References

References1. Boussen H, Bouaouina N, Mokni-Baizig N, et al. [Nasopharyngeal carcinoma.] Recent data. Pathol Biol (Paris) 2005;53:45–51 [in French].2. Evans JL, Goldfine ID, Maddux BA, et al. Are oxidative stress-activated signaling pathways mediators of insulin resistance and beta-cell dysfunction? Diabetes 2003;52:1–8.EvansJL]]GoldfineID]]MadduxBA&etal;Are oxidative stress-activated signaling pathways mediators of insulin resistance and beta-cell dysfunction?Diabetes2003521-83. Sies H. Role of reactive oxygen species in biological processes. Klin Wochenschr 1991;69:965–968.SiesHRole of reactive oxygen species in biological processes.Klin Wochenschr199169965-9684. Valko M, Leibfritz D, Moncol J, et al. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol 2007;39:44–84.ValkoM]]LeibfritzD]]MoncolJ&etal;Free radicals and antioxidants in normal physiological functions and human disease.Int J Biochem Cell Biol20073944-845. Matés JM, Pérez-Gómez C, Núñez de Castro I. Antioxidant enzymes and human disease. Clin Biochem 1999;1411:385–400.MatésJM]]Pérez-GómezC]]Núñez de CastroIAntioxidant enzymes and human disease.Clin Biochem19991411385-4006. Ames BN. Dietary carcinogens and anticarcinogens. Oxygen radicals and degenerative disease. Science 1983;221:1256–1264.AmesBNDietary carcinogens and anticarcinogens. Oxygen radicals and degenerative disease.Science19832211256-12647. Raab-traub N. Epstein-Barr virus and nasopharyngeal carcinoma. Semin Cancer Biol 1992;3:297–307.Raab-traubNEpstein-Barr virus and nasopharyngeal carcinoma.Semin Cancer Biol19923297-3078. Middeldorp JM, Brink AA, van den Brule AJ, et al. Pathogenic roles for Epstein-Barr virus (EBV) gene products in EBV-associated proliferative disorders. Crit Rev Oncol Hematol 2003;45:1–36.MiddeldorpJM]]BrinkAA]]van den BruleAJ&etal;Pathogenic roles for Epstein-Barr virus (EBV) gene products in EBV-associated proliferative disorders.Crit Rev Oncol Hematol2003451-369. Henle G, Henle W. Epstein-Barr-Virus specific IgA serum antibodies as an outstanding feature of nasopharyngeal carcinoma. Int J Cancer 1976;17:1–7.HenleG]]HenleWEpstein-Barr-Virus specific IgA serum antibodies as an outstanding feature of nasopharyngeal carcinoma.Int J Cancer1976171-710. Rickinson AB, Kieff E. Eptein-Barr Virus, in Fields BN, Knipe DM, Howley PM (eds): Fields Virology. Philadelphia, PA, Lippincot-Raven Publishers, 1996, pp 2397–2446.RickinsonAB]]KieffEEptein-Barr Virus,Fields BN, Knipe DM, Howley PMFields Virology.Philadelphia, PALippincot-Raven Publishers19962397-244611. Jalbout M, Bel Hadj Jrad B, Bouaouina N, et al. Autoantibodies to tubulin are specifically associated with the young age onset of the nasopharyngeal carcinoma. Int J Cancer 2002;101:146–150.12. Niller HH, Wolf H, Minarovits J. Regulation and dysregulation of Epstein–Barr virus latency: implications for the development of autoimmune diseases. Autoimmunity 2008;41:298–328.NillerHH]]WolfH]]MinarovitsJRegulation and dysregulation of Epstein–Barr virus latency: implications for the development of autoimmune diseases.Autoimmunity200841298-32813. Ritter K, Kühl RJ, Semrau F, et al. Manganese superoxide dismutase as a target of auto-antibodies in acute Epstein-Barr virus infection. J Exp Med 1994;180:1995–1998.RitterK]]KühlRJ]]SemrauF&etal;Manganese superoxide dismutase as a target of auto-antibodies in acute Epstein-Barr virus infection.J Exp Med19941801995-199814. Semrau F, Kühl RJ, Ritter S, et al. Manganese superoxide dismutase (MnSOD) and auto-antibodies against MnSOD in acute viral infection. J Med Virol 1998;55:161–167.SemrauF]]KühlRJ]]RitterS&etal;Manganese superoxide dismutase (MnSOD) and auto-antibodies against MnSOD in acute viral infection.J Med Virol199855161-16715. Aebi H. Catalase in vitro. Methods Enzymol 1984;105:121–126.AebiHCatalase in vitro.Methods Enzymol1984105121-12616. Markland S, Markland G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974;47:469–474.MarklandS]]MarklandGInvolvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase.Eur J Biochem197447469-47417. Henle W, Henle G, Zajac BA, et al. Differential reactivity of human serums with early antigens induced by Epstein-Barr virus. Science 1970;169:188–190.HenleW]]HenleG]]ZajacBA&etal;Differential reactivity of human serums with early antigens induced by Epstein-Barr virus.Science1970169188-19018. Jiang X, Chen F. The effect of lipid peroxides and superoxide dismutase in systemic lupus erythematosus: a preliminary study. Clin immunol immunopathol 1992;63:39–44.JiangX]]ChenFThe effect of lipid peroxides and superoxide dismutase in systemic lupus erythematosus: a preliminary study.Clin immunol immunopathol19926339-4419. Winterbourn CC, Stern A. Human red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical. J Clin Invest 1987;80:1486–1491.WinterbournCC]]SternAHuman red cells scavenge extracellular hydrogen peroxide and inhibit formation of hypochlorous acid and hydroxyl radical.J Clin Invest1987801486-149120. Marklund SL. Expression of extracellular superoxide dismutase by human cell lines. Biochem J 1990;266:213–219.MarklundSLExpression of extracellular superoxide dismutase by human cell lines.Biochem J1990266213-21921. Taysi S, Kocer I, Memisogullari R, et al. Serum oxidant/antioxidant status in patients with Behçet’s disease. Ann Clin Lab Sci 2002;32:377–382.TaysiS]]KocerI]]MemisogullariR&etal;Serum oxidant/antioxidant status in patients with Behçet’s disease.Ann Clin Lab Sci200232377-38222. Yasmineh WG, Parkin JL, Caspers JI, et al. Tumor necrosis factor/cachectin decreases catalase activity of rat liver. Cancer Res 1991;51:3990–3995.YasminehWG]]ParkinJL]]CaspersJI&etal;Tumor necrosis factor/cachectin decreases catalase activity of rat liver.Cancer Res1991513990-399523. Karlsson K, Marklund SL. Heparin-induced release of extracellular superoxide dismutase to human blood plasma. Biochem J 1987;242: 55–59.KarlssonK]]MarklundSLHeparin-induced release of extracellular superoxide dismutase to human blood plasma.Biochem J198724255-5924. Kokkaliari M, Fawibe O, Berry H, et al. Serum catalase as the protective agent against inactivation of alpha 1-proteinase inhibitor by hydrogen peroxide; comparison between normal and rheumatoid sera. Biochem Int 1992;28:219–227.KokkaliariM]]FawibeO]]BerryH&etal;Serum catalase as the protective agent against inactivation of alpha 1-proteinase inhibitor by hydrogen peroxide; comparison between normal and rheumatoid sera.Biochem Int199228219-22725. Su Y, Xia YF, Yang HL, et al. [Changes of superoxide dismutase (SOD) and metallothionien (MT) before, during, and after radiotherapy for nasopharyngeal carcinoma and their significance.] Ai Zheng 2003;22:629–633 [in Chinese].26. Zhang M, Liu L, Cheng L, et al. [Express of plasma ROS, SOD and GSH-PX in patients with nasopharyngeal carcinoma.] Lin Chuang Er Bi Yan Hou Ke Za Zhi 2003;17:650–651 [in Chinese].27. Schaade L, Meilicke R, Büttgen S, et al. [Manganese superoxide dismutase-inhibiting auto-antibodies in cholestatic Epstein-Barr viral hepatitis.] Dtsch Med Wochenschr 1998;123:1478–1482 [in German].28. Karray H, Ayadi W, Fki L, et al. Comparison of three different serological techniques for primary diagnosis and monitoring of nasopharyngeal carcinoma in two age groups from Tunisia. J Med Virol 2005;75:593–602.KarrayH]]AyadiW]]FkiL&etal;Comparison of three different serological techniques for primary diagnosis and monitoring of nasopharyngeal carcinoma in two age groups from Tunisia.J Med Virol200575593-60229. Fujiwara N, Nakano M, Kato S, et al. Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase. J Biol Chem 2007;282:35933–35944.FujiwaraN]]NakanoM]]KatoS&etal;Oxidative modification to cysteine sulfonic acid of Cys111 in human copper-zinc superoxide dismutase.J Biol Chem200728235933-3594430. Orth T, Kellner R, Diekmann O, et al. Identification and characterization of auto-antibodies against catalase and alpha-enolase in patients with primary sclerosing cholangitis. Clin Exp Immunol 1998;112:507–515.OrthT]]KellnerR]]DiekmannO&etal;Identification and characterization of auto-antibodies against catalase and alpha-enolase in patients with primary sclerosing cholangitis.Clin Exp Immunol1998112507-51531. Roozendaal C, Zhao MH, Horst G, et al. Catalase and alpha-enolase: two novel granulocyte autoantigens in inflammatory bowel disease (IBD). Clin Exp Immunol 1998;1:10–16.RoozendaalC]]ZhaoMH]]HorstG&etal;Catalase and alpha-enolase: two novel granulocyte autoantigens in inflammatory bowel disease (IBD).Clin Exp Immunol1998110-1632. Mansour RB, Lassoued S, Gargouri B, et al. Increased levels of autoantibodies against catalase and superoxide dismutase associated with oxidative stress in patients with rheumatoid arthritis and systemic lupus erythematosus. Scand J Rheumatol 2008;37:103–108.MansourRB]]LassouedS]]GargouriB&etal;Increased levels of autoantibodies against catalase and superoxide dismutase associated with oxidative stress in patients with rheumatoid arthritis and systemic lupus erythematosus.Scand J Rheumatol200837103-10833. D’souza A, Kurien BT, Rodgers R, et al. Detection of catalase as a major protein target of the lipid peroxidation product 4-HNE and the lack of its genetic association as a risk factor in SLE. BMC Med Genet 2008;9:62.D’souzaA]]KurienBT]]RodgersR&etal;Detection of catalase as a major protein target of the lipid peroxidation product 4-HNE and the lack of its genetic association as a risk factor in SLE.BMC Med Genet200896234. Gargouri B, Van Pelt J, El feki A, et al. Induction of Epstein Barr Virus (EBV) lytic cycle in vitro causes oxidative stress in lymphoblastoïde B cell lines. Mol Cell Biochem 2009;324:55–63.GargouriB]]Van PeltJ]]El fekiA&etal;Induction of Epstein Barr Virus (EBV) lytic cycle in vitro causes oxidative stress in lymphoblastoïde B cell lines.Mol Cell Biochem200932455-6335. Lassoued S, Ben Ameur R, Ayadi W, et al. Epstein-Barr virus induces an oxidative stress during the early stages of infection in B lymphocytes, epithelial, and lymphoblastoid cell lines. Mol Cell Biochem 2008;313:179–186.LassouedS]]Ben AmeurR]]AyadiW&etal;Epstein-Barr virus induces an oxidative stress during the early stages of infection in B lymphocytes, epithelial, and lymphoblastoid cell lines.Mol Cell Biochem2008313179-186