Academic literature on the topic 'NADPH oxidase (Nox) family'
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Journal articles on the topic "NADPH oxidase (Nox) family"
Bedard, Karen, and Karl-Heinz Krause. "The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology." Physiological Reviews 87, no. 1 (January 2007): 245–313. http://dx.doi.org/10.1152/physrev.00044.2005.
Full textMaturana, Andrés, Karl-Heinz Krause, and Nicolas Demaurex. "NOX Family NADPH Oxidases." Journal of General Physiology 120, no. 6 (November 25, 2002): 781–86. http://dx.doi.org/10.1085/jgp.20028713.
Full textDonkó, Ágnes, Zalán Péterfi, Adrienn Sum, Thomas Leto, and Miklós Geiszt. "Dual oxidases." Philosophical Transactions of the Royal Society B: Biological Sciences 360, no. 1464 (November 4, 2005): 2301–8. http://dx.doi.org/10.1098/rstb.2005.1767.
Full textVermot, Annelise, Isabelle Petit-Härtlein, Susan M. E. Smith, and Franck Fieschi. "NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology." Antioxidants 10, no. 6 (June 1, 2021): 890. http://dx.doi.org/10.3390/antiox10060890.
Full textGray, Stephen P., Ajay M. Shah, and Ioannis Smyrnias. "NADPH oxidase 4 and its role in the cardiovascular system." Vascular Biology 1, no. 1 (August 12, 2019): H59—H66. http://dx.doi.org/10.1530/vb-19-0014.
Full textMontezano, Augusto C., Dylan Burger, Graziela S. Ceravolo, Hiba Yusuf, Maria Montero, and Rhian M. Touyz. "Novel Nox homologues in the vasculature: focusing on Nox4 and Nox5." Clinical Science 120, no. 4 (November 2, 2010): 131–41. http://dx.doi.org/10.1042/cs20100384.
Full textBánfi, Botond, Brigitte Malgrange, Judit Knisz, Klaus Steger, Michel Dubois-Dauphin, and Karl-Heinz Krause. "NOX3, a Superoxide-generating NADPH Oxidase of the Inner Ear." Journal of Biological Chemistry 279, no. 44 (August 23, 2004): 46065–72. http://dx.doi.org/10.1074/jbc.m403046200.
Full textMaraldi, Tullia. "Natural Compounds as Modulators of NADPH Oxidases." Oxidative Medicine and Cellular Longevity 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/271602.
Full textRoy, Krishnendu, Yongzhong Wu, Jennifer L. Meitzler, Agnes Juhasz, Han Liu, Guojian Jiang, Jiamo Lu, Smitha Antony, and James H. Doroshow. "NADPH oxidases and cancer." Clinical Science 128, no. 12 (March 27, 2015): 863–75. http://dx.doi.org/10.1042/cs20140542.
Full textMatuz-Mares, Deyamira, Héctor Vázquez-Meza, and María Magdalena Vilchis-Landeros. "NOX as a Therapeutic Target in Liver Disease." Antioxidants 11, no. 10 (October 16, 2022): 2038. http://dx.doi.org/10.3390/antiox11102038.
Full textDissertations / Theses on the topic "NADPH oxidase (Nox) family"
Okasha, Mohamed Elsir Elnabeeb. "Identification and quantification of regional expression of members of the NADPH oxidase (NOX) enzyme family during the estrous cycles in the bovine oviduct /." Berlin : Mbv, 2009. http://d-nb.info/994595913/04.
Full textOkasha, Mohamed Elsir Elnageeb [Verfasser]. "Identification and quantification of regional expression of members of the NADPH oxidase (NOX) enzyme family during the estrous cycles in the bovine oviduct / Mohamed Elsir Elnageeb Okasha." Berlin : Freie Universität Berlin, 2009. http://d-nb.info/1023582287/34.
Full textCavallin, Lucas E. "The Role of PDGF AND Rac1-induced Oxidative Signaling in the Viral Oncogenesis of Kaposi's Sarcoma." Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_dissertations/441.
Full textChen, Alpha Yan. "Role of Intracellular Oxidant Release in Oxidised Low Lipoprotein - Induced U937 Cell Death." Thesis, University of Canterbury. School of Biological Science, 2012. http://hdl.handle.net/10092/7006.
Full textBednorz, Mariola [Verfasser]. "Die Rolle der NADPH-Oxidase (NOX)-Untereinheit, Nox Organizer 1 (NOXO1), in der Pathogenese des Zigarettenrauch-induzierten Lungenemphysem und der pulmonalen Hypertonie im Mausmodell / Mariola Bednorz." Gießen : Universitätsbibliothek, 2021. http://d-nb.info/1225774217/34.
Full textLambeth, Elise. "Characterisation of a family of NADPH oxidase encoding genes in the roice blast Magnaporthe oryzae." Thesis, University of Exeter, 2010. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.529318.
Full textKarimi, Gilda. "Etude de l'assemblage de la NADPH oxydase du phagocyte." Thesis, Paris 11, 2014. http://www.theses.fr/2014PA112025.
Full textThe NADPH oxidase of phagocytes is an enzyme involved in the innate defense of organisms against pathogens. After phagocyte activation, this enzyme produces superoxide ions by reduction of dioxygen by NADPH. It is constituted of four cytosolic sub-units (p47phox ; p67phox ; p40phox et Rac) and two membrane proteins (gp91 ; p22phox). Its activation takes place through a complex process that involves protein-protein interaction changes leading to assembly and functionning of the catalytic core. In order to obtain information on this process, I have reconstituted the enzyme in a cell free systeme using recombinant proteins, to be able to fully control all the measurement conditions. In this work, we have compared different activation modes of p47phox i) phosphorylation; ii) substitution serine - aspartate by mutations at positions S303, S304 and S328 to mimic phosphorylation; iii) addition of arachidonic acid (AA), a well known activator molecule in vitro. It has been shown that these three activating methods transform p47phox to an open configuration with similar characteristics. However, we have found that the effects of these methods are significantly different. Indeed, the conformational changes observed by circular dichroism are different. For p47phox, the addition of AA destructures the protein. Its phosphorylation induces a bathochromic displacement of the bands, whereas the mutations S-D lead to an opposite displacement. For the dimer p47phox-p67phox , the addition of AA destructures the proteins while mutations induce hardly no changes. We have measured the dissociation constant Kd of the complex p47phox-p67phox. For wild type proteins, Kd value is low (4±2 nM), while mutations of p47phox as well as addition of AA increase its value up to 50 nM, showing a decrease of affinity between p47phox and p67phox. Moreover, on the whole complex, the effect of phosphorylation of p47phox is different from mutations. We have shown that the EC50 values relative to p67phox are sensitive to the various modifications of p47phox. Phosphorylation of p47phox decreases EC₅₀, while double or triple mutations increase its value. We have confirmed that phosphorylation and mutation are not sufficient to activate the enzyme. The presence of AA is a prerequisite for the functionning of the complex, i.e. production of superoxide. The binding order of the cytosolic proteins seems random but it is necessary that all the components be present during the activation by AA. Finally, deletion of the C terminal part of p47phox (aa 343 to 390, interaction domain with p67phox) leads to the absence of dimer formation but does not affect the enzyme activity. These results bring new information on the role of dimerisation of p47-p67 and on that of phosphorylation in the activation of NADPH oxidase in vitro
Debbabi, Maya. "Mécanismes de régulation de la NADPH Oxydase NOX1 : rôle de la phosphorylation de NOXA1 ( NOX Activator 1 ) et de NOXO1 ( NOX Organizer 1)." Phd thesis, Université Paris Sud - Paris XI, 2011. http://tel.archives-ouvertes.fr/tel-00769943.
Full textFan, Lampson Min. "The role of endothelial cells in the regulation of the vascular response to Angiotensin II." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:3723698f-11e4-456f-9988-4020ec94ae87.
Full textHernandez, Isabelle. "Étude de l’expression, de l’activité et du rôle de la NADPH oxydase dans la villosité choriale au premier trimestre de la grossesse : implication dans la physiopathologie de la prééclampsie NADPH oxidase is the major source of placental superoxide in early pregnancy: association with MAPK pathway activation sFlt-1 secretion in early first trimester chorionic villi is associated with p38 MAPK pathway activation NADPH oxydase : enzyme potentiellement impliquée dans la physiopathologie de la prééclampsie." Thesis, Sorbonne Paris Cité, 2019. http://www.theses.fr/2019USPCB051.
Full textThe placenta is a transitory organ allowing gas and nutrients exchanges between mother and fetus. The structural and functional unit of the human placenta is the chorionic villi (CV). It is composed by a mesenchymal axis covered with a cellular layer called villous cytotrophoblast (VCT), which merges to form the syncytiotrophoblast (ST). The ST secretes hormones essential to maintain pregnancy, especially hCG. During the first trimester of pregnancy (T1), placenta develops itself in a poor oxygenated environment because of the obstruction of uterine spiraled arteries by cytotrophoblastic plugs which restrain the entry of the oxygenated maternal blood into the intervillous space (IVS). Between 10-12 gestational weeks (GW), the plugs will gradually disappear allowing blood to enter IVS in direct contact with CV. The pO2 will increase from 20 mmHg to 60 mmHg. Exposed to O2, the cell produces reactive oxygen species (ROS). ROS play a role as second messenger in redox-sensitive signaling pathways involved in physiological processes (proliferation, differentiation, apoptosis). They may become cytotoxic when oxidative stress occurs: the cell has an antioxidant defense system responsible for keeping low physiological levels of intracellular ROS, enough to ensure signal transduction. The balance between pro- and antioxidant systems is called redox homeostasis. The first trimester placenta is submitted to an environmental transition requiring redox balance adaptation to allow correct placental development in early pregnancy. The aim of this works are: (i) to determine the principal source of superoxide anion O2.- before and after the increase of pO2 in the intervillous space and the associated antioxidant defenses. (ii) To study the impact of the O2 transition on the activity of redox-sensitive pathways, specifically MAPKs involved in trophoblastic proliferation, differentiation. (iii) To determine, during T1, the placental NADPH oxidase (Nox) activity influence on the secretion of the antiangiogenic factor sFlt-1, which is involved in the pathophysiology of preeclampsia (PE), to offer new insight about Nox involvement in genesis of this pathology with placental origin. We measured the O2.- production in CV (7-9 GW vs. 12-14 GW). The O2.- assay was performed with specific inhibitors of ROS sources. The results show that NADPH oxidase (Nox) is the major source of O2.- in first trimester CV. Nox activity is significantly higher before 10 GW. This is confirmed by the modification of the Nox2 organizer subunit location, p47phox. This Nox activation in early stage of pregnancy is associated with p38 MAPK activation. p38 protein is mainly located within the villous cytotrophoblast in first trimester CV. Genic and protein expression study reveals the expression of Nox2, Nox4 and Nox5 isoforms in T1 trophoblast. Nox1 expression remains undetectable. The antioxidant enzymes (SOD1, catalase, and Gpx1) activities are increased at 12-14 GW, revealing an antioxidant system adaptation to the oxygen transition. We exposed CV from 7 to 9 GW to TGF-B1, described as an activator of Nox4 and p38MAPK, and to p38 inhibitor (SB203580). The results showed that the activation of p38MAPK pathway in first trimester CV by TGF-B1 increases the level of secreted sFlt-1. This effect is abolished using SB203580. TGF-B1 exposure does not influence the activation of placental Nox in our model, but the use of a Nox inhibitor (DPI) decreases the secretion of sFlt-1. To conclude, our work shows that Nox is the main source of O2.- in first trimester placenta and is associated with the activation of the p38MAPK pathway. Our results also demonstrate that first trimester CV sFlt-1 secretion relies on the p38MAPK activation. This work allows a better understanding of the cellular sources of ROS involvement in early placental development and their role in pathogenesis of preeclampsia
Book chapters on the topic "NADPH oxidase (Nox) family"
Sumimoto, Hideki, Reiko Minakami, and Kei Miyano. "Soluble Regulatory Proteins for Activation of NOX Family NADPH Oxidases." In Methods in Molecular Biology, 121–37. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9424-3_8.
Full textRada, Balázs, and Thomas L. Leto. "Oxidative Innate Immune Defenses by Nox/Duox Family NADPH Oxidases." In Contributions to Microbiology, 164–87. Basel: KARGER, 2008. http://dx.doi.org/10.1159/000136357.
Full textSumimoto, Hideki, Reiko Minakami, and Kei Miyano. "The Nox Family of NADPH Oxidases that Deliberately Produce Reactive Oxygen Species." In Frontiers of Gastrointestinal Research, 23–34. Basel: KARGER, 2010. http://dx.doi.org/10.1159/000319935.
Full textMiyano, Kei, and Hideki Sumimoto. "Assessment of the Role for Rho Family GTPases in NADPH Oxidase Activation." In Methods in Molecular Biology, 195–212. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-442-1_14.
Full textAbo, Arie, and Anthony W. Segal. "[29] Reconstitution of cell-free NADPH oxidase activity by purified components." In Small GTPases and Their Regulators Part B: Rho Family, 268–78. Elsevier, 1995. http://dx.doi.org/10.1016/0076-6879(95)56031-9.
Full textConference papers on the topic "NADPH oxidase (Nox) family"
Zhao, Guiqing, Sherene Thomas, Gregory Kowalsky, John W. Christman, Feng Qian, Irena Levitan, Jing Deng, and Lei Xiao. "Lipopolysaccharide (LPS) Stimulation Up-regulates The Expression Of NADPH Oxidase (NOX) In Mouse Bone Marrow-derived Macrophages (BMDM)." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1277.
Full textWang, Rong, Wan-Mohaiza Dashwood, Hui Nian, Naoto Tsuchiya, Hitoshi Nakagama, and Roderick Dashwood. "Abstract B84: NADPH oxidase 1 (NOX1) and related NOX isoforms as key mediators of NFκB signaling in colon cancer." In Abstracts: Frontiers in Cancer Prevention Research 2008. American Association for Cancer Research, 2008. http://dx.doi.org/10.1158/1940-6207.prev-08-b84.
Full textLin, Yun, Nicholas Hoffman, Mark Aksoy, Madesh Muniswamy, and Steven Kelsen. "Cigarette Smoke-Induced Reactive Oxygen Species (ROS) Production In Human Airway Epithelial Cells Is Calcium And NADPH-Oxidase (NOX) Dependent." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4561.
Full textThomas, Sherene, Guiqing Zhao, John W. Christman, and Lei Xiao. "Activation Of Toll-Like Receptor (TLR) 9 And TLR4 Differentially Regulate The Expression Of Nadph Oxidase (NOX) Enzyme Isoforms In Bone Marrow-Derived Macrophages (BMDM)." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2810.
Full textReports on the topic "NADPH oxidase (Nox) family"
Dickman, Martin B., and Oded Yarden. Modulation of the Redox Climate and Phosphatase Signaling in a Necrotroph: an Axis for Inter- and Intra-cellular Communication that Regulates Development and Pathogenicity. United States Department of Agriculture, August 2011. http://dx.doi.org/10.32747/2011.7697112.bard.
Full textHorwitz, Benjamin A., and Barbara Gillian Turgeon. Fungal Iron Acquisition, Oxidative Stress and Virulence in the Cochliobolus-maize Interaction. United States Department of Agriculture, March 2012. http://dx.doi.org/10.32747/2012.7709885.bard.
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