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Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
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“Thus, in some assays, Oz reduces tetranitro methane [11], cytochrome c or nitro tetrazolium blue [100], and in others it oxidises epinephrine, tiron pyrogallol or 6-hydroxydopamine [101,102], Figure 38.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [100]
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DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *
Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citationThe Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,196
Self-citationA Mechanism for the Production of Ethylene from Methional
Beauchamp, C., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62842-x · Cited by 667
Self-citationSuperoxide Dismutase from Escherichia coli B
Keele, B. B., McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62675-4 · Cited by 559
Self-citationThe Utility of Superoxide Dismutase in Studying Free Radical Reactions
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63505-7 · Cited by 559
Self-citationMassey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., & Sullivan, P. A. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90287-3 · Cited by 426
The Utility of Superoxide Dismutase in Studying Free Radical Reactions
McCord, J. M., & Fridovich, I. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63246-6 · Cited by 387
Self-citationBallou, D. P., Palmer, G., & Massey, V. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90288-5 · Cited by 223
Further Characterization of Bovine Superoxide Dismutase and Its Isolation from Bovine Heart
Keele, B. B., McCord, J. M., & Fridovich, I. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62263-x · Cited by 203
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Research works printed but not linked: 2
- McCord, 1971, 68, 1024
- Brewer, 1967, Amer. J. Hum. Genet, 19, 674
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Hollensworth, S. B., Shen, C.-C., Sim, J. E., Spitz, D. R., Wilson, G. L., & LeDoux, S. P. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00214-8 · Cited by 195
Free-Radical Intermediates in the Metabolism of Toxic Chemicals
Mason, R. P. (1982) · Elsevier eBooks · doi:10.1016/b978-0-12-566505-6.50013-2 · Cited by 193
Jin, Q., Zhu, K., Cui, W., Xie, Y., Han, B., & Shen, W. (2012) · Plant Cell & Environment · doi:10.1111/pce.12029 · Cited by 192
Singh, B., Sharma, S., & Dhiman, A. (2013) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2013.09.028 · Cited by 192
Antioxidant systems in sunflower (Helianthus annuus L.) seeds as affected by priming
Bailly, C., Benamar, A., Corbineau, F., & Côme, D. (2000) · Seed Science Research · doi:10.1017/s0960258500000040 · Cited by 192
Gidalevitz, T., Krupinski, T., Garcia, S. M. D. A., & Morimoto, R. I. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000399 · Cited by 197
Siddaiah, C. N., Prashanth, K. H., Satyanarayana, N. R., Mudili, V., Gupta, V. K., Kalagatur, N. K., Satyavati, T., Dai, X.-F., Chen, J.-Y., Mocan, A., et al. (2018) · Scientific Reports · doi:10.1038/s41598-017-19016-z · Cited by 192
Pangeni, R., Sharma, S., Mustafa, G., Ali, J., & Baboota, S. (2014) · Nanotechnology · doi:10.1088/0957-4484/25/48/485102 · Cited by 192
Sekmen, A. H., Ozgur, R., Uzilday, B., & Türkan, İ. (2013) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2013.11.010 · Cited by 192
Effects of benzoic and cinnamic acids on membrane permeability of soybean roots
Baziramakenga, R., Leroux, G. D., & Simard, R. R. (1995) · Journal of Chemical Ecology · doi:10.1007/bf02027561 · Cited by 191
Physiological and biochemical responses of three Veneridae clams exposed to salinity changes
Carregosa, V., Velez, C., Soares, A. M. V. M., Figueira, E. M. D. A. P., & Freitas, R. (2014) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2014.08.001 · Cited by 191
Chang, C., Ślesak, I., Jordá, L., Sotnikov, A., Melzer, M., Miszalski, Z., Mullineaux, P. M., Parker, J. E., Karpińska, B., & Karpiński, S. M. (2009) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.135566 · Cited by 191
Kim, S. Y., Lim, J.-H., Park, M. R., Kim, Y.-J., Park, T. I., Seo, Y.-W., Choi, K.-G., & Yun, S.-J. (2005) · BMB Reports · doi:10.5483/bmbrep.2005.38.2.218 · Cited by 191
Gomez, J. M. (2003) · Journal of Experimental Botany · doi:10.1093/jxb/erh013 · Cited by 191
Compan, I., & Touati, D. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.6.1687-1696.1993 · Cited by 189
Lenda, D. M., Sauls, B. A., & Boegehold, M. A. (2000) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2000.279.1.h7 · Cited by 191
The regulation and role of the periplasmic copper, zinc superoxide dismutase of Escherichia coli
Gort, A. S., Ferber, D. M., & Imlay, J. A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01343.x · Cited by 191
Ecotoxicological effects of aluminum and zinc on growth and antioxidants in Lemna minor L.
Brkanac, S. R., Babić, M., Škobić, D., Roje, V., & Pevalek‐Kozlina, B. (2009) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2009.10.014 · Cited by 190
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Lambou, K., Lamarre, C., Beau, R., Dufour, N., & Latge, J. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.07024.x · Cited by 188
Antioxidative defense to lead stress in subcellular compartments of pea root cells.
Małecka, A., Jarmuszkiewicz, W., & Tomaszewska, B. (2001) · Acta Biochimica Polonica · doi:10.18388/abp.2001_3903 · Cited by 188
Wu, G. L., Cui, J., Tao, L., & Yang, H. (2009) · Ecotoxicology · doi:10.1007/s10646-009-0396-0 · Cited by 188
Ajmal, G., Bonde, G. V., Mittal, P., Khan, G., Pandey, V. K., Bakade, B. V., & Mishra, B. (2019) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2019.118480 · Cited by 191
Perl‐Treves, R., & Galun, E. (1991) · Plant Molecular Biology · doi:10.1007/bf00037058 · Cited by 188
Gallagher, K. P., Buda, A. J., Pace, D. P., Gerren, R. A., & Shlafer, M. (1986) · Circulation · doi:10.1161/01.cir.73.5.1065 · Cited by 188
Siddhuraju, P. (2006) · Food Chemistry · doi:10.1016/j.foodchem.2005.07.029 · Cited by 186
Magnesium deficiency induced oxidative stress and antioxidant responses in mulberry plants
Tewari, R. K., Kumar, P., & Sharma, P. N. (2006) · Scientia Horticulturae · doi:10.1016/j.scienta.2005.12.006 · Cited by 190
Clements, M. O., Watson, S. P., & Foster, S. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.13.3898-3903.1999 · Cited by 185
Ananieva, E. A., Christov, K., & Popova, L. P. (2004) · Journal of Plant Physiology · doi:10.1078/0176-1617-01022 · Cited by 183
Hai, D. Q., Varga, S. I., & Matkovics, B. (1997) · Comparative Biochemistry and Physiology Part C Pharmacology Toxicology and Endocrinology · doi:10.1016/s0742-8413(96)00234-4 · Cited by 185
Gowtham, H. G., Brijesh Singh, S., Murali, M., Shilpa, N. C., Prasad, M., Aiyaz, M., Amruthesh, K. N., & Niranjana, S. R. (2020) · Microbiological Research · doi:10.1016/j.micres.2020.126422 · Cited by 191
PprI: a general switch responsible for extreme radioresistance of Deinococcus radiodurans
Hua, Y., Narumi, I., Gao, G., Tian, B., Satoh, K., Kitayama, S., & Shen, B. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00965-3 · Cited by 184
Drought tolerance in a Saharian plant Oudneya africana: Role of antioxidant defences
Talbi, S., Romero‐Puertas, M. C., Hernández, A., Terron-Camero, L. C., Ferchichi, A., & Sandalio, L. M. (2014) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2014.11.004 · Cited by 182
Janulczyk, R., Ricci, S., & Björck, L. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2656-2664.2003 · Cited by 182
Antioxidative enzymes in cultivars of pepper plants with different sensitivity to cadmium
León, A. M., Palma, J. M., Corpas, F. J., Gómez, M., Romero‐Puertas, M. C., Chatterjee, D., Mateos, R. M., del Río, L. A., & Sandalio, L. M. (2002) · Plant Physiology and Biochemistry · doi:10.1016/s0981-9428(02)01444-4 · Cited by 182
WANG, C., ZHANG, S., WANG, P., Hou, J., LI, W., & ZHANG, W. (2008) · Aquatic Toxicology · doi:10.1016/j.aquatox.2008.01.009 · Cited by 182
Chu, C., Lee, W., Wen-yu, G., Pan, S., Chen, L., Li, H., & Jinn, T.-L. (2005) · PLANT PHYSIOLOGY · doi:10.1104/pp.105.065284 · Cited by 182
Isolation and characterization of a manganese-containing superoxide dismutase from yeast.
Ravindranath, S. D., & Fridovich, I. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41165-4 · Cited by 182
Self-citationMazza, C. A. D. S., Battista, D., Zima, A. M., Szwarcberg-Bracchitta, M., Giordano, C. V., Acevedo, A., Scopel, A. L., & Ballaré, C. L. (1999) · Plant Cell & Environment · doi:10.1046/j.1365-3040.1999.00381.x · Cited by 180
Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis
Zhang, Y., Lathigra, R. B., Garbe, T. R., Catty, D., & Young, D. B. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb02120.x · Cited by 182
Asada, K., Urano, M., & Takahashi, M. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02908.x · Cited by 182
Role of pH on antioxidants production by spirulina (Arthrospira) platensis
Ismaiel, M. M. S., El-Ayouty, Y. M., & Piercey-Normore, M. (2016) · Brazilian Journal of Microbiology · doi:10.1016/j.bjm.2016.01.003 · Cited by 181
Photodestruction of pheomelanin: role of oxygen.
Chedekel, M. R., Smith, S. K., Post, P. W., Pokora, A., & Vessell, D. L. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.11.5395 · Cited by 181
Tewari, R. K., Kumar, P. S., Tewari, N., Srivastava, S., & Sharma, P. N. (2003) · Plant Science · doi:10.1016/j.plantsci.2003.11.004 · Cited by 181
Dinler, B. S., Sekmen, A. H., & Türkan, İ. (2008) · Journal of Plant Growth Regulation · doi:10.1007/s00344-008-9068-1 · Cited by 179
Bioaccumulation and physiological effects of mercury in Pteris vittata and Nephrolepis exaltata
Chen, J., Shiyab, S. M., Han, F. X., Monts, D. L., Waggoner, C. A., Yang, Z., & Su, Y. (2008) · Ecotoxicology · doi:10.1007/s10646-008-0264-3 · Cited by 181
Guha, T., Ravikumar, K. V. G., Mukherjee, A., Mukherjee, A., & Kundu, R. (2018) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2018.04.014 · Cited by 182
Kučerová, K., Henselova, M., Slováková, Ľ., & Hensel, K. (2019) · Plasma Processes and Polymers · doi:10.1002/ppap.201800131 · Cited by 181
Zhang, H. J., Zhao, W., Venkataraman, S., Robbins, M. E. C., Buettner, G. R., Kregel, K. C., & Oberley, L. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109801200 · Cited by 179
Ratovitski, T., Corson, L., Strain, J., Wong, P., Cleveland, D. W., Culotta, V., & Borchelt, D. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.8.1451 · Cited by 180
Effect of cadmium on the growth and antioxidant enzymes in two varieties of Brassica juncea
Irfan, M., Ahmad, A., & Hayat, S. (2013) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2013.08.001 · Cited by 180
LeBlanc, J. G., del Carmen, S., Miyoshi, A., Azevedo, V., Sesma, F. J. M., Langella, P., Bermúdez‐Humarán, L. G., Watterlot, L., Perdigón, G., & de LeBlanc, A. D. M. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.11.008 · Cited by 179
Protein tyrosine nitration in pea roots during development and senescence
Begara-Morales, J. C., Chaki, M., Sánchez-Calvo, B., Mata-Pérez, C., Leterrier, M., Palma, J. M., Barroso, J. B., & Corpas, F. J. (2013) · Journal of Experimental Botany · doi:10.1093/jxb/ert006 · Cited by 179
Wu, Z., Liu, S., Zhao, J., Wang, F., Du, Y., Sumin, Z., Li, H., Wen, D., & Huang, Y. (2016) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2016.09.005 · Cited by 178
Nazir, F., Hussain, A., & Fariduddin, Q. (2019) · Chemosphere · doi:10.1016/j.chemosphere.2019.05.001 · Cited by 179
Buettner, G. R., Oberley, L. W., & Leuthauser, S. W. C. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07001.x · Cited by 179
Shao, J., Wu, Z., Yu, G., Peng, X., & Li, R. (2009) · Chemosphere · doi:10.1016/j.chemosphere.2009.01.021 · Cited by 175
Ozgur, R., Türkan, İ., Uzilday, B., & Sekmen, A. H. (2014) · Journal of Experimental Botany · doi:10.1093/jxb/eru034 · Cited by 180
Fat metabolism in higher plants
Matsumura, S., & Stumpf, P. K. (1968) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(68)90533-x · Cited by 178
Raja, D. S., Ganesan, P., Bhuvanesh, N. S. P., Reibenspies, J. H., Renganathan, R., & Natarajan, K. (2011) · Dalton Transactions · doi:10.1039/c0dt01657h · Cited by 177
Siddhuraju, P. (2006) · LWT · doi:10.1016/j.lwt.2006.07.010 · Cited by 177
Tohma, H., & Gülçın, İ. (2010) · International Journal of Food Properties · doi:10.1080/10942911003773916 · Cited by 177
Waxman, A. B., Einarsson, Ó., Seres, T., Knickelbein, R. G., Warshaw, J. B., Johnston, R. B., Homer, R., & Elias, J. A. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1337 · Cited by 176
Yasur, J., & Rani, P. U. (2014) · Chemosphere · doi:10.1016/j.chemosphere.2014.11.029 · Cited by 183
24-Epibrassinolide protects against the stress generated by salinity and nickel in Brassica juncea
Ali, B., Hayat, S., Fariduddin, Q., & Ahmad, A. (2008) · Chemosphere · doi:10.1016/j.chemosphere.2008.04.012 · Cited by 176
Manganese complexes displaying superoxide dismutase activity: A balance between different factors
Iranzo, O. (2011) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2011.02.001 · Cited by 180
Regier, N., Streb, S., Cocozza, C., SCHAUB, M. C., Cherubini, P., Zeeman, S. C., & Frey, B. (2009) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2009.02030.x · Cited by 178
Mozafari, A. A., Havas, F., & Ghaderi, N. (2017) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/s11240-017-1347-8 · Cited by 176
Mishra, S., Srivastava, S., Tripathi, R. D., & Trivedi, P. K. (2007) · Aquatic Toxicology · doi:10.1016/j.aquatox.2007.11.001 · Cited by 176
Jain, S., Thakare, V., Das, M., Godugu, C., Jain, A., Mathur, R., Chuttani, K., & Mishra, A. K. (2011) · Chemical Research in Toxicology · doi:10.1021/tx2003728 · Cited by 175
Vouldoukis, I., Lacan, D., Kamaté, C., Coste, P., Calenda, A., Mazier, D., Conti, M., & Dugas, B. (2004) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2004.04.023 · Cited by 177
Sathyadevi, P., Krishnamoorthy, P., Butorac, R. R., Cowley, A. H., Bhuvanesh, N. S. P., & Dharmaraj, N. (2011) · Dalton Transactions · doi:10.1039/c1dt10767d · Cited by 174
Khan, M. N., Mobin, M., Abbas, Z. K., & Siddiqui, M. H. (2017) · Nitric Oxide · doi:10.1016/j.niox.2017.01.001 · Cited by 173
Stappen, C. V., Deng, Y., Liu, Y., Heidari, H., Wang, J., Zhou, Y., Ledray, A. P., & Lu, Y. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00106 · Cited by 187
Antioxidant activities of red versus green leaves in Elatostema rugosum
Neill, S., Gould, K. S., Kilmartin, P. A., Mitchell, K. A., & Markham, K. R. (2002) · Plant Cell & Environment · doi:10.1046/j.1365-3040.2002.00837.x · Cited by 174
Wang, Q., Xiong, D., Zhao, P., Yu, X., Tu, B., & Wang, G. (2011) · Journal of Applied Microbiology · doi:10.1111/j.1365-2672.2011.05142.x · Cited by 173
Oxidative stress during aging of stationary cultures of the yeast Saccharomyces cerevisiae
Jakubowski, W., Biliński, T., & Bartosz, G. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00266-x · Cited by 173
Antioxidant properties of benzoic acid derivatives against Superoxide radical
Veliká, B., & Kron, I. (2012) · Free Radicals and Antioxidants · doi:10.5530/ax.2012.4.11 · Cited by 177
Awasthi, G., Singh, A. P., Kumar, A., Mishra, S., Dwivedi, S., Kumar, S., Trivedi, P. K., Pandey, V., & Tripathi, R. D. (2015) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2015.11.005 · Cited by 173
Stress Responses of Zea mays to Cadmium and Mercury
Rellán‐Álvarez, R., Ortega‐Villasante, C., Álvarez‐Fernández, A., del Campo, F. F., & Hernández, L. E. (2006) · Plant and Soil · doi:10.1007/s11104-005-3900-1 · Cited by 173
Rajeshkumar, S., Venkatesan, C., Sarathi, M., Sarathbabu, V., Thomas, J., Basha, K. A., & Hameed, A. S. S. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2009.01.003 · Cited by 173
Rios-Gonzalez, K., Erdei, L., & Lips, S. H. (2002) · Plant Science · doi:10.1016/s0168-9452(02)00040-7 · Cited by 173
O’Malley, Y., Reszka, K. J., Spitz, D. R., Denning, G. M., & Britigan, B. E. (2004) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00025.2004 · Cited by 173
Rao, S. S. R., & Shekhawat, G. S. (2013) · Journal of environmental chemical engineering · doi:10.1016/j.jece.2013.11.029 · Cited by 175
Giannakoula, A. E., Moustakas, M., Syros, T. D., & Yupsanis, T. A. (2009) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2009.07.010 · Cited by 172
Rangani, J., Parida, A. K., Panda, A., & Kumari, A. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00050 · Cited by 171
Meena, M., Zehra, A., Dubey, M. K., Aamir, M., Gupta, V. K., & Upadhyay, R. S. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01408 · Cited by 175
Rizwan, M., Mostofa, M. G., Ahmad, M. Z., Imtiaz, M., Mehmood, S., Adeel, M., Dai, Z., Li, Z., Aziz, O., Zhang, Y., et al. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.09.068 · Cited by 170
Long, L., Zhang, H., Ni, Q., Liu, H., Wu, F., & Wang, X. (2019) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2019.02.002 · Cited by 172
Wang, X., Huang, W., Wei, S., Shang, Y., Gu, H., Wu, F., Lan, Z., Hu, M., Shi, H., & Wang, Y. (2019) · Environmental Pollution · doi:10.1016/j.envpol.2019.113691 · Cited by 171
Induction of superoxide dismutase in Escherichia coli by heat shock.
Privalle, C. T., & Fridovich, I. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.9.2723 · Cited by 172
Self-citationKrueger, T., Hawkins, T. D., Becker, S., Pontasch, S., Dove, S., Hoegh‐Guldberg, O., Leggat, W. P., Fisher, P. L., & Davy, S. K. (2015) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2015.08.012 · Cited by 166
EFFECT OF DROUGHT STRESS ON GROWTH, PROLINE AND ANTIOXIDANT ENZYME ACTIVITIES OF UPLAND RICE
Lum, M. S., Hanafi, M. M., Rafii, M. Y., & Abdullah, S. N. A. (2014) · UMS Institutional Repository (Universiti Malaysia Sabah) · Cited by 173
Gao, S., Ouyang, C., Wang, S., Xu, Y., Tang, L., & Chen, F. (2008) · Plant Soil and Environment · doi:10.17221/410-pse · Cited by 169
Variation in heat stress-induced antioxidant enzyme activities among three mulberry cultivars
Chaitanya, K. V., Sundar, D., Masilamani, S., & Reddy, A. R. (2002) · Plant Growth Regulation · doi:10.1023/a:1015092628374 · Cited by 171
Activated oxygen species and oxidation of food constituents
Korycka-Dahl, M., Richardson, T., & Foote, C. S. (1978) · C R C Critical Reviews in Food Science and Nutrition · doi:10.1080/10408397809527250 · Cited by 170
Rat-Liver Superoxide Dismutase. Purification and Age-Related Modifications
Reiss, U., & Gershon, D. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10266.x · Cited by 171
Tewari, R. K., Kumar, P. S., & Sharma, P. N. (2007) · Journal of Integrative Plant Biology · doi:10.1111/j.1744-7909.2007.00358.x · Cited by 168
Enhancement of antioxidant activity of chitosan by irradiation
Feng, T., Du, Y., Li, J., Hu, Y., & Kennedy, J. F. (2007) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2007.11.003 · Cited by 170
González, A., Cabrera, M. D. L. Á., Henríquez, M. J., Contreras, R. A., Morales, B., & Moenne, A. (2012) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.191759 · Cited by 170
Pan, Y., Luo, Z., Zhuo, M., Wei, C., Chen, G., & Song, Y. (2018) · Aquatic Toxicology · doi:10.1016/j.aquatox.2018.03.017 · Cited by 166
Metadata
- Authors
- Beauchamp, C., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- Venue
- Analytical Biochemistry
- Publisher
- Elsevier BV
- Published
- 1971-11
- Volume
- 44
- Issue
- 1
- Pages
- 276-287
- ISSN
- 0003-2697 (ISSN-L)
- OpenAlex
- W2101422765
- Cited by
- 12,892
- References
- 21
- Citations by year
- 2026: 577 · 2025: 678 · 2024: 591 · 2023: 617 · 2022: 654 · 2021: 674 · 2020: 577 · 2019: 535 · 2018: 500 · 2017: 463 · 2016: 436 · 2015: 467 · 2014: 500 · 2013: 435 · 2012: 429
- FWCI
- 11.16
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- superoxide dismutase, nitroblue tetrazolium, superoxide, enzyme activity assay, polyacrylamide gel electrophoresis, enzyme localization, Escherichia coli, bovine tissues, enzyme stoichiometry
- MeSH terms
- Animals, Brain, Cattle, Electrophoresis, Disc, Erythrocytes, Escherichia coli, Free Radicals, Indicators and Reagents, Kinetics, Lung, Methods, Myocardium, Oxidation-Reduction, Oxidoreductases, Oxygen, Photochemistry, Spectrophotometry, Tetrazolium Salts, Xanthine Oxidase
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