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Manganese Superoxide Dismutase Overexpression Attenuates MPTP Toxicity
Open accessAbstract
There is substantial evidence implicating mitochondrial dysfunction and free radical generation in the neurotoxicity of MPTP. Manganese superoxide dismutase (MnSOD) is the primary antioxidant enzyme protecting against superoxide radicals produced within mitochondria. Overexpression of human MnSOD in transgenic mice resulted in increased MnSOD localized to mitochondria in neurons and a 50% increase in total MnSOD activity in brain homogenates. We found that MPTP toxicity was significantly attenuated in the MnSOD transgenic mice which overexpress the human manganese superoxide dismutase gene, with these mice showing threefold greater dopamine levels than controls following MPTP. There were no alterations in MPP+ levels, suggesting that the effects were not due to altered metabolism of MPTP. A significant increase in 3-nitrotyrosine levels was seen in littermate controls but not in transgenic mice overexpressing human MnSOD. These results provide further evidence implicating mitochondrial dysfunction and oxidative damage in the pathogenesis of MPTP neurotoxicity.
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“the neurotoxicity of MPTP was significantly reduced in SOD2-overexpressing mice compared to wild-type mice [81]”
From Healthy Human Fecal Microbiota Transplantation into Mice Attenuates MPTP-Induced Neurotoxicity via AMPK/SOD2 Pathway (2023) · cites this paper as [81]
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Cites
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,499
Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023
Mitochondrial Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960
Keller, J. N., Kindy, M. S., Holtsberg, F. W., St. Clair, D. K., Yen, H.-C., Germeyer, A., Steiner, S. M., Bruce-Keller, A. J., Hutchins, J. B., & Mattson, M. P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-02-00687.1998 · Cited by 863
Self-citationAn assay for superoxide dismutase activity in mammalian tissue homogenates
Spitz, D. R., & Oberley, L. W. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90192-9 · Cited by 751
Human copper-containing superoxide dismutase of high molecular weight.
Marklund, S. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7634 · Cited by 749
Pathological implications of nitric oxide, superoxide and peroxynitrite formation
Beckman, J. S., & Crow, J. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210330 · Cited by 674
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Oxidative stress in neurodegeneration: Cause or consequence?
Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869
Brand, M. D. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.04.001 · Cited by 1,063
Experimental models of Parkinson's disease
Beal, M. F. (2001) · Nature reviews. Neuroscience · doi:10.1038/35072550 · Cited by 645
Self-citationWu, D., Teismann, P., Tieu, K., Vila, M., Jackson-Lewis, V. R., Ischiropoulos, H., & Przedborski, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0937239100 · Cited by 634
Neurotoxin-based models of Parkinson's disease
Bové, J., & Perier, C. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.10.057 · Cited by 534
Greenacre, S., & Ischiropoulos, H. (2001) · Free Radical Research · doi:10.1080/10715760100300471 · Cited by 500
Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications
Lei, X. G., Zhu, J., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A. R., Holmgren, A., & Arnér, E. S. J. (2015) · Physiological Reviews · doi:10.1152/physrev.00010.2014 · Cited by 455
Oxidative Stress and Genetics in the Pathogenesis of Parkinson's Disease
Zhang, Y., Dawson, V. L., & Dawson, T. M. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0319 · Cited by 408
Manganese superoxide dismutase in disease
MacMillan-Crow, L. A., & Cruthirds, D. L. (2001) · Free Radical Research · doi:10.1080/10715760100300281 · Cited by 371
Drechsel, D. A., & Patel, M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.02.008 · Cited by 314
Targeting Oxidative Stress in Central Nervous System Disorders
Patel, M. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.06.007 · Cited by 312
Mitochondrial superoxide production in kainate-induced hippocampal damage
Liang, L., Ho, Y.-S., & Patel, M. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00397-3 · Cited by 309
The Parkinsonism-inducing Drug 1-Methyl-4-phenylpyridinium Triggers Intracellular Dopamine Oxidation
Lotharius, J., & O’Malley, K. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005385200 · Cited by 306
MPTP as a Mitochondrial Neurotoxic Model of Parkinson's Disease
Przedborski, S., Tieu, K., Perier, C., & Vila, M. (2004) · Journal of Bioenergetics and Biomembranes · doi:10.1023/b:jobb.0000041771.66775.d5 · Cited by 289
ROLE of MITOCHONDRIA in TOXIC OXIDATIVE STRESS
Fariss, M. W. (2005) · Molecular Interventions · doi:10.1124/mi.5.2.7 · Cited by 295
Giasson, B. I., Ischiropoulos, H., Lee, V. M. ‐., & Trojanowski, J. Q. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00804-3 · Cited by 285
Oxidative and Antioxidative Potential of Brain Microglial Cells
Dringen, R. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1223 · Cited by 270
Neuronal Apoptosis in Neurodegeneration
Okouchi, M., Ekshyyan, O. Y., Maracine, M., & Aw, T. Y. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1511 · Cited by 222
Lee, D.-H., Kim, C., & Lee, Y. J. (2010) · Food and Chemical Toxicology · doi:10.1016/j.fct.2010.10.029 · Cited by 215
Fujita, K., Seike, T., Yutsudo, N., Ohno, M., Yamada, H., Yamaguchi, H., Sakumi, K., Yamakawa, Y., Kido, M. A., Takaki, A., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007247 · Cited by 204
Przedborski, S., & Ischiropoulos, H. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.685 · Cited by 202
Overexpression of Mn Superoxide Dismutase Does Not Increase Life Span in Mice
Jang, Y. C., Pérez, V., Song, W. J., Lustgarten, M. S., Salmon, A. B., Mele, J., Qi, W., Liu, Y., Liang, H., Chaudhuri, A. R., et al. (2009) · The Journals of Gerontology Series A · doi:10.1093/gerona/glp100 · Cited by 205
Hu, D., Serrano, F., Oury, T. D., & Klann, E. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5566-05.2006 · Cited by 187
Nitric Oxide and Reactive Oxygen Species in Parkinson's Disease
Tieu, K., Ischiropoulos, H., & Przedborski, S. (2003) · IUBMB Life · doi:10.1080/1521654032000114320 · Cited by 180
Antioxidant gene therapy against neuronal cell death
Navarro-Yepes, J., Zavala-Flores, L. M., Anandhan, A., Wang, F., Skotak, M., Chandra, N., Li, M., Pappa, A., Martínez‐Fong, D., Razo, L. M. D., et al. (2013) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2013.12.007 · Cited by 182
Qin, G., Meng, X., Wang, Q., & Tian, S. (2009) · Journal of Proteome Research · doi:10.1021/pr801046m · Cited by 167
Anandhan, A., Jacome, M. S., Lei, S., Hernández-Franco, P., Pappa, A., Panayiotidis, M. I., Powers, R., & Franco, R. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.009 · Cited by 165
Retinoic acid reduces apoptosis and oxidative stress by preservation of SOD protein level
Ahlemeyer, B., Bauerbach, E., Plath, M., Steuber, M., Heers, C., Tegtmeier, F., & Krieglstein, J. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(01)00495-6 · Cited by 162
Evaluation of animal models of Parkinson's disease for neuroprotective strategies
Emborg, M. E. (2004) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2004.08.004 · Cited by 160
Lee, J. E., Park, J. H., Shin, I. C., & Koh, H. C. (2012) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2012.06.005 · Cited by 151
Robb, E. L., Page, M. M., Wiens, B. E., & Stuart, J. A. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.138 · Cited by 147
Role of α-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice
Schlüter, O. M., Fornai, F., Alessandri, M., TAKAMORI, S., Geppert, M., Jahn, R., & Südhof, T. C. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00036-8 · Cited by 146
Giordano, S. S., Lee, J., Darley-Usmar, V. M., & Zhang, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044610 · Cited by 142
Fucoidan protects against dopaminergic neuron death in vivo and in vitro
Luo, D., Zhang, Q., Wang, H., Cui, Y., Sun, Z., Yang, J., Zheng, Y., Jia, J., Yu, F., Wang, X., et al. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.06.015 · Cited by 141
Sompol, P. M., Ittarat, W., Tangpong, J., Chen, Y., Doubinskaia, I. E., Batinic-Haberle, I., Abdul, H. M., Butterfield, D. A., & Clair, D. K. S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.044 · Cited by 137
Pong, K. (2003) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.3.1.127 · Cited by 131
Hu, D., Cao, P., Thiels, E., Chu, C. T., Wu, G., Oury, T. D., & Klann, E. (2006) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2006.10.003 · Cited by 127
Brand, M. D. (2020) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2020.1828258 · Cited by 123
Andreassen, O. A., Ferrante, R. J., Dedeoglu, A., Albers, D. W., Klivènyi, P., Carlson, E. J., Epstein, C. J., & Beal, M. F. (2001) · Experimental Neurology · doi:10.1006/exnr.2000.7525 · Cited by 114
Self-citationDietary resveratrol administration increases MnSOD expression and activity in mouse brain
Robb, E. L., Winkelmolen, L., Visanji, N. P., Brotchie, J. M., & Stuart, J. A. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.05.028 · Cited by 122
Zhang, J., Graham, D. G., Montine, T. J., & Ho, Y.-S. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.1.53 · Cited by 114
Protection of dopaminergic cells from MPP+-mediated toxicity by histone deacetylase inhibition
Kidd, S. K., & Schneider, J. S. (2010) · Brain Research · doi:10.1016/j.brainres.2010.07.041 · Cited by 113
Wearable Ultrasound Improves Motor Function in an MPTP Mouse Model of Parkinson's Disease
Zhou, H., Niu, L., Xia, X., Lin, Z., Liu, X., Su, M., Guo, R., Meng, L., & Zheng, H. (2019) · IEEE Transactions on Biomedical Engineering · doi:10.1109/tbme.2019.2899631 · Cited by 113
Salvemini, D., Muscoli, C., Riley, D. P., & Cuzzocrea, S. (2002) · Pulmonary Pharmacology & Therapeutics · doi:10.1006/pupt.2002.0374 · Cited by 105
Manganese Superoxide Dismutase Protects against 6-Hydroxydopamine Injury in Mouse Brains
Callio, J., Oury, T. D., & Chu, C. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413224200 · Cited by 103
Quijano, C., Romero, N., & Radí, R. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.04.014 · Cited by 102
Mitochondrial protein tyrosine nitration
Castro, L., Demicheli, V., Tórtora, V., & Radí, R. (2010) · Free Radical Research · doi:10.3109/10715762.2010.516254 · Cited by 101
The Use of Transgenic and Mutant Mice to Study Oxygen Free Radical Metabolism
Huang, T., Carlson, E. J., Raineri, I., Gillespie, A. M., Kozy, H. M., & Epstein, C. J. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07820.x · Cited by 101
Choi, J., Jang, E.-H., Park, C., & Kang, J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.12.008 · Cited by 98
Lee, D. W., Rajagopalan, S., Siddiq, A., Gwiazda, R. H., Yang, L., Beal, M. F., Ratan, R. R., & Andersen, J. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.000638 · Cited by 97
Self-citationSalvemini, D., & Cuzzocrea, S. (2003) · Critical Care Medicine · doi:10.1097/00003246-200301001-00005 · Cited by 96
Dang, D.-K., Shin, E., Nam, Y., Ryoo, S., Jeong, J. H., Jang, C., Nabeshima, T., Hong, J., & Kim, H. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0478-x · Cited by 94
A novel in vivo post‐translational modification of p53 by PARP‐1 in MPTP‐induced parkinsonism
Mandir, A. S., Simbulan-Rosenthal, C. M., Poitras, M. F., Lumpkin, J. R., Dawson, V. L., Smulson, M. E., & Dawson, T. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01144.x · Cited by 92
Liang, L., Huang, J., Fulton, R. E., Day, B. J., & Patel, M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0019-07.2007 · Cited by 91
Iron‐sulfur enzyme mediated mitochondrial superoxide toxicity in experimental Parkinson's disease
Liang, L., & Patel, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02567.x · Cited by 90
Pong, K., Doctrow, S. R., & Baudry, M. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02841-9 · Cited by 87
Mitochondrial Inhibition and Oxidative Stress: Reciprocating Players in Neurodegeneration
Zeevalk, G. D., Bernard, L. P., Song, C., Gluck, M. J., & Ehrhart, J. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1117 · Cited by 89
Overexpression of Mn-Containing Superoxide Dismutase in Transgenic Drosophila melanogaster
Mockett, R. J., Orr, W. C., Rahmandar, J. J., Benes, J. J., Radyuk, S. N., Klichko, V. I., & Sohal, R. S. (1999) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1999.1460 · Cited by 86
Xie, Z., Zhang, M., Luo, Y., Jin, D., Guo, X., Yang, W., Zheng, J., Zhang, H., Zhang, L., Deng, C., et al. (2023) · Aging and disease · doi:10.14336/ad.2023.0309 · Cited by 80
“Furthermore, the neurotoxicity of MPTP was significantly reduced in SOD2-overexpressing mice compared to wild-type mice [81].”
Rodríguez‐Rocha, H., García‐García, A., Pickett, C. S., Li, S., Jones, J., Chen, H., Webb, B., Choi, J. H., Zhou, Y., Zimmerman, M. C., et al. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.04.021 · Cited by 80
The Antioxidative Effect of Electro-Acupuncture in a Mouse Model of Parkinson's Disease
Wang, H., Pan, Y., Xue, B., Wang, X., Zhao, F., Jia, J., Liang, X., & Wang, X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019790 · Cited by 78
Jackson-Lewis, V. R., & Smeyne, R. J. (2005) · Neurotoxicity Research · doi:10.1007/bf03036449 · Cited by 77
Potential Mechanisms for the Inhibition of Tumor Cell Growth by Manganese Superoxide Dismutase
Kim, K.-H., Rodriguez, A. M., Carrico, P. M., & Melendez, J. A. (2001) · Antioxidants and Redox Signaling · doi:10.1089/15230860152409013 · Cited by 77
Iron overload, oxidative stress, and axonal dystrophy in brain disorders
Chiueh, C. C. (2001) · Pediatric Neurology · doi:10.1016/s0887-8994(01)00266-1 · Cited by 76
Mejı́as, R., Villadiego, J., Pintado, C. O., Vime, P. J., Gao, L., Toledo‐Aral, J. J., Echevarrı́a, M., & López‐Barneo, J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.0122-06.2006 · Cited by 74
Superoxide Radical Dismutation as New Therapeutic Strategy in Parkinson’s Disease
Lazzari, F. D., Bubacco, L., Whitworth, A. J., & Bisaglia, M. (2018) · Aging and Disease · doi:10.14336/ad.2017.1018 · Cited by 66
Mitochondrial kinases in Parkinson’s disease: Converging insights from neurotoxin and genetic models
Dagda, R. K., Zhu, J., & Chu, C. T. (2009) · Mitochondrion · doi:10.1016/j.mito.2009.06.001 · Cited by 64
Chiueh, C., Andoh, T., & Chock, P. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1338.034 · Cited by 67
Schwarting, R. K. W., Sedelis, M., Hofele, K., Auburger, G. W. J., & Huston, J. P. (1999) · Neurotoxicity Research · doi:10.1007/bf03033338 · Cited by 57
Quantitative Proteomics of a Presymptomatic A53T α-Synuclein Drosophila Model of Parkinson Disease
Xun, Z., Sowell, R. A., Kaufman, T. C., & Clemmer, D. E. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700467-mcp200 · Cited by 57
Neuroprotective Role of Atractylenolide-I in an In Vitro and In Vivo Model of Parkinson’s Disease
More, S. V., & Choi, D. (2017) · Nutrients · doi:10.3390/nu9050451 · Cited by 56
Methamphetamine toxicity is attenuated in mice that overexpress human manganese superoxide dismutase
Maragos, W. F., Jakel, R. J., Chesnut, D., Pocernich, C. B., Butterfield, D. A., Clair, D. K. S., & Cass, W. A. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02707-4 · Cited by 52
trans-Resveratrol as A Neuroprotectant
Robb, E. L., & Stuart, J. A. (2010) · Molecules · doi:10.3390/molecules15031196 · Cited by 52
Lee, J. G., Yon, J., Lin, C., Jung, A., Jung, K. Y., & Nam, S.-Y. (2012) · Food and Chemical Toxicology · doi:10.1016/j.fct.2012.08.040 · Cited by 51
Tangpong, J., Sompol, P. M., Vore, M. E., Clair, W. H. S., Butterfield, D. A., & Clair, D. K. S. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.046 · Cited by 50
NF-kappaB-associated MnSOD induction protects against beta-amyloid-induced neuronal apoptosis.
Sompol, P. M., Xu, Y., Ittarat, W., Daosukho, C., & Clair, D. K. S. (2006) · PubMed · doi:10.1385/jmn:29:3:279 · Cited by 49
A novel azulenyl nitrone antioxidant protects against MPTP and 3-nitropropionic acid neurotoxicities
Yang, L., Calingasan, N. Y., Chen, J., Ley, J. J., Becker, D. A., & Beal, M. F. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.07.012 · Cited by 46
Self-citationEffects of selegiline on antioxidant systems in the nigrostriatum in rat
Takahata, K., Shimazu, S., Katsuki, H., Yoneda, F., & AKAIKE, A. (2005) · Journal of Neural Transmission · doi:10.1007/s00702-005-0309-1 · Cited by 45
Kim, A., Joseph, S., Khan, A., Epstein, C. J., Sobel, R. A., & Huang, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.02.028 · Cited by 44
MAZZIO, E. A., Close, F. T., & Soliman, K. F. A. (2011) · International Journal of Molecular Sciences · doi:10.3390/ijms12010506 · Cited by 41
Nakai, M., Mori, A., Watanabe, A., & Mitsumoto, Y. (2002) · Experimental Neurology · doi:10.1006/exnr.2002.8056 · Cited by 39
Expression and activity of antioxidants in the brain in progressive supranuclear palsy
Cantuti‐Castelvetri, I., Keller-McGandy, C. E., Albers, D. S., Beal, M. F., Vonsattel, J., Standaert, D. G., & Augood, S. J. (2002) · Brain Research · doi:10.1016/s0006-8993(02)02244-8 · Cited by 39
Self-citationJia, Z., Misra, B. R., Zhu, H., Li, Y., & Misra, H. P. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.11.007 · Cited by 38
Yune, T. Y., Lee, S. M., Kim, S. J., Park, H. K., Oh, Y. J., Kim, Y. C., Markelonis, G. J., & Oh, T. H. (2004) · Journal of Neurotrauma · doi:10.1089/neu.2004.21.1778 · Cited by 37
Leak, R. K., Liou, A. K. F., & Zigmond, M. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04149.x · Cited by 36
Wang, J., Liu, H., Jin, W., Zhang, H., & Zhang, Q. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.10.042 · Cited by 34
Tripanichkul, W., Sripanichkulchai, K., Duce, J. A., & Finkelstein, D. I. (2007) · Brain Research · doi:10.1016/j.brainres.2007.05.076 · Cited by 32
Demicheli, V., Moreno, D. M., & Radí, R. (2018) · Metallomics · doi:10.1039/c7mt00348j · Cited by 31
Kawajiri, S., Machida, Y., Saiki, S., Sato, S., & Hattori, N. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.06.058 · Cited by 29
Strategies for the protection of dopaminergic neurons against neurotoxicity
Gerlach, M., Double, K. L., Youdim, M. B. H., & Riederer, P. (2000) · Neurotoxicity Research · doi:10.1007/bf03033788 · Cited by 29
Barkats, M., Horellou, P., Colin, P., Millecamps, S., Biguet, N. F., & Mallet, J. J. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20696 · Cited by 28
Franco, J. L., Prediger, R. D., Pandolfo, P., Takahashi, R. N., Farina, M., & Dafré, A. L. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.02.021 · Cited by 28
Zonisamide up-regulated the mRNAs encoding astrocytic anti-oxidative and neurotrophic factors
Choudhury, M., Sugimoto, K., Kubo, M., Iwaki, H., Tsujii, T., Kyaw, W. T., Nishikawa, N., Nagai, M., Tanaka, J., & Nomoto, M. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.05.012 · Cited by 27
Ponzoni, S., Guimarães, F. S., Bel, E. A. D., & Garcia‐Cairasco, N. (2000) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/s0278-5846(99)00090-1 · Cited by 26
Lithium and oxidative stress lessons from the MPTP model of Parkinson's disease
Arraf, Z., Amit, T., Youdim, M. B. H., & Farah, R. (2012) · Neuroscience Letters · doi:10.1016/j.neulet.2012.03.055 · Cited by 25
Role of nitroso radicals as drug targets in circulatory shock
Esposito, E., & Cuzzocrea, S. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00255.x · Cited by 22
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Metadata
- Authors
- Klivenyi, P., St. Clair, D., Wermer, M., Yen, H.-C., Oberley, T., Yang, L., & Beal, M. F.
- Affiliations
- Harvard University (US)
- University of Kentucky (US)
- University of Wisconsin–Madison (US)
- Venue
- Neurobiology of Disease
- Publisher
- Elsevier BV
- Published
- 1998-10
- Volume
- 5
- Issue
- 4
- Pages
- 253-258
- ISSN
- 0969-9961 (ISSN-L)
- OpenAlex
- W2009842580
- Cited by
- 142
- References
- 25
- Citations by year
- 2024: 3 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 6
- FWCI
- 5.93
- Type
- journal article
- Language
- en
- Open access
- green
- doaj.org
- Licence
- Locations
- Neurobiology of Disease (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (5r01ns032365-03, 5p01ns031579-05)
- National Cancer Institute (CA49797)
- National Institute of Neurological Disorders and Stroke (NS31579, NS32365)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- manganese superoxide dismutase, MPTP-induced neurotoxicity, Parkinson's disease, mitochondrial dysfunction, oxidative stress, superoxide, dopamine levels, MPP+, nitrotyrosine, neuroprotection, transgenic mice, antioxidant enzymes
- MeSH terms
- Animals, Brain, Brain Diseases, Cerebral Cortex, Dopamine, Humans, Mice, Transgenic, Mitochondria, Neurons, Superoxide Dismutase, 3,4-Dihydroxyphenylacetic Acid, Dopamine Agents, 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine, 1-Methyl-4-phenylpyridinium, Gene Expression, Microscopy, Immunoelectron, Transgenes, Mice
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