Cited by 433Redox biology and oxidative stressNitric Oxide and Endothelin EffectsNeutrophil, Myeloperoxidase and Oxidative Mechanisms

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NADPH oxidase in brain injury and neurodegenerative disorders

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Ma, Merry W., Wang, Jing, Zhang, Quanguang, Wang, Ruimin, Dhandapani, Krishnan M., Vadlamudi, Ratna K., Brann, Darrell W.·2017·Molecular Neurodegeneration

DOI 10.1186/s13024-017-0150-7PMC PMC5240251

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Abstract

Oxidative stress is a common denominator in the pathology of neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, and multiple sclerosis, as well as in ischemic and traumatic brain injury. The brain is highly vulnerable to oxidative damage due to its high metabolic demand. However, therapies attempting to scavenge free radicals have shown little success. By shifting the focus to inhibit the generation of damaging free radicals, recent studies have identified NADPH oxidase as a major contributor to disease pathology. NADPH oxidase has the primary function to generate free radicals. In particular, there is growing evidence that the isoforms NOX1, NOX2, and NOX4 can be upregulated by a variety of neurodegenerative factors. The majority of recent studies have shown that genetic and pharmacological inhibition of NADPH oxidase enzymes are neuroprotective and able to reduce detrimental aspects of pathology following ischemic and traumatic brain injury, as well as in chronic neurodegenerative disorders. This review aims to summarize evidence supporting the role of NADPH oxidase in the pathology of these neurological disorders, explores pharmacological strategies of targeting this major oxidative stress pathway, and outlines obstacles that need to be overcome for successful translation of these therapies to the clinic.

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Fig. 1 a Cellular Sources of ROS. ROS can be generated intracellularly via the action of various organelles, enzymes, and processes. b Conversion of Superoxide to Secondary ROS. Once produced, superoxide can interact with various molecules to generate secondary radicals. Superoxide can react with nitric oxide to produce peroxynitrite. Superoxide dismutase can also convert superoxide into hydrogen peroxide, which can then undergo a Fenton reaction to produce hydroxyl radicals and ions. Interaction of superoxide with protons can produce hydroperoxyl radicals. These secondary radicals are highly reactive and can be neurotoxic via alterations of macromolecules and amplification of oxidative stressCC BY · PubMed Central

Fig. 2 NOX isoforms and regulatory subunits. NADPH oxidases have a primary role to generate ROS. Several components and domains make up the transmembrane active enzyme complexes of NADPH oxidase isoforms. NOX1-5 and DUOX1/DUOX2 are shown here. Upon activation, an electron will be transferred from NADPH to O2 to form superoxide. NOX4 generated superoxide undergoes rapid conversion into hydrogen peroxide, which mediates many of its downstream effects. NOX5 and the DUOX enzymes are sensitive to cellular Ca2+ concentrationsCC BY · PubMed Central

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Items 201–400 of 417

Apocynin prevents cyclooxygenase 2 expression in human monocytes through NADPH oxidase and glutathione redox-dependent mechanisms
Barbieri, S. S., Cavalca, V., Eligini, S., Brambilla, M., Caiani, A., Tremoli, E., & Colli, S. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.04.020 · Cited by 161
Constitutive NADPH-Dependent Electron Transferase Activity of the Nox4 Dehydrogenase Domain
Nisimoto, Y., Jackson, H. M., Ogawa, H., Kawahara, T., & Lambeth, J. D. (2010) · Biochemistry · doi:10.1021/bi9022285 · Cited by 161
Delayed gastric emptying in Parkinson's disease
Marrinan, S. L., Emmanuel, A. V., & Burn, D. J. (2013) · Movement Disorders · doi:10.1002/mds.25708 · Cited by 160
Oxidative Burst of Circulating Neutrophils Following Traumatic Brain Injury in Human
Liao, Y., Liu, P., Guo, F., Zhang, Z., & Zhang, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068963 · Cited by 160
Genetics and immunopathology of chronic granulomatous disease
Stasia, M. J., & Li, X. J. (2008) · Seminars in Immunopathology · doi:10.1007/s00281-008-0121-8 · Cited by 159
Riluzole for amyotrophic lateral sclerosis (ALS)/motor neuron disease (MND)
Rg, M., Jd, M., Lyon, M., & Moore, D. (2003) · Amyotrophic Lateral Sclerosis and Other Motor Neuron Disorders · doi:10.1080/14660820310002601 · Cited by 159
The oxidation of apocynin catalyzed by myeloperoxidase: Proposal for NADPH oxidase inhibition
Ximenes, V. F., Kanegae, M. P. P., Rissato, S. R., & Galhiane, M. S. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.11.010 · Cited by 157
Reactive Oxygen Species Derived from NOX1/NADPH Oxidase Enhance Inflammatory Pain
Ibi, M., Matsuno, K., Shiba, D., Katsuyama, M., Iwata, K., Kakehi, T., Nakagawa, T., Sango, K., Shirai, Y., Yokoyama, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.1857-08.2008 · Cited by 156
Increased NADPH-Oxidase Activity and Nox4 Expression During Chronic Hypertension Is Associated With Enhanced Cerebral Vasodilatation to NADPH In Vivo
Paravicini, T. M., Chrissobolis, S., Drummond, G. R., & Sobey, C. G. (2004) · Stroke · doi:10.1161/01.str.0000112974.37028.58 · Cited by 156
Is Modulation of Oxidative Stress an Answer? The State of the Art of Redox Therapeutic Actions in Neurodegenerative Diseases
Chiurchiù, V., Orlacchio, A., & Maccarrone, M. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/7909380 · Cited by 156
Tolerance of high‐dose (3,000 mg/day) coenzyme Q10 in ALS
Ferrante, K. L., Shefner, J., Zhang, H., Betensky, R., O'Brien, M., Yu, H., Fantasia, M., Taft, J., Beal, M. F., Traynor, B., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000187070.35365.d7 · Cited by 154
Diphenylene iodonium as an inhibitor of the NADPH oxidase complex of bovine neutrophils: Factors controlling the inhibitory potency of diphenylene iodonium in a cell‐free system of oxidase activation
DOUSSIÈRE, J., & VIGNAIS, P. V. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17159.x · Cited by 153
Nox2-containing NADPH oxidase and Akt activation play a key role in angiotensin II-induced cardiomyocyte hypertrophy
Hingtgen, S., Tian, X., Yang, J., Dunlay, S. M., Peek, A. S., Wu, Y., Sharma, R. V., Engelhardt, J. F., & Davisson, R. L. (2006) · Physiological Genomics · doi:10.1152/physiolgenomics.00029.2005 · Cited by 153
Activation of p47 , a Cytosolic Subunit of the Leukocyte NADPH Oxidase
Johnson, J. L., Park, J., Benna, J. E., Faust, L. P., Inanami, O., & BABIOR, B. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.35147 · Cited by 151
Involvement of phenyl radicals in iodonium inhibition of flavoenzymes.
O’Donnell, V. B., Smith, G. C., & Jones, O. T. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09813-x · Cited by 149
Apocynin: Chemical and Biophysical Properties of a NADPH Oxidase Inhibitor
Petrônio, M., Zeraik, M., Fonseca, L., & Ximenes, V. (2013) · Molecules · doi:10.3390/molecules18032821 · Cited by 149
NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation
Hassani, R. A. E., Talbot, M., dos Santos, M. C. D. S., Ghuzlan, A. A., Hartl, D. M., Bidart, J., Deken, X. D., Miot, F., Diallo, I., de Vathaire, F., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1420707112 · Cited by 148
NADPH Oxidase Inhibitors: New Antihypertensive Agents?
Williams, H. C., & Griendling, K. K. (2007) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e318063e820 · Cited by 146
NADPH Oxidase 2-Derived Reactive Oxygen Species Mediate FFAs-Induced Dysfunction and Apoptosis of β-Cells via JNK, p38 MAPK and p53 Pathways
Yuan, H., Zhang, X., Huang, X., Lu, Y., Tang, W., Man, Y., Wang, S., Xi, J., & Li, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015726 · Cited by 145
INVOLVEMENT OF OXIDATIVE STRESS IN 3-NITROPROPIONIC ACID NEUROTOXICITY
Schulz, J. B., Henshaw, D. R., MacGarvey, U. M., & Beal, M. F. (1996) · Neurochemistry International · doi:10.1016/0197-0186(95)00122-0 · Cited by 145
Redox modifier genes in amyotrophic lateral sclerosis in mice
Marden, J. J., Harraz, M. M., Williams, A. J., Nelson, K., Luo, M., Paulson, H., & Engelhardt, J. F. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31265 · Cited by 145
Targeting Vascular NADPH Oxidase 1 Blocks Tumor Angiogenesis through a PPARα Mediated Mechanism
Garrido-Urbani, S., Jemelin, S., Deffert, C., Carnesecchi, S., Basset, O., Szyndralewiez, C., Heitz, F., Page, P., Montet, X., Michalik, L., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014665 · Cited by 143
Apocynin improves outcome in experimental stroke with a narrow dose range
Tang, X. N., Cairns, B., Cairns, N., & Yenari, M. A. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.03.090 · Cited by 142
Airway epithelial dual oxidase 1 mediates allergen-induced IL-33 secretion and activation of type 2 immune responses
Hristova, M., Habibovic, A., Veith, C., Janssen-Heininger, Y. M. W., Dixon, A. E., Geiszt, M., & van der Vliet, A. (2016) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2015.10.003 · Cited by 141
Lactate and P o 2 Modulate Superoxide Anion Production in Bovine Cardiac Myocytes
Mohazzab-H., K. M., Kaminski, P. M., & Wolin, M. S. (1997) · Circulation · doi:10.1161/01.cir.96.2.614 · Cited by 140
Current Progress of RNA Aptamer-Based Therapeutics
Zhou, J., Bobbin, M. L., Burnett, J., & Rossi, J. J. (2012) · Frontiers in Genetics · doi:10.3389/fgene.2012.00234 · Cited by 140
Suppression of Microglial Inflammatory Activity by Myelin Phagocytosis: Role of p47-PHOX-Mediated Generation of Reactive Oxygen Species
Liu, Y., Hao, W., Letièmbre, M., Walter, S., Kulanga, M., Neumann, H., & Fassbender, K. C. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.2531-06.2006 · Cited by 139
Oxidative damage to DNA in plaques of MS brains
Vladimirova, O. V., O'Connor, J. J., Cahill, A., Alder, H., Butunoi, C., & Kálmán, B. (1998) · Multiple Sclerosis Journal · doi:10.1177/135245859800400503 · Cited by 138
NAD(P)H Oxidases in Rat Basilar Arterial Endothelial Cells
Ago, T., Kitazono, T., Kuroda, J., Kumai, Y., Kamouchi, M., Ooboshi, H., Wakisaka, M., Kawahara, T., Rokutan, K., Ibayashi, S., et al. (2005) · Stroke · doi:10.1161/01.str.0000163111.05825.0b · Cited by 136
Targeting microglia-mediated neurotoxicity: the potential of NOX2 inhibitors
Surace, M. J., & Block, M. L. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1015-4 · Cited by 134
Nephropathy and Elevated BP in Mice with Podocyte-Specific NADPH Oxidase 5 Expression
Holterman, C. E., Thibodeau, J.-F., Towaij, C., Gutsol, A. A., Montezano, A. C. I., Parks, R. J., Cooper, M. E., Touyz, R. M., & Kennedy, C. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013040371 · Cited by 133
Natural Compounds as Modulators of NADPH Oxidases
Maraldi, T. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/271602 · Cited by 133
NADPH oxidase plays a crucial role in the activation of pancreatic stellate cells
Masamune, A., Watanabe, T., Kikuta, K., Satoh, K., & Shimosegawa, T. (2007) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00272.2007 · Cited by 133
NADPH-oxidase activation and cognition in Alzheimer disease progression
Ansari, M. A., & Scheff, S. W. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.025 · Cited by 131
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Han, B. H., Zhou, M.-L., Johnson, A. W., Singh, I., Liao, F., Vellimana, A. K., Nelson, J. W., Milner, E., Cirrito, J. R., Basak, J., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414930112 · Cited by 131
Increased hippocampal neurogenesis in the progressive stage of Alzheimer's disease phenotype in an APP/PS1 double transgenic mouse model
Yu, Y., He, J., Zhang, Y., Luo, H., Zhu, S., Yang, Y., Zhao, T., Wu, J., Huang, Y., Kong, J., et al. (2009) · Hippocampus · doi:10.1002/hipo.20587 · Cited by 131
Atorvastatin protects against cerebral infarction via inhibition of NADPH oxidase-derived superoxide in ischemic stroke
Hong, H., Zeng, J.-S., Kreulen, D. L., Kaufman, D. I., & Chen, A. F. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01270.2005 · Cited by 131
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Raz, L., Zhang, Q.-G., Zhou, C.-F., Han, D. K., Gulati, P., Yang, L.-C., Yang, F., Wang, R. M., & Brann, D. W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012606 · Cited by 129
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Hernandes, M. S., d’Avila, J. C., Trevelin, S. C., Reis, P. A., Kinjo, É. R., Lopes, L. R., Castro-Faria-Neto, H. C., Cunha, F. Q., Britto, L. R. G., & Bozza, F. A. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-36 · Cited by 129
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Pendyala, S., & Natarajan, V. (2010) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2010.09.016 · Cited by 128
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Stielow, C., Catar, R. A., Müller, G. M., Wingler, K., Scheurer, P., Schmidt, H. H. H. W., & Morawietz, H. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.114 · Cited by 127
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Mancuso, R., & Navarro, X. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.07.004 · Cited by 125
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Kahles, T., & Brandes, R. P. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4721 · Cited by 125
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Zawada, W. M., Banninger, G. P., Thornton, J., Marriott, B., Cantu, D., Rachubinski, A. L., Das, M., Griffin, W. S. T., & Jones, S. M. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-129 · Cited by 125
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Bizzozero, O. A., DeJesus, G., Callahan, K., & Pastuszyn, A. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20587 · Cited by 124
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Ghosh, A., Kanthasamy, A., Joseph, J., Anantharam, V., Srivastava, P., Dranka, B. P., Kalyanaraman, B., & Kanthasamy, A. G. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-241 · Cited by 124
Immune markers and differential signaling networks in ulcerative colitis and Crohnʼs disease
Christophi, G. P., Rong, R., Holtzapple, P. G., Massa, P. T., & LANDAS, S. K. (2012) · Inflammatory Bowel Diseases · doi:10.1002/ibd.22957 · Cited by 123
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Jiang, T., Hoekstra, J., Heng, X., Kang, W., Ding, J., Liu, J., Chen, S., & Zhang, J. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.03.015 · Cited by 123
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Benov, L. (2001) · PROTOPLASMA · doi:10.1007/bf01289410 · Cited by 122
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Jackman, K. A., Miller, A. A., Silva, T. M. D., Crack, P. J., Drummond, G. R., & Sobey, C. G. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2008.00073.x · Cited by 120
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Li, Q., Spencer, N. Y., Oakley, F. D., Buettner, G. R., & Engelhardt, J. F. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2407 · Cited by 119
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Guggilam, A., Haque, M., Kerut, E. K., McIlwain, E., Lucchesi, P. A., Seghal, I., & Francis, J. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00286.2007 · Cited by 119
NADPH oxidase is involved in post-ischemic brain inflammation
Chen, H., Kim, G. S., Okami, N., Narasimhan, P., & Chan, P. H. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.01.027 · Cited by 117
The Pathology of MS
Pittock, S. J., & Lucchinetti, C. F. (2007) · The Neurologist · doi:10.1097/01.nrl.0000253065.31662.37 · Cited by 117
Prevention of traumatic brain injury-induced neuronal death by inhibition of NADPH oxidase activation
Choi, B. Y., Jang, B. G., Kim, J. H., Lee, B. E., Sohn, M., Song, H. K., & Suh, S. W. (2012) · Brain Research · doi:10.1016/j.brainres.2012.08.032 · Cited by 117
Traumatic Brain Injury Causes Aberrant Migration of Adult-Born Neurons in the Hippocampus
Ibrahim‐Shaikh, S., Hu, W., Wang, X., Gao, X., He, C., & Chen, J. (2016) · Scientific Reports · doi:10.1038/srep21793 · Cited by 117
Aptamer That Binds to the gD Protein of Herpes Simplex Virus 1 and Efficiently Inhibits Viral Entry
Gopinath, S. C. B., Hayashi, K., & Kumar, P. K. R. (2012) · Journal of Virology · doi:10.1128/jvi.00377-12 · Cited by 116
A Role for NOX NADPH Oxidases in Alzheimer's Disease and Other Types of Dementia?
Zekry, D., Epperson, T. K., & Krause, K. (2003) · IUBMB Life · doi:10.1080/1521654031000153049 · Cited by 115
Oxidative tissue injury in multiple sclerosis is only partly reflected in experimental disease models
Schuh, C., Wimmer, I., Hametner, S., Haider, L., van Dam, A., Liblau, R., Smith, K. J., Probert, L., Binder, C. J., Bauer, J., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1263-5 · Cited by 115
Free Radical Trapping as a Therapeutic Approach to Neuroprotection in Stroke: Experimental and Clinical Studies with NXY-059 and Free Radical Scavengers
Green, A., & Ashwood, T. (2005) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007053544156 · Cited by 113
The immunology of traumatic brain injury: a prime target for Alzheimer’s disease prevention
Giunta, B., Obregon, D., Velisetty, R., Sanberg, P. R., Borlongan, C. V., & Tan, J. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-185 · Cited by 112
Regional and temporal characterization of neuronal, glial, and axonal response after traumatic brain injury in the mouse
Carbonell, W. S., & Grady, M. S. (1999) · Acta Neuropathologica · doi:10.1007/s004010051100 · Cited by 110
Atrial Natriuretic Peptide Induces Mitogen-Activated Protein Kinase Phosphatase-1 in Human Endothelial Cells via Rac1 and NAD(P)H Oxidase/Nox2-Activation
Fürst, R., Brueckl, C., Kuebler, W. M., Stefan Zahler, A., Krötz, F., Görlach, A., Vollmar, A. M., & Kiemer, A. K. (2004) · Circulation Research · doi:10.1161/01.res.0000151983.01148.06 · Cited by 110
Oxidative stress, redox signalling and endothelial dysfunction in ageing‐related neurodegenerative diseases: a role of NADPH oxidase 2
Cahill‐Smith, S., & Li, J. (2014) · British Journal of Clinical Pharmacology · doi:10.1111/bcp.12357 · Cited by 109
Role of NADPH oxidase in the brain injury of intracerebral hemorrhage
Tang, J., Liu, J., Zhou, C., Ostanin, D. V., Grisham, M. B., Granger, D. N., & Zhang, J. H. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03292.x · Cited by 109
Role of the NADPH Oxidases in the Subfornical Organ in Angiotensin II–Induced Hypertension
Lob, H. E., Schultz, D. W., Marvar, P. J., Davisson, R. L., & Harrison, D. G. (2012) · Hypertension · doi:10.1161/hypertensionaha.111.00546 · Cited by 109
Oxidized phosphatidylcholine is a marker for neuroinflammation in multiple sclerosis brain
Qin, J., Goswami, R., Balabanov, R. D., & Dawson, G. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21206 · Cited by 108
Role of the Rho GTPase Rac in the activation of the phagocyte NADPH oxidase
Pick, E. (2014) · Small GTPases · doi:10.4161/sgtp.27952 · Cited by 106
Oxidative Stress Mediates the Stimulation of Sympathetic Nerve Activity in the Phenol Renal Injury Model of Hypertension
Ye, S., Zhong, H., & Campese, V. M. (2006) · Hypertension · doi:10.1161/01.hyp.0000231307.69761.2e · Cited by 105
NADPH Oxidases as Regulators of Tumor Angiogenesis: Current and Emerging Concepts
Coso, S., Harrison, I., Harrison, C. B., Vinh, A., Sobey, C. G., Drummond, G. R., Williams, E. D., & Selemidis, S. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4489 · Cited by 101
NADPH Oxidase 1, a Novel Molecular Source of ROS in Hippocampal Neuronal Death in Vascular Dementia
Choi, D.-H., Lee, K.-H., Kim, J.-H., Seo, J.-H., Kim, H. Y., Shin, C. Y., Han, J., Han, S., Kim, Y.-S., & Lee, J. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5129 · Cited by 101
NADPH Oxidase 1 Mediates α-Synucleinopathy in Parkinson's Disease
Cristóvão, A. C., Guhathakurta, S., Bok, E., Je, G., Yoo, S. D., Choi, D., & Kim, Y. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.2246-12.2012 · Cited by 100
A key role for the microglial NADPH oxidase in APP-dependent killing of neurons
Qin, B., Cartier, L., Dubois‐Dauphin, M., Li, B., Serrander, L., & Krause, K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.036 · Cited by 99
Transplantation of human neural stem cells restores cognition in an immunodeficient rodent model of traumatic brain injury
Haus, D. L., López-Velázquez, L., Gold, E. M., Cunningham, K. M., Perez, H. D., Anderson, A. J., & Cummings, B. J. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2016.04.008 · Cited by 99
Cognitive impairment in humanized APP×PS1 mice is linked to Aβ1–42 and NOX activation
Bruce-Keller, A. J., Gupta, S., Knight, A. G., Beckett, T. L., McMullen, J. M., Davis, P. R., Murphy, M. P., Van Eldik, L. J., St Clair, D., & Keller, J. N. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.012 · Cited by 96 · cited 1×
“In addition to elevation of NOX2, there is evidence that NOX4 expression is significantly increased in the brain of aged humanized APPxPS1 knock-in mice, and that there is a significant linear correlation between NOX activity and age-dependent increases of Aβ (1–42) and cognitive dysfunction [200].”
Background
Endogenous reactive oxygen species are essential for proliferation of neural stem/progenitor cells
Yoneyama, M., Kawada, K., Gotoh, Y., Shiba, T., & Ogita, K. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.11.018 · Cited by 96
The novel NADPH oxidase 4 inhibitor GLX351322 counteracts glucose intolerance in high-fat diet-treated C57BL/6 mice
Anvari, E., Wikström, P., Walum, E., & Welsh, N. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1067697 · Cited by 95
Nadph Oxidase Mediates Striatal Neuronal Injury after Transient Global Cerebral Ischemia
Yoshioka, H., Niizuma, K., Katsu, M., Okami, N., Sakata, H., Kim, G. S., Narasimhan, P., & Chan, P. H. (2010) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.166 · Cited by 95
Revisiting oxidative damage in ALS: microglia, Nox, and mutant SOD1
Boillée, S., & Cleveland, D. W. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34613 · Cited by 95
Superoxide Prevents Nitric Oxide-Mediated Suppression of Helper T Lymphocytes: Decreased Autoimmune Encephalomyelitis in Nicotinamide Adenine Dinucleotide Phosphate Oxidase Knockout Mice
van der Veen, R. C., Dietlin, T. A., Hofman, F. M., Pen, L., Segal, B. H., & Holland, S. M. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.10.5177 · Cited by 93
Critical roles for p22phox in the structural maturation and subcellular targeting of Nox3
Nakano, Y., Bánfi, B., Jesaitis, A. J., Dinauer, M. C., Allen, L. H., & Nauseef, W. M. (2007) · Biochemical Journal · doi:10.1042/bj20060819 · Cited by 92
The NADPH Oxidase of Phagocytic Leukocytesa
Segal, A. W., & Shatwell, K. P. (1997) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1997.tb46249.x · Cited by 92
Persistent activation of microglia and NADPH oxidase drive hippocampal dysfunction in experimental multiple sclerosis
Filippo, M. D., de Iure, A., Giampà, C., Chiasserini, D., Tozzi, A., Orvietani, P. L., Ghiglieri, V., Tantucci, M., Durante, V., Quiroga‐Varela, A., et al. (2016) · Scientific Reports · doi:10.1038/srep20926 · Cited by 92
NADPH oxidase Nox1 contributes to ischemic injury in experimental stroke in mice
Kahles, T., Kohnen, A., Heumueller, S., Rappert, A., Bechmann, I., Liebner, S., Wittko, I. M., Neumann-Haefelin, T., Steinmetz, H., Schroeder, K., et al. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.023 · Cited by 91
Fyn tyrosine kinase regulates oligodendroglial cell development but is not required for morphological differentiation of oligodendrocytes
Sperber, B. R., & McMorris, F. A. (2001) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20010215)63:4 · Cited by 90
Apocynin Attenuates Cerebral Infarction after Transient Focal Ischaemia in Rats
Tang, L.-L., Ye, K., Yang, X., & Zheng, J. (2007) · Journal of International Medical Research · doi:10.1177/147323000703500411 · Cited by 90
Effect of apocynin on ozone-induced airway hyperresponsiveness to methacholine in asthmatics
Peters, E. A., Hiltermann, T. J. N., & Stolk, J. N. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00725-0 · Cited by 89
Silencing Nox4 in the Paraventricular Nucleus Improves Myocardial Infarction–Induced Cardiac Dysfunction by Attenuating Sympathoexcitation and Periinfarct Apoptosis
Infanger, D. W., Cao, X., Butler, S. D., Burmeister, M. A., Zhou, Y., Stupinski, J. A., Sharma, R. V., & Davisson, R. L. (2010) · Circulation Research · doi:10.1161/circresaha.109.213025 · Cited by 89
Microglial neurotransmitter receptors trigger superoxide production in microglia; consequences for microglial–neuronal interactions
Mead, E., Mosley, A. J., Eaton, S. D., Dobson, L., Heales, S., & Pocock, J. M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07659.x · Cited by 87
Alterations in the time course of expression of the Nox family in the brain in a rat experimental cerebral ischemia and reperfusion model: effects of melatonin
Li, H., Wang, Y., Feng, D., Liu, Y., Xu, M., Gao, A., Tian, F., Zhang, L., Cui, Y., Wang, Z., et al. (2014) · Journal of Pineal Research · doi:10.1111/jpi.12148 · Cited by 87
NOD2 is Involved in the Inflammatory Response after Cerebral Ischemia-Reperfusion Injury and Triggers NADPH Oxidase 2-Derived Reactive Oxygen Species
Liu, H., Wei, X., Kong, L., Liu, X., Cheng, L. T., Yan, S., Zhang, X., & Chen, L. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.10927 · Cited by 87
DJ-1/PARK7 Impairs Bacterial Clearance in Sepsis
Amatullah, H., Shan, Y., Beauchamp, B. L., Gali, P. L., Gupta, S., Maron‐Gutierrez, T., Speck, E. R., Fox‐Robichaud, A., Tsang, J. L. Y., Mei, S. H. J., et al. (2016) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201604-0730oc · Cited by 87
Cyclooxygenase-2 Does Not Contribute to Postischemic Production of Reactive Oxygen Species
Kunz, A. B., Anrather, J., Zhou, P., Orio, M., & Iadecola, C. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600369 · Cited by 86
Substance P Exacerbates Dopaminergic Neurodegeneration through Neurokinin-1 Receptor-Independent Activation of Microglial NADPH Oxidase
Wang, Q., Chu, C., Li, Q., Chen, S., Wilson, B. C., Oyarzabal, E. A., Jiang, L., Ali, S. F., Robinson, B. L., Kim, H., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2238-14.2014 · Cited by 86
Traumatic brain injury enhances neuroinflammation and lesion volume in caveolin deficient mice
Niesman, I., Schilling, J., Shapiro, L. A., Kellerhals, S., Bonds, J. A., Kleschevnikov, A., Cui, W.-H., Voong, A., Krajewski, S., Ali, S., et al. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-39 · Cited by 84
IL-13-induced oxidative stress via microglial NADPH oxidase contributes to death of hippocampal neurons in vivo
Park, K. W., Baik, H. H., & Jin, B. K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803392 · Cited by 84
Expression of the kidney injury molecule 1 in the rat cochlea and induction by cisplatin
Mukherjea, D., Whitworth, C. A., Nandish, S., Dunaway, G., Rybak, L. P., & Ramkumar, V. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2005.12.044 · Cited by 83
Identification of a Conserved Rac-binding Site on NADPH Oxidases Supports a Direct GTPase Regulatory Mechanism
Kao, Y.-Y., Gianni, D., Bohl, B. P., Taylor, R. M., & Bokoch, G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801010200 · Cited by 82
Hsp90 Regulates NADPH Oxidase Activity and Is Necessary for Superoxide but Not Hydrogen Peroxide Production
Chen, F., Pandey, D., Chadli, A., Catravas, J. D., Chen, T., & Fulton, D. J. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3669 · Cited by 81
Inhibition of NADPH oxidase activation reduces EAE-induced white matter damage in mice
Choi, B. Y., Kim, J. H., Kho, A. R., Kim, I. Y., Lee, S. H., Lee, B. E., Choi, E., Sohn, M., Stevenson, M., Chung, T. N., et al. (2015) · Journal of Neuroinflammation · doi:10.1186/s12974-015-0325-5 · Cited by 80
Nox2 Oxidase Activity Accounts for the Oxidative Stress and Vasomotor Dysfunction in Mouse Cerebral Arteries following Ischemic Stroke
Silva, T. M. D., Brait, V. H., Drummond, G. R., Sobey, C. G., & Miller, A. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0028393 · Cited by 80
Phosphoinositide 3-kinase couples NMDA receptors to superoxide release in excitotoxic neuronal death
Brennan, A., Shen, Y., Benna, J. E., & Swanson, R. A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.111 · Cited by 80
Expression of iron homeostasis proteins in the spinal cord in experimental autoimmune encephalomyelitis and their implications for iron accumulation.
Zarruk, J. G., Berard, J. L., dos Santos, R. P., Kroner, A., Lee, J., Arosio, P., & David, S. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.001 · Cited by 79
Intracellular pH reduction prevents excitotoxic and ischemic neuronal death by inhibiting NADPH oxidase
Lam, T. I., Brennan-Minnella, A. M., Won, S. J., Shen, Y., Hefner, C., Shi, Y., Sun, D., & Swanson, R. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313029110 · Cited by 79
A Differential Role for Endocytosis in Receptor-Mediated Activation of Nox1
Miller, F. J., Chu, X., Stanić, B., Tian, X., Sharma, R. V., Davisson, R. L., & Lamb, F. S. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2857 · Cited by 79
NOX1/NADPH oxidase negatively regulates nerve growth factor-induced neurite outgrowth
Ibi, M., Katsuyama, M., Fan, C., Iwata, K., Nishinaka, T., Yokoyama, T., & Yabe‐Nishimura, C. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.009 · Cited by 79
Detrimental role of pericyte Nox4 in the acute phase of brain ischemia
Nishimura, A., Ago, T., Kuroda, J., Arimura, K., Tachibana, M., Nakamura, K., Wakisaka, Y., Sadoshima, J., Iihara, K., & Kitazono, T. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x15606456 · Cited by 79
The effect of NADPH-oxidase inhibitor apocynin on cognitive impairment induced by moderate lateral fluid percussion injury: Role of inflammatory and oxidative brain damage
Ferreira, A. P. O., Rodrigues, F. S., Della-Pace, I. D., Mota, B. C., Oliveira, S. M., Gewehr, C. D. C. V., Bobinski, F., de Oliveira, C. V., Brum, J. S., Oliveira, M. S., et al. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.09.012 · Cited by 78
Role of Nox isoforms in angiotensin II-induced oxidative stress and endothelial dysfunction in brain
Chrissobolis, S., Bánfi, B., Sobey, C. G., & Faraci, F. M. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00455.2012 · Cited by 78
Vascular NAD(P)H Oxidase Triggers Delayed Cerebral Vasospasm After Subarachnoid Hemorrhage in Rats
Kim, D., Suh, Y. S., Lee, M., Kim, K. Y., Lee, J. H., Lee, H. S., Hong, K. W., & Kim, C. D. (2002) · Stroke · doi:10.1161/01.str.0000033071.99143.9e · Cited by 78
Role of Renal DJ-1 in the Pathogenesis of Hypertension Associated With Increased Reactive Oxygen Species Production
Cuevas, S., Zhang, Y., Yang, Y., Escano, C. S., Asico, L. D., Jones, J. E., Armando, I., & José, P. A. (2012) · Hypertension · doi:10.1161/hypertensionaha.111.185744 · Cited by 77
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
NADPH oxidase-dependent and -independent mechanisms of reported inhibitors of reactive oxygen generation
Gatto, G. J. J., Ao, Z., Kearse, M. G., Zhou, M., Morales, C. R., Daniels, E., Bradley, B. T., Goserud, M. T., Goodman, K. B., Douglas, S. A., et al. (2011) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2011.636360 · Cited by 76
Off-target thiol alkylation by the NADPH oxidase inhibitor 3-benzyl-7-(2-benzoxazolyl)thio-1,2,3-triazolo[4,5-d]pyrimidine (VAS2870)
Sun, Q.-A., Hess, D. T., Wang, B., Miyagi, M., & Stamler, J. S. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.02.046 · Cited by 76
Park7 interacts with p47phox to direct NADPH oxidase-dependent ROS production and protect against sepsis
Liu, W., Wu, H., Chen, L., Wen, Y., Kong, X., & Gao, W. (2015) · Cell Research · doi:10.1038/cr.2015.63 · Cited by 75
Phosphatidylinositol-3-Kinase Gamma Plays a Central Role in Blood–Brain Barrier Dysfunction in Acute Experimental Stroke
Jin, R., Song, Z., Yu, S., Piazza, A., Nanda, A., Penninger, J. M., Granger, D. N., & Li, G. (2011) · Stroke · doi:10.1161/strokeaha.110.601369 · Cited by 75
Ischemia-activated microglia induces neuronal injury via activation of gp91phox NADPH oxidase
Hur, J., Lee, P., Kim, M. J., Kim, Y., & Cho, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.114 · Cited by 74
CK2 Is a Novel Negative Regulator of NADPH Oxidase and a Neuroprotectant in Mice after Cerebral Ischemia
Kim, G. S., Jung, J. E., Niizuma, K., & Chan, P. H. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4161-09.2009 · Cited by 74
Nox4 Is a Major Source of Superoxide Production in Human Brain Pericytes
Kuroda, J., Ago, T., Nishimura, A., Nakamura, K., Matsuo, R., Wakisaka, Y., Kamouchi, M., & Kitazono, T. (2014) · Journal of Vascular Research · doi:10.1159/000369930 · Cited by 73 · cited 1×
“It is reported to be a major source of superoxide in human pericytes [110].”
Background
Multiple sclerosis is primarily a neurodegenerative disease
Chaudhuri, A. (2013) · Journal of Neural Transmission · doi:10.1007/s00702-013-1080-3 · Cited by 72
Early increase of Nox4 NADPH oxidase and superoxide generation following endothelin‐1‐induced stroke in conscious rats
McCann, S., Dusting, G. J., & Roulston, C. L. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21700 · Cited by 72
Importance of NOX1 for angiotensin II-induced cerebrovascular superoxide production and cortical infarct volume following ischemic stroke
Jackman, K. A., Miller, A. A., Drummond, G. R., & Sobey, C. G. (2009) · Brain Research · doi:10.1016/j.brainres.2009.06.056 · Cited by 72
Vascular cognitive impairment and Alzheimer’s disease: role of cerebral hypoperfusion and oxidative stress
Kim, H. A., Miller, A. A., Drummond, G. R., Thrift, A. G., Arumugam, T. V., Phan, T. G., Srikanth, V. K., & Sobey, C. G. (2012) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-012-0790-7 · Cited by 71
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
Traumatic brain injury precipitates cognitive impairment and extracellular Aβ aggregation in Alzheimer’s disease transgenic mice
Tajiri, N., Kellogg, S. L., Shimizu, T., Arendash, G. W., & Borlongan, C. V. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078851 · Cited by 70
Hyperbaric Oxygen Suppresses NADPH Oxidase in a Rat Subarachnoid Hemorrhage Model
Ostrowski, R. P., Tang, J., & Zhang, J. H. (2006) · Stroke · doi:10.1161/01.str.0000217310.88450.c3 · Cited by 70
Long-Term Stimulation of Neural Progenitor Cell Migration After Cortical Ischemia in Mice
Osman, A. M., Porritt, M. J., Nilsson, M., & Kuhn, H. G. (2011) · Stroke · doi:10.1161/strokeaha.111.627802 · Cited by 70
Erratum: Phosphoinositide 3-kinase couples NMDA receptors to superoxide release in excitotoxic neuronal death
Brennan, A., Shen, Y., Benna, J. E., & Swanson, R. A. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.164 · Cited by 69
Significance of marrow‐derived nicotinamide adenine dinucleotide phosphate oxidase in experimental ischemic stroke
Tang, X. N., Zheng, Z., Giffard, R. G., & Yenari, M. A. (2011) · Annals of Neurology · doi:10.1002/ana.22476 · Cited by 69
Activation of NOX2 by the Stimulation of Ionotropic and Metabotropic Glutamate Receptors Contributes to Glutamate Neurotoxicity In Vivo Through the Production of Reactive Oxygen Species and Calpain Activation
Guemez‐Gamboa, A., Estrada‐Sánchez, A. M., Montiel, T., Páramo, B., Massieu, L., & Morán, J. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3182358e4e · Cited by 68
Cerebrospinal fluid levels of free 3-nitrotyrosine are not elevated in the majority of patients with amyotrophic lateral sclerosis or Alzheimer's disease
Ryberg, H. (2004) · Neurochemistry International · doi:10.1016/j.neuint.2003.12.012 · Cited by 68
Characterisation of Brain Edema Following “Controlled Cortical Impact Injury” in Rats
Unterberg, A. W., Stroop, R., Thomale, U., Kiening, K. L., Päuser, S., & Vollmann, W. (1997) · Springer eBooks · doi:10.1007/978-3-7091-6837-0_33 · Cited by 67
Brain‐derived neurotrophic factor promotes angiogenic tube formation through generation of oxidative stress in human vascular endothelial cells
Usui, T., Naruo, A., Okada, M., Hayabe, Y., & Yamawaki, H. (2014) · Acta Physiologica · doi:10.1111/apha.12249 · Cited by 67
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
NOX activity in brain aging: Exacerbation by high fat diet
Bruce‐Keller, A. J., White, C. L., Gupta, S., Knight, A. G., Pistell, P. J., Ingram, D. K., Morrison, C. D., & Keller, J. N. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.006 · Cited by 66
Nox2 regulates endothelial cell cycle arrest and apoptosis via p21cip1 and p53
Li, J., Fan, L. M., George, V. T., & Brooks, G. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.06.001 · Cited by 65
Distinct role of nitric oxide and peroxynitrite in mediating oligodendrocyte toxicity in culture and in experimental autoimmune encephalomyelitis
Li, S., Vana, A. C., Ribeiro, R., & Zhang, Y. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.04.007 · Cited by 65
Pharmacological and genetic inhibition of NADPH oxidase does not reduce brain damage in different models of perinatal brain injury in newborn mice
Doverhag, C., Keller, M., Karlsson, A., Hedtjärn, M., Nilsson, U., Kapeller, E., Sárközy, G., Klimaschewski, L. P., Humpel, C., Hagberg, H., et al. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.04.003 · Cited by 64
Apocynin reduces reactive oxygen species concentrations in exhaled breath condensate in asthmatics
Stefanska, J., Sarniak, A., Włodarczyk, A., Sokołowska, M., Pniewska, E., Doniec, Z., Nowak, D., & Pawliczak, R. (2012) · Experimental Lung Research · doi:10.3109/01902148.2011.649823 · Cited by 64
Partitioning of superoxide and hydrogen peroxide production by mitochondrial respiratory complex I
Grivennikova, V. G., & Vinogradov, A. D. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.01.002 · Cited by 64
Aptamers as Promising Molecular Recognition Elements for Diagnostics and Therapeutics in the Central Nervous System
McConnell, E. M., Holahan, M. R., & DeRosa, M. C. (2014) · Nucleic Acid Therapeutics · doi:10.1089/nat.2014.0492 · Cited by 62
The NADPH oxidase Nox2 regulates VEGFR1/CSF‐1R‐mediated microglial chemotaxis and promotes early postnatal infiltration of phagocytes in the subventricular zone of the mouse cerebral cortex
Lelli, A., Gervais, A., Colin, C., Chéret, C., de Almodóvar, C. R., Carmeliet, P., Krause, K., Boillée, S., & Mallat, M. (2013) · Glia · doi:10.1002/glia.22540 · Cited by 60
Characterization of NADPH oxidase 5 expression in human tumors and tumor cell lines with a novel mouse monoclonal antibody
Antony, S., Wu, Y., Hewitt, S. M., Anver, M. R., Butcher, D. O., Jiang, G., Meitzler, J. L., Liu, H., Juhasz, A. N., Lu, J., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.005 · Cited by 60
NADPH oxidase inhibition improves neurological outcomes in surgically-induced brain injury
Lo, W., Bravo, T. P., Jadhav, V. R., Titova, E., Zhang, J. H., & Tang, J. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2006.12.055 · Cited by 60
NADPH oxidase inhibition improves neurological outcome in experimental traumatic brain injury
Lu, X., Wang, H., Xu, J., Ding, K., & Li, T. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.02.006 · Cited by 59
Nox5 Forms a Functional Oligomer Mediated by Self-Association of Its Dehydrogenase Domain
Kawahara, T., Jackson, H. M., Smith, S. M. E., Simpson, P. D., & Lambeth, J. D. (2011) · Biochemistry · doi:10.1021/bi1020088 · Cited by 59
Modulation of NADPH oxidase activation in cerebral ischemia/reperfusion injury in rats
Genovese, T., Mazzon, E., Paterniti, I., Esposito, E., Bramanti, P., & Cuzzocrea, S. (2010) · Brain Research · doi:10.1016/j.brainres.2010.11.088 · Cited by 58
Subpicomolar diphenyleneiodonium inhibits microglial NADPH oxidase with high specificity and shows great potential as a therapeutic agent for neurodegenerative diseases
Wang, Q., Chu, C., Oyarzabal, E. A., Jiang, L., Chen, S., Wilson, B. C., Li, Q., & Hong, J. (2014) · Glia · doi:10.1002/glia.22724 · Cited by 57
NOX2 deficiency ameliorates cerebral injury through reduction of complexin II-mediated glutamate excitotoxicity in experimental stroke
Wang, Z., Wei, X., Liu, K., Zhang, X., Yang, F., Zhang, H., He, Y., Zhu, T., Li, F., Shi, W., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.08.166 · Cited by 56
Role of Neuronal NADPH Oxidase 1 in the Peri-Infarct Regions after Stroke
Choi, D.-H., Kim, J.-H., Lee, K.-H., Kim, H.-Y., Kim, Y.-S., Choi, W. S., & Lee, J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0116814 · Cited by 56
Diapocynin and apocynin administration fails to significantly extend survival in G93A SOD1 ALS mice
Trumbull, K. A., McAllister, D. M., Gandelman, M., Fung, W. Y., Lew, T. K., Brennan, L. D., Lopez, N. I., Morré, J. T., Kalyanaraman, B., & Beckman, J. S. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.015 · Cited by 56
Role of NADPH oxidase in H9c2 cardiac muscle cells exposed to simulated ischaemia‐reperfusion
Borchi, E., Parri, M., Papucci, L., Becatti, M., Nassi, N., Nassi, P., & Nediani, C. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00485.x · Cited by 56
Translating the oxidative stress hypothesis into the clinic: NOX versus NOS
Armitage, M. E., Wingler, K., Schmidt, H. H. H. W., & La, M. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0544-2 · Cited by 56
Role of NADPH oxidase in the apoptotic death of cultured cerebellar granule neurons
Coyoy-Salgado, A., Valencia, A., Guemez‐Gamboa, A., & Morán, J. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.06.027 · Cited by 55
Placental Gene Expression in a Rat ‘Model’ of Placental Insufficiency
Goyal, R., Yellon, S. M., Longo, L. D., & Mata‐Greenwood, E. (2010) · Placenta · doi:10.1016/j.placenta.2010.05.004 · Cited by 55
Noise-induced changes in expression levels of NADPH oxidases in the cochlea
Vlajkovic, S. M., Lin, S. C. Y., Wong, A. C. Y., Wackrow, B., & Thorne, P. R. (2013) · Hearing Research · doi:10.1016/j.heares.2013.07.012 · Cited by 55
The NOX1/4 Inhibitor GKT136901 as Selective and Direct Scavenger of Peroxynitrite
Schildknecht, S., Weber, A., Gerding, H., Pape, R., Robotta, M., Drescher, M., Marquardt, A., Daiber, A., Ferger, B., & Leist, M. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990179 · Cited by 55
Microglial Cells Are Involved in the Susceptibility of NADPH Oxidase Knockout Mice to 6-Hydroxy-Dopamine-Induced Neurodegeneration
Hernandes, M. S., Santos, G. D. R., Café-Mendes, C. C., Lima, L. S., Scavone, C., Munhoz, C. D., & Britto, L. R. G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075532 · Cited by 54
Negative Regulation of NADPH Oxidase 4 by Hydrogen Peroxide-inducible Clone 5 (Hic-5) Protein
Desai, L. P., Zhou, Y., Venado, A. E., Ding, Q., Cheng, G., Collawn, J. F., & Thannickal, V. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.562249 · Cited by 53
NADPH Oxidase-2: Linking Glucose, Acidosis, and Excitotoxicity in Stroke
Brennan, A., Won, S. J., & Swanson, R. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5767 · Cited by 53
NADPH Oxidase and the Degeneration of Dopaminergic Neurons in Parkinsonian Mice
Hernandes, M. S., Café-Mendes, C. C., & Britto, L. R. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/157857 · Cited by 51
Chronic Cocaine-Induced Cardiac Oxidative Stress and Mitogen-Activated Protein Kinase Activation: The Role of Nox2 Oxidase
Fan, L. M., Sawbridge, D., George, V. T., Teng, L., Bailey, A., Kitchen, I., & Li, J. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.145201 · Cited by 51
Apocyanin, a Microglial NADPH Oxidase Inhibitor Prevents Dopaminergic Neuronal Degeneration in Lipopolysaccharide-Induced Parkinson’s Disease Model
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Danta, C. C., & Piplani, P. (2014) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2014.942218 · Cited by 48
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Fu, P., Mohan, V., Syed, M. A., Tiruppathì, C., Sadikot, R. T., & Natarajan, V. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0242oc · Cited by 47
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Lucke-Wold, B. P., Naser, Z. J., Logsdon, A. F., Turner, R. C., Smith, K. E., Robson, M. J., Bailes, J. E., Lee, J. M., Rosen, C. L., & Huber, J. D. (2015) · Translational research · doi:10.1016/j.trsl.2015.08.005 · Cited by 44
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Kim, M., Ryu, J., Kwon, Y., Lee, S., Bae, Y. S., Yoon, J., & Ryu, J.-H. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5677 · Cited by 44
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Galbussera, A. A., Tremolizzo, L., Brighina, L., Testa, D., Lovati, R., Ferrarese, C., Cavaletti, G., & Filippini, G. (2006) · Neurological Sciences · doi:10.1007/s10072-006-0668-x · Cited by 44
Oral Treatment with the NADPH Oxidase Antagonist Apocynin Mitigates Clinical and Pathological Features of Parkinsonism in the MPTP marmoset Model
Philippens, I. H. C. H. M., Wubben, J. A. M., Finsen, B. R., & Hart, B. A. ‘. (2013) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-013-9450-z · Cited by 44
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Marrali, G., Casale, F., Salamone, P., Fuda, G., Caorsi, C., Amoroso, A., Brunetti, M., Restagno, G., Barberis, M., Bertuzzo, D., et al. (2014) · Journal of Neurology · doi:10.1007/s00415-014-7470-0 · Cited by 43
Diapocynin prevents early Parkinson's disease symptoms in the leucine-rich repeat kinase 2 (LRRK2R1441G) transgenic mouse
Dranka, B. P., Gifford, A., Ghosh, A., Zielonka, J., Joseph, J., Kanthasamy, A. G., & Kalyanaraman, B. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.05.034 · Cited by 43
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Ling, Q., Shi, W., Huang, C., Zheng, J., Cheng, Q., Yu, K., Chen, S., Zhang, H., Li, N., & Chen, M. (2014) · Europe PMC (PubMed Central) · Cited by 42
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Streeter, J., Schickling, B., Jiang, S., Stanić, B., Thiel, W. H., Gakhar, L., Houtman, J. C. D., & Miller, F. J. (2014) · Circulation Research · doi:10.1161/circresaha.115.304267 · Cited by 42
Oxygen radical production in leukocytes and disease severity in multiple sclerosis
Mossberg, N., Movitz, C., Hellstrand, K., Bergström, T. B., Nilsson, S., & Andersen, O. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.05.013 · Cited by 40
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José, G. S., Bidegain, J., Robador, P. A., Dı́ez, J., Fortuño, A., & Zalba, G. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.009 · Cited by 40
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Yamamoto, A., Takeya, R., Matsumoto, M., Nakayama, K. I., & Sumimoto, H. (2013) · FEBS Journal · doi:10.1111/febs.12489 · Cited by 39
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Liu, Z., Tuo, Y.-H., Chen, J., Wang, Q.-Y., Li, S., Li, M., Dai, G., Wang, J., Zhang, Y., Feng, L., et al. (2016) · Journal of NeuroInterventional Surgery · doi:10.1136/neurintsurg-2016-012463 · Cited by 39
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Zhang, H., Li, T., Liu, B., Lou, Z., Zhang, J.-J., Peng, J.-J., Zhang, X.-J., Ma, Q., Peng, J., & Luo, X. (2015) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-015-1125-2 · Cited by 38
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Shin, H. K., Lee, J. H., Kim, K. Y., Kim, C. D., Lee, W. S., Rhim, B. Y., & Hong, K. W. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200207000-00012 · Cited by 38
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Authors: Ma, M. W., Wang, J., Zhang, Q., Wang, R., Dhandapani, K. M., Vadlamudi, R. K., & Brann, D. W.
Affiliations: Augusta University (US)
The University of Texas at San Antonio Health Science Center (US)
Corresponding author: Brann, Darrell W.
ORCID: Ma, Merry W.
Wang, Jing
Zhang, Quanguang
Wang, Ruimin
Dhandapani, Krishnan M.
Vadlamudi, Ratna K.
Brann, Darrell W.
Venue: Molecular Neurodegeneration
Publisher: Springer Science and Business Media LLC
Published: 2017-01-17
Volume: 12
Issue: 1
Pages: 7-7
ISSN: 1750-1326 (ISSN-L)
DOI: 10.1186/s13024-017-0150-7
PMC: PMC5240251
OpenAlex: W2574254633
Cited by: 432
References: 417
Citations by year: 2026: 21 · 2025: 45 · 2024: 43 · 2023: 59 · 2022: 44 · 2021: 67 · 2020: 49 · 2019: 38 · 2018: 40 · 2017: 26
FWCI: 3.92
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Molecular Neurodegeneration (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: U.S. Department of Veterans Affairs (5l101BX001117)
National Institute of Neurological Disorders and Stroke (5R01NS050730, R01NS088058)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Keywords: NADPH oxidase, oxidative stress, neurodegenerative diseases, brain injury, ischemic brain injury, traumatic brain injury, NOX1, NOX2, NOX4, neuroprotection, antioxidant therapy, Alzheimer's disease, Parkinson's disease, Huntington's disease, amyotrophic lateral sclerosis, multiple sclerosis
MeSH terms: Animals, Brain Injuries, Humans, NADPH Oxidases, Neurodegenerative Diseases

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NADPH oxidase in brain injury and neurodegenerative disorders

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