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Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
Abstract
Superoxide dismutases are an ubiquitous family of enzymes that function to efficiently catalyze the dismutation of superoxide anions. Three unique and highly compartmentalized mammalian superoxide dismutases have been biochemically and molecularly characterized to date. SOD1, or CuZn-SOD (EC 1.15.1.1), was the first enzyme to be characterized and is a copper and zinc-containing homodimer that is found almost exclusively in intracellular cytoplasmic spaces. SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. SOD3, or EC-SOD (EC 1.15.1.1), is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. What role(s) these SODs play in both normal and disease states is only slowly beginning to be understood. A molecular understanding of each of these genes has proven useful toward the deciphering of their biological roles. For example, a variety of single amino acid mutations in SOD1 have been linked to familial amyotrophic lateral sclerosis. Knocking out the SOD2 gene in mice results in a lethal cardiomyopathy. A single amino acid mutation in human SOD3 is associated with 10 to 30-fold increases in serum SOD3 levels. As more information is obtained, further insights will be gained.
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“This enzyme catalyzes the dismutation of superoxide anion radical very effectively by a “Ping Pong” mechanism with remarkably high reaction rates according to the reaction (Zelko et al. 2002)12”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Zelko et al. 2002
In the citing paper
“There are three main forms of superoxide dismutase present in humans, Cu, Zn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) (Zelko et al. 2002).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as Zelko et al. 2002
Citations
Cites
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Motor Neuron Degeneration in Mice that Express a Human Cu,Zn Superoxide Dismutase Mutation
Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y., Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H.-X., et al. (1994) · Science · doi:10.1126/science.8209258 · Cited by 4,143
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Roizen, N., & Patterson, D. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12987-x · Cited by 1,386
Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters
Fridovich, I. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18515 · Cited by 1,337
Reaume, A. G., Elliott, J. L., Hoffman, E. K., Kowall, N. W., Ferrante, R. J., Siwek, D. F., Wilcox, H. M., Flood, D. G., Beal, M. F., Brown, R. H., et al. (1996) · Nature Genetics · doi:10.1038/ng0596-43 · Cited by 1,285
Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1
Bruijn, L. I., Houseweart, M. K., Kato, S., Anderson, K. L., Anderson, S., Ohama, E., Reaume, A. G., Scott, R. W., & Cleveland, D. W. (1998) · Science · doi:10.1126/science.281.5384.1851 · Cited by 1,250
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
Role of superoxide dismutase in cancer: a review.
Oberley, L. W., & Buettner, G. R. (1979) · PubMed · Cited by 982
Fridovich, I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83102-7 · Cited by 970
Research works printed but not linked: 3
- Oberley, 1979, Role of superoxide dismutase in cancer, Cancer Res., 39, 1141
- Clerch, 1992, Rat lung antioxidant enzymes, Am. J. Physiol., 263, L466
- Warner, 1991, Tumor necrosis factor-alpha increases Mn-SOD expression, Am. J. Physiol., 260, L296
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Brady, P., Elizur, A., Williams, R. R., Cummins, S. F., & Knibb, W. (2012) · International Journal of Biological Sciences · doi:10.7150/ijbs.3517 · Cited by 24
Sowrirajan, B., Saito, Y., Poudyal, D., Chen, Q., Sui, H., Ravin, S. S. D., Imamichi, H., Sato, T., Kuhns, D. B., Noguchi, N., et al. (2017) · Scientific Reports · doi:10.1038/srep43441 · Cited by 24
PARK, W. H. (2013) · Oncology Letters · doi:10.3892/ol.2013.1216 · Cited by 23
Saad, M. I., Abdelkhalek, T. M., Haiba, M. M., Saleh, M. M., Hanafi, M. Y., Tawfik, S. H., & Kamel, M. A. E.-N. (2015) · Journal of Endocrinological Investigation · doi:10.1007/s40618-015-0413-5 · Cited by 23
Wen, Z., Ma, L., Xiang, X., Tang, Z., Guan, R., & Qu, Y. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.01.191 · Cited by 23
Gerstenberg, M. K., Nilsson, C., Nielsen, M. O., Grove, K. L., & Raun, K. (2018) · Nutrition and Diabetes · doi:10.1038/s41387-018-0051-z · Cited by 23
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Graça, V. C., Ferreira, I. C. F. R., & Santos, P. F. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200114110323 · Cited by 23
Rodrigues, W. D. S., Pereira, Y. C., de Souza, A. L. M., Batista, B. L., & Lobato, A. K. D. S. (2020) · Journal of Plant Growth Regulation · doi:10.1007/s00344-020-10091-7 · Cited by 24
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Li, C. V., Fan, Y., Li, S., Zhou, X., Park, K., Zhao, X., & Liu, H. (2021) · Frontiers in Nutrition · doi:10.3389/fnut.2021.667643 · Cited by 23
Dileep, N., Pradhan, C., Peter, N., Kaippilly, D., Sashidharan, A., & Sankar, T. V. (2021) · Tropical Animal Health and Production · doi:10.1007/s11250-021-02855-4 · Cited by 23
Burgos-Aceves, M. A., Migliaccio, V., Lepretti, M., Paolella, G., Gregorio, I. D., Penna, S., Faggio, C., & Lionetti, L. (2021) · Toxics · doi:10.3390/toxics9110270 · Cited by 23
Proteomic and Genomic Studies of Micronutrient Deficiency and Toxicity in Plants
Prusty, S., Sahoo, R. K., Nayak, S., Poosapati, S., & Swain, D. M. (2022) · Plants · doi:10.3390/plants11182424 · Cited by 23
Ojo, O. A., Grant, S., Amanze, J. C., Oni, A. I., Ojo, A. B., Elebiyo, T. C., Obafemi, T. O., Ayokunle, D. I., & Ogunlakin, A. D. (2022) · PLoS ONE · doi:10.1371/journal.pone.0276984 · Cited by 28
Orzołek, A., Wysocki, P., Strzeżek, J., & Kordan, W. (2013) · Reproductive Biology · doi:10.1016/j.repbio.2013.01.176 · Cited by 23
Santovito, G., Cassini, A., & Piccinni, E. (2006) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.04.007 · Cited by 24
Nolan, L. S., Cadge, B., Gómez-Dorado, M., & Dawson, S. (2013) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2013.02.009 · Cited by 20
Cárdenas, L., Sánchez, R., Gomez, D., Fuenzalida, G., Gallardo‐Escárate, C., & Tanguy, A. (2011) · Marine Genomics · doi:10.1016/j.margen.2011.05.002 · Cited by 23
Zhang, Y., Hu, Z., Xu, G., Gao, C., Wu, R., & Zou, H. (2014) · Nano Research · doi:10.1007/s12274-014-0473-4 · Cited by 23
Gene expression analysis of oxidative stress and apoptosis in proton-irradiated rat retina.
Mao, X. W., Green, L. M., Mekonnen, T., Lindsey, N., & Gridley, D. S. (2010) · PubMed · Cited by 23
Unraveling the venom components of an encyrtid endoparasitoid wasp Diversinervus elegans
Liu, N., Wang, J., Zhang, Z.-B., Huang, J.-M., & Zhu, J. (2017) · Toxicon · doi:10.1016/j.toxicon.2017.06.011 · Cited by 21
Nazari, M., Zarinkamar, F., & Niknam, V. (2017) · Environmental Science and Pollution Research · doi:10.1007/s11356-017-0889-y · Cited by 23
Gu, M., Liu, C., Wan, X., Yang, T., Chen, Y., Zhou, J., Chen, Q., & Wang, Z. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/1393641 · Cited by 23
Cheng, Y., Xu, Q., Chen, Y., Su, Y., Wen, C., & Zhou, Y. (2018) · Toxins · doi:10.3390/toxins10110482 · Cited by 23
Xie, L., Zhang, Y., Qu, Y., Chai, L., Li, X., & Wang, H. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.06.177 · Cited by 23
Wang, L., Zhou, Y., Qin, Y., Wang, Y., Liu, B., Fang, R., & Bai, M. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10625 · Cited by 23
Association between SOD2 V16A variant and urological cancer risk
Zhang, L., Xu, K., Tang, B., Zhang, W., Yuan, W., Yue, C., Shi, L., Mi, Y., Zuo, L., & Zhu, L.-J. (2020) · Aging · doi:10.18632/aging.102658 · Cited by 23
Gusti, A. M. T., Qusti, S. Y., Bahijri, S., Toraih, E. A., Bokhari, S., Attallah, S. M., Alzahrani, A., Alshehri, W. M., Alotaibi, H., & Fawzy, M. S. (2021) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s300525 · Cited by 24
Current Trends in the Pharmacotherapy of Cataracts
Heruye, S., N., L. N. M., Singh, N. U., Yalzadeh, D., Ngele, K. K., Mbye, Y. F. N., Ohia, S. E., & Opere, C. A. (2020) · Vide Leaf, Hyderabad eBooks · doi:10.37247/up.1.2020.4 · Cited by 23
Yokoe, H., Nomura, H., Yamano, Y., Fushimi, K., Sakamoto, Y., Ogawara, K., Shiiba, M., Bukawa, H., Uzawa, K., Takiguchi, Y., et al. (2009) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-009-0610-8 · Cited by 23
Cockell, K. A., Wotherspoon, A. T. L., Belonje, B., Fritz, M. E., Madère, R., Hidiroglou, N., Plouffe, L. J., Ratnayake, W. M. N., & Kubow, S. J. (2005) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2005.04.003 · Cited by 22
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Ookawara, T., Eguchi, H., Nishimura, M., Kizaki, T., Takayama, E., Saitoh, D., Ohno, H., & Suzuki, K. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00441-8 · Cited by 23
Ding, L., Zhang, S., Li, Y., Li, Y., Liu, X., Xu, D., Zhao, K., Xu, C., Yu, B., Huang, X., et al. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.150177 · Cited by 22
Moradi, Z., Haghjou, M. M., Zarei, M., & Sharifan, H. (2024) · Algal Research · doi:10.1016/j.algal.2024.103660 · Cited by 23
Won, E., Ra, K., Kim, K.-T., Lee, J., & Lee, Y.-M. (2014) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2014.03.026 · Cited by 22
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Messner, D. J., Murray, K. F., & Kowdley, K. V. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00055-5 · Cited by 24
Lau, Y.-T., Santos, B., Barbosa, M., Espinosa, E. P., & Allam, B. (2018) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.09.006 · Cited by 21
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Chang, H.-Y., Lin, T., Anraku, K., & Shao, Y. T. (2018) · PubMed Central · doi:10.6620/zs.2018.57-59 · Cited by 22
Yoon, H., Kim, H.-C., & Kim, S. (2021) · Journal of Environmental Management · doi:10.1016/j.jenvman.2021.113515 · Cited by 22
Xu, Z., Yang, Y., Babu, V. S., Chen, J., Li, F., Yang, M., Li, N., Li, J., Lin, L., & Qin, Z. (2021) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2021.10.001 · Cited by 22
Rehman, S., Rashid, A., Manzoor, M. A., Li, L., Sun, W., Riaz, M. W., Li, D., & Zhuge, Q. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2021.784878 · Cited by 22
Guglielmi, V., Cheli, M., Tonin, P., & Vattemi, G. N. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052742 · Cited by 21
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He, J., Chi, C., & Liu, H. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.06.010 · Cited by 22
Xu, H., Ma, H., Hu, B., Lowrie, D. B., Fan, X., & Wen, C. (2010) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2010.06.013 · Cited by 22
Wu, M., Shariat‐Madar, B., Haron, M. H., Wu, M., Khan, I. A., & Dasmahapatra, A. K. (2010) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2010.10.002 · Cited by 22
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Xu, L., Zhang, H., Yue, H., Wu, S., Yang, H., Wang, Z., & Qi, G. (2018) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-018-0252-2 · Cited by 22
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Feng, Y., Liao, C.-Y., Xia, W.-K., Jiang, X., Shang, F., Yuan, G., & Wang, J. (2015) · Experimental and Applied Acarology · doi:10.1007/s10493-015-9930-3 · Cited by 22
Chaudhuri, L., Sarsour, E. H., Kalen, A. L., Aykin‐Burns, N., Spitz, D. R., & Goswami, P. C. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.012 · Cited by 22
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Kim, S.-J., Kim, T. S., Kim, I. Y., Hong, S., Rhim, H., & Kang, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01241-5 · Cited by 22
Gross, J., Machulik, A., Amarjargal, N., Moller, R., Ungethüm, U., Kuban, R., Fuchs, F.-U., Andreeva, N., Fuchs, J., Henke, W., et al. (2007) · Brain Research · doi:10.1016/j.brainres.2007.05.061 · Cited by 22
Managing odds in stem cells: insights into the role of mitochondrial antioxidant enzyme MnSOD
Sheshadri, P., & Kumar, A. (2016) · Free Radical Research · doi:10.3109/10715762.2016.1155708 · Cited by 21
Zhao, J., Jin, H., Gao, J., Pu, C., Zhāng, P., Huang, J., Cheng, L., & Feng, G. L. (2018) · Disease Markers · doi:10.1155/2018/8721379 · Cited by 21
Ojo, O. A., Osukoya, O. A., Ekakitie, L. I., Ajiboye, B. O., Oyinloye, B. E., Agboinghale, P. E., & Kappo, A. P. (2020) · Journal of Diabetes & Metabolic Disorders · doi:10.1007/s40200-020-00533-0 · Cited by 21
Rost-Roszkowska, M. M., Poprawa, I., Chajec, Ł., Chachulska-Żymełka, A., Wilczek, G., Wilczek, P., Tarnawska, M., Student, S., & Leśniewska, M. (2021) · The European Zoological Journal · doi:10.1080/24750263.2021.1912199 · Cited by 20
Boeing, T., Speca, S., de Souza, P., Mena, A. M., Bertin, B., Desreumax, P., da Silva, L. M., de Andrade, S. F., & Dubuquoy, L. (2021) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2021.109712 · Cited by 21
Chanaj-Kaczmarek, J., Wysocki, M. P., Karachitos, A., Wojcińska, M., Bartosz, G., Matławska, I., & Kmita, H. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.04.046 · Cited by 21
Xu, Y., Zeng, Q., Sun, B., Wei, S., Wang, Q., & Zhang, A. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/9865606 · Cited by 21
RetractedYu, H., Ge, X., Zhang, L., Chen, X., Ren, M., & Liang, H. (2023) · Aquaculture · doi:10.1016/j.aquaculture.2023.739441 · Cited by 21
Zhang, H., Dai, J., Cai, M., Cheng, K.-M., Hu, Y., & Luo, Z. (2023) · Aquaculture Reports · doi:10.1016/j.aqrep.2023.101639 · Cited by 21
Arcone, R., D’Errico, A., Nasso, R., Rullo, R., Poli, A., Donato, P. D., & Masullo, M. (2023) · Molecules · doi:10.3390/molecules28176332 · Cited by 22
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von Knethen, A., Neb, H., Morbitzer, V., Schmidt, M. V., Kühn, A., Kuchler, L., & Brüne, B. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.04.033 · Cited by 22
Park, W. H. (2014) · Oncology Reports · doi:10.3892/or.2014.3084 · Cited by 21
Kim, E., Kim, E. J., Seo, S.-W., Hur, C., McGregor, R. A., & Choi, M. (2013) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.619283 · Cited by 22
Lapointe, J. (2014) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.12160 · Cited by 21
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Husain, N., & Kumar, A. (2012) · Cited by 21
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Roy, C., Lavoie, M., Richard, G., Archambault, A., & Lapointe, J. (2016) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.12462 · Cited by 21
Duan, Y., Zhou, M., Xiao, J. R., Wu, C., Zhou, L., Zhou, F., Du, C., & Song, Y. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2761 · Cited by 21
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Deska, M., Romuk, E. B., Segiet, O. A., Buła, G., Truchanowski, W., Stolecka, D., Birkner, E., & Gawrychowski, J. (2016) · European surgery. Supplement/European surgery · doi:10.1007/s10353-016-0457-6 · Cited by 21
Kolarzyk, E., Pietrzycka, A., Zając, J., & Morawiecka-Baranek, J. (2017) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/61834 · Cited by 20
Morales‐Prieto, N., & Abril, N. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.08.057 · Cited by 24
Tamaoki, M., Komatsuzaki, R., Komatsu, M., Minashi, K., Aoyagi, K., Nishimura, T., Chiwaki, F., Hiroki, T., Daiko, H., Morishita, K., et al. (2018) · Cancer Science · doi:10.1111/cas.13531 · Cited by 21
Production of functional human CuZn-SOD and EC-SOD in bitransgenic cloned goat milk
Lü, R., Zhang, T., Wu, D., He, Z., Jiang, L., Zhou, M., & Cheng, Y. (2018) · Transgenic Research · doi:10.1007/s11248-018-0080-3 · Cited by 20
Giudice, A., Barbieri, A., Bimonte, S., Cascella, M., Cuomo, A., Crispo, A., D'Arena, G. F., Galdiero, M., Pepa, M. E. D., Botti, G., et al. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s183192 · Cited by 21
Sasaki, T., Abe, Y., Takayama, M., Adachi, T., Okano, H., Hirose, N., & Arai, Y. (2021) · Scientific Reports · doi:10.1038/s41598-021-87982-6 · Cited by 21
Molecular structure and organization of the wheat genomic manganese superoxide dismutase gene
Baek, K.-H., Skinner, D. Z., Peng, L., & Chen, X. (2006) · Genome · doi:10.1139/g05-102 · Cited by 21
Ihnat, M. A., Kaltreider, R. C., Thorpe, J. E., Green, D. E., Kamat, C. D., Leeper, M., Shanner, A. C., Warnke, L. A., Piconi, L., & Ceriello, A. (2007) · American journal of biochemistry & biotechnology/American journal of biochemistry and biotechnology · doi:10.3844/ajbbsp.2007.16.23 · Cited by 21
Ourique, F., Kviecinski, M. R., Zirbel, G., Castro, L. S. E. P. W., Castro, A. J. G., Silva, F. R. M. B., Valderrama, J. A., Ríos, D., Benites, J. F., Calderón, P. B., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.06.113 · Cited by 21
RetractedDentofacial Parameters Explaining Variability in Retroclination of the Maxillary Central Incisors
Lapatki, B. G., Klatt, A., Schulte‐Mönting, J., & Jonas, I. E. (2007) · Journal of Orofacial Orthopedics / Fortschritte der Kieferorthopädie · doi:10.1007/s00056-007-0637-x · Cited by 21
Effects of salinity on the clam Chamelea gallina haemocytes. Part II: Superoxide dismutase response
Monari, M., Serrazanetti, G. P., Foschi, J., Matozzo, V., Marin, M. G., & Cattani, O. (2006) · Marine Biology · doi:10.1007/s00227-006-0544-5 · Cited by 21
Park, J. W., Qi, W., Liu, J. Q., Urbaniak, J. R., Folz, R. J., & Chen, L. (2005) · Microsurgery · doi:10.1002/micr.20175 · Cited by 21
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Metadata
- Authors
- Zelko, I. N., Mariani, T. J., & Folz, R. J.
- Affiliations
- Duke University (US)
- Brigham and Women's Hospital (US)
- Corresponding author
- Folz, Rodney J
- Venue
- Free Radical Biology and Medicine
- Publisher
- Elsevier BV
- Published
- 2002-08
- Volume
- 33
- Issue
- 3
- Pages
- 337-349
- ISSN
- 0891-5849 (ISSN-L)
- OpenAlex
- W2104109524
- Cited by
- 2,212
- References
- 162
- Citations by year
- 2026: 77 · 2025: 123 · 2024: 119 · 2023: 109 · 2022: 131 · 2021: 140 · 2020: 117 · 2019: 130 · 2018: 134 · 2017: 133 · 2016: 124 · 2015: 93 · 2014: 103 · 2013: 99 · 2012: 104
- FWCI
- 12.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Free Radical Biology and Medicine (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01hl055166-04)
- National Heart, Lung, and Blood Institute (HL55166, P01HL031992, HL 31992)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- superoxide dismutase, SOD1, manganese superoxide dismutase, SOD3, gene structure, gene evolution, gene expression, SOD1 mutations, amyotrophic lateral sclerosis, superoxide dismutase isoforms
- MeSH terms
- Animals, Multigene Family, Humans, Superoxide Dismutase, Gene Expression Regulation, Enzymologic, Evolution, Molecular
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