NOX3

NADPH oxidases, such as NOX3, are plasma membrane-associated enzymes found in many cell types. They catalyze the production of superoxide by a 1-electron reduction of oxygen, using NADPH as the electron donor.[supplied by OMIM]{{cite web | title = Entrez Gene: NOX3 NADPH oxidase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=50508}}

{{reflist}}

{{refbegin | 2}}

• {{cite journal | vauthors = Lachgar A, Sojic N, Arbault S, Bruce D, Sarasin A, Amatore C, Bizzini B, Zagury D, Vuillaume M | title = Amplification of the inflammatory cellular redox state by human immunodeficiency virus type 1-immunosuppressive tat and gp160 proteins | journal = J. Virol. | volume = 73 | issue = 2 | pages = 1447–52 | year = 1999 | pmid = 9882350 | pmc = 103969 | doi = 10.1128/JVI.73.2.1447-1452.1999}}
• {{cite journal | vauthors = Kikuchi H, Hikage M, Miyashita H, Fukumoto M | title = NADPH oxidase subunit, gp91(phox) homologue, preferentially expressed in human colon epithelial cells | journal = Gene | volume = 254 | issue = 1–2 | pages = 237–43 | year = 2000 | pmid = 10974555 | doi = 10.1016/S0378-1119(00)00258-4 }}
• {{cite journal | vauthors = Cheng G, Ritsick D, Lambeth JD | title = Nox3 regulation by NOXO1, p47phox, and p67phox | journal = J. Biol. Chem. | volume = 279 | issue = 33 | pages = 34250–5 | year = 2004 | pmid = 15181005 | doi = 10.1074/jbc.M400660200 | doi-access = free }}
• {{cite journal | vauthors = Jana A, Pahan K | title = Human immunodeficiency virus type 1 gp120 induces apoptosis in human primary neurons through redox-regulated activation of neutral sphingomyelinase | journal = J. Neurosci. | volume = 24 | issue = 43 | pages = 9531–40 | year = 2004 | pmid = 15509740 | pmc = 1955476 | doi = 10.1523/JNEUROSCI.3085-04.2004 }}
• {{cite journal | vauthors = Ueno N, Takeya R, Miyano K, Kikuchi H, Sumimoto H | title = The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators | journal = J. Biol. Chem. | volume = 280 | issue = 24 | pages = 23328–39 | year = 2005 | pmid = 15824103 | doi = 10.1074/jbc.M414548200 | doi-access = free }}
• {{cite journal | vauthors = Ueyama T, Geiszt M, Leto TL | title = Involvement of Rac1 in activation of multicomponent Nox1- and Nox3-based NADPH oxidases | journal = Mol. Cell. Biol. | volume = 26 | issue = 6 | pages = 2160–74 | year = 2006 | pmid = 16507994 | pmc = 1430270 | doi = 10.1128/MCB.26.6.2160-2174.2006 | url = http://www.lib.kobe-u.ac.jp/repository/90000354.pdf | access-date = 2018-11-04 | archive-date = 2020-10-09 | archive-url = https://web.archive.org/web/20201009210504/http://www.lib.kobe-u.ac.jp/repository/90000354.pdf | url-status = dead }}
• {{cite journal | vauthors = Carnesecchi S, Carpentier JL, Foti M, Szanto I | title = Insulin-induced vascular endothelial growth factor expression is mediated by the NADPH oxidase NOX3 | journal = Exp. Cell Res. | volume = 312 | issue = 17 | pages = 3413–24 | year = 2006 | pmid = 16949073 | doi = 10.1016/j.yexcr.2006.07.003 }}
• {{cite journal | vauthors = Nakano Y, Banfi B, Jesaitis AJ, Dinauer MC, Allen LA, Nauseef WM | title = Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3 | journal = Biochem. J. | volume = 403 | issue = 1 | pages = 97–108 | year = 2007 | pmid = 17140397 | pmc = 1828898 | doi = 10.1042/BJ20060819 }}
• {{cite journal | vauthors = Chen G, Adeyemo AA, Zhou J, Chen Y, Doumatey A, Lashley K, Huang H, Amoah A, Agyenim-Boateng K, Eghan BA, Okafor G, Acheampong J, Oli J, Fasanmade O, Johnson T, Rotimi C | title = A genome-wide search for linkage to renal function phenotypes in West Africans with type 2 diabetes | journal = Am. J. Kidney Dis. | volume = 49 | issue = 3 | pages = 394–400 | year = 2007 | pmid = 17336700 | doi = 10.1053/j.ajkd.2006.12.011 }}

{{refend}}

{{gene-6-stub}}