Cited by 202Neuroinflammation and Neurodegeneration MechanismsRedox biology and oxidative stressInflammasome and immune disorders

The DOI matches its Crossref record; 163 of the 163 references it cites were found in a registry or an index.

NADPH oxidase- and mitochondria-derived reactive oxygen species in proinflammatory microglial activation: a bipartisan affair?

Open access

Bordt, Evan A., Polster, Brian M.·2014·Free Radical Biology and Medicine

DOI 10.1016/j.freeradbiomed.2014.07.033PMC PMC4252610

Open this paper in CoChat — free account

Abstract

Microglia are the resident immune cells of the brain and play major roles in central nervous system development, maintenance, and disease. Brain insults cause microglia to proliferate, migrate, and transform into one or more activated states. Classical M1 activation triggers the production of proinflammatory factors such as tumor necrosis factor-α, interleukin-1β (IL-1β), nitric oxide, and reactive oxygen species (ROS), which, in excess, can exacerbate brain injury. The mechanisms underlying microglial activation are not fully understood, yet reactive oxygen species are increasingly implicated as mediators of microglial activation. In this review, we highlight studies linking reactive oxygen species, in particular hydrogen peroxide derived from NADPH oxidase-generated superoxide, to the classical activation of microglia. In addition, we critically evaluate controversial evidence suggesting a specific role for mitochondrial reactive oxygen species in the activation of the NLRP3 inflammasome, a multiprotein complex that mediates the production of IL-1β and IL-18. Finally, the limitations of common techniques used to implicate mitochondrial ROS in microglial and inflammasome activation, such as the use of the mitochondrially targeted ROS indicator MitoSOX and the mitochondrially targeted antioxidant MitoTEMPO, are also discussed.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.freeradbiomed.2014.07.033

Cites

163 of 163 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80434-1 · Cited by 7,289
A role for mitochondria in nlrp3 inflammasome activation
Zhou, R., Yazdi, A. S., Menu, P., & Tschopp, J. (2011) · Nature · doi:10.1038/nature09663 · Cited by 5,602
Microglia: a sensor for pathological events in the CNS
Kreutzberg, G. W. (1996) · Trends in Neurosciences · doi:10.1016/0166-2236(96)10049-7 · Cited by 4,396
Microglia-mediated neurotoxicity: uncovering the molecular mechanisms
Block, M. L., Zecca, L., & Hong, J.-S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2038 · Cited by 4,110
Chronic systemic pesticide exposure reproduces features of Parkinson's disease
Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Cutting Edge: NF-κB Activating Pattern Recognition and Cytokine Receptors License NLRP3 Inflammasome Activation by Regulating NLRP3 Expression
Bauernfeind, F. G., Horvath, G. L., Stutz, A., Alnemri, E. S., MacDonald, K. L., Speert, D. P., Fernandes‐Alnemri, T., Wu, J., Monks, B. G., Fitzgerald, K. A., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901363 · Cited by 3,087
Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization
Hornung, V., Bauernfeind, F., Halle, A., Samstad, E. O., Kono, H., Rock, K. L., Fitzgerald, K. A., & Latz, E. (2008) · Nature Immunology · doi:10.1038/ni.1631 · Cited by 3,065
Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
Nakahira, K., Haspel, J. A., Rathinam, V. A. K., Lee, S.-J., Dolinay, T., Lam, H. C., Englert, J. A., Rabinovitch, M., Cernadas, M., Kim, H. P., et al. (2011) · Nature Immunology · doi:10.1038/ni.1980 · Cited by 3,049
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898
Thioredoxin-interacting protein links oxidative stress to inflammasome activation
Zhou, R., Tardivel, A., Thorens, B., Choi, I., & Tschopp, J. (2010) · Nature Immunology · doi:10.1038/ni.1831 · Cited by 2,708
Innate Immune Activation Through Nalp3 Inflammasome Sensing of Asbestos and Silica
Dostert, C., Pétrilli, V., Van Bruggen, R., Steele, C., Mossman, B. T., & Tschopp, J. (2008) · Science · doi:10.1126/science.1156995 · Cited by 2,658
The NALP3 inflammasome is involved in the innate immune response to amyloid-β
Halle, A., Hornung, V., Petzold, G. C., Stewart, C. R., Monks, B. G., Reinheckel, T., Fitzgerald, K. A., Latz, E., Moore, K. J., & Golenbock, D. T. (2008) · Nature Immunology · doi:10.1038/ni.1636 · Cited by 2,441
Cellular response to oxidative stress: Signaling for suicide and survival*
Martindale, J. L., & Holbrook, N. J. (2002) · Journal of Cellular Physiology · doi:10.1002/jcp.10119 · Cited by 2,314
Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis
Shimada, K., Crother, T. R., Karlin, J., Dagvadorj, J., Chiba, N., Chen, S., Ramanujan, V. K., Wolf, A. J., Vergnes, L., Ojcius, D. M., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.009 · Cited by 2,282
K+ Efflux Is the Common Trigger of NLRP3 Inflammasome Activation by Bacterial Toxins and Particulate Matter
Muñoz-Planillo, R., Kuffa, P., Martínez-Colón, G. J., Smith, B. L., Rajendiran, T. M., & Núñez, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.05.016 · Cited by 2,167
Reactive Oxygen Species Promote TNFα-Induced Death and Sustained JNK Activation by Inhibiting MAP Kinase Phosphatases
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
Onset and Progression in Inherited ALS Determined by Motor Neurons and Microglia
Boillée, S., Yamanaka, K., Lobsiger, C. S., Copeland, N. G., Jenkins, N. A., Kassiotis, G., Kollias, G., & Cleveland, D. W. (2006) · Science · doi:10.1126/science.1123511 · Cited by 1,623
Microglia and inflammation-mediated neurodegeneration: Multiple triggers with a common mechanism
Block, M. L., & Hong, J.-S. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.06.004 · Cited by 1,557
The microglial sensome revealed by direct RNA sequencing
Hickman, S. E., Kingery, N. D., Ohsumi, T. K., Borowsky, M. L., Wang, L.-C., Means, T. K., & El Khoury, J. (2013) · Nature Neuroscience · doi:10.1038/nn.3554 · Cited by 1,511
Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
Pétrilli, V, Papin, S., Dostert, C., Mayor, A., Martinon, F., & Tschopp, J. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402195 · Cited by 1,445
Toxicity of iron and hydrogen peroxide: the Fenton reaction
Winterbourn, C. C. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03532-x · Cited by 1,415
Superoxide activates mitochondrial uncoupling proteins
Echtay, K. S., Roussel, D., St-Pierre, J., Jekabsons, M. B., Cadenas, S., Stuart, J. A., Harper, J. A., Roebuck, S. J., Morrison, A., Pickering, S., et al. (2002) · Nature · doi:10.1038/415096a · Cited by 1,382
Mitochondrial metabolism of reactive oxygen species
Andreyev, A. Y., Kushnareva, Y. E., & Starkov, A. A. (2005) · Biochemistry (Moscow) · doi:10.1007/s10541-005-0102-7 · Cited by 1,336
Activation of the NLRP3 inflammasome by islet amyloid polypeptide provides a mechanism for enhanced IL-1β in type 2 diabetes
Masters, S. L., Dunne, A., Subramanian, S. L., Hull, R. L., Tannahill, G. M., Sharp, F. A., Becker, C., Franchi, L., Yoshihara, E., Chen, Z., et al. (2010) · Nature Immunology · doi:10.1038/ni.1935 · Cited by 1,330 · cited 1×
“However, a subsequent study failed to reproduce this finding [149].”
Mechanism of Toxicity in Rotenone Models of Parkinson's Disease
Sherer, T., Betarbet, R. S., Testa, C. M., Seo, B. B., Richardson, J. R., Kim, J. H., Miller, G. W., Yagi, T., Matsuno‐Yagi, A., & Greenamyre, J. T. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-34-10756.2003 · Cited by 1,102
Disruption of the uncoupling protein-2 gene in mice reveals a role in immunity and reactive oxygen species production
Arsenijevic, D., Onuma, H., Pecqueur, C., Raimbault, S., Manning, B. S., Miroux, B., Couplan, E., Alves‐Guerra, M., Goubern, M., Surwit, R. S., et al. (2000) · Nature Genetics · doi:10.1038/82565 · Cited by 1,100
Microglial cell origin and phenotypes in health and disease
Saijo, K., & Glass, C. K. (2011) · Nature Reviews Immunology · doi:10.1038/nri3086 · Cited by 1,100
Microglial Activation and Chronic Neurodegeneration
Lull, M. E., & Block, M. L. (2010) · Neurotherapeutics · doi:10.1016/j.nurt.2010.05.014 · Cited by 1,047
The Role of Microglia in the Healthy Brain: Figure 1.
Tremblay, M.-È., Stevens, B., Sierra, A., Wake, H., Bessis, A., & Nimmerjahn, A. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4158-11.2011 · Cited by 992
Mitochondrial Cardiolipin Is Required for Nlrp3 Inflammasome Activation
Iyer, S. S., He, Q., Janczy, J. R., Elliott, E. I., Zhong, Z., Olivier, A. K., Sadler, J. J., Knepper-Adrian, V., Han, R., Qiao, L., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.08.001 · Cited by 968
Specific and Reversible Inactivation of Protein Tyrosine Phosphatases by Hydrogen Peroxide: Evidence for a Sulfenic Acid Intermediate and Implications for Redox Regulation
Denu, J. M., & Tanner, K. G. (1998) · Biochemistry · doi:10.1021/bi973035t · Cited by 945
Heterogeneity of Microglial Activation in the Innate Immune Response in the Brain
Colton, C. A. (2009) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-009-9164-4 · Cited by 916
Extension of Life-Span with Superoxide Dismutase/Catalase Mimetics
Melov, S., Ravenscroft, J., Malik, S., Gill, M. S., Walker, D. W., Clayton, P., Wallace, D. C., Malfroy, B., Doctrow, S. R., & Lithgow, G. J. (2000) · Science · doi:10.1126/science.289.5484.1567 · Cited by 913
An essential role for free radicals and derived species in signal transduction
Lander, H. M. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.2.9039953 · Cited by 908
Microtubule-driven spatial arrangement of mitochondria promotes activation of the NLRP3 inflammasome
Misawa, T., Takahama, M., Kozaki, T., Lee, H., Zou, J., Saitoh, T., & Akira, S. (2013) · Nature Immunology · doi:10.1038/ni.2550 · Cited by 894
Mitochondrial reactive oxygen species promote production of proinflammatory cytokines and are elevated in TNFR1-associated periodic syndrome (TRAPS)
Bulua, A. C., Simon, A., Maddipati, R., Pelletier, M., Park, H., Kim, K.-Y., Sack, M. N., Kastner, D. L., & Siegel, R. M. (2011) · Journal of Experimental Medicine · doi:10.1084/jem.20102049 · Cited by 860
Mitochondrial permeability transition and oxidative stress
Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02316-x · Cited by 832
Glyburide inhibits the Cryopyrin/Nalp3 inflammasome
Lamkanfi, M., Mueller, J. L., Vitari, A. C., Misaghi, S., Fedorova, A., Deshayes, K., Lee, W. P., Hoffman, H. M., & Dixit, V. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200903124 · Cited by 820
Selective fluorescent imaging of superoxide in vivo using ethidium-based probes
Robinson, K. M., Janes, M. S., Pehar, M., Monette, J. S., Ross, M. F., Hagen, T. M., Murphy, M. P., & Beckman, J. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601945103 · Cited by 777
Microglia and neurodegeneration: The role of systemic inflammation
Cunningham, C. (2013) · Glia · doi:10.1002/glia.22350 · Cited by 769
Therapeutic Targeting of Mitochondrial Superoxide in Hypertension
Dikalova, A., Bikineyeva, A. T., Budzyn, K., Nazarewicz, R. R., McCann, L. A., Lewis, W., Harrison, D. G., & Dikalov, S. (2010) · Circulation Research · doi:10.1161/circresaha.109.214601 · Cited by 745
Neuroinflammation after traumatic brain injury: Opportunities for therapeutic intervention
Kumar, A., & Loane, D. J. (2012) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2012.06.008 · Cited by 710
Production of hydroxyl radicals from the simultaneous generation of superoxide and nitric oxide
Hogg, N., Darley-Usmar, V. M., Wilson, M. T., & Moncada, S. (1992) · Biochemical Journal · doi:10.1042/bj2810419 · Cited by 698
A Neurodegeneration-Specific Gene-Expression Signature of Acutely Isolated Microglia from an Amyotrophic Lateral Sclerosis Mouse Model
Chiu, I. M., Morimoto, E. T. A., Goodarzi, H., Liao, J. T., O’Keeffe, S., Phatnani, H. P., Muratet, M., Carroll, M. C., Levy, S., Tavazoie, S., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.018 · Cited by 651
Microglia Induce Motor Neuron Death via the Classical NF-κB Pathway in Amyotrophic Lateral Sclerosis
Frakes, A. E., Ferraiuolo, L., Haidet-Phillips, A. M., Schmelzer, L., Braun, L., Miranda, C. J., Ladner, K. J., Bevan, A. K., Foust, K. D., Godbout, J. P., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.01.013 · Cited by 638
Cutting Edge: Reactive Oxygen Species Inhibitors Block Priming, but Not Activation, of the NLRP3 Inflammasome
Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Núñez, G., & Hornung, V. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100613 · Cited by 617
Signaling by ROS drives inflammasome activation
Martinon, F. (2010) · European Journal of Immunology · doi:10.1002/eji.200940168 · Cited by 604
Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies
Codolo, G., Plotegher, N., Pozzobon, T., Brucale, M., Tessari, I., Bubacco, L., & de Bernard, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055375 · Cited by 585
NADPH Oxidase Mediates Lipopolysaccharide-induced Neurotoxicity and Proinflammatory Gene Expression in Activated Microglia
Qin, L., Liu, Y., Wang, T., Wei, S.-J., Block, M. L., Wilson, B., Liu, B., & Hong, J.-S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307657200 · Cited by 574
Mitochondrial Reactive Oxygen Species Induces NLRP3-Dependent Lysosomal Damage and Inflammasome Activation
Heid, M. E., Keyel, P. A., Kamga, C., Shiva, S., Watkins, S. C., & Salter, R. D. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1301490 · Cited by 570
Hydroethidine- and MitoSOX-derived red fluorescence is not a reliable indicator of intracellular superoxide formation: Another inconvenient truth
Zielonka, J., & Kalyanaraman, B. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.028 · Cited by 543
Microglia, macrophages, perivascular macrophages, and pericytes: a review of function and identification
Guillemin, G. J., & Brew, B. J. (2003) · Journal of Leukocyte Biology · doi:10.1189/jlb.0303114 · Cited by 520
Progressive Neurodegeneration After Experimental Brain Trauma: Association With Chronic Microglial Activation
Loane, D. J., Kumar, A., Stoica, B. A., Cabatbat, R., & Faden, A. I. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000021 · Cited by 498
P53, cell cycle control and apoptosis: Implications for cancer
Kastan, M. B., Canman, C. E., & Leonard, C. J. (1995) · Cancer and Metastasis Reviews · doi:10.1007/bf00690207 · Cited by 482
The Transcription Factor Nrf2 Is a Therapeutic Target against Brain Inflammation
Innamorato, N. G., Rojo, A. I., García‐Yagüe, Á. J., Yamamoto, M. P., CEBALLOS, M. L. D., & Cuadrado, A. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.1.680 · Cited by 479
Diphenyleneiodonium, an NAD(P)H Oxidase Inhibitor, also Potently Inhibits Mitochondrial Reactive Oxygen Species Production
Li, Y., & Trush, M. A. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9729 · Cited by 470
Selective targeting of an antioxidant to mitochondria
Smith, R. A. J., Porteous, C. M., Coulter, C. V., & Murphy, M. P. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00543.x · Cited by 466
Distinct Role for Microglia in Rotenone-Induced Degeneration of Dopaminergic Neurons
Gao, H., Hong, J., Zhang, W., & Liu, B. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-03-00782.2002 · Cited by 439
Brain microglia constitutively express β-2 integrins
Akiyama, H., & McGeer, P. L. (1990) · Journal of Neuroimmunology · doi:10.1016/0165-5728(90)90055-r · Cited by 430
Drug delivery to mitochondria: the key to mitochondrial medicine
Murphy, M. P., & Smith, R. A. J. (2000) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(99)00069-1 · Cited by 429
Redox regulation of glial inflammatory response to lipopolysaccharide and interferonγ
Pawate, S., Shen, Q., Fan, F., & Bhat, N. R. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20180 · Cited by 428
Biochemical-physiology correlations in studies of the γ-aminobutyric acid system
Roberts, E., & Kuriyama, K. (1968) · Brain Research · doi:10.1016/0006-8993(68)90170-4 · Cited by 409
UCP2 transports C4 metabolites out of mitochondria, regulating glucose and glutamine oxidation
Vozza, A., Parisi, G., De Leonardis, F., Lasorsa, F. M., Castegna, A., Amorese, D., Marmo, R., Calcagnile, V. M., Palmieri, L., Ricquier, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317400111 · Cited by 407
Nrf2 regulates microglial dynamics and neuroinflammation in experimental Parkinson's disease
Rojo, A. I., Innamorato, N. G., Martín-Moreno, A. M., CEBALLOS, M. L. D., Yamamoto, M. P., & Cuadrado, A. (2009) · Glia · doi:10.1002/glia.20947 · Cited by 390
Inflammasomes: current understanding and open questions
Bauernfeind, F. G., Ablasser, A., Bartok, E., Kim-Hellmuth, S., Schmid-Burgk, J. L., Cavlar, T., & Hornung, V. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0567-4 · Cited by 369
HMGB1 acts on microglia Mac1 to mediate chronic neuroinflammation that drives progressive neurodegeneration
Gao, H.-M., Zhou, H., Zhang, F., Wilson, B. C., Kam, W., & Hong, J.-S. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3732-10.2011 · Cited by 369
Oxidative damage to macromolecules in human Parkinson disease and the rotenone model
Sanders, L. H., & Greenamyre, J. T. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.003 · Cited by 360
Phagocytosis executes delayed neuronal death after focal brain ischemia
Neher, J. J., Emmrich, J., Fricker, M., Mander, P. K., Théry, C., & Brown, G. C. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1308679110 · Cited by 357
Extracellular superoxide dismutase and cardiovascular disease
Fukai, T. (2002) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00328-0 · Cited by 347
Critical Role for Microglial NADPH Oxidase in Rotenone-Induced Degeneration of Dopaminergic Neurons
Gao, H., Liu, B., & Hong, J. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-15-06181.2003 · Cited by 338
Simple quantitative detection of mitochondrial superoxide production in live cells
Mukhopadhyay, P., Rajesh, M., Kashiwaya, Y., Haskó, G., & Pacher, P. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.04.106 · Cited by 333
Superoxide dismutase 1 regulates caspase-1 and endotoxic shock
Meissner, F., Molawi, K., & Zychlinsky, A. (2008) · Nature Immunology · doi:10.1038/ni.1633 · Cited by 308
NLRP3 inflammasome contributes to inflammation after intracerebral hemorrhage
Ma, Q., Chen, S., Hu, Q., Feng, H., Zhang, J. H., & Tang, J. (2013) · Annals of Neurology · doi:10.1002/ana.24070 · Cited by 299
Reactive Oxygen Species and Antioxidants in Signal Transduction and Gene Expression
Palmer, H. J., & Paulson, K. E. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1997.tb01561.x · Cited by 277
S100A8 and S100A9 Induce Cytokine Expression and Regulate the NLRP3 Inflammasome via ROS-Dependent Activation of NF-κB1
Simard, J.-C., Césaro, A., Chapeton-Montes, J. A., Tardif, M. R., Antoine, F., Girard, D., & Tessier, P. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072138 · Cited by 274
Selective inhibition of protein tyrosine phosphatase activities by H2O2 and vanadate In vitro
Hecht, D., & Zick, Y. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91123-8 · Cited by 273
Inflammasome activation in nadph oxidase defective mononuclear phagocytes from patients with chronic granulomatous disease
Meissner, F., Seger, R. A., Moshous, D., Fischer, A., Reichenbach, J., & Zychlinsky, A. (2010) · Blood · doi:10.1182/blood-2010-01-264218 · Cited by 269
The multifaceted profile of activated microglia
Lynch, M. A. (2009) · Molecular Neurobiology · doi:10.1007/s12035-009-8077-9 · Cited by 268
Differential migration, LPS‐induced cytokine, chemokine, and NO expression in immortalized BV‐2 and HAPI cell lines and primary microglial cultures
Horvath, R. J., Nutile‐McMenemy, N., Alkaitis, M. S., & DeLeo, J. A. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05633.x · Cited by 264
The selective detection of mitochondrial superoxide by live cell imaging
Robinson, K. M., Janes, M. S., & Beckman, J. S. (2008) · Nature Protocols · doi:10.1038/nprot.2008.56 · Cited by 263
Sex, glia, and development: Interactions in health and disease
Schwarz, J. M., & Bilbo, S. D. (2012) · Hormones and Behavior · doi:10.1016/j.yhbeh.2012.02.018 · Cited by 247
Traumatic brain injury in aged animals increases lesion size and chronically alters microglial/macrophage classical and alternative activation states
Kumar, A., Stoica, B. A., Sabirzhanov, B., Burns, M. P., Faden, A. I., & Loane, D. J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.11.013 · Cited by 244
Importance of MAPK pathways for microglial pro-inflammatory cytokine IL-1β production
Kim, S. H., Smith, C. J., & Eldik, L. J. V. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00126-x · Cited by 241
Mitochondrial apoptosis is dispensable for NLRP3 inflammasome activation but non‐apoptotic caspase‐8 is required for inflammasome priming
Allam, R., Lawlor, K. E., Yu, E. C.-W., Mildenhall, A., Moujalled, D. M., Lewis, R. S., Ke, F., Mason, K. D., White, M. J., Stacey, K. J., et al. (2014) · EMBO Reports · doi:10.15252/embr.201438463 · Cited by 238
Inflammatory response of microglial BV‐2 cells includes a glycolytic shift and is modulated by mitochondrial glucose‐regulated protein 75/mortalin
Voloboueva, L. A., Emery, J. F., Sun, X., & Giffard, R. G. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.067 · Cited by 234
Oligomeric amyloid β induces IL-1β processing via production of ROS: implication in Alzheimer’s disease
Parajuli, B., Sonobe, Y., Horiuchi, H., Takeuchi, H., Mizuno, T., & Suzumura, A. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.503 · Cited by 232
Inhibition of NADPH oxidase promotes alternative and anti‐inflammatory microglial activation during neuroinflammation
Choi, S., Aïd, S., Kim, H., Jackson, S. H., & Bosetti, F. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07572.x · Cited by 228
Mitochondrially targeted compounds and their impact on cellular bioenergetics
Reily, C., Mitchell, T., Chacko, B. K., Benavides, G. A., Murphy, M. P., & Darley-Usmar, V. M. (2013) · Redox Biology · doi:10.1016/j.redox.2012.11.009 · Cited by 227
Interactive role of the toll‐like receptor 4 and reactive oxygen species in LPS‐induced microglia activation
Qin, L., Li, G., Qian, X., Liu, Y., Wu, X., Liu, B., Hong, J., & Block, M. L. (2005) · Glia · doi:10.1002/glia.20225 · Cited by 218
Neuronal Death Induced by Nanomolar Amyloid β Is Mediated by Primary Phagocytosis of Neurons by Microglia
Neniškytė, U., Neher, J. J., & Brown, G. C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.267583 · Cited by 215
Up-regulation of Microglial CD11b Expression by Nitric Oxide
Roy, A., Fung, Y. K., Liu, X., & Pahan, K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600236200 · Cited by 214
Critical Role of NADPH Oxidase in Neuronal Oxidative Damage and Microglia Activation following Traumatic Brain Injury
Zhang, Q.-G., Laird, M. D., Han, D., Nguyen, K., Scott, E., Dong, Y., Dhandapani, K. M., & Brann, D. W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034504 · Cited by 211
Mitochondria-targeted antioxidant MitoQ ameliorates experimental mouse colitis by suppressing NLRP3 inflammasome-mediated inflammatory cytokines
Dashdorj, A., Jyothi, K. R., Lim, S., Jo, A., Nguyen, M. N., Ha, J., Yoon, K., Kim, H. J., Park, J., Murphy, M. P., et al. (2013) · BMC Medicine · doi:10.1186/1741-7015-11-178 · Cited by 206
Microglia Proliferation Is Regulated by Hydrogen Peroxide from NADPH Oxidase
Mander, P. K., Jekabsone, A., & Brown, G. C. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.2.1046 · Cited by 206
Classical Inhibitors of NOX NAD(P)H Oxidases Are Not Specific
Aldieri, E., Riganti, C., Polimeni, M., Gazzano, E., Lussiana, C., Campia, I., & Ghigo, D. (2008) · Current Drug Metabolism · doi:10.2174/138920008786049285 · Cited by 201
Diphenyleneiodonium inhibits reduction of iron-sulfur clusters in the mitochondrial NADH-ubiquinone oxidoreductase (Complex I).
Majander, A. S., Finel, M., & Wikström, M. K. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31926-9 · Cited by 200
Microglial Scavenger Receptors and Their Roles in the Pathogenesis of Alzheimer's Disease
Wilkinson, K., & Khoury, J. B. E. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/489456 · Cited by 197
Cysteine 203 of Cyclophilin D Is Critical for Cyclophilin D Activation of the Mitochondrial Permeability Transition Pore
Nguyen, T. T. M., Stevens, M. V., Kohr, M. J., Steenbergen, C., Sack, M. N., & Murphy, E. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.243469 · Cited by 194
Activation of murine microglial cell lines by lipopolysaccharide and interferon‐γ causes NO‐mediated decreases in mitochondrial and cellular function
Moss, D. W., & Bates, T. E. (2001) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2001.01418.x · Cited by 192
Selective Vulnerability of Dopaminergic Neurons to Microtubule Depolymerization
Ren, Y., Liu, W., Jiang, H., Jiang, Q., & Feng, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503483200 · Cited by 188
Loss of mitochondrial complex I activity potentiates dopamine neuron death induced by microtubule dysfunction in a Parkinson’s disease model
Choi, W.-S., Palmiter, R. D., & Xia, Z. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201009132 · Cited by 183
Uncoupling proteins: A role in protection against reactive oxygen species—or not?
Cannon, B., Shabalina, I. G., Kramarova, T. V., Petrovic, N., & Nedergaard, J. (2006) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2006.05.016 · Cited by 182
Mitochondria contribute to LPS-induced MAPK activation via uncoupling protein UCP2 in macrophages
Emre, Y., Hurtaud, C., Nübel, T., Criscuolo, F., Ricquier, D., & Cassard, A. (2007) · Biochemical Journal · doi:10.1042/bj20061430 · Cited by 181
Microglial PHOX and Mac‐1 are essential to the enhanced dopaminergic neurodegeneration elicited by A30P and A53T mutant alpha‐synuclein
Zhang, W., Dallas, S., Zhang, D., Guo, J., Pang, H., Wilson, B. C., Miller, D. S., Chen, B., Zhang, W., McGeer, P. L., et al. (2007) · Glia · doi:10.1002/glia.20532 · Cited by 166
‘Mild Uncoupling’ does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress
Johnson-Cadwell, L. I., Jekabsons, M. B., Wang, A., Polster, B. M., & Nicholls, D. G. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04516.x · Cited by 164
Self-citation
Inflammasome activation and IL‐1β/IL‐18 processing are influenced by distinct pathways in microglia
Hanamsagar, R., Torres, V. J., & Kielian, T. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07481.x · Cited by 163
Redox/ROS regulation of lipopolysaccharide‐induced mitogen‐activated protein kinase (MAPK) activation and MAPK‐mediated TNF‐α biosynthesis
Haddad, J. J., & Land, S. C. (2002) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0704467 · Cited by 163
Mitochondrial NLRP3 Protein Induces Reactive Oxygen Species to Promote Smad Protein Signaling and Fibrosis Independent from the Inflammasome
Bracey, N. A., Gershkovich, B., Chun, J., Vilaysane, A., Meijndert, H. C., Wright, J. R., Fedak, P. W. M., Beck, P. L., Muruve, D. A., & Duff, H. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.550624 · Cited by 156
NLRP3 Inflammasome: Key Mediator of Neuroinflammation in Murine Japanese Encephalitis
Kaushik, D. K., Gupta, M., Kumawat, K. L., & Basu, A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032270 · Cited by 152
Reactive oxygen species up-regulate CD11b in microglia via nitric oxide: Implications for neurodegenerative diseases
Roy, A., Jana, A., Yatish, K., Freidt, M. B., Fung, Y. K., Martinson, J., & Pahan, K. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.026 · Cited by 139
Persistent Nuclear Factor-κB Activation in Ucp2-/- Mice Leads to Enhanced Nitric Oxide and Inflammatory Cytokine Production
Bai, Y., Onuma, H., Bai, X., Medvedev, A. V., Misukonis, M. A., Weinberg, J. B., Cao, W., Robidoux, J., Floering, L. M., Daniel, K. W., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500566200 · Cited by 137
Primary phagocytosis of viable neurons by microglia activated with LPS or Aβ is dependent on calreticulin/LRP phagocytic signalling
Fricker, M., Oliva-Martín, M. J., & Brown, G. C. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-196 · Cited by 137
Uncoupling protein 2 plays an important role in nitric oxide production of lipopolysaccharide-stimulated macrophages
Kizaki, T., Suzuki, K., Hitomi, Y., Taniguchi, N., Saitoh, D., Watanabe, K., Onoé, K., Day, N. K. B., Good, R. A., & Ohno, H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.142206299 · Cited by 136
Macrophage Antigen Complex-1 Mediates Reactive Microgliosis and Progressive Dopaminergic Neurodegeneration in the MPTP Model of Parkinson’s Disease
Hu, X., Zhang, D., Pang, H., Caudle, W. M., Li, Y., Gao, H., Liu, Y., Li, Q., Wilson, B. C., Monte, D. A. D., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.10.7194 · Cited by 128
Sulforaphane suppresses LPS-induced inflammation in primary rat microglia
Brandenburg, L., Kipp, M., Lucius, R., Pufe, T., & Wruck, C. J. (2009) · Inflammation Research · doi:10.1007/s00011-009-0116-5 · Cited by 126
Mesenchymal Stem/Stromal Cells Inhibit the NLRP3 Inflammasome by Decreasing Mitochondrial Reactive Oxygen Species
Oh, J. Y., Ko, J. H., Lee, H. J., Yu, J. M., Choi, H., Kim, M. K., Wee, W. R., & Prockop, D. J. (2014) · Stem Cells · doi:10.1002/stem.1608 · Cited by 125
Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
Lambert, A. J., Buckingham, J. A., Boysen, H. M., & Brand, M. D. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.005 · Cited by 123
Effects of mitochondrial dysfunction on the immunological properties of microglia
Ferger, A. I., Campanelli, L., Reimer, V., Muth, K. N., Merdian, I., Ludolph, A. C., & Witting, A. (2010) · Journal of Neuroinflammation · doi:10.1186/1742-2094-7-45 · Cited by 122
Activation of Metabotropic Glutamate Receptor 5 Modulates Microglial Reactivity and Neurotoxicity by Inhibiting NADPH Oxidase
Loane, D. J., Stoica, B. A., Pajoohesh‐Ganji, A., Byrnes, K. R., & Faden, A. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806139200 · Cited by 121
Inhibition of the Sur1-Trpm4 Channel Reduces Neuroinflammation and Cognitive Impairment in Subarachnoid Hemorrhage
Tosun, Ç., Kurland, D. B., Mehta, R. I., Castellani, R. J., deJong, J. L., Kwon, M. S., Woo, S. K., Gerzanich, V., & Simard, J. M. (2013) · Stroke · doi:10.1161/strokeaha.113.002904 · Cited by 121
Rotenone inhibition of tubulin self-assembly
Marshall, L. E., & Himes, R. H. (1978) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(78)90315-x · Cited by 120
Schisandrin B exerts anti-neuroinflammatory activity by inhibiting the Toll-like receptor 4-dependent MyD88/IKK/NF-κB signaling pathway in lipopolysaccharide-induced microglia
Zeng, K.-W., Zhang, T., Fu, H., Liu, G.-X., & Wang, X.-M. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.05.030 · Cited by 116
Rotenone inhibition of spindle microtubule assembly in mammalian cells
Brinkley, B. R., Barham, S. S., BARRANCO, S. C., & Fuller, G. M. (1974) · Experimental Cell Research · doi:10.1016/0014-4827(74)90210-9 · Cited by 115
The NALP3 inflammasome is involved in neurotoxic prion peptide-induced microglial activation
Shi, F., Yang, L., Kouadir, M., Yang, Y., Wang, J., Zhou, X., Yin, X., & Zhao, D. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-73 · Cited by 112
Resistance to cerebral ischemic injury in UCP2 knockout mice: evidence for a role of UCP2 as a regulator of mitochondrial glutathione levels
De Bilbao, F., Arsenijevic, D., Vallet, P., Hjelle, O. P., Ottersen, O. P., Bouras, C., Raffin, Y., Abou, K., Langhans, W., Collins, S., et al. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02432.x · Cited by 108 · cited 2×
“observed a steady-state upregulation of MnSOD in UCP2 mouse brain [107], indicating that secondary, potentially complicating changes to the proteome should be considered when using these constitutive knockout mice to assign protein function.”
MAC1 mediates LPS-induced production of superoxide by microglia: The role of pattern recognition receptors in dopaminergic neurotoxicity
Pei, Z., Pang, H., Qian, L., Yang, S., Wang, T., Zhang, W., Wu, X., Dallas, S., Wilson, B., Reece, J. M., et al. (2007) · Glia · doi:10.1002/glia.20545 · Cited by 105
Oxidative metabolism enables Salmonella evasion of the NLRP3 inflammasome
Wynosky-Dolfi, M. A., Snyder, A. G., Philip, N. H., Doonan, P. J., Poffenberger, M. C., Avizonis, D. Z., Zwack, E. E., Riblett, A. M., Hu, B., Strowig, T., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20130627 · Cited by 105
Uncoupling Protein 2 Negatively Regulates Mitochondrial Reactive Oxygen Species Generation and Induces Phosphatase-Mediated Anti-Inflammatory Response in Experimental Visceral Leishmaniasis
Ball, W. B., Kar, S., Mukherjee, M., Chande, A. G., Mukhopadhyaya, R., & Das, P. K. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1004237 · Cited by 101
Activation of mGluR5 and Inhibition of NADPH Oxidase Improves Functional Recovery after Traumatic Brain Injury
Loane, D. J., Stoica, B. A., Byrnes, K. R., Jeong, W. J., & Faden, A. I. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2012.2589 · Cited by 100
Isoorientin attenuates lipopolysaccharide-induced pro-inflammatory responses through down-regulation of ROS-related MAPK/NF-κB signaling pathway in BV-2 microglia
Li, Y., Wu, Y., Ren, X., Liu, Q., Wang, J., & Liu, X. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1854-9 · Cited by 99
Rotenone Directly Induces BV2 Cell Activation via the p38 MAPK Pathway
Gao, F., Chen, D., Hu, Q., & Wang, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072046 · Cited by 91
Mitochondria-targeted drugs enhance Nlrp3 inflammasome-dependent IL-1β secretion in association with alterations in cellular redox and energy status
Jabaut, J., Ather, J. L., Taracanova, A., Poynter, M. E., & Ckless, K. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.01.025 · Cited by 89
Peroxiredoxin I is a ROS/p38 MAPK-dependent inducible antioxidant that regulates NF-κB-mediated iNOS induction and microglial activation
Kim, S., Park, Y., Min, J., Sun, H.-N., Han, Y., Hua, J.-M., Lee, T., Lee, S., Chang, K.-T., Kang, S. W., et al. (2013) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2013.03.006 · Cited by 88
Microglial MAC1 receptor and PI3K are essential in mediating β-amyloid peptide-induced microglial activation and subsequent neurotoxicity
Zhang, D., Hu, X., Li, Q., Chen, S., Zhou, H., Wilson, B. C., Miller, D. S., & Hong, J. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-3 · Cited by 87
Iptakalim Alleviates Rotenone-Induced Degeneration of Dopaminergic Neurons through Inhibiting Microglia-Mediated Neuroinflammation
Zhou, F., Wu, J., Sun, X., Yao, H., Ding, J., & Hu, G. (2007) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301381 · Cited by 85
Naringenin more effectively inhibits inducible nitric oxide synthase and cyclooxygenase-2 expression in macrophages than in microglia
Chao, C., Weng, C.-S., Chang, N., Lin, J.-S., Kao, S.-T., & Ho, F. (2010) · Nutrition Research · doi:10.1016/j.nutres.2010.10.011 · Cited by 85
Opening of microglial KATP channels inhibits rotenone‐induced neuroinflammation
Zhou, F., Yao, H., Wu, J., Ding, J., Sun, T., & Hu, G. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2007.00144.x · Cited by 84
Purification of a Multipotent Antideath Activity from Bovine Liver and Its Identification as Arginase: Nitric Oxide-Independent Inhibition of Neuronal Apoptosis
Esch, F. S., Lin, K., Hills, A., Zaman, K., Baraban, J. M., Chatterjee, S., Rubin, L. L., Ash, D. E., & Ratan, R. R. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-11-04083.1998 · Cited by 83
Reactive oxygen species and p47phox activation are essential for the Mycobacterium tuberculosis-induced pro-inflammatory response in murine microglia
Yang, C., Lee, H., Ji-Yeon, L., Kim, J., Lee, S. J., Shin, D., Lee, Y., Lee, D., Benna, J. E., & Jo, E. (2007) · Journal of Neuroinflammation · doi:10.1186/1742-2094-4-27 · Cited by 77
Glibenclamide for the Treatment of Acute CNS Injury
Kurland, D. B., Tosun, Ç., Pampori, A., Karimy, J. K., Caffes, N. M., Gerzanich, V., & Simard, J. M. (2013) · Pharmaceuticals · doi:10.3390/ph6101287 · Cited by 73
Reactive oxygen species mediate A??(25-35)-induced activation of BV-2 microglia
Kang, J., Park, E. J., Jou, I., Kim, J., & Joe, E.-H. (2001) · Neuroreport · doi:10.1097/00001756-200105250-00030 · Cited by 68
The generation of free radicals by nitric oxide synthase
Porasuphatana, S., Tsai, P., & Rosen, G. M. (2003) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/s1532-0456(02)00271-5 · Cited by 68
Inhibiting p53 pathways in microglia attenuates microglial‐evoked neurotoxicity following exposure to Alzheimer peptides
Davenport, C. M., Sevastou, I. G., Hooper, C., & Pocock, J. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06485.x · Cited by 67
Fructose-1,6-bisphosphate preserves intracellular glutathione and protects cortical neurons against oxidative stress
Vexler, Z. S., Wong, A. L., Francisco, C., Manabat, C., Christen, S., Täuber, M. G., Ferriero, D. M., & Gregory, G. A. (2003) · Brain Research · doi:10.1016/s0006-8993(02)03777-0 · Cited by 65
Love and death: microglia, NLRP3 and the Alzheimer's brain
Goldmann, T., Tay, T. L., & Prinz, M. (2013) · Cell Research · doi:10.1038/cr.2013.24 · Cited by 63
Impact of endogenous nitric oxide on microglial cell energy metabolism and labile iron pool
Chénais, B., Morjani, H., & Drapier, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00864.x · Cited by 55
An Essential Role for Lipopolysaccharide-Binding Protein in Pulmonary Innate Immune Responses
Fan, M.-H., Klein, R. D., Steinstraesser, L., Merry, A. C., Nemzek, J. A., Remick, D. G., Wang, S. C., & Su, G. L. (2002) · Shock · doi:10.1097/00024382-200209000-00008 · Cited by 54
Rotenone activates phagocyte NADPH oxidase by binding to its membrane subunit gp91phox
Zhou, H., Zhang, F., Chen, S., Zhang, D., Wilson, B. C., Hong, J., & Gao, H. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.10.488 · Cited by 54
Rotenone and paraquat do not directly activate microglia or induce inflammatory cytokine release
Klintworth, H. M., Garden, G. A., & Xia, Z. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.06.065 · Cited by 53
Transcription factor p53 influences microglial activation phenotype
Jayadev, S., Nesser, N. K., Hopkins, S., Myers, S. J., Case, A., Lee, R. J., Seaburg, L., Uo, T., Murphy, S. P., Morrison, R. S., et al. (2011) · Glia · doi:10.1002/glia.21178 · Cited by 52
Protective effect of the SOD/catalase mimetic MnTMPyP on inflammation-mediated dopaminergic neurodegeneration in mesencephalic neuronal-glial cultures
Wang, T., Liu, B., Qin, L., Wilson, B. C., & Hong, J. (2004) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2003.10.040 · Cited by 51
Integrin Mac-1 and β-amyloid in microglial release of nitric oxide
Goodwin, J. L., Kehrli, M. E., & Uemura, E. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00653-7 · Cited by 49
Rotenone Could Activate Microglia Through NFκB Associated Pathway
Yuan, Y., Sun, J., Wu, M., Hu, J., Peng, S.-Y., & Chen, N. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1055-7 · Cited by 41
A self-propelling cycle mediated by reactive oxide species and nitric oxide exists in LPS-activated microglia
Lijia, Z., Zhao, S., Wang, X., Wu, C., & Yang, J. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.09.002 · Cited by 40
Mitochondrial density contributes to the immune response of macrophages to lipopolysaccharide via the MAPK pathway
Kasahara, E., Sekiyama, A., Hori, M., Hara, K., Takahashi, N., Konishi, M., Sato, E. F., Matsumoto, S., Okamura, H., & Inoue, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.049 · Cited by 39
Neuroprotection through Stimulation of Mitochondrial Antioxidant Protein Expression
Greco, T., & Fiskum, G. M. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100519 · Cited by 34
TNFα and IL-1β are mediated by both TLR4 and Nod1 pathways in the cultured HAPI cells stimulated by LPS
Zheng, W., Zheng, X.-X., Liu, S., Ouyang, H., Levitt, R., Candiotti, K., & Hao, S.-L. (2012) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2012.03.068 · Cited by 30
sCD14 prevents endotoxin inducible oxidative burst response of human monocytes.
Schütt, C., Schilling, T., & Krüger, C. L. (1991) · PubMed · Cited by 29
Fructose-1,6-bisphosphate attenuates induction of nitric oxide synthase in microglia stimulated with lipopolysaccharide
Kim, Y., Park, T. Y., Baik, E. C., & Lee, S. (2011) · Life Sciences · doi:10.1016/j.lfs.2011.12.011 · Cited by 25
Hydrogen peroxide enhances LPS-induced nitric oxide production via the expression of interferon beta in BV-2 microglial cells
Eguchi, H., Fujiwara, N., Sakiyama, H., Yoshihara, D., & Suzuki, K. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.02.047 · Cited by 22
Superoxide anion contributes to the induction of tumor necrosis factor alpha (TNFα) through activation of the MKK3/6-p38 MAPK cascade in rat microglia
Yoshino, Y., Yamamoto, S., Kohsaka, S., Oshiro, S., & Nakajima, K. (2011) · Brain Research · doi:10.1016/j.brainres.2011.09.009 · Cited by 9
An Introduction to CNS-Resident Microglia: Definitions, Assays, and Functional Roles in Health and Disease
Davis, D. S., & Carson, M. J. (2012) · Springer eBooks · doi:10.1007/978-1-4614-4729-0_1 · Cited by 8
Untitled work
(1999) · doi:10.1002/(sici)1097-4547(19990915)57:6

Research works printed but not linked: 2

Kumar, 2012, Neuroinflammation after traumatic brain injury: opportunities for therapeutic intervention, Brain Behav. Immun., 26, 1191, 10.1016/j.bbi.2012.06.008 · DOI · Paper page
Kurland, 2013, 6, 1287

Sorted by citations

Microglial M1/M2 polarization and metabolic states
Orihuela, R., McPherson, C. A., & Harry, G. J. (2016) · British Journal of Pharmacology · doi:10.1111/bph.13139 · Cited by 2,070
ROS Generation in Microglia: Understanding Oxidative Stress and Inflammation in Neurodegenerative Disease
Simpson, D. S. A., & Oliver, P. L. (2020) · Antioxidants · doi:10.3390/antiox9080743 · Cited by 1,044
The reactive oxygen species in macrophage polarization: reflecting its dual role in progression and treatment of human diseases
Tan, H.-Y., Wang, N., Li, S., Hong, M., Wang, X., & Feng, Y. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/2795090 · Cited by 657
Microglial cell dysregulation in brain aging and neurodegeneration
von Bernhardi, R., Eugenín-von Bernhardi, L., & Eugenín, J. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00124 · Cited by 556
NAD+ improves cognitive function and reduces neuroinflammation by ameliorating mitochondrial damage and decreasing ROS production in chronic cerebral hypoperfusion models through Sirt1/PGC-1α pathway
Zhao, Y., Zhang, J., Zheng, Y., Zhang, Y., Zhang, X. J., Wang, H., Du, Y., Guan, J., Wang, X., & Fu, J. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02250-8 · Cited by 362

See all 202

Authors: Bordt, E. A., & Polster, B. M.
Affiliations: University of Maryland, Baltimore (US)
Corresponding author: Polster, Brian M.
ORCID: Bordt, Evan A.
Polster, Brian M.
Venue: Free Radical Biology and Medicine
Publisher: Elsevier BV
Published: 2014-11
Volume: 76
Pages: 34-46
ISSN: 0891-5849 (ISSN-L)
DOI: 10.1016/j.freeradbiomed.2014.07.033
PMC: PMC4252610
OpenAlex: W1971167579
Cited by: 202
References: 163
Citations by year: 2026: 15 · 2025: 15 · 2024: 17 · 2023: 14 · 2022: 19 · 2021: 24 · 2020: 16 · 2019: 18 · 2018: 20 · 2017: 16 · 2016: 15 · 2015: 12 · 2014: 1
FWCI: 1.19
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Free Radical Biology and Medicine (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (R01 NS085165)
Topics: Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Keywords: microglial activation, reactive oxygen species, NADPH oxidase, mitochondrial reactive oxygen species, hydrogen peroxide, superoxide, M1 macrophage polarization, NLRP3 inflammasome, IL-1β, IL-18, MitoSOX, MitoTEMPO, neuroinflammation, brain injury
MeSH terms: Animals, Humans, Mitochondria, Reactive Oxygen Species, Microglia, Inflammation Mediators, NADPH Oxidases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

NADPH oxidase- and mitochondria-derived reactive oxygen species in proinflammatory microglial activation: a bipartisan affair?

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks