Myeloperoxidase-derived oxidation: Mechanisms of biological damage and its prevention
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There is considerable interest in the role that mammalian heme peroxidase enzymes, primarily myeloperoxidase, eosinophil peroxidase and lactoperoxidase, may play in a wide range of human pathologies. This has been sparked by rapid developments in our understanding of the basic biochemistry of these enzymes, a greater understanding of the basic chemistry and biochemistry of the oxidants formed by these species, the development of biomarkers that can be used damage induced by these oxidants in vivo, and the recent identification of a number of compounds that show promise as inhibitors of these enzymes. Such compounds offer the possibility of modulating damage in a number of human pathologies. This reviews recent developments in our understanding of the biochemistry of myeloperoxidase, the oxidants that this enzyme generates, and the use of inhibitors to inhibit such damage.
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HOCl is a very reactive and oxidizing agent, can act as a chlorinating agent, and is the main strong oxidant generated by neutrophils in appreciable quantities.
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
Myeloperoxidase MPO catalyzes the oxidation of Cl− by H2O2 to give hypochlorous acid HOCl.
“The reaction catalyzed by MPO is the oxidation of the Cl− anion by H2O2 to give hypochlorous acid HOCl, a very reactive and oxidizing agent, which can also act as a chlorinating agent and is the main strong oxidant generated by neutrophils in appreciable quantities [30].”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
Hypochlorous acid HOCl and hypothiocyanous acid HOSCN are important inorganic bactericidal molecules effective against a wide range of microbes.
“Hypochlorous acid HOCl and hypothiocyanous acid HOSCN synthesized through the enzyme myeloperoxidase MPO, which catalyzes the reaction between H2O2 and Cl− or SCN−, are important inorganic bactericidal molecules, effective against a wide range of microbes.”
From The Role of Reactive Species on Innate Immunity (2022) · cites this paper as [30]
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Cites
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455 · see citing works
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 2,002 · see citing works
Nitric oxide, oxidants, and protein tyrosine nitration
Radí, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307446101 · Cited by 1,456 · see citing works
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 · see citing works
Self-citationDaugherty, A., Dunn, J. L., Rateri, D. L., & Heinecke, J. W. (1994) · Journal of Clinical Investigation · doi:10.1172/jci117342 · Cited by 1,269 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790 · see citing works
Self-citationZheng, 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 · see citing works
Bessems, J. G. M., & Vermeulen, N. P. E. (2001) · Critical Reviews in Toxicology · doi:10.1080/20014091111677 · Cited by 716 · see citing works
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 706 · see citing works
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 · see citing works
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 660 · see citing works
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 · see citing works
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 · see citing works
Self-citationMammalian 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 556 · see citing works
Self-citationMyeloperoxidase: 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 522 · see citing works
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 · see citing works
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 · see citing works
Li, Y., & Trush, M. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9729 · Cited by 470 · see citing works
Winterbourn, C. C. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90120-5 · Cited by 463 · see citing works
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 · see citing works
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 · see citing works
Reactive species formed on proteins exposed to singlet oxygen
Davies, M. J. (2004) · Photochemical & Photobiological Sciences · doi:10.1039/b307576c · Cited by 399 · see citing works
Self-citationNitric 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 398 · see citing works
Fiedler, T. J., Davey, C. A., & Fenna, R. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.16.11964 · Cited by 374 · see citing works
Pattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 359 · see citing works
Self-citationActive 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 · see citing works
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 · see citing works
[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 348 · see citing works
Savenkova, M. L., Mueller, D. M., & Heinecke, J. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32005-7 · Cited by 339 · see citing works
Pattison, D. I., & Davies, M. J. (2006) · Biochemistry · doi:10.1021/bi060348s · Cited by 338 · see citing works
Self-citationPeskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 335 · see citing works
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 · see citing works
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 · see citing works
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 314 · see citing works
Hawkins, C. L., & Davies, M. J. (1998) · Biochemical Journal · doi:10.1042/bj3320617 · Cited by 305 · see citing works
Self-citationBaldus, S. E., Eiserich, J. P., Mani, A. R., et al. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200112617 · Cited by 281 · see citing works
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 · see citing works
O'Brien, P. J. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00201-5 · Cited by 259 · see citing works
Thomas, E. L. (1979) · Infection and Immunity · doi:10.1128/iai.23.2.522-531.1979 · Cited by 251 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationInteraction 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 · see citing works
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 · see citing works
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 221 · see citing works
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 · see citing works
Pattison, D. I., & Davies, M. J. (2004) · Biochemistry · doi:10.1021/bi035946a · Cited by 209 · see citing works
Self-citationKim, H., & Gladyshev, V. N. (2007) · Biochemical Journal · doi:10.1042/bj20070929 · Cited by 204 · see citing works
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 203 · see citing works
Hawkins, C. L., & Davies, M. J. (1999) · Biochemical Journal · doi:10.1042/bj3400539 · Cited by 201 · see citing works
Self-citationBaldus, 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 200 · see citing works
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 195 · see citing works
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 · see citing works
Neutrophils convert tyrosyl residues in albumin to chlorotyrosine
Kettle, A. J. (1996) · FEBS Letters · doi:10.1016/0014-5793(95)01494-2 · Cited by 188 · see citing works
(2008) · International Union of Pure and Applied Chemistry (IUPAC) eBooks · doi:10.1351/goldbook.f02360 · Cited by 187 · see citing works
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 187 · see citing works
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 187 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Kettle, A. J., & Winterbourn, C. C. (1988) · Biochemical Journal · doi:10.1042/bj2520529 · Cited by 177 · see citing works
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 · see citing works
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 · see citing works
Ellis, J. A., Mayer, S. J., & Jones, O. T. G. (1988) · Biochemical Journal · doi:10.1042/bj2510887 · Cited by 164 · see citing works
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 164 · see citing works
Gas Chromatography Mass Spectrometry
Kopka, J. (2006) · Springer eBooks · doi:10.1007/3-540-29782-0_1 · Cited by 163 · see citing works
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 159 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Heinecke, J. W., Li, W., Mueller, D. M., Bohrer, A., & TURK, J. W. (1994) · Biochemistry · doi:10.1021/bi00199a041 · Cited by 141 · see citing works
Henderson, J. P., Byun, J., Takeshita, J., & Heinecke, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303928200 · Cited by 141 · see citing works
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 · see citing works
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2003) · Chemical Research in Toxicology · doi:10.1021/tx025670s · Cited by 139 · see citing works
Self-citationNitrite 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 · see citing works
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 · see citing works
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 · see citing works
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 131 · see citing works
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 · see citing works
Skaff, O., Pattison, D. I., & Davies, M. J. (2009) · Biochemical Journal · doi:10.1042/bj20090276 · Cited by 130 · see citing works
Self-citationAqueous 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 · see citing works
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 · see citing works
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 125 · see citing works
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 · see citing works
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 · see citing works
Self-citationProduction 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 · see citing works
[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 123 · see citing works
Senthilmohan, R., & Kettle, A. J. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.005 · Cited by 122 · see citing works
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 · see citing works
Prütz, W. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0440 · Cited by 121 · see citing works
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 · see citing works
Pattison, D. I., Hawkins, C. L., & Davies, M. J. (2007) · Biochemistry · doi:10.1021/bi7008294 · Cited by 118 · see citing works
Self-citationBABIOR, B. M. (1987) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(87)90118-6 · Cited by 117 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Self-citationNagy, P., Jameson, G. N. L., & Winterbourn, C. C. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900249d · Cited by 111 · see citing works
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 · see citing works
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 · see citing works
Hawkins, C. L., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050207b · Cited by 109 · see citing works
Self-citationFurtmüller, 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 · see citing works
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 · see citing works
Fu, X., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi015777z · Cited by 107 · see citing works
Zederbauer, M., Furtmüller, P. G., Brogioni, S., Jakopitsch, C., Smulevich, G., & Obinger, C. (2007) · Natural Product Reports · doi:10.1039/b604178g · Cited by 106 · see citing works
VISSERS, C. M. M., Carr, A. C., & Chapman, L. (1998) · Biochemical Journal · doi:10.1042/bj3300131 · Cited by 103 · see citing works
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 103 · see citing works
Nauseef, W. M. (1988) · Hematology/Oncology Clinics of North America · doi:10.1016/s0889-8588(18)30634-8 · Cited by 103 · see citing works
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 · see citing works
Zhang, C., Yang, J., & Jennings, L. K. (2004) · Diabetes · doi:10.2337/diabetes.53.11.2950 · Cited by 101 · see citing works
REES, M. D., HAWKINS, C. L., & DAVIES, M. J. (2004) · Biochemical Journal · doi:10.1042/bj20040148 · Cited by 100 · see citing works
Self-citationReactions 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 · see citing works
Khor, H. K., Fisher, M. T., & Schöneich, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310045200 · Cited by 99 · see citing works
Pattison, D. I., & Davies, M. J. (2005) · Biochemistry · doi:10.1021/bi0474665 · Cited by 99 · see citing works
Self-citationPeskin, A. V., & Winterbourn, C. C. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.019 · Cited by 98 · see citing works
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 98 · see citing works
Kettle, A. J., Gedye, C. A., & Winterbourn, C. C. (1993) · Biochemical Pharmacology · doi:10.1016/0006-2952(93)90010-t · Cited by 96 · see citing works
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 · see citing works
Rees, M. D., Hawkins, C. L., & Davies, M. J. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0370591 · Cited by 95 · see citing works
Self-citationA Kinetic Analysis of the Catalase Activity of Myeloperoxidase
Kettle, A. J., & Winterbourn, C. C. (2001) · Biochemistry · doi:10.1021/bi010940b · Cited by 94 · see citing works
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 · see citing works
Stelmaszyńska, T., & Zgliczyński, J. M. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12748.x · Cited by 92 · see citing works
Pullar, J. M., Vissers, M. C. M., & Winterbourn, C. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102088200 · Cited by 91 · see citing works
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 90 · see citing works
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 · see citing works
Self-citationPeroxidases: 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 86 · see citing works
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 · see citing works
Harwood, D. T., Kettle, A. J., & Winterbourn, C. C. (2006) · Biochemical Journal · doi:10.1042/bj20060978 · Cited by 85 · see citing works
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 · see citing works
Midwinter, R. G., Cheah, F.-C., Moskovitz, J., Vissers, M. C., & Winterbourn, C. C. (2006) · Biochemical Journal · doi:10.1042/bj20052026 · Cited by 85 · see citing works
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 · see citing works
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 · see citing works
Self-citationSuperoxide-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 · see citing works
van den Berg, J., Winterbourn, C., & Kuypers, F. (1993) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)35117-8 · Cited by 83 · see citing works
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 · see citing works
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 · see citing works
The role of hypothiocyanous acid (HOSCN) in biological systems
Hawkins, C. L. (2009) · Free Radical Research · doi:10.3109/10715760903214462 · Cited by 81 · see citing works
Lloyd, M. M., van Reyk, D. M., Davies, M. J., & Hawkins, C. L. (2008) · Biochemical Journal · doi:10.1042/bj20080468 · Cited by 79 · see citing works
Self-citationMeotti, 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 · see citing works
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 · see citing works
Kawai, Y., Kiyokawa, H., Kimura, Y., Kato, Y., Tsuchiya, K., & Terao, J. (2006) · Biochemistry · doi:10.1021/bi0610909 · Cited by 78 · see citing works
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 · see citing works
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 · see citing works
Substrates and products of eosinophil peroxidase
van DALEN, C. J., & Kettle, A. J. (2001) · Biochemical Journal · doi:10.1042/bj3580233 · Cited by 77 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Vissers, M. C. M., & Winterbourn, C. C. (1987) · Biochemical Journal · doi:10.1042/bj2450277 · Cited by 72 · see citing works
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 · see citing works
Skaff, O., Pattison, D. I., & Davies, M. J. (2008) · Biochemistry · doi:10.1021/bi800786q · Cited by 71 · see citing works
Self-citationDaphna, E.-M., Sharabani, M., Eynat, P., Aviram, I., & Sara, R. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006848730927 · Cited by 70 · see citing works
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 · see citing works
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 68 · see citing works
Self-citationGriffin, 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 · see citing works
Hampton, M. B., & Winterbourn, C. C. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00181-i · Cited by 67 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 65 · see citing works
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 · see citing works
Henderson, J. P., Byun, J., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi002015f · Cited by 64 · see citing works
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 64 · see citing works
Self-citationMechanisms 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 · see citing works
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 · see citing works
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 · see citing works
Matheson, N., & Travis, J. W. (1985) · Biochemistry · doi:10.1021/bi00329a021 · Cited by 60 · see citing works
Hawkins, C. L., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx0502084 · Cited by 60 · see citing works
Self-citationPeskin, A. V., & Winterbourn, C. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00502-1 · Cited by 59 · see citing works
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 · see citing works
Self-citationCarr, 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 · see citing works
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 · see citing works
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 · see citing works
Davies, M. J., & Hawkins, C. L. (2000) · Free Radical Research · doi:10.1080/10715760000301241 · Cited by 57 · see citing works
Self-citationHypobromous 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 · see citing works
Self-citationArming 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 · see citing works
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 · see citing works
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 · see citing works
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 54 · see citing works
Nagy, P., Kettle, A. J., & Winterbourn, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809396200 · Cited by 53 · see citing works
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 · see citing works
Self-citationAv, 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 · see citing works
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 · see citing works
Self-citationSuperoxide 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 · see citing works
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 · see citing works
Self-citationEosinophil 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 · see citing works
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 · see citing works
Hazen, S. L., Gaut, J. P., Crowley, J. R., Hsu, F., & Heinecke, J. W. (2000) · Biochemical Journal · doi:10.1042/bj3520693 · Cited by 46 · see citing works
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 · see citing works
Albert, C. J., Thukkani, A. K., Heuertz, R. M., Slungaard, A., Hazen, S. L., & Ford, D. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211634200 · Cited by 45 · see citing works
Reaction of compound III of myeloperoxidase with ascorbic acid.
Marquez‐Curtis, L. A., & Dunford, H. B. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39293-2 · Cited by 43 · see citing works
Subrahmanyam, V. V., Kolachana, P., & Smith, M. T. (1991) · Free Radical Research Communications · doi:10.3109/10715769109105224 · Cited by 43 · see citing works
Kettle, A. J., & Candaeis, L. P. (2000) · Redox Report · doi:10.1179/135100000101535726 · Cited by 41 · see citing works
Miyasaki, K. T., Zambon, J. J., Jones, C. A., & Wilson, M. E. (1987) · Infection and Immunity · doi:10.1128/iai.55.5.1029-1036.1987 · Cited by 40 · see citing works
Flagged first, then by citations
Research works printed but not linked: 2
- [174]Lentner C Geigy Scientific Tables vol. 3: Physical Chemistry, Composition of Blood, Hematology, Somatometric Data Basle Ciba-Geigy Ltd 1984
- [226]Kettle AJ Gedye CA Winterbourn CC Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide Biochem J 1997 321 503 508 9020887 PMC1218097
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Sedgwick, A. C., Wu, L., Han, H., Bull, S. D., He, X., James, T. D., Sessler, J. L., Tang, B. Z., Tian, H., & Yoon, J. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00185e · Cited by 1,577 · see citing works
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Myeloperoxidase as an Active Disease Biomarker: Recent Biochemical and Pathological Perspectives
Khan, A. A., Alsahli, M. A., & Rahmani, A. H. (2018) · Medical Sciences · doi:10.3390/medsci6020033 · Cited by 419 · see citing works
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ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications
Moldogazieva, N. T., Mokhosoev, I. M., Feldman, N. B., & Lutsenko, S. V. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1457217 · Cited by 291 · see citing works
Gou, S., Huang, Y., Wan, Y., Ma, Y., Zhou, X., Tong, X., Huang, J. T., Kang, Y., Pan, G., Dai, F., et al. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.05.012 · Cited by 279 · see citing works
Dispersibility‐Dependent Biodegradation of Graphene Oxide by Myeloperoxidase
Kurapati, R., Russier, J., Squillaci, M. A., Treossi, E., Ménard‐Moyon, C., Castillo, A. E. D. R., Vázquez, E., Samorı́, P., Palermo, V., & Bianco, A. (2015) · Small · doi:10.1002/smll.201500038 · Cited by 270 · see citing works
Involvement of free radicals and oxidative stress in NAFLD/NASH
Sumida, Y., Niki, E., Naito, Y., & Yoshikawa, T. (2013) · Free Radical Research · doi:10.3109/10715762.2013.837577 · Cited by 280 · see citing works
Zhang, X., Deeke, S. A., Ning, Z., Starr, A. E., Butcher, J., Li, J. S. Y., Mayne, J., Cheng, K., Liao, B., Li, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05357-4 · Cited by 260 · see citing works
The Role of Reactive Oxygen Species (ROS) in the Formation of Extracellular Traps (ETs) in Humans
Stoiber, W., Obermayer, A., Steinbacher, P., & Krautgartner, W.-D. (2015) · Biomolecules · doi:10.3390/biom5020702 · Cited by 250 · see citing works
Sulfur-based fluorescent probes for HOCl: Mechanisms, design, and applications
Hou, J., Kwon, N., Wang, S., Wang, B., He, X., Yoon, J., & Shen, J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214232 · Cited by 241 · see citing works
Hydrogen peroxide: A central player in physical plasma-induced oxidative stress in human blood cells
Bekeschus, S., Kolata, J., Winterbourn, C. C., Krämer, A., Turner, R., Weltmann, K. D., Bröker, B. M., & Masur, K. (2014) · Free Radical Research · doi:10.3109/10715762.2014.892937 · Cited by 239 · see citing works
Ulfig, A., & Leichert, L. I. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03591-y · Cited by 239 · see citing works
Neutrophils in Rheumatoid Arthritis: Breaking Immune Tolerance and Fueling Disease
O’Neil, L. J., & Kaplan, M. J. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.12.008 · Cited by 228 · see citing works
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · Stresses · doi:10.3390/stresses2030019 · Cited by 218 · see citing works
Grabcanovic-Musija, F., Obermayer, A., Stoiber, W., Krautgartner, W.-D., Steinbacher, P., Winterberg, N., Bathke, A. C., Klappacher, M., & Studnicka, M. (2015) · Respiratory Research · doi:10.1186/s12931-015-0221-7 · Cited by 211 · see citing works
Myeloperoxidase: A Leukocyte-Derived Protagonist of Inflammation and Cardiovascular Disease
Nußbaum, C., Klinke, A., Adam, M., Baldus, S. E., & Sperandio, M. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4783 · Cited by 196 · see citing works
Reactivity and degradation products of tryptophan in solution and proteins
Bellmaine, S. F., Schnellbaecher, A., & Zimmer, A. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.002 · Cited by 194 · see citing works
Natural Products Containing a Nitrogen–Sulfur Bond
Petkowski, J. J., Bains, W., & Seager, S. (2018) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00921 · Cited by 180 · see citing works
Redox regulation by reversible protein S-thiolation in bacteria
Vu, L. V., Rossius, M., & Antelmann, H. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00187 · Cited by 173 · see citing works
Karimi, M., Ignasiak, M. T., Chan, B., Croft, A. K., Radom, L., Schiesser, C. H., Pattison, D. I., & Davies, M. J. (2016) · Scientific Reports · doi:10.1038/srep38572 · Cited by 174 · see citing works
Self-citationPattison, D. I., Davies, M. J., & Hawkins, C. L. (2012) · Free Radical Research · doi:10.3109/10715762.2012.667566 · Cited by 175 · see citing works
Self-citationChi, B. K., Gronau, K., Mäder, U., Heßling, B., Becher, D., & Antelmann, H. (2011) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m111.009506 · Cited by 169 · see citing works
Andrés, C. M. C., Pérez de la Lastra, J. M., Juan, C. A., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810735 · Cited by 166 · see citing works
Siraki, A. G. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102109 · Cited by 150 · see citing works
Molecular Magnetic Resonance Imaging Using a Redox-Active Iron Complex
Wang, H., Jordan, V. C., Ramsay, I. A., Sojoodi, M., Fuchs, B. C., Tanabe, K. K., Caravan, P. D., & Gale, E. M. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b00603 · Cited by 144 · see citing works
The Role of Reactive Species on Innate Immunity
Andrés, C., Pérez de la Lastra, J., Juan, C., Plou, F., & Pérez-Lebeña, E. (2022) · Vaccines · doi:10.3390/vaccines10101735 · Cited by 142 · see citing works
Do antioxidants impair signaling by reactive oxygen species and lipid oxidation products?
Niki, E. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.09.025 · Cited by 138 · see citing works
Zhang, Y., He, S., Bonneil, É., & Simpson, B. K. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125581 · Cited by 135 · see citing works
Low zinc and selenium concentrations in sepsis are associated with oxidative damage and inflammation
Mertens, K., Lowes, D. A., Webster, N. R., Talib, J., Hall, L., Davies, M. J., Beattie, J. H., & Galley, H. F. (2015) · British Journal of Anaesthesia · doi:10.1093/bja/aev073 · Cited by 132 · see citing works
Self-citationSaha, P., Yeoh, B. S., Singh, R., Chandrasekar, B., Vemula, P. K., Haribabu, B., Vijay‐Kumar, M., & Jala, V. R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156811 · Cited by 121 · see citing works
Zhang, S., Li, K., Hu, S., Hu, J., Fù, Y., Hu, Y., & Yang, X. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.117 · Cited by 124 · see citing works
Houée-Lévin, C., Bobrowski, K., Horakova, L., Karademir, B., Schöneich, C., Davies, M. J., & Spickett, C. M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1007968 · Cited by 126 · see citing works
Self-citationESIPT-based fluorescence probe for the rapid detection of hypochlorite (HOCl/ClO − )
Wu, L., Yang, Q., Liu, L., Sedgwick, A. C., Cresswell, A. J., Bull, S. D., Huang, C., & James, T. D. (2018) · Chemical Communications · doi:10.1039/c8cc03717e · Cited by 122 · see citing works
The Role of Bacillithiol in Gram-Positive <i>Firmicutes</i>
Chandrangsu, P., Loi, V. V., Antelmann, H., & Helmann, J. D. (2018) · Antioxidants & Redox Signaling · doi:10.1089/ars.2017.7057 · Cited by 120 · see citing works
Davies, M. J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107685 · Cited by 119 · see citing works
Self-citationA highly selective fluorescent probe for hypochlorite and its endogenous imaging in living cells
Reja, S. I., Bhalla, V., Sharma, A., Kaur, G., & Kumar, M. (2014) · Chemical Communications · doi:10.1039/c4cc05356g · Cited by 115 · see citing works
Uremic Toxins and Their Relation with Oxidative Stress Induced in Patients with CKD
Pieniążek, A., Bernasinska-Slomczewska, J., & Gwoździński, Ł. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126196 · Cited by 116 · see citing works
Kratzer, A., Giral, H., & Landmesser, U. (2014) · Cardiovascular Research · doi:10.1093/cvr/cvu139 · Cited by 109 · see citing works
Evidence for beneficial effects of vitamin E
Niki, E. (2015) · The Korean Journal of Internal Medicine · doi:10.3904/kjim.2015.30.5.571 · Cited by 108 · see citing works
Low-Density Lipoprotein Modified by Myeloperoxidase in Inflammatory Pathways and Clinical Studies
Delporte, C., Antwerpen, P. V., Vanhamme, L., Roumeguère, T., & Boudjeltia, K. Z. (2013) · Mediators of Inflammation · doi:10.1155/2013/971579 · Cited by 108 · see citing works
Identification and molecular docking of antioxidant peptides from hemp seed protein hydrolysates
Gao, J., Li, T., Chen, D., Gu, H., & Mao, X. (2021) · LWT · doi:10.1016/j.lwt.2021.111453 · Cited by 106 · see citing works
Role of Myeloperoxidase in Patients with Chronic Kidney Disease
Kisić, B., Miric, D. J., Dragojević, I. M., Rašić, J., & Popović, L. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/1069743 · Cited by 101 · see citing works
Cysteine-mediated redox signalling in the mitochondria
Bak, D. W., & Weerapana, E. (2014) · Molecular BioSystems · doi:10.1039/c4mb00571f · Cited by 100 · see citing works
Han, J., Liu, X., Xiong, H., Wang, J., Wang, B., Song, X., & Wang, W. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05604 · Cited by 96 · see citing works
Vanadium in Biosphere and Its Role in Biological Processes
Tripathi, D., Mani, V., & Pal, R. P. (2018) · Biological Trace Element Research · doi:10.1007/s12011-018-1289-y · Cited by 93 · see citing works
Myeloperoxidase As a Multifaceted Target for Cardiovascular Protection
Ramachandra, C. J. A., Ja, K. P. M. M., Chua, J., Cong, S., SHIM, W. S. N., & Hausenloy, D. J. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7971 · Cited by 94 · see citing works
Kato, Y. (2016) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.15-104 · Cited by 89 · see citing works
Plasma iron controls neutrophil production and function
Frost, J. N., Wideman, S. K., Preston, A. E., Teh, M. R., Ai, Z., Wang, L., Cross, A. R., White, N., Yazicioglu, Y. F., Bonadonna, M., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq5384 · Cited by 88 · see citing works
Khanh, B., Roberts, A. A., Huyền, T. T. T., Bäsell, K., Becher, D., Albrecht, D., Hamilton, C. J., & Antelmann, H. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4686 · Cited by 87 · see citing works
OSBP-Related Protein Family in Lipid Transport over Membrane Contact Sites
Olkkonen, V. M. (2015) · Lipid Insights · doi:10.4137/lpi.s31726 · Cited by 85 · see citing works
Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid
Sultana, S., Foti, A., & Dahl, J. (2020) · Infection and Immunity · doi:10.1128/iai.00964-19 · Cited by 76 · see citing works
Immunomodulatory Role of Urolithin A on Metabolic Diseases
Toney, A. M., Fox, D., Chaidez, V., Ramer‐Tait, A. E., & Chung, S. (2021) · Biomedicines · doi:10.3390/biomedicines9020192 · Cited by 79 · see citing works
A cafeteria diet triggers intestinal inflammation and oxidative stress in obese rats
Gil‐Cardoso, K., Ginés, I., Pinent, M., Ardèvol, A., Terra, X., & Blay, M. (2017) · British Journal Of Nutrition · doi:10.1017/s0007114516004608 · Cited by 75 · see citing works
Madrigal‐Matute, J., Martínez-Pinna, R., Ramos‐Mozo, P., Blanco‐Colio, L. M., Moreno, J. A., Tarín, C., Burillo, E., Fernandez‐Garcia, C. E., Egido, J., Meilhac, O., et al. (2012) · Thrombosis and Haemostasis · doi:10.1160/th12-04-0248 · Cited by 74 · see citing works
Oxidative Stress and Microvessel Barrier Dysfunction
He, P., Talukder, M. A. H., & Gao, F. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00472 · Cited by 75 · see citing works
Díaz‐Garrido, N., Cordero, C., Olivo-Martínez, Y., Badı́a, J., & Baldomà, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042213 · Cited by 74 · see citing works
Morais, L. H., Hara, D. B., Bicca, M. A., Poli, A., & Takahashi, R. N. (2018) · Behavioural Pharmacology · doi:10.1097/fbp.0000000000000389 · Cited by 58 · see citing works
The development of myeloperoxidase inhibitors
Galijašević, S. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.11.031 · Cited by 70 · see citing works
Bao, X., Cao, X., Yuan, Y. C., Zhou, B., & Huo, C. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.130210 · Cited by 69 · see citing works
Impact of Reactive Species on Amino Acids—Biological Relevance in Proteins and Induced Pathologies
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214049 · Cited by 71 · see citing works
Lung extracellular matrix and redox regulation
Watson, W. H., Ritzenthaler, J. D., & Roman, J. (2016) · Redox Biology · doi:10.1016/j.redox.2016.02.005 · Cited by 69 · see citing works
Extracellular Vesicles with Possible Roles in Gut Intestinal Tract Homeostasis and IBD
Chang, X., Wang, S., Zhao, S., Shi, Y., Pan, P., Gu, L., Yao, J., Li, Z., & Bai, Y. (2020) · Mediators of Inflammation · doi:10.1155/2020/1945832 · Cited by 68 · see citing works
Kumaravel, S., Balamurugan, T. S. T., Jia, S.-H., Lin, H., & Huang, S. (2020) · Analytica Chimica Acta · doi:10.1016/j.aca.2020.01.065 · Cited by 68 · see citing works
Interactions of reactive sulfur species with metalloproteins
Domán, A., Dóka, É., Garai, D., Bogdándi, V., Balla, G., Balla, J., & Nagy, P. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102617 · Cited by 67 · see citing works
Pseudomonas aeruginosa defense systems against microbicidal oxidants
Groitl, B., Dahl, J., Schroeder, J. W., & Jakob, U. (2017) · Molecular Microbiology · doi:10.1111/mmi.13768 · Cited by 67 · see citing works
Yazıcı, C., Köse, K., Utaş, S., Tanrıkulu, E., & Taşlıdere, N. (2016) · Archives of Dermatological Research · doi:10.1007/s00403-016-1624-0 · Cited by 66 · see citing works
Schroder, A. L., Chami, B., Liu, Y., Doyle, C. M., Kazzi, M. E., Ahlenstiel, G., Ahmad, G., Pathma‐Nathan, N., Collins, G. P., Toh, J. W. T., et al. (2021) · Inflammatory Bowel Diseases · doi:10.1093/ibd/izab239 · Cited by 68 · see citing works
Chang, C. Y., Choi, D., Lee, D., Hong, Y. J., & Park, E. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060654 · Cited by 65 · see citing works
Mechanisms and consequences of oxidative damage to extracellular matrix
Kennett, E. C., Chuang, C. Y., Degendorfer, G., Whitelock, J. M., & Davies, M. J. (2011) · Biochemical Society Transactions · doi:10.1042/bst0391279 · Cited by 61 · see citing works
Self-citationImber, M., Huyền, N. T. T., Pietrzyk‐Brzezinska, A. J., Loi, V. V., Hillion, M., Bernhardt, J., Thärichen, L., Kolšek, K., Saleh, M., Hamilton, C. J., et al. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6897 · Cited by 60 · see citing works
Jiang, Y., Zheng, G., Duan, Q., Yang, L., Zhang, J., Zhang, H., He, J. H., Sun, H., & Ho, D. L. (2018) · Chemical Communications · doi:10.1039/c8cc03963a · Cited by 59 · see citing works
Structural insights into the redox-switch mechanism of the MarR/DUF24-type regulator HypR
Palm, G. J., Chi, B. K., Waack, P., Gronau, K., Becher, D., Albrecht, D., Hinrichs, W., Read, R. J., & Antelmann, H. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1316 · Cited by 59 · see citing works
Potential of levitated drops to serve as microreactors for biophysical measurements
Scheeline, A., & Behrens, R. L. (2012) · Biophysical Chemistry · doi:10.1016/j.bpc.2012.03.008 · Cited by 58 · see citing works
Ruggeri, R. B., Buckbinder, L., Bagley, S. W., Carpino, P. A., Conn, E. L., Dowling, M., Fernando, D. P., Jiao, W., Kung, D. W., Orr, S. T. M., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00963 · Cited by 58 · see citing works
Oxidation and modification of extracellular matrix and its role in disease
Chuang, C. Y., Degendorfer, G., & Davies, M. J. (2014) · Free Radical Research · doi:10.3109/10715762.2014.920087 · Cited by 57 · see citing works
Self-citationCook, N. L., Viola, H. M., Sharov, V. S., Hool, L. C., Schöneich, C., & Davies, M. J. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.001 · Cited by 56 · see citing works
Self-citationZhang, M., Ma, Y., Li, P., Jia, Y., & Han, K. (2020) · Chemical Communications · doi:10.1039/d0cc00090f · Cited by 56 · see citing works
Schrijver, I. T., Kemperman, H., Roest, M., Kesecioğlu, J., & de Lange, D. W. (2017) · Intensive Care Medicine Experimental · doi:10.1186/s40635-017-0157-y · Cited by 55 · see citing works
Jia, M., Mi, W., Guo, S., Yang, Q., Jin, Y., & Shao, N. (2020) · Talanta · doi:10.1016/j.talanta.2020.120926 · Cited by 55 · see citing works
Acute organ injury and long-term sequelae of severe pneumococcal infections
Kruckow, K. L., Zhao, K., Bowdish, D. M. E., & Orihuela, C. J. (2023) · Pneumonia · doi:10.1186/s41479-023-00110-y · Cited by 54 · see citing works
Malecki, C., Hambly, B. D., Jeremy, R., & Robertson, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207678 · Cited by 53 · see citing works
Goswami, S., Aich, K., Das, S., Pakhira, B., Ghoshal, K., Quah, C. K., Bhattacharyya, M., Fun, H., & Sarkar, S. (2015) · Chemistry - An Asian Journal · doi:10.1002/asia.201403234 · Cited by 52 · see citing works
Suspène, R., Aynaud, M.-M., Vartanian, J., & Wain–Hobson, S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063461 · Cited by 52 · see citing works
Thiol-based redox switches in the major pathogen Staphylococcus aureus
Linzner, N., Loi, V. V., Fritsch, V. N., & Antelmann, H. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0272 · Cited by 52 · see citing works
Kazzi, M. E., Rayner, B. S., Chami, B., Dennis, J. M., Thomas, S. R., & Witting, P. K. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7928 · Cited by 51 · see citing works
Detection of atherosclerosis-associated HOCl using a mitochondria-targeted fluorescent probe
Wang, B., Yuan, F., Wang, S., Duan, R., Ren, W. X., & Hou, J. (2021) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2021.130695 · Cited by 50 · see citing works
Talib, J., Pattison, D. I., Harmer, J. A., Celermajer, D. S., & Davies, M. J. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.04.018 · Cited by 49 · see citing works
Self-citationChen, F., Wang, H., Zhao, J., Yan, J., Meng, H., Zhan, H., Chen, L., & Yuan, L. (2019) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2019.01.013 · Cited by 48 · see citing works
Salt, chloride, bleach, and innate host defense
Wang, G., & Nauseef, W. M. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.4ru0315-109r · Cited by 47 · see citing works
Pizzi, A., Pigliacelli, C., Bergamaschi, G., Gori, A., & Metrangolo, P. (2020) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2020.213242 · Cited by 47 · see citing works
Pulli, B., Buré, L., Wojtkiewicz, G. R., Iwamoto, Y., Ali, M. Y. J., Li, D., Schob, S., Hsieh, K. L., Jacobs, A. H., & Chen, J. W. (2014) · Radiology · doi:10.1148/radiol.14141495 · Cited by 47 · see citing works
Owumi, S. E., & Dim, U. J. (2019) · Toxicology Research and Application · doi:10.1177/2397847319874359 · Cited by 46 · see citing works
The lipid peroxidation product EKODE exacerbates colonic inflammation and colon tumorigenesis
Lei, L., Yang, J., Zhang, J., & Zhang, G. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101880 · Cited by 46 · see citing works
Jiang, Y., Zheng, G., Cai, N., Zhang, H., Tan, Y., Huang, M., He, Y., He, J. H., & Sun, H. (2017) · Chemical Communications · doi:10.1039/c7cc07373a · Cited by 45 · see citing works
- Authors
- Davies, M. J.
- Affiliations
- The University of Sydney (AU)
- Corresponding author
- Davies, Michael J.
- ORCID
- Davies, Michael J.
- Venue
- Journal of Clinical Biochemistry and Nutrition
- Published
- 2010
- Volume
- 48
- Issue
- 1
- Pages
- 8-19
- ISSN
- 0912-0009 (ISSN-L)
- 1880-5086
- PMC
- PMC3022070
- OpenAlex
- W2028031080
- Cited by
- 412
- References
- 227
- Citations by year
- 2026: 18 · 2025: 15 · 2024: 31 · 2023: 30 · 2022: 34 · 2021: 40 · 2020: 41 · 2019: 37 · 2018: 27 · 2017: 29 · 2016: 23 · 2015: 21 · 2014: 19 · 2013: 16 · 2012: 24
- FWCI
- 6.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Biochemistry and Nutrition (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Fondation pour la Recherche Médicale
- Medical Research Council
- Australian Research Council (CE0561607, DP0988311)
- National Health and Medical Research Council (570829)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- myeloperoxidase, heme peroxidase, eosinophil peroxidase, lactoperoxidase, oxidative damage, oxidative damage biomarkers, enzyme inhibitors
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