The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“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]
Citations
Cites
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
Self-citation
Research works printed but not linked: 2
- McCord, 1971, 68, 1024
- Brewer, 1967, Amer. J. Hum. Genet, 19, 674
Cited by
Sorted by citations
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45228-9 · Cited by 9,097
Self-citationZhishen, J., Mengcheng, T., & Wu, J. (1999) · Food Chemistry · doi:10.1016/s0308-8146(98)00102-2 · Cited by 8,868
Giannopolitis, C. N., & Ries, S. K. (1977) · PLANT PHYSIOLOGY · doi:10.1104/pp.59.2.309 · Cited by 6,510
Superoxide radical and superoxide dismutases
Fridovich, I. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.000525 · Cited by 3,455
Self-citationAssaying for superoxide dismutase activity: Some large consequences of minor changes in conditions
Beyer, W. F., & Fridovich, I. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90489-1 · Cited by 2,944
Self-citationThe effect of drought and ultraviolet radiation on growth and stress markers in pea and wheat
Alexieva, V., Sergiev, I., Mapelli, S., & Karanov, E. N. (2001) · Plant Cell & Environment · doi:10.1046/j.1365-3040.2001.00778.x · Cited by 2,265
Tetrazolium dyes as tools in cell biology: new insights into their cellular reduction
Berridge, M. V., Herst, P. M., & Tan, A. S. (2005) · Biotechnology Annual Review · doi:10.1016/s1387-2656(05)11004-7 · Cited by 2,222
Antioxidants and antioxidant methods: an updated overview
Gulcin, İ. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02689-3 · Cited by 2,205
Antioxidant responses of rice seedlings to salinity stress
Dionisio‐Sese, M. L., & Tobita, S. (1998) · Plant Science · doi:10.1016/s0168-9452(98)00025-9 · Cited by 2,010
Antioxidant and radical scavenging properties of curcumin
Ak, T. P., & Gülçın, İ. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.05.003 · Cited by 1,942
Elstner, E. F., & Heupel, A. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90488-7 · Cited by 1,886
Antioxidant activity of food constituents: an overview
Gülçın, İ. (2011) · Archives of Toxicology · doi:10.1007/s00204-011-0774-2 · Cited by 1,728
Weydert, C. J. D., & Cullen, J. J. (2009) · Nature Protocols · doi:10.1038/nprot.2009.197 · Cited by 1,573
[10] Superoxide dismutase assays
Flohé, L., & Ötting, F. (1984) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(84)05013-8 · Cited by 1,509
Dithiocarbamates as potent inhibitors of nuclear factor kappa B activation in intact cells.
Schreck, R., Meier, B., Männel, D. N., Dröge, W., & Baeuerle, P. A. (1992) · The Journal of experimental medicine · doi:10.1084/jem.175.5.1181 · Cited by 1,508
Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
Deng, H., Hentati, A., Tainer, J. A., Iqbal, Z., Cayabyab, A., Hung, W.-Y., Getzoff, E. D., Hu, P., Herzfeldt, B., Roos, R. P., et al. (1993) · Science · doi:10.1126/science.8351519 · Cited by 1,479
Wong, P. C., Pardo, C. A., Borchelt, D., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., & Price, D. L. (1995) · Neuron · doi:10.1016/0896-6273(95)90259-7 · Cited by 1,439
Cadmium‐induced changes in the growth and oxidative metabolism of pea plants
Sandalio, L. M., Dalurzo, H. C., Gómez, M., Romero‐Puertas, M. C., & del Río, L. A. (2001) · Journal of Experimental Botany · doi:10.1093/jexbot/52.364.2115 · Cited by 1,422
Siddhuraju, P., & Becker, K. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf020444+ · Cited by 1,415
Bruijn, L. I., Becher, M. W., Lee, M. K., Anderson, K. L., Jenkins, N. A., Copeland, N. G., Sisodia, S. S., Rothstein, J. D., Borchelt, D. R., Price, D. L., et al. (1997) · Neuron · doi:10.1016/s0896-6273(00)80272-x · Cited by 1,341
Role of oxygen-derived free radicals and metabolites in leukocyte-dependent inflammatory reactions.
Fantone, J. C., & Ward, P. A. (1982) · PubMed Central · Cited by 1,231
Rao, K. V. M., & Tavva, V. S. (2000) · Plant Science · doi:10.1016/s0168-9452(00)00273-9 · Cited by 1,199
In vitro antioxidant activities of methanol extracts of five Phyllanthus species from India
Kumaran, A., & Karunakaran, R. (2005) · LWT · doi:10.1016/j.lwt.2005.09.011 · Cited by 1,195
The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44679-6 · Cited by 1,173
Self-citationVisualization and Interpretation of Plant Isozymes
Wendel, J. F., & Weeden, N. F. (1989) · Springer eBooks · doi:10.1007/978-94-009-1840-5_2 · Cited by 1,170
Mutants of Salmonella typhimurium that cannot survive within the macrophage are avirulent.
Fields, P. I., Swanson, R. V., Haidaris, C. G., & Heffron, F. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.14.5189 · Cited by 1,114
Saeed, N., Khan, M. R., & Shabbir, M. (2012) · BMC Complementary and Alternative Medicine · doi:10.1186/1472-6882-12-221 · Cited by 1,141
A review of the antioxidant potential of medicinal plant species
Krishnaiah, D., Sarbatly, R., & Nithyanandam, R. (2010) · Food and Bioproducts Processing · doi:10.1016/j.fbp.2010.04.008 · Cited by 1,118
Yoshioka, T., Kawada, K., Shimada, T., & Mori, M. (1979) · American Journal of Obstetrics and Gynecology · doi:10.1016/0002-9378(79)90708-7 · Cited by 1,056
Christman, M. F., Morgan, R. W., Jacobson, F. S., & Ames, B. N. (1985) · Cell · doi:10.1016/s0092-8674(85)80056-8 · Cited by 1,029
Lipid Peroxidation Associated with Accelerated Aging of Soybean Axes
Stewart, R. R., & Bewley, J. D. (1980) · PLANT PHYSIOLOGY · doi:10.1104/pp.65.2.245 · Cited by 1,006
Prasad, T. K., Anderson, M. D., Martin, B. A., & Stewart, C. R. (1994) · The Plant Cell · doi:10.1105/tpc.6.1.65 · Cited by 997
Radical scavenging and antioxidant activity of tannic acid
Gülçın, İ., Huyut, Z., Elmastaş, M., & Aboul-Enein, H. Y. (2009) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2009.12.008 · Cited by 977
Mitochondrial Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960
Self-citationWeisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43969-0 · Cited by 895
Self-citationAspects of the Structure, Function, and Applications of Superoxide Dismutas
Bannister, J. V., Bannister, W. H., & Rotilio, G. (1987) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238709083738 · Cited by 860
Demiral, T., & Türkan, İ. (2004) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2004.03.017 · Cited by 791
Carlioz, A., & Touati, D. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04256.x · Cited by 784
MacMillan-Crow, L.-A., Crow, J. P., Kerby, J. D., Beckman, J. S., & Thompson, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.21.11853 · Cited by 769
Evaluation of toxicity and biodegradability of choline chloride based deep eutectic solvents
Radošević, K., Cvjetko Bubalo, M., Gaurina Srček, V., Grgas, D., Landeka Dragičević, T., & Radojčić Redovniković, I. (2015) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2014.09.034 · Cited by 770
Does oxidative damage to DNA increase with age?
Hamilton, M. L., Van Remmen, H., Drake, J. A., Yang, H., Guo, Z. M., Kewitt, K., Walter, C. A., & Richardson, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171202698 · Cited by 768
Banerjee, P., Satapathy, M. K., Mukhopahayay, A., & Das, P. (2014) · Bioresources and Bioprocessing · doi:10.1186/s40643-014-0003-y · Cited by 756
An 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
Dendrimer toxicity: Let's meet the challenge
Jain, K., Kesharwani, P., Gupta, U. D., & Jain, N. K. (2010) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2010.04.027 · Cited by 711
Johnston, R. B., Keele, B. B., Misra, H. P., Lehmeyer, J. E., Webb, L., Baehner, R. L., & Rajagopalan, K. V. (1975) · Journal of Clinical Investigation · doi:10.1172/jci108055 · Cited by 704
Mullarkey, C. J., Edelstein, D., & Brownlee, M. (1990) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(05)80875-7 · Cited by 691
[41] Preparation and assay of superioxide dismutases
Crapo, J. D., McCord, J. M., & Fridovich, I. (1978) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(78)53044-9 · Cited by 686
Self-citationMeier, B., Radeke, H. H., Selle, S., Younes, M., Sies, H., Resch, K., & Habermehl, G. (1989) · Biochemical Journal · doi:10.1042/bj2630539 · Cited by 650
Zhang, F., Wang, Y., Lou, Z., & Dong, J. (2006) · Chemosphere · doi:10.1016/j.chemosphere.2006.10.007 · Cited by 643
Paoletti, F., Aldinucci, D., Mocali, A., & Caparrini, A. (1986) · Analytical Biochemistry · doi:10.1016/0003-2697(86)90026-6 · Cited by 637
Superoxide Dismutase in Plants
Bowler, C., Camp, W. V., MONTAGU, M. V., Inzé, D., & Asada, K. (1994) · Critical Reviews in Plant Sciences · doi:10.1080/07352689409701914 · Cited by 639
Kliebenstein, D. J., Monde, R., & Last, R. L. (1998) · PLANT PHYSIOLOGY · doi:10.1104/pp.118.2.637 · Cited by 632
Mendis, E., Rajapakse, N., & Kim, S. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf048877v · Cited by 623
Borchelt, D., Lee, M. K., Slunt, H. S., Guarnieri, M., Xu, Z. S., Wong, P. C., Brown, R. H., Price, D. L., Sisodia, S. S., & Cleveland, D. W. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.17.8292 · Cited by 622
Mattiazzi, M., D’Aurelio, M., Gajewski, C. D., Martushova, K., Kiaei, M., Beal, M. F., & Manfredi, G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203065200 · Cited by 639
Bor, M., Özdemir, F., & Türkan, İ. (2002) · Plant Science · doi:10.1016/s0168-9452(02)00338-2 · Cited by 598
Intracellular production of superoxide radical and of hydrogen peroxide by redox active compounds
Hassan, H. M., & Fridovich, I. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90289-3 · Cited by 596
Self-citationVallejos, C. E. (1983) · Developments in plant genetics and breeding · doi:10.1016/b978-0-444-42226-2.50031-1 · Cited by 592
Ahmad, P., Latef, A. A. H. A., Hashem, A., Allah, E. F. A., Gücel, S., & Tran, L. P. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00347 · Cited by 587
Antioxidant and free radical scavenging activity of an aqueous extract of Coleus aromaticus
Kumaran, A., & karunakaran, R. J. (2005) · Food Chemistry · doi:10.1016/j.foodchem.2005.03.032 · Cited by 585
Sudhakar, C., Lakshmi, A., & Surabhi, G. (2001) · Plant Science · doi:10.1016/s0168-9452(01)00450-2 · Cited by 583
The antioxidant action of taurine, hypotaurine and their metabolic precursors
Aruoma, O. I., Halliwell, B. B., Hoey, B. M., & Butler, J. (1988) · Biochemical Journal · doi:10.1042/bj2560251 · Cited by 580
Gupta, A. S., Webb, R. P., Holaday, A. S., & Allen, R. D. (1993) · PLANT PHYSIOLOGY · doi:10.1104/pp.103.4.1067 · Cited by 571
Anderson, M. D., Prasad, T. K., & Stewart, C. R. (1995) · PLANT PHYSIOLOGY · doi:10.1104/pp.109.4.1247 · Cited by 568
Türkan, İ., Bor, M., Özdemir, F., & Koca, H. (2004) · Plant Science · doi:10.1016/j.plantsci.2004.07.032 · Cited by 568
Buettner, G. R., & Oberley, L. W. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)90398-4 · Cited by 565
h CTR1 : A human gene for copper uptake identified by complementation in yeast
Zhou, B., & Gitschier, J. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7481 · Cited by 572
de Lamirande, E., & Gagnon, C. (1992) · PubMed · Cited by 561
Gupta, A. S., Heinen, J. L., Holaday, A. S., BURKE, J. J., & Allen, R. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1629 · Cited by 559
A simplified assay method of superoxide dismutase activity for clinical use
Masayasu, M., & Hiroshi, Y. (1979) · Clinica Chimica Acta · doi:10.1016/0009-8981(79)90211-0 · Cited by 557
Greenberg, J. T., Monach, P. A., Chou, J. H., Josephy, P. D., & Demple, B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6181 · Cited by 556
Generation of Superoxide Free Radical during the Autoxidation of Thiols
Misra, H. P. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42810-x · Cited by 556
Biochemical responses in aquatic animals: A review of determinants of oxidative stress
Giulio, R. T. D., Washburn, P. C., Wenning, R. J., Winston, G. W., & Jewell, C. S. E. (1989) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5620081203 · Cited by 554
Bowler, C., Slooten, L., Vandenbranden, S., Rycke, R. M. D., Botterman, J., Sybesma, C., MONTAGU, M. V., & Inzé, D. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07696.x · Cited by 551
Assays for Superoxide Dismutase
Bannister, J. V., & Calabrese, L. (1987) · Methods of biochemical analysis · doi:10.1002/9780470110539.ch5 · Cited by 551
A microtiter plate assay for superoxide dismutase using a water-soluble tetrazolium salt (WST-1)
Peskin, A. V., & Winterbourn, C. C. (2000) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00246-6 · Cited by 548
Rodríguez‐Serrano, M., Romero‐Puertas, M. C., Zabalza, A., Corpas, F. J., Gómez, M., del Río, L. A., & Sandalio, L. M. (2006) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2006.01531.x · Cited by 547
Treatment with salicylic acid decreases the effect of cadmium on photosynthesis in maize plants
Krantev, A., Yordanova, R., Janda, T., Szalai, G., & Popova, L. P. (2007) · Journal of Plant Physiology · doi:10.1016/j.jplph.2006.11.014 · Cited by 539
Koca, H., Bor, M., Özdemir, F., & Türkan, İ. (2007) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2006.12.005 · Cited by 539
Antioxidant properties of potentially probiotic bacteria: in vitro and in vivo activities
Amaretti, A., Nunzio, M. D., Pompei, A., Raimondi, S., Rossi, M., & Bordoni, A. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4241-7 · Cited by 532
Mishra, S., Srivastava, S., Tripathi, R. D., Kumar, R., Seth, C. S., & Gupta, D. K. (2006) · Chemosphere · doi:10.1016/j.chemosphere.2006.03.033 · Cited by 530
Siddhuraju, P. (2002) · Food Chemistry · doi:10.1016/s0308-8146(02)00179-6 · Cited by 526
Two antioxidative lactobacilli strains as promising probiotics
Kullisaar, T., Zilmer, M., Mikelsaar, M., Vihalemm, T., Annuk, H., Kairane, Č., & Kilk, A. (2002) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(01)00674-2 · Cited by 525
Phytochelatin synthesis and response of antioxidants during cadmium stress in Bacopa monnieri L◊
Mishra, S., Srivastava, S., Tripathi, R. D., Govindarajan, R., Kuriakose, S. V., & Prasad, M. N. V. (2006) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2006.01.007 · Cited by 516
Controlling Tumor Growth by Modulating Endogenous Production of Reactive Oxygen Species
Laurent, A., Nicco, C., Chéreau, C., Goulvestre, C., Alexandre, J., Alvès, A., Lévy, E., Goldwasser, F., Panis, Y. H., Soubrane, O., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.948.65.3 · Cited by 516
Salicylic acid induced physiological and biochemical changes in wheat seedlings under water stress
Singh, B., & Usha, K. (2003) · Plant Growth Regulation · doi:10.1023/a:1022556103536 · Cited by 509
Liposome oxidation and erythrocyte lysis by enzymically generated superoxide and hydrogen peroxide.
Kellogg, E. W., & Fridovich, I. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39909-x · Cited by 509
Self-citationBarroso, J. B., Chaki, M., & Begara-Morales, J. C. (2020) · MDPI eBooks · doi:10.3390/books978-3-03943-007-9 · Cited by 505
Rehana, D., Dharmasivam, M., Kumar, R. S., & Rahiman, A. K. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.02.101 · Cited by 498
Characterization of , a Yeast Gene Involved in Copper Metabolism and Assembly of Cytochrome Oxidase
Glerum, D. M., Shtanko, A., & Tzagoloff, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14504 · Cited by 496
Klug-Roth, D., Rabani, J., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44987-9 · Cited by 495
Self-citationA comparative and evolutionary approach to oxidative stress in fish: A review
Birnie‐Gauvin, K., Costantini, D., Cooke, S. J., & Willmore, W. G. (2017) · Fish and Fisheries · doi:10.1111/faf.12215 · Cited by 481
Lee, D. H., & Lee, C. B. (2000) · Plant Science · doi:10.1016/s0168-9452(00)00326-5 · Cited by 480
Marklund, S. L., Westman, N. G., Lundgren, E., & Roos, G. (1982) · PubMed · Cited by 474
Tiwari, S., Lata, C., Chauhan, P. S., & Nautiyal, C. S. (2015) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2015.11.001 · Cited by 478
Superoxide Radical and Iron Modulate Aconitase Activity in Mammalian Cells
Gardner, P. R., Raineri, I., Epstein, L. B., & White, C. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.22.13399 · Cited by 469
Antioxidant activity of clove oil – A powerful antioxidant source
Gülçın, İ., Elmastaş, M., & Aboul-Enein, H. Y. (2010) · Arabian Journal of Chemistry · doi:10.1016/j.arabjc.2010.09.016 · Cited by 471
Mittler, R., & Zilinskas, B. A. (1994) · The Plant Journal · doi:10.1111/j.1365-313x.1994.00397.x · Cited by 470
Fridovich, I. (1986) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123041.ch2 · Cited by 472
Self-citation
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
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