Proteins Homologous to p47 and p67 Support Superoxide Production by NAD(P)H Oxidase 1 in Colon Epithelial Cells

Cell transformation by the superoxide-generating oxidase Mox1

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Genetic, Biochemical, and Clinical Features of Chronic Granulomatous Disease

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Identification of Renox, an NAD(P)H oxidase in kidney

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Cloning of Two Human Thyroid cDNAs Encoding New Members of the NADPH Oxidase Family

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A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes

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Inflammation: Basic Principles and Clinical Correlates

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A Novel Superoxide-producing NAD(P)H Oxidase in Kidney

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Two Novel Proteins Activate Superoxide Generation by the NADPH Oxidase NOX1

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Hydrogen peroxide mediates the cell growth and transformation caused by the mitogenic oxidase Nox1

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Purification of a Novel Flavoprotein Involved in the Thyroid NADPH Oxidase

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NADPH oxidases: redox regulation of cell homeostasis and disease

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Inactivation of NADPH oxidase organizer 1 Results in Severe Imbalance

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Nox enzymes and oxidative stress in the immunopathology of the gastrointestinal tract

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The Role of NADPH Oxidases in the Etiology of Obesity and Metabolic Syndrome: Contribution of Individual Isoforms and Cell Biology

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NADPH Oxidases as Regulators of Tumor Angiogenesis: Current and Emerging Concepts

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NADPH Oxidases in the Gastrointestinal Tract: A Potential Role of Nox1 in Innate Immune Response and Carcinogenesis

Rokutan, K., Kawahara, T., Kuwano, Y., Tominaga, K., Sekiyama, A., & Teshima-Kondo, S. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1573 · Cited by 105

A Constitutive NADPH Oxidase-Like System Containing gp91phox Homologs in Human Keratinocytes

Chamulitrat, W., Stremmel, W., Kawahara, T., Rokutan, K., Fujii, H. G., Wingler, K., Schmidt, H. H. H. W., & Schmidt, R. (2004) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2004.22410.x · Cited by 96

Pathophysiological Roles of NADPH Oxidase/Nox Family Proteins in the Vascular System - Review and Perspective -

Ago, T., Kuroda, J., Kamouchi, M., Sadoshima, J., & Kitazono, T. (2011) · Circulation Journal · doi:10.1253/circj.cj-11-0388 · Cited by 98

Antagonistic Cross-talk between Rac and Cdc42 GTPases Regulates Generation of Reactive Oxygen Species

Diebold, B. A., Fowler, B. J., Lu, J., Dinauer, M. C., & Bokoch, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313891200 · Cited by 94

Molecular evolution of Phox-related regulatory subunits for NADPH oxidase enzymes

Kawahara, T., & Lambeth, J. D. (2007) · BMC Evolutionary Biology · doi:10.1186/1471-2148-7-178 · Cited by 95

NOX enzymes and Toll-like receptor signaling

Ogier‐Denis, É., Mkaddem, S. B., & Vandewalle, A. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0120-9 · Cited by 94

GTPases and reactive oxygen species: switches for killing and signaling

Werner, E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00937 · Cited by 97

Noxa1 is a central component of the smooth muscle NADPH oxidase in mice

Ambasta, R. K., Schreiber, J. G., Janiszewski, M., Busse, R., & Brandes, R. P. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.12.035 · Cited by 89

The NADPH Oxidase Family and Its Inhibitors

Chocry, M., & Leloup, L. (2019) · Antioxidants and Redox Signaling · doi:10.1089/ars.2019.7915 · Cited by 91

Role of the small GTPase Rac in p22 -dependent NADPH oxidases

Miyano, K., & Sumimoto, H. (2007) · Biochimie · doi:10.1016/j.biochi.2007.05.003 · Cited by 91

Telmisartan attenuates oxidative stress and renal fibrosis in streptozotocin induced diabetic mice with the alteration of angiotensin-(1–7) mas receptor expression associated with its PPAR-γ agonist action

Lakshmanan, A. P., Watanabe, K., Thandavarayan, R. A., Sari, F. R., Harima, M., Giridharan, V. V., Soetikno, V., Kodama, M., & Aizawa, Y. (2011) · Free Radical Research · doi:10.3109/10715762.2011.560149 · Cited by 87

Regulation of Src Family Kinases during Colorectal Cancer Development and Its Clinical Implications

Jin, W. (2020) · Cancers · doi:10.3390/cancers12051339 · Cited by 86

Molecular Mechanism for Activation of Superoxide-producing NADPH Oxidases

Takeya, R., & Sumimoto, H. (2003) · Molecules and Cells · doi:10.1016/s1016-8478(23)13800-3 · Cited by 88

NADPH Oxidase-Mediated Oxidative Stress: Genetic Studies of the p22 phox Gene in Hypertension

Zalba, G., José, G. S., Moreno, M. U., Fortuño, A., & Díez, J. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1327 · Cited by 86

Differential vascular functions of Nox family NADPH oxidases

Brandes, R. P., & Schröder, K. (2008) · Current Opinion in Lipidology · doi:10.1097/mol.0b013e32830c91e3 · Cited by 86

Novel sources of reactive oxygen species in the human body

Orient, A., Donkó, Á., Szabo, A. J., Leto, T. L., & Geiszt, M. (2007) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfm077 · Cited by 88

Functional association of nox1 with p22phox in vascular smooth muscle cells

Hanna, I. R., Hilenski, L. L., Dikalova, A., Taniyama, Y., Dikalov, S., Lyle, A. N., Quinn, M. T., Lassegue, B. P., & Griendling, K. K. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.08.011 · Cited by 82

Identification of a Novel Partner of Duox

Wang, D., Deken, X. D., Milenkovic, M., Song, Y., Pirson, I., Dumont, J. E., & Miot, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407709200 · Cited by 86

Regulation of Novel Superoxide-Producing NAD(P)H Oxidases

Takeya, R., & Sumimoto, H. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1523 · Cited by 81

HSP90 inhibition by 17-DMAG attenuates oxidative stress in experimental atherosclerosis

Madrigal‐Matute, J., Fernandez‐Garcia, C. E., Gómez‐Guerrero, C., López‐Franco, Ó., Muñoz‐García, B., Egido, J., Blanco‐Colio, L. M., & Martı́n-Ventura, J. L. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs158 · Cited by 77

Genetics, biology and clinical management of myeloid cell primary immune deficiencies: chronic granulomatous disease and leukocyte adhesion deficiency

Malech, H. L., & Hickstein, D. D. (2007) · Current Opinion in Hematology · doi:10.1097/00062752-200701000-00007 · Cited by 75

Nox1 in cardiovascular diseases: regulation and pathophysiology

Gimenez, M., Schickling, B., Lopes, L. R., & Miller, F. J. (2015) · Clinical Science · doi:10.1042/cs20150404 · Cited by 77

Evidence for cancer-associated expression of NADPH oxidase 1 (Nox1)-based oxidase system in the human stomach

Tominaga, K., Kawahara, T., Sano, T., Toida, K., Kuwano, Y., Sasaki, H., Kawai, T., Teshima-Kondo, S., & Rokutan, K. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.08.029 · Cited by 75

Mechanism of Angiotensin II-induced Superoxide Production in Cells Reconstituted with Angiotensin Type 1 Receptor and the Components of NADPH Oxidase

Choi, H. S., Leto, T. L., Hunyady, L., Catt, K. J., Bae, Y. S., & Rhee, S. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708000200 · Cited by 74

Inducible nitric oxide synthase‐dependent DNA damage in mouse model of inflammatory bowel disease

Ding, X., Hiraku, Y., Ma, N., Kato, T., Saito, K., Nagahama, M., Semba, R., Kuribayashi, K., & Kawanishi, S. (2005) · Cancer Science · doi:10.1111/j.1349-7006.2005.00024.x · Cited by 72

A molecular mechanism for autoinhibition of the tandem SH3 domains of p47phox, the regulatory subunit of the phagocyte NADPH oxidase

Yuzawa, S., Suzuki, N. N., Fujioka, Y., Ogura, K., Sumimoto, H., & Inagaki, F. (2004) · Genes to Cells · doi:10.1111/j.1356-9597.2004.00733.x · Cited by 72

Cigarette smoke condensate induces MMP-12 gene expression in airway-like epithelia

Lavigne, M. C., & Eppihimer, M. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.144 · Cited by 75

Tumor necrosis factor α activates transcription of the NADPH oxidase organizer 1 (NOXO1) gene and upregulates superoxide production in colon epithelial cells

Kuwano, Y., Tominaga, K., Kawahara, T., Sasaki, H., Takeo, K., Nishida, K., Masuda, K., Kawai, T., Teshima-Kondo, S., & Rokutan, K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.033 · Cited by 73

NADPH oxidase-derived ROS and the regulation of pulmonary vessel tone

Frazziano, G., Champion, H. C., & Pagano, P. J. (2012) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00780.2011 · Cited by 69

Role of NADPH Oxidases in the Control of Vascular Gene Expression

Brandes, R. P. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770380115 · Cited by 67

Pharmacological strategies to lower crosstalk between nicotinamide adenine dinucleotide phosphate (NADPH) oxidase and mitochondria

Koju, N., Taleb, A., Zhou, J., Ge, L., Yang, J., Cao, X., Lei, H., & Ding, Q. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.11.128 · Cited by 72

Redox Control of GTPases: From Molecular Mechanisms to Functional Significance in Health and Disease

Heo, J. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2984 · Cited by 72

Expression of NADPH oxidases and enhanced H2O2-generating activity in human coronary artery endothelial cells upon induction with tumor necrosis factor-α

Yoshida, L. S., & Tsunawaki, S. (2008) · International Immunopharmacology · doi:10.1016/j.intimp.2008.05.004 · Cited by 68

Oxygen sensors in hypoxic pulmonary vasoconstriction

Weißmann, N., Sommer, N., SCHERMULY, R. T., Ghofrani, H. A., Seeger, W., & Grimminger, F. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2006.04.009 · Cited by 67

Regulation of NOXO1 Activity through Reversible Interactions with p22phox and NOXA1

Dutta, S., & Rittinger, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010478 · Cited by 69

Intracellular Redox Regulation by the Family of Small GTPases

Finkel, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1857 · Cited by 67

Phosphorylation of NADPH oxidase activator 1 (NOXA1) on serine 282 by MAP kinases and on serine 172 by protein kinase C and protein kinase A prevents NOX1 hyperactivation

Kroviarski, Y., Debbabi, M., Bachoual, R., Périanin, A., Gougerot‐Pocidalo, M., Benna, J. E., & Dang, P. M. (2010) · The FASEB Journal · doi:10.1096/fj.09-147629 · Cited by 71

Emerging Evidence for the Importance of Phosphorylation in the Regulation of NADPH Oxidases

Bokoch, G., Diebold, B. A., Kim, J.-S., & Gianni, D. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2590 · Cited by 68

The role of NADPH oxidases in neuronal development

Terzi, A., & Suter, D. M. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.04.027 · Cited by 68

Regulation of smooth muscle by inducible nitric oxide synthase and NADPH oxidase in vascular proliferative diseases

Ginnan, R. G., Guikema, B. J., Halligan, K. E., Singer, H. A., & Jourd’heuil, D. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.025 · Cited by 67

Tumor Necrosis Factor-α-Induced Colitis Increases NADPH Oxidase 1 Expression, Oxidative Stress, and Neutrophil Recruitment in the Colon: Preventive Effect of Apocynin

Mouzaoui, S., Djerdjouri, B., Makhezer, N., Kroviarski, Y., Benna, J. E., & Dang, P. M. (2014) · Mediators of Inflammation · doi:10.1155/2014/312484 · Cited by 66

Function of NADPH Oxidases in Diabetic Nephropathy and Development of Nox Inhibitors

Lee, S. R., An, E. J., Kim, J., & Bae, Y. S. (2019) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2019.188 · Cited by 64

The Dual Role of Reactive Oxygen Species-Generating Nicotinamide Adenine Dinucleotide Phosphate Oxidases in Gastrointestinal Inflammation and Therapeutic Perspectives

Dang, P. M., Rolas, L., & Benna, J. E. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8018 · Cited by 62

Alternative mRNA splice forms of NOXO1: Differential tissue expression and regulation of Nox1 and Nox3

Cheng, G., & Lambeth, J. D. (2005) · Gene · doi:10.1016/j.gene.2005.03.008 · Cited by 62

Potential role of the NADPH oxidase NOX1 in the pathogenesis of 5-fluorouracil-induced intestinal mucositis in mice

Yasuda, M., Kato, S., Yamanaka, N., Iimori, M., Utsumi, D., Kitahara, Y., Iwata, K., Matsuno, K., Amagase, K., Yabe‐Nishimura, C., et al. (2012) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00535.2011 · Cited by 61

The ‘A’s and ‘O’s of NADPH oxidase regulation: A commentary on “Subcellular localization and function of alternatively spliced Noxo1 isoforms”

Opitz, N., Drummond, G. R., Selemidis, S., Meurer, S., & Schmidt, H. H. H. W. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.11.003 · Cited by 64

Subcellular localization and function of alternatively spliced Noxo1 isoforms

Ueyama, T., Lekstrom, K. J., Tsujibe, S., Saito, N., & Leto, T. L. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.08.024 · Cited by 61

Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation

Gianni, D., DerMardirossian, C. M., & Bokoch, G. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.05.007 · Cited by 60

Trans-Plasma Membrane Electron Transport in Mammals: Functional Significance in Health and Disease

Principe, D. D., Avigliano, L., Savini, I., & Catani, M. V. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3247 · Cited by 58

Gene Expression inPorphyromonas gingivalisafter Contact with Human Epithelial Cells

Hosogi, Y., & Duncan, M. J. (2005) · Infection and Immunity · doi:10.1128/iai.73.4.2327-2335.2005 · Cited by 58

NADPH Oxidases as Novel Pharmacologic Targets against Influenza A Virus Infection

Vlahos, R., & Selemidis, S. (2014) · Molecular Pharmacology · doi:10.1124/mol.114.095216 · Cited by 58

Innate host defense: Nox and Duox on phox's tail

Grandvaux, N., Soucy-Faulkner, A., & Fink, K. (2007) · Biochimie · doi:10.1016/j.biochi.2007.04.008 · Cited by 61

Peptide-based inhibitors of the phagocyte NADPH oxidase

Benna, J. E., Dang, P. M., & Périanin, A. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.05.020 · Cited by 54

Peroxiredoxin 6 (Prdx6) supports NADPH oxidase1 (Nox1)-based superoxide generation and cell migration

Kwon, J., Wang, A., Burke, D. J., Boudreau, H. E., Lekstrom, K. J., Korzeniowska, A., Sugamata, R., Kim, Y., Liang, Y., Ersoy, I., et al. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.009 · Cited by 55

Differential roles of NADPH oxidases in vascular physiology and pathophysiology

Griendling, K. K. (2012) · Frontiers in Bioscience-Scholar · doi:10.2741/s317 · Cited by 52

Nox and Inflammation in the Vascular Adventitia

Meijles, D. N., & Pagano, P. J. (2015) · Hypertension · doi:10.1161/hypertensionaha.115.03622 · Cited by 54

Adventitial delivery of dominant-negative p67phoxattenuates neointimal hyperplasia of the rat carotid artery

Weaver, M., Liu, J. J., Pimentel, D. R., Reddy, D. J., Harding, P., Peterson, E. L., & Pagano, P. J. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00690.2005 · Cited by 49

Expression of functionally phagocyte‐type NAD(P)H oxidase in pericytes: effect of angiotensin II and high glucose

Manea, A., Raicu, M., & Simionescu, M. (2005) · Biology of the Cell · doi:10.1042/bc20040107 · Cited by 51

Expression of nonphagocytic NADPH oxidase system in the ocular lens.

Rao, P. V., Maddala, R., John, F., & Zigler, J. S. (2004) · PubMed · Cited by 51

Transcriptional regulation of the NADPH oxidase isoform, Nox1, in colon epithelial cells: Role of GATA-binding factor(s)

Brewer, A. C., Sparks, E., & Shah, A. M. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.022 · Cited by 51

Nox4 B-loop Creates an Interface between the Transmembrane and Dehydrogenase Domains

Jackson, H. M., Kawahara, T., Nisimoto, Y., Smith, S. M. E., & Lambeth, J. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.084939 · Cited by 51

Overexpression of human NOX1 complex induces genome instability in mammalian cells

Chiera, F., Meccia, E., Degan, P., Aquilina, G., Pietraforte, D., Minetti, M., Lambeth, D. J., & Bignami, M. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.09.018 · Cited by 50

T3SS effector VopL inhibits the host ROS response, promoting the intracellular survival of Vibrio parahaemolyticus

Santos, M. D. S., Salomon, D., & Orth, K. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006438 · Cited by 46

NOXO1 phosphorylation on serine 154 is critical for optimal NADPH oxidase 1 assembly and activation

Debbabi, M., Kroviarski, Y., Bournier, O., Gougerot‐Pocidalo, M., Benna, J. E., & Dang, P. M. (2013) · The FASEB Journal · doi:10.1096/fj.12-216432 · Cited by 48

Crucial Role of Two Potential Cytosolic Regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH Oxidase Activation

Li, X. J., Grünwald, D., Mathieu, J., Morel, F., & Stasia, M. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500226200 · Cited by 45

NOX, NOX Who is There? The Contribution of NADPH Oxidase One to Beta Cell Dysfunction

Taylor, D. (2013) · Frontiers in Endocrinology · doi:10.3389/fendo.2013.00040 · Cited by 46

Oxidative stress and aging: the potential role of iron

Galaris, D., Mantzaris, M. D., & Amorgianiotis, C. (2008) · HORMONES · doi:10.1007/bf03401502 · Cited by 44

Analysis of mRNA Transcripts from the NAD(P)H Oxidase 1 (Nox1) Gene

Geiszt, M., Lekstrom, K. J., & Leto, T. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409325200 · Cited by 48

Inhibitory Action of NoxA1 on Dual Oxidase Activity in Airway Cells

Pacquelet, S., Lehmann, M. D., Luxen, S., Regazzoni, K., Frausto, M., Noack, D., & Knaus, U. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709108200 · Cited by 43

Prevention of salt-induced renal injury by activation of NAD(P)H:quinone oxidoreductase 1, associated with NADPH oxidase

Kim, Y., Hwang, J. H., Noh, J., Gang, G., Tadi, S., Yim, Y., Jeoung, N. H., Kwak, T. H., Lee, S., Kweon, G. R., et al. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.007 · Cited by 43

The role of phosphoinositides and phosphorylation in regulation of NADPH oxidase

Perišić, O., Wilson, M. I., Karathanassis, D., Bravo, J., Pacold, M. E., Ellson, C. D., Hawkins, P. T., Stephens, L., & Williams, R. L. (2004) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2003.11.003 · Cited by 43

NADPH Oxidase–Generated Reactive Oxygen Species Are Required for Stromal Cell–Derived Factor-1α–Stimulated Angiogenesis

Pi, X., Xie, L., Portbury, A. L., Kumar, S., Lockyer, P. P., Li, X., & Patterson, C. (2014) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.114.303733 · Cited by 42

Essential Role of NOXA1 in Generation of Reactive Oxygen Species Induced by Oxidized Low-Density Lipoprotein in Human Vascular Endothelial Cells

Honjo, T., Otsui, K., Shiraki, R., Kawashima, S., Sawamura, T., Yokoyama, M., & Inoue, N. (2008) · Endothelium · doi:10.1080/10623320802125433 · Cited by 40

NADPH oxidase: recent evidence for its role in erectile dysfunction

Jin, L., & Burnett, A. L. “. (2008) · Asian Journal of Andrology · doi:10.1111/j.1745-7262.2008.00371.x · Cited by 37

The insert region of the Rac GTPases is dispensable for activation of superoxide-producing NADPH oxidases

Miyano, K., Koga, H., Minakami, R., & Sumimoto, H. (2009) · Biochemical Journal · doi:10.1042/bj20082182 · Cited by 40

Small-Angle X-ray Scattering Reveals an Extended Organization for the Autoinhibitory Resting State of the p47phox Modular Protein

Christiane, D. D., Cannella, D., Dubosclard, V., Pebay‐Peyroula, E., Vachette, P., & Fieschi, F. (2006) · Biochemistry · doi:10.1021/bi060274k · Cited by 38

Phosphorylation of Noxo1 at threonine 341 regulates its interaction with Noxa1 and the superoxide‐producing activity of Nox1

Yamamoto, A., Takeya, R., Matsumoto, M., Nakayama, K. I., & Sumimoto, H. (2013) · FEBS Journal · doi:10.1111/febs.12489 · Cited by 39

Octanoic Acid—An Insecticidal Metabolite of Conidiobolus coronatus (Entomopthorales) That Affects Two Majors Antifungal Protection Systems in Galleria mellonella (Lepidoptera): Cuticular Lipids and Hemocytes

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Activation of NADPH oxidase 1 in tumour colon epithelial cells.

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