DUOX2

Dual oxidase 2, also known as DUOX2, is a human gene.cite web | title = Entrez Gene: DUOX2 dual oxidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50506| accessdate = ]

PBB_Summary
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summary_text = The protein encoded by this gene is a glycoprotein and a member of the NADPH oxidase family. The synthesis of thyroid hormone is catalyzed by a protein complex located at the apical membrane of thyroid follicular cells. This complex contains an iodide transporter, thyroperoxidase, and a peroxide generating system that includes this encoded protein and DUOX1. This protein is known as dual oxidase because it has both a peroxidase homology domain and a gp91phox domain.cite web | title = Entrez Gene: DUOX2 dual oxidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50506| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lambeth JD |title=Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. |journal=Curr. Opin. Hematol. |volume=9 |issue= 1 |pages= 11–7 |year= 2002 |pmid= 11753072 |doi=
*cite journal | author=Moreno JC, Visser TJ |title=New phenotypes in thyroid dyshormonogenesis: hypothyroidism due to DUOX2 mutations. |journal=Endocrine development |volume=10 |issue= |pages= 99–117 |year= 2007 |pmid= 17684392 |doi= 10.1159/0000106822
*cite journal | author=Dupuy C, Ohayon R, Valent A, "et al." |title=Purification of a novel flavoprotein involved in the thyroid NADPH oxidase. Cloning of the porcine and human cdnas. |journal=J. Biol. Chem. |volume=274 |issue= 52 |pages= 37265–9 |year= 2000 |pmid= 10601291 |doi=
*cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, "et al." |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=
*cite journal | author=De Deken X, Wang D, Many MC, "et al." |title=Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23227–33 |year= 2000 |pmid= 10806195 |doi= 10.1074/jbc.M000916200
*cite journal | author=Dupuy C, Pomerance M, Ohayon R, "et al." |title=Thyroid oxidase (THOX2) gene expression in the rat thyroid cell line FRTL-5. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 2 |pages= 287–92 |year= 2000 |pmid= 11032719 |doi= 10.1006/bbrc.2000.3671
*cite journal | author=Caillou B, Dupuy C, Lacroix L, "et al." |title=Expression of reduced nicotinamide adenine dinucleotide phosphate oxidase (ThoX, LNOX, Duox) genes and proteins in human thyroid tissues. |journal=J. Clin. Endocrinol. Metab. |volume=86 |issue= 7 |pages= 3351–8 |year= 2001 |pmid= 11443211 |doi=
*cite journal | author=Edens WA, Sharling L, Cheng G, "et al." |title=Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. |journal=J. Cell Biol. |volume=154 |issue= 4 |pages= 879–91 |year= 2001 |pmid= 11514595 |doi= 10.1083/jcb.200103132
*cite journal | author=Lacroix L, Nocera M, Mian C, "et al." |title=Expression of nicotinamide adenine dinucleotide phosphate oxidase flavoprotein DUOX genes and proteins in human papillary and follicular thyroid carcinomas. |journal=Thyroid |volume=11 |issue= 11 |pages= 1017–23 |year= 2002 |pmid= 11762710 |doi= 10.1089/105072501753271699
*cite journal | author=De Deken X, Wang D, Dumont JE, Miot F |title=Characterization of ThOX proteins as components of the thyroid H(2)O(2)-generating system. |journal=Exp. Cell Res. |volume=273 |issue= 2 |pages= 187–96 |year= 2002 |pmid= 11822874 |doi= 10.1006/excr.2001.5444
*cite journal | author=Moreno JC, Bikker H, Kempers MJ, "et al." |title=Inactivating mutations in the gene for thyroid oxidase 2 (THOX2) and congenital hypothyroidism. |journal=N. Engl. J. Med. |volume=347 |issue= 2 |pages= 95–102 |year= 2002 |pmid= 12110737 |doi= 10.1056/NEJMoa012752
*cite journal | author=Geiszt M, Witta J, Baffi J, "et al." |title=Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. |journal=FASEB J. |volume=17 |issue= 11 |pages= 1502–4 |year= 2003 |pmid= 12824283 |doi= 10.1096/fj.02-1104fje
*cite journal | author=Pachucki J, Wang D, Christophe D, Miot F |title=Structural and functional characterization of the two human ThOX/Duox genes and their 5'-flanking regions. |journal=Mol. Cell. Endocrinol. |volume=214 |issue= 1-2 |pages= 53–62 |year= 2004 |pmid= 15062544 |doi= 10.1016/j.mce.2003.11.026
*cite journal | author=Morand S, Agnandji D, Noel-Hudson MS, "et al." |title=Targeting of the dual oxidase 2 N-terminal region to the plasma membrane. |journal=J. Biol. Chem. |volume=279 |issue= 29 |pages= 30244–51 |year= 2004 |pmid= 15150274 |doi= 10.1074/jbc.M405406200
*cite journal | author=Schwarzer C, Machen TE, Illek B, Fischer H |title=NADPH oxidase-dependent acid production in airway epithelial cells. |journal=J. Biol. Chem. |volume=279 |issue= 35 |pages= 36454–61 |year= 2004 |pmid= 15210697 |doi= 10.1074/jbc.M404983200
*cite journal | author=Wang D, De Deken X, Milenkovic M, "et al." |title=Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. |journal=J. Biol. Chem. |volume=280 |issue= 4 |pages= 3096–103 |year= 2005 |pmid= 15561711 |doi= 10.1074/jbc.M407709200
*cite journal | author=El Hassani RA, Benfares N, Caillou B, "et al." |title=Dual oxidase2 is expressed all along the digestive tract. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=288 |issue= 5 |pages= G933–42 |year= 2005 |pmid= 15591162 |doi= 10.1152/ajpgi.00198.2004
*cite journal | author=Forteza R, Salathe M, Miot F, "et al." |title=Regulated hydrogen peroxide production by Duox in human airway epithelial cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=32 |issue= 5 |pages= 462–9 |year= 2005 |pmid= 15677770 |doi= 10.1165/rcmb.2004-0302OC
*cite journal | author=Ameziane-El-Hassani R, Morand S, Boucher JL, "et al." |title=Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity. |journal=J. Biol. Chem. |volume=280 |issue= 34 |pages= 30046–54 |year= 2005 |pmid= 15972824 |doi= 10.1074/jbc.M500516200

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