NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology

Antioxidants - Tập 10 Số 6 - Trang 890
Annelise Vermot1, Isabelle Petit-Härtlein1, Susan M. E. Smith2, Franck Fieschi1
1IBS - UMR 5075 - Institut de biologie structurale (Institut de Biologie Structurale, 71 avenue des martyrs, CS 10090, 38044 Grenoble Cedex 9 - France)
2Department of Molecular and Cellular Biology, Kennesaw State University, Kennesaw, GA 30144, USA

Tóm tắt

The reactive oxygen species (ROS)-producing enzyme NADPH oxidase (NOX) was first identified in the membrane of phagocytic cells. For many years, its only known role was in immune defense, where its ROS production leads to the destruction of pathogens by the immune cells. NOX from phagocytes catalyzes, via one-electron trans-membrane transfer to molecular oxygen, the production of the superoxide anion. Over the years, six human homologs of the catalytic subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the NOX2/gp91phox component present in the phagocyte NADPH oxidase assembly itself, the homologs are now referred to as the NOX family of NADPH oxidases. NOX are complex multidomain proteins with varying requirements for assembly with combinations of other proteins for activity. The recent structural insights acquired on both prokaryotic and eukaryotic NOX open new perspectives for the understanding of the molecular mechanisms inherent to NOX regulation and ROS production (superoxide or hydrogen peroxide). This new structural information will certainly inform new investigations of human disease. As specialized ROS producers, NOX enzymes participate in numerous crucial physiological processes, including host defense, the post-translational processing of proteins, cellular signaling, regulation of gene expression, and cell differentiation. These diversities of physiological context will be discussed in this review. We also discuss NOX misregulation, which can contribute to a wide range of severe pathologies, such as atherosclerosis, hypertension, diabetic nephropathy, lung fibrosis, cancer, or neurodegenerative diseases, giving this family of membrane proteins a strong therapeutic interest.

Từ khóa


Tài liệu tham khảo

Warburg, 1908, Beobachtungen uber die Oxydationsprozeesse im Seeigelei, Z. Physiol. Chem., 57, 1, 10.1515/bchm2.1908.57.1-2.1

Baldridge, 1932, The Extra Respiration of Phagocytosis, Am. J. Physiol., 103, 235, 10.1152/ajplegacy.1932.103.1.235

Sbarra, 1959, The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes, J. Biol. Chem., 234, 1355, 10.1016/S0021-9258(18)70011-2

Iyer, 1961, Biochemical Aspects of Phagocytosis, Nature, 192, 535, 10.1038/192535a0

Rossi, 1964, Biochemical Aspects of Phagocytosis in Polymorphonuclear Leucocytes. NADH and NADPH Oxidation by the Granules of Resting and Phagocytizing Cells, Experientia, 20, 21, 10.1007/BF02146019

Babior, 1975, Pyridine nucleotide-dependent superoxide production by a cell-free system from human granulocytes, J. Clin. Investig., 56, 1035, 10.1172/JCI108150

Clark, 1987, NADPH oxidase of human neutrophils. Subcellular localization and characterization of an arachidonate-activatable superoxide generating system, J. Biol. Chem., 262, 4065, 10.1016/S0021-9258(18)61312-2

Klebanoff, 1970, Myeloperoxidase: Contribution to the microbicidal activity of intact leukocytes, Science, 169, 1095, 10.1126/science.169.3950.1095

Babior, 1973, Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent, J. Clin. Investig., 52, 741, 10.1172/JCI107236

Abuaita, 2018, Mitochondria-Derived Vesicles Deliver Antimicrobial Reactive Oxygen Species to Control Phagosome-Localized Staphylococcus aureus, Cell Host Microbe, 24, 625, 10.1016/j.chom.2018.10.005

Berendes, 1957, A fatal granulomatosus of childhood: The clinical study of a new syndrome, Minn. Med., 40, 309

Quie, 1967, In Vitro Bactericidal Capacity of Human Polymorphonuclear Leukocytes: Diminished Activity in Chronic Granulomatous Disease of Childhood, J. Clin. Investig., 46, 668, 10.1172/JCI105568

Johnston, 1971, Chronic Granulamatous Disease: Correlation Between Pathogenesis and Clinical Findings, Pediatrics, 48, 730, 10.1542/peds.48.5.730

Baehner, 1967, Leukocyte oxidase: Defective activity in chronic granulomatous disease, Science, 155, 835, 10.1126/science.155.3764.835

Holmes, 1967, Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function, J. Clin. Investig., 46, 1422, 10.1172/JCI105634

Cross, 2004, The NADPH oxidase of professional phagocytes-prototype of the NOX electron transport chain systems, Biochim. Biophys. Acta, 1657, 1, 10.1016/j.bbabio.2004.03.008

Bellavite, 1983, The cytochrome b and flavin content and properties of the O2−-forming NADPH oxidase solubilized from activated neutrophils, Biochim. Biophys. Acta, 746, 40, 10.1016/0167-4838(83)90008-0

Gabig, 1978, Solubilization of the 02--forming Activity Responsible for the Respiratory Burst in Human Neutrophils, J. Biol. Chem., 253, 6663, 10.1016/S0021-9258(17)37968-1

Bellavite, 1988, The superoxide-forming enzymatic system of phagocytes, Free Radic. Biol. Med., 4, 225, 10.1016/0891-5849(88)90044-5

Hattori, 1961, Studies on the labile, stable Nadi oxidase and peroxidase staining reactions in the isolated particles of horse granulocyte, Nagoya J. Med. Sci., 23, 362

Segal, 2011, Chronic granulomatous disease: Lessons from a rare disorder, Biol. Blood Marrow Transplant., 17, S123, 10.1016/j.bbmt.2010.09.008

Winkelstein, 2000, Chronic granulomatous disease: Report on a national registry of 368 patients, Medicine, 79, 155, 10.1097/00005792-200005000-00003

Segal, 1978, Novel cytochrome b system in phagocytic vacuoles of human granulocytes, Nature, 276, 515, 10.1038/276515a0

Segal, 1979, The Subcellular Distribution and some Properties of the Cytochrome b Component of the Microbicidal Oxidase System of Human Neutrophils, Biochem. J., 182, 181, 10.1042/bj1820181

Yu, 1998, Gp91phox is the heme binding subunit of the superoxide-generating NADPH oxidase, Proc. Natl. Acad. Sci. USA, 95, 7993, 10.1073/pnas.95.14.7993

Quinn, 1992, Human Neutrophil Cytochrome b Contains Multiple Hemes, J. Biol. Chem., 267, 7303, 10.1016/S0021-9258(18)42519-7

Cross, 1995, Cytochrome b−245 of the Neutrophil Superoxide-generating System Contains Two Nonidentical Hemes, J. Biol. Chem., 270, 17075, 10.1074/jbc.270.29.17075

Segal, 1992, Cytochrome b-245 is a flavocytochrome containing FAD and the NADPH-binding site of the microbicidal oxidase of phagocytes, Biochem. J., 284, 781, 10.1042/bj2840781

Cross, 1984, The superoxide-generating oxidase of leucocytes. NADPH-dependent reduction of flavin and cytochrome b in solubilized preparations, Biochem. J., 223, 337, 10.1042/bj2230337

Dinauer, 1987, The glycoprotein encoded by the X-linked chronic granulomatous disease locus is a component of the neutrophil cytochrome b complex, Nature, 327, 717, 10.1038/327717a0

Parkos, 1987, Purified cytochrome b from human granulocyte plasma membrane is comprised of two polypeptides with relative molecular weights of 91,000 and 22,000, J. Clin. Investig., 80, 732, 10.1172/JCI113128

1928, Oxidation von Glukose mit Extrakten aus Aspegillus niger, Biochem. Z., 199, 136

Rossi, 1964, Changes in the Metabolic Pattern of Polymorpho-Nuclear Leucocytes during Phagocytosis, Br. J. Exp. Pathol., 45, 548

Klebanoff, 1975, Antimicrobial mechanisms in neutrophilic polymorphonuclear leukocytes, Semin. Hematol., 12, 117

Babior, 1978, Oxygen-dependent microbial killing by phagocytes (first of two parts), N. Engl. J. Med., 298, 659, 10.1056/NEJM197803232981205

Bromberg, 1984, Unsaturated fatty acids stimulate NADPH-dependent superoxide production by cell-free system derived from macrophages, Cell. Immunol., 88, 213, 10.1016/0008-8749(84)90066-2

Kunkel, 1986, Cloning the gene for an inherited human disorder-chronic granulomatous disease-on the basis of its chromosomal location, Nature, 322, 32, 10.1038/322032a0

Teahan, 1987, The X-linked chronic granulomatous disease gene codes for the beta-chain of cytochrome b-245, Nature, 327, 720, 10.1038/327720a0

Nunoi, 1988, Two forms of autosomal chronic granulomatous disease lack distinct neutrophil cytosol factors, Science, 242, 1298, 10.1126/science.2848319

Volpp, 1988, Two cytosolic neutrophil oxidase components absent in autosomal chronic granulomatous disease, Science, 242, 1295, 10.1126/science.2848318

Abo, 1991, Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1, Nature, 353, 668, 10.1038/353668a0

Knaus, 1991, Regulation of the phagocyte oxygen radical production by the GTP-binding protein Rac 2, Science, 254, 1512, 10.1126/science.1660188

Wientjes, 1993, p40phox, a third cytosolic componet of the activation complex of the NADPH oxidase that contain src homology 3 domains, Biochem. J., 296, 557, 10.1042/bj2960557

Someya, 1993, Purification of the 260 kDa cytosolic complex involved in the superoxide production of guinea pig neutrophils, FEBS Lett., 330, 215, 10.1016/0014-5793(93)80276-Z

Groom, 1996, RbohA, a rice homologue of the mammalian gp91phox respiratory burst oxidase gene, Plant J., 10, 515, 10.1046/j.1365-313X.1996.10030515.x

Suh, 1999, Cell transformation by the superoxide-generating oxidase Mox1, Nature, 401, 79, 10.1038/43459

Dupuy, 1999, Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase, J. Biol. Chem., 274, 37265, 10.1074/jbc.274.52.37265

Wang, 2000, Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family, J. Biol. Chem., 275, 23227, 10.1074/jbc.M000916200

Lapouge, 2000, Structure of the TPR Domain of p67phox in Complex with Rac·GTP, Mol. Cell, 6, 899, 10.1016/S1097-2765(05)00091-2

Grizot, 2001, Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation, Biochemistry, 40, 10007, 10.1021/bi010288k

Bravo, 2001, The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate, Mol. Cell, 8, 829, 10.1016/S1097-2765(01)00372-0

Hiroaki, 2001, Solution structure of the PX domain, a target of the SH3 domain, Nat. Struct. Biol., 8, 526, 10.1038/88591

Karathanassis, 2002, Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction, EMBO J., 21, 5057, 10.1093/emboj/cdf519

Kami, 2002, Diverse recognition of non-PxxP peptide ligands by the SH3 domains from p67phox, Grb2 and Pex13p, EMBO J., 21, 4268, 10.1093/emboj/cdf428

Groemping, 2003, Molecular basis of phosphorylation-induced activation of the NADPH oxidase, Cell, 113, 343, 10.1016/S0092-8674(03)00314-3

Wilson, 2003, PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62, Mol. Cell, 12, 39, 10.1016/S1097-2765(03)00246-6

Yuzawa, 2004, A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase, Genes Cells, 9, 443, 10.1111/j.1356-9597.2004.00733.x

Massenet, 2005, Effects of p47phox C terminus phosphorylations on binding interactions with p40phox and p67phox. Structural and functional comparison of p40phox and p67phox SH3 domains, J. Biol. Chem., 280, 13752, 10.1074/jbc.M412897200

Durand, 2006, Small-Angle X-ray Scattering Reveals an Extended Organization for the Autoinhibitory Resting State of the p47phox Modular Protein, Biochemistry, 45, 7185, 10.1021/bi060274k

Honbou, 2007, Full-length p40phox structure suggests a basis for regulation mechanism of its membrane binding, EMBO J., 26, 1176, 10.1038/sj.emboj.7601561

Marcoux, 2010, p47phox Molecular Activation for Assembly of the Neutrophil NADPH Oxidase Complex, J. Biol. Chem., 285, 28980, 10.1074/jbc.M110.139824

Durand, 2010, NADPH oxidase activator p67(phox) behaves in solution as a multidomain protein with semi-flexible linkers, J. Struct. Biol., 169, 45, 10.1016/j.jsb.2009.08.009

Hajjar, 2017, The NOX Family of Proteins Is Also Present in Bacteria, mBio, 8, 1487, 10.1128/mBio.01487-17

Magnani, 2017, Crystal structures and atomic model of NADPH oxidase, Proc. Natl. Acad. Sci. USA, 114, 6764, 10.1073/pnas.1702293114

Sun, 2020, Structures of Mouse DUOX1–DUOXA1 Provide Mechanistic Insights into Enzyme Activation and Regulation, Nat. Struct. Mol. Biol., 27, 1086, 10.1038/s41594-020-0501-x

Harper, 1985, Cytochrome b-245 from human neutrophils is a glycoprotein, Biochem. J., 227, 783, 10.1042/bj2270783

Pick, 2020, Cell-Free NADPH Oxidase Activation Assays: A Triumph of Reductionism, Methods Mol. Biol., 2087, 325, 10.1007/978-1-0716-0154-9_23

Wilde, 1989, Chemoattractant-stimulated GTPase activity is decreased on membranes from polymorphonuclear leukocytes incubated in chemoattractant, J. Biol. Chem., 264, 190, 10.1016/S0021-9258(17)31242-5

Ambruso, 2000, Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation, Proc. Natl. Acad. Sci. USA, 97, 4654, 10.1073/pnas.080074897

Williams, 2000, Dominant negative mutation of the hematopoietic-specific Rho GTPase, Rac2, is associated with a human phagocyte immunodeficiency, Blood, 96, 1646

DeCoursey, 2001, The gp91phox component of NADPH oxidase is not the voltage-gated proton channel in phagocytes, but it helps, J. Biol. Chem., 276, 36063, 10.1074/jbc.C100352200

Lambeth, 2004, NOX enzymes and the biology of reactive oxygen, Nat. Rev. Immunol., 4, 181, 10.1038/nri1312

Arbault, 1997, Activation of the NADPH oxidase in human fibroblasts by mechanical intrusion of a single cell with an ultramicroelectrode, Carcinogenesis, 18, 569, 10.1093/carcin/18.3.569

Szatrowski, 1991, Production of large amounts of hydrogen peroxide by human tumor cells, Cancer Res., 51, 794

Griendling, 2000, NAD(P)H Oxidase Role in Cardiovascular Biology and Disease, Circ Res., 86, 494, 10.1161/01.RES.86.5.494

Maturana, 2000, A mammalian H+ channel generated through alternative splicing of the NADPH oxidase homolog NOH-1, Science, 287, 138, 10.1126/science.287.5450.138

Kikuchi, 2000, NADPH oxidase subunit, gp91phox homologue, preferentially expressed in human colon epithelial cells, Gene, 254, 237, 10.1016/S0378-1119(00)00258-4

Geiszt, 2000, Identification of Renox, an NAD(P)H oxidase in kidney, Proc. Natl. Acad. Sci. USA, 97, 8010, 10.1073/pnas.130135897

Molnar, 2001, A Ca2+ activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes, J. Biol. Chem., 276, 37594, 10.1074/jbc.M103034200

Zhang, X., Krause, K.H., Xenarios, I., Soldati, T., and Boeckmann, B. (2013). Evolution of the Ferric Reductase Domain (FRD) Superfamily: Modularity, Functional Diversification, and Signature Motifs. PLoS ONE, 8.

Ambasta, 2004, Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase, J. Biol. Chem., 279, 45935, 10.1074/jbc.M406486200

Kuroda, 2005, The superoxide-producing NAD(P)H oxidase Nox4 in the nucleus of human vascular endothelial cells, Genes Cells, 10, 1139, 10.1111/j.1365-2443.2005.00907.x

Ago, 2010, Upregulation of Nox4 by hypertrophic stimuli promotes apoptosis and mitochondrial dysfunction in cardiac myocytes, Circ. Res., 106, 1253, 10.1161/CIRCRESAHA.109.213116

Gabig, 1979, The O2(-)-forming oxidase responsible for the respiratory burst in human neutrophils. Properties of the solubilized enzyme, J. Biol. Chem., 254, 9070, 10.1016/S0021-9258(19)86810-2

Ray, 2012, Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling, Cell. Signal., 24, 981, 10.1016/j.cellsig.2012.01.008

Lambeth, 2014, Nox Enzymes and New Thinking on Reactive Oxygen: A Double-Edged Sword Revisited, Annu. Rev. Pathol., 9, 119, 10.1146/annurev-pathol-012513-104651

Nathan, 2013, Beyond oxidative stress: An immunologist’s guide to reactive oxygen species, Nat. Rev. Immunol., 13, 349, 10.1038/nri3423

Parvez, 2018, Redox Signaling by Reactive Electrophiles and Oxidants, Chem. Rev., 118, 8798, 10.1021/acs.chemrev.7b00698

Bedard, 2007, The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology, Physiol. Rev., 87, 245, 10.1152/physrev.00044.2005

Dang, 2001, Assembly of the neutrophil respiratory burst oxidase: A direct interaction between p67phox and cytochrome b558, Proc. Natl. Acad. Sci. USA, 98, 3001, 10.1073/pnas.061029698

Babior, 2004, NADPH oxidase, Curr. Opin. Immunol., 16, 42, 10.1016/j.coi.2003.12.001

Clark, 1990, Two cytosolic components of the human neutrophil respiratory burst oxidase translocate to the plasma membrane during cell activation, J. Clin. Investig., 85, 714, 10.1172/JCI114496

Leto, 2006, Role of Nox Family NADPH Oxidases in Host Defense, Antioxid. Redox Signal., 8, 1549, 10.1089/ars.2006.8.1549

Parkos, 1989, Absence of both the 91kD and 22kD subunits of human neutrophil cytochrome b in two genetic forms of chronic granulomatous disease, Blood, 73, 1416, 10.1182/blood.V73.6.1416.1416

DeLeo, 1995, Mapping sites of interaction of p47-phox and flavocytochrome b with random-sequence peptide phage display libraries, Proc. Natl. Acad. Sci. USA, 92, 7110, 10.1073/pnas.92.15.7110

Kawahara, T., Quinn, M.T., and Lambeth, J.D. (2007). Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes. BMC Evol. Biol., 7.

Magnani, 2019, Structure and mechanisms of ROS generation by NADPH Oxidases, Curr. Opin. Struct. Biol., 59, 91, 10.1016/j.sbi.2019.03.001

Cross, 1995, The Cytosolic Activating Factors p47phox and p67phox Have Distinct Roles in the Regulation of Electron Flow in NADPH Oxidase, J. Biol. Chem., 270, 6543, 10.1074/jbc.270.12.6543

Nguyen, 2015, NADPH oxidases, Nox: New isoenzymes family, Med. Sci., 31, 43

Debeurme, 2010, Regulation of NADPH oxidase activity in phagocytes: Relationship between FAD/NADPH binding and oxidase complex assembly, J. Biol. Chem., 285, 33197, 10.1074/jbc.M110.151555

Gaillard, 1996, Electron Transfer Across the O2-Generating Flavocytochrome b of Neutrophils. Evidence for a Transition from a Low-Spin State to a High-Spin State of the Heme Iron Component, Biochemistry, 35, 13400, 10.1021/bi960916b

Vignais, 2002, The superoxide-generating NADPH oxidase: Structural aspects and activation mechanism, Cell. Mol. Life Sci. CMLS, 59, 1428, 10.1007/s00018-002-8520-9

Koshkin, 1995, Spatial and electrogenic properties of superoxide-producing cytochrome b-559 incorporated into liposomes, Biochim. Biophys. Acta, 1229, 329, 10.1016/0005-2728(95)00009-8

Cross, 1985, Mechanism of the superoxide-producing oxidase of neutrophils, Biochem. J., 226, 881, 10.1042/bj2260881

Ceccon, 2017, Engineering stability in NADPH oxidases: A common strategy for enzyme production, Mol. Membr. Biol., 34, 67, 10.1080/09687688.2018.1535141

Isogai, 1995, The Mechanism of Electron Donation to Molecular Oxygen by Phagocytic Cytochrome b558, J. Biol. Chem., 270, 7853, 10.1074/jbc.270.14.7853

DeLeo, 2000, Processing and maturation of flavocytochrome b558 include incorporation of heme as a prerequisite for heterodimer assembly, J. Biol. Chem., 275, 13986, 10.1074/jbc.275.18.13986

Leto, 1994, Assembly of the phagocyte NADPH oxidase: Binding of Src homology 3 domains to proline-rich targets, Proc. Natl. Acad. Sci. USA, 91, 10650, 10.1073/pnas.91.22.10650

Ogura, 2006, NMR solution structure of the tandem Src homology 3 domains of p47phox complexed with a p22phox-derived proline-rich peptide, J. Biol. Chem., 281, 3660, 10.1074/jbc.M505193200

Sumimoto, 2008, Structure, regulation and evolution of Nox-family NADPH oxidases that produce reactive oxygen species, FEBS J., 275, 3249, 10.1111/j.1742-4658.2008.06488.x

Taylor, 2004, Site-Specific Inhibitors of NADPH Oxidase Activity and Structural Probes of Flavocytochrome b: Characterization of Six Monoclonal Antibodies to the p22phox Subunit, J. Immunol., 173, 7349, 10.4049/jimmunol.173.12.7349

Dahan, 2002, Mapping of functional domains in the p22(phox) subunit of flavocytochrome b(559) participating in the assembly of the NADPH oxidase complex by peptide walking, J. Biol. Chem., 277, 8421, 10.1074/jbc.M109778200

Rae, 2000, Molecular analysis of 9 new families with chronic granulomatous disease caused by mutations in CYBA, the gene encoding p22(phox), Blood, 96, 1106, 10.1182/blood.V96.3.1106

Meijles, 2012, Consensus in silico computational modelling of the p22phox subunit of the NADPH oxidase, Comput. Biol. Chem., 39, 6, 10.1016/j.compbiolchem.2012.05.001

Zhu, 2006, Deletion Mutagenesis of p22phox Subunit of Flavocytochrome b558: Identification of regions critical for gp91phox maturation and NADPH oxidase activity, J. Biol. Chem., 281, 30336, 10.1074/jbc.M607191200

Nobuhisa, 2006, Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognitionof a polyproline type II helix and an adjacent α-helix of p22phox, Biochem. J., 396, 183, 10.1042/BJ20051899

Adams, 1996, Multiple SH3 domain interactions regulate NADPH oxidase assembly in whole cells, EMBO J., 15, 1211, 10.1002/j.1460-2075.1996.tb00462.x

Ito, 2001, Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions, EMBO J., 20, 3938, 10.1093/emboj/20.15.3938

Noda, 2003, Molecular recognition in dimerization between PB1 domains, J. Biol. Chem., 278, 43516, 10.1074/jbc.M306330200

Ago, 1999, Mechanism for Phosphorylation-induced Activation of the Phagocyte NADPH Oxidase Protein p47 phox, J. Biol. Chem., 274, 33644, 10.1074/jbc.274.47.33644

Ziegler, 2019, Quantitative live-cell imaging and 3D modeling reveal critical functional features in the cytosolic complex of phagocyte NADPH oxidase, J. Biol. Chem., 294, 3824, 10.1074/jbc.RA118.006864

Nisimoto, 1999, The p67(phox) activation domain regulates electron flow from NADPH to flavin in flavocytochrome b(558), J. Biol. Chem., 274, 22999, 10.1074/jbc.274.33.22999

Yatomi, 2001, Rac, a small guanosine triphosphate–binding protein, and p21-activated kinase are activated during platelet spreading on collagen-coated surfaces: Roles of integrin α2β1, Blood, 98, 3708, 10.1182/blood.V98.13.3708

Caron, 2003, Cellular functions of the Rap1 GTP-binding protein: A pattern emerges, J. Cell Sci., 116, 435, 10.1242/jcs.00238

Ueyama, 2005, Isoform-Specific Membrane Targeting Mechanism of Rac during FcγR-Mediated Phagocytosis: Positive Charge-Dependent and Independent Targeting Mechanism of Rac to the Phagosome, J. Immunol., 175, 2381, 10.4049/jimmunol.175.4.2381

Jaśkiewicz, A., Pająk, B., and Orzechowski, A. (2018). The Many Faces of Rap1 GTPase. Int. J. Mol. Sci., 19.

Joseph, 1994, Inhibition of NADPH oxidase activation by synthetic peptides mapping within the carboxyl-terminal domain of small GTP-binding proteins. Lack of amino acid sequence specificity and importance of polybasic motif, J. Biol. Chem., 269, 29024, 10.1016/S0021-9258(19)62008-9

Wilson, 2016, Differences in the Phosphorylation-Dependent Regulation of Prenylation of Rap1A and Rap1B, J. Mol. Biol., 428, 4929, 10.1016/j.jmb.2016.10.016

Miyano, 2006, Direct Involvement of the Small GTPase Rac in Activation of the Superoxide-producing NADPH Oxidase Nox1, J. Biol. Chem., 281, 21857, 10.1074/jbc.M513665200

Quinn, 2004, Structure and regulation of the neutrophil respiratory burst oxidase: Comparison with nonphagocyte oxidases, J. Leuk. Biol., 76, 760, 10.1189/jlb.0404216

Bokoch, 1991, Inhibition of Rap1A binding to cytochrome b558 of NADPH oxidase by phosphorylation of Rap1A, Science, 254, 1794, 10.1126/science.1763330

Gabig, 1995, Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated HL60 cell NADPH oxidase activation, Blood, 85, 804, 10.1182/blood.V85.3.804.bloodjournal853804

Li, 2007, Rap1a null mice have altered myeloid cell functions suggesting distinct roles for the closely related Rap1a and 1b proteins, J. Immunol., 179, 8322, 10.4049/jimmunol.179.12.8322

Nguyen, 2017, Neutrophils to the ROScue: Mechanisms of NADPH Oxidase Activation and Bacterial Resistance, Front Cell Infect. Microbiol., 25, 373, 10.3389/fcimb.2017.00373

Yang, 2012, Autophagy Protein Rubicon Mediates Phagocytic NADPH Oxidase Activation in Response to Microbial Infection or TLR Stimulation, Cell Host Microbe, 11, 264, 10.1016/j.chom.2012.01.018

DeLeo, 1999, NADPH oxidase activation and assembly during phagocytosis, J. Immunol., 163, 6732, 10.4049/jimmunol.163.12.6732

Ueyama, 2007, A regulated adaptor function of p40phox: Distinct p67phox membrane targeting by p40phox and by p47phox, Mol. Biol. Cell, 18, 441, 10.1091/mbc.e06-08-0731

Freeman, 1996, NADPH oxidase activity is independent of p47phox in vitro, J. Biol. Chem., 271, 22578, 10.1074/jbc.271.37.22578

Koshkin, 1991, The cytosolic component p47(phox) is not a sine qua non participant in the activation of NADPH oxidase but is required for optimal superoxide production, J. Biol. Chem., 271, 30326, 10.1074/jbc.271.48.30326

Morgan, 2011, Crosstalk of reactive oxygen species and NF-κB signaling, Cell Res., 21, 103, 10.1038/cr.2010.178

Dickinson, 2012, Chemistry and biology of reactive oxygen species in signaling, Nat. Chem. Biol., 7, 504, 10.1038/nchembio.607

Alloul, 2001, Activation of the Superoxide-Generating NADPH Oxidase by Chimeric Proteins Consisting of Segments of the Cytosolic Component p67phox and the Small GTPase Rac1, Biochemistry, 40, 14557, 10.1021/bi0117347

Berdichevsky, 2007, Tripartite Chimeraripartite chimeras comprising functional domains derived from the cytosolic NADPH oxidase components p47phox, p67phox, and Rac1 elicit activator-independent superoxide production by phagocyte membranes, J. Biol. Chem., 282, 22122, 10.1074/jbc.M701497200

Miyano, 2003, Remarkable Stabilization of Neutrophil NADPH Oxidase Using RacQ61L and a p67phox−p47phox Fusion Protein, Biochemistry, 42, 184, 10.1021/bi0269052

Ebisu, 2001, Fused p47phox and p67phox truncations efficiently reconstitute NADPH oxidase with higher activity and stability than the individual components, J. Biol. Chem., 276, 24498, 10.1074/jbc.M101122200

Valenta, H., Dupré-Crochet, S., Bizouarn, T., Baciou, L., Nüsse, O., Deniset-Besseau, A., and Erard, M. (2021). Consequences of the constitutive NOX2 activity in living cells: Cytosol acidification, apoptosis, and localized lipid peroxidation. BioRxiv Prepr.

Si, 2007, STAT5 Mediates Platelet-Activating Factor (PAF)-Induced NADPH Oxidase NOX5-S Expression In Barrett’s Esophageal Adenocarcinoma Cells, Am. J. Physiol. Gastrointest. Liver Physiol., 294, G174, 10.1152/ajpgi.00291.2007

Bylund, 2003, NADPH-oxidase activation in murine neutrophils via formyl peptide receptors, Exp. Cell. Res., 282, 70, 10.1016/S0014-4827(02)00010-1

Kim, 2007, TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death, Mol. Cell, 26, 675, 10.1016/j.molcel.2007.04.021

Boussetta, 2010, The prolyl isomerase Pin1 acts as a novel molecular switch for TNF-alpha-induced priming of the NADPH oxidase in human neutrophils, Blood, 116, 5795, 10.1182/blood-2010-03-273094

Liu, 2019, The Prolyl Isomerase Pin1 Controls Lipopolysaccharide-Induced Priming of NADPH Oxidase in Human Neutrophils, Front. Immunol., 10, 2567, 10.3389/fimmu.2019.02567

Faust, 1994, The phosphorylation of the respiratory burst oxidase component p47(phox) during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases, J. Biol. Chem., 269, 23431, 10.1016/S0021-9258(17)31534-X

Inanami, 1998, Activation of the leukocyte NADPH oxidase by phorbol ester requires the phosphorylation of p47(PHOX) on serine 303 or 304, J. Biol. Chem., 273, 9539, 10.1074/jbc.273.16.9539

Marcoux, 2009, Conformational changes in p47phox upon activation highlighted by mass spectrometry coupled to hydrogen/deuterium exchange and limited proteolysis, FEBS Lett., 583, 835, 10.1016/j.febslet.2009.01.046

Dang, 2006, A specific p47phox-serine phosphorylated by convergent MAPKs mediates neutrophil NADPH oxidase priming at inflammatory sites, J. Clin. Investig., 116, 2033, 10.1172/JCI27544

Fontayne, 2002, Phosphorylation of p47phox sites by PKC alpha, beta II, delta, and zeta: Effect on binding to p22phox and on NADPH oxidase activation, Biochemistry, 41, 7743, 10.1021/bi011953s

Inanami, 2010, Phosphorylation of threonine 154 in p40phox is an important physiological signal for activation of the neutrophil NADPH oxidase, Blood, 116, 6026

DerMardirossian, 2004, Phosphorylation of RhoGDI by Pak1 Mediates Dissociation of Rac GTPase, Mol. Cell, 25, 117, 10.1016/j.molcel.2004.05.019

Pick, 2014, Role of the Rho GTPase Rac in the activation of the phagocyte NADPH oxidase: Outsourcing a key task, Small GTPases, 5, e27952, 10.4161/sgtp.27952

Nisimoto, 2004, Activation of the flavoprotein domain of gp91phox upon interaction with N-terminal p67phox (1-210) and the Rac complex, Biochemistry, 43, 9567, 10.1021/bi0400249

Regier, 2000, Phosphorylation of p22phox is mediated by phospholipase D-dependant and independent mechanisms. Correlation of NADPH oxidase activity and p22phox phopshorylation, J. Biol. Chem., 275, 28406, 10.1074/jbc.M004703200

Waite, 1997, Phosphatidic Acid-mediated Phosphorylation of the NADPH Oxidase Component p47-phox: Evidence That Phosphatidic Acid May Activate a Novel Protein Kinase, J. Biol. Chem., 272, 15569, 10.1074/jbc.272.24.15569

Regier, 1999, A novel protein kinase target for the lipid second messenger phosphatidic acid, J. Biol. Chem., 274, 36601, 10.1074/jbc.274.51.36601

Beaumel, 2017, Down-regulation of NOX2 activity in phagocytes mediated by ATM-kinase dependent phosphorylation, Free Radic. Biol. Med., 113, 1, 10.1016/j.freeradbiomed.2017.09.007

Raad, 2020, The protein kinase A negatively regulates reactive oxygen species production by phosphorylating gp91phox/NOX2 in human neutrophils, Free Radic. Biol. Med., 160, 19, 10.1016/j.freeradbiomed.2020.07.021

Kanai, 2001, The PX domains of p47phox and p40phox bind to lipid products of PI(3)K, Nat. Cell Biol., 3, 675, 10.1038/35083070

MLee, 1991, Mechanism of protein kinase C activation by phosphatidylinositol 4,5-bisphosphate, Biochemistry, 30, 1041, 10.1021/bi00218a023

Handlogten, 2001, The Ca21-sensing Receptor Activates Cytosolic Phospholipase A2 via a Gqa-dependent ERK-independent Pathway, J. Biol. Chem., 276, 13941, 10.1074/jbc.M007306200

Sellmayer, 1996, Arachidonic acid increases activation of NADPH oxidase in monocytic U937 cells by accelerated translocation of p47-phox and co-stimulation of protein kinase C, Cell. Signal., 8, 397, 10.1016/0898-6568(96)00077-0

Bizouarn, 2016, Exploring the arachidonic acid-induced structural changes in phagocyte NADPH oxidase p47phox and p67phox via thiol accessibility and SRCD spectroscopy, FEBS J., 283, 2896, 10.1111/febs.13779

Gaillard, 1999, The heme component of the neutrophil NADPH oxidase complex is a target for aryliodonium compounds, Biochemistry, 38, 3694, 10.1021/bi9823481

Shiose, 2000, Arachidonic acid and phosphorylation synergistically induce a conformational change of p47phox to activate the phagocyte NADPH oxidase, J. Biol. Chem., 275, 13793, 10.1074/jbc.275.18.13793

Swain, 1997, Analysis of activation-induced conformational changes in p47phox using tryptophan fluorescence spectroscopy, J. Biol. Chem., 272, 29502, 10.1074/jbc.272.47.29502

Bizouarn, 2019, A Close-Up View of the Impact of Arachidonic Acid on the Phagocyte NADPH Oxidase, Methods Mol. Biol., 1982, 75, 10.1007/978-1-4939-9424-3_5

Kim, 2006, Impaired NADPH oxidase activity in Rac2-deficient murine neutrophils does not result from defective translocation of p47phox and p67phox and can be rescued by exogenous arachidonic acid, J. Leukoc. Biol., 79, 223, 10.1189/jlb.0705371

Hata, 1998, Anionic amphiphile-independent activation of the phagocyte NADPH oxidase in a cell-free system by p47phox and p67phox, both in C terminally truncated forms. Implication for regulatory Src homology 3 domain-mediated interactions, J. Biol. Chem., 13, 4232, 10.1074/jbc.273.7.4232

Davis, 1998, Cloning and sequencing of the bovine flavocytochrome b subunit proteins, gp91-phox and p22-phox: Comparison with other known flavocytochrome b sequences, J. Leukoc. Biol., 64, 114, 10.1002/jlb.64.1.114

Segal, 2008, The function of the NADPH oxidase of phagocytes and its relationship to other NOXs in plants, invertebrates, and mammals, Int. J. Biochem. Cell Biol., 40, 604, 10.1016/j.biocel.2007.10.003

Takemoto, 2007, NADPH oxidases in fungi: Diverse roles of reactive oxygen species in fungal cellular differentiation, Fungal Genet. Biol., 44, 1065, 10.1016/j.fgb.2007.04.011

Bedard, 2007, NOX family NADPH oxidases: Not just in mammals, Biochimie, 89, 1107, 10.1016/j.biochi.2007.01.012

Krause, 2004, Tissue distribution and putative physiological function of NOX family NADPH oxydases, J. Infect. Dis., 57, 28

Rybak, 2012, siRNA-mediated knock-down of NOX3: Therapy for hearing loss?, Cell. Mol. Life Sci. CMLS, 69, 2429, 10.1007/s00018-012-1016-3

Cooney, 2013, Cellular and temporal expression of NADPH oxidase (NOX) isotypes after brain injury, J. Neuroinflamm., 10, 917, 10.1186/1742-2094-10-155

Zhang, 2006, Toll-like receptor four deficiency causes pulmonary emphysema, J. Clin. Investig., 116, 3050, 10.1172/JCI28139

Ruwanpura, S.M., McLeod, L., Lilja, A.R., Brooks, G., Dousha, L.F., Seow, H.J., Bozinovski, S., Vlahos, R., Hertzog, P.J., and Anderson, G.P. (2013). Non-essential role for TLR2 and its signaling adaptor Mal/TIRAP in preserving normal lung architecture in mice. PLoS ONE, 8.

Nakano, 2007, Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3, Biochem. J., 403, 97, 10.1042/BJ20060819

Miyano, 2014, N-linked glycosylation of the superoxide-producing NADPH oxidase Nox1, Biochem. Biophys. Res. Commun., 443, 1060, 10.1016/j.bbrc.2013.12.086

Takeya, 2003, Novel Human Homologues of p47phox and p67phox Participate in Activation of Superoxide-producing NADPH Oxidases, J. Biol. Chem., 278, 25234, 10.1074/jbc.M212856200

Cheng, 2004, Nox3 Regulation by NOXO1, p47phox, and p67phox, J. Biol. Chem., 279, 34250, 10.1074/jbc.M400660200

Nisimoto, 2010, Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain, Biochemistry, 49, 2433, 10.1021/bi9022285

Prior, 2016, CRISPR/Cas9-mediated knockout of p22phox leads to loss of Nox1 and Nox4, but not Nox5 activity, Redox Biol., 9, 287, 10.1016/j.redox.2016.08.013

Shiose, 2001, A novel superoxide-producing NAD(P)H oxidase in kidney, J. Biol. Chem., 276, 1417, 10.1074/jbc.M007597200

Goyal, 2005, Identification of novel Nox4 splice variants with impact on ROS levels in A549 cells, Biochem. Biophys. Res. Commun., 329, 32, 10.1016/j.bbrc.2005.01.089

Lyle, 2009, Poldip2, a novel regulator of Nox4 and cytoskeletal integrity in vascular smooth muscle cells, Circ. Res., 105, 249, 10.1161/CIRCRESAHA.109.193722

Chen, 2008, Regulation of ROS signal transduction by NADPH oxidase 4 localization, J. Cell Biol., 181, 1129, 10.1083/jcb.200709049

Lee, 2010, Nox4 is a Novel Inducible Source of Reactive Oxygen Species in Monocytes and Macrophages and Mediates Oxidize, Circ. Res., 106, 1489, 10.1161/CIRCRESAHA.109.215392

Nisimoto, 2014, Nox4: A hydrogen peroxide-generating oxygen sensor, Biochemistry, 53, 5111, 10.1021/bi500331y

Takac, 2011, The E-loop Is Involved in Hydrogen Peroxide Formation by the NADPH Oxidase Nox4, J. Biol. Chem., 286, 13304, 10.1074/jbc.M110.192138

Kawahara, 2011, Nox5 forms a functional oligomer mediated by self-association of its dehydrogenase domain, Biochemistry, 50, 2013, 10.1021/bi1020088

Kiyohara, 2018, Differential cell surface recruitment of the superoxide-producing NADPH oxidases Nox1, Nox2 and Nox5: The role of the small GTPase Sar1, Genes Cells, 23, 480, 10.1111/gtc.12590

Chin, 2000, Calmodulin: A prototypical calcium sensor, Trends Cell Biol., 10, 322, 10.1016/S0962-8924(00)01800-6

Wei, 2012, Characterization of the 1st and 2nd EF-hands of NADPH oxidase 5 by fluorescence, isothermal titration calorimetry, and circular dichroism, Chem. Cent. J., 6, 1, 10.1186/1752-153X-6-29

Tirone, 2007, NADPH oxidase 5 (NOX5) interacts with and is regulated by calmodulin, FEBS Lett., 581, 1202, 10.1016/j.febslet.2007.02.047

Meitzler, 2009, Caenorhabditis elegans and human dual oxidase 1 (DUOX1) peroxidase domains: Insights into heme binding and catalytic activity, J. Biol. Chem., 284, 18634, 10.1074/jbc.M109.013581

Wang, 2002, Characterization of ThOX proteins as components of the thyroid H2O2-generating system, Exp. Cell Res., 273, 187, 10.1006/excr.2001.5444

Morand, 2003, Effect of iodide on nicotinamide adenine dinucleotide phosphate oxidase activity and Duox2 protein expression in isolated porcine thyroid follicles, Endocrinology, 144, 1241, 10.1210/en.2002-220981

Grasberger, 2012, Mice deficient in dual oxidase maturation factors are severely hypothyroid, Mol. Endocrinol., 26, 481, 10.1210/me.2011-1320

Ueyama, 2015, The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release, J. Biol. Chem., 290, 6495, 10.1074/jbc.M114.592717

Milenkovic, 2007, Duox expression and related H2O2 measurement in mouse thyroid: Onset in embryonic development and regulation by TSH in adult, J. Endocrinol., 192, 615, 10.1677/JOE-06-0003

Yen, 2004, The YedZ family: Possible heme binding proteins that can be fused to transporters and electron carriers, J. Mol. Microbiol. Biotechnol., 8, 129

Sanchez-Pulido, L., Rojas, A.M., Valencia, A., Martinez, C., and Andrade, M.A. (2004). ACRATA: A novel electron transfer domain associated to apoptosis and cancer. BMC Cancer, 4.

Tonon, 2006, NADPH oxidases in Eukaryotes: Red algae provide new hints!, Curr. Genet., 49, 190, 10.1007/s00294-005-0044-z

Keller, 1998, A plant homolog of the neutrophil NADPH oxidase gp91phox subunit gene encodes a plasma membrane protein with Ca2+ binding motifs, Plant Cell, 10, 255

Lardy, 2005, NADPH oxidase homologs are required for normal cell differentiation and morphogenesis in Dictyostelium discoideum, Biochim. Biophys. Acta, 1744, 199, 10.1016/j.bbamcr.2005.02.004

Aguirre, 2003, Reactive oxygen species generated by microbial NADPH oxidase NoxA regulate sexual development in Aspergillus nidulans, Mol. Microbiol., 50, 1241, 10.1046/j.1365-2958.2003.03800.x

Aguirre, 2010, Nox enzymes from fungus to fly to fish and what they tell us about Nox function in mammals, Free Radic. Biol. Med., 49, 1342, 10.1016/j.freeradbiomed.2010.07.027

Segal, 1992, Biochemistry and molecular biology of chronic granulomatous disease, J. Inherit. Metab. Dis., 15, 683, 10.1007/BF01799624

Finegold, 1996, Intramembrane bis-heme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase, J. Biol. Chem., 271, 31021, 10.1074/jbc.271.49.31021

Cramer, 2006, Consequences of the structure of the cytochrome b6f complex for its charge transfer pathways, Biochim. Biophys. Acta, 1757, 339, 10.1016/j.bbabio.2006.04.020

Baniulis, 2011, Purification and crystallization of the cyanobacterial cytochrome b6f complex, Methods Mol. Biol., 684, 65, 10.1007/978-1-60761-925-3_7

Picciocchi, 2017, A Two-component NADPH Oxidase (NOX)-like System in Bacteria Is Involved in the Electron Transfer Chain to the Methionine Sulfoxide Reductase MsrP, J. Biol. Chem., 10, 2485

Gennaris, 2015, Repairing oxidized proteins in the bacterial envelope using respiratory chain electrons, Nature, 528, 409, 10.1038/nature15764

Taylor, 1993, A structural model for the nucleotide binding domains of the flavocytochrome b-245 beta-chain, Protein Sci., 2, 1675, 10.1002/pro.5560021013

Burritt, 2003, Functional epitope on human neutrophil flavocytochrome b558, J. Immunol., 170, 6082, 10.4049/jimmunol.170.12.6082

Streeter, 2014, Phosphorylation of Nox1 regulates association with NoxA1 activation domain, Circ. Res., 115, 911, 10.1161/CIRCRESAHA.115.304267

Vermot, 2020, Interdomain Flexibility within NADPH Oxidase Suggested by SANS Using LMNG Stealth Carrier, Biophys. J., 119, 605, 10.1016/j.bpj.2020.06.025

Pick, 1987, Activation of the superoxide forming NADPH oxidase in a cell-free system by sodium dodecyl sulfate. Characterization of the membrane-associated component, J. Biol. Chem., 262, 16476, 10.1016/S0021-9258(18)49281-2

Shpungin, 1989, Activation of the superoxide forming NADPH oxidase in a cell-free system by sodium dodecyl sulfate. Absolute lipid dependence of the solubilized enzyme, J. Biol. Chem., 264, 9195, 10.1016/S0021-9258(18)60513-7

Heyneman, 1984, Activation of a NADPH oxidase from horse polymorphonuclear leukocytes in a cell-free system, J. Leukoc. Biol., 36, 751, 10.1002/jlb.36.6.751

McPhail, 1985, Activation of the respiratory burst enzyme from human neutrophils in a cell-free system. Evidence for a soluble cofactor, J. Clin. Investig., 75, 1735, 10.1172/JCI111884

Curnutte, 1985, Activation of human neutrophil nicotinamide adenine dinucleotide phosphate, reduced (triphosphopyridine nucleotide, reduced) oxidase by arachidonic acid in a cell-free system, J. Clin. Investig., 75, 1740, 10.1172/JCI111885

Levine, 2016, The NADPH Oxidase and Microbial Killing by Neutrophils, With a Particular Emphasis on the Proposed Antimicrobial Role of Myeloperoxidase within the Phagocytic Vacuole, Microbiol. Spectr., 4, 1, 10.1128/microbiolspec.MCHD-0018-2015

Rada, 2008, Oxidative innate immune defenses by Nox/Duox family NADPH Oxidases, Contrib. Microbiol., 15, 164, 10.1159/000136357

Fu, 2004, The mechanism for activation of the neutrophil NADPH-oxidase by the peptides formyl-Met-Leu-Phe and Trp-Lys-Tyr-Met-Val-Met differs from that for interleukin-8, Immunology, 112, 201, 10.1111/j.1365-2567.2004.01884.x

Gallin, J.I., and Snyderman, R. (1999). Chemoattractant stimulus-response coupling. Inflammation Basic Principles and Clinical Correlates, Lippincott Williams & Wilkins.

DeCoursey, 2016, The Intimate and Controversial Relationship between Voltage Gated Proton Channels and the Phagocyte NADPH Oxidase, Immunol. Rev., 273, 194, 10.1111/imr.12437

Henderson, 1987, The superoxide-generating NADPH oxidase of human neutrophils is electrogenic and associated with an H+ channel, Biochem. J., 246, 325, 10.1042/bj2460325

Schrenzel, 1998, Electron currents generated by the human phagocyte NADPH oxidase, Nature, 392, 734, 10.1038/33725

Nunes, 2013, Regulation of the NADPH Oxidase and Associated Ion Fluxes during Phagocytosis, Traffic, 14, 1118, 10.1111/tra.12115

Capasso, 2011, pH regulation and beyond: Unanticipated functions for the voltage-gated proton channel, HVCN1, Trends Cell Biol., 21, 20, 10.1016/j.tcb.2010.09.006

Morgan, 2009, Voltage-gated proton channels maintain pH in human neutrophils during phagocytosis, Proc. Natl. Acad. Sci. USA, 106, 18022, 10.1073/pnas.0905565106

Nanda, 1994, Assessment of the contribution of the cytochrome b moiety of the NADPH oxidase to the transmembrane H+ conductance of leukocytes, J. Biol. Chem., 269, 27280, 10.1016/S0021-9258(18)46981-5

Morgan, 2002, Absence of proton channels in COS-7 cells expressing functional NADPH oxidase components, J. Gen. Physiol., 119, 571, 10.1085/jgp.20018544

Ramsey, 2006, A voltage-gated proton-selective channel lacking the pore domain, Nature, 440, 1213, 10.1038/nature04700

Sasaki, 2006, A Volt. Sens.-Domain Protein Is A Volt.-Gated Proton Channel, Science, 392, 589, 10.1126/science.1122352

Ramsey, 2009, Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst, Proc. Natl. Acad. Sci. USA, 106, 7642, 10.1073/pnas.0902761106

Okamura, 2007, Phagocytosis and membrane potential, Seikagaku, 79, 454

Femling, 2006, The antibacterial activity of human neutrophils and eosinophils requires proton channels but not BK channels, J. Gen. Physiol., 127, 659, 10.1085/jgp.200609504

Klebanoff, 2013, Myeloperoxidase: A front-line defender against phagocytosed microorganisms, J. Leukoc. Biol., 93, 185, 10.1189/jlb.0712349

Rothfork, 2004, Inactivation of a bacterial virulence pheromone by phagocyte-derived oxidants: New role for the NADPH oxidase in host defense, Proc. Natl. Acad. Sci. USA, 101, 13867, 10.1073/pnas.0402996101

Mittal, 2014, Reactive oxygen species in inflammation and tissue injury, Antioxid. Redox Signal., 20, 1126, 10.1089/ars.2012.5149

Valavanidis, 2013, Pulmonary oxidative stress, inflammation and cancer: Respirable particulate matter, fibrous dusts and ozone as major causes of lung carcinogenesis through reactive oxygen species mechanisms, Int. J. Environ. Res. Public Health, 10, 3886, 10.3390/ijerph10093886

Shaeib, F., Khan, S.N., Thakur, M., Kohan-Ghadr, H.R., Drewlo, S., Saed, G.M., Pennathur, S., and Abu-Soud, H.M. (2016). The Impact of Myeloperoxidase and Activated Macrophages on Metaphase II Mouse Oocyte Quality. PLoS ONE, 11.

Davies, 2005, The oxidative environment and protein damage, Biochim. Biophys. Acta, 1703, 93, 10.1016/j.bbapap.2004.08.007

Hazen, 1999, Modification of proteins and lipids by myeloperoxidase, Methods Enzym., 300, 88, 10.1016/S0076-6879(99)00117-2

Bagaitkar, 2015, NADPH oxidase controls neutrophilic response to steril inflammation in mice by regulating the IL-1α/G-CSF axis, Blood, 126, 2724, 10.1182/blood-2015-05-644773

Dupont, 2016, NADPH oxidase: Double agent during inflammation?, Med. Sci., 32, 833

Takei, 1996, Rapid killing of human neutrophils by the potent activator phorbol 12-myristate 13-acetat (PMA) accompanied by changes different from typical apoptosis or necrosis, J. Leukoc. Biol., 59, 229, 10.1002/jlb.59.2.229

Brinkmann, 2004, Neutrophil Extracellular Traps Kill Bacteria, Science, 303, 1532, 10.1126/science.1092385

Kumar, 2015, Neutrophil Extracellular Trap-Related Extracellular Histones Cause Vascular Necrosis in Severe GN, J. Am. Soc. Nephrol., 26, 2399, 10.1681/ASN.2014070673

Parker, 2013, Reactive oxydants and myeloperoxidase and their involvment in neutrophil extracellular traps, Front. Immunol., 3, 424, 10.3389/fimmu.2012.00424

Fuchs, 2007, Novel cell death program leads to neutrophil extracellular traps, J. Cell. Biol., 176, 231, 10.1083/jcb.200606027

Parker, 2012, Requirements for NADPH oxidase and myeloperoxidase in neutrophil extracellular trap formation differ depending on the stimulus, J. Leukoc. Biol., 92, 841, 10.1189/jlb.1211601

Grimm, 2014, NADPH Oxidase Promotes Neutrophil Extracellular Trap Formation in Pulmonary Aspergillosis, Infect. Immun., 82, 1766, 10.1128/IAI.00096-14

Bianchi, 2009, Restoration of NET formation by gene therapy in CGD controls aspergillosis, Blood, 114, 2619, 10.1182/blood-2009-05-221606

Chen, 2012, Endocytosis of soluble immune complexes leads to their clearance by FcγRIIIB but induces neutrophil extracellular traps via FcγRIIA in vivo, Blood, 120, 4421, 10.1182/blood-2011-12-401133

Byrd, 2013, An extracellular matrix-based mechanism of rapid neutrophil extracellular trap formation in response to Candida albicans, J. Immunol., 190, 4136, 10.4049/jimmunol.1202671

Tatsiy, 2018, Physiological Stimuli Induce PAD4-Dependent, ROS-Independent NETosis, With Early and Late Events Controlled by Discrete Signaling Pathways, Front. Immunol., 9, 2036, 10.3389/fimmu.2018.02036

Grandvaux, 2007, Innate host defense: Nox and Duox on phox’s tail, Biochimie, 89, 1113, 10.1016/j.biochi.2007.04.008

Geiszt, 2003, Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense, FASEB J., 17, 1502, 10.1096/fj.02-1104fje

Ha, 2005, A direct role for dual oxidase in Drosophila gut immunity, Science, 310, 847, 10.1126/science.1117311

Geiszt, 2003, 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, 299, 10.4049/jimmunol.171.1.299

Kuwano, 2006, Interferon-gamma activates transcription of NADPH oxidase 1 gene and upregulates production of superoxide anion by human large intestinal epithelial cells, Am. J. Physiol. Cell Physiol., 290, C433, 10.1152/ajpcell.00135.2005

Park, 2006, Role of NADPH oxidase 4 in lipopolysaccharide-induced proinflammatory responses by human aortic endothelial cells, Cardiovas. Res., 72, 447, 10.1016/j.cardiores.2006.09.012

Park, 2004, Cutting edge: Direct interaction of TLR4 with NAD(P)H oxidase 4 isozyme is essential for lipopolysaccharide-induced production of reactive oxygen species and activation of NF-kappa B, J. Immunol., 173, 3589, 10.4049/jimmunol.173.6.3589

Akira, 2006, Pathogen recognition and innate immunity, Cell, 124, 783, 10.1016/j.cell.2006.02.015

Smith, 2017, Redox signaling during hypoxia in mammalian cells, Redox Biol., 13, 228, 10.1016/j.redox.2017.05.020

Winterbourn, 2020, Hydrogen peroxide reactivity and specificity in thiol-based cell signalling, Biochem. Soc. Trans., 48, 745, 10.1042/BST20190049

Knaus, 2021, Oxidants in Physiological Processes, Handb. Exp. Pharm., 264, 27, 10.1007/164_2020_380

Heo, S., Kim, S., and Kang, D. (2020). The Role of Hydrogen Peroxide and Peroxiredoxins throughout the Cell Cycle. Antioxidants, 9.

Winterbourn, 2008, Reconciling the chemistry and biology of reactive oxygen species, Nat. Chem. Biol., 4, 278, 10.1038/nchembio.85

Hunter, 2000, Signaling: 2000 and Beyond, Cell, 100, 113, 10.1016/S0092-8674(00)81688-8

Barford, 2004, The role of cysteine residues as redox-sensitive regulatory switches, Curr. Opin. Struct. Biol., 14, 679, 10.1016/j.sbi.2004.09.012

Salmeen, 2005, Functions and Mechanisms of Redox Regulation of Cysteine-Based Phosphatases, Antioxid. Redox Signal., 7, 560, 10.1089/ars.2005.7.560

Denu, 1998, Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation, Biochemistry, 37, 5633, 10.1021/bi973035t

Goldstein, 2005, Redox Paradox: Insulin Action Is Facilitated by Insulin-Stimulated Reactive Oxygen Species With Multiple Potential Signaling Targets, Diabetes, 54, 311, 10.2337/diabetes.54.2.311

Kwon, 2005, Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76–ADAP, EMBO J., 24, 2331, 10.1038/sj.emboj.7600706

Han, 2003, Cell Proliferation Induced by Reactive Oxygen Species Is Mediated via Mitogen-activated Protein Kinase in Chinese Hamster Lung Fibroblast (V79) Cells, Mol. Cells, 15, 94, 10.1016/S1016-8478(23)13713-7

Brueckl, 2005, Atrial Natriuretic Peptide Induces Mitogen-Activated Protein Kinase Phosphatase-1 in Human Endothelial Cells via Rac1 and NAD(P)H Oxidase/Nox2-Activation, Circ. Res., 7, 43

Li, 2006, The NADPH Oxidase NOX4 Drives Cardiac Differentiation: Role in Regulating Cardiac Transcription Factors and MAP Kinase Activation, Mol. Biol. Cell., 17, 3978, 10.1091/mbc.e05-06-0532

Bertram, 2015, Calcium and ROS: A mutual interplay, Redox Biol., 6, 260, 10.1016/j.redox.2015.08.010

Santos, 2011, Redox signaling in cardiac myocytes, Free Radic. Biol. Med., 50, 777, 10.1016/j.freeradbiomed.2011.01.003

Wang, 2008, STIM, ORAI and TRPC Channels in the Control of Calcium Entry Signals in Smooth Muscle, Clin. Exp. Pharm. Physiol., 35, 1127, 10.1111/j.1440-1681.2008.05018.x

Grupe, 2010, Activation of store-operated ICRAC by hydrogen peroxide, Cell Calcium, 48, 1, 10.1016/j.ceca.2010.05.005

Cho, 2004, Redox regulation of PTEN and protein tyrosine phosphatases in H2O2-mediated cell signaling, FEBS Lett., 560, 7, 10.1016/S0014-5793(04)00112-7

Lei, 2009, Growth factors outside of the platelet-derived growth factor (PDGF) family employ reactive oxygen species/Src family kinases to activate PDGF receptor alpha and thereby promote proliferation and survival of cells, J. Biol. Chem., 284, 6329, 10.1074/jbc.M808426200

Granados, 2006, Dose-dependent effect of hydrogen peroxide on calcium mobilization in mouse pancreatic acinar cells, Biochem. Cell Biol., 84, 39, 10.1139/o05-150

Wang, 1999, Mechanisms of Hydrogen Peroxide-Induced Increase in Intracellular Calcium in Cardiomyocytes, J. Cardiovasc. Pharm., 4, 41, 10.1177/107424849900400107

Liu, 1994, Molecular Interaction between Ryanodine Receptor andMolecular Interaction between Ryanodine Receptor and Glycoprotein Triadin Involves Redox Cycling of Functionally Important Hyperreactive Sulfhydryls, J. Biol. Chem., 269, 33028, 10.1016/S0021-9258(20)30093-4

Favero, 1995, Hydrogen peroxide stimuthe Ca2+ release channel from skeletal muscle sarcoplasmic reticulum, J. Biol. Chem., 270, 25557, 10.1074/jbc.270.43.25557

Suzuki, 1998, Glutathione is a cofactor for H2O2-mediated stimulation of Ca2+induced Ca2+ release in cardiac myocytes, Free Radic. Biol. Med., 24, 318, 10.1016/S0891-5849(97)00227-X

Kawakami, 1998, Superoxide anion radical-triggered Ca2+ release from cardiac sarcoplasmic reticulum through ryanodine receptor Ca2+ channel, Mol. Pharmacol., 53, 497, 10.1124/mol.53.3.497

Cheranov, 2006, TNF-alpha dilates cerebral arteries via NAD(P)H oxidase-dependent Ca2+ spark activation, Am. J. Physiol. Cell. Physiol., 290, C964, 10.1152/ajpcell.00499.2005

Hidalgo, 2006, A transverse tubule NOX activity stimulates calcium release from isolated triads via RYR1 S-glutathionylation, J. Biol. Chem., 281, 26473, 10.1074/jbc.M600451200

Yi, 2006, Characteristics and actions of NAD(P)H oxidase on the sarcoplasmic reticulum of coronary artery smooth muscle, Am. J. Physiol. Heart Circ. Physiol., 290, H1136, 10.1152/ajpheart.00296.2005

Xie, 2019, Size Matters: Ryanodine Receptor Cluster Size Heterogeneity Potentiates Calcium Waves, Biophys. J., 116, 530, 10.1016/j.bpj.2018.12.017

Hu, 2002, Critical Role of NADPH Oxidase-derived Reactive Oxygen Species in Generating Ca2+ Oscillations in Human Aortic Endothelial Cells Stimulated by Histamine, J. Biol. Chem., 277, 32546, 10.1074/jbc.M201550200

Adachi, 2004, S-Glutathiolation by peroxynitrite activates SERCA during arterial relaxation by nitric oxide, Nat. Med., 10, 1200, 10.1038/nm1119

Redondo, 2004, Effect of hydrogen peroxide on Ca2+ mobilisation in human platelets through sulphydryl oxidation dependent and independent mechanisms, Biochem. Pharm., 67, 491, 10.1016/j.bcp.2003.09.031

Irani, 2000, Oxidant Signaling in Vascular Cell Growth, Death, and Survival: A Review of the Roles of Reactive Oxygen Species in Smooth Muscle and Endothelial Cell Mitogenic and Apoptotic Signaling, Circ. Res., 87, 179, 10.1161/01.RES.87.3.179

Hampton, 1997, Redox Regulation of the Caspases during Apoptosis, Ann. N. Y. Acad. Sci., 854, 328, 10.1111/j.1749-6632.1998.tb09913.x

Hampton, 1997, Dual regulation of caspase activity by hydrogen peroxide: Implications for apoptosis, FEBS Lett., 414, 552, 10.1016/S0014-5793(97)01068-5

Deshpande, 2000, Rac1 inhibits TNF-alpha-induced endothelial cell apoptosis: Dual regulation by reactive oxygen species, FASEB J., 14, 1705, 10.1096/fj.99-0910com

Mochizuki, 2006, Inhibition of NADPH oxidase 4 activates apoptosis via the AKT/apoptosis signal-regulating kinase 1 pathway in pancreatic cancer PANC-1 cells, Oncogene, 25, 3699, 10.1038/sj.onc.1209406

Clement, 1996, Superoxide anion is a natural inhibitor of FAS-mediated cell death, EMBO J., 15, 216, 10.1002/j.1460-2075.1996.tb00352.x

Adachi, 2005, NAD(P)H oxidase plays a crucial role in PDGF-induced proliferation of hepatic stellate cells, Hepathology, 41, 1272, 10.1002/hep.20719

Irani, 1997, Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts, Science, 275, 1649, 10.1126/science.275.5306.1649

Laurent, 2005, Controlling Tumor Growth by Modulating Endogenous Production of Reactive Oxygen Species, Cancer Res., 65, 948, 10.1158/0008-5472.948.65.3

Arnold, 2001, Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1, Proc. Natl. Acad. Sci. USA, 98, 5550, 10.1073/pnas.101505898

Fu, 2006, cAMP-response element-binding protein mediates acid-induced NADPH oxidase NOX5-S expression in Barrett esophageal adenocarcinoma cells, J. Biol. Chem., 281, 20368, 10.1074/jbc.M603353200

Kitamoto, 2018, Inhibition of NADPH oxidase 2 induces apoptosis in osteosarcoma: The role of reactive oxygen species in cell proliferation, Oncol. Lett., 15, 7955

Brault, 2020, NOX4 is the main NADPH oxidase involved in the early stages of hematopoietic differentiation from human induced pluripotent stem cells, Free Radic. Biol. Med., 146, 107, 10.1016/j.freeradbiomed.2019.10.005

Szanto, I., Pusztaszeri, M., and Mavromati, M. (2019). H2O2 Metabolism in Normal Thyroid Cells and in Thyroid Tumorigenesis: Focus on NADPH Oxidases. Antioxidants, 8.

Moreno, 2002, Inactivating Mutations in the Gene for Thyroid Oxidase(THOX2) and Congenital Hypothroidism, N. Engl. J. Med., 347, 95, 10.1056/NEJMoa012752

Malgrange, 2004, NOX3: A superoxide-generating NADPH oxidase of the inner ear, J. Biol. Chem., 279, 46065, 10.1074/jbc.M403046200

Rousset, 2015, NOX3-Targeted therapies for inner ear pathologies, Curr. Pharm. Des., 21, 5977, 10.2174/1381612821666151029112421

Mohri, H., Ninoyu, Y., Sakaguchi, H., Hirano, S., Saito, N., and Ueyama, T. (2021). Nox3-derived superoxide in cochleae induces sensorineural hearing loss Mechanisms of Nox3-dependent hearing loss. J. Neurosci.

Malec, 2010, HIF-1α signaling is augmented during intermittent hypoxia by induction of the Nrf2 pathway in NOX1-expressing adenocarcinoma A549 cells, Free Radic. Biol. Med., 48, 1626, 10.1016/j.freeradbiomed.2010.03.008

Kim, 2017, ROS-induced ROS release orchestrated by Nox4, Nox2, and mitochondria in VEGF signaling and angiogenesis, Am. J. Physiol. Cell Physiol., 312, C749, 10.1152/ajpcell.00346.2016

Wang, 2014, Endothelial NADPH oxidase 4 mediates vascular endothelial growth factor receptor 2-induced intravitreal neovascularization in a rat model of retinopathy of prematurity, Mol. Vis., 20, 231

Cartland, 2015, Tumor necrosis factor-related apoptosis-inducing ligand (trail) promotes angiogenesis and ischemia-induced neneovascularization via NADPH oxidase 4 (NOX4) and nitric oxide-dependent mechanisms, J. Am. Heart Assoc., 4, e002527, 10.1161/JAHA.115.002527

Peshavariya, 2014, Transforming growth factor-β1 requires NADPH oxidase 4 for angiogenesis in vitro and in vivo, J. Cell. Mol. Med., 18, 1172, 10.1111/jcmm.12263

Chen, 2014, Both hydrogen peroxide and transforming growth factor β1 contribute to endothelial Nox4 mediated angiogenesis in endothelial Nox4 transgenic mouse lines, Biochim. Biophys. Acta., 1842, 2489, 10.1016/j.bbadis.2014.10.007

Shafique, 2017, Mitochondrial redox plays a critical role in the paradoxical effects of NAPDH oxidase-derived ROS on coronary endothelium, Cardiovasc. Res., 113, 234, 10.1093/cvr/cvw249

Evangelista, 2012, Nox4- and Nox2-dependent oxidant production is required for VEGF-induced SERCA cysteine-674 s-glutathiolation and endothelial cell migration, Free Rad. Biol. Med., 53, 2327, 10.1016/j.freeradbiomed.2012.10.546

Craige, 2011, NADPH oxidase 4 promotes endothelial angiogenesis through endothelial nitric oxide synthase activation, Circulation, 124, 731, 10.1161/CIRCULATIONAHA.111.030775

Chen, 2007, NADPH oxidase modulates myocardial Akt, ERK1/2 activation, and angiogenesis after hypoxia-reoxygenation, Am. J. Physiol. Heart Circ. Physiol., 292, 1664, 10.1152/ajpheart.01138.2006

Garrido-Urbani, S., Jemelin, S., Deffert, C., Carnesecchi, S., Basset, O., Szyndralewiez, C., Heitz, F., Page, P., Montet, X., and Michalik, L. (2011). Targeting vascular NADPH oxidase 1 blocks tumor angiogenesis through a PPARα mediated mechanism. PLoS ONE, 6.

Krock, 2011, Hypoxia-Induced Angiogenesis Good and Evil, Genes Cancer, 2, 1117, 10.1177/1947601911423654

Pendyala, 2009, Role of Nox4 and Nox2 in Hyperoxia-Induced Reactive Oxygen Species Generation and Migration of Human Lung Endothelial Cells, Antioxid. Redox Signal, 11, 747, 10.1089/ars.2008.2203

Menden, 2015, Lipopolysaccharide (LPS)-mediated angiopoietin-2-dependent autocrine angiogenesis is regulated by NADPH oxidase 2 (Nox2) in human pulmonary microvascular endothelial cells, J. Biol. Chem., 290, 5449, 10.1074/jbc.M114.600692

Ho, 2010, Angiogenic effects of stromal cell-derived factor-1 (SDF-1/CXCL12) variants in vitro and the in vivo expressions of CXCL12 variants and CXCR4 in human critical leg ischemia, J. Vasc. Surg., 51, 689, 10.1016/j.jvs.2009.10.044

Pi, 2014, NADPH Oxidase-Generated Reactive Oxygen Species Are Required for Stromal Cell-Derived Factor-1 -Stimulated Angiogenesis, Arterioscler. Thromb. Vasc. Biol., 34, 2023, 10.1161/ATVBAHA.114.303733

Brault, 2015, Genetic disorders coupled to ROS deficiency, Redox Biol., 6, 135, 10.1016/j.redox.2015.07.009

Roos, 2010, Hematologically important mutations: X-linked chronic granulomatous disease (third update), Blood Cells Mol. Dis., 45, 246, 10.1016/j.bcmd.2010.07.012

Beaumel, 2019, The X-CGD PLB-985 Cell Model for NOX2 Structure-Function Analysis, Methods Mol. Biol., 1982, 153, 10.1007/978-1-4939-9424-3_10

Stasia, 2008, Genetics and immunopathology of chronic granulomatous disease, Semin. Immunopathol., 30, 209, 10.1007/s00281-008-0121-8

Rae, 1998, X-Linked Chronic Granulomatous Disease: Mutations in the CYBB Gene, Am. J. Hum. Genet., 62, 1320, 10.1086/301874

Porter, 1994, p22-phox-deficient chronic granulomatous disease: Reconstitution by retrovirus-mediated expression and identification of a biosynthetic intermediate of gp91-phox, Blood, 84, 2767, 10.1182/blood.V84.8.2767.2767

Stasia, 2009, Chronic-granulomatous disease, Rev. Med. Interne, 30, 221, 10.1016/j.revmed.2008.05.023

Klein, 1992, Cytochrome b558-negative, autosomal recessive chronic granulomatous disease: Two new mutations in the cytochrome b558 light chain of the NADPH oxidase (p22-phox), Am. J. Hum. Genet., 51, 1127

Roos, 2010, Hematologically important mutations: The autosomal recessive forms of chronic granulomatous disease (second update), Blood Cells Mol. Dis., 44, 291, 10.1016/j.bcmd.2010.01.009

van den Berg, J.M., van Koppen, E., Ahlin, A., Belohradsky, B., Bernatowska, E., Corbeel, L., Español, T., Fischer, A., Kurenko-Deptuch, M., and Mouy, R. (2009). Chronic Granulomatous Disease: The European Experience. PLoS ONE, 4.

Mitran, 2013, ROS and brain diseases: The good, the bad, and the ugly, Oxid. Med. Cell. Longev., 2013, 963520

Sorce, 2009, NOX enzymes in the central nervous system: From signaling to disease, Antioxid. Redox Signal, 11, 2481, 10.1089/ars.2009.2578

Gervais, 2008, Neurotoxic activation of microglia is promoted by a nox1-dependent NADPH oxidase, J. Neurosci., 12, 12039

Li, 2009, NOX4 expression in human microglia leads to constitutive generation of reactive oxygen species and to constitutive IL-6 expression, J. Innate Immun., 1, 570, 10.1159/000235563

Yao, H., Ago, T., Kitazono, T., and Nabika, T. (2017). NADPH Oxidase-Related Pathophysiology in Experimental Models of Stroke. Int. J. Mol. Sci., 18.

Hernandes, 2013, NADPH oxidase and the degeneration of dopaminergic neurons in parkinsonian mice, Oxid. Med. Cell. Longev., 2013, 157857, 10.1155/2013/157857

Przedborski, 2003, The 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine mouse model: A tool to explore the pathogenesis of Parkinson’s disease, Ann. N. Y. Acad. Sci., 991, 189, 10.1111/j.1749-6632.2003.tb07476.x

Meredith, 2011, MPTP mouse models of Parkinson’s disease: An update, J. Parkinsons Dis., 1, 19, 10.3233/JPD-2011-11023

George, 2009, Targeting the Progression of Parkinson’s Disease, Curr. Neuropharmacol., 7, 9, 10.2174/157015909787602814

Huh, 2011, Ethyl pyruvate rescues nigrostriatal dopaminergic neurons by regulating glial activation in a mouse model of Parkinson’s disease, J. Immunol., 187, 960, 10.4049/jimmunol.1100009

Dias, 2013, The role of oxidative stress in Parkinson’s disease, J. Parkinsons Dis., 3, 461, 10.3233/JPD-130230

Guo, 2018, Damage to dopaminergic neurons by oxidative stress in Parkinson’s disease, Int. J. Mol. Med., 41, 1817

Belarbi, 2017, NADPH oxidases in Parkinson’s disease: A systematic review, Mol. Neurodegener., 12, 84, 10.1186/s13024-017-0225-5

Rey, 2008, Brain angiotensin enhances dopaminergic cell death via microglial activation and NADPH-derived ROS, Neurobiol. Dis., 31, 58, 10.1016/j.nbd.2008.03.003

Kim, 2008, Role of protein kinase in paraquat-induced glial cell death, J. Neurosci. Res., 86, 2062, 10.1002/jnr.21643

Shimohama, 2000, Activation of NADPH Oxidase in Alzheimer’s Disease Brains, Biochem. Biophys. Res. Commun., 273, 5, 10.1006/bbrc.2000.2897

Park, 2008, Nox2-derived radicals contribute to neurovascular and behavioral dysfunction in mice overexpressing the amyloid precursor protein, Proc. Natl. Acad. Sci. USA, 105, 1347, 10.1073/pnas.0711568105

Gamba, 2011, Interaction between 24-hydroxycholesterol, oxidative stress, and amyloid-b in amplifying neuronal damage in Alzheimer’s disease: Three partners in crime, Aging Cell, 10, 403, 10.1111/j.1474-9726.2011.00681.x

Gupta, 2011, Cognitive Impairment in Humanized APPxPS1 Mice is Linked to Aβ1-42 and NOX Activation, Neurobiol. Dis., 44, 317, 10.1016/j.nbd.2011.07.012

Akhter, 2011, Therapeutic potential and anti-amyloidosis mechanisms of tert-butylhydroquinone for Alzheimer’s disease, J. Alzheimers Dis., 26, 767, 10.3233/JAD-2011-110512

Choi, 2014, NADPH Oxidase 1, a Novel Molecular Source of ROS in Hippocampal Neuronal Death in Vascular Dementia, Antioxid. Redox Signal., 21, 533, 10.1089/ars.2012.5129

Wands, 2006, Molecular indices of oxidative stress and mitochondrial dysfunction occur early and often progress with severity of Alzheimer’s disease, J. Alzheimers Dis., 9, 167, 10.3233/JAD-2006-9209

Hernandes, 2012, NADPH Oxidase and Neurodegeneration, Curr. Neuropharmacol., 10, 321, 10.2174/157015912804499483

Meitzler, 2014, NADPH Oxidases: A Perspective on Reactive Oxygen Species Production in Tumor Biology, Antioxid. Redox Signal., 20, 2873, 10.1089/ars.2013.5603

Juhasz, 2009, Expression of NADPH oxidase homologues and accessory genes in human cancer cell lines, tumours and adjacent normal tissues, Free Radic. Res., 43, 523, 10.1080/10715760902918683

Day, 2005, Cell Proliferation, Reactive Oxygen and Cellular Glutathione, Dose Response, 3, 425, 10.2203/dose-response.003.03.010

Wang, 2015, Relationship between expression of NADPH oxidase 2 and invasion and prognosis of human gastric cancer, World J. Gastroenterol., 21, 6271, 10.3748/wjg.v21.i20.6271

You, 2018, Gene expression and prognosis of NOX family members in gastric cancer, Onco Targets Ther., 11, 3065, 10.2147/OTT.S161287

Ren, 2001, Hydroxyl radical-induced apoptosis in human tumor cells is associated with telomere shortening but not telomerase inhibition and caspase activation, FEBS Lett., 488, 123, 10.1016/S0014-5793(00)02377-2

Matsura, 1999, Hydrogen peroxide-induced apoptosis in HL-60 cells requires caspase-3 activation, Free Radic. Res., 30, 73, 10.1080/10715769900300081

Simizu, 1998, Requirement of Caspase-3(-like) Protease-mediated Hydrogen Peroxide Production for Apoptosis Induced by Various Anticancer Drugs, J. Biol. Chem., 273, 26900, 10.1074/jbc.273.41.26900

Skonieczna, M., Hejmo, T., Poterala-Hejmo, A., Cieslar-Pobuda, A., and Buldak, R.J. (2017). NADPH Oxidases: Insights into Selected Functions and Mechanisms of Action in Cancer and Stem Cells. Oxid. Med. Cell. Longev., 2017.

Limoli, 2003, Induction of chromosomal instability by chronic oxidative stress, Neoplasia, 5, 339, 10.1016/S1476-5586(03)80027-1

Hunt, 1998, Genomic instability and catalase gene amplification induced by chronic exposure to oxidative stress, Cancer Res., 58, 3986

Limoli, 1998, Apoptosis, reproductive failure, and oxidative stress in Chinese hamster ovary cells with compromised genomic integrity, Cancer Res., 58, 3712

Clutton, 1996, Radiation-induced genomic instability and persisting oxidative stress in primary bone marrow cultures, Carcinogenesis, 17, 1633, 10.1093/carcin/17.8.1633

Graham, 2010, NADPH oxidase 4 is an oncoprotein localized to mitochondria, Cancer Biol., 10, 223, 10.4161/cbt.10.3.12207

Kartha, 2008, Renal mitochondrial damage and protein modification in type-2 diabetes, Acta Diabetol., 45, 75, 10.1007/s00592-008-0025-z

Spencer, 2011, Control of Hepatic Nuclear Superoxide Production by Glucose 6-Phosphate Dehydrogenase and NADPH Oxidase-4, J. Biol. Chem., 286, 8977, 10.1074/jbc.M110.193821

Salmeen, 2010, The NADPH oxidases NOX4 and DUOX2 regulate cell cycle entry via a p53-dependent pathway, Oncogene, 29, 4473, 10.1038/onc.2010.200

Eid, 2010, AMP-activated protein kinase (AMPK) negatively regulates Nox4-dependent activation of p53 and epithelial cell apoptosis in diabetes, J. Biol. Chem., 285, 37503, 10.1074/jbc.M110.136796

Boudreau, 2014, Wild-type and mutant p53 differentially regulate NADPH oxidase 4 in TGF-beta-mediated migration of human lung and breast epithelial cells, Br. J. Cancer, 110, 2569, 10.1038/bjc.2014.165

Vaziri, 2001, hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase, Cell, 107, 149, 10.1016/S0092-8674(01)00527-X

Laurent, 2008, Nox1 is over-expressed in human colon cancers and correlates with activating mutations in K-Ras, Int. J. Cancer, 123, 100, 10.1002/ijc.23423

Thiery, 2003, Epithelial–mesenchymal transitions in development and pathologies, Curr. Opin Cell. Biol., 15, 740, 10.1016/j.ceb.2003.10.006

Leong, 2014, Invadopodia Are Required for Cancer Cell Extravasation and Are a Therapeutic Target for Metastasis, Cell Rep., 8, 1558, 10.1016/j.celrep.2014.07.050

Diaz, 2009, Tks5-dependent, Nox-mediated Generation of Reactive Oxygen Species is Necessary for Invadopodia Formation, Sci. Signal., 2, 1, 10.1126/scisignal.2000368

Krupitza, 2011, Initial steps of metastasis: Cell invasion and endothelial transmigration, Mutat. Res., 728, 23, 10.1016/j.mrrev.2011.05.002

Paz, 2014, Invading one step at a time: The role of invadopodia in tumor metastasis, Oncogene, 33, 4193, 10.1038/onc.2013.393

Lock, 1998, A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate, EMBO J., 17, 4346, 10.1093/emboj/17.15.4346

Gianni, 2009, Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity, Sci. Signal., 2, ra54, 10.1126/scisignal.2000370

Seals, 2005, The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells, Cancer Cell, 7, 155, 10.1016/j.ccr.2005.01.006

Revach, 2019, Cross-talk between receptor tyrosine kinases AXL and ERBB3 regulates invadopodia formation in melanoma cells, Cancer Res., 79, 2634, 10.1158/0008-5472.CAN-18-2316

Liu, 2015, NADPH oxidase 1-dependent ROS is crucial for TLR4 signaling to promote tumor metastasis of non-small cell lung cancer, Tumour Biol., 36, 1493, 10.1007/s13277-014-2639-9

Pei, 2014, MMP9 activation triggered by epidermal growth factor induced FoxO1 nuclear exclusion in nonsmall cell lung cancer, Tumour Biol., 35, 6673, 10.1007/s13277-014-1850-z

Choi, 2014, CXCR4, but not CXCR7, discriminates metastatic behavior in nonsmall cell lung cancer cells, Mol. Cancer Res., 12, 38, 10.1158/1541-7786.MCR-12-0334

O’Leary, D.P., Bhatt, L., Woolley, J.F., Gough, D.R., Wang, J.H., Cotter, T.G., and Redmond, H.P. (2012). TLR-4 signalling accelerates colon cancer cell adhesion via NF-κB mediated transcriptional up-regulation of Nox-1. PLoS ONE, 7.

Huang, 2012, TG-interacting factor-induced superoxide production from NADPH oxidase contributes to the migration/invasion of urothelial carcinoma, Free. Radic. Biol. Med., 53, 769, 10.1016/j.freeradbiomed.2012.06.014

Nishida, 2006, Angiogenesis in cancer, Vasc. Health Risk Manag., 2, 213, 10.2147/vhrm.2006.2.3.213

Helfinger, 2016, The NADPH oxidase Nox4 mediates tumour angiogenesis, Acta Physiol., 216, 435, 10.1111/apha.12625

Jung, 2008, Reactive oxygen species stabilize hypoxia-inducible factor-1 alpha protein and stimulate transcriptional activity via AMP-activated protein kinase in DU145 human prostate cancer cells, Carcinogenesis, 29, 713, 10.1093/carcin/bgn032

Xia, 2007, Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor, Cancer Res., 67, 10823, 10.1158/0008-5472.CAN-07-0783

Arbiser, 2002, Reactive oxygen generated by Nox1 triggers the angiogenic switch, Proc. Natl. Acad. Sci. USA, 99, 715, 10.1073/pnas.022630199

Karar, 2011, PI3K/AKT/mTOR pathway in angiogenesis, Front. Mol. Neurosci., 4, 51, 10.3389/fnmol.2011.00051

Block, 2012, Aiding and abetting roles of NOX oxidases in cellular transformation, Nat. Rev. Cancer, 12, 627, 10.1038/nrc3339

Govindarajan, 2007, Overexpression of Akt converts radial growth melanoma to vertical growth melanoma, J. Clin. Investig., 117, 719, 10.1172/JCI30102

Pozzi, 2007, Peroxisomal proliferator-activated receptor-α-dependent inhibition of endothelial cell proliferation and tumorigenesis, J. Biol. Chem., 282, 17685, 10.1074/jbc.M701429200

Banskota, S., Gautam, J., Regmi, S.C., Gurung, P., Park, M.H., Kim, S.J., Nam, T.G., Jeong, B.S., and Kim, J.A. (2016). BJ-1108, a 6-amino- 2,4,5-trimethylpyridin-3-ol analog, inhibits serotonininduced angiogenesis and tumor growth through PI3K/NOX pathway. PLoS ONE, 11.

Konior, 2014, NADPH Oxidases in Vascular Pathology, Antioxid. Redox Signal., 20, 2794, 10.1089/ars.2013.5607

Zhang, 2020, NADPH oxidases and oxidase crosstalk in cardiovascular diseases: Novel therapeutic targets, Nat. Rev. Cardiol., 17, 170, 10.1038/s41569-019-0260-8

Burtenshaw, D., Hakimjavadi, R., Redmond, E., and Cahill, P. (2017). Nox Reactive Oxygen Species and Regulation of Vascular Cell Fate. Antioxidants, 6.

Alexander, 1998, Tumour necrosis factor alpha activates a p22phox-based NADH oxidase in vascular smooth muscle, Biochem. J., 329, 653, 10.1042/bj3290653

Brandes, 2001, Thrombin-induced MCP-1 expression involves activation of the p22phox-containing NADPH oxidase in human vascular smooth muscle cells, Thromb. Haemost., 85, 1104, 10.1055/s-0037-1615970

Jansen, 2013, High glucose condition increases NADPH oxidase activity in endothelial microparticles that promote vascular inflammation, Cardiovasc. Res., 98, 94, 10.1093/cvr/cvt013

Brandes, 2010, Vascular Functions of NADPH Oxidases, Hypertension, 56, 17, 10.1161/HYPERTENSIONAHA.108.120295

Rajagopalan, 1996, Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. Contribution to alterations of vasomotor tone, J. Clin. Investig., 97, 1916, 10.1172/JCI118623

Guzik, 2002, Mechanisms of increased vascular superoxide production in human diabetes mellitus: Role of NAD(P)H oxidase and endothelial nitric oxide synthase, Circulation, 105, 1656, 10.1161/01.CIR.0000012748.58444.08

Dikalova, 2005, Nox1 Overexpression Potentiates Angiotensin II-Induced Hypertension and Vascular Smooth Muscle Hypertrophy in Transgenic Mice, Circulation, 112, 2668, 10.1161/CIRCULATIONAHA.105.538934

Landmesser, 2002, Role of p47phox in Vascular Oxidative Stress and Hypertension Caused by Angiotensin II, Hypertension, 40, 511, 10.1161/01.HYP.0000032100.23772.98

Landmesser, 2003, Oxidation of tetrahydrobiopterin leads to uncoupling of endothelial cell nitric oxide synthase in hypertension, J. Clin. Investig., 111, 1201, 10.1172/JCI200314172

Zhang, 2012, Nox4 is a protective reactive oxygen species generating vascular NADPH oxidase, Circ. Res., 110, 1217, 10.1161/CIRCRESAHA.112.267054

Ray, 2011, Endothelial Nox4 NADPH Oxidase Enhances Vasodilatation and Reduces Blood Pressure In Vivo, Arterioscler. Thromb. Vasc. Biol., 31, 1368, 10.1161/ATVBAHA.110.219238

Quesada, 2015, Selective inactivation of NADPH oxidase 2 causes regression of vascularization and the size and stability of atherosclerotic plaques, Atherosclerosis, 242, 469, 10.1016/j.atherosclerosis.2015.08.011

Khatri, 2004, Vascular Oxidant Stress Enhances Progression and Angiogenesis of Experimental Atheroma, Circulation, 109, 520, 10.1161/01.CIR.0000109698.70638.2B

Meyer, 2000, A central role for the endothelial NADPH oxidase in atherosclerosis, FEBS Lett., 472, 1, 10.1016/S0014-5793(00)01397-1

Hink, 2001, Mechanisms Underlying Endothelial Dysfunction in Diabetes Mellitus, Circ. Res., 8, E14

Guzik, 2000, Vascular Superoxide Production by NAD(P)H Oxidase. Association With Endothelial Dysfunction and Clinical Risk Factors, Circ. Res., 86, e85

Ding, 2007, Increased oxidative stress in the streptozotocin-induced diabetic apoE-deficient mouse: Changes in expression of NADPH oxidase subunits and eNOS, Eur. J. Pharm., 561, 121, 10.1016/j.ejphar.2006.12.034

Liang, 2013, Toll-Like Receptor 4 Mutation Protects Obese Mice Against Endothelial Dysfunction by Decreasing NADPH Oxidase Isoforms 1 and 4, Arterioscler. Thromb. Vasc. Biol., 33, 777, 10.1161/ATVBAHA.112.301087

Gray, 2013, NADPH Oxidase 1 Plays a Key Role in Diabetes Mellitus–Accelerated Atherosclerosis, Circulation, 127, 1888, 10.1161/CIRCULATIONAHA.112.132159

Augsburger, 2019, Pharmacological characterization of the seven human NOX isoforms and their inhibitors, Redox Biol., 26, 101272, 10.1016/j.redox.2019.101272

Wandzioch, 2009, Nox4 Acts as a Switch Between Differentiation and Proliferation in Preadipocytes, Arterioscler. Thromb. Vasc. Biol., 29, 239, 10.1161/ATVBAHA.108.174219

Barton, 2009, Getting Radical About Obesity New Links Between Fat and Heart Disease, Arterioscler. Thromb. Vasc. Biol., 29, 447, 10.1161/ATVBAHA.108.181529

Wautier, 2001, Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE, Am. J. Physiol. Endocrinol. Metab., 280, E685, 10.1152/ajpendo.2001.280.5.E685