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NADPH oxidase organizer 1

NOXO1, Nox organizer 1, NADPH oxidase organizer 1
NADPH oxidases (NOXs) catalyze the transfer of electrons from NADPH to molecular oxygen to generate reactive oxygen species (ROS). NOX organizers, such as NOXO1, target NOX activators (see NOXA1; MIM 611255) to NOX and also target NOX to different subcellular compartments (Opitz et al., 2007 [PubMed 17189823]).[supplied by OMIM, Mar 2008] (from NCBI)
Papers on NOXO1
NOXO1 phosphorylation on serine 154 is critical for optimal NADPH oxidase 1 assembly and activation.
New
Dang et al., Paris, France. In Faseb J, 15 Feb 2013
Reactive oxygen species (ROS) production by NADPH oxidase 1 (NOX1), which is mainly expressed in colon epithelial cells, requires the membrane-bound component p22(PHOX) and the cytosolic partners NOX organizer 1 (NOXO1), NOX activator 1 (NOXA1), and Rac1.
Bmi-1 confers adaptive radioresistance to KYSE-150R esophageal carcinoma cells.
New
Dong et al., Hangzhou, China. In Biochem Biophys Res Commun, Sep 2012
Furthermore, Bmi-1 depletion increased the generation of reactive oxygen species (ROS) and the expression of oxidase genes (Lpo, Noxo1 and Alox15) in KYSE-150R cells exposed to irradiation.
HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis.
New
Martin-Ventura et al., Madrid, Spain. In Cardiovasc Res, Aug 2012
17-DMAG also diminished the expression of Nox1 and Nox organizer-1 (Noxo1) in VSMCs and monocytes.
The p47phox- and NADPH oxidase organiser 1 (NOXO1)-dependent activation of NADPH oxidase 1 (NOX1) mediates endothelial nitric oxide synthase (eNOS) uncoupling and endothelial dysfunction in a streptozotocin-induced murine model of diabetes.
New
Cai et al., Los Angeles, United States. In Diabetologia, Jul 2012
The eNOS uncoupling activity was markedly attenuated in diabetic mice transfected with Nox1 or Nox1 organiser 1 (Noxo1) short interfering RNA (siRNA), and abolished in Nox1 (-/y) diabetic mice.
Neuronal NAD(P)H oxidases contribute to ROS production and mediate RGC death after ischemia.
New
Ivanov et al., Miami, United States. In Invest Ophthalmol Vis Sci, May 2012
RESULTS: It was reported that RGCs express catalytic Nox1, Nox2, Nox4, Duox1, as well as regulatory Ncf1/p47phox, Ncf2/p67phox, Cyba/p22phox, Noxo1, and Noxa1 subunits of NAD(P)H oxidases under normal conditions and after ischemia.
The NOXO1β PX domain preferentially targets PtdIns(4,5)P2 and PtdIns(3,4,5)P3.
New
Horita et al., Winston-Salem, United States. In J Mol Biol, May 2012
NOXO1β [NOXO1 (Nox organizer 1) β] is a cytosolic protein that, in conjunction with NOXA1 (Nox activator 1), regulates generation of reactive oxygen species by the NADPH oxidase 1 (Nox1) enzyme complex.
Noxa1 as a moderate activator of Nox2-based NADPH oxidase.
New
Tamura et al., Japan. In Arch Biochem Biophys, Apr 2012
In the present study, we used purified cyt.b(558) (Nox2 plus p22(phox)), Rac(Q61L), and Noxo1 to examine the ability of Noxa1 to activate Nox2.
Death receptors 4 and 5 activate Nox1 NADPH oxidase through riboflavin kinase to induce reactive oxygen species-mediated apoptotic cell death.
New
Kim et al., Suwŏn, South Korea. In J Biol Chem, Feb 2012
KD548-Fc treatment induces the formation of a DR4/DR5 signaling complex containing riboflavin kinase (RFK), Nox1, the Nox1 subunits (Rac1, Noxo1, and Noxa1), TNF receptor-associated death domain (TRADD), and TNF receptor-associated factor 2 (TRAF2).
Backbone 1H, 15N, and 13C resonance assignments for the NOXO1β PX domain.
GeneRIF
Horita et al., Winston-Salem, United States. In Biomol Nmr Assign, 2011
The backbone assignments of NOXO1beta PX are studied using NMR.
NADPH oxidase (NOX) isoforms are inhibited by celastrol with a dual mode of action.
Bedard et al., Genève, Switzerland. In Br J Pharmacol, 2011
Celastrol bound to a recombinant p47(phox) and disrupted the binding of the proline rich region of p22(phox) to the tandem SH3 domain of p47(phox) and NOXO1, the cytosolic subunits of NOX2 and NOX1, respectively.
Receptor activation of NADPH oxidases.
Review
Görlach et al., München, Germany. In Antioxid Redox Signal, 2010
They mainly differ in containing one out of seven homologous catalytic core proteins termed NOX1 to NOX5 and DUOX1 or 2. NADPH oxidase activity is controlled by regulatory subunits, including the NOX regulators p47phox and p67phox, their homologs NOXO1 and NOXA1, or the DUOX1 or 2 regulators DUOXA1 and 2. In addition, the GTPase Rac modulates activity of several of these enzymes.
Regulation of NOXO1 activity through reversible interactions with p22 and NOXA1.
GeneRIF
Rittinger et al., London, United Kingdom. In Plos One, 2009
The first quantitative characterization of the interactions made between the cytosolic regulators NOXO1 and NOXA1 and membrane-bound p22(phox), is presented.
Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases.
Review
Ueyama et al., Bethesda, United States. In Antioxid Redox Signal, 2009
Determinants of subcellular targeting include: (a) formation of Nox-p22(phox) heterodimeric complexes allowing plasma membrane translocation, (b) phospholipids-binding specificities of PX domain-containing organizer proteins (p47(phox) or Nox organizer 1 (Noxo1 and p40(phox)), and (c) variably splicing of Noxo1 PX domains directing them to nuclear or plasma membranes.
Signaling components of redox active endosomes: the redoxosomes.
Review
Engelhardt et al., Iowa City, United States. In Antioxid Redox Signal, 2009
Unique features of redox-active signaling endosomes can include NADPH oxidase complex components (Nox1, Noxo1, Noxa1, Nox2, p47phox, p67phox, and/or Rac1), ROS processing enzymes (SOD1 and/or peroxiredoxins), chloride channels capable of mediating superoxide transport and/or membrane gradients required for Nox activity, and novel redox-dependent sensors that control Nox activity.
Role of the small GTPase Rac in p22phox-dependent NADPH oxidases.
Review
Sumimoto et al., Fukuoka, Japan. In Biochimie, 2007
The p22(phox)-complexed Nox2 and Nox1 are dormant on their own, and their activation requires soluble supportive proteins such as a Nox organizer (p47(phox) or Noxo1) and a Nox activator (p67(phox) or Noxa1).
[Two breakthroughs in CGD studies].
Review
Nunoi, Miyazaki, Japan. In Nihon Rinsho Meneki Gakkai Kaishi, 2007
First, the discovery of 7 Nox/Duox family proteins, Noxo1 and Noxa1 (homologues of gp91(phox), p47(phox) and p67(phox)) may clarify novel physiological mechanisms for superoxide regulation in various organs, such as the regulation of blood pressure, mucosal defense system in respiratory/digestive tract and nephron.
Interaction between the SH3 domains and C-terminal proline-rich region in NADPH oxidase organizer 1 (Noxo1).
GeneRIF
Sumimoto et al., Fukuoka, Japan. In Biochem Biophys Res Commun, 2007
These findings suggest that Nox activation involves a conformational change leading to disruption of the bis-SH3-PRR interaction in Noxo1.
Expression and function of Noxo1gamma, an alternative splicing form of the NADPH oxidase organizer 1.
GeneRIF
Sumimoto et al., Fukuoka, Japan. In Febs J, 2006
This study shows the expression of alternatively spliced transcripts of the NOXO1 gene and the roles of the protein products in the activation of Nox oxidases.
Molecular interaction of NADPH oxidase 1 with betaPix and Nox Organizer 1.
GeneRIF
Bae et al., Seoul, South Korea. In Biochem Biophys Res Commun, 2006
These results suggest that the formation of the complex consisting of Nox1, betaPix, and NoxO1 is likely to be a critical step in EGF-induced ROS generation.
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