Antimicrobial actions of dual oxidases and lactoperoxidase
Open accessAbstract
The NOX/DUOX family of NADPH oxidases are transmembrane proteins generating reactive oxygen species as their primary enzymatic products. NADPH oxidase (NOX) 1-5 and Dual oxidase (DUOX) 1 and 2 are members of this family. These enzymes have several biological functions including immune defense, hormone biosynthesis, fertilization, cell proliferation and differentiation, extracellular matrix formation and vascular regulation. They are found in a variety of tissues such as the airways, salivary glands, colon, thyroid gland and lymphoid organs. The discovery of NADPH oxidases has drastically transformed our view of the biology of reactive oxygen species and oxidative stress. Roles of several isoforms including DUOX1 and DUOX2 in host innate immune defense have been implicated and are still being uncovered. DUOX enzymes highly expressed in the respiratory and salivary gland epithelium have been proposed as the major sources of hydrogen peroxide supporting mucosal oxidative antimicrobial defenses. In this review, we shortly present data on DUOX discovery, structure and function, and provide a detailed, up-to-date summary of discoveries regarding antibacterial, antiviral, antifungal, and antiparasitic functions of DUOX enzymes. We also present all the literature describing the immune functions of lactoperoxidase, an enzyme working in partnership with DUOX to produce antimicrobial substances.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Salivary peroxidase and lactoperoxidase (LPO) are present in multiple human exocrine secretions, including tears, milk, saliva, and vaginal fluid, and serve anti-microbial killing actions similar to MPO.
“Other related hemoproteins include salivary peroxidase and lactoperoxidase (LPO) which are present in multiple human exocrine secretions, including tears, milk, saliva, and vaginal fluid, and also serves anti-microbial killing actions similar to MPO (Sarr et al., 2018).”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Sarr et al., 2018
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Aging: a theory based on free radical and radiation chemistry
Harman, D. (1956) · Journal of Gerontology · doi:10.1093/geronj/11.3.298 · Cited by 8,567 · 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
Oxyl radicals, redox-sensitive signalling cascades and antioxidants
Genestra, M. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.04.009 · Cited by 4,930 · see citing works
Reactive Oxygen Species in Inflammation and Tissue Injury
Mittal, M., Siddiqui, M. R., Tran, K., Reddy, S. P., & Malik, A. B. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.5149 · Cited by 4,897 · 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
Harman, D. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.11.7124 · Cited by 1,915 · 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
A tissue-scale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
Niethammer, P., Grabher, C., Look, A. T., & Mitchison, T. J. (2009) · Nature · doi:10.1038/nature08119 · Cited by 1,541 · see citing works
NADPH oxidases: An overview from structure to innate immunity-associated pathologies
Panday, A., Sahoo, M. K., Osorio, D., & Batra, S. (2015) · Cellular & Molecular Immunology · doi:10.1038/cmi.2014.89 · Cited by 944 · see citing works
A Direct Role for Dual Oxidase in Drosophila Gut Immunity
Ha, E.-M., Oh, C.-T., Bae, Y. S., & Lee, W. (2005) · Science · doi:10.1126/science.1117311 · Cited by 824 · see citing works
Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family
Deken, X. D., Wang, D., Many, M., Costagliola, S., Libert, F., Vassart, G., Dumont, J. E., & Miot, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000916200 · Cited by 639 · see citing works
Park, H. S., Jung, H. Y., Park, E. Y., Kim, J., Lee, W. J., & Bae, Y. S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.6.3589 · Cited by 635 · see citing works
Involvement of Reactive Oxygen Species in Toll-Like Receptor 4-Dependent Activation of NF-κB
Asehnoune, K., Strassheim, D., Mitra, S., Kim, J. Y., & Abraham, E. H. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.4.2522 · Cited by 562 · 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
Herpes simplex encephalitis: adolescents and adults.
Whitley, R. (2006) · Antiviral Research · doi:10.1016/j.antiviral.2006.04.002 · Cited by 532 · see citing works
Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense
Geiszt, M., Witta, J., Baff, J., Lekstrom, K. J., & Leto, T. L. (2003) · The FASEB Journal · doi:10.1096/fj.02-1104fje · Cited by 505 · 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
Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase
Dupuy, C., Ohayon, R., Valent, A., Noël‐Hudson, M., Dème, D., & Virion, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37265 · Cited by 464 · see citing works
Collins, P. L., & Melero, J. A. (2011) · Virus Research · doi:10.1016/j.virusres.2011.09.020 · Cited by 455 · see citing works
The Nox Family of NAD(P)H Oxidases: Host Defense and Beyond
Geiszt, M., & Leto, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400024200 · Cited by 452 · see citing works
Oxidative Innate Immune Defenses by Nox/Duox Family NADPH Oxidases
Rada, B., & Leto, T. L. (2008) · KARGER eBooks · doi:10.1159/000136357 · Cited by 449 · see citing works
Self-citationNADPH oxidases: not just for leukocytes anymore!
Bokoch, G., & Knaus, U. G. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00194-4 · Cited by 383 · see citing works
Edens, W. A., Sharling, L., Cheng, G., Shapira, R., Kinkade, J. M., Lee, T., Edens, H. A., Tang, X., Sullards, C., Flaherty, D. B., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200103132 · Cited by 375 · 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
Identification of the Maturation Factor for Dual Oxidase
Grasberger, H., & Refetoff, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600095200 · Cited by 333 · see citing works
A Peroxidase/Dual Oxidase System Modulates Midgut Epithelial Immunity in Anopheles gambiae
Kumar, S., Molina-Cruz, A., Gupta, L., Rodrigues, J., & Barillas-Mury, C. V. (2010) · Science · doi:10.1126/science.1184008 · Cited by 332 · see citing works
Ha, E.-M., Lee, K.-A., Seo, Y. Y., Kim, S.-H., Lim, J.-H., Oh, B., Kim, J., & Lee, W. (2009) · Nature Immunology · doi:10.1038/ni.1765 · Cited by 331 · see citing works
NOX family NADPH oxidases: Not just in mammals
Bedard, K., Lardy, B., & KRAUSE, K. (2007) · Biochimie · doi:10.1016/j.biochi.2007.01.012 · Cited by 321 · see citing works
Host resistance factors in human milk
Goldman, A. S., & Smith, C. W. (1973) · The Journal of Pediatrics · doi:10.1016/s0022-3476(73)80453-6 · Cited by 296 · see citing works
A Novel Host Defense System of Airways is Defective in Cystic Fibrosis
Moskwa, P., Lorentzen, D., Excoffon, K. J. D. A., Zabner, J., McCray, P. B., Nauseef, W. M., Dupuy, C., & Bánfi, B. (2006) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200607-1029oc · Cited by 277 · see citing works
Dual oxidase 1-dependent MUC5AC mucin expression in cultured human airway epithelial cells
Shao, M. X. G., & Nadel, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408932102 · Cited by 251 · see citing works
Dual Oxidase-2 Has an Intrinsic Ca2+-dependent H2O2-generating Activity
Ameziane-El-Hassani, R., Morand, S., Boucher, J.-L., Frapart, Y.-M., Apostolou, D., Agnandji, D., Gnidehou, S., Ohayon, R., Noël-Hudson, M.-S., Francon, J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500516200 · Cited by 248 · 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
van der Hoeven, R., McCallum, K. C., Cruz, M. R., & Garsin, D. A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002453 · Cited by 240 · see citing works
Regulated Hydrogen Peroxide Production by Duox in Human Airway Epithelial Cells
Forteza, R., Salathe, M. A., Miot, F., Forteza, R., & Conner, G. E. (2005) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0302oc · Cited by 240 · see citing works
Dual oxidase2 is expressed all along the digestive tract
Hassani, R. A. E., Benfares, N., Caillou, B., Talbot, M., Sabourin, J., Belotte, V., Morand, S. C., Gnidehou, S., Agnandji, D., Ohayon, R., et al. (2004) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00198.2004 · Cited by 234 · see citing works
Harper, R. W., Xu, C., Eiserich, J. P., Chen, Y., Kao, C., Thai, P., Setiadi, H., & Wu, R. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.08.002 · Cited by 231 · see citing works
Regulation of DUOX by the Gαq-Phospholipase Cβ-Ca2+ Pathway in Drosophila Gut Immunity
Ha, E.-M., Lee, K., Park, S. H., Kim, S., Nam, H.-J., Lee, H.-Y., Kang, D., & Lee, W. (2009) · Developmental Cell · doi:10.1016/j.devcel.2008.12.015 · Cited by 226 · see citing works
Physiological role of reactive oxygen species as promoters of natural defenses
Roy, J., Galano, J., Durand, T., Guennec, J. L., & Lee, J. C. (2017) · The FASEB Journal · doi:10.1096/fj.201700170r · Cited by 223 · see citing works
Lactoperoxidase and Human Airway Host Defense
Wijkstrom-Frei, C., El‐Chemaly, S., Ali-Rachedi, R., et al. (2003) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2002-0152oc · Cited by 214 · see citing works
Activation of Dual Oxidases Duox1 and Duox2
Rigutto, S., Hoste, C., Grasberger, H., Milenkovic, M., Communi, D., Dumont, J. E., Corvilain, B., Miot, F., & De Deken, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806893200 · Cited by 213 · see citing works
NADPH oxidases in lung biology and pathology: Host defense enzymes, and more
van der Vliet, A. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.11.016 · Cited by 201 · see citing works
Szántó, I., Rubbia‐Brandt, L., Kiss, P. J., Steger, K., Bánfi, B., Kövari, E., Herrmann, F. R., Hadengue, A., & Krause, K. (2005) · The Journal of Pathology · doi:10.1002/path.1824 · Cited by 199 · see citing works
DUOX2-derived reactive oxygen species are effectors of NOD2-mediated antibacterial responses
Lipinski, S., Till, A., Sina, C., Arlt, A., Grasberger, H., Schreiber, S., & Rosenstiel, P. C. (2009) · Journal of Cell Science · doi:10.1242/jcs.050690 · Cited by 196 · see citing works
The peroxidase-thiocyanate-hydrogen peroxide antimicrobial system
Klebanoff, S. J., Clem, W., & Luebke, R. G. (1966) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(66)90152-8 · Cited by 183 · see citing works
The Lactoperoxidase System Functions in Bacterial Clearance of Airways
Gerson, C., Sabater, J. R., Scuri, M., et al. (2000) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.22.6.3980 · Cited by 176 · see citing works
THIOCYANATE: A potentially useful therapeutic agent with host defense and antioxidant properties
Chandler, J. D., & Day, B. J. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.07.029 · Cited by 175 · see citing works
Morand, S. C., Ueyama, T., Tsujibe, S., Saito, N., Korzeniowska, A., & Leto, T. L. (2008) · The FASEB Journal · doi:10.1096/fj.08-120006 · Cited by 171 · see citing works
Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review
Bafort, F., Parisi, O., Perraudin, J. P., & Jijakli, M. H. (2014) · Enzyme Research · doi:10.1155/2014/517164 · Cited by 159 · see citing works
Thomas, E. L., Milligan, T. W., Joyner, R. E., & Jefferson, M. M. (1994) · Infection and Immunity · doi:10.1128/iai.62.2.529-535.1994 · Cited by 155 · see citing works
Björck, L., Rosén, C., Marshall, V. M., & Reiter, B. (1975) · Applied Microbiology · doi:10.1128/am.30.2.199-204.1975 · Cited by 152 · see citing works
Thomas, E. L., & Aune, T. M. (1978) · Infection and Immunity · doi:10.1128/iai.20.2.456-463.1978 · Cited by 151 · see citing works
Reactive Oxygen Species Mediate Virus-induced STAT Activation
Liu, T., Castro, S. M., Brasier, A. R., Jamaluddin, M., Garofalo, R. P., & Casola, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307251200 · Cited by 146 · see citing works
Chávez, V., Mohri‐Shiomi, A., & Garsin, D. A. (2009) · Infection and Immunity · doi:10.1128/iai.00627-09 · Cited by 145 · see citing works
Lactoperoxidase and Hydrogen Peroxide Metabolism in the Airway
Conner, G. E., Salathe, M. A., & Forteza, R. (2002) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.2206018 · Cited by 142 · see citing works
Welliver, C., Checchia, P. A., Bauman, J. H., et al. (2010) · Current Medical Research and Opinion · doi:10.1185/03007995.2010.505126 · Cited by 141 · see citing works
Dual oxidase, hydrogen peroxide and thyroid diseases
Ohye, H., & Sugawara, M. (2010) · Experimental Biology and Medicine · doi:10.1258/ebm.2009.009241 · Cited by 140 · see citing works
NADPH Oxidase-dependent Acid Production in Airway Epithelial Cells
Schwarzer, C., Machen, T. E., Illek, B., & Fischer, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404983200 · Cited by 140 · see citing works
Roles of DUOX-Mediated Hydrogen Peroxide in Metabolism, Host Defense, and Signaling
Deken, X. D., Corvilain, B., Dumont, J. E., & Miot, F. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5602 · Cited by 139 · see citing works
Kawahara, T., Kuwano, Y., Teshima-Kondo, S., Takeya, R., Sumimoto, H., Kishi, K., Tsunawaki, S., Hirayama, T., & Rokutan, K. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.5.3051 · Cited by 138 · see citing works
Lee, K., Kim, B., Bhin, J., Kim, D. H., You, H., Kim, E.-K., Kim, S., Ryu, J.-H., Hwang, D., & Lee, W. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2014.12.012 · Cited by 135 · see citing works
Nox/Duox Family of NADPH Oxidases: Lessons from Knockout Mouse Models
Sirokmány, G., Donkó, Á., & Geiszt, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.006 · Cited by 132 · see citing works
Donkó, Á., Péterfi, Z., Sum, A., Leto, T. L., & Geiszt, M. (2005) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2005.1767 · Cited by 131 · see citing works
The Oxidative Burst at Fertilization Is Dependent upon Activation of the Dual Oxidase Udx1
Wong, J. L., Créton, R., & Wessel, G. M. (2004) · Developmental Cell · doi:10.1016/j.devcel.2004.10.014 · Cited by 128 · see citing works
The Antilactobacillus System of Saliva. Role of Salivary Peroxidase.
Klebanoff, S. J., & Luebke, R. G. (1965) · Experimental Biology and Medicine · doi:10.3181/00379727-118-29882 · Cited by 124 · see citing works
Sommer, F., & Bäckhed, F. (2014) · Mucosal Immunology · doi:10.1038/mi.2014.74 · Cited by 120 · see citing works
Rada, B., Lekstrom, K. J., Damian, S., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.7.4883 · Cited by 119 · see citing works
Self-citationThe lactoperoxidase system links anion transport to host defense in cystic fibrosis
Conner, G. E., Wijkstrom-Frei, C., Randell, S. H., Fernandez, V. E., & Salathe, M. A. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.12.025 · Cited by 118 · see citing works
Kim, H. J., Kim, C., Ryu, J.-H., Kim, M., Park, C. Y., Lee, J. M., Holtzman, M. J., & Yoon, J. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0003oc · Cited by 118 · see citing works
Defects of thyroidal hydrogen peroxide generation in congenital hypothyroidism
Grasberger, H. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.01.029 · Cited by 113 · see citing works
NADPH oxidases as drug targets and biomarkers in neurodegenerative diseases: What is the evidence?
Sorce, S., Stocker, R., Seredenina, T. S., Holmdahl, R., Aguzzi, A., Chiò, A., Depaulis, A., Heitz, F., Olofsson, P., Olsson, T. P., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.08.006 · Cited by 113 · see citing works
Generation of H2O2in Isolated Porcine Thyroid Follicles*
Björkman, U., & EKHOLM, R. (1984) · Endocrinology · doi:10.1210/endo-115-1-392 · Cited by 111 · see citing works
Iodide handling disorders (NIS, TPO, TG, IYD)
Targovnik, H. M., Citterio, C. E., & Rivolta, C. M. (2017) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2017.03.006 · Cited by 106 · see citing works
Johnson, K. R., Marden, C. C., Ward‐Bailey, P. F., Gagnon, L. H., Bronson, R. T., & Donahue, L. R. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0085 · Cited by 103 · see citing works
Bosch, E. H., van Doorne, H., & Vries, S. D. (2000) · Journal of Applied Microbiology · doi:10.1046/j.1365-2672.2000.01098.x · Cited by 99 · see citing works
Boots, A. W., Hristova, M., Kasahara, D. I., Haenen, G. R. M. M., Bast, A., & van der Vliet, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809761200 · Cited by 97 · see citing works
Nox enzymes and oxidative stress in the immunopathology of the gastrointestinal tract
Rokutan, K., Kawahara, T., Kuwano, Y., Tominaga, K., Nishida, K., & Teshima-Kondo, S. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0124-5 · Cited by 97 · see citing works
Herpes simplex virus encephalitis: new infection or reactivation?
Steiner, I. (2011) · Current Opinion in Neurology · doi:10.1097/wco.0b013e328346be6f · Cited by 93 · see citing works
Fink, K., Duval, A., Martel, A., Soucy-Faulkner, A., & Grandvaux, N. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.10.6911 · Cited by 88 · see citing works
Strengert, M., Jennings, R., Davanture, S., Hayes, P., Gabriel, G., & Knaus, U. G. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5353 · Cited by 88 · see citing works
Functional consequences of dual oxidase-thyroperoxidase interaction at the plasma membrane”
Fortunato, R. S., Lima de Souza, E. C., Hassani, R. A.-E., Boufraqech, M., Weyemi, U., Talbot, M., Lagente-Chevallier, O., de Carvalho, D. P., Bidart, J.-M., Schlumberger, M., et al. (2010) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2010-1085 · Cited by 88 · see citing works
Urothelial cells produce hydrogen peroxide through the activation of duox1
Donkó, Á., Ruisanchez, É., Orient, A., Enyedi, B., Kapui, R., Péterfi, Z., de Deken, X., Benyó, Z., & Geiszt, M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.09.027 · Cited by 87 · see citing works
Grasberger, H., Deken, X. D., Miot, F., Pohlenz, J., & Refetoff, S. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0018 · Cited by 87 · see citing works
Ryu, J.-C., Kim, M.-J., Kwon, Y., Oh, J., Yoon, S. S., Shin, S. J., Yoon, J.-H., & Ryu, J.-H. (2016) · Mucosal Immunology · doi:10.1038/mi.2016.73 · Cited by 87 · see citing works
Mice Deficient in Dual Oxidase Maturation Factors Are Severely Hypothyroid
Grasberger, H., Deken, X. D., Barca‐Mayo, O., Raad, H., Weiss, M. C., Liao, X.-H., & Refetoff, S. (2012) · Molecular Endocrinology · doi:10.1210/me.2011-1320 · Cited by 85 · see citing works
Touch, V., Hayakawa, S., Yamada, S., et al. (2004) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2003.11.004 · Cited by 81 · see citing works
Enhancement of Respiratory Mucosal Antiviral Defenses by the Oxidation of Iodide
Fischer, A. J., Lennemann, N. J., Krishnamurthy, S., et al. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0329oc · Cited by 81 · see citing works
Role of the NADPH Oxidases DUOX and NOX4 in Thyroid Oxidative Stress
de Carvalho, D. P., & Dupuy, C. (2013) · European Thyroid Journal · doi:10.1159/000354745 · Cited by 80 · see citing works
Pachucki, J., Wang, D., Christophe, D., & Miot, F. E. L. (2004) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2003.11.026 · Cited by 80 · see citing works
Oxidative epithelial host defense is regulated by infectious and inflammatory stimuli
Gattas, M. V., Forteza, R., Fragoso, M. A., Fregien, N. L., Salas, P. J. I., Salathe, M. A., & Conner, G. E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.08.017 · Cited by 79 · see citing works
Microvascular NADPH oxidase in health and disease
Li, Y., & Pagano, P. J. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.02.049 · Cited by 79 · see citing works
Association of duoxes with thyroid peroxidase and its regulation in thyrocytes
Song, Y., Ruf, J., Lothaire, P., Dequanter, D., Andry, G., Willemse, E., Dumont, J. E., Van Sande, J., & De Deken, X. (2010) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-1727 · Cited by 77 · see citing works
Habibovic, A., Hristova, M., Heppner, D. E., Danyal, K., Ather, J. L., Janssen-Heininger, Y. M. W., Irvin, C. G., Poynter, M. E., Lundblad, L. K. A., Dixon, A. E., et al. (2016) · JCI Insight · doi:10.1172/jci.insight.88811 · Cited by 77 · see citing works
Mikola, H., Waris, M. E., & Tenovuo, J. O. (1995) · Antiviral Research · doi:10.1016/0166-3542(94)00073-h · Cited by 73 · see citing works
The Importance of NADPH Oxidases and Redox Signaling in Angiogenesis
Prieto-Bermejo, R., & Hernández‐Hernández, Á. (2017) · Antioxidants · doi:10.3390/antiox6020032 · Cited by 73 · see citing works
Concentration of the antibacterial precursor thiocyanate in cystic fibrosis airway secretions
Lorentzen, D., Durairaj, L., Pezzulo, A. A., Nakano, Y., Launspach, J. L., Stoltz, D. A., Zamba, G., McCray, P. B., Zabner, J., Welsh, M. J., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.013 · Cited by 69 · see citing works
Fink, K., Martin, L., Mukawera, E., Chartier, S., Deken, X. D., Brochiero, E., Miot, F., & Grandvaux, N. (2013) · Cell Research · doi:10.1038/cr.2013.47 · Cited by 69 · see citing works
Inhibition of Candida albicans by the peroxidase/SCN−/H2O2 system
Lenander‐Lumikari, M. (1992) · Oral Microbiology and Immunology · doi:10.1111/j.1399-302x.1992.tb00595.x · Cited by 68 · see citing works
Developmental regulation of DUOX1 expression and function in human fetal lung epithelial cells
Fischer, H., Gonzales, L. K., Kolla, V., et al. (2007) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00029.2007 · Cited by 68 · see citing works
Muzza, M., & Fugazzola, L. (2017) · Best Practice & Research Clinical Endocrinology & Metabolism · doi:10.1016/j.beem.2017.04.006 · Cited by 68 · see citing works
MARSHALL, V. M. E., & Reiter, B. (1980) · Microbiology · doi:10.1099/00221287-120-2-513 · Cited by 66 · see citing works
Joo, J.-H., Ryu, J.-H., Kim, C., Kim, H. J., Suh, M.-S., Kim, J.-O., Chung, S. Y., Lee, S. N., Kim, H. M., Bae, Y. S., et al. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.3898 · Cited by 66 · see citing works
Dual oxidase regulates neutrophil recruitment in allergic airways
Chang, S., Linderholm, A., Franzi, L. M., Kenyon, N. J., Grasberger, H., & Harper, R. W. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.06.012 · Cited by 64 · see citing works
Thiocyanate mediated antifungal and antibacterial property of goat milk lactoperoxidase
Jacob, B. M., Antony, K. E., Sreekumar, B., et al. (2000) · Life Sciences · doi:10.1016/s0024-3205(00)80003-x · Cited by 64 · see citing works
Meitzler, J. L., Hinde, S. L., Bánfi, B., Nauseef, W. M., & de Montellano, P. R. O. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.414797 · Cited by 62 · see citing works
NADPH‐dependent H2O2 generation catalyzed by thyroid plasma membranes
Dupuy, C., Kaniewski, J., Danièle, D. E. M. E., et al. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15155.x · Cited by 61 · see citing works
NADPH-dependent H2O2 generation and peroxidase activity in thyroid particular fraction
Virion, A., Michot, J., Dème, D., Kaniewski, J., & Pommier, J. (1984) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(84)90088-1 · Cited by 61 · see citing works
Hydrogen Peroxide–Scavenging Properties of Normal Human Airway Secretions
El‐Chemaly, S., Salathe, M. A., Baier, S., et al. (2003) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.200206-531oc · Cited by 61 · see citing works
Rada, B., Park, J. J.-Y., Sil, P., Geiszt, M., & Leto, T. L. (2014) · Inflammation Research · doi:10.1007/s00011-014-0756-y · Cited by 58 · see citing works
Self-citationWelk, A., Meller, C., Schubert, R., et al. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-134 · Cited by 58 · see citing works
The emerging role of NADPH oxidase NOX5 in vascular disease
Jha, J. C., Watson, A. M. D., Mathew, G., de Vos, L. C., & Jandeleit-Dahm, K. A. M. (2017) · Clinical Science · doi:10.1042/cs20160846 · Cited by 58 · see citing works
Yang, X., Smith, A. A., Williams, M. S., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.538272 · Cited by 57 · see citing works
Biosynthesis of human myeloperoxidase
Nauseef, W. M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.02.001 · Cited by 57 · see citing works
Moreau‐Marquis, S., Coutermarsh, B., & Stanton, B. A. (2014) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dku357 · Cited by 56 · see citing works
Derscheid, R. J., Geelen, A. V., Berkebile, A. R., et al. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0529oc · Cited by 53 · see citing works
Moribe, H., Konakawa, R., Koga, D., Ushiki, T., Nakamura, K., & Mekada, E. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002957 · Cited by 53 · see citing works
Paradoxical roles of dual oxidases in cancer biology
Little, A. C., Sulovari, A., Danyal, K., Heppner, D. E., Seward, D. J., & van der Vliet, A. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.05.024 · Cited by 53 · see citing works
Dickinson, J. D., Sweeter, J. M., Warren, K. J., Ahmad, I. M., Deken, X. D., Zimmerman, M. C., & Brody, S. L. (2017) · Redox Biology · doi:10.1016/j.redox.2017.09.013 · Cited by 53 · see citing works
Asymptomatic Shedding of Herpes Simplex Virus From the Cervix and Lesion Site During Pregnancy
Wittek, A. E. (1984) · American journal of diseases of children · doi:10.1001/archpedi.1984.02140430017005 · Cited by 49 · see citing works
Csillag, C., Nielsen, O. H., Vainer, B., Olsen, J., Dieckgraefe, B. K., Hendel, J. W., Vind, I., Dupuy, C., Nielsen, F. C., & Borup, R. (2006) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520600976266 · Cited by 48 · see citing works
Soukka, T., Lumikari, M., & Tenovuo, J. O. (1991) · European Journal Of Oral Sciences · doi:10.1111/j.1600-0722.1991.tb01046.x · Cited by 48 · see citing works
Redox warfare between airway epithelial cells and Pseudomonas: dual oxidase versus pyocyanin
Rada, B., & Leto, T. L. (2008) · Immunologic Research · doi:10.1007/s12026-008-8071-8 · Cited by 47 · see citing works
Self-citationIsolation and Characterization of a Peroxidase from the Airway
Salathe, M. A., Holderby, M., Forteza, R., et al. (1997) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb.17.1.2719 · Cited by 47 · see citing works
El‐Fakharany, E. M., Uversky, V. N., & Redwan, E. M. M. M. (2016) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-016-2327-x · Cited by 47 · see citing works
Majerus, P., & Courtois, P. (1992) · PubMed · Cited by 46 · see citing works
In vitro antiviral activity of hypothiocyanite against A/H1N1/2009 pandemic influenza virus
Cegolon, L., Salata, C., Piccoli, E., Juárez, V., Palù, G., Mastrangelo, G., & Calistri, A. (2013) · International Journal of Hygiene and Environmental Health · doi:10.1016/j.ijheh.2013.03.001 · Cited by 46 · see citing works
Rada, B., & Leto, T. L. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.01.025 · Cited by 46 · see citing works
Self-citationBactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures
Carlsson, J., Edlund, M. B., & Hänström, L. (1984) · Infection and Immunity · doi:10.1128/iai.44.3.581-586.1984 · Cited by 46 · see citing works
Kim, J. H., Lee, J., Bae, S.-J., Kim, Y., Park, B.-J., Choi, J.-W., Kwon, J., Cha, G.-H., Yoo, H. J., Jo, E.-K., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-06610-4 · Cited by 45 · see citing works
Influence of a model human defensive peroxidase system on oral streptococcal antagonism
Ashby, M. T., Kreth, J., Soundarajan, M., & Sivuilu, L. S. (2009) · Microbiology · doi:10.1099/mic.0.031310-0 · Cited by 44 · see citing works
van der Hoeven, R., Cruz, M. R., Chávez, V., & Garsin, D. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124091 · Cited by 43 · see citing works
Antibacterial effect of lactoperoxidase and myeloperoxidase against Bacillus cereus
Tenovuo, J. O., Mäkinen, K. K., & Sievers, G. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.27.1.96 · Cited by 43 · see citing works
The Role of NOX4 and TRX2 in Angiogenesis and Their Potential Cross-Talk
Chen, C., Li, L., Zhou, H. J., & Wang, M. (2017) · Antioxidants · doi:10.3390/antiox6020042 · Cited by 43 · see citing works
Ihalin, R., Loimaranta, V., Lenander‐Lumikari, M., & Tenovuo, J. O. (1998) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1998.tb02338.x · Cited by 42 · see citing works
Inhibition of HIV infectivity by lactoperoxidase-produced hypothiocyanite.
Pourtois, M., Binet, C., Tieghem, N. V., Courtois, P., Vandenabbeele, A., & Thiry, L. F. (1990) · PubMed · Cited by 41 · see citing works
Duox2 exhibits potent heme peroxidase activity in human respiratory tract epithelium
Harper, R. W., Xu, C., McManus, M. T., Heidersbach, A. J., & Eiserich, J. P. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.08.048 · Cited by 41 · see citing works
Rada, B., Boudreau, H. E., Park, J. J.-Y., et al. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0254oc · Cited by 41 · see citing works
Self-citationLung epithelial NOX/DUOX and respiratory virus infections
Grandvaux, N., Mariani, M. K., & Fink, K. (2014) · Clinical Science · doi:10.1042/cs20140321 · Cited by 39 · see citing works
The Extracellular A-loop of Dual Oxidases Affects the Specificity of Reactive Oxygen Species Release
Ueyama, T., Sakuma, M., Ninoyu, Y., Hamada, T., Dupuy, C., Geiszt, M., Leto, T. L., & Saito, N. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592717 · Cited by 39 · see citing works
Thomas, E. L., & Aune, T. M. (1978) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.13.2.261 · Cited by 38 · see citing works
Targeting of the Dual Oxidase 2 N-terminal Region to the Plasma Membrane
Morand, S. C., Agnandji, D., Noël‐Hudson, M., Nicolas, V., Buisson, S., Maçon‐Lemaître, L., Gnidehou, S., Kaniewski, J., Ohayon, R., Virion, A., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405406200 · Cited by 37 · see citing works
Popper, L., & Knorr, D. (1997) · Food / Nahrung · doi:10.1002/food.19970410108 · Cited by 37 · see citing works
Redox regulation of gasotransmission in the vascular system: A focus on angiogenesis
Mistry, R. K., & Brewer, A. C. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.025 · Cited by 37 · see citing works
Genetic defects of hydrogen peroxide generation in the thyroid gland.
Weber, G., Rabbiosi, S., Zamproni, I., et al. (2013) · PubMed · doi:10.3275/8847 · Cited by 36 · see citing works
The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA
Hoste, C., Dumont, J. E., Miot, F., & Deken, X. D. (2012) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.07.007 · Cited by 36 · see citing works
Wang, H., & Hartnett, M. E. (2017) · Antioxidants · doi:10.3390/antiox6020040 · Cited by 36 · see citing works
When an Intramolecular Disulfide Bridge Governs the Interaction of DUOX2 with Its Partner DUOXA2
Carré, A., Louzada, R. A. N., Fortunato, R. S., Hassani, R. A. E., Morand, S. C., Ogryzko, V. V., de Carvalho, D. P., Grasberger, H., Leto, T. L., & Dupuy, C. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2015.6265 · Cited by 35 · see citing works
Molecular interaction of NADPH oxidase 1 with βPix and Nox Organizer 1
Park, H. S., Park, D., & Bae, Y. S. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.108 · Cited by 33 · see citing works
Kim, H. J., Kim, C., Kim, M., Ryu, J.-H., Seong, S. Y., Kim, S.-J., Lim, S. J., Holtzman, M. J., & Yoon, J. (2015) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2014-0334oc · Cited by 32 · see citing works
Antibacterial action of lactoperoxidase-thiocyanate-hydrogen peroxide on Streptococcus agalactiae
Mickelson, M. N. (1979) · Applied and Environmental Microbiology · doi:10.1128/aem.38.5.821-826.1979 · Cited by 32 · see citing works
Antibacterial Effect of Salivary Peroxidases on a Cariogenic Strain of Streptococcus mutans
Tenovuo, J. O., & Knuuttila, M. L. E. (1977) · Journal of Dental Research · doi:10.1177/00220345770560123301 · Cited by 28 · see citing works
Degradation of aflatoxin by lactoperoxidase
Doyle, M. P., & Marth, E. H. (1978) · European Food Research and Technology · doi:10.1007/bf01127651 · Cited by 28 · see citing works
Candida albicans susceptibility to lactoperoxidase-generated hypoiodite
Courtois, P. (2010) · Clinical Cosmetic and Investigational Dentistry · doi:10.2147/cciden.s10891 · Cited by 27 · see citing works
The Lactoperoxidase-Thiocyanate-Hydrogen Peroxide Antibacterium System
Reiter, B. (2008) · Novartis Foundation symposium · doi:10.1002/9780470715413.ch16 · Cited by 27 · see citing works
Induction of Airway Allergic Inflammation by Hypothiocyanite via Epithelial Cells
Suzuki, S., Ogawa, M., Ohta, S., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.746909 · Cited by 26 · see citing works
Allen, P. Z., & Morrison, M. (1966) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(66)90231-1 · Cited by 25 · see citing works
Gingerich, A. D., Pang, L., Hanson, J. M., Dlugolenski, D. A., Streich, R., Lafontaine, E. R., Nagy, T., Tripp, R. A., & Rada, B. (2015) · Inflammation Research · doi:10.1007/s00011-015-0892-z · Cited by 25 · see citing works
Self-citationStephens, S., HARKNESS, R. A., & Cockle, S. M. (1979) · PubMed · Cited by 24 · see citing works
Donkó, Á., Morand, S. C., Korzeniowska, A., et al. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.05.006 · Cited by 23 · see citing works
Rada, B. (2017) · Communicative & Integrative Biology · doi:10.1080/19420889.2017.1296610 · Cited by 23 · see citing works
Self-citationCandida albicans susceptibility to lactoperoxidase-generated hypoiodite
Courtois, P. (2010) · Clinical Cosmetic and Investigational Dentistry · doi:10.2147/ccide.s10891 · Cited by 23 · see citing works
Asymptomatic Shedding of Herpes Simplex Virus from the Cervix and Lesion Site During Pregnancy
Wittek, A. B., Yeager, A. S., Au, D. S., et al. (1984) · Obstetric Anesthesia Digest · doi:10.1097/00132582-198404030-00005 · Cited by 21 · see citing works
Uracil-induced signaling pathways for DUOX-dependent gut immunity
Lee, K., Kim, B., You, H., & Lee, W. (2015) · Fly · doi:10.1080/19336934.2015.1126011 · Cited by 21 · see citing works
Malhotra, K., Salmon, D., Bras, J. L., et al. (1988) · Infection and Immunity · doi:10.1128/iai.56.12.3305-3309.1988 · Cited by 20 · see citing works
Susceptibility of anaerobic microorganisms to hypothiocyanite produced by lactoperoxidase.
Courtois, P., Majerus, P., Labbé, M., et al. (1992) · PubMed · Cited by 18 · see citing works
Candidacidal activities of the glucose oxidase-mediated lactoperoxidase system
Kho, H., Kim, Y.-Y., Chang, J., et al. (2011) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2011.11.007 · Cited by 18 · see citing works
Sensitivity of alpha-amanitin to oxidation by a lactoperoxidase-hydrogen peroxide system
Zheleva, A. M., MICHELOT, D., & Zhelev, Z. D. (2000) · Toxicon · doi:10.1016/s0041-0101(99)00217-2 · Cited by 16 · see citing works
McGovern, F., Magee, D. A., Browne, J. A., et al. (2015) · animal · doi:10.1017/s1751731115002505 · Cited by 14 · see citing works
Simmons, J. H., Purdy, G. A., Franklin, C. L., et al. (2002) · PubMed · Cited by 14 · see citing works
Ihalin, R., Pienihäkkinen, K., Lenander, M., et al. (2003) · International Journal of Antimicrobial Agents · doi:10.1016/s0924-8579(03)00008-6 · Cited by 13 · see citing works
Different modes of herpes simplex virus type 1 spread in brain and skin tissues
Tsalenchuck, Y., Tzur, T., Steiner, I., & Panet, A. (2014) · Journal of NeuroVirology · doi:10.1007/s13365-013-0224-4 · Cited by 13 · see citing works
Co-occurrence of tetraspanin and ROS generators
Moribe, H., & Mekada, E. (2013) · Worm · doi:10.4161/worm.23415 · Cited by 12 · see citing works
Tenovuo, J. O., & Knuuttila, M. L. E. (1977) · Journal of Dental Research · doi:10.1177/00220345770560123201 · Cited by 10 · see citing works
Parasiticidal activity of bovine lactoperoxidase against Toxoplasma gondii
Tanaka, T., Murakami, S., Kumura, H., et al. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-142 · Cited by 8 · see citing works
α-Amanitin: Inactivation by bovine lactoperoxidase
Morris, P. W., Kelley, K. M., & Logas, W. G. (1979) · Cellular and Molecular Life Sciences · doi:10.1007/bf01960335 · Cited by 7 · see citing works
Grieve, P. A., Dionysius, D. A., & Vos, A. C. (1992) · Journal of Veterinary Medicine Series B · doi:10.1111/j.1439-0450.1992.tb01203.x · Cited by 6 · see citing works
Mickelson, M. N., & Anderson, A. J. (1984) · Applied and Environmental Microbiology · doi:10.1128/aem.47.2.338-342.1984 · Cited by 5 · see citing works
Asymptomatic Shedding of Herpes Simplex Virus From the Cervix and Lesion Site During Pregnancy
Wittek, A. E., Yeager, A. S., Au, D. S., et al. (1985) · Obstetrical & Gynecological Survey · doi:10.1097/00006254-198503000-00007 · Cited by 3 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Csillag C, Nielsen OH, Vainer B, Olsen J, Dieckgraefe BK, Hendel J, Vind I, Dupuy C, Nielsen FC, and Borup R 2007 Expression of the genes dualoxidase 2, lipocalin 2 and regenerating islet-derived 1 alpha in Crohn’s disease. Scand. J. Gastroenterol 42, 454– 463. 17454855
Cited by
Sorted by citations
The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works
Al-Shehri, S. S., Duley, J. A., & Bansal, N. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101524 · Cited by 82 · see citing works
Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion
Jing, L., & Zhang, Q. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.992883 · Cited by 61 · see citing works
- Authors
- Sarr, D., Tóth, E., Gingerich, A., & Rada, B.
- Affiliations
- University of Georgia (US)
- Corresponding author
- Rada, Balázs
- Venue
- Journal of Microbiology
- Publisher
- The Microbiological Society of Korea
- Published
- 2018-06
- Volume
- 56
- Issue
- 6
- Pages
- 373-386
- ISSN
- 1225-8873 (ISSN-L)
- 1976-3794
- PMC
- PMC7336354
- OpenAlex
- W2805722840
- Cited by
- 98
- References
- 178
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 12 · 2023: 11 · 2022: 16 · 2021: 22 · 2020: 12 · 2019: 5 · 2018: 1
- FWCI
- 1.02
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Microbiology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Georgia
- National Institute of Allergy and Infectious Diseases (R21AI124189)
- 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
- dual oxidase, DUOX1, DUOX2, NADPH oxidase, lactoperoxidase, reactive oxygen species, hydrogen peroxide, antimicrobial defense, innate immunity, antibacterial activity, antiviral activity, antifungal activity, antiparasitic activity, salivary gland epithelium, respiratory epithelium, oxidative stress
- MeSH terms
- Dual Oxidases, NADPH Oxidase 1, NADPH Oxidase 5, Animals, Anti-Infective Agents, Antifungal Agents, Antiparasitic Agents, Antiviral Agents, Humans, Hydrogen Peroxide, Immunity, Innate, Lactoperoxidase, Membrane Proteins, Salivary Glands, Thiocyanates, Thyroid Gland, Reactive Oxygen Species, Oxidative Stress, NADPH Oxidases, Respiratory Mucosa
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
