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Volumn 12, Issue 8, 2016, Pages 485-494

NADPH oxidases: New actors in thyroid cancer?

Author keywords

[No Author keywords available]

Indexed keywords

DUAL OXIDASE; OXIDOREDUCTASE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE 4; TUMOR MARKER; UNCLASSIFIED DRUG; HYDROGEN PEROXIDE; IODIDE PEROXIDASE;

EID: 84968626434     PISSN: 17595029     EISSN: 17595037     Source Type: Journal    
DOI: 10.1038/nrendo.2016.64     Document Type: Review
Times cited : (71)

References (125)
  • 1
    • 0019406986 scopus 로고
    • Iodination of thyroglobulin: An intracellular or extracellular process?
    • Ekholm, R. Iodination of thyroglobulin: an intracellular or extracellular process? Mol. Cell. Endocrinol. 24, 141-163 (1981).
    • (1981) Mol. Cell. Endocrinol , vol.24 , pp. 141-163
    • Ekholm, R.1
  • 2
    • 0033601327 scopus 로고    scopus 로고
    • Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs
    • Dupuy, C. et al. Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cDNAs. J. Biol. Chem. 274, 37265-37269 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 37265-37269
    • Dupuy, C.1
  • 3
    • 0034725643 scopus 로고    scopus 로고
    • Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family
    • De Deken, X. et al. Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. J. Biol. Chem. 275, 23227-23233 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 23227-23233
    • De Deken, X.1
  • 4
    • 77449129856 scopus 로고    scopus 로고
    • Intracellular expression of reactive oxygen species-generating NADPH oxidase NOX4 in normal and cancer thyroid tissues
    • Weyemi, U. et al. Intracellular expression of reactive oxygen species-generating NADPH oxidase NOX4 in normal and cancer thyroid tissues. Endocr. Relat. Cancer 17, 27-37 (2010).
    • (2010) Endocr. Relat. Cancer , vol.17 , pp. 27-37
    • Weyemi, U.1
  • 5
    • 44949106317 scopus 로고    scopus 로고
    • Structure regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species
    • Sumimoto, H. Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species. FEBS J. 275, 3249-3277 (2008).
    • (2008) FEBS J , vol.275 , pp. 3249-3277
    • Sumimoto, H.1
  • 6
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. NOX enzymes and the biology of reactive oxygen. Nat. Rev. Immunol. 4, 181-189 (2004).
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 7
    • 84901036297 scopus 로고    scopus 로고
    • Roles of DUOX-mediated hydrogen peroxide in metabolism, host defense, and signaling
    • De Deken, X., Corvilain, B., Dumont, J. E., Miot, F. Roles of DUOX-mediated hydrogen peroxide in metabolism, host defense, and signaling. Antioxid. Redox Signal. 20, 2776-2793 (2014).
    • (2014) Antioxid. Redox Signal , vol.20 , pp. 2776-2793
    • De Deken, X.1    Corvilain, B.2    Dumont, J.E.3    Miot, F.4
  • 8
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K., Krause, K. H. The NOX family of ROS-generating NADPH oxidases: physiology and pathophysiology. Physiol. Rev. 87, 245-313 (2007).
    • (2007) Physiol. Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 9
    • 84921932554 scopus 로고    scopus 로고
    • DNA replication stress as a hallmark of cancer
    • Macheret, M., Halazonetis, T. D. DNA replication stress as a hallmark of cancer. Annu. Rev. Pathol. 10, 425-448 (2015).
    • (2015) Annu. Rev. Pathol , vol.10 , pp. 425-448
    • MacHeret, M.1    Halazonetis, T.D.2
  • 10
    • 33745144355 scopus 로고    scopus 로고
    • Deoxyribonucleic acid damage and spontaneous mutagenesis in the thyroid gland of rats and mice
    • Maier, J. et al. Deoxyribonucleic acid damage and spontaneous mutagenesis in the thyroid gland of rats and mice. Endocrinology 147, 3391-3397 (2006).
    • (2006) Endocrinology , vol.147 , pp. 3391-3397
    • Maier, J.1
  • 11
    • 34648824394 scopus 로고    scopus 로고
    • Mechanisms of disease: Hydrogen peroxide DNA damage and mutagenesis in the development of thyroid tumors
    • Krohn, K., Maier, J., Paschke, R. Mechanisms of disease: hydrogen peroxide, DNA damage and mutagenesis in the development of thyroid tumors. Nat. Clin. Pract. Endocrinol. Metab. 3, 713-720 (2007).
    • (2007) Nat. Clin. Pract. Endocrinol. Metab , vol.3 , pp. 713-720
    • Krohn, K.1    Maier, J.2    Paschke, R.3
  • 12
    • 84855947011 scopus 로고    scopus 로고
    • Evidence of oncogene-induced senescence in thyroid carcinogenesis
    • Vizioli, M. G. et al. Evidence of oncogene-induced senescence in thyroid carcinogenesis. Endocr. Relat. Cancer 18, 743-757 (2011).
    • (2011) Endocr. Relat. Cancer , vol.18 , pp. 743-757
    • Vizioli, M.G.1
  • 13
    • 38749090568 scopus 로고    scopus 로고
    • Foci formation of P53-binding protein 1 in thyroid tumors: Activation of genomic instability during thyroid carcinogenesis
    • Nakashima, M. et al. Foci formation of P53-binding protein 1 in thyroid tumors: activation of genomic instability during thyroid carcinogenesis. Int. J. Cancer 122, 1082-1088 (2008).
    • (2008) Int. J. Cancer , vol.122 , pp. 1082-1088
    • Nakashima, M.1
  • 14
    • 84885432843 scopus 로고    scopus 로고
    • Significance of p53-binding protein 1 (53BP1) expression in thyroid papillary microcarcinoma: Association with BRAFV600E mutation status
    • Mussazhanova, Z. et al. Significance of p53-binding protein 1 (53BP1) expression in thyroid papillary microcarcinoma: association with BRAFV600E mutation status. Histopathology 63, 726-734 (2013).
    • (2013) Histopathology , vol.63 , pp. 726-734
    • Mussazhanova, Z.1
  • 15
    • 84857790798 scopus 로고    scopus 로고
    • ROS-generating NADPH oxidase NOX4 is a critical mediator in oncogenic H-Ras-induced DNA damage and subsequent senescence
    • Weyemi, U. et al. ROS-generating NADPH oxidase NOX4 is a critical mediator in oncogenic H-Ras-induced DNA damage and subsequent senescence. Oncogene 31, 1117-1129 (2012).
    • (2012) Oncogene , vol.31 , pp. 1117-1129
    • Weyemi, U.1
  • 16
    • 84928152214 scopus 로고    scopus 로고
    • NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation
    • Ameziane-El-Hassani, R. et al. NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation. Proc. Natl Acad. Sci. USA 112, 5051-5056 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. 5051-5056
    • Ameziane-El-Hassani, R.1
  • 17
    • 77649250810 scopus 로고    scopus 로고
    • Nuclear redox signaling
    • Lukosz, M. et al. Nuclear redox signaling. Antioxid. Redox Signal. 12, 713-742 (2010).
    • (2010) Antioxid. Redox Signal , vol.12 , pp. 713-742
    • Lukosz, M.1
  • 18
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Veal, E. A., Day, A. M., Morgan, B. A. Hydrogen peroxide sensing and signaling. Mol. Cell 26, 1-14 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 19
    • 77957652745 scopus 로고    scopus 로고
    • Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
    • Miller, E. W., Dickinson, B. C., Chang, C. J. Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc. Natl Acad. Sci. USA 107, 15681-15686 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 15681-15686
    • Miller, E.W.1    Dickinson, B.C.2    Chang, C.J.3
  • 20
    • 0029394936 scopus 로고
    • Hydrogen peroxide and the proliferation of BHK-21 cells
    • Burdon, R. H., Alliangana, D., Gill, V. Hydrogen peroxide and the proliferation of BHK-21 cells. Free Radic. Res. 23, 471-486 (1995).
    • (1995) Free Radic. Res , vol.23 , pp. 471-486
    • Burdon, R.H.1    Alliangana, D.2    Gill, V.3
  • 21
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng, T. C., Fukada, T., Tonks, N. K. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 22
    • 48249149472 scopus 로고    scopus 로고
    • A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells
    • Boivin, B., Zhang, S., Arbiser, J. L., Zhang, Z. Y., Tonks, N. K. A modified cysteinyl-labeling assay reveals reversible oxidation of protein tyrosine phosphatases in angiomyolipoma cells. Proc. Natl Acad. Sci. USA 105, 9959-9964 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9959-9964
    • Boivin, B.1    Zhang, S.2    Arbiser, J.L.3    Zhang, Z.Y.4    Tonks, N.K.5
  • 23
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis, S., Curran, T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. EMBO J. 11, 653-665 (1992).
    • (1992) EMBO J , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 24
    • 84947748326 scopus 로고    scopus 로고
    • Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins
    • Verrastro, I., Tveen-Jensen, K., Woscholski, R., Spickett, C. M., Pitt, A. R. Reversible oxidation of phosphatase and tensin homolog (PTEN) alters its interactions with signaling and regulatory proteins. Free Radic. Biol. Med. 90, 24-34 (2015).
    • (2015) Free Radic. Biol. Med , vol.90 , pp. 24-34
    • Verrastro, I.1    Tveen-Jensen, K.2    Woscholski, R.3    Spickett, C.M.4    Pitt, A.R.5
  • 25
    • 0027361046 scopus 로고
    • Redox modulation of p53 conformation and sequence-specific DNA binding in vitro
    • Hainaut, P., Milner, J. Redox modulation of p53 conformation and sequence-specific DNA binding in vitro. Cancer Res. 53, 4469-4473 (1993).
    • (1993) Cancer Res , vol.53 , pp. 4469-4473
    • Hainaut, P.1    Milner, J.2
  • 26
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • Abate, C., Patel, L., Rauscher, F. J., 3rd & Curran, T. Redox regulation of fos and jun DNA-binding activity in vitro. Science 249, 1157-1161 (1990).
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher, F.J.3    Curran, T.4
  • 27
    • 0023175462 scopus 로고
    • Absence of both cytochrome b-245 subunits from neutrophils in X-linked chronic granulomatous disease
    • Segal, A. W. Absence of both cytochrome b-245 subunits from neutrophils in X-linked chronic granulomatous disease. Nature 326, 88-91 (1987).
    • (1987) Nature , vol.326 , pp. 88-91
    • Segal, A.W.1
  • 28
    • 0024513954 scopus 로고
    • Absence of both the 91kD and 22kD subunits of human neutrophil cytochrome b in two genetic forms of chronic granulomatous disease
    • Parkos, C. A., Dinauer, M. C., Jesaitis, A. J., Orkin, S. H., Curnutte, J. T. Absence of both the 91kD and 22kD subunits of human neutrophil cytochrome b in two genetic forms of chronic granulomatous disease. Blood 73, 1416-1420 (1989).
    • (1989) Blood , vol.73 , pp. 1416-1420
    • Parkos, C.A.1    Dinauer, M.C.2    Jesaitis, A.J.3    Orkin, S.H.4    Curnutte, J.T.5
  • 29
    • 70350380878 scopus 로고    scopus 로고
    • DUOX2-derived reactive oxygen species are effectors of NOD2-mediated antibacterial responses
    • Lipinski, S. et al. DUOX2-derived reactive oxygen species are effectors of NOD2-mediated antibacterial responses. J. Cell Sci. 122, 3522-3530 (2009).
    • (2009) J. Cell Sci , vol.122 , pp. 3522-3530
    • Lipinski, S.1
  • 30
    • 77950234253 scopus 로고    scopus 로고
    • A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae
    • Kumar, S., Molina-Cruz, A., Gupta, L., Rodrigues, J., Barillas-Mury, C. A peroxidase/dual oxidase system modulates midgut epithelial immunity in Anopheles gambiae. Science 327, 1644-1648 (2010).
    • (2010) Science , vol.327 , pp. 1644-1648
    • Kumar, S.1    Molina-Cruz, A.2    Gupta, L.3    Rodrigues, J.4    Barillas-Mury, C.5
  • 31
    • 33845430467 scopus 로고    scopus 로고
    • Pseudomonas lipopolysaccharide accelerates wound repair via activation of a novel epithelial cell signaling cascade
    • Koff, J. L., Shao, M. X., Kim, S., Ueki, I. F., Nadel, J. A. Pseudomonas lipopolysaccharide accelerates wound repair via activation of a novel epithelial cell signaling cascade. J. Immunol. 177, 8693-8700 (2006).
    • (2006) J. Immunol , vol.177 , pp. 8693-8700
    • Koff, J.L.1    Shao, M.X.2    Kim, S.3    Ueki, I.F.4    Nadel, J.A.5
  • 32
    • 0042203535 scopus 로고    scopus 로고
    • Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense
    • Geiszt, M., Witta, J., Baffi, J., Lekstrom, K., Leto, T. L. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J. 17, 1502-1504 (2003).
    • (2003) FASEB J , vol.17 , pp. 1502-1504
    • Geiszt, M.1    Witta, J.2    Baffi, J.3    Lekstrom, K.4    Leto, T.L.5
  • 33
    • 67650519057 scopus 로고    scopus 로고
    • ATP-mediated activation of the NADPH oxidase DUOX1 mediates airway epithelial responses to bacterial stimuli
    • Boots, A. W. et al. ATP-mediated activation of the NADPH oxidase DUOX1 mediates airway epithelial responses to bacterial stimuli. J. Biol. Chem. 284, 17858-17867 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 17858-17867
    • Boots, A.W.1
  • 34
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T. P., Nathan, C. F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51, 794-798 (1991).
    • (1991) Cancer Res , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 35
    • 59849084800 scopus 로고    scopus 로고
    • Increased levels of superoxide and H2O2 mediate the differential susceptibility of cancer cells versus normal cells to glucose deprivation
    • Aykin-Burns, N., Ahmad, I. M., Zhu, Y., Oberley, L. W., Spitz, D. R. Increased levels of superoxide and H2O2 mediate the differential susceptibility of cancer cells versus normal cells to glucose deprivation. Biochem. J. 418, 29-37 (2009).
    • (2009) Biochem. J , vol.418 , pp. 29-37
    • Aykin-Burns, N.1    Ahmad, I.M.2    Zhu, Y.3    Oberley, L.W.4    Spitz, D.R.5
  • 36
    • 17244367849 scopus 로고    scopus 로고
    • DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
    • Bartkova, J. et al. DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis. Nature 434, 864-870 (2005).
    • (2005) Nature , vol.434 , pp. 864-870
    • Bartkova, J.1
  • 37
    • 0028208968 scopus 로고
    • A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox
    • Leusen, J. H. et al. A point mutation in gp91-phox of cytochrome b558 of the human NADPH oxidase leading to defective translocation of the cytosolic proteins p47-phox and p67-phox. J. Clin. Invest. 93, 2120-2126 (1994).
    • (1994) J. Clin. Invest , vol.93 , pp. 2120-2126
    • Leusen, J.H.1
  • 38
    • 33745821178 scopus 로고    scopus 로고
    • Identification of the maturation factor for dual oxidase Evolution of an eukaryotic operon equivalent
    • Grasberger, H., Refetoff, S. Identification of the maturation factor for dual oxidase. Evolution of an eukaryotic operon equivalent. J. Biol. Chem. 281, 18269-18272 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 18269-18272
    • Grasberger, H.1    Refetoff, S.2
  • 39
    • 1142309762 scopus 로고    scopus 로고
    • Structural and functional characterization of the two human ThOX/Duox genes and their 5?-flanking regions
    • Pachucki, J., Wang, D., Christophe, D., Miot, F. Structural and functional characterization of the two human ThOX/Duox genes and their 5?-flanking regions. Mol. Cell. Endocrinol. 214, 53-62 (2004).
    • (2004) Mol. Cell. Endocrinol , vol.214 , pp. 53-62
    • Pachucki, J.1    Wang, D.2    Christophe, D.3    Miot, F.4
  • 40
    • 20244385005 scopus 로고    scopus 로고
    • Dual oxidase2 is expressed all along the digestive tract
    • El Hassani, R. A. et al. Dual oxidase2 is expressed all along the digestive tract. Am. J. Physiol. Gastrointest. Liver Physiol. 288, G933-G942 (2005).
    • (2005) Am. J. Physiol. Gastrointest. Liver Physiol , vol.288 , pp. G933-G942
    • El Hassani, R.A.1
  • 41
    • 66849111512 scopus 로고    scopus 로고
    • Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells
    • Luxen, S. et al. Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. J. Cell Sci. 122, 1238-1247 (2009).
    • (2009) J. Cell Sci , vol.122 , pp. 1238-1247
    • Luxen, S.1
  • 42
    • 65349172964 scopus 로고    scopus 로고
    • Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation
    • Morand, S. et al. Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation. FASEB J. 23, 1205-1218 (2009).
    • (2009) FASEB J , vol.23 , pp. 1205-1218
    • Morand, S.1
  • 43
    • 84866978507 scopus 로고    scopus 로고
    • Dual oxidase 2 bidirectional promoter polymorphisms confer differential immune responses in airway epithelia
    • Xu, C., Linderholm, A., Grasberger, H., Harper, R. W. Dual oxidase 2 bidirectional promoter polymorphisms confer differential immune responses in airway epithelia. Am. J. Respir. Cell. Mol. Biol. 47, 484-490 (2012).
    • (2012) Am. J. Respir. Cell. Mol. Biol , vol.47 , pp. 484-490
    • Xu, C.1    Linderholm, A.2    Grasberger, H.3    Harper, R.W.4
  • 44
    • 24044546151 scopus 로고    scopus 로고
    • Dual oxidase-2 has an intrinsic Ca2+dependent H2O2-generating activity
    • Ameziane-El-Hassani, R. et al. Dual oxidase-2 has an intrinsic Ca2+dependent H2O2-generating activity. J. Biol. Chem. 280, 30046-30054 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 30046-30054
    • Ameziane-El-Hassani, R.1
  • 45
    • 84924942012 scopus 로고    scopus 로고
    • The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release
    • Ueyama, T. et al. The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release. J. Biol. Chem. 290, 6495-6506 (2015).
    • (2015) J. Biol. Chem , vol.290 , pp. 6495-6506
    • Ueyama, T.1
  • 46
    • 84874841030 scopus 로고    scopus 로고
    • Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins
    • Meitzler, J. L., Hinde, S., Banfi, B., Nauseef, W. M., Ortiz de Montellano, P. R. Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins. J. Biol. Chem. 288, 7147-7157 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 7147-7157
    • Meitzler, J.L.1    Hinde, S.2    Banfi, B.3    Nauseef, W.M.4    Ortiz De Montellano, P.R.5
  • 47
    • 78650061731 scopus 로고    scopus 로고
    • Functional consequences of dual oxidase-thyroperoxidase interaction at the plasma membrane
    • Fortunato, R. S. et al. Functional consequences of dual oxidase-thyroperoxidase interaction at the plasma membrane. J. Clin. Endocrinol. Metab. 95, 5403-5411 (2010).
    • (2010) J. Clin. Endocrinol. Metab , vol.95 , pp. 5403-5411
    • Fortunato, R.S.1
  • 48
    • 84937784976 scopus 로고    scopus 로고
    • When an intramolecular disulfide bridge governs the interaction of DUOX2 with its partner DUOXA2
    • Carre, A. et al. When an intramolecular disulfide bridge governs the interaction of DUOX2 with its partner DUOXA2. Antioxid. Redox Signal. 23, 724-733 (2015).
    • (2015) Antioxid. Redox Signal , vol.23 , pp. 724-733
    • Carre, A.1
  • 49
    • 75149131560 scopus 로고    scopus 로고
    • Association of duoxes with thyroid peroxidase and its regulation in thyrocytes
    • Song, Y. et al. Association of duoxes with thyroid peroxidase and its regulation in thyrocytes. J. Clin. Endocrinol. Metab. 95, 375-382 (2010).
    • (2010) J. Clin. Endocrinol. Metab , vol.95 , pp. 375-382
    • Song, Y.1
  • 50
    • 65449180375 scopus 로고    scopus 로고
    • Activation of dual oxidases Duox1 and Duox2: Differential regulation mediated by camp-dependent protein kinase and protein kinase C-dependent phosphorylation
    • Rigutto, S. et al. Activation of dual oxidases Duox1 and Duox2: differential regulation mediated by camp-dependent protein kinase and protein kinase C-dependent phosphorylation. J. Biol. Chem. 284, 6725-6734 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 6725-6734
    • Rigutto, S.1
  • 51
    • 0028224772 scopus 로고
    • The human thyrotropin receptor activates G-proteins Gs and Gq/11
    • Allgeier, A. et al. The human thyrotropin receptor activates G-proteins Gs and Gq/11. J. Biol. Chem. 269, 13733-13735 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 13733-13735
    • Allgeier, A.1
  • 52
    • 0041328169 scopus 로고    scopus 로고
    • An outline of inherited disorders of the thyroid hormone generating system
    • Knobel, M., Medeiros-Neto, G. An outline of inherited disorders of the thyroid hormone generating system. Thyroid 13, 771-801 (2003).
    • (2003) Thyroid , vol.13 , pp. 771-801
    • Knobel, M.1    Medeiros-Neto, G.2
  • 53
    • 0025905588 scopus 로고
    • Unlike thyrotropin, thyroid-stimulating antibodies do not activate phospholipase C in human thyroid slices
    • Laurent, E. et al. Unlike thyrotropin, thyroid-stimulating antibodies do not activate phospholipase C in human thyroid slices. J. Clin. Invest. 87, 1634-1642 (1991).
    • (1991) J. Clin. Invest , vol.87 , pp. 1634-1642
    • Laurent, E.1
  • 54
    • 0026499881 scopus 로고
    • Thyroid expression of an A2 adenosine receptor transgene induces thyroid hyperplasia and hyperthyroidism
    • Ledent, C., Dumont, J. E., Vassart, G., Parmentier, M. Thyroid expression of an A2 adenosine receptor transgene induces thyroid hyperplasia and hyperthyroidism. EMBO J. 11, 537-542 (1992).
    • (1992) EMBO J , vol.11 , pp. 537-542
    • Ledent, C.1    Dumont, J.E.2    Vassart, G.3    Parmentier, M.4
  • 55
    • 0031035909 scopus 로고    scopus 로고
    • Costimulation of adenylyl cyclase and phospholipase C by a mutant ? 1B-adrenergic receptor transgene promotes malignant transformation of thyroid follicular cells
    • Ledent, C. et al. Costimulation of adenylyl cyclase and phospholipase C by a mutant ? 1B-adrenergic receptor transgene promotes malignant transformation of thyroid follicular cells. Endocrinology 138, 369-378 (1997).
    • (1997) Endocrinology , vol.138 , pp. 369-378
    • Ledent, C.1
  • 56
    • 0017665385 scopus 로고
    • Human thyroid peroxidase activity in benign and malign thyroid disorders
    • Fragu, P., Nataf, B. M. Human thyroid peroxidase activity in benign and malign thyroid disorders. J. Clin. Endocrinol. Metab. 45, 1089-1096 (1977).
    • (1977) J. Clin. Endocrinol. Metab , vol.45 , pp. 1089-1096
    • Fragu, P.1    Nataf, B.M.2
  • 57
    • 0034853752 scopus 로고    scopus 로고
    • Ca2 adenine dinucleotide phosphate-dependent H2O2 generation is inhibited by iodide in human thyroids
    • Cardoso, L. C. et al. Ca2 adenine dinucleotide phosphate-dependent H2O2 generation is inhibited by iodide in human thyroids. J. Clin. Endocrinol. Metab. 86, 4339-4343 (2001).
    • (2001) J. Clin. Endocrinol. Metab , vol.86 , pp. 4339-4343
    • Cardoso, L.C.1
  • 59
    • 0037390485 scopus 로고    scopus 로고
    • Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles
    • Morand, S. et al. Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles. Endocrinology 144, 1241-1248 (2003).
    • (2003) Endocrinology , vol.144 , pp. 1241-1248
    • Morand, S.1
  • 60
    • 8544270180 scopus 로고    scopus 로고
    • Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
    • Ambasta, R. K. et al. Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase. J. Biol. Chem. 279, 45935-45941 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 45935-45941
    • Ambasta, R.K.1
  • 61
    • 69249246990 scopus 로고    scopus 로고
    • Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells
    • Lyle, A. N. et al. Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells. Circ. Res. 105, 249-259 (2009).
    • (2009) Circ. Res , vol.105 , pp. 249-259
    • Lyle, A.N.1
  • 63
    • 0038148216 scopus 로고    scopus 로고
    • Nox4 mediates angiotensin II-induced activation of Akt/protein kinase B in mesangial cells
    • Gorin, Y. et al. Nox4 mediates angiotensin II-induced activation of Akt/protein kinase B in mesangial cells. Am. J. Physiol. Renal Physiol. 285, F219-F229 (2003).
    • (2003) Am. J. Physiol. Renal Physiol , vol.285 , pp. F219-F229
    • Gorin, Y.1
  • 64
    • 79953881843 scopus 로고    scopus 로고
    • The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4
    • Takac, I. et al. The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4. J. Biol. Chem. 286, 13304-13313 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 13304-13313
    • Takac, I.1
  • 65
    • 70149091965 scopus 로고    scopus 로고
    • Subcellular localization of Nox4 and regulation in diabetes
    • Block, K., Gorin, Y., Abboud, H. E. Subcellular localization of Nox4 and regulation in diabetes. Proc. Natl Acad. Sci. USA 106, 14385-14390 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 14385-14390
    • Block, K.1    Gorin, Y.2    Abboud, H.E.3
  • 66
    • 84907367024 scopus 로고    scopus 로고
    • N?-carboxymethyllysine-mediated endoplasmic reticulum stress promotes endothelial cell injury through Nox4/MKP-3 interaction
    • Lee, W. J. et al. N?-carboxymethyllysine-mediated endoplasmic reticulum stress promotes endothelial cell injury through Nox4/MKP-3 interaction. Free Radic. Biol. Med. 74, 294-306 (2014).
    • (2014) Free Radic. Biol. Med , vol.74 , pp. 294-306
    • Lee, W.J.1
  • 67
    • 79953183600 scopus 로고    scopus 로고
    • Control of hepatic nuclear superoxide production by glucose 6-phosphate dehydrogenase and NADPH oxidase-4
    • Spencer, N. Y. et al. Control of hepatic nuclear superoxide production by glucose 6-phosphate dehydrogenase and NADPH oxidase-4. J. Biol. Chem. 286, 8977-8987 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 8977-8987
    • Spencer, N.Y.1
  • 68
    • 84910680242 scopus 로고    scopus 로고
    • Clinical genetics of congenital hypothyroidism
    • Szinnai, G. Clinical genetics of congenital hypothyroidism. Endocr. Dev. 26, 60-78 (2014).
    • (2014) Endocr. Dev , vol.26 , pp. 60-78
    • Szinnai, G.1
  • 69
    • 0037063119 scopus 로고    scopus 로고
    • Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism
    • Moreno, J. C. et al. Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. N. Engl. J. Med. 347, 95-102 (2002).
    • (2002) N. Engl. J. Med , vol.347 , pp. 95-102
    • Moreno, J.C.1
  • 70
    • 80655134848 scopus 로고    scopus 로고
    • Molecular basis of thyroid dyshormonogenesis: Genetic screening in population-based Japanese patients
    • Narumi, S., Muroya, K., Asakura, Y., Aachi, M., Hasegawa, T. Molecular basis of thyroid dyshormonogenesis: genetic screening in population-based Japanese patients. J. Clin. Endocrinol. Metab. 96, E1838-E1842 (2011).
    • (2011) J. Clin. Endocrinol. Metab , vol.96 , pp. E1838-E1842
    • Narumi, S.1    Muroya, K.2    Asakura, Y.3    Aachi, M.4    Hasegawa, T.5
  • 71
    • 39049092782 scopus 로고    scopus 로고
    • Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism
    • Zamproni, I. et al. Biallelic inactivation of the dual oxidase maturation factor 2 (DUOXA2) gene as a novel cause of congenital hypothyroidism. J. Clin. Endocrinol. Metab. 93, 605-610 (2008).
    • (2008) J. Clin. Endocrinol. Metab , vol.93 , pp. 605-610
    • Zamproni, I.1
  • 72
    • 78650132026 scopus 로고    scopus 로고
    • Urothelial cells produce hydrogen peroxide through the activation of Duox1
    • Donko, A. et al. Urothelial cells produce hydrogen peroxide through the activation of Duox1. Free Radic. Biol. Med. 49, 2040-2048 (2010).
    • (2010) Free Radic. Biol. Med , vol.49 , pp. 2040-2048
    • Donko, A.1
  • 73
    • 34347208727 scopus 로고    scopus 로고
    • Congenital hypothyroidism, dwarfism, and hearing impairment caused by a missense mutation in the mouse dual oxidase 2 gene, Duox2
    • Johnson, K. R. et al. Congenital hypothyroidism, dwarfism, and hearing impairment caused by a missense mutation in the mouse dual oxidase 2 gene, Duox2. Mol. Endocrinol. 21, 1593-1602 (2007).
    • (2007) Mol. Endocrinol , vol.21 , pp. 1593-1602
    • Johnson, K.R.1
  • 74
    • 84857466174 scopus 로고    scopus 로고
    • Mice deficient in dual oxidase maturation factors are severely hypothyroid
    • Grasberger, H. et al. Mice deficient in dual oxidase maturation factors are severely hypothyroid. Mol. Endocrinol. 26, 481-492 (2012).
    • (2012) Mol. Endocrinol , vol.26 , pp. 481-492
    • Grasberger, H.1
  • 75
    • 0035893558 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced production of a 40 kDa immunoreactive thyroglobulin fragment in human thyroid cells: The onset of thyroid autoimmunity
    • Duthoit, C. et al. Hydrogen peroxide-induced production of a 40 kDa immunoreactive thyroglobulin fragment in human thyroid cells: the onset of thyroid autoimmunity? Biochem. J. 360, 557-562 (2001).
    • (2001) Biochem. J , vol.360 , pp. 557-562
    • Duthoit, C.1
  • 76
    • 2942620244 scopus 로고    scopus 로고
    • Antigenicity and immunogenicity of the C-terminal peptide of human thyroglobulin
    • El Hassani, R. A. et al. Antigenicity and immunogenicity of the C-terminal peptide of human thyroglobulin. Peptides 25, 1021-1029 (2004).
    • (2004) Peptides , vol.25 , pp. 1021-1029
    • El Hassani, R.A.1
  • 77
    • 15744401552 scopus 로고    scopus 로고
    • Peroxiredoxin 5 expression in the human thyroid gland
    • Gerard, A. C., Many, M. C., Daumerie, C., Knoops, B., Colin, I. M. Peroxiredoxin 5 expression in the human thyroid gland. Thyroid 15, 205-209 (2005).
    • (2005) Thyroid , vol.15 , pp. 205-209
    • Gerard, A.C.1    Many, M.C.2    Daumerie, C.3    Knoops, B.4    Colin, I.M.5
  • 78
    • 77954606305 scopus 로고    scopus 로고
    • N-acetylcysteine and 15 deoxy-?12,14-prostaglandin J2 exert a protective effect against autoimmune thyroid destruction in vivo but not against interleukin-1?/interferon ?-induced inhibitory effects in thyrocytes in vitro
    • Poncin, S. et al. N-acetylcysteine and 15 deoxy-?12,14-prostaglandin J2 exert a protective effect against autoimmune thyroid destruction in vivo but not against interleukin-1?/interferon ?-induced inhibitory effects in thyrocytes in vitro. Am. J. Pathol. 177, 219-228 (2010).
    • (2010) Am. J. Pathol , vol.177 , pp. 219-228
    • Poncin, S.1
  • 79
    • 84874109230 scopus 로고    scopus 로고
    • Thyroid hydrogen peroxide production is enhanced by the Th2 cytokines, IL-4 and IL-13, through increased expression of the dual oxidase 2 and its maturation factor DUOXA2
    • Raad, H., Eskalli, Z., Corvilain, B., Miot, F., De Deken, X. Thyroid hydrogen peroxide production is enhanced by the Th2 cytokines, IL-4 and IL-13, through increased expression of the dual oxidase 2 and its maturation factor DUOXA2. Free Radic. Biol. Med. 56, 216-225 (2013).
    • (2013) Free Radic. Biol. Med , vol.56 , pp. 216-225
    • Raad, H.1    Eskalli, Z.2    Corvilain, B.3    Miot, F.4    De Deken, X.5
  • 80
    • 84899967474 scopus 로고    scopus 로고
    • The expression of dual oxidase, thyroid peroxidase, and caveolin-1 differs according to the type of immune response (TH1/TH2) involved in thyroid autoimmune disorders
    • Marique, L. et al. The expression of dual oxidase, thyroid peroxidase, and caveolin-1 differs according to the type of immune response (TH1/TH2) involved in thyroid autoimmune disorders. J. Clin. Endocrinol. Metab. 99, 1722-1732 (2014).
    • (2014) J. Clin. Endocrinol. Metab , vol.99 , pp. 1722-1732
    • Marique, L.1
  • 81
    • 67650151005 scopus 로고    scopus 로고
    • Cancer-related inflammation, the seventh hallmark of cancer: Links to genetic instability
    • Colotta, F., Allavena, P., Sica, A., Garlanda, C., Mantovani, A. Cancer-related inflammation, the seventh hallmark of cancer: links to genetic instability. Carcinogenesis 30, 1073-1081 (2009).
    • (2009) Carcinogenesis , vol.30 , pp. 1073-1081
    • Colotta, F.1    Allavena, P.2    Sica, A.3    Garlanda, C.4    Mantovani, A.5
  • 83
    • 33744962523 scopus 로고    scopus 로고
    • RET/papillary thyroid cancer rearrangement in nonneoplastic thyrocytes: Follicular cells of Hashimoto's thyroiditis share low-level recombination events with a subset of papillary carcinoma
    • Rhoden, K. J. et al. RET/papillary thyroid cancer rearrangement in nonneoplastic thyrocytes: follicular cells of Hashimoto's thyroiditis share low-level recombination events with a subset of papillary carcinoma. J. Clin. Endocrinol. Metab. 91, 2414-2423 (2006).
    • (2006) J. Clin. Endocrinol. Metab , vol.91 , pp. 2414-2423
    • Rhoden, K.J.1
  • 84
    • 80053150200 scopus 로고    scopus 로고
    • Molecular genetics and diagnosis of thyroid cancer
    • Nikiforov, Y. E., Nikiforova, M. N. Molecular genetics and diagnosis of thyroid cancer. Nat. Rev. Endocrinol. 7, 569-580 (2011).
    • (2011) Nat. Rev. Endocrinol , vol.7 , pp. 569-580
    • Nikiforov, Y.E.1    Nikiforova, M.N.2
  • 85
    • 77952794328 scopus 로고    scopus 로고
    • Role of H2O2 in RET/PTC1 chromosomal rearrangement produced by ionizing radiation in human thyroid cells
    • Ameziane-El-Hassani, R. et al. Role of H2O2 in RET/PTC1 chromosomal rearrangement produced by ionizing radiation in human thyroid cells. Cancer Res. 70, 4123-4132 (2010).
    • (2010) Cancer Res , vol.70 , pp. 4123-4132
    • Ameziane-El-Hassani, R.1
  • 86
    • 72749107885 scopus 로고    scopus 로고
    • Hydrogen peroxide induces DNA single-and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ
    • Driessens, N. et al. Hydrogen peroxide induces DNA single-and double-strand breaks in thyroid cells and is therefore a potential mutagen for this organ. Endocr. Relat. Cancer 16, 845-856 (2009).
    • (2009) Endocr. Relat. Cancer , vol.16 , pp. 845-856
    • Driessens, N.1
  • 87
    • 77951977494 scopus 로고    scopus 로고
    • Role of oxidatively induced DNA lesions in human pathogenesis
    • Sedelnikova, O. A. et al. Role of oxidatively induced DNA lesions in human pathogenesis. Mutat. Res. 704, 152-159 (2010).
    • (2010) Mutat. Res , vol.704 , pp. 152-159
    • Sedelnikova, O.A.1
  • 88
    • 84861139727 scopus 로고    scopus 로고
    • Distinct pattern of oxidative DNA damage and DNA repair in follicular thyroid tumours
    • Karger, S. et al. Distinct pattern of oxidative DNA damage and DNA repair in follicular thyroid tumours. J. Mol. Endocrinol. 48, 193-202 (2012).
    • (2012) J. Mol. Endocrinol , vol.48 , pp. 193-202
    • Karger, S.1
  • 90
    • 84917673867 scopus 로고    scopus 로고
    • No association between XRCC1 genetic polymorphisms and differentiated thyroid carcinoma risk: A meta-analysis
    • Li, C., Xiang, X., Zhou, Y. No association between XRCC1 genetic polymorphisms and differentiated thyroid carcinoma risk: a meta-analysis. Mol. Biol. Rep. 41, 7613-7621 (2014).
    • (2014) Mol. Biol. Rep , vol.41 , pp. 7613-7621
    • Li, C.1    Xiang, X.2    Zhou, Y.3
  • 91
    • 84902985518 scopus 로고    scopus 로고
    • Association of XRCC1 polymorphisms with thyroid cancer risk
    • Wang, C., Ai, Z. Association of XRCC1 polymorphisms with thyroid cancer risk. Tumour Biol. 35, 4791-4797 (2014).
    • (2014) Tumour Biol , vol.35 , pp. 4791-4797
    • Wang, C.1    Ai, Z.2
  • 92
    • 84867452253 scopus 로고    scopus 로고
    • 3rd Pathways for repairing and tolerating the spectrum of oxidative DNA lesions
    • Berquist, B. R., Wilson, D. M. 3rd Pathways for repairing and tolerating the spectrum of oxidative DNA lesions. Cancer Lett. 327, 61-72 (2012).
    • (2012) Cancer Lett , vol.327 , pp. 61-72
    • Berquist, B.R.1    Wilson, D.M.2
  • 93
    • 0034621854 scopus 로고    scopus 로고
    • Frequent chromosomal translocations induced by DNA double-strand breaks
    • Richardson, C., Jasin, M. Frequent chromosomal translocations induced by DNA double-strand breaks. Nature 405, 697-700 (2000).
    • (2000) Nature , vol.405 , pp. 697-700
    • Richardson, C.1    Jasin, M.2
  • 94
    • 0028825189 scopus 로고
    • RET/PTC oncogene activation is an early event in thyroid carcinogenesis
    • Viglietto, G. et al. RET/PTC oncogene activation is an early event in thyroid carcinogenesis. Oncogene 11, 1207-1210 (1995).
    • (1995) Oncogene , vol.11 , pp. 1207-1210
    • Viglietto, G.1
  • 95
    • 84885214495 scopus 로고    scopus 로고
    • Comparative analysis of the thyrocytes and T cells: Responses to H2O2 and radiation reveals an H2O2-induced antioxidant transcriptional program in thyrocytes
    • Versteyhe, S. et al. Comparative analysis of the thyrocytes and T cells: responses to H2O2 and radiation reveals an H2O2-induced antioxidant transcriptional program in thyrocytes. J. Clin. Endocrinol. Metab. 98, E1645-E1654 (2013).
    • (2013) J. Clin. Endocrinol. Metab , vol.98 , pp. E1645-E1654
    • Versteyhe, S.1
  • 96
    • 0036488604 scopus 로고    scopus 로고
    • Second cancers in survivors of childhood cancer
    • Bhatia, S., Sklar, C. Second cancers in survivors of childhood cancer. Nat. Rev. Cancer 2, 124-132 (2002).
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 124-132
    • Bhatia, S.1    Sklar, C.2
  • 97
    • 33750603975 scopus 로고    scopus 로고
    • Long-term risks for thyroid cancer and other neoplasms after exposure to radiation
    • Schneider, A. B., Sarne, D. H. Long-term risks for thyroid cancer and other neoplasms after exposure to radiation. Nat. Clin. Pract. Endocrinol. Metab. 1, 82-91 (2005).
    • (2005) Nat. Clin. Pract. Endocrinol. Metab , vol.1 , pp. 82-91
    • Schneider, A.B.1    Sarne, D.H.2
  • 98
    • 84867483822 scopus 로고    scopus 로고
    • Ionizing radiation-induced metabolic oxidative stress and prolonged cell injury
    • Azzam, E. I., Jay-Gerin, J. P., Pain, D. Ionizing radiation-induced metabolic oxidative stress and prolonged cell injury. Cancer Lett. 327, 48-60 (2012).
    • (2012) Cancer Lett , vol.327 , pp. 48-60
    • Azzam, E.I.1    Jay-Gerin, J.P.2    Pain, D.3
  • 99
    • 0033646576 scopus 로고    scopus 로고
    • Hypoxia relieves X-ray-induced delayed effects in normal human embryo cells
    • Roy, K., Kodama, S., Suzuki, K., Fukase, K., Watanabe, M. Hypoxia relieves X-ray-induced delayed effects in normal human embryo cells. Radiat. Res. 154, 659-666 (2000).
    • (2000) Radiat. Res , vol.154 , pp. 659-666
    • Roy, K.1    Kodama, S.2    Suzuki, K.3    Fukase, K.4    Watanabe, M.5
  • 100
    • 0242406772 scopus 로고    scopus 로고
    • Radiation-induced DNA damage and delayed induced genomic instability
    • Suzuki, K., Ojima, M., Kodama, S., Watanabe, M. Radiation-induced DNA damage and delayed induced genomic instability. Oncogene 22, 6988-6993 (2003).
    • (2003) Oncogene , vol.22 , pp. 6988-6993
    • Suzuki, K.1    Ojima, M.2    Kodama, S.3    Watanabe, M.4
  • 101
    • 0242490151 scopus 로고    scopus 로고
    • Radiation-induced genomic instability and bystander effects: Inter-related nontargeted effects of exposure to ionizing radiation
    • Lorimore, S. A., Coates, P. J., Wright, E. G. Radiation-induced genomic instability and bystander effects: inter-related nontargeted effects of exposure to ionizing radiation. Oncogene 22, 7058-7069 (2003).
    • (2003) Oncogene , vol.22 , pp. 7058-7069
    • Lorimore, S.A.1    Coates, P.J.2    Wright, E.G.3
  • 102
    • 84907212782 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species are scavenged by Cockayne syndrome B protein in human fibroblasts without nuclear DNA damage
    • Cleaver, J. E. et al. Mitochondrial reactive oxygen species are scavenged by Cockayne syndrome B protein in human fibroblasts without nuclear DNA damage. Proc. Natl Acad. Sci. USA 111, 13487-13492 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 13487-13492
    • Cleaver, J.E.1
  • 103
    • 84901025723 scopus 로고    scopus 로고
    • Mucosal reactive oxygen species are required for antiviral response: Role of Duox in influenza a virus infection
    • Strengert, M. et al. Mucosal reactive oxygen species are required for antiviral response: role of Duox in influenza a virus infection. Antioxid. Redox Signal. 20, 2695-2709 (2014).
    • (2014) Antioxid. Redox Signal , vol.20 , pp. 2695-2709
    • Strengert, M.1
  • 104
    • 34548588388 scopus 로고    scopus 로고
    • Genome-wide gene expression profiling suggests distinct radiation susceptibilities in sporadic and post-Chernobyl papillary thyroid cancers
    • Detours, V. et al. Genome-wide gene expression profiling suggests distinct radiation susceptibilities in sporadic and post-Chernobyl papillary thyroid cancers. Br. J. Cancer 97, 818-825 (2007).
    • (2007) Br. J. Cancer , vol.97 , pp. 818-825
    • Detours, V.1
  • 105
    • 84865866443 scopus 로고    scopus 로고
    • A gene expression signature distinguishes normal tissues of sporadic and radiation-induced papillary thyroid carcinomas
    • Dom, G. et al. A gene expression signature distinguishes normal tissues of sporadic and radiation-induced papillary thyroid carcinomas. Br. J. Cancer 107, 994-1000 (2012).
    • (2012) Br. J. Cancer , vol.107 , pp. 994-1000
    • Dom, G.1
  • 106
    • 0035185319 scopus 로고    scopus 로고
    • Expression of nicotinamide adenine dinucleotide phosphate oxidase flavoprotein DUOX genes and proteins in human papillary and follicular thyroid carcinomas
    • Lacroix, L. et al. Expression of nicotinamide adenine dinucleotide phosphate oxidase flavoprotein DUOX genes and proteins in human papillary and follicular thyroid carcinomas. Thyroid 11, 1017-1023 (2001).
    • (2001) Thyroid , vol.11 , pp. 1017-1023
    • Lacroix, L.1
  • 107
    • 84924350333 scopus 로고    scopus 로고
    • Epigenetic silencing of dual oxidase 1 by promoter hypermethylation in human hepatocellular carcinoma
    • Ling, Q. et al. Epigenetic silencing of dual oxidase 1 by promoter hypermethylation in human hepatocellular carcinoma. Am. J. Cancer Res. 4, 508-517 (2014).
    • (2014) Am. J. Cancer Res , vol.4 , pp. 508-517
    • Ling, Q.1
  • 108
    • 39449091629 scopus 로고    scopus 로고
    • Silencing of DUOX NADPH oxidases by promoter hypermethylation in lung cancer
    • Luxen, S., Belinsky, S. A., Knaus, U. G. Silencing of DUOX NADPH oxidases by promoter hypermethylation in lung cancer. Cancer Res. 68, 1037-1045 (2008).
    • (2008) Cancer Res , vol.68 , pp. 1037-1045
    • Luxen, S.1    Belinsky, S.A.2    Knaus, U.G.3
  • 109
    • 84874642904 scopus 로고    scopus 로고
    • Functional activity and tumor-specific expression of dual oxidase 2 in pancreatic cancer cells and human malignancies characterized with a novel monoclonal antibody
    • Wu, Y. et al. Functional activity and tumor-specific expression of dual oxidase 2 in pancreatic cancer cells and human malignancies characterized with a novel monoclonal antibody. Int. J. Oncol. 42, 1229-1238 (2013).
    • (2013) Int. J. Oncol , vol.42 , pp. 1229-1238
    • Wu, Y.1
  • 110
    • 33750533387 scopus 로고    scopus 로고
    • ROS as a tumour suppressor? Nat
    • Ramsey, M. R., Sharpless, N. E. ROS as a tumour suppressor? Nat. Cell Biol. 8, 1213-1215 (2006).
    • (2006) Cell Biol , vol.8 , pp. 1213-1215
    • Ramsey, M.R.1    Sharpless, N.E.2
  • 111
    • 33845235459 scopus 로고    scopus 로고
    • Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints
    • Bartkova, J. et al. Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints. Nature 444, 633-637 (2006).
    • (2006) Nature , vol.444 , pp. 633-637
    • Bartkova, J.1
  • 112
    • 0033583242 scopus 로고    scopus 로고
    • Ras proteins induce senescence by altering the intracellular levels of reactive oxygen species
    • Lee, A. C. et al. Ras proteins induce senescence by altering the intracellular levels of reactive oxygen species. J. Biol. Chem. 274, 7936-7940 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 7936-7940
    • Lee, A.C.1
  • 113
    • 0036285034 scopus 로고    scopus 로고
    • C-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: A mechanism for oncogene-induced genetic instability
    • Vafa, O. et al. c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability. Mol. Cell 9, 1031-1044 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1031-1044
    • Vafa, O.1
  • 114
    • 84891301320 scopus 로고    scopus 로고
    • Causes and consequences of replication stress
    • Zeman, M. K., Cimprich, K. A. Causes and consequences of replication stress. Nat. Cell Biol. 16, 2-9 (2014).
    • (2014) Nat. Cell Biol , vol.16 , pp. 2-9
    • Zeman, M.K.1    Cimprich, K.A.2
  • 115
    • 84899929645 scopus 로고    scopus 로고
    • Oncogene-induced reactive oxygen species fuel hyperproliferation and DNA damage response activation
    • Ogrunc, M. et al. Oncogene-induced reactive oxygen species fuel hyperproliferation and DNA damage response activation. Cell Death Differ. 21, 998-1012 (2014).
    • (2014) Cell Death Differ , vol.21 , pp. 998-1012
    • Ogrunc, M.1
  • 116
    • 84908027700 scopus 로고    scopus 로고
    • Oxidative stress preferentially induces a subtype of micronuclei and mediates the genomic instability caused by p53 dysfunction
    • Xu, B. et al. Oxidative stress preferentially induces a subtype of micronuclei and mediates the genomic instability caused by p53 dysfunction. Mutat. Res. 770, 1-8 (2014).
    • (2014) Mutat. Res , vol.770 , pp. 1-8
    • Xu, B.1
  • 117
    • 84898987305 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress-induced epigenetic modifications in pancreatic epithelial cells
    • Mishra, P. K. et al. Mitochondrial oxidative stress-induced epigenetic modifications in pancreatic epithelial cells. Int. J. Toxicol. 33, 116-129 (2014).
    • (2014) Int. J. Toxicol , vol.33 , pp. 116-129
    • Mishra, P.K.1
  • 118
    • 81255162523 scopus 로고    scopus 로고
    • Oxidative damage targets complexes containing DNA methyltransferases SIRT1, and polycomb members to promoter CpG Islands
    • O'Hagan, H. M. et al. Oxidative damage targets complexes containing DNA methyltransferases, SIRT1, and polycomb members to promoter CpG Islands. Cancer Cell 20, 606-619 (2011).
    • (2011) Cancer Cell , vol.20 , pp. 606-619
    • O'Hagan, H.M.1
  • 119
    • 84978849685 scopus 로고    scopus 로고
    • Ch.2 (eds Groot, L. J. et al.) (South Dartmouth
    • Miot, F., Dupuy, C., Dumont, J., Rousset, B. Endotext Ch.2 (eds Groot, L. J. et al.) (South Dartmouth, 2000)
    • (2000)
    • Miot, F.1    Dupuy, C.2    Dumont, J.3    Endotext, R.B.4
  • 120
    • 84934904648 scopus 로고    scopus 로고
    • Aquaporin-3-mediated hydrogen peroxide transport is required for NF-?B signalling in keratinocytes and development of psoriasis
    • Hara-Chikuma, M. et al. Aquaporin-3-mediated hydrogen peroxide transport is required for NF-?B signalling in keratinocytes and development of psoriasis. Nat. Commun. 6, 7454 (2015).
    • (2015) Nat. Commun , vol.6 , pp. 7454
    • Hara-Chikuma, M.1
  • 121
    • 84877001084 scopus 로고    scopus 로고
    • Suppression of nucleotide metabolism underlies the establishment and maintenance of oncogene-induced senescence
    • Aird, K. M. et al. Suppression of nucleotide metabolism underlies the establishment and maintenance of oncogene-induced senescence. Cell Rep. 3, 1252-1265 (2013).
    • (2013) Cell Rep , vol.3 , pp. 1252-1265
    • Aird, K.M.1
  • 122
    • 79955525482 scopus 로고    scopus 로고
    • Nucleotide deficiency promotes genomic instability in early stages of cancer development
    • Bester, A. C. et al. Nucleotide deficiency promotes genomic instability in early stages of cancer development. Cell 145, 435-446 (2011).
    • (2011) Cell , vol.145 , pp. 435-446
    • Bester, A.C.1
  • 123
    • 84949293830 scopus 로고    scopus 로고
    • Singlet oxygen-mediated oxidation during UVA radiation alters the dynamic of genomic DNA replication
    • Graindorge, D. et al. Singlet oxygen-mediated oxidation during UVA radiation alters the dynamic of genomic DNA replication. PLoS ONE 10, e0140645 (2015).
    • (2015) PLoS ONE , vol.10 , pp. e0140645
    • Graindorge, D.1
  • 124
    • 77951060421 scopus 로고    scopus 로고
    • DNA breaks at fragile sites generate oncogenic RET/PTC rearrangements in human thyroid cells
    • Gandhi, M., Dillon, L. W., Pramanik, S., Nikiforov, Y. E., Wang, Y. H. DNA breaks at fragile sites generate oncogenic RET/PTC rearrangements in human thyroid cells. Oncogene 29, 2272-2280 (2010).
    • (2010) Oncogene , vol.29 , pp. 2272-2280
    • Gandhi, M.1    Dillon, L.W.2    Pramanik, S.3    Nikiforov, Y.E.4    Wang, Y.H.5
  • 125
    • 79955036320 scopus 로고    scopus 로고
    • Dual oxidase 1 induced by Th2 cytokines promotes STAT6 phosphorylation via oxidative inactivation of protein tyrosine phosphatase 1B in human epidermal keratinocytes
    • Hirakawa, S., Saito, R., Ohara, H., Okuyama, R., Aiba, S. Dual oxidase 1 induced by Th2 cytokines promotes STAT6 phosphorylation via oxidative inactivation of protein tyrosine phosphatase 1B in human epidermal keratinocytes. J. Immunol. 186, 4762-4770 (2011).
    • (2011) J. Immunol , vol.186 , pp. 4762-4770
    • Hirakawa, S.1    Saito, R.2    Ohara, H.3    Okuyama, R.4    Aiba, S.5


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