L + J. Am. Chem. Soc. 94 1972 3195 3200
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 3195-3200
    • Swain, C.G.1    Crist, D.R.2
  • 38
    • 0001557667 scopus 로고
    • Kinetics of oxidation of tetracyanonickelate(Ii) by chlorine monoxide, chlorine, and hypochlorous acid and kinetics of chlorine monoxide formation
    • M.W. Beach, and D.W. Margerum Kinetics of oxidation of tetracyanonickelate(Ii) by chlorine monoxide, chlorine, and hypochlorous acid and kinetics of chlorine monoxide formation Inorg. Chem. 29 1990 1225 1232
    • (1990) Inorg. Chem. , vol.29 , pp. 1225-1232
    • Beach, M.W.1    Margerum, D.W.2
  • 39
    • 77951815622 scopus 로고    scopus 로고
    • Chlorine monoxide (Cl2O) and molecular chlorine (Cl-2) as active chlorinating agents in reaction of dimethenamid with aqueous free chlorine
    • J.D. Sivey, C.E. McCullough, and A.L. Roberts Chlorine monoxide (Cl2O) and molecular chlorine (Cl-2) as active chlorinating agents in reaction of dimethenamid with aqueous free chlorine Environ. Sci. Technol. 44 2010 3357 3362
    • (2010) Environ. Sci. Technol. , vol.44 , pp. 3357-3362
    • Sivey, J.D.1    McCullough, C.E.2    Roberts, A.L.3
  • 40
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • DOI 10.2174/092986706778773095
    • D.I. Pattison, and M.J. Davies Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases Curr. Med. Chem. 13 2006 3271 3290 (Pubitemid 44669775)
    • (2006) Current Medicinal Chemistry , vol.13 , Issue.27 , pp. 3271-3290
    • Pattison, D.I.1    Davies, M.J.2
  • 41
    • 67649986506 scopus 로고    scopus 로고
    • What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach
    • D.I. Pattison, C.L. Hawkins, and M.J. Davies What are the plasma targets of the oxidant hypochlorous acid? A kinetic modeling approach Chem. Res. Toxicol. 22 2009 807 817
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 807-817
    • Pattison, D.I.1    Hawkins, C.L.2    Davies, M.J.3
  • 44
    • 0032558979 scopus 로고    scopus 로고
    • Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate
    • DOI 10.1021/bi9818772
    • P.G. Fürtmuller, U. Burner, and C. Obinger Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate Biochemistry 37 1998 17923 17930 (Pubitemid 29023948)
    • (1998) Biochemistry , vol.37 , Issue.51 , pp. 17923-17930
    • Furtmuller, P.G.1    Burner, U.2    Obinger, C.3
  • 46
    • 0028211341 scopus 로고
    • Spectral and kinetic studies on the formation of myeloperoxidase compounds I and II: Roles of hydrogen peroxide and superoxide
    • L.A. Marquez, J.T. Huang, and H.B. Dunford Spectral and kinetic studies on the formation of myeloperoxidase compounds I and II: Roles of hydrogen peroxide and superoxide Biochemistry 33 1994 1447 1454 (Pubitemid 24093692)
    • (1994) Biochemistry , vol.33 , Issue.6 , pp. 1447-1454
    • Marquez, L.A.1    Huang, J.T.2    Dunford, H.B.3
  • 47
    • 0024450467 scopus 로고
    • Influence of superoxide on myeloperoxidase kinetics measured with a hydrogen peroxide electrode
    • A.J. Kettle, and C.C. Winterbourn Influence of superoxide on myeloperoxidase kinetics measured with a hydrogen peroxide electrode Biochem. J. 263 1989 823 828 (Pubitemid 19276462)
    • (1989) Biochemical Journal , vol.263 , Issue.3 , pp. 823-828
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 49
    • 0033833128 scopus 로고    scopus 로고
    • Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production
    • A.J. Kettle, and L.P. Candaeis Oxidation of tryptophan by redox intermediates of myeloperoxidase and inhibition of hypochlorous acid production Redox Rep. 5 2000 179 184
    • (2000) Redox Rep. , vol.5 , pp. 179-184
    • Kettle, A.J.1    Candaeis, L.P.2
  • 51
    • 0026079216 scopus 로고
    • Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs
    • A.J. Kettle, and C.C. Winterbourn Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs Biochem. Pharmacol. 41 1991 1485 1492
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1485-1492
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 53
    • 72449125795 scopus 로고    scopus 로고
    • Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione
    • V.F. Ximenes, G.J. Maghzal, R. Turner, Y. Kato, C.C. Winterbourn, and A.J. Kettle Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione Biochem. J. 425 2010 285 293
    • (2010) Biochem. J. , vol.425 , pp. 285-293
    • Ximenes, V.F.1    Maghzal, G.J.2    Turner, R.3    Kato, Y.4    Winterbourn, C.C.5    Kettle, A.J.6
  • 55
    • 0023951778 scopus 로고
    • Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid
    • A.J. Kettle, and C.C. Winterbourn Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid Biochem. J. 252 1988 529 536
    • (1988) Biochem. J. , vol.252 , pp. 529-536
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 56
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • DOI 10.1016/S0076-6879(94)33056-5
    • A.J. Kettle, and C.C. Winterbourn Assays for the chlorination activity of myeloperoxidase Methods Enzymol. 233 1994 502 512 (Pubitemid 24177576)
    • (1994) Methods in Enzymology , vol.233 , pp. 502-512
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 58
    • 0026780059 scopus 로고
    • Reaction of myeloperoxidase with its product HOCl
    • R. Floris, and R. Wever Reaction of myeloperoxidase with its product HOCl Eur. J. Biochem. 207 1992 697 702
    • (1992) Eur. J. Biochem. , vol.207 , pp. 697-702
    • Floris, R.1    Wever, R.2
  • 59
    • 0023370351 scopus 로고
    • Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes
    • M.C.M. Vissers, and C.C. Winterbourn Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes Biochem. J. 245 1987 277 280
    • (1987) Biochem. J. , vol.245 , pp. 277-280
    • Vissers, M.C.M.1    Winterbourn, C.C.2
  • 60
    • 33947093539 scopus 로고
    • Mechanisms of chlorine oxidation of hydrogen peroxide
    • A.M. Held, D.J. Halko, and J.K. Hurst Mechanisms of chlorine oxidation of hydrogen peroxide J. Am. Chem. Soc. 100 1978 5732 5740
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 5732-5740
    • Held, A.M.1    Halko, D.J.2    Hurst, J.K.3
  • 61
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • R.J. Beers, and I.W. Sizer A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase J. Biol. Chem. 195 1952 133 140
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers, R.J.1    Sizer, I.W.2
  • 62
    • 27544498793 scopus 로고    scopus 로고
    • A sensitive and selective assay for chloramine production by myeloperoxidase
    • DOI 10.1016/j.freeradbiomed.2005.07.008, PII S0891584905003953
    • J.M. Dypbukt, C. Bishop, W.M. Brooks, B. Thong, H. Eriksson, and A.J. Kettle A sensitive and selective assay for chloramine production by myeloperoxidase Free Radic. Biol. Med. 39 2005 1468 1477 (Pubitemid 41547227)
    • (2005) Free Radical Biology and Medicine , vol.39 , Issue.11 , pp. 1468-1477
    • Dypbukt, J.M.1    Bishop, C.2    Brooks, W.M.3    Thong, B.4    Eriksson, H.5    Kettle, A.J.6
  • 63
    • 0020478887 scopus 로고
    • The horseradish peroxidase-catalyzed oxidation of 3,5,3′,5′- tetramethylbenzidine. Free radical and charge-transfer complex intermediates
    • P.D. Josephy, T. Eling, and R.P. Mason The horseradish peroxidase-catalyzed oxidation of 3,5,3′,5′-tetramethylbenzidine. Free radical and charge-transfer complex intermediates J. Biol. Chem. 257 1982 3669 3675
    • (1982) J. Biol. Chem. , vol.257 , pp. 3669-3675
    • Josephy, P.D.1    Eling, T.2    Mason, R.P.3
  • 64
    • 30544453005 scopus 로고    scopus 로고
    • Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride
    • DOI 10.1016/j.abb.2005.07.005, PII S0003986105002882
    • R. Senthilmohan, and A.J. Kettle Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride Arch. Biochem. Biophys. 445 2006 235 244 (Pubitemid 43082216)
    • (2006) Archives of Biochemistry and Biophysics , vol.445 , Issue.2 , pp. 235-244
    • Senthilmohan, R.1    Kettle, A.J.2
  • 65
    • 0019988650 scopus 로고
    • Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation
    • S.J. Weiss, R. Klein, A. Slivka, and M. Wei Chlorination of taurine by human neutrophils. Evidence for hypochlorous acid generation J. Clin. Invest. 70 1982 598 607 (Pubitemid 12054584)
    • (1982) Journal of Clinical Investigation , vol.70 , Issue.3 , pp. 598-607
    • Weiss, S.J.1    Klein, R.2    Slivka, A.3    Wei, M.4
  • 66
    • 0034254665 scopus 로고    scopus 로고
    • On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids
    • DOI 10.1006/abbi.2000.1914
    • W.A. Prutz, R. Kissner, W.H. Koppenol, and H. Ruegger On the irreversible destruction of reduced nicotinamide nucleotides by hypohalous acids Arch. Biochem. Biophys. 380 2000 181 191 (Pubitemid 30616785)
    • (2000) Archives of Biochemistry and Biophysics , vol.380 , Issue.1 , pp. 181-191
    • Prutz, W.A.1    Kissner, R.2    Koppenol, W.H.3    Ruegger, H.4
  • 67
    • 0034830639 scopus 로고    scopus 로고
    • Purification and structure of the major product obtained by reaction of NADPH and NMNH with the myeloperoxidase/hydrogen peroxide/chloride system
    • DOI 10.1046/j.1432-1327.2001.02175.x
    • F. Auchere, G. Bertho, I. Artaud, J.P. Girault, and C. Capeillere-Blandin Purification and structure of the major product obtained by reaction of NADPH and NMNH with the myeloperoxidase/hydrogen peroxide/chloride system Eur. J. Biochem. 268 2001 2889 2895 (Pubitemid 32862972)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.10 , pp. 2889-2895
    • Auchere, F.1    Bertho, G.2    Artaud, I.3    Girault, J.P.4    Capeillere-Blandin, C.5
  • 68
    • 2442743845 scopus 로고    scopus 로고
    • NADPH as a co-substrate for studies of the chlorinating activity of myeloperoxidase
    • DOI 10.1042/0264-6021:3430603
    • F. Auchere, and C. Capeillere-Blandin NADPH as a co-substrate for studies of the chlorinating activity of myeloperoxidase Biochem. J. 343 Pt 3 1999 603 613 (Pubitemid 29537372)
    • (1999) Biochemical Journal , vol.343 , Issue.3 , pp. 603-613
    • Auchere, F.1    Capeillere-Blandin, C.2
  • 70
    • 0021807129 scopus 로고
    • Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite
    • DOI 10.1016/0304-4165(85)90120-5
    • C.C. Winterbourn Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of the oxidant to hypochlorite Biochim. Biophys. Acta 840 1985 204 210 (Pubitemid 15049536)
    • (1985) Biochimica et Biophysica Acta - General Subjects , vol.840 , Issue.2 , pp. 204-210
    • Winterbourn, C.C.1
  • 71
    • 0026200339 scopus 로고
    • A spectrophotometric assay for chlorine-containing compounds
    • J.A. Chesney, J.R. Mahoney, and J.W. Eaton A spectrophotometric assay for chlorine-containing compounds Anal. Biochem. 196 1991 262 266
    • (1991) Anal. Biochem. , vol.196 , pp. 262-266
    • Chesney, J.A.1    Mahoney, J.R.2    Eaton, J.W.3
  • 72
    • 0033567245 scopus 로고    scopus 로고
    • Oxidation of clozapine and ascorbate by myeloperoxidase
    • DOI 10.1006/abbi.1999.1328
    • Y. Hsuanyu, and H.B. Dunford Oxidation of clozapine and ascorbate by myeloperoxidase Arch. Biochem. Biophys. 368 1999 413 420 (Pubitemid 29406569)
    • (1999) Archives of Biochemistry and Biophysics , vol.368 , Issue.2 , pp. 413-420
    • Hsuanyu, Y.1    Dunford, H.B.2
  • 75
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • S.P. Wolff Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides Methods Enzymol. 233 1994 182 189
    • (1994) Methods Enzymol. , vol.233 , pp. 182-189
    • Wolff, S.P.1
  • 76
    • 59849120642 scopus 로고    scopus 로고
    • Hypobromous acid and bromamine production by neutrophils and modulation by superoxide
    • A.L. Chapman, O. Skaff, R. Senthilmohan, A.J. Kettle, and M.J. Davies Hypobromous acid and bromamine production by neutrophils and modulation by superoxide Biochem. J. 417 2009 773 781
    • (2009) Biochem. J. , vol.417 , pp. 773-781
    • Chapman, A.L.1    Skaff, O.2    Senthilmohan, R.3    Kettle, A.J.4    Davies, M.J.5
  • 77
    • 84865469048 scopus 로고    scopus 로고
    • Isoniazid as a substrate and inhibitor of myeloperoxidase: Identification of amine adducts and the influence of superoxide dismutase on their formation
    • L.V. Forbes, P.G. Furtmuller, I. Khalilova, R. Turner, C. Obinger, and A.J. Kettle Isoniazid as a substrate and inhibitor of myeloperoxidase: identification of amine adducts and the influence of superoxide dismutase on their formation Biochem. Pharmacol. 84 2012 949 960
    • (2012) Biochem. Pharmacol. , vol.84 , pp. 949-960
    • Forbes, L.V.1    Furtmuller, P.G.2    Khalilova, I.3    Turner, R.4    Obinger, C.5    Kettle, A.J.6
  • 78
    • 36248932605 scopus 로고    scopus 로고
    • Myricitrin as a substrate and inhibitor of myeloperoxidase: Implications for the pharmacological effects of flavonoids
    • DOI 10.1016/j.freeradbiomed.2007.09.017, PII S0891584907006521
    • F.C. Meotti, R. Senthilmohan, D.T. Harwood, F.C. Missau, M.G. Pizzolatti, and A.J. Kettle Myricitrin as a substrate and inhibitor of myeloperoxidase: implications for the pharmacological effects of flavonoids Free Radic. Biol. Med. 44 2008 109 120 (Pubitemid 350138636)
    • (2008) Free Radical Biology and Medicine , vol.44 , Issue.1 , pp. 109-120
    • Meotti, F.C.1    Senthilmohan, R.2    Harwood, D.T.3    Missau, F.C.4    Pizzolatti, M.G.5    Kettle, A.J.6
  • 80
    • 33845997473 scopus 로고    scopus 로고
    • Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: Implications for microbial killing
    • DOI 10.1074/jbc.M605898200
    • C.C. Winterbourn, M.B. Hampton, J.H. Livesey, and A.J. Kettle Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing J. Biol. Chem. 281 2006 39860 39869 (Pubitemid 46041789)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 39860-39869
    • Winterbourn, C.C.1    Hampton, M.B.2    Livesey, J.H.3    Kettle, A.J.4
  • 81
    • 33646537788 scopus 로고    scopus 로고
    • Direct measurement of free chloride concentrations in the phagolysosomes of human neutrophils
    • DOI 10.1021/ac0521706
    • R.G. Painter, and G. Wang Direct measurement of free chloride concentrations in the phagolysosomes of human neutrophils Anal. Chem. 78 2006 3133 3137 (Pubitemid 43726135)
    • (2006) Analytical Chemistry , vol.78 , Issue.9 , pp. 3133-3137
    • Painter, R.G.1    Wang, G.2
  • 82
    • 0037155914 scopus 로고    scopus 로고
    • Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus
    • DOI 10.1074/jbc.M106134200
    • A.L.P. Chapman, M.B. Hampton, R. Senthilmohan, C.C. Winterbourn, and A.J. Kettle Chlorination of bacterial and neutrophil proteins during phagocytosis and killing of Staphylococcus aureus J. Biol. Chem. 277 2002 9757 9762 (Pubitemid 34968078)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 9757-9762
    • Chapman, A.L.P.1    Hampton, M.B.2    Senthilmohan, R.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 83
    • 73249129955 scopus 로고    scopus 로고
    • Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils
    • H. Rosen, S.J. Klebanoff, Y. Wang, N. Brot, J.W. Heinecke, and X. Fu Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils Proc. Natl. Acad. Sci. U. S. A. 106 2009 18686 18691
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 18686-18691
    • Rosen, H.1    Klebanoff, S.J.2    Wang, Y.3    Brot, N.4    Heinecke, J.W.5    Fu, X.6
  • 85
    • 0030046117 scopus 로고    scopus 로고
    • Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
    • DOI 10.1016/0014-5793(95)01494-2
    • A.J. Kettle Neutrophils convert tyrosyl residues in albumin to chlorotyrosine FEBS Lett. 379 1996 103 106 (Pubitemid 26033928)
    • (1996) FEBS Letters , vol.379 , Issue.1 , pp. 103-106
    • Kettle, A.J.1
  • 86
    • 0034194459 scopus 로고    scopus 로고
    • Comparison of mono- and dichlorinated tyrosines with carbonyls for detection of hypochlorous acid modified proteins
    • DOI 10.1006/abbi.2000.1744
    • A.L. Chapman, R. Senthilmohan, C.C. Winterbourn, and A.J. Kettle Comparison of mono- and dichlorinated tyrosines with carbonyls for detection of hypochlorous acid modified proteins Arch. Biochem. Biophys. 377 2000 95 100 (Pubitemid 30257291)
    • (2000) Archives of Biochemistry and Biophysics , vol.377 , Issue.1 , pp. 95-100
    • Chapman, A.L.P.1    Senthilmohan, R.2    Winterbourn, C.C.3    Kettle, A.J.4
  • 87
    • 0034282230 scopus 로고    scopus 로고
    • Biomarkers of myeloperoxidase-derived hypochlorous acid
    • C.C. Winterbourn, and A.J. Kettle Biomarkers of myeloperoxidase-derived hypochlorous acid Free Radic. Biol. Med. 29 2000 403 409
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 403-409
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 88
    • 18244393452 scopus 로고    scopus 로고
    • Green fluorescent protein-expressing Escherichia coli as a selective probe for HOCl generation within neutrophils
    • DOI 10.1021/bi047342s
    • A.M. Palazzolo, C. Suquet, M.E. Konkel, and J.K. Hurst Green fluorescent protein-expressing Escherichia coli as a selective probe for HOCl generation within neutrophils Biochemistry 44 2005 6910 6919 (Pubitemid 40632409)
    • (2005) Biochemistry , vol.44 , Issue.18 , pp. 6910-6919
    • Palazzolo, A.M.1    Suquet, C.2    Konkel, M.E.3    Hurst, J.K.4
  • 89
    • 70149091118 scopus 로고    scopus 로고
    • Neutrophil bleaching of GFP-expressing Staphylococci: Probing the intraphagosomal fate of individual bacteria
    • J. Schwartz, K.G. Leidal, J.K. Femling, J.P. Weiss, and W.M. Nauseef Neutrophil bleaching of GFP-expressing Staphylococci: probing the intraphagosomal fate of individual bacteria J. Immunol. 183 2009 2632 2641
    • (2009) J. Immunol. , vol.183 , pp. 2632-2641
    • Schwartz, J.1    Leidal, K.G.2    Femling, J.K.3    Weiss, J.P.4    Nauseef, W.M.5
  • 90
    • 0031438748 scopus 로고    scopus 로고
    • Relative chlorinating, nitrating, and oxidizing capabilities of neutrophils determined with phagocytosable probes
    • DOI 10.1074/jbc.272.52.32767
    • Q. Jiang, and J.K. Hurst Relative chlorinating, nitrating, and oxidizing capabilities of neutrophils determined with phagocytosable probes J. Biol. Chem. 272 1997 32767 32772 (Pubitemid 28023608)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.52 , pp. 32767-32772
    • Jiang, Q.1    Hurst, J.K.2
  • 91
    • 0030778901 scopus 로고    scopus 로고
    • Intraphagosomal chlorination dynamics and yields determined using unique fluorescent bacterial mimics
    • DOI 10.1021/tx9700984
    • Q. Jiang, D.A. Griffin, D.F. Barofsky, and J.K. Hurst Intraphagosomal chlorination dynamics and yields determined using unique fluorescent bacterial mimics Chem. Res. Toxicol. 10 1997 1080 1089 (Pubitemid 27449510)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.10 , pp. 1080-1089
    • Jiang, Q.1    Griffin, D.A.2    Barofsky, D.F.3    Hurst, J.K.4
  • 92
    • 79151480820 scopus 로고    scopus 로고
    • Kinetic analysis of phagosomal production of reactive oxygen species
    • A. Tlili, S. Dupre-Crochet, M. Erard, and O. Nusse Kinetic analysis of phagosomal production of reactive oxygen species Free Radic. Biol. Med. 50 2011 438 447
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 438-447
    • Tlili, A.1    Dupre-Crochet, S.2    Erard, M.3    Nusse, O.4
  • 93
    • 79957745742 scopus 로고    scopus 로고
    • A BODIPY-based probe for the selective detection of hypochlorous acid in living cells
    • T.I. Kim, S. Park, Y. Choi, and Y. Kim A BODIPY-based probe for the selective detection of hypochlorous acid in living cells Chem. Asian J. 6 2011 1358 1361
    • (2011) Chem. Asian J. , vol.6 , pp. 1358-1361
    • Kim, T.I.1    Park, S.2    Choi, Y.3    Kim, Y.4
  • 94
    • 34250807959 scopus 로고    scopus 로고
    • Development of a highly specific rhodamine-based fluorescence probe for hypochlorous acid and its application to real-time imaging of phagocytosis
    • DOI 10.1021/ja068740g
    • S. Kenmoku, Y. Urano, H. Kojima, and T. Nagano Development of a highly specific rhodamine-based fluorescence probe for hypochlorous acid and its application to real-time imaging of phagocytosis J. Am. Chem. Soc. 129 2007 7313 7318 (Pubitemid 46980809)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.23 , pp. 7313-7318
    • Kenmoku, S.1    Urano, Y.2    Kojima, H.3    Nagano, T.4
  • 95
    • 36048967878 scopus 로고    scopus 로고
    • A fluorescent probe for the detection of myeloperoxidase activity in Atherosclerosis-Associated macrophages
    • DOI 10.1016/j.chembiol.2007.10.005, PII S107455210700333X
    • J. Shepherd, S.A. Hilderbrand, P. Waterman, J.W. Heinecke, R. Weissleder, and P. Libby A fluorescent probe for the detection of myeloperoxidase activity in atherosclerosis-associated macrophages Chem. Biol. 14 2007 1221 1231 (Pubitemid 350102238)
    • (2007) Chemistry and Biology , vol.14 , Issue.11 , pp. 1221-1231
    • Shepherd, J.1    Hilderbrand, S.A.2    Waterman, P.3    Heinecke, J.W.4    Weissleder, R.5    Libby, P.6
  • 96
    • 84876557461 scopus 로고    scopus 로고
    • A strategy for highly selective detection and imaging of hypochlorite using selenoxide elimination
    • G. Li, D. Zhu, Q. Liu, L. Xue, and H. Jiang A strategy for highly selective detection and imaging of hypochlorite using selenoxide elimination Org. Lett. 15 2013 2002 2005
    • (2013) Org. Lett. , vol.15 , pp. 2002-2005
    • Li, G.1    Zhu, D.2    Liu, Q.3    Xue, L.4    Jiang, H.5
  • 98
    • 84872066559 scopus 로고    scopus 로고
    • A reversible fluorescence probe based on Se-BODIPY for the redox cycle between HClO oxidative stress and H2S repair in living cells
    • B. Wang, P. Li, F. Yu, P. Song, X. Sun, S. Yang, Z. Lou, and K. Han A reversible fluorescence probe based on Se-BODIPY for the redox cycle between HClO oxidative stress and H2S repair in living cells Chem. Commun. 49 2013 1014 1016
    • (2013) Chem. Commun. , vol.49 , pp. 1014-1016
    • Wang, B.1    Li, P.2    Yu, F.3    Song, P.4    Sun, X.5    Yang, S.6    Lou, Z.7    Han, K.8
  • 99
    • 79954486027 scopus 로고    scopus 로고
    • Development of an Si-rhodamine-based far-red to near-infrared fluorescence probe selective for hypochlorous acid and its applications for biological imaging
    • Y. Koide, Y. Urano, K. Hanaoka, T. Terai, and T. Nagano Development of an Si-rhodamine-based far-red to near-infrared fluorescence probe selective for hypochlorous acid and its applications for biological imaging J. Am. Chem. Soc. 133 2011 5680 5682
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 5680-5682
    • Koide, Y.1    Urano, Y.2    Hanaoka, K.3    Terai, T.4    Nagano, T.5
  • 100
    • 62749100714 scopus 로고    scopus 로고
    • A rhodamine-hydroxamic acid-based fluorescent probe for hypochlorous acid and its applications to biological imagings
    • Y.K. Yang, H.J. Cho, J. Lee, I. Shin, and J. Tae A rhodamine-hydroxamic acid-based fluorescent probe for hypochlorous acid and its applications to biological imagings Org. Lett. 11 2009 859 861
    • (2009) Org. Lett. , vol.11 , pp. 859-861
    • Yang, Y.K.1    Cho, H.J.2    Lee, J.3    Shin, I.4    Tae, J.5
  • 101
    • 52649151914 scopus 로고    scopus 로고
    • A highly specific BODIPY-based fluorescent probe for the detection of hypochlorous acid
    • Z.N. Sun, F.Q. Liu, Y. Chen, P.K. Tam, and D. Yang A highly specific BODIPY-based fluorescent probe for the detection of hypochlorous acid Org. Lett. 10 2008 2171 2174
    • (2008) Org. Lett. , vol.10 , pp. 2171-2174
    • Sun, Z.N.1    Liu, F.Q.2    Chen, Y.3    Tam, P.K.4    Yang, D.5
  • 102
    • 79958166662 scopus 로고    scopus 로고
    • Sensitive and selective off-on rhodamine hydrazide fluorescent chemosensor for hypochlorous acid detection and bioimaging
    • Z. Zhang, Y. Zheng, W. Hang, X. Yan, and Y. Zhao Sensitive and selective off-on rhodamine hydrazide fluorescent chemosensor for hypochlorous acid detection and bioimaging Talanta 85 2011 779 786
    • (2011) Talanta , vol.85 , pp. 779-786
    • Zhang, Z.1    Zheng, Y.2    Hang, W.3    Yan, X.4    Zhao, Y.5
  • 103
    • 84873952648 scopus 로고    scopus 로고
    • Hypochlorous acid turn-on fluorescent probe based on oxidation of diphenyl selenide
    • S.R. Liu, and S.P. Wu Hypochlorous acid turn-on fluorescent probe based on oxidation of diphenyl selenide Org. Lett. 15 2013 878 881
    • (2013) Org. Lett. , vol.15 , pp. 878-881
    • Liu, S.R.1    Wu, S.P.2
  • 104
    • 84890114880 scopus 로고    scopus 로고
    • The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells
    • C.C. Winterbourn The challenges of using fluorescent probes to detect and quantify specific reactive oxygen species in living cells Biochim. Biophys. Acta 1840 2013 730 738
    • (2013) Biochim. Biophys. Acta , vol.1840 , pp. 730-738
    • Winterbourn, C.C.1
  • 105
    • 78649705408 scopus 로고    scopus 로고
    • CdSe-ZnS quantum dots for selective and sensitive detection and quantification of hypochlorite
    • Y. Yan, S. Wang, Z. Liu, H. Wang, and D. Huang CdSe-ZnS quantum dots for selective and sensitive detection and quantification of hypochlorite Anal. Chem. 82 2010 9775 9781
    • (2010) Anal. Chem. , vol.82 , pp. 9775-9781
    • Yan, Y.1    Wang, S.2    Liu, Z.3    Wang, H.4    Huang, D.5
  • 106
    • 0035881517 scopus 로고    scopus 로고
    • Substrates and products of eosinophil peroxidase
    • DOI 10.1042/0264-6021:3580233
    • C.J. van Dalen, and A.J. Kettle Substrates and products of eosinophil peroxidase Biochem. J. 358 2001 233 239 (Pubitemid 32778118)
    • (2001) Biochemical Journal , vol.358 , Issue.1 , pp. 233-239
    • Van Dalen, C.J.1    Kettle, A.J.2
  • 107
    • 72749119238 scopus 로고    scopus 로고
    • Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione
    • P. Nagy, G.N. Jameson, and C.C. Winterbourn Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione Chem. Res. Toxicol. 22 2009 1833 1840
    • (2009) Chem. Res. Toxicol. , vol.22 , pp. 1833-1840
    • Nagy, P.1    Jameson, G.N.2    Winterbourn, C.C.3
  • 108
    • 84863890440 scopus 로고    scopus 로고
    • Reactions and reactivity of myeloperoxidase-derived oxidants: Differential biological effects of hypochlorous and hypothiocyanous acids
    • D.I. Pattison, M.J. Davies, and C.L. Hawkins Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids Free Radic. Res. 46 2012 975 995
    • (2012) Free Radic. Res. , vol.46 , pp. 975-995
    • Pattison, D.I.1    Davies, M.J.2    Hawkins, C.L.3
  • 109
    • 84878044208 scopus 로고    scopus 로고
    • A ratiometric fluorescent probe based on a BODIPY-DCDHF conjugate for the detection of hypochlorous acid in living cells
    • J. Park, H. Kim, Y. Choi, and Y. Kim A ratiometric fluorescent probe based on a BODIPY-DCDHF conjugate for the detection of hypochlorous acid in living cells Analyst 138 2013 3368 3371
    • (2013) Analyst , vol.138 , pp. 3368-3371
    • Park, J.1    Kim, H.2    Choi, Y.3    Kim, Y.4
  • 110
    • 84876478507 scopus 로고    scopus 로고
    • A fluorescence ratiometric sensor for hypochlorite based on a novel dual-fluorophore response approach
    • L. Long, D. Zhang, X. Li, J. Zhang, C. Zhang, and L. Zhou A fluorescence ratiometric sensor for hypochlorite based on a novel dual-fluorophore response approach Anal. Chim. Acta 775 2013 100 105
    • (2013) Anal. Chim. Acta , vol.775 , pp. 100-105
    • Long, L.1    Zhang, D.2    Li, X.3    Zhang, J.4    Zhang, C.5    Zhou, L.6
  • 111
    • 84875442814 scopus 로고    scopus 로고
    • Neutrophil recruitment and function in health and inflammation
    • E. Kolaczkowska, and P. Kubes Neutrophil recruitment and function in health and inflammation Nat. Rev. Immunol. 13 2013 159 175
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 159-175
    • Kolaczkowska, E.1    Kubes, P.2
  • 114
    • 34247471787 scopus 로고    scopus 로고
    • The neutrophil in chronic obstructive pulmonary disease
    • DOI 10.1016/j.jaci.2006.12.640, PII S0091674906039133
    • J.K. Quint, and J.A. Wedzicha The neutrophil in chronic obstructive pulmonary disease J. Allergy Clin. Immunol. 119 2007 1065 1071 (Pubitemid 46654162)
    • (2007) Journal of Allergy and Clinical Immunology , vol.119 , Issue.5 , pp. 1065-1071
    • Quint, J.K.1    Wedzicha, J.A.2
  • 115
    • 74249109159 scopus 로고    scopus 로고
    • Innate inflammation and resolution in acute gout
    • W.J. Martin, and J.L. Harper Innate inflammation and resolution in acute gout Immunol. Cell Biol. 88 2010 15 19
    • (2010) Immunol. Cell Biol. , vol.88 , pp. 15-19
    • Martin, W.J.1    Harper, J.L.2
  • 118
    • 84876998466 scopus 로고    scopus 로고
    • The dichotomy of neutrophil granulocytes in cancer
    • S. Brandau The dichotomy of neutrophil granulocytes in cancer Semin. Cancer Biol. 23 2013 139 140
    • (2013) Semin. Cancer Biol. , vol.23 , pp. 139-140
    • Brandau, S.1
  • 119
    • 0032510811 scopus 로고    scopus 로고
    • Human neutrophils employ myeloperoxidase to convert α-amino acids to a battery of reactive aldehydes: A pathway for aldehyde generation at sites of inflammation
    • DOI 10.1021/bi972449j
    • S.L. Hazen, F.F. Hsu, A. d'Avignon, and J.W. Heinecke Human neutrophils employ myeloperoxidase to convert alpha-amino acids to a battery of reactive aldehydes: a pathway for aldehyde generation at sites of inflammation Biochemistry 37 1998 6864 6873 (Pubitemid 28228123)
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6864-6873
    • Hazen, S.L.1    Hsu, F.F.2    D'Avignon, A.3    Heinecke, J.W.4
  • 120
    • 0037040239 scopus 로고    scopus 로고
    • Reactive chlorinating species produced during neutrophil activation target tissue plasmalogens: Production of the chemoattractant, 2-chlorohexadecanal
    • DOI 10.1074/jbc.M109489200
    • A.K. Thukkani, F.F. Hsu, J.R. Crowley, R.B. Wysolmerski, C.J. Albert, and D.A. Ford Reactive chlorinating species produced during neutrophil activation target tissue plasmalogens: production of the chemoattractant, 2-chlorohexadecanal J. Biol. Chem. 277 2002 3842 3849 (Pubitemid 34968634)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 3842-3849
    • Thukkani, A.K.1    Hsu, F.-F.2    Crowley, J.R.3    Wysolmerski, R.B.4    Albert, C.J.5    Ford, D.A.6
  • 121
    • 0035968168 scopus 로고    scopus 로고
    • Reactive chlorinating species produced by myeloperoxidase target the vinyl ether bond of plasmalogens: Identification of 2-chlorohexadecanal
    • C.J. Albert, J.R. Crowley, F.F. Hsu, A.K. Thukkani, and D.A. Ford Reactive chlorinating species produced by myeloperoxidase target the vinyl ether bond of plasmalogens: identification of 2-chlorohexadecanal J. Biol. Chem. 276 2001 23733 23741
    • (2001) J. Biol. Chem. , vol.276 , pp. 23733-23741
    • Albert, C.J.1    Crowley, J.R.2    Hsu, F.F.3    Thukkani, A.K.4    Ford, D.A.5
  • 122
    • 48649109320 scopus 로고    scopus 로고
    • The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: A kinetic study
    • O. Skaff, D.I. Pattison, and M.J. Davies The vinyl ether linkages of plasmalogens are favored targets for myeloperoxidase-derived oxidants: a kinetic study Biochemistry 47 2008 8237 8245
    • (2008) Biochemistry , vol.47 , pp. 8237-8245
    • Skaff, O.1    Pattison, D.I.2    Davies, M.J.3
  • 124
    • 0029055476 scopus 로고
    • Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils
    • N.M. Domigan, T.S. Charlton, M.W. Duncan, C.C. Winterbourn, and A.J. Kettle Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils J. Biol. Chem. 270 1995 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
  • 125
    • 1542289811 scopus 로고    scopus 로고
    • Lysine residues direct the chlorination of tyrosines in yxxk motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein
    • DOI 10.1074/jbc.M309046200
    • C. Bergt, X. Fu, N.P. Huq, J. Kao, and J.W. Heinecke Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein J. Biol. Chem. 279 2004 7856 7866 (Pubitemid 38294672)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7856-7866
    • Bergt, C.1    Fu, X.2    Huq, N.P.3    Kao, J.4    Heinecke, J.W.5
  • 127
    • 42949147076 scopus 로고    scopus 로고
    • Loss of 3-chlorotyrosine by inflammatory oxidants: Implications for the use of 3-chlorotyrosine as a bio-marker in vivo
    • DOI 10.1016/j.bbrc.2008.03.153, PII S0006291X08006359
    • M. Whiteman, and J.P. Spencer Loss of 3-chlorotyrosine by inflammatory oxidants: implications for the use of 3-chlorotyrosine as a bio-marker in vivo Biochem. Biophys. Res. Commun. 371 2008 50 53 (Pubitemid 351615217)
    • (2008) Biochemical and Biophysical Research Communications , vol.371 , Issue.1 , pp. 50-53
    • Whiteman, M.1    Spencer, J.P.E.2
  • 128
    • 79952950041 scopus 로고    scopus 로고
    • Kinetics of 3-chlorotyrosine formation and loss due to hypochlorous acid and chloramines
    • M.P. Curtis, A.J. Hicks, and J.W. Neidigh Kinetics of 3-chlorotyrosine formation and loss due to hypochlorous acid and chloramines Chem. Res. Toxicol. 24 2011 418 428
    • (2011) Chem. Res. Toxicol. , vol.24 , pp. 418-428
    • Curtis, M.P.1    Hicks, A.J.2    Neidigh, J.W.3
  • 129
    • 0030777056 scopus 로고    scopus 로고
    • Hypochlorous acid-induced base modifications in isolated calf thymus DNA
    • DOI 10.1021/tx970086i
    • M. Whiteman, A. Jenner, and B. Halliwell Hypochlorous acid-induced base modifications in isolated calf thymus DNA Chem. Res. Toxicol. 10 1997 1240 1246 (Pubitemid 27524829)
    • (1997) Chemical Research in Toxicology , vol.10 , Issue.11 , pp. 1240-1246
    • Whiteman, M.1    Jenner, A.2    Halliwell, B.3
  • 130
    • 0035798575 scopus 로고    scopus 로고
    • Chlorination of guanosine and other nucleosides by hypochlorous acid and myeloperoxidase of activated human neutrophils. Catalysis by nicotine and trimethylamine
    • M. Masuda, T. Suzuki, M.D. Friesen, J.L. Ravanat, J. Cadet, B. Pignatelli, H. Nishino, and H. Ohshima Chlorination of guanosine and other nucleosides by hypochlorous acid and myeloperoxidase of activated human neutrophils. Catalysis by nicotine and trimethylamine J. Biol. Chem. 276 2001 40486 40496
    • (2001) J. Biol. Chem. , vol.276 , pp. 40486-40496
    • Masuda, M.1    Suzuki, T.2    Friesen, M.D.3    Ravanat, J.L.4    Cadet, J.5    Pignatelli, B.6    Nishino, H.7    Ohshima, H.8
  • 131
    • 0042357366 scopus 로고    scopus 로고
    • 5-Chlorouracil, a marker of DNA damage from hypochlorous acid during inflammation: A gas chromatography-mass spectrometry assay
    • DOI 10.1074/jbc.M304021200
    • Q. Jiang, B.C. Blount, and B.N. Ames 5-Chlorouracil, a marker of DNA damage from hypochlorous acid during inflammation. A gas chromatography-mass spectrometry assay J. Biol. Chem. 278 2003 32834 32840 (Pubitemid 37055725)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 32834-32840
    • Jiang, Q.1    Blount, B.C.2    Ames, B.N.3
  • 132
    • 33645638306 scopus 로고    scopus 로고
    • Myeloperoxidase generates 5-chlorouracil in human atherosclerotic tissue: A Potential pathway for somatic mutagenesis by macrophages
    • DOI 10.1074/jbc.M509236200
    • J. Takeshita, J. Byun, T.Q. Nhan, D.K. Pritchard, S. Pennathur, S.M. Schwartz, A. Chait, and J.W. Heinecke Myeloperoxidase generates 5-chlorouracil in human atherosclerotic tissue: a potential pathway for somatic mutagenesis by macrophages J. Biol. Chem. 281 2006 3096 3104 (Pubitemid 43845919)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.6 , pp. 3096-3104
    • Takeshita, J.1    Byun, J.2    Nhan, T.Q.3    Pritchard, D.K.4    Pennathur, S.5    Schwartz, S.M.6    Chait, A.7    Heinecke, J.W.8
  • 133
    • 0038268570 scopus 로고    scopus 로고
    • Phagocytes produce 5-chlorouracil and 5-bromouracil, two mutagenic products of myeloperoxidase, in human inflammatory tissue
    • DOI 10.1074/jbc.M303928200
    • J.P. Henderson, J. Byun, J. Takeshita, and J.W. Heinecke Phagocytes produce 5-chlorouracil and 5-bromouracil, two mutagenic products of myeloperoxidase, in human inflammatory tissue J. Biol. Chem. 278 2003 23522 23528 (Pubitemid 36830171)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23522-23528
    • Henderson, J.P.1    Byun, J.2    Takeshita, J.3    Heinecke, J.W.4
  • 134
    • 77955403185 scopus 로고    scopus 로고
    • Ability of hypochlorous acid and N-chloramines to chlorinate DNA and its constituents
    • N.R. Stanley, D.I. Pattison, and C.L. Hawkins Ability of hypochlorous acid and N-chloramines to chlorinate DNA and its constituents Chem. Res. Toxicol. 23 2010 1293 1302
    • (2010) Chem. Res. Toxicol. , vol.23 , pp. 1293-1302
    • Stanley, N.R.1    Pattison, D.I.2    Hawkins, C.L.3
  • 135
    • 0030220396 scopus 로고    scopus 로고
    • Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates
    • DOI 10.1006/abbi.1996.0322
    • W.A. Prutz Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates Arch. Biochem. Biophys. 332 1996 110 120 (Pubitemid 26286139)
    • (1996) Archives of Biochemistry and Biophysics , vol.332 , Issue.1 , pp. 110-120
    • Prutz, W.A.1
  • 136
    • 72949104133 scopus 로고    scopus 로고
    • Comparative study of HOCl-inflicted damage to bacterial DNA ex vivo and within cells
    • C. Suquet, J.J. Warren, N. Seth, and J.K. Hurst Comparative study of HOCl-inflicted damage to bacterial DNA ex vivo and within cells Arch. Biochem. Biophys. 493 2010 135 142
    • (2010) Arch. Biochem. Biophys. , vol.493 , pp. 135-142
    • Suquet, C.1    Warren, J.J.2    Seth, N.3    Hurst, J.K.4
  • 138
    • 0030928562 scopus 로고    scopus 로고
    • Characterization of the oxidation products of the reaction between reduced glutathione and hypochlorous acid
    • C.C. Winterbourn, and S.O. Brennan Characterization of the oxidation products of the reaction between reduced glutathione and hypochlorous acid Biochem. J. 326 Pt 1 1997 87 92 (Pubitemid 27386921)
    • (1997) Biochemical Journal , vol.326 , Issue.1 , pp. 87-92
    • Winterbourn, C.C.1    Brennan, S.O.2
  • 139
    • 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
    • DOI 10.1042/BJ20060978
    • D.T. Harwood, A.J. Kettle, and C.C. Winterbourn Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC-MS/MS method Biochem. J. 399 2006 161 168 (Pubitemid 44505417)
    • (2006) Biochemical Journal , vol.399 , Issue.1 , pp. 161-168
    • Harwood, D.T.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 140
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic. Biol. Med. 45 2008 549 561
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 141
    • 0035823537 scopus 로고    scopus 로고
    • Novel intra- and inter-molecular sulfinamide bonds in s100a8 produced by hypochlorite oxidation
    • M.J. Raftery, Z. Yang, S.M. Valenzuela, and C.L. Geczy Novel intra- and inter-molecular sulfinamide bonds in s100a8 produced by hypochlorite oxidation J. Biol. Chem. 276 2001 33393 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
  • 142
    • 70149109384 scopus 로고    scopus 로고
    • Oxidative modifications of S100 proteins: Functional regulation by redox
    • S.Y. Lim, M.J. Raftery, J. Goyette, K. Hsu, and C.L. Geczy Oxidative modifications of S100 proteins: functional regulation by redox J. Leukoc. Biol. 86 2009 577 587
    • (2009) J. Leukoc. Biol. , vol.86 , pp. 577-587
    • Lim, S.Y.1    Raftery, M.J.2    Goyette, J.3    Hsu, K.4    Geczy, C.L.5
  • 144
    • 0037192149 scopus 로고    scopus 로고
    • Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: A potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase
    • DOI 10.1021/bi015777z
    • X. Fu, D.M. Mueller, and J.W. Heinecke Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: a potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase Biochemistry 41 2002 1293 1301 (Pubitemid 34083782)
    • (2002) Biochemistry , vol.41 , Issue.4 , pp. 1293-1301
    • Fu, X.1    Mueller, D.M.2    Heinecke, J.W.3
  • 145
    • 70350222052 scopus 로고    scopus 로고
    • Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils
    • A.V. Peskin, R. Turner, G.J. Maghzal, C.C. Winterbourn, and A.J. Kettle Oxidation of methionine to dehydromethionine by reactive halogen species generated by neutrophils Biochemistry 48 2009 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
  • 146
    • 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
    • J.L. Beal, S.B. Foster, and M.T. Ashby Hypochlorous acid reacts with the N-terminal methionines of proteins to give dehydromethionine, a potential biomarker for neutrophil-induced oxidative stress Biochemistry 48 2009 11142 11148
    • (2009) Biochemistry , vol.48 , pp. 11142-11148
    • Beal, J.L.1    Foster, S.B.2    Ashby, M.T.3
  • 147
    • 70350012762 scopus 로고    scopus 로고
    • Hypochlorous acid converts the gamma-glutamyl group of glutathione disulfide to 5-hydroxybutyrolactam, a potential marker for neutrophil activation
    • W. Yuan, Y. Wang, J.W. Heinecke, and X. Fu Hypochlorous acid converts the gamma-glutamyl group of glutathione disulfide to 5-hydroxybutyrolactam, a potential marker for neutrophil activation J. Biol. Chem. 284 2009 26908 26917
    • (2009) J. Biol. Chem. , vol.284 , pp. 26908-26917
    • Yuan, W.1    Wang, Y.2    Heinecke, J.W.3    Fu, X.4
  • 148
    • 0037081029 scopus 로고    scopus 로고
    • Artifact-free quantification of free 3-chlorotyrosine, 3-bromotyrosine, and 3-nitrotyrosine in human plasma by electron capture-negative chemical ionization gas chromatography mass spectrometry and liquid chromatography- electrospray ionization tandem mass spectrometry
    • DOI 10.1006/abio.2001.5469
    • J.P. Gaut, J. Byun, H.D. Tran, and J.W. Heinecke Artifact-free quantification of free 3-chlorotyrosine, 3-bromotyrosine, and 3-nitrotyrosine in human plasma by electron capture-negative chemical ionization gas chromatography mass spectrometry and liquid chromatography-electrospray ionization tandem mass spectrometry Anal. Biochem. 300 2002 252 259 (Pubitemid 34093701)
    • (2002) Analytical Biochemistry , vol.300 , Issue.2 , pp. 252-259
    • Gaut, J.P.1    Byun, J.2    Tran, H.D.3    Heinecke, J.W.4
  • 149
    • 0030803161 scopus 로고    scopus 로고
    • Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: A sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation
    • DOI 10.1016/S0891-5849(97)00084-1, PII S0891584997000841
    • S.L. Hazen, J.R. Crowley, D.M. Mueller, and J.W. Heinecke Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation Free Radic. Biol. Med. 23 1997 909 916 (Pubitemid 27402616)
    • (1997) Free Radical Biology and Medicine , vol.23 , Issue.6 , pp. 909-916
    • Hazen, S.L.1    Crowley, J.R.2    Mueller, D.M.3    Heinecke, J.W.4
  • 152
    • 0030979720 scopus 로고    scopus 로고
    • 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima
    • S.L. Hazen, and J.W. Heinecke 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic intima J. Clin. Invest. 99 1997 2075 2081 (Pubitemid 27203762)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.9 , pp. 2075-2081
    • Hazen, S.L.1    Heinecke, J.W.2
  • 153
    • 27244461333 scopus 로고    scopus 로고
    • 2-macroglobulin from rheumatoid arthritis synovial fluid: Functional analysis defines a role for oxidation in inflammation
    • DOI 10.1006/abbi.2001.2408
    • S.M. Wu, and S.V. Pizzo alpha(2)-Macroglobulin from rheumatoid arthritis synovial fluid: functional analysis defines a role for oxidation in inflammation Arch. Biochem. Biophys. 391 2001 119 126 (Pubitemid 32612579)
    • (2001) Archives of Biochemistry and Biophysics , vol.391 , Issue.1 , pp. 119-126
    • Wu, S.M.1    Pizzo, S.V.2
  • 154
    • 0037372157 scopus 로고    scopus 로고
    • 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: Association with adverse respiratory outcome
    • DOI 10.1203/01.PDR.0000050655.25689.CE
    • I.H. Buss, R. Senthilmohan, B.A. Darlow, N. Mogridge, A.J. Kettle, and C.C. Winterbourn 3-Chlorotyrosine as a marker of protein damage by myeloperoxidase in tracheal aspirates from preterm infants: association with adverse respiratory outcome Pediatr. Res. 53 2003 455 462 (Pubitemid 36237401)
    • (2003) Pediatric Research , vol.53 , Issue.3 , pp. 455-462
    • Hendrikje Buss, I.1    Senthilmohan, R.2    Darlow, B.A.3    Mogridge, N.4    Kettle, A.J.5    Winterbourn, C.C.6
  • 159
    • 12844268120 scopus 로고    scopus 로고
    • Localization of nitration and chlorination sites on apolipoprotein A-I catalysed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages
    • DOI 10.1074/jbc.M407019200
    • L. Zheng, M. Settle, G. Brubaker, D. Schmitt, S.L. Hazen, J.D. Smith, and M. Kinter Localization of nitration and chlorination sites on apolipoprotein A-I catalyzed by myeloperoxidase in human atheroma and associated oxidative impairment in ABCA1-dependent cholesterol efflux from macrophages J. Biol. Chem. 280 2005 38 47 (Pubitemid 40164962)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.1 , pp. 38-47
    • Zheng, L.1    Settle, M.2    Brubaker, G.3    Schmitt, D.4    Hazen, S.L.5    Smith, J.D.6    Kinter, M.7
  • 160
    • 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
    • DOI 10.1074/jbc.M411484200
    • B. Shao, C. Bergt, X. Fu, P. Green, J.C. Voss, M.N. Oda, J.F. Oram, and J.W. Heinecke 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. 280 2005 5983 5993 (Pubitemid 40280082)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5983-5993
    • Shao, B.1    Bergt, C.2    Fu, X.3    Green, P.4    Voss, J.C.5    Oda, M.N.6    Oram, J.F.7    Heinecke, J.W.8
  • 161
    • 84857491459 scopus 로고    scopus 로고
    • Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions
    • B. Shao, S. Pennathur, and J.W. Heinecke Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions J. Biol. Chem. 287 2012 6375 6386
    • (2012) J. Biol. Chem. , vol.287 , pp. 6375-6386
    • Shao, B.1    Pennathur, S.2    Heinecke, J.W.3
  • 164
    • 0348049466 scopus 로고    scopus 로고
    • Identification of α-Chloro Fatty Aldehydes and Unsaturated Lysophosphatidylcholine Molecular Species in Human Atherosclerotic Lesions
    • DOI 10.1161/01.CIR.0000104564.01539.6A
    • A.K. Thukkani, J. McHowat, F.F. Hsu, M.L. Brennan, S.L. Hazen, and D.A. Ford Identification of alpha-chloro fatty aldehydes and unsaturated lysophosphatidylcholine molecular species in human atherosclerotic lesions Circulation 108 2003 3128 3133 (Pubitemid 38031803)
    • (2003) Circulation , vol.108 , Issue.25 , 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
  • 165
    • 41149106758 scopus 로고    scopus 로고
    • Identification of lysophosphatidylcholine-chlorohydrin in human atherosclerotic lesions
    • M.C. Messner, C.J. Albert, J. McHowat, and D.A. Ford Identification of lysophosphatidylcholine-chlorohydrin in human atherosclerotic lesions Lipids 43 2008 243 249
    • (2008) Lipids , vol.43 , pp. 243-249
    • Messner, M.C.1    Albert, C.J.2    McHowat, J.3    Ford, D.A.4
  • 166
    • 78650658029 scopus 로고    scopus 로고
    • Omega-Oxidation of {alpha}-Chlorinated fatty acids: Identification of {alpha}-Chlorinated dicarboxylic acids
    • V.V. Brahmbhatt, C.J. Albert, D.S. Anbukumar, B.A. Cunningham, W.L. Neumann, and D.A. Ford {Omega}-oxidation of {alpha}-chlorinated fatty acids: identification of {alpha}-chlorinated dicarboxylic acids J. Biol. Chem. 285 2010 41255 41269
    • (2010) J. Biol. Chem. , vol.285 , pp. 41255-41269
    • Brahmbhatt, V.V.1    Albert, C.J.2    Anbukumar, D.S.3    Cunningham, B.A.4    Neumann, W.L.5    Ford, D.A.6
  • 167
    • 84876478882 scopus 로고    scopus 로고
    • Strategies for the analysis of chlorinated lipids in biological systems
    • B.K. Wacker, C.J. Albert, B.A. Ford, and D.A. Ford Strategies for the analysis of chlorinated lipids in biological systems Free Radic. Biol. Med. 59 2013 92 99
    • (2013) Free Radic. Biol. Med. , vol.59 , pp. 92-99
    • Wacker, B.K.1    Albert, C.J.2    Ford, B.A.3    Ford, D.A.4
  • 168
    • 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
    • D.T. Harwood, S.L. Nimmo, A.J. Kettle, C.C. Winterbourn, and M.T. Ashby 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. 21 2008 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
  • 169
    • 70249098135 scopus 로고    scopus 로고
    • Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatography-tandem mass spectrometry
    • D.T. Harwood, A.J. Kettle, S. Brennan, and C.C. Winterbourn Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatography-tandem mass spectrometry J. Chromatogr. B 877 2009 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
  • 170
    • 0023263523 scopus 로고
    • Normal alveolar epithelial lining fluid contains high levels of glutathione
    • A.M. Cantin, S.L. North, R.C. Hubbard, and R.G. Crystal Normal alveolar epithelial lining fluid contains high levels of glutathione J. Appl. Physiol. 63 1987 152 157 (Pubitemid 17107139)
    • (1987) Journal of Applied Physiology , vol.63 , Issue.1 , pp. 152-157
    • Cantin, A.M.1    North, S.L.2    Hubbard, R.C.3    Crystal, R.G.4
  • 171
    • 78650833245 scopus 로고    scopus 로고
    • Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: Association with bacterial infection
    • D.T. Harwood, B.A. Darlow, F.C. Cheah, N. McNeill, P. Graham, and C.C. Winterbourn Biomarkers of neutrophil-mediated glutathione and protein oxidation in tracheal aspirates from preterm infants: association with bacterial infection Pediatr. Res. 69 2011 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
  • 173
    • 0032213375 scopus 로고    scopus 로고
    • Inside the neutrophil phagosome: Oxidants, myeloperoxidase, and bacterial killing
    • M.B. Hampton, A.J. Kettle, and C.C. Winterbourn Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing Blood 92 1998 3007 3017 (Pubitemid 28492304)
    • (1998) Blood , vol.92 , Issue.9 , pp. 3007-3017
    • Hampton, M.B.1    Kettle, A.J.2    Winterbourn, C.C.3


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