Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Abstract
Significance: When neutrophils kill microorganisms, they ingest them into phagosomes and bombard them with a burst of reactive oxygen species. Recent Advances: This review focuses on what oxidants are produced and how they kill. The neutrophil NADPH oxidase is activated and shuttles electrons from NADPH in the cytoplasm to oxygen in the phagosomal lumen. Superoxide is generated in the narrow space between the ingested organism and the phagosomal membrane and kinetic modeling indicates that it reaches a concentration of around 20 μ M . Degranulation leads to a very high protein concentration with up to millimolar myeloperoxidase (MPO). MPO has many substrates, but its main phagosomal reactions should be to dismutate superoxide and, provided adequate chloride, catalyze efficient conversion of hydrogen peroxide to hypochlorous acid (HOCl). Studies with specific probes have shown that HOCl is produced in the phagosome and reacts with ingested bacteria. The amount generated should be high enough to kill. However, much of the HOCl reacts with phagosomal proteins. Generation of chloramines may contribute to killing, but the full consequences of this are not yet clear. Critical Issues: Isolated neutrophils kill most of the ingested microorganisms rapidly by an MPO-dependent mechanism that is almost certainly due to HOCl. However, individuals with MPO deficiency rarely have problems with infection. A possible explanation is that HOCl provides a frontline response that kills most of the microorganisms, with survivors killed by nonoxidative processes. The latter may deal adequately with low-level infection but with high exposure, more efficient HOCl-dependent killing is required. Future Directions: Better quantification of HOCl and other oxidants in the phagosome should clarify their roles in antimicrobial action. Antioxid. Redox Signal. 18, 642–660.
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Dinitrogen trioxide (N2O3) is a strong nitrosating species also formed in the oxidation of NO.
“Dinitrogen trioxide (N2O3) is a strong nitrosating species also formed in the oxidation of NO (Eq. 29) (691, 692, 1018).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1018]
Nitrogen dioxide (NO2·) is formed in the reaction of NO with oxygen.
“Nitrogen dioxide (NO2·) is formed in the reaction of NO with oxygen (Eq. 28) (509, 1018).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [1018]
Generation of oxidative stress in pathogen-containing phagosomes of phagocytes is a crucial component of antimicrobial immunity.
“Generation of oxidative stress in pathogen-containing phagosomes of phagocytes, for example, is a crucial component of antimicrobial immunity [58,61,79].”
From Functions of ROS in Macrophages and Antimicrobial Immunity (2021) · cites this paper as [79]
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
Neutrophil Extracellular Traps Kill Bacteria
Brinkmann, V., Reichard, U., Goosmann, C., Fauler, B., Uhlemann, Y., Weiss, D. S., Weinrauch, Y., & Zychlinsky, A. (2004) · Science · doi:10.1126/science.1092385 · Cited by 10,268 · see citing works
Free Radicals in Biology and Medicine
Halliwell, B., & Gutteridge, J. M. C. (2015) · doi:10.1093/acprof:oso/9780198717478.001.0001 · Cited by 8,990 · see citing works
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989 · see citing works
NOX enzymes and the biology of reactive oxygen
Lambeth, J. D. (2004) · Nature Reviews Immunology · doi:10.1038/nri1312 · Cited by 3,125 · see citing works
Neutrophils and immunity: challenges and opportunities
Nathan, C. (2006) · Nature reviews. Immunology · doi:10.1038/nri1785 · Cited by 2,971 · see citing works
Babior, B. M., Kipnes, R. S., & Curnutte, J. T. (1973) · Journal of Clinical Investigation · doi:10.1172/jci107236 · Cited by 2,931 · see citing works
Reconciling the chemistry and biology of reactive oxygen species
Winterbourn, C. C. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.85 · Cited by 2,504 · see citing works
Self-citationMyeloperoxidase: friend and foe
Klebanoff, S. J. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.1204697 · Cited by 2,282 · see citing works
Imlay, J. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090938 · Cited by 2,206 · see citing works
Segal, A. W. (2005) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115653 · Cited by 1,783 · see citing works
Chronic Granulomatous Disease: Report on a National Registry of 368 Patients
Winkelstein, J. A., Marino, M. C., Johnston, R. B., Boyle, J., Curnutte, J., Gallin, J. I., Malech, H. L., Holland, S. M., Ochs, H., Quie, P., et al. (2000) · Medicine · doi:10.1097/00005792-200005000-00003 · Cited by 1,728 · see citing works
Antimicrobial reactive oxygen and nitrogen species: concepts and controversies
Fang, F. C. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro1004 · Cited by 1,676 · see citing works
Inside the Neutrophil Phagosome: Oxidants, Myeloperoxidase, and Bacterial Killing
Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1998) · Blood · doi:10.1182/blood.v92.9.3007.421k47_3007_3017 · Cited by 1,640 · see citing works
Self-citationGlucose-6-phosphate dehydrogenase deficiency
Cappellini, M., & Fiorelli, G. (2008) · The Lancet · doi:10.1016/s0140-6736(08)60073-2 · Cited by 1,590 · see citing works
Cellular Defenses against Superoxide and Hydrogen Peroxide
Imlay, J. A. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061606.161055 · Cited by 1,563 · see citing works
Savill, J. S., Wyllie, A. H., Henson, J. E., Walport, M. J., Henson, P. M., & Haslett, C. (1989) · Journal of Clinical Investigation · doi:10.1172/jci113970 · Cited by 1,536 · see citing works
Granules of the Human Neutrophilic Polymorphonuclear Leukocyte
Borregaard, N., & Cowland, J. B. (1997) · Blood · doi:10.1182/blood.v89.10.3503 · Cited by 1,514 · see citing works
Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., & van der Vliet, A. (1998) · Nature · doi:10.1038/34923 · Cited by 1,496 · see citing works
Sawyer, D. T., & Valentine, J. S. (1981) · Accounts of Chemical Research · doi:10.1021/ar00072a005 · Cited by 1,352 · see citing works
Killing activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153 · see citing works
Ischiropoulos, H. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0755 · Cited by 1,024 · see citing works
Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
Urban, C. F., Reichard, U., Brinkmann, V., & Zychlinsky, A. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00659.x · Cited by 1,014 · see citing works
Allen, R. C., STJERNHOLM, R. L., & Steele, R. H. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90545-1 · Cited by 960 · see citing works
Genetic, Biochemical, and Clinical Features of Chronic Granulomatous Disease
Segal, B. H., Leto, T. L., Gallin, J. I., Malech, H. L., & Holland, S. M. (2000) · Medicine · doi:10.1097/00005792-200005000-00004 · Cited by 877 · see citing works
Nox proteins in signal transduction
Brown, D. I., & Griendling, K. (2009) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2009.07.023 · Cited by 841 · see citing works
Chlorination of Taurine by Human Neutrophils
Weiss, S. J., Klein, R., Slivka, A., & Wei, M. L. (1982) · Journal of Clinical Investigation · doi:10.1172/jci110652 · Cited by 806 · see citing works
Pattison, D. I., & Davies, M. J. (2001) · Chemical Research in Toxicology · doi:10.1021/tx0155451 · Cited by 790 · see citing works
Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
Ferrer-Sueta, G., & Radi, R. (2009) · ACS Chemical Biology · doi:10.1021/cb800279q · Cited by 776 · cited 1× · see citing works
“Generation of NO by neutrophils opens up a rich panoply of chemistry that could be used to kill bacteria (58, 60).”
How human neutrophils kill and degrade microbes: an integrated view
Nauseef, W. M. (2007) · Immunological Reviews · doi:10.1111/j.1600-065x.2007.00550.x · Cited by 756 · 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
Self-citationRoot, R. K., Metcalf, J. A., Oshino, N., & Chance, B. (1975) · Journal of Clinical Investigation · doi:10.1172/jci108024 · Cited by 646 · 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
Self-citationInflammation: Basic Principles and Clinical Correlates
Ehrlich, G. E. (2000) · JAMA · doi:10.1001/jama.283.1.123 · Cited by 624 · see citing works
Koide, Y., Urano, Y., Hanaoka, K., Terai, T., & Nagano, T. (2011) · Journal of the American Chemical Society · doi:10.1021/ja111470n · Cited by 576 · see citing works
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 556 · see citing works
A Cholesterol Biosynthesis Inhibitor Blocks <i>Staphylococcus aureus</i> Virulence
Liu, C.-I., Liu, G. Y., Song, Y., Yin, F., Hensler, M. E., Jeng, W.-Y., Nizet, V., Wang, A. H.-J., & Oldfield, E. (2008) · Science · doi:10.1126/science.1153018 · Cited by 490 · see citing works
Heinecke, J. W., Li, W., Daehnke, H. L., & Goldstein, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53581-x · Cited by 485 · see citing works
Free radicals and phagocytic cells
Rosen, G. M., Pou, S., Ramos, C. L., Cohen, M. S., & Britigan, B. E. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.2.7540156 · Cited by 478 · 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
Self-citationKenmoku, S., Urano, Y., Kojima, H., & Nagano, T. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068740g · Cited by 462 · see citing works
Formation of Nitrating and Chlorinating Species by Reaction of Nitrite with Hypochlorous Acid
Eiserich, J. P., Cross, C. E., Jones, A. D., Halliwell, B., & van der Vliet, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19199 · Cited by 447 · see citing works
Albrich, J. M., McCarthy, C. A., & Hurst, J. K. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.210 · Cited by 442 · see citing works
The respiratory burst of phagocytic cells is associated with a rise in vacuolar pH
Segal, A. W., Geisow, M. J., Garcia, R. C., Harper, A., & Miller, R. F. (1981) · Nature · doi:10.1038/290406a0 · Cited by 422 · 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
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
Biomarkers of myeloperoxidase-derived hypochlorous acid
Winterbourn, C. C., & Kettle, A. J. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00204-5 · Cited by 390 · see citing works
Self-citationFiedler, 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
Sheppard, F. R., Kelher, M. R., Moore, E. E., McLaughlin, N. J. D., Banerjee, A. M., & Silliman, C. C. (2005) · Journal of Leukocyte Biology · doi:10.1189/jlb.0804442 · Cited by 374 · see citing works
Permeation of the erythrocyte stroma by superoxide radical
Lynch, R. E., & Fridovich, I. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30446-5 · Cited by 370 · see citing works
Morgenstern, D. E., Gifford, M. A. C., Li, L. L., Doerschuk, C. M., & Dinauer, M. C. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.2.207 · Cited by 370 · see citing works
Imlay, J. A., & Linn, S. (1986) · Journal of Bacteriology · doi:10.1128/jb.166.2.519-527.1986 · Cited by 361 · see citing works
(2012) · SpringerReference · doi:10.1007/springerreference_172807 · Cited by 360 · see citing works
Pattison, D. I., & Davies, M. J. (2006) · Current Medicinal Chemistry · doi:10.2174/092986706778773095 · Cited by 359 · see citing works
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 · see citing works
Evidence for Antibody-Catalyzed Ozone Formation in Bacterial Killing and Inflammation
Wentworth, P., McDunn, J. E., Wentworth, A. D., Takeuchi, C., Nieva, J. J., Jones, T., Bautista, C., Ruedi, J. M., Gutierrez, A., Janda, K. D., et al. (2002) · Science · doi:10.1126/science.1077642 · Cited by 349 · 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
Myeloperoxidase: Contribution to the Microbicidal Activity of Intact Leukocytes
Klebanoff, S. J. (1970) · Science · doi:10.1126/science.169.3950.1095 · Cited by 347 · see citing works
Targeting and Regulation of Reactive Oxygen Species Generation by Nox Family NADPH Oxidases
Leto, T. L., Morand, S. C., Hurt, D. E., & Ueyama, T. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2637 · Cited by 343 · see citing works
Parker, H. A., Albrett, A. M., Kettle, A. J., & Winterbourn, C. C. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.0711387 · Cited by 342 · see citing works
Self-citationKasahara, Y., Iwai, K., Yachie, A., Ohta, K., Konno, A., Seki, H., Miyawaki, T., & Taniguchi, N. (1997) · Blood · doi:10.1182/blood.v89.5.1748 · Cited by 339 · see citing works
Mechanisms of chlorine oxidation of hydrogen peroxide
Held, A. M., Halko, D. J., & Hurst, J. K. (1978) · Journal of the American Chemical Society · doi:10.1021/ja00486a025 · Cited by 339 · see citing works
Peskin, A. V., & Winterbourn, C. C. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00506-2 · Cited by 338 · see citing works
Self-citationDEGRANULATION OF POLYMORPHONUCLEAR LEUCOCYTES FOLLOWING PHAGOCYTOSIS OF MICROORGANISMS
Hirsch, J. G., & Cohn, Z. A. (1960) · The Journal of Experimental Medicine · doi:10.1084/jem.112.6.1005 · Cited by 335 · see citing works
Chlorination of Tyrosyl Residues in Peptides by Myeloperoxidase and Human Neutrophils
Domigan, N. M., Charlton, T. S., Duncan, M. W., Winterbourn, C. C., & Kettle, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16542 · Cited by 329 · see citing works
Self-citationNADPH Oxidase Activation and Assembly During Phagocytosis
DeLeo, F. R., Allen, L. H., Apicella, M. A., & Nauseef, W. M. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.12.6732 · Cited by 313 · see citing works
Evans, T. J., Buttery, L. D. K., Carpenter, A., Springall, D. R., Polak, J. M., & Cohen, J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9553 · Cited by 311 · see citing works
Molecular basis of chronic granulomatous disease [see comments]
Rm, S., & Curnutte, J. T. (1991) · Blood · doi:10.1182/blood.v77.4.673.bloodjournal774673 · Cited by 298 · see citing works
Bacterial infection induces nitric oxide synthase in human neutrophils.
Wheeler, M. A., Smith, S. D., García‐Cardeña, G., Nathan, C., Weiss, R. M., & Sessa, W. C. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119121 · Cited by 296 · see citing works
Reaction of Myeloperoxidase Compound I with Chloride, Bromide, Iodide, and Thiocyanate
Furtmüller, P. G., Burner, U., & Obinger, C. (1998) · Biochemistry · doi:10.1021/bi9818772 · Cited by 290 · see citing works
HO <sub>2</sub> •: The Forgotten Radical
de Grey, A. D. N. J. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759672 · Cited by 279 · see citing works
Innate immunity turned inside-out: antimicrobial defense by phagocyte extracellular traps
von Köckritz‐Blickwede, M., & Nizet, V. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0481-0 · Cited by 270 · see citing works
CFTR Expression in Human Neutrophils and the Phagolysosomal Chlorination Defect in Cystic Fibrosis
Painter, R. G., Valentine, V. G., Lanson, N. A., et al. (2006) · Biochemistry · doi:10.1021/bi060490t · Cited by 269 · see citing works
Regulation and termination of NADPH oxidase activity
DeCoursey, T. E., & Ligeti, E. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5177-1 · Cited by 268 · see citing works
Antibody Catalysis of the Oxidation of Water
Wentworth, P., Jones, L. H., Wentworth, A. D., et al. (2001) · Science · doi:10.1126/science.1062722 · Cited by 267 · see citing works
Test, S. T., & Weiss, S. J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43674-x · Cited by 266 · see citing works
Singlet oxygen production by biological systems
Kanofsky, J. R. (1989) · Chemico-Biological Interactions · doi:10.1016/0009-2797(89)90059-8 · Cited by 259 · see citing works
Steinbeck, M. J., Khan, A. U., & Karnovsky, M. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42228-4 · Cited by 258 · see citing works
Ramsey, I. S., Ruchti, E., Kaczmarek, J. S., & Clapham, D. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902761106 · Cited by 255 · see citing works
Myeloperoxidase-dependent effect of amines on functions of isolated neutrophils.
Thomas, E. L., Grisham, M. B., & Jefferson, M. M. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110992 · 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
Chen, X., Lee, K.-A., Ha, E.-M., Lee, K. M., Seo, Y. Y., Choi, H. K., Kim, H. N., Kim, M. J., Cho, C.-S., Lee, S. Y., et al. (2011) · Chemical Communications · doi:10.1039/c1cc10589b · Cited by 246 · see citing works
Poole, L. B. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.09.006 · Cited by 246 · see citing works
Parry, M. F., ROOT, R. K., METCALF, J. A., DELANEY, K. K., KAPLOW, L. S., & RICHAR, W. J. (1981) · Annals of Internal Medicine · doi:10.7326/0003-4819-95-3-293 · Cited by 243 · see citing works
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 · see citing works
Ramos, C. L., Pou, S., Britigan, B. E., Cohen, M. S., & Rosen, G. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42443-x · Cited by 230 · see citing works
Hazen, S. L., Hsu, F. F., Duffin, K., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23080 · Cited by 221 · see citing works
Lancaster, J. R. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060061w · Cited by 219 · see citing works
Reactive oxygen species in phagocytic leukocytes
Robinson, J. M. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0461-4 · Cited by 216 · see citing works
Álvarez, M. N., Peluffo, G., Piacenza, L., & Radí, R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167247 · Cited by 216 · see citing works
Hampton, M. B., Kettle, A. J., & Winterbourn, C. C. (1996) · Infection and Immunity · doi:10.1128/iai.64.9.3512-3517.1996 · Cited by 213 · see citing works
Self-citationCandeias, L. P., Patel, K. B., Stratford, M. R. L., & Wardman, P. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80394-a · Cited by 212 · see citing works
Investigating antibody-catalyzed ozone generation by human neutrophils
BABIOR, B. M., Takeuchi, C., Ruedi, J. M., Gutierrez, A., & Wentworth, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0530251100 · Cited by 211 · see citing works
Antimicrobial polypeptides of human neutrophils
Lehrer, R., & Ganz, T. (1990) · Blood · doi:10.1182/blood.v76.11.2169.bloodjournal76112169 · Cited by 206 · see citing works
Reactions involving singlet oxygen and the superoxide anion
Koppenol, W. H. (1976) · Nature · doi:10.1038/262420a0 · Cited by 202 · see citing works
Chapman, A., Hampton, M. B., Senthilmohan, R., Winterbourn, C. C., & Kettle, A. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106134200 · Cited by 200 · see citing works
Self-citationIntracellular generation of superoxide by the phagocyte NADPH oxidase: How, where, and what for?
Bylund, J., Brown, K. L., Movitz, C., Dahlgren, C., & Karlsson, A. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.016 · Cited by 196 · see citing works
Isolation procedure and some properties of myeloperoxidase from human leucocytes
Bakkenist, A. R. J., Wever, R., Vulsma, T., Plat, H., & GELDER, B. F. V. (1978) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(78)90101-8 · Cited by 193 · see citing works
General mechanism for the bacterial toxicity of hypochlorous acid: abolition of ATP production
Barrette, W. C., Hannum, D. M., Wheeler, W. D., et al. (1989) · Biochemistry · doi:10.1021/bi00449a032 · Cited by 192 · see citing works
Effects of oxygen tension and pH on the respiratory burst of human neutrophils
Gabig, T., Bearman, S., & Babior, B. (1979) · Blood · doi:10.1182/blood.v53.6.1133.1133 · Cited by 190 · see citing works
Chemaly, A. E., Okochi, Y., Sasaki, M., Arnaudeau, S., Okamura, Y., & Demaurex, N. (2009) · The Journal of Experimental Medicine · doi:10.1084/jem.20091837 · Cited by 189 · see citing works
Determinants of the Phagosomal pH in Neutrophils
Jankowski, A. W., Scott, C. C., & Grinstein, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110059200 · Cited by 181 · see citing works
Gene Expression Profiling Provides Insight into the Pathophysiology of Chronic Granulomatous Disease
Kobayashi, S. D., Voyich, J. M., Braughton, K. R., Whitney, A. R., Nauseef, W. M., Malech, H. L., & DeLeo, F. R. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.1.636 · 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
Human Neutrophils Kill Streptococcus pneumoniae via Serine Proteases
Standish, A. J., & Weiser, J. N. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900688 · Cited by 174 · see citing works
Tiden, A. K., Sjögren, T., Svensson, M., Bernlind, A., Senthilmohan, R., Auchère, F., Norman, H. L., Markgren, P.-O., Gustavsson, S., Schmidt, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.266981 · Cited by 163 · see citing works
Self-citationGray, G. R., Stamatoyannopoulos, G., Naiman, S. C., Kliman, M. R., Klebanoff, S. J., Austin, T., Yoshida, A., & Robinson, G. C. F. (1973) · The Lancet · doi:10.1016/s0140-6736(73)92350-7 · Cited by 162 · see citing works
Dual role of phagocytic NADPH oxidase in bacterial killing
Rada, B., Geiszt, M., Káldi, K., Tímár, C. I., & Ligeti, E. (2004) · Blood · doi:10.1182/blood-2004-03-1005 · Cited by 161 · see citing works
Phagolysosomal pH of human neutrophils
Čech, P., & Lehrer, R. (1984) · Blood · doi:10.1182/blood.v63.1.88.88 · Cited by 156 · see citing works
Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils
Rosen, H., Klebanoff, S. J., Wang, Y., Brot, N., Heinecke, J. W., & Fu, X. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909464106 · Cited by 154 · 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
Winterbourn, C. C., Garcia, R. C., & Segal, A. W. (1985) · Biochemical Journal · doi:10.1042/bj2280583 · Cited by 153 · see citing works
Self-citationCharge compensation during the phagocyte respiratory burst
Murphy, R., & DeCoursey, T. E. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.01.005 · Cited by 151 · see citing works
Superoxide Converts Indigo Carmine to Isatin Sulfonic Acid
Kettle, A. J., Clark, B. M., & Winterbourn, C. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400334200 · Cited by 142 · see citing works
Self-citationAratani, Y., Kura, F., Watanabe, H., Akagawa, H., Takano, Y., Suzuki, K. T., Dinauer, M. C., Maeda, N., & Koyama, H. (2002) · Medical Mycology · doi:10.1080/mmy.40.6.557.563 · Cited by 142 · see citing works
Beaman, B. L., Black, C. M., Doughty, F. A., & Beaman, L. (1985) · Infection and Immunity · doi:10.1128/iai.47.1.135-141.1985 · Cited by 137 · see citing works
Marquez‐Curtis, L. A., Huang, J., & Dunford, H. B. (1994) · Biochemistry · doi:10.1021/bi00172a022 · Cited by 135 · see citing works
Borregaard, N., Schwartz, J. H., & Tauber, A. I. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111442 · Cited by 135 · see citing works
Urate as a Physiological Substrate for Myeloperoxidase
Meotti, F. C., Jameson, G. N. L., Turner, R., Harwood, D. T., Stockwell, S., Rees, M. D., Thomas, S. R., & Kettle, A. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172460 · Cited by 133 · see citing works
Self-citationHazen, S. L., Hsu, F., d'Avignon, A., & Heinecke, J. W. (1998) · Biochemistry · doi:10.1021/bi972449j · Cited by 133 · 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
Self-citationThomas, E. L., Jefferson, M. M., & Grisham, M. B. (1982) · Biochemistry · doi:10.1021/bi00267a040 · Cited by 128 · see citing works
CdSe-ZnS Quantum Dots for Selective and Sensitive Detection and Quantification of Hypochlorite
Yan, Y., Wang, S., Liu, Z., et al. (2010) · Analytical Chemistry · doi:10.1021/ac101929q · Cited by 128 · 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
What really happens in the neutrophil phagosome?
Hurst, J. K. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.05.008 · Cited by 124 · see citing works
Bergt, C., Fu, X., Saifee, N. H., Kao, J. L.-F., & Heinecke, J. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309046200 · 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
Lundqvist, H., Foilin, P., Khalfan, L., & Dahlgren, C. (1996) · Journal of Leukocyte Biology · doi:10.1002/jlb.59.2.270 · Cited by 121 · see citing works
Radical–radical reactions of superoxide: A potential route to toxicity
Winterbourn, C. C., & Kettle, A. J. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00810-6 · Cited by 118 · see citing works
Self-citationAratani, Y., Kura, F., Watanabe, H., Akagawa, H., Takano, Y., Suzuki, K. T., Maeda, N., & Koyama, H. (2000) · The Journal of Infectious Diseases · doi:10.1086/315843 · Cited by 116 · see citing works
Superoxide production by polymorphonuclear leukocytes
Briggs, R. T., Robinson, J. M., Karnovsky, M. J., & Karnovsky, M. J. (1986) · Histochemistry and Cell Biology · doi:10.1007/bf00482965 · Cited by 116 · see citing works
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 · see citing works
Fu, X., Mueller, D. M., & Heinecke, J. W. (2001) · Biochemistry · doi:10.1021/bi015777z · Cited by 107 · see citing works
Reeves, E. P., Nagl, M., Godovac‐Zimmermann, J., & Segal, A. W. (2003) · Journal of Medical Microbiology · doi:10.1099/jmm.0.05181-0 · Cited by 105 · see citing works
Reactive Oxygen Species Are Partially Involved in the Bacteriocidal Action of Hypochlorous Acid
Dukan, S., Belkin, S., & Touati, D. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1265 · Cited by 104 · 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
Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidase
Arnhold, J., Furtmüller, P. G., Regelsberger, G., & Obinger, C. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02449.x · Cited by 101 · see citing works
The NADPH oxidase complex of phagocytic leukocytes: a biochemical and cytochemical view
Robinson, J. M., & Badwey, J. A. (1995) · Histochemistry and Cell Biology · doi:10.1007/bf01454021 · Cited by 101 · see citing works
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 · see citing works
Self-citationKinetics of oxygen consumption by phagocytosing human neutrophils
Segal, A. W., & Coade, S. B. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90749-0 · Cited by 99 · see citing works
Baehner, R., Rb, J., & Nathan, D. (1972) · PubMed · Cited by 99 · see citing works
Voltage-Gated Proton Channels Find Their Dream Job Managing the Respiratory Burst in Phagocytes
DeCoursey, T. E. (2010) · Physiology · doi:10.1152/physiol.00039.2009 · Cited by 98 · see citing works
Superoxide Dismutase from Mycobacterium tuberculosis
Kusunose, E., Ichihara, K., Yojiro, N. O. D. A., et al. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131407 · Cited by 97 · see citing works
Regulation of Glycogen Metabolism in Polymorphonuclear Leukocytes
Stossel, T. P., Murad, F., Mason, R. J., et al. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62682-1 · Cited by 95 · see citing works
A 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
Self-citationCFTR-mediated halide transport in phagosomes of human neutrophils
Painter, R. G., Marrero, L., Lombard, G. A., Valentine, V. G., Nauseef, W. M., & Wang, G. (2010) · Journal of Leukocyte Biology · doi:10.1189/jlb.1009655 · 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
Self-citationFemling, J., Cherny, V. V., Morgan, D., Rada, B., Volk, A. P. D., Czirják, G., Enyedi, P., England, S. K., Moreland, J. G., Ligeti, E., et al. (2006) · The Journal of General Physiology · doi:10.1085/jgp.200609504 · Cited by 90 · see citing works
Jiang, Q., Griffin, D. A., Barofsky, D. F., & Hurst, J. K. (1997) · Chemical Research in Toxicology · doi:10.1021/tx9700984 · Cited by 89 · see citing works
Chronic Granulomatous Disease; fundamental stages in our understanding of CGD
Assari, T. (2006) · Medical Immunology · doi:10.1186/1476-9433-5-4 · Cited by 87 · see citing works
Schwartz, J., Leidal, K. G., Femling, J., Weiss, J. P., & Nauseef, W. M. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804110 · Cited by 86 · see citing works
Jiang, Q., & Hurst, J. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.52.32767 · Cited by 84 · see citing works
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 · see citing works
Self-citationNauseef, W. M. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0117-4 · Cited by 82 · 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
Self-citationChloride movements in human neutrophils. Diffusion, exchange, and active transport.
Simchowitz, L., & Weer, P. D. (1986) · The Journal of General Physiology · doi:10.1085/jgp.88.2.167 · Cited by 81 · see citing works
Hampton, M. B., Vissers, M. C. M., Keenan, J. I., & Winterbourn, C. C. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.71.5.775 · Cited by 81 · see citing works
Self-citationGinsburg, I., & Kohen, R. (1995) · Free Radical Research · doi:10.3109/10715769509150323 · Cited by 75 · see citing works
Brovkovych, V. M., Gao, X.-P., Ong, E., Brovkovych, S. D., Brennan, M., Su, X., Hazen, S. L., Malik, A. B., & Skidgel, R. A. (2008) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00450.2007 · Cited by 74 · see citing works
Neutrophils autoinactivate secretory products by myeloperoxidase- catalyzed oxidation
Clark, R. A., & Borregaard, N. (1985) · Blood · doi:10.1182/blood.v65.2.375.375 · Cited by 74 · see citing works
Oxygen, oxysterols, ouabain, and ozone: a cautionary tale
Smith, L. L. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.024 · Cited by 72 · see citing works
Vissers, M. C. M., & Winterbourn, C. C. (1987) · Biochemical Journal · doi:10.1042/bj2450277 · Cited by 72 · see citing works
Self-citationMyeloperoxidase-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
Self-citationGottardi, W., & Nagl, M. (2005) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dki054 · Cited by 70 · see citing works
Physiological production of singlet molecular oxygen in the myeloperoxidase‐H2O2‐chloride system
Kiryu, C., Makiuchi, M., Miyazaki, J., FUJINAGA, T., & Kakinuma, K. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01700-1 · Cited by 68 · see citing works
Baggiolini, M., & Dewald, B. (1984) · Springer eBooks · doi:10.1007/978-1-4757-4862-8_8 · Cited by 65 · see citing works
Zatti, M., & Rossi, F. (1965) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/s0926-6593(65)80213-2 · Cited by 64 · see citing works
Menegazzi, R., Busetto, S., Dri, P., Cramer, R., & Patriarca, P. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.2.511 · Cited by 64 · see citing works
NADPH oxidase is functionally assembled in specific granules during activation of human neutrophils
Vaissière, C., Cabec, V. L., & Maridonneau‐Parini, I. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.65.5.629 · Cited by 63 · see citing works
Molecular and Functional Characterization of Hv1 Proton Channel in Human Granulocytes
Petheö, G. L., Orient, A., Baráth, M., Kovács, I. A., Réthi, B., Lányi, Á., Rajki, A., Rajnavölgyi, É., & Geiszt, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014081 · Cited by 63 · see citing works
Electron transfer in the superoxide-generating NADPH oxidase complex reconstituted in vitro
Koshkin, V., Lotan, O., & Pick, E. (1997) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00154-5 · Cited by 61 · see citing works
Role of NADPH Oxidase versus Neutrophil Proteases in Antimicrobial Host Defense
Vethanayagam, R. R., Almyroudis, N. G., Grimm, M. J., Lewandowski, D. C., Pham, C. T. N., Blackwell, T. S., Petraitienė, R., Petraitis, V., Walsh, T. J., Urban, C. F., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028149 · Cited by 59 · see citing works
Myeloperoxidase Selectively Binds and Selectively Kills Microbes
Allen, R. C., & Stephens, J. T. (2010) · Infection and Immunity · doi:10.1128/iai.00910-09 · Cited by 59 · see citing works
Kettle, A. J., Sangster, D. F., Gebicki, J. M., & Winterbourn, C. C. (1988) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(88)90297-x · Cited by 58 · see citing works
Self-citationOxidation of Methionine to Dehydromethionine by Reactive Halogen Species Generated by Neutrophils
Peskin, A. V., Turner, R., Maghzal, G. J., Winterbourn, C. C., & Kettle, A. J. (2009) · Biochemistry · doi:10.1021/bi901266w · Cited by 58 · see citing works
Self-citationEnhanced 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
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 · see citing works
Self-citationXimenes, 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
Self-citationNagy, P., Kettle, A. J., & Winterbourn, C. C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809396200 · Cited by 53 · see citing works
Self-citationDirect Measurement of Free Chloride Concentrations in the Phagolysosomes of Human Neutrophils
Painter, R. G., & Wang, G. (2006) · Analytical Chemistry · doi:10.1021/ac0521706 · Cited by 53 · see citing works
Pathways for the Decay of Organic Dichloramines and Liberation of Antimicrobial Chloramine Gases
Coker, M. S. A., Hu, W., Senthilmohan, S. T., et al. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800232v · Cited by 49 · see citing works
Cytochemical demonstration of hydrogen peroxide in polymorphonuclear leukocyte phagosomes
Briggs, R., Karnovsky, M. L., & Mj, K. (1975) · The Journal of Cell Biology · doi:10.1083/jcb.64.1.254 · Cited by 49 · see citing works
Oxidation of Clozapine and Ascorbate by Myeloperoxidase
Hsuanyu, Y., & Dunford, H. B. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1328 · Cited by 49 · see citing works
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 · see citing works
Self-citationPalazzolo, A. M., Suquet, C., Konkel, M. E., & Hurst, J. K. (2005) · Biochemistry · doi:10.1021/bi047342s · Cited by 48 · see citing works
Electrophysiology of Reactive Oxygen Production in Signaling Endosomes
Lamb, F. S., Moreland, J. G., & Miller, F. J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2448 · Cited by 47 · see citing works
Kinetic analysis of phagosomal production of reactive oxygen species
Tlili, A., Dupré‐Crochet, S., Erard, M., & Nüße, O. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.11.024 · Cited by 46 · see citing works
Padgett, E. L., & Pruett, S. B. (1995) · PubMed · Cited by 43 · see citing works
Tomono, S., Miyoshi, N., Shiokawa, H., Iwabuchi, T., Aratani, Y., Higashi, T., Nukaya, H., & Ohshima, H. (2010) · Journal of Lipid Research · doi:10.1194/jlr.m006775 · Cited by 43 · see citing works
Interrogation of Heme Pocket Environment of Mammalian Peroxidases with Diatomic Ligands
Abu‐Soud, H. M., & Hazen, S. L. (2001) · Biochemistry · doi:10.1021/bi010478v · Cited by 42 · see citing works
Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA
Prado, F. M., de Oliveira, M. C. B., Miyamoto, S., Martinez, G. R., de Medeiros, M. H. G., Ronsein, G. E., & Mascio, P. D. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.001 · 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
Granfeldt, D., & Dahlgren, C. (2001) · Inflammation · doi:10.1023/a:1011084330283 · Cited by 39 · see citing works
Physiological roles of voltage-gated proton channels in leukocytes
Demaurex, N., & Chemaly, A. E. (2010) · The Journal of Physiology · doi:10.1113/jphysiol.2010.194225 · Cited by 36 · see citing works
Beal, J. L., Foster, S. B., & Ashby, M. T. (2009) · Biochemistry · doi:10.1021/bi901343d · Cited by 36 · see citing works
Phagocyte‐derived reactive oxygen species as suppressors of inflammatory disease
Björkman, L. I., Dahlgren, C., Karlsson, A., Brown, K. L., & Bylund, J. (2008) · Arthritis & Rheumatism · doi:10.1002/art.23941 · Cited by 36 · see citing works
Busetto, S., Trevisan, E., Decleva, E., Dri, P., & Menegazzi, R. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.6.4110 · Cited by 35 · see citing works
Electron microscopic study of phagocytosis of Escherichia coli by human polymorphonuclear leukocytes
Rozenberg-Arska, M., Salters, M. E., van Strijp, J. A. G., et al. (1985) · Infection and Immunity · doi:10.1128/iai.50.3.852-859.1985 · Cited by 34 · see citing works
Gerber, C. E., Bruchelt, G., Falk, U. B., Kimpfler, A., Hauschild, O., Kuçi, S., Bächi, T., NIETHAMMER, D., & Schubert, R. (2001) · Blood · doi:10.1182/blood.v98.10.3097 · Cited by 32 · see citing works
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13 reasons why the brain is susceptible to oxidative stress
Cobley, J. N., Fiorello, M. L., & Bailey, D. M. (2018) · Redox Biology · doi:10.1016/j.redox.2018.01.008 · Cited by 1,215 · see citing works
Metzler, K. D., Goosmann, C., Lubojemska, A., Zychlinsky, A., & Papayannopoulos, V. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.06.044 · Cited by 741 · see citing works
Functions of ROS in Macrophages and Antimicrobial Immunity
Herb, M., & Schramm, M. (2021) · Antioxidants · doi:10.3390/antiox10020313 · Cited by 633 · see citing works
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541 · see citing works
Nox enzymes and new thinking on reactive oxygen: A double-edged sword revisited
Lambeth, J. D., & Neish, A. S. (2014) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012513-104651 · Cited by 495 · see citing works
The Role of Myeloperoxidase in Biomolecule Modification, Chronic Inflammation, and Disease
Davies, M. J., & Hawkins, C. L. (2020) · Antioxidants & Redox Signaling · doi:10.1089/ars.2020.8030 · Cited by 332 · 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
Abuaita, B. H., Schultz, T. L., & O’Riordan, M. X. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.10.005 · Cited by 223 · see citing works
Vitamin C: a novel regulator of neutrophil extracellular trap formation.
Mohammed, B., Fisher, B., Kraskauskas, D., Farkas, D., Brophy, D., Fowler, A., & Natarajan, R. (2013) · Nutrients · doi:10.3390/nu5083131 · Cited by 187 · see citing works
The phagocyte NOX2 NADPH oxidase in microbial killing and cell signaling
Nauseef, W. M. (2019) · Current Opinion in Immunology · doi:10.1016/j.coi.2019.05.006 · Cited by 188 · see citing works
Detection of superoxide anion and hydrogen peroxide production by cellular NADPH oxidases
Nauseef, W. M. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.040 · Cited by 180 · see citing works
Brown, G. C. (2024) · Nature Reviews Immunology · doi:10.1038/s41577-023-00921-6 · Cited by 129 · see citing works
Davies, M. J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107685 · Cited by 119 · see citing works
Topical hypochlorite ameliorates NF-κB–mediated skin diseases in mice
Leung, T. H., Zhang, L. F., Wang, J., Ning, S., Knox, S. J., & Kim, S. K. (2013) · Journal of Clinical Investigation · doi:10.1172/jci70895 · Cited by 107 · see citing works
Maitra, D., Shaeib, F., Abdulhamid, I., Abdulridha, R. M., Saed, G. M., Diamond, M. P., Pennathur, S., & Abu-Soud, H. M. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.009 · Cited by 64 · see citing works
Martínez, A., Prolo, C., Estrada, D., Rios, N., Alvarez, M. N., Piñeyro, M. D., Robello, C., Radi, R., & Piacenza, L. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821487116 · Cited by 41 · see citing works
Topical Hypochlorous Acid (HOCl) as a Potential Treatment of Pruritus
Pelgrift, R. Y., & Friedman, A. J. (2013) · Current Dermatology Reports · doi:10.1007/s13671-013-0052-z · Cited by 24 · see citing works
Serotonin as a Putative Scavenger of Hypohalous Acid in the Brain
Kalogiannis, M., Delikatny, E. J., & Jeitner, T. M. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.012 · Cited by 19 · see citing works
“The presence of this enzyme in neurodegenerative diseases may therefore reflect a crucial pathological transition, especially since HOCl is a powerful 2-electron oxidant [10].”
BackgroundTürkoğlu, O., Barış, N., Tervahartiala, T., Şenarslan, Ö., Sorsa, T., & Atilla, G. (2014) · Journal of Periodontology · doi:10.1902/jop.2013.130346 · Cited by 17 · see citing works
- Authors
- Winterbourn, C. C., & Kettle, A. J.
- Affiliations
- University of Otago (NZ)
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2013-02
- Volume
- 18
- Issue
- 6
- Pages
- 642-660
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W1980734840
- Cited by
- 468
- References
- 213
- Citations by year
- 2026: 23 · 2025: 20 · 2024: 22 · 2023: 36 · 2022: 39 · 2021: 36 · 2020: 56 · 2019: 33 · 2018: 45 · 2017: 22 · 2016: 33 · 2015: 31 · 2014: 37 · 2013: 32 · 2012: 3
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- 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
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
- Keywords
- microbial killing, reactive oxygen species, NADPH oxidase, superoxide, myeloperoxidase, hypochlorous acid, hydrogen peroxide, chloramines, kinetic modeling
- MeSH terms
- Anti-Bacterial Agents, Bacteria, Catalysis, Chlorides, Humans, Hydrogen Peroxide, Hypochlorous Acid, Kinetics, Neutrophils, Oxidation-Reduction, Oxygen, Phagocytosis, Phagosomes, Reactive Oxygen Species, NADPH Oxidases
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