Myeloperoxidase-derived oxidation: mechanisms of biological damage and its prevention

Superoxide radical and superoxide dismutases

Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455

Dietary phenolics: chemistry, bioavailability and effects on health

Crozier, A., Jaganath, I. B., & Clifford, M. N. (2009) · Natural Product Reports · doi:10.1039/b802662a · Cited by 2,062

Nitric oxide, oxidants, and protein tyrosine nitration

Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,477

The oxidative environment and protein damage

Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392

Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions.

Daugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269

Phagocytes and oxidative stress

Babior, B. M. (2000) · The American Journal of Medicine · doi:10.1016/s0002-9343(00)00481-2 · Cited by 1,061

The Acid Ionization Constant of HOCl from 5 to 35°

Morris, J. C. (1966) · The Journal of Physical Chemistry · doi:10.1021/j100884a007 · Cited by 927

Myeloperoxidase-Halide-Hydrogen Peroxide Antibacterial System

Klebanoff, S. J. (1968) · Journal of Bacteriology · doi:10.1128/jb.95.6.2131-2138.1968 · Cited by 820

Absolute Rate Constants for the Reaction of Hypochlorous Acid with Protein Side Chains and Peptide Bonds

Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790

Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease

Zheng, L., Nukuna, B. N., Brennan, M., Sun, M., Goormastic, M., Settle, M., Schmitt, D., Fu, X., Thomson, L., Fox, P. L., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci21109 · Cited by 735

Protein carbamylation links inflammation, smoking, uremia and atherogenesis

Wang, Z., Nicholls, S. J., Rodríguez, E. R., Kummu, O., Hörkkö, S., Barnard, J., Reynolds, W. F., Topol, E. J., DiDonato, J. A., & Hazen, S. L. (2007) · Nature Medicine · doi:10.1038/nm1637 · Cited by 722

Paracetamol (Acetaminophen)-Induced Toxicity: Molecular and Biochemical Mechanisms, Analogues and Protective Approaches

Bessems, J. G. M., & Vermeulen, N. P. E. (2001) · Critical Reviews in Toxicology · doi:10.1080/20014091111677 · Cited by 716

Myeloperoxidase, a Leukocyte-Derived Vascular NO Oxidase

Eiserich, J. P., Baldus, S. E., Brennan, M., Ma, W., Zhang, C., Tousson, A., Castro, L., Lusis, A. J., Nauseef, W. M., White, C. R., et al. (2002) · Science · doi:10.1126/science.1106830 · Cited by 685

Myeloperoxidase: a key regulator of neutrophil oxidant production

Kettle, A. J., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747085 · Cited by 671

Modeling the Reactions of Superoxide and Myeloperoxidase in the Neutrophil Phagosome

Winterbourn, C. C., Hampton, M. B., Livesey, J. H., & Kettle, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605898200 · Cited by 633

Hypochlorite-induced oxidation of amino acids, peptides and proteins

Hawkins, C. L., Pattison, D. I., & Davies, M. J. (2003) · Amino Acids · doi:10.1007/s00726-003-0016-x · Cited by 600

Mammalian Heme Peroxidases: From Molecular Mechanisms to Health Implications

Davies, M. J., Hawkins, C. L., Pattison, D. I., & Rees, M. D. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1927 · Cited by 559

Myeloperoxidase: Molecular Mechanisms of Action and Their Relevance to Human Health and Disease

van der Veen, B. S., de Winther, M. P. J., & Heeringa, P. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2538 · Cited by 530

A Tale of Two Controversies

Brennan, M.-L., Wu, W., Fu, X., Shen, Z., Song, W., Frost, H., Vadseth, C., Narine, L., Lenkiewicz, E., Borchers, M. T., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112400200 · Cited by 486

Hypochlorous Acid Oxygenates the Cysteine Switch Domain of Pro-matrilysin (MMP-7)

Fu, X., Kassim, S. Y., Parks, W. C., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106958200 · Cited by 482

Diphenyleneiodonium, an NAD(P)H Oxidase Inhibitor, also Potently Inhibits Mitochondrial Reactive Oxygen Species Production

Li, Y., & Trush, M. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9729 · Cited by 470

Comparative reactivities of various biological compounds with myeloperoxidase-hydrogen peroxide-chloride, and similarity of oxidant to hypochlorite

Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463

Thiocyanate and chloride as competing substrates for myeloperoxidase

van DALEN, J. C., WHITEHOUSE, W. M., WINTERBOURN, C. C., & KETTLE, J. A. (1997) · Biochemical Journal · doi:10.1042/bj3270487 · Cited by 406

Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization

Schultz, J., & Kaminker, K. (1962) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(62)90321-1 · Cited by 403

Nitric Oxide Is a Physiological Substrate for Mammalian Peroxidases

Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.48.37524 · Cited by 399

Reactive species formed on proteins exposed to singlet oxygen

Davies, M. J. (2004) · Photochemical & Photobiological Sciences · doi:10.1039/b307576c · Cited by 399

X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution

Fiedler, T. J., Davey, C. A., & Fenna, R. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11964 · Cited by 374

Reactions of Myeloperoxidase-Derived Oxidants with Biological Substrates:Gaining Chemical Insight into Human Inflammatory Diseases

Pattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 361

Active site structure and catalytic mechanisms of human peroxidases

Furtmüller, P. G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., & Obinger, C. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.09.017 · Cited by 358

Tyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.

Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354

[40] Preparation and characterization of chloramines

Thomas, E. L., Grisham, M. B., & Jefferson, M. M. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)32042-1 · Cited by 344

Evidence for Rapid Inter- and Intramolecular Chlorine Transfer Reactions of Histamine and Carnosine Chloramines: Implications for the Prevention of Hypochlorous-Acid-Mediated Damage

Pattison, D. I., & Davies, M. J. (2006) · Biochemistry · doi:10.1021/bi060348s · Cited by 338

Kinetics of the reactions of hypochlorous acid and amino acid chloramines with thiols, methionine, and ascorbate

Peskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 335

Tyrosyl radical generated by myeloperoxidase is a physiological catalyst for the initiation of lipid peroxidation in low density lipoprotein.

Savenkova, M. L., Mueller, D. M., & Heinecke, J. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32005-7 · Cited by 333

Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration

Baldus, S. E., Eiserich, J. P., Mani, A. R., Castro, L., Figueroa, M., Chumley, P. H., Ma, W., Tousson, A., White, C. R., Bullard, D. C., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12617 · Cited by 332

Hypochlorous Acid Interactions with Thiols, Nucleotides, DNA, and Other Biological Substrates

Prütz, W. A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0322 · Cited by 327

X-ray crystal structure of canine myeloperoxidase at 3 Å resolution

Zeng, J., & Fenna, R. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90133-5 · Cited by 310

Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation

Hawkins, C. L., & Davies, M. J. (1998) · Biochemical Journal · doi:10.1042/bj3320617 · Cited by 305

Endothelial transcytosis of myeloperoxidase confers specificity to vascular ECM proteins as targets of tyrosine nitration

Baldus, S. E., Eiserich, J. P., Mani, A. R., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200112617 · Cited by 281

Chloramines as intermediates of oxidation reaction of amino acids by myeloperoxidase

Zgliczyński, J. M., Stelmaszyńska, T., Domański, J., & Ostrowski, W. (1971) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(71)90281-6 · Cited by 275

Peroxidases

O'Brien, P. J. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00201-5 · Cited by 264

Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli

Thomas, E. L. (1979) · Infection and Immunity · doi:10.1128/iai.23.2.522-531.1979 · Cited by 251

Consequences of Total and Subtotal Myeloperoxidase Deficiency: Risk or Benefit ?

Kutter, D., Devaquet, P., Vanderstocken, G., Paulus, J., Marchal, V., & Gothot, A. (2000) · Acta Haematologica · doi:10.1159/000041062 · Cited by 250

Biological reactivity and biomarkers of the neutrophil oxidant, hypochlorous acid

Winterbourn, C. C. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00286-x · Cited by 247

Immunohistochemical evidence for the myeloperoxidase/H2O2/halide system in human atherosclerotic lesions: Colocalization of myeloperoxidase and hypochlorite‐modified proteins

Malle, E., Waeg, G., Schreiber, R., Gröne, E. F., Sattler, W., & Gröne, H. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01498.x · Cited by 245

Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide

Kettle, A. J., Gedye, C. A., & Winterbourn, C. C. (1997) · Biochemical Journal · doi:10.1042/bj3210503 · Cited by 245

Protein hydroperoxides can give rise to reactive free radicals

Davies, M. J., Fu, S., & Dean, R. T. (1995) · Biochemical Journal · doi:10.1042/bj3050643 · Cited by 238

Interaction of myeloperoxidase with peroxynitrite

Floris, R., Piersma, S. R., Guang, Y. A. N. G., Jones, P. M., & Wever, R. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18091.x · Cited by 237

Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II

Marquez‐Curtis, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 237

Nitric oxide suppresses NADPH oxidase-dependent superoxide production by S-nitrosylation in human endothelial cells

Selemidis, S., Dusting, G. J., Peshavariya, H., Kemp‐Harper, B. K., & Drummond, G. R. (2007) · Cardiovascular Research · doi:10.1016/j.cardiores.2007.03.030 · Cited by 226

Mechanism of Reaction of Myeloperoxidase with Nitrite

Burner, U., Furtmüller, P. G., Kettle, A. J., Koppenol, W. H., & Obinger, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000181200 · Cited by 220

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

Pattison, D. I., & Davies, M. J. (2004) · Biochemistry · doi:10.1021/bi035946a · Cited by 209

Origin, structure, and biological activities of peroxidases in human saliva

Ihalin, R., Loimaranta, V., & Tenovuo, J. O. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.004 · Cited by 208

Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals

Kim, H., & Gladyshev, V. N. (2007) · Biochemical Journal · doi:10.1042/bj20070929 · Cited by 204

Hypochlorite-induced oxidation of proteins in plasma: formation of chloramines and nitrogen-centred radicals and their role in protein fragmentation

Hawkins, C. L., & Davies, M. J. (1999) · Biochemical Journal · doi:10.1042/bj3400539 · Cited by 201

Heparins Increase Endothelial Nitric Oxide Bioavailability by Liberating Vessel-Immobilized Myeloperoxidase

Baldus, S. E., Rudolph, V., Roiss, M., Ito, W. D., Rudolph, T. K., Eiserich, J. P., Sydow, K., Lau, D., Szöcs, K., Klinke, A., et al. (2006) · Circulation · doi:10.1161/circulationaha.105.590083 · Cited by 198

Nitric Oxide Modulates the Catalytic Activity of Myeloperoxidase

Abu‐Soud, H. M., & Hazen, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5425 · Cited by 194

Identification of α-Chloro Fatty Aldehydes and Unsaturated Lysophosphatidylcholine Molecular Species in Human Atherosclerotic Lesions

Thukkani, A. K., McHowat, J., Hsu, F.-F., Brennan, M.-L., Hazen, S. L., & Ford, D. A. (2003) · Circulation · doi:10.1161/01.cir.0000104564.01539.6a · Cited by 194

Inhibition of myeloperoxidase by benzoic acid hydrazides

Kettle, A. J., Gedye, C. A., Hampton, M. B., & Winterbourn, C. C. (1995) · Biochemical Journal · doi:10.1042/bj3080559 · Cited by 188

field ionization

(2008) · International Union of Pure and Applied Chemistry (IUPAC) eBooks · doi:10.1351/goldbook.f02360 · Cited by 187

Neutrophils convert tyrosyl residues in albumin to chlorotyrosine

Kettle, A. J. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01494-2 · Cited by 187

Oxidation of Bromide by the Human Leukocyte Enzymes Myeloperoxidase and Eosinophil Peroxidase

Thomas, E. L., Bozeman, P. M., Jefferson, M. M., & King, C. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2906 · Cited by 186

Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family.

TEN, R. M., Pease, L. R., McKEAN, D. J., Bell, M. P., & Gleich, G. J. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.5.1757 · Cited by 186

Mechanism of inhibition of myeloperoxidase by anti-inflammatory drugs

Kettle, A. J., & Winterbourn, C. C. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90565-m · Cited by 185

Eosinophil granule proteins in peripheral blood granulocytes

Abu-Ghazaleh, R. I., Dunnette, S. L., Loegering, D. A., Checked, J. L., Kita, H., Thomas, L. L., & Gleich, G. J. (1992) · Journal of Leukocyte Biology · doi:10.1002/jlb.52.6.611 · Cited by 184

Superoxide modulates the activity of myeloperoxidase and optimizes the production of hypochlorous acid

Kettle, A. J., & Winterbourn, C. C. (1988) · Biochemical Journal · doi:10.1042/bj2520529 · Cited by 177

Human Neutrophils Employ the Myeloperoxidase-Hydrogen Peroxide-Chloride System to Oxidize α-Amino Acids to a Family of Reactive Aldehydes

Hazen, S. L., d'Avignon, A., Anderson, M. M., Hsu, F., & Heinecke, J. W. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4997 · Cited by 174

Hypochlorous Acid-Induced Base Modifications in Isolated Calf Thymus DNA

Whiteman, M., Jenner, A. M., & Halliwell, B. B. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970086i · Cited by 167

Mechanisms for Oxidative Stress in Diabetic Cardiovascular Disease

Pennathur, S., & Heinecke, J. W. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1595 · Cited by 165

The effect of the NADPH oxidase inhibitor diphenyleneiodonium on aerobic and anaerobic microbicidal activities of human neutrophils

Ellis, J. A., Mayer, S. J., & Jones, O. T. G. (1988) · Biochemical Journal · doi:10.1042/bj2510887 · Cited by 164

Gas Chromatography Mass Spectrometry

Kopka, J. (2006) · Springer eBooks · doi:10.1007/3-540-29782-0_1 · Cited by 163

Albumin mediates the transcytosis of myeloperoxidase by means of caveolae in endothelial cells

Tiruppathì, C., Naqvi, T., Wu, Y.-B., Vogel, S. M., Minshall, R. D., & Malik, A. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401712101 · Cited by 158

Generation of nitrogen-chlorine oxidants by human phagocytes.

Test, S. T., Lampert, M. B., Ossanna, P. J., Thoene, J. G., & Weiss, S. J. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111544 · Cited by 154

The Maillard Hypothesis on Aging: Time to Focus on DNA

Baynes, J. (2002) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2002.tb02107.x · Cited by 150

Concerted Nitric Oxide Formation and Release from the Simultaneous Reactions of Nitrite with Deoxy- and Oxyhemoglobin

Grubina, R., Huang, Z., Shiva, S., Joshi, M. S., Azarov, I., Basu, S., Ringwood, L. A., Jiang, A., Hogg, N., Kim‐Shapiro, D. B., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m700546200 · Cited by 147

Chlorination of Guanosine and Other Nucleosides by Hypochlorous Acid and Myeloperoxidase of Activated Human Neutrophils

Masuda, M., Suzuki, T., Friesen, M. D., Ravanat, J.-L., Cadet, J., Pignatelli, B., Nishino, H., & Ohshima, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102700200 · Cited by 144

Role of monochloramine in the oxidation of erythrocyte hemoglobin by stimulated neutrophils.

Grisham, M. B., Jefferson, M. M., & Thomas, E. L. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39793-4 · Cited by 141

Cholesterol Chlorohydrin Synthesis by the Myeloperoxidase-Hydrogen Peroxide-Chloride System: Potential Markers for Lipoproteins Oxidatively Damaged by Phagocytes

Heinecke, J. W., Li, W., Mueller, D. M., Bohrer, A., & TURK, J. W. (1994) · Biochemistry · doi:10.1021/bi00199a041 · Cited by 141

Phagocytes Produce 5-Chlorouracil and 5-Bromouracil, Two Mutagenic Products of Myeloperoxidase, in Human Inflammatory Tissue

Henderson, J. P., Byun, J., Takeshita, J., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303928200 · Cited by 141

Autocatalytic radical reactions in physiological prosthetic heme modification

Colas, C., & Ortiz de Montellano, P. R. (2003) · Chemical Reviews · doi:10.1021/cr0204303 · Cited by 139

Hypochlorous Acid-Mediated Oxidation of Lipid Components and Antioxidants Present in Low-Density Lipoproteins: Absolute Rate Constants, Product Analysis, and Computational Modeling

Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2003) · Chemical Research in Toxicology · doi:10.1021/tx025670s · Cited by 139

Nitrite as a Substrate and Inhibitor of Myeloperoxidase

van Dalen, C. J., Winterbourn, C. C., Senthilmohan, R., & Kettle, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11638 · Cited by 139

Binding and inhibition of myeloperoxidase (MPO): a major function of ceruloplasmin?

Segelmark, M., PERSSON, B., Hellmark, T., & Wieslander, J. (1997) · Clinical & Experimental Immunology · doi:10.1046/j.1365-2249.1997.d01-992.x · Cited by 138

Reaction of Lactoperoxidase Compound I with Halides and Thiocyanate

Furtmüller, P. G., Jantschko, W., Regelsberger, G., Jakopitsch, C., Arnhold, J., & Obinger, C. (2002) · Biochemistry · doi:10.1021/bi026326x · Cited by 134

Oxidation of intracellular glutathione after exposure of human red blood cells to hypochlorous acid

Vissers, M. C. M., & Winterbourn, C. C. (1995) · Biochemical Journal · doi:10.1042/bj3070057 · Cited by 130

Eosinophil Peroxidase Oxidation of Thiocyanate

Arlandson, M. E., Decker, T., Roongta, V. A., Bonilla, L. E., Mayo, K. H., MacPherson, J. C., Hazen, S. L., & Slungaard, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004881200 · Cited by 130

Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance

Skaff, O., Pattison, D. I., & Davies, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090276 · Cited by 130

Aqueous chemistry of N-halo-compounds

Armesto, X. L., Canle, M., García, M. V., & Santaballa, J. A. (1998) · Chemical Society Reviews · doi:10.1039/a827453z · Cited by 130

Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate.

Marquez‐Curtis, L. A., & Dunford, H. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37143-0 · Cited by 126

Novel Intra- and Inter-molecular Sulfinamide Bonds in S100A8 Produced by Hypochlorite Oxidation

Raftery, M. J., Yang, Z., Valenzuela, S. M., & Geczy, C. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101566200 · Cited by 126

Chlorination of Cholesterol in Cell Membranes by Hypochlorous Acid

Carr, A. C., van den Berg, J. J. M., & Winterbourn, C. C. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0317 · Cited by 124

What Are the Plasma Targets of the Oxidant Hypochlorous Acid? A Kinetic Modeling Approach

Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800372d · Cited by 123

Production of Brominating Intermediates by Myeloperoxidase

Henderson, J. P., Byun, J., Williams, M. V., Mueller, D. M., McCormick, M. L., & Heinecke, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005379200 · Cited by 123

Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride

Senthilmohan, R., & Kettle, A. J. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.005 · Cited by 122

Hypochlorous Acid-Mediated Protein Oxidation: How Important Are Chloramine Transfer Reactions and Protein Tertiary Structure?

Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2007) · Biochemistry · doi:10.1021/bi7008294 · Cited by 122

A kinetic study of the reaction between human myeloperoxidase, hydroperoxides and cyanide inhibition by chloride and thiocyanate

Bolscher, B. G. J. M., & Wever, R. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90290-5 · Cited by 121

Interactions of Hypochlorous Acid with Pyrimidine Nucleotides, and Secondary Reactions of Chlorinated Pyrimidines with GSH, NADH, and Other Substrates

Prütz, W. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0440 · Cited by 121

The peroxidase-catalyzed oxidation of tyrosine

Bayse, G. S., Michaels, A. W., & Morrison, M. (1972) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(72)90043-5 · Cited by 121

[41] Cytotoxicity of chloramines

Thomas, E. L., Grisham, M. B., & Jefferson, M. M. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)32043-3 · Cited by 121

The respiratory burst oxidase

BABIOR, B. M. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90118-6 · Cited by 117

Myeloperoxidase of the leucocyte of normal human blood

Schultz, J., Corlin, R. F., Oddi, F., Kaminker, K., & Jones, W. (1965) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(65)90324-3 · Cited by 115

Kinetics and Thermodynamics of Halide and Nitrite Oxidation by Mammalian Heme Peroxidases

Arnhold, J., Monzani, E., Furtmüller, P. G., Zederbauer, M., Casella, L., & Obinger, C. (2006) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200600436 · Cited by 113

Redox Buffering of Hypochlorous Acid by Thiocyanate in Physiologic Fluids

Ashby, M. T., Carlson, A. C., & Scott, M. J. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0438361 · Cited by 113

Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides

WINTERBOURN, C. C., PARSONS-MAIR, H. N., GEBICKI, S., GEBICKI, J. M., & DAVIES, M. J. (2004) · Biochemical Journal · doi:10.1042/bj20040259 · Cited by 112

Kinetics and Mechanisms of the Reaction of Hypothiocyanous Acid with 5-Thio-2-nitrobenzoic Acid and Reduced Glutathione

Nagy, P., Jameson, G. N. L., & Winterbourn, C. C. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900249d · Cited by 111

Pathways of phospholipid oxidation by HOCl in human LDL detected by LC-MS

Jerlich, A., Pitt, A. R., Schaur, R. J., & Spickett, C. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00273-7 · Cited by 110

Inactivation of Protease Inhibitors and Lysozyme by Hypochlorous Acid: Role of Side-Chain Oxidation and Protein Unfolding in Loss of Biological Function

Hawkins, C. L., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050207b · Cited by 110

Substrates and products of eosinophil peroxidase

van Dalen, C. J., & Kettle, A. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3580233 · Cited by 109

Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase

Furtmüller, P. G., Arnhold, J., Jantschko, W., Pichler, H., & Obinger, C. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03075-9 · Cited by 109

Oxidation of neutrophil glutathione and protein thiols by myeloperoxidase-derived hypochlorous acid

Carr, A. C., & Winterbourn, C. C. (1997) · Biochemical Journal · doi:10.1042/bj3270275 · Cited by 108

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

Fu, X., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi015777z · Cited by 107

Heme to protein linkages in mammalian peroxidases: impact on spectroscopic, redox and catalytic properties

Zederbauer, M., Furtmüller, P. G., Brogioni, S., Jakopitsch, C., Smulevich, G., & Obinger, C. (2007) · Natural Product Reports · doi:10.1039/b604178g · Cited by 106

Comparison of human red cell lysis by hypochlorous and hypobromous acids: insights into the mechanism of lysis

VISSERS, C. M. M., Carr, A. C., & Chapman, L. (1998) · Biochemical Journal · doi:10.1042/bj3300131 · Cited by 103

Myeloperoxidase Deficiency

Nauseef, W. M. (1988) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(18)30634-8 · Cited by 103

Myeloperoxidase binds to low‐density lipoprotein: potential implications for atherosclerosis

Carr, A. C., Myzak, M. C., Stocker, R., McCall, M. R., & Frei, B. B. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02227-4 · Cited by 102

Loss of GSH and thiol enzymes in endothelial cells exposed to sublethal concentrations of hypochlorous acid

Pullar, J. M., Winterbourn, C. C., & Vissers, M. C. M. (1999) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1999.277.4.h1505 · Cited by 102

Potential Role of Methionine Sulfoxide in the Inactivation of the Chaperone GroEL by Hypochlorous Acid (HOCl) and Peroxynitrite (ONOO–)

Khor, H. K., Fisher, M. T., & Schöneich, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310045200 · Cited by 101

Leukocyte-Derived Myeloperoxidase Amplifies High-Glucose—Induced Endothelial Dysfunction Through Interaction With High-Glucose—Stimulated, Vascular Non—Leukocyte-Derived Reactive Oxygen Species

Zhang, C., Yang, J., & Jennings, L. K. (2004) · Diabetes · doi:10.2337/diabetes.53.11.2950 · Cited by 101

Kinetic Analysis of the Role of Histidine Chloramines in Hypochlorous Acid Mediated Protein Oxidation

Pattison, D. I., & Davies, M. J. (2005) · Biochemistry · doi:10.1021/bi0474665 · Cited by 100

Hypochlorite and superoxide radicals can act synergistically to induce fragmentation of hyaluronan and chondroitin sulphates

REES, M. D., HAWKINS, C. L., & DAVIES, M. J. (2004) · Biochemical Journal · doi:10.1042/bj20040148 · Cited by 100

Reactions of Superoxide with Myeloperoxidase

Kettle, A. J., Anderson, R. F., Hampton, M. B., & Winterbourn, C. C. (2007) · Biochemistry · doi:10.1021/bi602587k · Cited by 99

Oxidative Cross-linking of Tryptophan to Glycine Restrains Matrix Metalloproteinase Activity

Fu, X., Kao, J. L.-F., Bergt, C., Kassim, S. Y., Saifee, N. H., d'Avignon, A., Parks, W. C., Mecham, R. P., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300506200 · Cited by 99

Taurine chloramine is more selective than hypochlorous acid at targeting critical cysteines and inactivating creatine kinase and glyceraldehyde-3-phosphate dehydrogenase

Peskin, A. V., & Winterbourn, C. C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.019 · Cited by 98

Myeloperoxidase Generates 5-Chlorouracil in Human Atherosclerotic Tissue

Takeshita, J., Byun, J., Nhan, T. Q., Pritchard, D. K., Pennathur, S., Schwartz, S. M., Chait, A., & Heinecke, J. W. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509236200 · Cited by 95

Hypochlorite-Mediated Fragmentation of Hyaluronan, Chondroitin Sulfates, and RelatedN-Acetyl Glycosamines: Evidence for Chloramide Intermediates, Free Radical Transfer Reactions, and Site-Specific Fragmentation

Rees, M. D., Hawkins, C. L., & Davies, M. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0370591 · Cited by 95

Superoxide is an antagonist of anti-inflammatory drugs that inhibit hypochlorous acid production by myeloperoxidase

Kettle, A. J., Gedye, C. A., & Winterbourn, C. C. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90010-t · Cited by 94

A Kinetic Analysis of the Catalase Activity of Myeloperoxidase

Kettle, A. J., & Winterbourn, C. C. (2001) · Biochemistry · doi:10.1021/bi010940b · Cited by 94

A low molecular weight antioxidant decreases weight and lowers tumor incidence

Mitchell, J. B., Xavier, S., DeLuca, A. M., Sowers, A. L., Cook, J. A., Krishna, M. C., Hahn, S. M., & Russo, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01193-0 · Cited by 94

N‐(2‐Oxoacyl)amino Acids and Nitriles as Final Products of Dipeptide Chlorination Mediated by the Myeloperoxidase/H2O2/Cl− System

Stelmaszyńska, T., & Zgliczyński, J. M. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12748.x · Cited by 92

Glutathione Oxidation by Hypochlorous Acid in Endothelial Cells Produces Glutathione Sulfonamide as a Major Product but Not Glutathione Disulfide

Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102088200 · Cited by 91

Chlorine transfer between glycine, taurine, and histamine: reaction rates and impact on cellular reactivity

Peskin, A. V., Midwinter, R. G., Harwood, D. T., & Winterbourn, C. C. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.010 · Cited by 91

Peroxidases: a role in the metabolism and side effects of drugs

Tafazoli, S., & O'Brien, P. J. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03394-5 · Cited by 89

The Myeloperoxidase-Derived Oxidant HOSCN Inhibits Protein Tyrosine Phosphatases and Modulates Cell Signalling via the Mitogen-Activated Protein Kinase (MAPK) Pathway in Macrophages

Lane, A. E., Tan, J. T. M., Hawkins, C. L., Heather, A. K., & Davies, M. J. (2010) · Biochemical Journal · doi:10.1042/bj20100082 · Cited by 86

Interaction of myeloperoxidase with vascular NAD(P)H oxidase-derived reactive oxygen species in vasculature: implications for vascular diseases

Zhang, C., Yang, J., Jacobs, J. D., & Jennings, L. K. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00435.2003 · Cited by 86

Production of glutathione sulfonamide and dehydroglutathione from GSH by myeloperoxidase-derived oxidants and detection using a novel LC–MS/MS method

Harwood, D. T., Kettle, A. J., & Winterbourn, C. C. (2006) · Biochemical Journal · doi:10.1042/bj20060978 · Cited by 85

Exploitation of the unusual thermodynamic properties of human myeloperoxidase in inhibitor design

Jantschko, W., Furtmüller, P. G., Zederbauer, M., Neugschwandtner, K., Lehner, I., Jakopitsch, C., Arnhold, J., & Obinger, C. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.02.006 · Cited by 85

IκB is a sensitive target for oxidation by cell-permeable chloramines: inhibition of NF-κB activity by glycine chloramine through methionine oxidation

Midwinter, R. G., Cheah, F.-C., Moskovitz, J., Vissers, M. C., & Winterbourn, C. C. (2006) · Biochemical Journal · doi:10.1042/bj20052026 · Cited by 85

p-Hydroxyphenylacetaldehyde, the Major Product of l-Tyrosine Oxidation by the Myeloperoxidase-H2O2-Chloride System of Phagocytes, Covalently Modifies ε-Amino Groups of Protein Lysine Residues

Hazen, S. L., Gaut, J. P., Hsu, F., Crowley, J. R., d'Avignon, A., & Heinecke, J. W. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.27.16990 · Cited by 83

Inhibition of myeloperoxidase-mediated hypochlorous acid production by nitroxides

Rees, M. D., Bottle, S. E., Fairfull‐Smith, K. E., Malle, E., Whitelock, J. M., & Davies, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090309 · Cited by 83

Superoxide-dependent Oxidation of Melatonin by Myeloperoxidase

Ximenes, V. F., Silva, S. D. O., Rodrigues, M. R., Catalani, L. H., Maghzal, G. J., Kettle, A. J., & Campa, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506384200 · Cited by 83

Hypochlorous acid-mediated modification of cholesterol and phospholipid: analysis of reaction products by gas chromatography-mass spectrometry.

van den Berg, J., Winterbourn, C., & Kuypers, F. (1993) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)35117-8 · Cited by 83

Superoxide-dependent hydroxylation by myeloperoxidase.

Kettle, A. J., & Winterbourn, C. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32533-4 · Cited by 82

Myeloperoxidase-derived Reactive Chlorinating Species from Human Monocytes Target Plasmalogens in Low Density Lipoprotein

Thukkani, A. K., Albert, C. J., Wildsmith, K. R., Messner, M. C., Martinson, B. D., Hsu, F., & Ford, D. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305449200 · Cited by 81

The role of hypothiocyanous acid (HOSCN) in biological systems

Hawkins, C. L. (2009) · Free Radical Research · doi:10.3109/10715760903214462 · Cited by 81

Hypothiocyanous acid is a more potent inducer of apoptosis and protein thiol depletion in murine macrophage cells than hypochlorous acid or hypobromous acid

Lloyd, M. M., van Reyk, D. M., Davies, M. J., & Hawkins, C. L. (2008) · Biochemical Journal · doi:10.1042/bj20080468 · Cited by 79

Myricitrin as a substrate and inhibitor of myeloperoxidase: Implications for the pharmacological effects of flavonoids

Meotti, F. C., Senthilmohan, R., Harwood, D. T., Missau, F. C., Pizzolatti, M. G., & Kettle, A. J. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.017 · Cited by 78

Molecular Cloning and Characterization of the Chromosomal Gene for Human Lactoperoxidase

Ueda, T., Sakamaki, K., Kuroki, T., Yano, I., & Nagata, S. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.0032a.x · Cited by 78

Hypochlorous Acid-Derived Modification of Phospholipids: Characterization of Aminophospholipids as Regulatory Molecules for Lipid Peroxidation

Kawai, Y., Kiyokawa, H., Kimura, Y., Kato, Y., Tsuchiya, K., & Terao, J. (2006) · Biochemistry · doi:10.1021/bi0610909 · Cited by 78

Bromination of deoxycytidine by eosinophil peroxidase: A mechanism for mutagenesis by oxidative damage of nucleotide precursors

Henderson, J. P., Byun, J., Williams, M. V., McCormick, M. L., Parks, W. C., Ridnour, L. A., & Heinecke, J. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1631 · Cited by 77

Quercetin and Its In Vivo Metabolites Inhibit Neutrophil-Mediated Low-Density Lipoprotein Oxidation

Loke, W. M., Proudfoot, J. M., McKinley, A. J., Needs, P. W., Kroon, P. A., Hodgson, J. M., & Croft, K. D. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8003042 · Cited by 77

Substrates and products of eosinophil peroxidase

van DALEN, C. J., & Kettle, A. J. (2001) · Biochemical Journal · doi:10.1042/bj3580233 · Cited by 77

Simultaneous determination of reduced glutathione, glutathione disulphide and glutathione sulphonamide in cells and physiological fluids by isotope dilution liquid chromatography–tandem mass spectrometry

Harwood, D. T., Kettle, A. J., Brennan, S., & Winterbourn, C. C. (2009) · Journal of Chromatography B · doi:10.1016/j.jchromb.2009.04.018 · Cited by 76

The action of hypochlorous acid on phosphatidylcholine liposomes in dependence on the content of double bonds. Stoichiometry and NMR analysis

Arnhold, J., Panasenko, O. M., Schiller, J., IuA, V., & Arnold, K. (1995) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(95)02484-z · Cited by 75

[20] Peroxynitrite-dependent tyrosine nitration catalyzed by superoxide dismutase, myeloperoxidase, and horseradish peroxidase

Sampson, J. B., Rosen, H., & Beckman, J. S. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)69023-5 · Cited by 74

Myeloperoxidase-dependent oxidative inactivation of neutrophil neutral proteinases and microbicidal enzymes

Vissers, M. C. M., & Winterbourn, C. C. (1987) · Biochemical Journal · doi:10.1042/bj2450277 · Cited by 72

Myeloperoxidase-Dependent Generation of a Tyrosine Peroxide by Neutrophils

Winterbourn, C. C., Pichorner, H., & Kettle, A. J. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.9773 · Cited by 71

The Vinyl Ether Linkages of Plasmalogens Are Favored Targets for Myeloperoxidase-Derived Oxidants: A Kinetic Study

Skaff, O., Pattison, D. I., & Davies, M. J. (2008) · Biochemistry · doi:10.1021/bi800786q · Cited by 71

Association of myeloperoxidase with heparin: Oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme

Daphna, E.-M., Sharabani, M., Eynat, P., Aviram, I., & Sara, R. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006848730927 · Cited by 70

Regulation of Apoptosis by Vitamin C

Vissers, M. C. M., Lee, W.-G., & Hampton, M. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107664200 · Cited by 70

Acetaminophen (paracetamol) inhibits myeloperoxidase-catalyzed oxidant production and biological damage at therapeutically achievable concentrations

Koelsch, M., Mallack, R., Graham, G. G., Kajer, T., Milligan, M. K., Nguyen, L. Q., Newsham, D. W., Keh, J. S., Kettle, A. J., Scott, K. F., et al. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2009.11.024 · Cited by 70

The inhibition of myeloperoxidase by ceruloplasmin can be reversed by anti-myeloperoxidase antibodies

Griffin, S., Chapman, P. T., Lianos, E. A., & Lockwood, C. M. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.055003917.x · Cited by 68

Modification of neutrophil oxidant production with diphenyleneiodonium and its effect on bacterial killing

Hampton, M. B., & Winterbourn, C. C. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00181-i · Cited by 67

On the Irreversible Destruction of Reduced Nicotinamide Nucleotides by Hypohalous Acids

Prütz, W. A., Kissner, R., Koppenol, W. H., & Rüegger, H. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1914 · Cited by 67

Thiocyanate Is an Efficient Endogenous Scavenger of the Phagocytic Killing Agent Hypobromous Acid

Nagy, P., Beal, J. L., & Ashby, M. T. (2006) · Chemical Research in Toxicology · doi:10.1021/tx050338c · Cited by 67

Formation of reactive halide species by myeloperoxidase and eosinophil peroxidase

Spalteholz, H., Panasenko, O. M., & Arnhold, J. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.06.025 · Cited by 67

Mechanistic insight into the peroxidase catalyzed nitration of tyrosine derivatives by nitrite and hydrogen peroxide

Monzani, E., Roncone, R., Galliano, M., Koppenol, W. H., & Casella, L. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.03992.x · Cited by 66

Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan

Rees, M. D., Whitelock, J. M., Malle, E., Chuang, C. Y., Iozzo, R. V., Nilasaroya, A., & Davies, M. J. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.09.005 · Cited by 65

Transient and Steady-state Kinetics of the Oxidation of Substituted Benzoic Acid Hydrazides by Myeloperoxidase

Burner, U., Obinger, C., Paumann, M., Furtmüller, P. G., & Kettle, A. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9494 · Cited by 65

The Eosinophil Peroxidase-Hydrogen Peroxide-Bromide System of Human Eosinophils Generates 5-Bromouracil, a Mutagenic Thymine Analogue

Henderson, J. P., Byun, J., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi002015f · Cited by 64

Mechanisms for suppressing NADPH oxidase in the vascular wall

Dusting, G. J., Selemidis, S., & Jiang, F. (2005) · Memórias do Instituto Oswaldo Cruz · doi:10.1590/s0074-02762005000900016 · Cited by 62

Oxidation of hydroquinone by myeloperoxidase. Mechanism of stimulation by benzoquinone.

Kettle, A. J., & Winterbourn, C. C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42445-3 · Cited by 60

Endogenous Formation of Novel Halogenated 2′-Deoxycytidine

Kawai, Y., Morinaga, H., KONDO, H., Miyoshi, N., Nakamura, Y., Uchida, K., & Osawa, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408210200 · Cited by 60

Differential effects of oxidizing agents on human plasma .alpha.1-proteinase inhibitor and human neutrophil myeloperoxidase

Matheson, N., & Travis, J. W. (1985) · Biochemistry · doi:10.1021/bi00329a021 · Cited by 60

The Role of Aromatic Amino Acid Oxidation, Protein Unfolding, and Aggregation in the Hypobromous Acid-Induced Inactivation of Trypsin Inhibitor and Lysozyme

Hawkins, C. L., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0502084 · Cited by 60

Histamine chloramine reactivity with thiol compounds, ascorbate, and methionine and with intracellular glutathione

Peskin, A. V., & Winterbourn, C. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00502-1 · Cited by 59

Kinetics of Hypobromous Acid-Mediated Oxidation of Lipid Components and Antioxidants

Skaff, O., Pattison, D. I., & Davies, M. J. (2007) · Chemical Research in Toxicology · doi:10.1021/tx7003097 · Cited by 59

Differential reactivities of hypochlorous and hypobromous acids with purified Escherichia coli phospholipid: formation of haloamines and halohydrins

Carr, A. C., van den Berg, J. J. M., & Winterbourn, C. C. (1998) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/s0005-2760(98)00038-1 · Cited by 58

Myeloperoxidase-induced formation of chlorohydrins and lysophospholipids from unsaturated phosphatidylcholines

Panasenko, O. M., Spalteholz, H., Schiller, J., & Arnhold, J. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01358-8 · Cited by 58

Enhanced Killing of Myeloperoxidase-Coated Bacteria in the Myeloperoxidase-H2O2-C1- System

Selvaraj, R. J., Zgliczyński, J. M., Paul, B. B., & Sbarra, A. J. (1978) · The Journal of Infectious Diseases · doi:10.1093/infdis/137.4.481 · Cited by 57

Hypochlorite-induced oxidation of thiols: Formation of thiyl radicals and the role of sulfenyl chlorides as intermediates

Davies, M. J., & Hawkins, C. L. (2000) · Free Radical Research · doi:10.1080/10715760000301241 · Cited by 57

Hypobromous acid and bromamine production by neutrophils and modulation by superoxide

Chapman, A., Skaff, O., Senthilmohan, R., Kettle, A. J., & Davies, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20071563 · Cited by 57

Arming of mononuclear phagocytes by eosinophil peroxidase bound to Staphylococcus aureus.

Ramsey, P. G., Martin, T. R., Chi, E. Y., & Klebanoff, S. J. (1982) · The Journal of Immunology · doi:10.4049/jimmunol.128.1.415 · Cited by 56

Myeloperoxidase Interacts with Endothelial Cell-Surface Cytokeratin 1 and Modulates Bradykinin Production by the Plasma Kallikrein-Kinin System

Astern, J., Pendergraft, W. F., Falk, R. J., Jennette, J. C., Schmaier, A. H., Mahdi, F., & Preston, G. A. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060831 · Cited by 56

Serotonin as a physiological substrate for myeloperoxidase and its superoxide-dependent oxidation to cytotoxic tryptamine-4,5-dione

Ximenes, V. F., Maghzal, G. J., Turner, R., Kato, Y., Winterbourn, C. C., & Kettle, A. J. (2009) · Biochemical Journal · doi:10.1042/bj20090776 · Cited by 56

Standard reduction potentials of all couples of the peroxidase cycle of lactoperoxidase

Furtmüller, P. G., Arnhold, J., Jantschko, W., Zederbauer, M., Jakopitsch, C., & Obinger, C. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.02.021 · Cited by 55

Superoxide-mediated Formation of Tyrosine Hydroperoxides and Methionine Sulfoxide in Peptides through Radical Addition and Intramolecular Oxygen Transfer

Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809396200 · Cited by 53

Tryptophan residues are targets in hypothiocyanous acid-mediated protein oxidation

Hawkins, C. L., Pattison, D. I., Stanley, N., & Davies, M. J. (2008) · Biochemical Journal · doi:10.1042/bj20070941 · Cited by 53

Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin

Av, S., Ageeva, K. V., Cherkalina, O. S., Pulina, M. O., Zakharova, E. T., Prozorovskii, V. N., Aksenov, D. V., Vasilyev, V. B., & Panasenko, O. M. (2010) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2010.02.002 · Cited by 50

Heparan Sulfate Degradation via Reductive Homolysis of Its N-Chloro Derivatives

Rees, M. D., & Davies, M. J. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0577239 · Cited by 49

Superoxide enhances hypochlorous acid production by stimulated human neutrophils

Kettle, A. J., & Winterbourn, C. C. (1990) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(90)90146-5 · Cited by 48

Cellular effects of peptide and protein hydroperoxides

Rahmanto, A. S., Morgan, P. E., Hawkins, C. L., & Davies, M. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.025 · Cited by 48

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, S. L., Gaut, J. P., Crowley, J. R., Hsu, F., & Heinecke, J. W. (2000) · Biochemical Journal · doi:10.1042/bj3520693 · Cited by 47

Eosinophil Peroxidase Catalyzes Bromination of Free Nucleosides and Double-Stranded DNA

Shen, Z., Mitra, S. N., Wu, W., Chen, Y., Yang, Y., Qin, J., & Hazen, S. L. (2001) · Biochemistry · doi:10.1021/bi001961t · Cited by 46

Thiocyanate catalyzes myeloperoxidase-initiated lipid oxidation in LDL

Exner, M., Hermann, M., Hofbauer, R., Hartmann, B. W., Kapiotis, S., & Gmeiner, B. M. K. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.039 · Cited by 46

Indole ring oxidation by activated leukocytes prevents the production of hypochlorous acid

Ximenes, V. F., Paino, I. M. M., Faria-Oliveira, O. M. M. D., da Fonseca, L. M., & Brunetti, I. L. (2005) · Brazilian Journal of Medical and Biological Research · doi:10.1590/s0100-879x2005001100003 · Cited by 46

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