NOXO1
NADPH oxidase organizer 1 is an enzyme that in humans is encoded by the NOXO1 gene.[5]
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| Aliases | NOXO1, P41NOX, P41NOXA, P41NOXB, P41NOXC, SH3PXD5, SNX28, NADPH oxidase organizer 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 611256 MGI: 1919143 HomoloGene: 12418 GeneCards: NOXO1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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References
- GRCh38: Ensembl release 89: ENSG00000196408 - Ensembl, May 2017
- GRCm38: Ensembl release 89: ENSMUSG00000019320 - Ensembl, May 2017
- "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- "Entrez Gene: NOXO1 NADPH oxidase organizer 1".
Further reading
- Bánfi B, Clark RA, Steger K, Krause KH (2003). "Two novel proteins activate superoxide generation by the NADPH oxidase NOX1". J. Biol. Chem. 278 (6): 3510–3. doi:10.1074/jbc.C200613200. PMID 12473664.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Geiszt M, Lekstrom K, Witta J, Leto TL (2003). "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. doi:10.1074/jbc.M301289200. PMID 12657628.
- Takeya R, Ueno N, Kami K, et al. (2003). "Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases". J. Biol. Chem. 278 (27): 25234–46. doi:10.1074/jbc.M212856200. PMID 12716910.
- Cheng G, Lambeth JD (2004). "NOXO1, regulation of lipid binding, localization, and activation of Nox1 by the Phox homology (PX) domain". J. Biol. Chem. 279 (6): 4737–42. doi:10.1074/jbc.M305968200. PMID 14617635.
- Cheng G, Ritsick D, Lambeth JD (2004). "Nox3 regulation by NOXO1, p47phox, and p67phox". J. Biol. Chem. 279 (33): 34250–5. doi:10.1074/jbc.M400660200. PMID 15181005.
- Bánfi B, Malgrange B, Knisz J, et al. (2004). "NOX3, a superoxide-generating NADPH oxidase of the inner ear". J. Biol. Chem. 279 (44): 46065–72. doi:10.1074/jbc.M403046200. PMID 15326186.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Ueno N, Takeya R, Miyano K, et al. (2005). "The NADPH oxidase Nox3 constitutively produces superoxide in a p22phox-dependent manner: its regulation by oxidase organizers and activators". J. Biol. Chem. 280 (24): 23328–39. doi:10.1074/jbc.M414548200. PMID 15824103.
- Cheng G, Lambeth JD (2005). "Alternative mRNA splice forms of NOXO1: differential tissue expression and regulation of Nox1 and Nox3". Gene. 356: 118–26. doi:10.1016/j.gene.2005.03.008. PMID 15949904.
- Park HS, Park D, Bae YS (2006). "Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1". Biochem. Biophys. Res. Commun. 339 (3): 985–90. doi:10.1016/j.bbrc.2005.11.108. PMID 16329988.
- Takeya R, Taura M, Yamasaki T, et al. (2006). "Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1". FEBS J. 273 (16): 3663–77. doi:10.1111/j.1742-4658.2006.05371.x. PMID 16911517. S2CID 701568.
- Yamamoto A, Kami K, Takeya R, Sumimoto H (2007). "Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1)". Biochem. Biophys. Res. Commun. 352 (2): 560–5. doi:10.1016/j.bbrc.2006.11.060. PMID 17126813.
External links
- PDBe-KB provides an overview of all the structure information available in the PDB for Human NADPH oxidase organizer 1
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