Biology:NOX1
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
NADPH oxidase 1 is an enzyme that in humans is encoded by the NOX1 gene.[1]
NOX1 is a homolog of the catalytic subunit of the superoxide-generating NADPH oxidase of phagocytes, gp91phox. Two transcript variants encoding different isoforms have been found for this gene.[2]
References
- ↑ "Cell transformation by the superoxide-generating oxidase Mox1". Nature 401 (6748): 79–82. Sep 1999. doi:10.1038/43459. PMID 10485709. Bibcode: 1999Natur.401...79S.
- ↑ "Entrez Gene: NOX1 NADPH oxidase 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27035.
Further reading
- "Amplification of the inflammatory cellular redox state by human immunodeficiency virus type 1-immunosuppressive tat and gp160 proteins.". J. Virol. 73 (2): 1447–52. 1999. doi:10.1128/JVI.73.2.1447-1452.1999. PMID 9882350.
- "NADPH oxidase subunit, gp91(phox) homologue, preferentially expressed in human colon epithelial cells.". Gene 254 (1–2): 237–43. 2000. doi:10.1016/S0378-1119(00)00258-4. PMID 10974555.
- "Ionomycin-induced neutrophil NADPH oxidase activity is selectively inhibited by the serine protease inhibitor diisopropyl fluorophosphate". Antioxid. Redox Signal. 4 (1): 17–25. 2002. doi:10.1089/152308602753625816. PMID 11970839.
- Babior BM (2002). "The activity of leukocyte NADPH oxidase: regulation by p47PHOX cysteine and serine residues". Antioxid. Redox Signal. 4 (1): 35–8. doi:10.1089/152308602753625834. PMID 11970841.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Proteins homologous to p47phox and p67phox support superoxide production by NAD(P)H oxidase 1 in colon epithelial cells". J. Biol. Chem. 278 (22): 20006–12. 2003. doi:10.1074/jbc.M301289200. PMID 12657628.
- "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". J. Biol. Chem. 278 (27): 25234–46. 2003. doi:10.1074/jbc.M212856200. PMID 12716910.
- "NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes". J. Immunol. 171 (1): 299–306. 2003. doi:10.4049/jimmunol.171.1.299. PMID 12817011.
- "Association of gp91phox homolog Nox1 with anchorage-independent growth and MAP kinase-activation of transformed human keratinocytes". Oncogene 22 (38): 6045–53. 2003. doi:10.1038/sj.onc.1206654. PMID 12955083.
- "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain". J. Biol. Chem. 279 (6): 4737–42. 2004. doi:10.1074/jbc.M305968200. PMID 14617635.
- "Distinct subcellular localizations of Nox1 and Nox4 in vascular smooth muscle cells". Arterioscler. Thromb. Vasc. Biol. 24 (4): 677–83. 2004. doi:10.1161/01.ATV.0000112024.13727.2c. PMID 14670934.
- "An aging-related cell surface NADH oxidase (arNOX) generates superoxide and is inhibited by coenzyme Q". Mol. Cell. Biochem. 254 (1–2): 101–9. 2004. doi:10.1023/A:1027301405614. PMID 14674687.
- "A constitutive NADPH oxidase-like system containing gp91phox homologs in human keratinocytes". J. Invest. Dermatol. 122 (4): 1000–9. 2004. doi:10.1111/j.0022-202X.2004.22410.x. PMID 15102091.
- "Upregulation of NAD(P)H oxidase 1 in hypoxia activates hypoxia-inducible factor 1 via increase in reactive oxygen species". Free Radic. Biol. Med. 36 (10): 1279–88. 2004. doi:10.1016/j.freeradbiomed.2004.02.071. PMID 15110393.
- "Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms". Free Radic. Biol. Med. 37 (2): 156–65. 2005. doi:10.1016/j.freeradbiomed.2004.04.020. PMID 15203187.
- "Systemic regulation of vascular NAD(P)H oxidase activity and nox isoform expression in human arteries and veins". Arterioscler. Thromb. Vasc. Biol. 24 (9): 1614–20. 2005. doi:10.1161/01.ATV.0000139011.94634.9d. PMID 15256399.
- "Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase". J. Biol. Chem. 279 (44): 45935–41. 2004. doi:10.1074/jbc.M406486200. PMID 15322091.
- "Analysis of mRNA transcripts from the NAD(P)H oxidase 1 (Nox1) gene. Evidence against production of the NADPH oxidase homolog-1 short (NOH-1S) transcript variant". J. Biol. Chem. 279 (49): 51661–8. 2005. doi:10.1074/jbc.M409325200. PMID 15375166.
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