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and is characterized by its fast but nonspecific response. One important mechanism of this system is the production of the biocidal reactive oxygen and nitrogen species, which are widely distributed within biological systems, including phagocytes and secretions. Reactive oxygen and nitrogen species are short-lived intermediates that are biochemically synthesized by various enzymatic reactions in aerobic organisms and are regulated by antioxidants. The physiological levels of reactive species play important roles in cellular signaling and proliferation. However, higher concentrations and prolonged exposure can fight infections by damaging important microbial biomolecules. One feature of the reactive species generation system is the interaction between its components to produce more biocidal agents. For example, the phagocytic NADPH oxidase complex generates superoxide, which functions as a precursor for antimicrobial hydrogen peroxide synthesis. Peroxide is then used by myeloperoxidase in the same cells to generate hypochlorous acid, a highly microbicidal agent. Studies on animal models and microorganisms have shown that deficiency of these antimicrobial agents is associated with severe recurrent infections and immunocompromised diseases, such as chronic granulomatous disease. There is accumulating evidence that reactive species have important positive aspects on human health and immunity; however, some important promising features of this system remain obscure. © 2020 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM)", "keywords" : [ { "otype" : "Keyword", "mtid" : 4603, "link" : "/api/keyword/4603", "label" : "innate immunity", "published" : true, "oldId" : 4603, "snippet" : true }, { "otype" : "Keyword", "mtid" : 15242, "link" : "/api/keyword/15242", "label" : "Reactive oxygen species", "published" : true, "oldId" : 15242, "snippet" : true }, { "otype" : "Keyword", "mtid" : 1027428, "link" : "/api/keyword/1027428", "label" : "Reactive nitrogen species", "published" : true, "oldId" : 1027428, "snippet" : true }, { "otype" : "Keyword", "mtid" : 1057723, "link" : "/api/keyword/1057723", "label" : "Antimicrobial", "published" : true, "oldId" : 1057723, "snippet" : true } ], "digital" : null, "printed" : null, "sourceYear" : 2021, "foreignEdition" : true, "foreignLanguage" : true, "fullPublication" : true, "conferencePublication" : false, "nationalOrigin" : null, "missingAuthor" : false, "oaType" : "NONE", "oaCheckDate" : "2022-10-04", "oaFree" : false, "citationCount" : 0, "citationCountUnpublished" : 0, "citationCountWoOther" : 0, "independentCitCountWoOther" : 0, "doiCitationCount" : 0, "wosCitationCount" : 0, "scopusCitationCount" : 0, "independentCitationCount" : 0, "unhandledCitationCount" : 0, "citingPubCount" : 0, "independentCitingPubCount" : 0, "unhandledCitingPubCount" : 0, "citedPubCount" : 2, "citedCount" : 2, "ratings" : [ { "otype" : "SjrRating", "mtid" : 11225443, "link" : "/api/sjrrating/11225443", "label" : "sjr:Q1 (2021) Scopus - Medicine (miscellaneous) BIOCHIMIE 0300-9084 1638-6183", "listPos" : 585, "rankValue" : 0.24, "type" : "journal", "ratingType" : { "otype" : "RatingType", "mtid" : 10002, "link" : "/api/ratingtype/10002", "label" : "sjr", "code" : "sjr", "published" : true, "snippet" : true }, "subject" : { "otype" : "ClassificationExternal", "mtid" : 2701, "link" : "/api/classificationexternal/2701", "label" : "Scopus - Medicine (miscellaneous)", "published" : true, "oldId" : 2701, "snippet" : true }, "ranking" : "Q1", "calculation" : "DIRECT", "published" : true, "snippet" : true } ], "ratingsForSort" : "Q1", "references" : [ { "otype" : "Reference", "mtid" : 19786865, "link" : "/api/reference/19786865", "label" : "1. Moller, M.N., Denicola, A., Diffusion of nitric oxide and oxygen in lipoproteins and membranes studied by pyrene fluorescence quenching (2018) Free Radic. Biol. Med., 128, pp. 137-143", "listPosition" : 1, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786864, "link" : "/api/reference/19786864", "label" : "2. Bonini, M.G., Siraki, A.G., Atanassov, B.S., Mason, R.P., Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes (2007) Free Radic. Biol. Med., 42, pp. 530-540", "listPosition" : 2, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786863, "link" : "/api/reference/19786863", "label" : "3. R Buettner, G., Superoxide dismutase in redox biology: the roles of superoxide and hydrogen peroxide (2011) Anti Canc. Agents Med. Chem., 11, pp. 341-346", "listPosition" : 3, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786862, "link" : "/api/reference/19786862", "label" : "4. Wong, H.S., Dighe, P.A., Mezera, V., Monternier, P.A., Brand, M.D., Production of superoxide and hydrogen peroxide from specific mitochondrial sites under different bioenergetic conditions (2017) J. Biol. Chem., 292, pp. 16804-16809", "listPosition" : 4, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786861, "link" : "/api/reference/19786861", "label" : "5. McCall, T.B., Boughton-Smith, N.K., Palmer, R.M., Whittle, B.J., Moncada, S., Synthesis of nitric oxide from L-arginine by neutrophils. Release and interaction with superoxide anion (1989) Biochem. J., 261, pp. 293-296", "listPosition" : 5, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786860, "link" : "/api/reference/19786860", "label" : "6. Wright, C.D., Mulsch, A., Busse, R., Osswald, H., Generation of nitric oxide by human neutrophils (1989) Biochem. Biophys. Res. Commun., 160, pp. 813-819", "listPosition" : 6, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786859, "link" : "/api/reference/19786859", "label" : "7. Reiling, N., Ulmer, A.J., Duchrow, M., Ernst, M., Flad, H.D., Hauschildt, S., Nitric oxide synthase: mRNA expression of different isoforms in human monocytes/macrophages (1994) Eur. J. Immunol., 24, pp. 1941-1944", "listPosition" : 7, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786858, "link" : "/api/reference/19786858", "label" : "8. Kobzik, L., Bredt, D.S., Lowenstein, C.J., Drazen, J., Gaston, B., Sugarbaker, D., Stamler, J.S., Nitric oxide synthase in human and rat lung: immunocytochemical and histochemical localization (1993) Am. J. Respir. Cell Mol. Biol., 9, pp. 371-377", "listPosition" : 8, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786857, "link" : "/api/reference/19786857", "label" : "9. Stuehr, D.J., Marletta, M.A., Mammalian nitrate biosynthesis: mouse macrophages produce nitrite and nitrate in response to Escherichia coli lipopolysaccharide (1985) Proc. Natl. Acad. Sci. U. S. A., 82, pp. 7738-7742", "listPosition" : 9, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786856, "link" : "/api/reference/19786856", "label" : "10. Suzuki, C., Aoki-Yoshida, A., Kimoto-Nira, H., Kobayashi, M., Sasaki, K., Mizumachi, K., Effects of strains of Lactococcus lactis on the production of nitric oxide and cytokines in murine macrophages (2014) Inflammation, 37, pp. 1728-1737", "listPosition" : 10, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786855, "link" : "/api/reference/19786855", "label" : "11. Stuehr, D.J., Gross, S.S., Sakuma, I., Levi, R., Nathan, C.F., Activated murine macrophages secrete a metabolite of arginine with the bioactivity of endothelium-derived relaxing factor and the chemical reactivity of nitric oxide (1989) J. Exp. Med., 169, pp. 1011-1020", "listPosition" : 11, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786854, "link" : "/api/reference/19786854", "label" : "12. Tiso, M., Schechter, A.N., Nitrate reduction to nitrite, nitric oxide and ammonia by gut bacteria under physiological conditions (2015) PloS One, 10", "listPosition" : 12, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786853, "link" : "/api/reference/19786853", "label" : "13. Hancock, J.T., Salisbury, V., Ovejero-Boglione, M.C., Cherry, R., Hoare, C., Eisenthal, R., Harrison, R., Antimicrobial properties of milk: dependence on presence of xanthine oxidase and nitrite (2002) Antimicrob. Agents Chemother., 46, pp. 3308-3310", "listPosition" : 13, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786852, "link" : "/api/reference/19786852", "label" : "14. Godber, B.L., Doel, J.J., Sapkota, G.P., Blake, D.R., Stevens, C.R., Eisenthal, R., Harrison, R., Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase (2000) J. Biol. Chem., 275, pp. 7757-7763", "listPosition" : 14, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786851, "link" : "/api/reference/19786851", "label" : "15. Jones, M.L., Ganopolsky, J.G., Labbe, A., Prakash, S., A novel nitric oxide producing probiotic patch and its antimicrobial efficacy: preparation and in vitro analysis (2010) Appl. Microbiol. Biotechnol., 87, pp. 509-516", "listPosition" : 15, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786850, "link" : "/api/reference/19786850", "label" : "16. Jones, M.L., Ganopolsky, J.G., Labbe, A., Wahl, C., Prakash, S., Antimicrobial properties of nitric oxide and its application in antimicrobial formulations and medical devices (2010) Appl. Microbiol. Biotechnol., 88, pp. 401-407", "listPosition" : 16, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786849, "link" : "/api/reference/19786849", "label" : "17. Gookin, J.L., Allen, J., Chiang, S., Duckett, L., Armstrong, M.U., Local peroxynitrite formation contributes to early control of Cryptosporidium parvum infection (2005) Infect. Immun., 73, pp. 3929-3936", "listPosition" : 17, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786848, "link" : "/api/reference/19786848", "label" : "18. Vazquez-Torres, A., Jones-Carson, J., Balish, E., Peroxynitrite contributes to the candidacidal activity of nitric oxide-producing macrophages (1996) Infect. Immun., 64, pp. 3127-3133", "listPosition" : 18, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786847, "link" : "/api/reference/19786847", "label" : "19. Padalko, E., Ohnishi, T., Matsushita, K., Sun, H., Fox-Talbot, K., Bao, C., Baldwin, W.M., 3rd, Lowenstein, C.J., Peroxynitrite inhibition of Coxsackievirus infection by prevention of viral RNA entry (2004) Proc. Natl. Acad. Sci. U. S. A., 101, pp. 11731-11736", "listPosition" : 19, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786846, "link" : "/api/reference/19786846", "label" : "20. Karupiah, G., Xie, Q.W., Buller, R.M., Nathan, C., Duarte, C., MacMicking, J.D., Inhibition of viral replication by interferon-gamma-induced nitric oxide synthase (1993) Science, 261, pp. 1445-1448", "listPosition" : 20, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786845, "link" : "/api/reference/19786845", "label" : "21. Akerstrom, S., Mousavi-Jazi, M., Klingstrom, J., Leijon, M., Lundkvist, A., Mirazimi, A., Nitric oxide inhibits the replication cycle of severe acute respiratory syndrome coronavirus (2005) J. Virol., 79, pp. 1966-1969", "listPosition" : 21, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786844, "link" : "/api/reference/19786844", "label" : "22. Rimmelzwaan, G.F., Baars, M.M., de Lijster, P., Fouchier, R.A., Osterhaus, A.D., Inhibition of influenza virus replication by nitric oxide (1999) J. Virol., 73, pp. 8880-8883", "listPosition" : 22, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786843, "link" : "/api/reference/19786843", "label" : "23. Brunelli, L., Crow, J.P., Beckman, J.S., The comparative toxicity of nitric oxide and peroxynitrite to Escherichia coli (1995) Arch. Biochem. Biophys., 316, pp. 327-334", "listPosition" : 23, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786842, "link" : "/api/reference/19786842", "label" : "24. Miller, C.C., Hergott, C.A., Rohan, M., Arsenault-Mehta, K., Doring, G., Mehta, S., Inhaled nitric oxide decreases the bacterial load in a rat model of Pseudomonas aeruginosa pneumonia (2013) J. Cyst. Fibros., 12, pp. 817-820", "listPosition" : 24, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786841, "link" : "/api/reference/19786841", "label" : "25. Shiloh, M.U., MacMicking, J.D., Nicholson, S., Brause, J.E., Potter, S., Marino, M., Fang, F., Nathan, C., Phenotype of mice and macrophages deficient in both phagocyte oxidase and inducible nitric oxide synthase (1999) Immunity, 10, pp. 29-38", "listPosition" : 25, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786840, "link" : "/api/reference/19786840", "label" : "26. MacMicking, J.D., Nathan, C., Hom, G., Chartrain, N., Fletcher, D.S., Trumbauer, M., Stevens, K., Hutchinson, N., Altered responses to bacterial infection and endotoxic shock in mice lacking inducible nitric oxide synthase (1995) Cell, 81, pp. 641-650", "listPosition" : 26, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786839, "link" : "/api/reference/19786839", "label" : "27. Richardson, A.R., Payne, E.C., Younger, N., Karlinsey, J.E., Thomas, V.C., Becker, L.A., Navarre, W.W., Fang, F.C., Multiple targets of nitric oxide in the tricarboxylic acid cycle of Salmonella enterica serovar typhimurium (2011) Cell Host Microbe, 10, pp. 33-43", "listPosition" : 27, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786838, "link" : "/api/reference/19786838", "label" : "28. Stevanin, T.M., Ioannidis, N., Mills, C.E., Kim, S.O., Hughes, M.N., Poole, R.K., Flavohemoglobin hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromesbo’ or bd, from nitric oxide (2000) J. Biol. Chem., 275, pp. 35868-35875", "listPosition" : 28, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786837, "link" : "/api/reference/19786837", "label" : "29. Schapiro, J.M., Libby, S.J., Fang, F.C., Inhibition of bacterial DNA replication by zinc mobilization during nitrosative stress (2003) Proc. Natl. Acad. Sci. U. S. A., 100, pp. 8496-8501", "listPosition" : 29, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786836, "link" : "/api/reference/19786836", "label" : "30. McLean, S., Bowman, L.A., Sanguinetti, G., Read, R.C., Poole, R.K., Peroxynitrite toxicity in Escherichia coli K12 elicits expression of oxidative stress responses and protein nitration and nitrosylation (2010) J. Biol. Chem., 285, pp. 20724-20731", "listPosition" : 30, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786835, "link" : "/api/reference/19786835", "label" : "31. Radi, R., Nitric oxide, oxidants, and protein tyrosine nitration (2004) Proc. Natl. Acad. Sci. U. S. A., 101, pp. 4003-4008", "listPosition" : 31, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786834, "link" : "/api/reference/19786834", "label" : "32. Chase, M.J., Klebanoff, S.J., Viricidal effect of stimulated human mononuclear phagocytes on human immunodeficiency virus type 1 (1992) Proc. Natl. Acad. Sci. U. S. A., 89, pp. 5582-5585", "listPosition" : 32, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786833, "link" : "/api/reference/19786833", "label" : "33. Klebanoff, S.J., Myeloperoxidase: friend and foe (2005) J. Leukoc. Biol., 77, pp. 598-625", "listPosition" : 33, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786832, "link" : "/api/reference/19786832", "label" : "34. Lehrer, R.I., Inhibition by sulfonamides of the candidacidal activity of human neutrophils (1971) J. Clin. Invest., 50, pp. 2498-2505", "listPosition" : 34, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786831, "link" : "/api/reference/19786831", "label" : "35. Lehrer, R.I., Hanifin, J., Cline, M.J., Defective bactericidal activity in myeloperoxidase-deficient human neutrophils (1969) Nature, 223, pp. 78-79", "listPosition" : 35, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786830, "link" : "/api/reference/19786830", "label" : "36. Lehrer, R.I., Cline, M.J., Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infection (1969) J. Clin. Invest., 48, pp. 1478-1488", "listPosition" : 36, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786829, "link" : "/api/reference/19786829", "label" : "37. Brovkovych, V., Gao, X.-P., Ong, E., Brovkovych, S., Brennan, M.-L., Su, X., Hazen, S.L., Skidgel, R.A., Augmented inducible nitric oxide synthase expression and increased NO production reduce sepsis-induced lung injury and mortality in myeloperoxidase-null mice (2008) Am. J. Physiol. Lung Cell Mol. Physiol., 295, pp. L96-L103", "listPosition" : 37, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786828, "link" : "/api/reference/19786828", "label" : "38. Rausch, P.G., Moore, T.G., Granule enzymes of polymorphonuclear neutrophils: a phylogenetic comparison (1975) Blood, 46, pp. 913-919", "listPosition" : 38, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786827, "link" : "/api/reference/19786827", "label" : "39. Koch, C., Effect of sodium azide upon normal and pathological granulocyte function (1974) Acta Pathologica Microbiologica Scandinavica Section B Microbiology and Immunology, 82, pp. 136-142", "listPosition" : 39, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786826, "link" : "/api/reference/19786826", "label" : "40. Hirche, T.O., Gaut, J.P., Heinecke, J.W., Belaaouaj, A., Myeloperoxidase plays critical roles in killing Klebsiella pneumoniae and inactivating neutrophil elastase: effects on host defense (2005) J. Immunol., 174, pp. 1557-1565", "listPosition" : 40, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786825, "link" : "/api/reference/19786825", "label" : "41. Aratani, Y., Koyama, H., Nyui, S.-I., Suzuki, K., Kura, F., Maeda, N., Severe impairment in early host defense againstCandida albicans in mice deficient in myeloperoxidase (1999) Infect. Immun., 67, pp. 1828-1836", "listPosition" : 41, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786824, "link" : "/api/reference/19786824", "label" : "42. Lymar, S.V., Hurst, J.K., Role of compartmentation in promoting toxicity of leukocyte-generated strong oxidants (1995) Chem. Res. Toxicol., 8, pp. 833-840", "listPosition" : 42, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786823, "link" : "/api/reference/19786823", "label" : "43. Albrich, J.M., McCarthy, C.A., Hurst, J.K., Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase (1981) Proc. Natl. Acad. Sci. U. S. A., 78, pp. 210-214", "listPosition" : 43, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786822, "link" : "/api/reference/19786822", "label" : "44. Thomas, E.L., Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: nitrogen-chlorine derivatives of bacterial components in bactericidal action against Escherichia coli (1979) Infect. Immun., 23, pp. 522-531", "listPosition" : 44, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786821, "link" : "/api/reference/19786821", "label" : "45. Vissers, M.C., Winterbourn, C.C., Oxidative damage to fibronectin. I. The effects of the neutrophil myeloperoxidase system and HOCl (1991) Arch. Biochem. Biophys., 285, pp. 53-59", "listPosition" : 45, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786820, "link" : "/api/reference/19786820", "label" : "46. Hazen, S.L., d'Avignon, A., Anderson, M.M., Hsu, F.F., Heinecke, J.W., Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway (1998) J. Biol. Chem., 273, pp. 4997-5005", "listPosition" : 46, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786819, "link" : "/api/reference/19786819", "label" : "47. Grisham, M.B., Jefferson, M.M., Melton, D.F., Thomas, E.L., Chlorination of endogenous amines by isolated neutrophils. Ammonia-dependent bactericidal, cytotoxic, and cytolytic activities of the chloramines (1984) J. Biol. Chem., 259, pp. 10404-10413", "listPosition" : 47, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786818, "link" : "/api/reference/19786818", "label" : "48. Hawkins, C.L., Davies, M.J., Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation (1998) Biochem. J., 332, pp. 617-625", "listPosition" : 48, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786817, "link" : "/api/reference/19786817", "label" : "49. Rosen, H., Klebanoff, S.J., Wang, Y., Brot, N., Heinecke, J.W., Fu, X., Methionine oxidation contributes to bacterial killing by the myeloperoxidase system of neutrophils (2009) Proc. Natl. Acad. Sci. U. S. A., 106, pp. 18686-18691", "listPosition" : 49, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786816, "link" : "/api/reference/19786816", "label" : "50. Pattison, D.I., Davies, M.J., Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds (2001) Chem. Res. Toxicol., 14, pp. 1453-1464", "listPosition" : 50, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786793, "link" : "/api/reference/19786793", "label" : "51. Thomas, E.L., Milligan, T.W., Joyner, R.E., Jefferson, M.M., Antibacterial activity of hydrogen peroxide and the lactoperoxidase-hydrogen peroxide-thiocyanate system against oral streptococci (1994) Infect. Immun., 62, pp. 529-535", "listPosition" : 51, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786792, "link" : "/api/reference/19786792", "label" : "52. Tenovuo, J., Makinen, K.K., Sievers, G., Antibacterial effect of lactoperoxidase and myeloperoxidase against Bacillus cereus (1985) Antimicrob. Agents Chemother., 27, pp. 96-101", "listPosition" : 52, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786791, "link" : "/api/reference/19786791", "label" : "53. Shin, K., Yamauchi, K., Teraguchi, S., Hayasawa, H., Imoto, I., Susceptibility of Helicobacter pylori and its urease activity to the peroxidase-hydrogen peroxide-thiocyanate antimicrobial system (2002) J. Med. Microbiol., 51, pp. 231-237", "listPosition" : 53, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786790, "link" : "/api/reference/19786790", "label" : "54. Haukioja, A., Ihalin, R., Loimaranta, V., Lenander, M., Tenovuo, J., Sensitivity of Helicobacter pylori to an innate defence mechanism, the lactoperoxidase system, in buffer and in human whole saliva (2004) J. Med. Microbiol., 53, pp. 855-860", "listPosition" : 54, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786789, "link" : "/api/reference/19786789", "label" : "55. Kirk, A.B., Dyke, J.V., Martin, C.F., Dasgupta, P.K., Temporal patterns in perchlorate, thiocyanate, and iodide excretion in human milk (2007) Environ. Health Perspect., 115, pp. 182-186", "listPosition" : 55, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786788, "link" : "/api/reference/19786788", "label" : "56. Minarowski, L., Sands, D., Minarowska, A., Karwowska, A., Sulewska, A., Gacko, M., Chyczewska, E., Thiocyanate concentration in saliva of cystic fibrosis patients (2008) Folia Histochem. Cytobiol., 46, pp. 245-246", "listPosition" : 56, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786787, "link" : "/api/reference/19786787", "label" : "57. Bafort, F., Parisi, O., Perraudin, J.P., Jijakli, M., Mode of action of lactoperoxidase as related to its antimicrobial activity: a review (2014) Enzyme research 2014", "listPosition" : 57, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786786, "link" : "/api/reference/19786786", "label" : "58. Love, D.T., Barrett, T.J., White, M.Y., Cordwell, S.J., Davies, M.J., Hawkins, C.L., Cellular targets of the myeloperoxidase-derived oxidant hypothiocyanous acid (HOSCN) and its role in the inhibition of glycolysis in macrophages (2016) Free Radic. Biol. Med., 94, pp. 88-98", "listPosition" : 58, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786785, "link" : "/api/reference/19786785", "label" : "59. Skaff, O., Pattison, D.I., Morgan, P.E., Bachana, R., Jain, V.K., Priyadarsini, K.I., Davies, M.J., Selenium-containing amino acids are targets for myeloperoxidase-derived hypothiocyanous acid: determination of absolute rate constants and implications for biological damage (2012) Biochem. J., 441, pp. 305-316", "listPosition" : 59, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786784, "link" : "/api/reference/19786784", "label" : "60. Skaff, O., Pattison, D.I., Davies, M.J., Hypothiocyanous acid reactivity with low-molecular-mass and protein thiols: absolute rate constants and assessment of biological relevance (2009) Biochem. J., 422, pp. 111-117", "listPosition" : 60, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786783, "link" : "/api/reference/19786783", "label" : "61. Barrett, T.J., Hawkins, C.L., Hypothiocyanous acid: benign or deadly? (2012) Chem. Res. Toxicol., 25, pp. 263-273", "listPosition" : 61, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786782, "link" : "/api/reference/19786782", "label" : "62. Hawkins, C.L., The role of hypothiocyanous acid (HOSCN) in biological systems (2009) Free Radic. Res., 43, pp. 1147-1158", "listPosition" : 62, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786781, "link" : "/api/reference/19786781", "label" : "63. Nagy, P., Jameson, G.N., Winterbourn, C.C., Kinetics and mechanisms of the reaction of hypothiocyanous acid with 5-thio-2-nitrobenzoic acid and reduced glutathione (2009) Chem. Res. Toxicol., 22, pp. 1833-1840", "listPosition" : 63, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786780, "link" : "/api/reference/19786780", "label" : "64. Tenovuo, J., Pruitt, K.M., Mansson-Rahemtulla, B., Harrington, P., Baldone, D.C., Products of thiocyanate peroxidation: properties and reaction mechanisms (1986) Biochim. Biophys. Acta, 870, pp. 377-384", "listPosition" : 64, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786779, "link" : "/api/reference/19786779", "label" : "65. Haddadin, M., Ibrahim, S.A., Robinson, R., Preservation of raw milk by activation of the natural lactoperoxidase systems (1996) Food Contr., 7, pp. 149-152", "listPosition" : 65, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786778, "link" : "/api/reference/19786778", "label" : "66. Wilks, M., Wiggins, R., Whiley, A., Hennessy, E., Warwick, S., Porter, H., Corfield, A., Millar, M., Identification and H2O2 production of vaginal lactobacilli from pregnant women at high risk of preterm birth and relation with outcome (2004) J. Clin. Microbiol., 42, pp. 713-717", "listPosition" : 66, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786777, "link" : "/api/reference/19786777", "label" : "67. Pendharkar, S., Magopane, T., Larsson, P.G., de Bruyn, G., Gray, G.E., Hammarstrom, L., Marcotte, H., Identification and characterisation of vaginal lactobacilli from South African women (2013) BMC Infect. Dis., 13, p. 43", "listPosition" : 67, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786776, "link" : "/api/reference/19786776", "label" : "68. Fang, F., Xu, J., Li, Q., Xia, X., Du, G., Characterization of a Lactobacillus brevis strain with potential oral probiotic properties (2018) BMC Microbiol., 18, p. 221", "listPosition" : 68, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786775, "link" : "/api/reference/19786775", "label" : "69. Herrero, E.R., Slomka, V., Bernaerts, K., Boon, N., Hernandez-Sanabria, E., Passoni, B.B., Quirynen, M., Teughels, W., Antimicrobial effects of commensal oral species are regulated by environmental factors (2016) J. Dent., 47, pp. 23-33", "listPosition" : 69, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786774, "link" : "/api/reference/19786774", "label" : "70. Hillman, J., Socransky, S., Shivers, M., The relationships between streptococcal species and periodontopathic bacteria in human dental plaque (1985) Arch. Oral Biol., 30, pp. 791-795", "listPosition" : 70, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786773, "link" : "/api/reference/19786773", "label" : "71. Sbordone, L., Bortolaia, C., Oral microbial biofilms and plaque-related diseases: microbial communities and their role in the shift from oral health to disease (2003) Clin. Oral Invest., 7, pp. 181-188", "listPosition" : 71, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786772, "link" : "/api/reference/19786772", "label" : "72. Rashad, A.L., Toffler, W.L., Wolf, N., Thornburg, K., Kirk, E.P., Ellis, G., Whitehead, W., Vaginal Po2 in healthy women and in women infected withTrichomonas vaginalis: potential implications for metronidazole therapy (1992) Am. J. Obstet. Gynecol., 166, pp. 620-624", "listPosition" : 72, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786771, "link" : "/api/reference/19786771", "label" : "73. Strus, M., Brzychczy-Włoch, M., Gosiewski, T., Kochan, P., Heczko, P.B., The in vitro effect of hydrogen peroxide onvaginal microbial communities (2006) FEMS Immunol. Med. Microbiol., 48, pp. 56-63", "listPosition" : 73, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786770, "link" : "/api/reference/19786770", "label" : "74. Liu, X., Ramsey, M.M., Chen, X., Koley, D., Whiteley, M., Bard, A.J., Real-time mapping of a hydrogen peroxide concentration profile across a polymicrobial bacterial biofilm using scanning electrochemical microscopy (2011) Proc. Natl. Acad. Sci. Unit. States Am., 108, pp. 2668-2673", "listPosition" : 74, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786769, "link" : "/api/reference/19786769", "label" : "75. Kreth, J., Zhang, Y., Herzberg, M.C., Streptococcal antagonism in oral biofilms: Streptococcus sanguinis and Streptococcus gordonii interference with Streptococcus mutans (2008) J. Bacteriol., 190, pp. 4632-4640", "listPosition" : 75, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786768, "link" : "/api/reference/19786768", "label" : "76. Carlsson, J., Edlund, M.B.K., Pyruvate oxidase in Streptococcus sanguis under various growth conditions (1987) Oral Microbiol. Immunol., 2, pp. 10-14", "listPosition" : 76, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786767, "link" : "/api/reference/19786767", "label" : "77. Al-Shehri, S.S., Sweeney, E.L., Cowley, D.M., Liley, H.G., Ranasinghe, P.D., Charles, B.G., Shaw, P.N., Knox, C.L., Deep sequencing of the 16S ribosomal RNA of the neonatal oral microbiome: a comparison of breast-fed and formula-fed infants (2016) Sci. Rep., 6, p. 38309", "listPosition" : 77, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786766, "link" : "/api/reference/19786766", "label" : "78. Ozturk, G., Shah, I.M., Mills, D.A., German, J.B., de Moura Bell, J., The antimicrobial activity of bovine milk xanthine oxidase (2020) Int. Dairy J., 102, p. 104581", "listPosition" : 78, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786765, "link" : "/api/reference/19786765", "label" : "79. Sweeney, E.L., Al-Shehri, S.S., Cowley, D.M., Liley, H.G., Bansal, N., Charles, B.G., Shaw, P.N., Knox, C.L., The effect of breastmilk and saliva combinations on the in vitro growth of oral pathogenic and commensal microorganisms (2018) Sci. Rep., 8, p. 15112", "listPosition" : 79, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786764, "link" : "/api/reference/19786764", "label" : "80. Gila-Diaz, A., Arribas, S.M., Algara, A., Martín-Cabrejas, M.A., López de Pablo, Á.L., Sáenz de Pipaón, M., Ramiro-Cortijo, D., A review of bioactive factors in human breastmilk: a focus on prematurity (2019) Nutrients, 11, p. 1307", "listPosition" : 80, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786763, "link" : "/api/reference/19786763", "label" : "81. Al-Kerwi, E.A., Al-Hashimi, A.H., Salman, A.M., Mother's milk and hydrogen peroxide (2005) Asia Pac. J. Clin. Nutr., 14, pp. 428-431", "listPosition" : 81, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786762, "link" : "/api/reference/19786762", "label" : "82. Silanikove, N., Shapiro, F., Leitner, G., Posttranslational ruling of xanthine oxidase activity in bovine milk by its substrates (2007) Biochem. Biophys. Res. Commun., 363, pp. 561-565", "listPosition" : 82, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786761, "link" : "/api/reference/19786761", "label" : "83. Ha, E.M., Oh, C.T., Bae, Y.S., Lee, W.J., A direct role for dual oxidase in Drosophila gut immunity (2005) Science, 310, pp. 847-850", "listPosition" : 83, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786760, "link" : "/api/reference/19786760", "label" : "84. Corcionivoschi, N., Alvarez, L.A., Sharp, T.H., Strengert, M., Alemka, A., Mantell, J., Verkade, P., Bourke, B., Mucosal reactive oxygen species decrease virulence by disrupting Campylobacter jejuni phosphotyrosine signaling (2012) Cell Host Microbe, 12, pp. 47-59", "listPosition" : 84, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786759, "link" : "/api/reference/19786759", "label" : "85. Gattas, M.V., Forteza, R., Fragoso, M.A., Fregien, N., Salas, P., Salathe, M., Conner, G.E., Oxidative epithelial host defense is regulated by infectious and inflammatory stimuli (2009) Free Radic. Biol. Med., 47, pp. 1450-1458", "listPosition" : 85, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786758, "link" : "/api/reference/19786758", "label" : "86. Boots, A.W., Hristova, M., Kasahara, D.I., Haenen, G.R., Bast, A., van der Vliet, A., ATP-mediated activation of the NADPH oxidase DUOX1 mediates airway epithelial responses to bacterial stimuli (2009) J. Biol. Chem., 284, pp. 17858-17867", "listPosition" : 86, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786757, "link" : "/api/reference/19786757", "label" : "87. Koff, J.L., Shao, M.X., Ueki, I.F., Nadel, J.A., Multiple TLRs activate EGFR via a signaling cascade to produce innate immune responses in airway epithelium (2008) Am. J. Physiol. Lung Cell Mol. Physiol., 294, pp. L1068-L1075", "listPosition" : 87, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786756, "link" : "/api/reference/19786756", "label" : "88. Rada, B., Leto, T.L., Oxidative innate immune defenses by Nox/Duox family NADPH oxidases (2008) Trends in Innate Immunity, pp. 164-187. , Karger Publishers", "listPosition" : 88, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786755, "link" : "/api/reference/19786755", "label" : "89. El Hassani, R.A., Benfares, N., Caillou, B., Talbot, M., Sabourin, J.-C., Belotte, V., Morand, S., Ohayon, R., Dual oxidase2 is expressed all along the digestive tract (2005) Am. J. Physiol. Gastrointest. Liver Physiol., 288, pp. G933-G942", "listPosition" : 89, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786754, "link" : "/api/reference/19786754", "label" : "90. Segal, B.H., Leto, T.L., Gallin, J.I., Malech, H.L., Holland, S.M., Genetic, biochemical, and clinical features of chronic granulomatous disease (2000) Medicine (Baltim.), 79, pp. 170-200", "listPosition" : 90, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786753, "link" : "/api/reference/19786753", "label" : "91. Winterbourn, C.C., The biological chemistry of hydrogen peroxide (2013) Methods Enzymol, pp. 3-25. , Elsevier", "listPosition" : 91, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786752, "link" : "/api/reference/19786752", "label" : "92. Bienert, G.P., Moller, A.L., Kristiansen, K.A., Schulz, A., Moller, I.M., Schjoerring, J.K., Jahn, T.P., Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes (2007) J. Biol. Chem., 282, pp. 1183-1192", "listPosition" : 92, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786751, "link" : "/api/reference/19786751", "label" : "93. Makino, N., Sasaki, K., Hashida, K., Sakakura, Y., A metabolic model describing the H2O2 elimination by mammalian cells including H2O2 permeation through cytoplasmic and peroxisomal membranes: comparison with experimental data (2004) Biochim. Biophys. Acta Gen. Subj., 1673, pp. 149-159", "listPosition" : 93, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786750, "link" : "/api/reference/19786750", "label" : "94. Antunes, F., Cadenas, E., Estimation of H2O2 gradients across biomembranes (2000) FEBS Lett., 475, pp. 121-126", "listPosition" : 94, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786749, "link" : "/api/reference/19786749", "label" : "95. Reth, M., Hydrogen peroxide as second messenger in lymphocyte activation (2002) Nat. Immunol., 3, pp. 1129-1134", "listPosition" : 95, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786748, "link" : "/api/reference/19786748", "label" : "96. Bienert, G.P., Schjoerring, J.K., Jahn, T.P., Membrane transport of hydrogen peroxide (2006) Biochim. Biophys. Acta, 1758, pp. 994-1003", "listPosition" : 96, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786747, "link" : "/api/reference/19786747", "label" : "97. Johnston, R.B., Jr., Keele, B.B., Jr., Misra, H.P., Lehmeyer, J.E., Webb, L.S., Baehner, R.L., RaJagopalan, K.V., The role of superoxide anion generation in phagocytic bactericidal activity. Studies with normal and chronic granulomatous disease leukocytes (1975) J. Clin. Invest., 55, pp. 1357-1372", "listPosition" : 97, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786746, "link" : "/api/reference/19786746", "label" : "98. Imlay, J.A., Cellular defenses against superoxide and hydrogen peroxide (2008) Annu. Rev. Biochem., 77, pp. 755-776", "listPosition" : 98, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786745, "link" : "/api/reference/19786745", "label" : "99. Landes, M.B., Rajaram, M.V., Nguyen, H., Schlesinger, L.S., Role for NOD2 in Mycobacterium tuberculosis-induced iNOS expression and NO production in human macrophages (2015) J. Leukoc. Biol., 97, pp. 1111-1119", "listPosition" : 99, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786744, "link" : "/api/reference/19786744", "label" : "100. Rajaram, K., Nelson, D.E., Chlamydia muridarum infection of macrophages elicits bactericidal nitric oxide production via reactive oxygen species and cathepsin B (2015) Infect. Immun., 83, pp. 3164-3175", "listPosition" : 100, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786743, "link" : "/api/reference/19786743", "label" : "101. Smith, B.C., Underbakke, E.S., Kulp, D.W., Schief, W.R., Marletta, M.A., Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation (2013) Proc. Natl. Acad. Sci. U. S. A., 110, pp. E3577-E3586", "listPosition" : 101, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786742, "link" : "/api/reference/19786742", "label" : "102. Schmidt, P.P., Lange, R., Gorren, A.C., Werner, E.R., Mayer, B., Andersson, K.K., Formation of a protonated trihydrobiopterin radical cation in the first reaction cycle of neuronal and endothelial nitric oxide synthase detected by electron paramagnetic resonance spectroscopy (2001) J. Biol. Inorg. Chem., 6, pp. 151-158", "listPosition" : 102, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786741, "link" : "/api/reference/19786741", "label" : "103. Stuehr, D., Pou, S., Rosen, G.M., Oxygen reduction by nitric-oxide synthases (2001) J. Biol. Chem., 276, pp. 14533-14536", "listPosition" : 103, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786740, "link" : "/api/reference/19786740", "label" : "104. Klatt, P., Pfeiffer, S., List, B.M., Lehner, D., Glatter, O., Bachinger, H.P., Werner, E.R., Mayer, B., Characterization of heme-deficient neuronal nitric-oxide synthase reveals a role for heme in subunit dimerization and binding of the amino acid substrate and tetrahydrobiopterin (1996) J. Biol. Chem., 271, pp. 7336-7342", "listPosition" : 104, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786739, "link" : "/api/reference/19786739", "label" : "105. Vasquez-Vivar, J., Hogg, N., Martasek, P., Karoui, H., Pritchard, K.A., Jr., Kalyanaraman, B., Tetrahydrobiopterin-dependent inhibition of superoxide generation from neuronal nitric oxide synthase (1999) J. Biol. Chem., 274, pp. 26736-26742", "listPosition" : 105, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786738, "link" : "/api/reference/19786738", "label" : "106. Calabrese, V., Mancuso, C., Calvani, M., Rizzarelli, E., Butterfield, D.A., Stella, A.M., Nitric oxide in the central nervous system: neuroprotection versus neurotoxicity (2007) Nat. Rev. Neurosci., 8, pp. 766-775", "listPosition" : 106, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786737, "link" : "/api/reference/19786737", "label" : "107. Forstermann, U., Sessa, W.C., Nitric oxide synthases: regulation and function (2012) Eur. Heart J., 33, pp. 829-837. , 837a-837d", "listPosition" : 107, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786736, "link" : "/api/reference/19786736", "label" : "108. Winterbourn, C.C., Hampton, M.B., Livesey, J.H., Kettle, A.J., Modeling the reactions of superoxide and myeloperoxidase in the neutrophil phagosome: implications for microbial killing (2006) J. Biol. Chem., 281, pp. 39860-39869", "listPosition" : 108, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786735, "link" : "/api/reference/19786735", "label" : "109. Winterbourn, C.C., Kettle, A.J., Redox reactions and microbial killing in the neutrophil phagosome (2013) Antioxidants Redox Signal., 18, pp. 642-660", "listPosition" : 109, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786734, "link" : "/api/reference/19786734", "label" : "110. van der Vliet, A., Eiserich, J.P., Halliwell, B., Cross, C.E., Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity (1997) J. Biol. Chem., 272, pp. 7617-7625", "listPosition" : 110, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786733, "link" : "/api/reference/19786733", "label" : "111. Furtmuller, P.G., Zederbauer, M., Jantschko, W., Helm, J., Bogner, M., Jakopitsch, C., Obinger, C., Active site structure and catalytic mechanisms of human peroxidases (2006) Arch. Biochem. Biophys., 445, pp. 199-213", "listPosition" : 111, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786732, "link" : "/api/reference/19786732", "label" : "112. Nauseef, W.M., Biosynthesis of human myeloperoxidase (2018) Arch. Biochem. Biophys., 642, pp. 1-9", "listPosition" : 112, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786731, "link" : "/api/reference/19786731", "label" : "113. Shin, K., Hayasawa, H., Lonnerdal, B., Purification and quantification of lactoperoxidase in human milk with use of immunoadsorbents with antibodies against recombinant human lactoperoxidase (2001) Am. J. Clin. Nutr., 73, pp. 984-989", "listPosition" : 113, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786730, "link" : "/api/reference/19786730", "label" : "114. Kussendrager, K.D., van Hooijdonk, A.C., Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications (2000) Br. J. Nutr., 84, pp. S19-S25", "listPosition" : 114, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786729, "link" : "/api/reference/19786729", "label" : "115. Battistuzzi, G., Bellei, M., Bortolotti, C.A., Sola, M., Redox properties of heme peroxidases (2010) Arch. Biochem. Biophys., 500, pp. 21-36", "listPosition" : 115, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786728, "link" : "/api/reference/19786728", "label" : "116. Davies, M.J., Hawkins, C.L., Pattison, D.I., Rees, M.D., Mammalian heme peroxidases: from molecular mechanisms to health implications (2008) Antioxidants Redox Signal., 10, pp. 1199-1234", "listPosition" : 116, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786727, "link" : "/api/reference/19786727", "label" : "117. Furtmuller, P.G., Jantschko, W., Regelsberger, G., Jakopitsch, C., Arnhold, J., Obinger, C., Reaction of lactoperoxidase compound I with halides and thiocyanate (2002) Biochemistry, 41, pp. 11895-11900", "listPosition" : 117, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786726, "link" : "/api/reference/19786726", "label" : "118. O'Brien, P.J., Peroxidases (2000) Chem. Biol. Interact., 129, pp. 113-139", "listPosition" : 118, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786725, "link" : "/api/reference/19786725", "label" : "119. Augsburger, F., Filippova, A., Jaquet, V., Methods for detection of NOX-derived superoxide radical anion and hydrogen peroxide in cells (2019) NADPH Oxidases, pp. 233-241. , Springer", "listPosition" : 119, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786724, "link" : "/api/reference/19786724", "label" : "120. Takac, I., Schröder, K., Zhang, L., Lardy, B., Anilkumar, N., Lambeth, J.D., Shah, A.M., Brandes, R.P., The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4 (2011) J. Biol. Chem., 286, pp. 13304-13313", "listPosition" : 120, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786723, "link" : "/api/reference/19786723", "label" : "121. Brandes, R.P., Weissmann, N., Schroder, K., Nox family NADPH oxidases: molecular mechanisms of activation (2014) Free Radic. Biol. Med., 76, pp. 208-226", "listPosition" : 121, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786722, "link" : "/api/reference/19786722", "label" : "122. Garcia-Redondo, A.B., Aguado, A., Briones, A.M., Salaices, M., NADPH oxidases and vascular remodeling in cardiovascular diseases (2016) Pharmacol. Res., 114, pp. 110-120", "listPosition" : 122, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786721, "link" : "/api/reference/19786721", "label" : "123. Song, Y., Ruf, J., Lothaire, P., Dequanter, D., Andry, G., Willemse, E., Dumont, J.E., De Deken, X., Association of duoxes with thyroid peroxidase and its regulation in thyrocytes (2010) J. Clin. Endocrinol. Metab., 95, pp. 375-382", "listPosition" : 123, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786720, "link" : "/api/reference/19786720", "label" : "124. Landry, W.D., Cotter, T.G., ROS Signalling, NADPH Oxidases and Cancer (2014), Portland Press Limited", "listPosition" : 124, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786719, "link" : "/api/reference/19786719", "label" : "125. Reddy, M.M., Fernandes, M.S., Salgia, R., Levine, R.L., Griffin, J.D., Sattler, M., NADPH oxidases regulate cell growth and migration in myeloid cells transformed by oncogenic tyrosine kinases (2011) Leukemia, 25, pp. 281-289", "listPosition" : 125, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786718, "link" : "/api/reference/19786718", "label" : "126. Bedard, K., Krause, K.H., The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology (2007) Physiol. Rev., 87, pp. 245-313", "listPosition" : 126, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786717, "link" : "/api/reference/19786717", "label" : "127. Rigutto, S., Hoste, C., Grasberger, H., Milenkovic, M., Communi, D., Dumont, J.E., Corvilain, B., De Deken, X., Activation of dual oxidases Duox1 and Duox2: differential regulation mediated by camp-dependent protein kinase and protein kinase C-dependent phosphorylation (2009) J. Biol. Chem., 284, pp. 6725-6734", "listPosition" : 127, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786716, "link" : "/api/reference/19786716", "label" : "128. Ameziane-El-Hassani, R., Morand, S., Boucher, J.-L., Frapart, Y.-M., Apostolou, D., Agnandji, D., Gnidehou, S., Francon, J., Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity (2005) J. Biol. Chem., 280, pp. 30046-30054", "listPosition" : 128, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786715, "link" : "/api/reference/19786715", "label" : "129. Touyz, R.M., Anagnostopoulou, A., Rios, F., Montezano, A.C., Camargo, L.L., NOX5: molecular biology and pathophysiology (2019) Exp. Physiol., 104, pp. 605-616", "listPosition" : 129, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786714, "link" : "/api/reference/19786714", "label" : "130. Lambeth, J.D., NOX enzymes and the biology of reactive oxygen (2004) Nat. Rev. Immunol., 4, pp. 181-189", "listPosition" : 130, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786713, "link" : "/api/reference/19786713", "label" : "131. Li, H., Samouilov, A., Liu, X., Zweier, J.L., Characterization of the magnitude and kinetics of xanthine oxidase-catalyzed nitrite reduction. Evaluation of its role in nitric oxide generation in anoxic tissues (2001) J. Biol. Chem., 276, pp. 24482-24489", "listPosition" : 131, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786712, "link" : "/api/reference/19786712", "label" : "132. Millar, T.M., Stevens, C.R., Benjamin, N., Eisenthal, R., Harrison, R., Blake, D.R., Xanthine oxidoreductase catalyses the reduction of nitrates and nitrite to nitric oxide under hypoxic conditions (1998) FEBS Lett., 427, pp. 225-228", "listPosition" : 132, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786711, "link" : "/api/reference/19786711", "label" : "133. Kelley, E.E., Khoo, N.K., Hundley, N.J., Malik, U.Z., Freeman, B.A., Tarpey, M.M., Hydrogen peroxide is the major oxidant product of xanthine oxidase (2010) Free Radic. Biol. Med., 48, pp. 493-498", "listPosition" : 133, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786710, "link" : "/api/reference/19786710", "label" : "134. Harrison, R., Physiological roles of xanthine oxidoreductase (2004) Drug Metab. Rev., 36, pp. 363-375", "listPosition" : 134, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786709, "link" : "/api/reference/19786709", "label" : "135. Vorbach, C., Harrison, R., Capecchi, M.R., Xanthine oxidoreductase is central to the evolution and function of the innate immune system (2003) Trends Immunol., 24, pp. 512-517", "listPosition" : 135, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786708, "link" : "/api/reference/19786708", "label" : "136. Harrison, R., Milk xanthine oxidase: properties and physiological roles (2006) Int. Dairy J., 16, pp. 546-554", "listPosition" : 136, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786707, "link" : "/api/reference/19786707", "label" : "137. Pritsos, C.A., Cellular distribution, metabolism and regulation of the xanthine oxidoreductase enzyme system (2000) Chem. Biol. Interact., 129, pp. 195-208", "listPosition" : 137, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786706, "link" : "/api/reference/19786706", "label" : "138. Nishino, T., Okamoto, K., Kawaguchi, Y., Hori, H., Matsumura, T., Eger, B.T., Pai, E.F., Nishino, T., Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant (2005) J. Biol. Chem., 280, pp. 24888-24894", "listPosition" : 138, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786705, "link" : "/api/reference/19786705", "label" : "139. Enroth, C., Eger, B.T., Okamoto, K., Nishino, T., Nishino, T., Pai, E.F., Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion (2000) Proc. Natl. Acad. Sci. U. S. A., 97, pp. 10723-10728", "listPosition" : 139, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786704, "link" : "/api/reference/19786704", "label" : "140. Hille, R., Structure and function of xanthine oxidoreductase (2006) Eur. J. Inorg. Chem., pp. 1913-1926", "listPosition" : 140, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786703, "link" : "/api/reference/19786703", "label" : "141. Barja, G., Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity (1999) J. Bioenerg. Biomembr., 31, pp. 347-366", "listPosition" : 141, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786702, "link" : "/api/reference/19786702", "label" : "142. Zmijewski, J.W., Lorne, E., Banerjee, S., Abraham, E., Participation of mitochondrial respiratory complex III in neutrophil activation and lung injury (2009) Am. J. Physiol. Lung Cell Mol. Physiol., 296, pp. L624-L634", "listPosition" : 142, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786701, "link" : "/api/reference/19786701", "label" : "143. Grivennikova, V.G., Vinogradov, A.D., Generation of superoxide by the mitochondrial Complex I (2006) Biochim. Biophys. Acta, 1757, pp. 553-561", "listPosition" : 143, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786700, "link" : "/api/reference/19786700", "label" : "144. Lambert, A.J., Brand, M.D., Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I) (2004) J. Biol. Chem., 279, pp. 39414-39420", "listPosition" : 144, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786699, "link" : "/api/reference/19786699", "label" : "145. Brand, M.D., The sites and topology of mitochondrial superoxide production (2010) Exp. Gerontol., 45, pp. 466-472", "listPosition" : 145, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786698, "link" : "/api/reference/19786698", "label" : "146. Cogliati, S., Lorenzi, I., Rigoni, G., Caicci, F., Soriano, M.E., Regulation of mitochondrial electron transport chain assembly (2018) J. Mol. Biol., 430, pp. 4849-4873", "listPosition" : 146, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786697, "link" : "/api/reference/19786697", "label" : "147. Korge, P., Calmettes, G., Weiss, J.N., Reactive oxygen species production in cardiac mitochondria after complex I inhibition: modulation by substrate-dependent regulation of the NADH/NAD(+) ratio (2016) Free Radic. Biol. Med., 96, pp. 22-33", "listPosition" : 147, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786696, "link" : "/api/reference/19786696", "label" : "148. Balaban, R.S., Nemoto, S., Finkel, T., Mitochondria, oxidants, and aging (2005) Cell, 120, pp. 483-495", "listPosition" : 148, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786695, "link" : "/api/reference/19786695", "label" : "149. Radi, R., Oxygen radicals, nitric oxide, and peroxynitrite: redox pathways in molecular medicine (2018) Proc. Natl. Acad. Sci. U. S. A., 115, pp. 5839-5848", "listPosition" : 149, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786694, "link" : "/api/reference/19786694", "label" : "150. Wang, G., Chloride flux in phagocytes (2016) Immunol. Rev., 273, pp. 219-231", "listPosition" : 150, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786693, "link" : "/api/reference/19786693", "label" : "151. Koppenol, W.H., The Haber-Weiss cycle–70 years later (2001) Redox Rep., 6, pp. 229-234", "listPosition" : 151, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786692, "link" : "/api/reference/19786692", "label" : "152. Fridovich, I., Superoxide anion radical (O· 2), superoxide dismutases, and related matters (1997) J. Biol. Chem., 272, pp. 18515-18517", "listPosition" : 152, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786691, "link" : "/api/reference/19786691", "label" : "153. Turrens, J.F., Mitochondrial formation of reactive oxygen species (2003) J. Physiol., 552, pp. 335-344", "listPosition" : 153, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786690, "link" : "/api/reference/19786690", "label" : "154. Slauch, J.M., How does the oxidative burst of macrophages kill bacteria? Still an open question (2011) Mol. Microbiol., 80, pp. 580-583", "listPosition" : 154, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786689, "link" : "/api/reference/19786689", "label" : "155. Stevens, C.R., Millar, T.M., Clinch, J.G., Kanczler, J.M., Bodamyali, T., Blake, D.R., Antibacterial properties of xanthine oxidase in human milk (2000) Lancet, 356, pp. 829-830", "listPosition" : 155, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786688, "link" : "/api/reference/19786688", "label" : "156. Rada, B., Leto, T.L., Characterization of hydrogen peroxide production by Duox in bronchial epithelial cells exposed to Pseudomonas aeruginosa (2010) FEBS Lett., 584, pp. 917-922", "listPosition" : 156, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786687, "link" : "/api/reference/19786687", "label" : "157. Conner, G.E., Salathe, M., Forteza, R., Lactoperoxidase and hydrogen peroxide metabolism in the airway (2002) Am. J. Respir. Crit. Care Med., 166, pp. S57-S61", "listPosition" : 157, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786686, "link" : "/api/reference/19786686", "label" : "158. Wijkstrom-Frei, C., El-Chemaly, S., Ali-Rachedi, R., Gerson, C., Cobas, M.A., Forteza, R., Salathe, M., Conner, G.E., Lactoperoxidase and human airway host defense (2003) Am. J. Respir. Cell Mol. Biol., 29, pp. 206-212", "listPosition" : 158, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786685, "link" : "/api/reference/19786685", "label" : "159. Sarr, D., Toth, E., Gingerich, A., Rada, B., Antimicrobial actions of dual oxidases and lactoperoxidase (2018) J. Microbiol., 56, pp. 373-386", "listPosition" : 159, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786684, "link" : "/api/reference/19786684", "label" : "160. Geiszt, M., Witta, J., Baffi, J., Lekstrom, K., Leto, T.L., Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense (2003) Faseb. J., 17, pp. 1502-1504", "listPosition" : 160, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786683, "link" : "/api/reference/19786683", "label" : "161. Welk, A., Rudolph, P., Kreth, J., Schwahn, C., Kramer, A., Below, H., Microbicidal efficacy of thiocyanate hydrogen peroxide after adding lactoperoxidase under saliva loading in the quantitative suspension test (2011) Arch. Oral Biol., 56, pp. 1576-1582", "listPosition" : 161, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786682, "link" : "/api/reference/19786682", "label" : "162. Al-Shehri, S.S., Duley, J.A., Bansal, N., Xanthine oxidase-lactoperoxidase system and innate immunity: biochemical actions and physiological roles (2020) Redox Biol, 34, p. 101524", "listPosition" : 162, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786681, "link" : "/api/reference/19786681", "label" : "163. Cieslak, M., Ferreira, C.H., Shifrin, Y., Pan, J., Belik, J., Human milk H 2 O 2 content: does it benefit preterm infants? (2018) Pediatr. Res., 83, p. 687", "listPosition" : 163, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786680, "link" : "/api/reference/19786680", "label" : "164. Palmerini, C.A., Marmottini, F., Arienti, G., Production of nitric oxide by human salivary peroxidase and by bovine lactoperoxidase (2012) J. Biochem. Mol. Toxicol., 26, pp. 87-93", "listPosition" : 164, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786679, "link" : "/api/reference/19786679", "label" : "165. Al-Shehri, S.S., Knox, C.L., Liley, H.G., Cowley, D.M., Wright, J.R., Henman, M.G., Hewavitharana, A.K., Duley, J.A., Breastmilk-saliva interactions boost innate immunity by regulating the oral microbiome in early infancy (2015) PloS One, 10", "listPosition" : 165, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786678, "link" : "/api/reference/19786678", "label" : "166. Carreras, M.C., Pargament, G.A., Catz, S.D., Poderoso, J.J., Boveris, A., Kinetics of nitric oxide and hydrogen peroxide production and formation of peroxynitrite during the respiratory burst of human neutrophils (1994) FEBS Lett., 341, pp. 65-68", "listPosition" : 166, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786677, "link" : "/api/reference/19786677", "label" : "167. Nauseef, W.M., Myeloperoxidase in human neutrophil host defence (2014) Cell Microbiol., 16, pp. 1146-1155", "listPosition" : 167, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786676, "link" : "/api/reference/19786676", "label" : "168. Thomas, D.C., The phagocyte respiratory burst: historical perspectives and recent advances (2017) Immunol. Lett., 192, pp. 88-96", "listPosition" : 168, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786675, "link" : "/api/reference/19786675", "label" : "169. Džoljić, E., Grabatinić, I., Kostić, V., Why is nitric oxide important for our brain? (2015) Funct. Neurol., 30, p. 159", "listPosition" : 169, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786674, "link" : "/api/reference/19786674", "label" : "170. Zang, Y., Popat, K.C., Reynolds, M.M., Nitric oxide-mediated fibrinogen deposition prevents platelet adhesion and activation (2018) Biointerphases, 13", "listPosition" : 170, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786673, "link" : "/api/reference/19786673", "label" : "171. Pinder, A.G., Pittaway, E., Morris, K., James, P.E., Nitrite directly vasodilates hypoxic vasculature via nitric oxide-dependent and -independent pathways (2009) Br. J. Pharmacol., 157, pp. 1523-1530", "listPosition" : 171, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786672, "link" : "/api/reference/19786672", "label" : "172. Thengchaisri, N., Kuo, L., Hydrogen peroxide induces endothelium-dependent and -independent coronary arteriolar dilation: role of cyclooxygenase and potassium channels (2003) Am. J. Physiol. Heart Circ. Physiol., 285, pp. H2255-H2263", "listPosition" : 172, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786671, "link" : "/api/reference/19786671", "label" : "173. Burke, T.M., Wolin, M.S., Hydrogen peroxide elicits pulmonary arterial relaxation and guanylate cyclase activation (1987) Am. J. Physiol., 252, pp. H721-H732", "listPosition" : 173, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786670, "link" : "/api/reference/19786670", "label" : "174. Fang, F.C., Antimicrobial reactive oxygen and nitrogen species: concepts and controversies (2004) Nat. Rev. Microbiol., 2, pp. 820-832", "listPosition" : 174, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786669, "link" : "/api/reference/19786669", "label" : "175. Lyle, A.N., Remus, E.W., Fan, A.E., Lassègue, B., Walter, G.A., Kiyosue, A., Griendling, K.K., Taylor, W.R., Hydrogen peroxide regulates osteopontin expression through activation of transcriptional and translational pathways (2014) J. Biol. Chem., 289, pp. 275-285", "listPosition" : 175, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786668, "link" : "/api/reference/19786668", "label" : "176. Gechev, T.S., Hille, J., Hydrogen peroxide as a signal controlling plant programmed cell death (2005) The Journal of cell biology, 168, pp. 17-20", "listPosition" : 176, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786667, "link" : "/api/reference/19786667", "label" : "177. Pan, Q., Qiu, W.Y., Huo, Y.N., Yao, Y.F., Lou, M.F., Low levels of hydrogen peroxide stimulate corneal epithelial cell adhesion, migration, and wound healing (2011) Invest. Ophthalmol. Vis. Sci., 52, pp. 1723-1734", "listPosition" : 177, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786666, "link" : "/api/reference/19786666", "label" : "178. Veal, E.A., Day, A.M., Morgan, B.A., Hydrogen peroxide sensing and signaling (2007) Mol Cell, 26, pp. 1-14", "listPosition" : 178, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786665, "link" : "/api/reference/19786665", "label" : "179. Asmat, U., Abad, K., Ismail, K., Diabetes mellitus and oxidative stress-A concise review (2016) Saudi Pharmaceut. J., 24, pp. 547-553", "listPosition" : 179, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786664, "link" : "/api/reference/19786664", "label" : "180. Reuter, S., Gupta, S.C., Chaturvedi, M.M., Aggarwal, B.B., Oxidative stress, inflammation, and cancer: how are they linked? (2010) Free Radic. Biol. Med., 49, pp. 1603-1616", "listPosition" : 180, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786663, "link" : "/api/reference/19786663", "label" : "181. Valko, M., Rhodes, C.J., Moncol, J., Izakovic, M., Mazur, M., Free radicals, metals and antioxidants in oxidative stress-induced cancer (2006) Chem. Biol. Interact., 160, pp. 1-40", "listPosition" : 181, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786662, "link" : "/api/reference/19786662", "label" : "182. Afanas’ ev, I., ROS and RNS signaling in heart disorders: could antioxidant treatment be successful? (2011) Oxid Med Cell Longev", "listPosition" : 182, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786661, "link" : "/api/reference/19786661", "label" : "183. Granger, D.N., Kvietys, P.R., Reperfusion injury and reactive oxygen species: the evolution of a concept (2015) Redox Biol, 6, pp. 524-551", "listPosition" : 183, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786660, "link" : "/api/reference/19786660", "label" : "184. Ahmad, W., Ijaz, B., Shabbiri, K., Ahmed, F., Rehman, S., Oxidative toxicity in diabetes and Alzheimer's disease: mechanisms behind ROS/RNS generation (2017) J. Biomed. Sci., 24, p. 76", "listPosition" : 184, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786659, "link" : "/api/reference/19786659", "label" : "185. Zhang, Y., Dawson, V.L., Dawson, T.M., Oxidative stress and genetics in the pathogenesis of Parkinson's disease (2000) Neurobiol. Dis., 7, pp. 240-250", "listPosition" : 185, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786658, "link" : "/api/reference/19786658", "label" : "186. Kausar, S., Wang, F., Cui, H., The role of mitochondria in reactive oxygen species generation and its implications for neurodegenerative diseases (2018) Cells, 7, p. 274", "listPosition" : 186, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786657, "link" : "/api/reference/19786657", "label" : "187. Tan, B.L., Norhaizan, M.E., Liew, W.P., Sulaiman Rahman, H., Antioxidant and oxidative stress: a mutual interplay in age-related diseases (2018) Front. Pharmacol., 9, p. 1162", "listPosition" : 187, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786656, "link" : "/api/reference/19786656", "label" : "188. Irshad, M., Chaudhuri, P.S., Oxidant-antioxidant system: role and significance in human body (2002) Indian J. Exp. Biol., 40, pp. 1233-1239", "listPosition" : 188, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786655, "link" : "/api/reference/19786655", "label" : "189. Chaudiere, J., Ferrari-Iliou, R., Intracellular antioxidants: from chemical to biochemical mechanisms (1999) Food Chem. Toxicol., 37, pp. 949-962", "listPosition" : 189, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786654, "link" : "/api/reference/19786654", "label" : "190. Samardzic, K., Rodgers, K.J., Oxidised protein metabolism: recent insights (2017) Biol. Chem., 398, pp. 1165-1175", "listPosition" : 190, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786653, "link" : "/api/reference/19786653", "label" : "191. Cadet, J., Davies, K.J.A., Oxidative DNA damage & repair: an introduction (2017) Free Radic. Biol. Med., 107, pp. 2-12", "listPosition" : 191, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786652, "link" : "/api/reference/19786652", "label" : "192. Zhu, L., Kreth, J., The role of hydrogen peroxide in environmental adaptation of oral microbial communities (2012) Oxid Med Cell Longev, p. 717843", "listPosition" : 192, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786651, "link" : "/api/reference/19786651", "label" : "193. Sobko, T., Reinders, C.I., Jansson, E., Norin, E., Midtvedt, T., Lundberg, J.O., Gastrointestinal bacteria generate nitric oxide from nitrate and nitrite (2005) Nitric Oxide, 13, pp. 272-278", "listPosition" : 193, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786650, "link" : "/api/reference/19786650", "label" : "194. Pattison, D.I., Davies, M.J., Hawkins, C.L., Reactions and reactivity of myeloperoxidase-derived oxidants: differential biological effects of hypochlorous and hypothiocyanous acids (2012) Free Radic. Res., 46, pp. 975-995", "listPosition" : 194, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786649, "link" : "/api/reference/19786649", "label" : "195. De Deken, X., Corvilain, B., Dumont, J.E., Miot, F., Roles of DUOX-mediated hydrogen peroxide in metabolism, host defense, and signaling (2014) Antioxidants Redox Signal., 20, pp. 2776-2793", "listPosition" : 195, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786648, "link" : "/api/reference/19786648", "label" : "196. Bokoch, G.M., NADPH oxidases in innate immunity (2009) J Innate Immun, 1, pp. 507-508", "listPosition" : 196, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786647, "link" : "/api/reference/19786647", "label" : "197. Silanikove, N., Shapiro, F., Shamay, A., Leitner, G., Role of xanthine oxidase, lactoperoxidase, and NO in the innate immune system of mammary secretion during active involution in dairy cows: manipulation with casein hydrolyzates (2005) Free Radic. Biol. Med., 38, pp. 1139-1151", "listPosition" : 197, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786646, "link" : "/api/reference/19786646", "label" : "198. Del Rio, L.A., Lopez-Huertas, E., ROS generation in peroxisomes and its role in cell signaling (2016) Plant Cell Physiol., 57, pp. 1364-1376", "listPosition" : 198, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786645, "link" : "/api/reference/19786645", "label" : "199. Grivennikova, V.G., Vinogradov, A.D., Mitochondrial production of reactive oxygen species (2013) Biochemistry (Mosc.), 78, pp. 1490-1511", "listPosition" : 199, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786815, "link" : "/api/reference/19786815", "label" : "200. Hawkins, C.L., Pattison, D.I., Davies, M.J., Hypochlorite-induced oxidation of amino acids, peptides and proteins (2003) Amino Acids, 25, pp. 259-274", "listPosition" : 200, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786814, "link" : "/api/reference/19786814", "label" : "201. Kettle, A.J., Albrett, A.M., Chapman, A.L., Dickerhof, N., Forbes, L.V., Khalilova, I., Turner, R., Measuring chlorine bleach in biology and medicine (2014) Biochim. Biophys. Acta, 1840, pp. 781-793", "listPosition" : 201, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786813, "link" : "/api/reference/19786813", "label" : "202. Morgan, P.E., Pattison, D.I., Talib, J., Summers, F.A., Harmer, J.A., Celermajer, D.S., Hawkins, C.L., Davies, M.J., High plasma thiocyanate levels in smokers are a key determinant of thiol oxidation induced by myeloperoxidase (2011) Free Radic. Biol. Med., 51, pp. 1815-1822", "listPosition" : 202, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786812, "link" : "/api/reference/19786812", "label" : "203. Painter, R.G., Valentine, V.G., Lanson, N.A., Jr., Leidal, K., Zhang, Q., Lombard, G., Thompson, C., Wang, G., CFTR Expression in human neutrophils and the phagolysosomal chlorination defect in cystic fibrosis (2006) Biochemistry, 45, pp. 10260-10269", "listPosition" : 203, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786811, "link" : "/api/reference/19786811", "label" : "204. Sun, Y.T., Shieh, C.C., Delpire, E., Shen, M.R., K(+)-Cl(-) cotransport mediates the bactericidal activity of neutrophils by regulating NADPH oxidase activation (2012) J. Physiol., 590, pp. 3231-3243", "listPosition" : 204, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786810, "link" : "/api/reference/19786810", "label" : "205. Painter, R.G., Marrero, L., Lombard, G.A., Valentine, V.G., Nauseef, W.M., Wang, G., CFTR-mediated halide transport in phagosomes of human neutrophils (2010) J. Leukoc. Biol., 87, pp. 933-942", "listPosition" : 205, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786809, "link" : "/api/reference/19786809", "label" : "206. Hurst, J.K., What really happens in the neutrophil phagosome? (2012) Free Radic. Biol. Med., 53, pp. 508-520", "listPosition" : 206, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786808, "link" : "/api/reference/19786808", "label" : "207. Bos, A., Wever, R., Roos, D., Characterization and quantification of the peroxidase in human monocytes (1978) Biochim. Biophys. Acta, 525, pp. 37-44", "listPosition" : 207, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786807, "link" : "/api/reference/19786807", "label" : "208. Schultz, J., Kaminker, K., Myeloperoxidase of the leucocyte of normal human blood. I. Content and localization (1962) Arch. Biochem. Biophys., 96, pp. 465-467", "listPosition" : 208, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786806, "link" : "/api/reference/19786806", "label" : "209. Tunney, M.M., Payne, J.E., McGrath, S.J., Einarsson, G.G., Ingram, R.J., Gilpin, D.F., Juarez-Perez, V., Elborn, J.S., Activity of hypothiocyanite and lactoferrin (ALX-009) against respiratory cystic fibrosis pathogens in sputum (2018) J. Antimicrob. Chemother., 73, pp. 3391-3397", "listPosition" : 209, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786805, "link" : "/api/reference/19786805", "label" : "210. Moskwa, P., Lorentzen, D., Excoffon, K.J., Zabner, J., McCray, P.B., Jr., Nauseef, W.M., Dupuy, C., Bánfi, B., A novel host defense system of airways is defective in cystic fibrosis (2007) Am. J. Respir. Crit. Care Med., 175, pp. 174-183", "listPosition" : 210, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786804, "link" : "/api/reference/19786804", "label" : "211. Conner, G.E., Wijkstrom-Frei, C., Randell, S.H., Fernandez, V.E., Salathe, M., The lactoperoxidase system links anion transport to host defense in cystic fibrosis (2007) FEBS Lett., 581, pp. 271-278", "listPosition" : 211, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786803, "link" : "/api/reference/19786803", "label" : "212. Lorentzen, D., Durairaj, L., Pezzulo, A.A., Nakano, Y., Launspach, J., Stoltz, D.A., Zamba, G., Banfi, B., Concentration of the antibacterial precursor thiocyanate in cystic fibrosis airway secretions (2011) Free Radic. Biol. Med., 50, pp. 1144-1150", "listPosition" : 212, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786802, "link" : "/api/reference/19786802", "label" : "213. Cegolon, L., Investigating hypothiocyanite against SARS-CoV-2 (2020) Int. J. Hyg Environ. Health, 227, p. 113520", "listPosition" : 213, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786801, "link" : "/api/reference/19786801", "label" : "214. Patel, U., Gingerich, A., Widman, L., Sarr, D., Tripp, R.A., Rada, B., Susceptibility of influenza viruses to hypothiocyanite and hypoiodite produced by lactoperoxidase in a cell-free system (2018) PloS One, 13", "listPosition" : 214, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786800, "link" : "/api/reference/19786800", "label" : "215. Gingerich, A., Pang, L., Hanson, J., Dlugolenski, D., Streich, R., Lafontaine, E.R., Nagy, T., Rada, B., Hypothiocyanite produced by human and rat respiratory epithelial cells inactivates extracellular H1N2 influenza A virus (2016) Inflamm. Res., 65, pp. 71-80", "listPosition" : 215, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786799, "link" : "/api/reference/19786799", "label" : "216. Cegolon, L., Salata, C., Piccoli, E., Juarez, V., Palu, G., Mastrangelo, G., Calistri, A., In vitro antiviral activity of hypothiocyanite against A/H1N1/2009 pandemic influenza virus (2014) Int. J. Hyg Environ. Health, 217, pp. 17-22", "listPosition" : 216, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786798, "link" : "/api/reference/19786798", "label" : "217. Tanaka, T., Murakami, S., Kumura, H., Igarashi, I., Shimazaki, K., Parasiticidal activity of bovine lactoperoxidase against Toxoplasma gondii (2006) Biochem. Cell. Biol., 84, pp. 774-779", "listPosition" : 217, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786797, "link" : "/api/reference/19786797", "label" : "218. Malhotra, K., Salmon, D., Le Bras, J., Vilde, J.L., Susceptibility of Plasmodium falciparum to a peroxidase-mediated oxygen-dependent microbicidal system (1988) Infect. Immun., 56, pp. 3305-3309", "listPosition" : 218, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786796, "link" : "/api/reference/19786796", "label" : "219. Popper, L., Knorr, D., Inactivation of yeast and filamentous fungi by the lactoperoxidase-hydrogen peroxide-thiocyanate-system (1997) Nahrung, 41, pp. 29-33", "listPosition" : 219, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786795, "link" : "/api/reference/19786795", "label" : "220. Jacob, B.M., Antony, K.E., Sreekumar, B., Haridas, M., Thiocyanate mediated antifungal and antibacterial property of goat milk lactoperoxidase (2000) Life Sci., 66, pp. 2433-2439", "listPosition" : 220, "published" : false, "snippet" : true }, { "otype" : "Reference", "mtid" : 19786794, "link" : "/api/reference/19786794", "label" : "221. Villa, V., Legowo, A., Bintoro, V., Al-Baarri, A., Quality of fresh bovine milk after addition of hypothiocyanite-rich-solution from lactoperoxidase system (2014) Int. J. Dairy Sci., 9, pp. 24-31", "listPosition" : 221, "published" : false, "snippet" : true } ], "hasCitationDuplums" : false, "userChangeableUntil" : "2021-07-12T15:25:14.149+0000", "directInstitutesForSort" : "", "ownerAuthorCount" : 2, "ownerInstituteCount" : 19, "directInstituteCount" : 0, "authorCount" : 1, "contributorCount" : 0, "hasQualityFactor" : true, "link" : "/api/publication/31963233", "label" : "Al-Shehri S.S.. Reactive oxygen and nitrogen species and innate immune response. (2021) BIOCHIMIE 0300-9084 1638-6183 181 52-64", "template" : "