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
Items 601–700 of 1,036
EL-BELTAGI, H. S., Mohamed, H. I., & Sofy, M. R. (2020) · Molecules · doi:10.3390/molecules25071702 · Cited by 174
Effect of salinity on antioxidant responses of chickpea seedlings
Eyidoğan, F., & Öz, M. T. (2007) · Acta Physiologiae Plantarum · doi:10.1007/s11738-007-0059-9 · Cited by 169
de Keyzer, Y., Valayannopoulos, V., Benoist, J., Batteux, F., Lacaille, F., Hubert, L., Chrétien, D., Chadefaux-Vekemans, B., Niaudet, P., Touati, G., et al. (2009) · Pediatric Research · doi:10.1203/pdr.0b013e3181a7c270 · Cited by 168
Haider, S., Saleem, S., Perveen, T., Tabassum, S., Batool, Z., Sadir, S., Liaquat, L., & Madiha, S. (2014) · AGE · doi:10.1007/s11357-014-9653-0 · Cited by 168
Presence of the pharmaceutical drug carbamazepine in coastal systems: Effects on bivalves
Almeida, Â., Calisto, V., Esteves, V. I., Schneider, R. J., Soares, A. M. V. M., Figueira, E. M. D. A. P., & Freitas, R. (2014) · Aquatic Toxicology · doi:10.1016/j.aquatox.2014.08.002 · Cited by 168
Al-Arjani, A.-B. F., Hashem, A., & Allah, E. F. A. (2019) · Saudi Journal of Biological Sciences · doi:10.1016/j.sjbs.2019.10.008 · Cited by 170
Superoxide Dismutase and Oxygen Toxicity in a Eukaryote
Gregory, E. M., Goscin, S. A., & Fridovich, I. (1974) · Journal of Bacteriology · doi:10.1128/jb.117.2.456-460.1974 · Cited by 168
Self-citationThe Role of Compartmentation in the Control of Glycolysis
Ottaway, J. H., & Mowbray, J. (1977) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152812-6.50010-x · Cited by 168
Ding, Z., Zhang, Y., Ye, J., Du, Z., & Kong, Y. (2015) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2015.02.024 · Cited by 167
Physiological and antioxidant responses of Mentha pulegium (Pennyroyal) to salt stress
Oueslati, S., Karray‐Bouraoui, N., Attia, H., Rabhi, M., Ksouri, R., & Lachaâl, M. (2009) · Acta Physiologiae Plantarum · doi:10.1007/s11738-009-0406-0 · Cited by 167
Nanoparticles formulation of Cuscuta chinensis prevents acetaminophen-induced hepatotoxicity in rats
Yen, F., Wu, T.-H., Lin, L., Cham, T., & Lin, C. (2008) · Food and Chemical Toxicology · doi:10.1016/j.fct.2008.01.021 · Cited by 167
Experimental evidence that flavonoid metal complexes may act as mimics of superoxide dismutase
Kostyuk, V. A., Potapovich, A. I., Strigunova, E. N., Kostyuk, T. V., & Afanasʹev, I. B. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.06.008 · Cited by 166
Fahnenstich, H., Scarpeci, T. E., Valle, E. M., Flügge, U., & Maurino, V. G. (2008) · PLANT PHYSIOLOGY · doi:10.1104/pp.108.126789 · Cited by 167
Inactivation of the human CuZn superoxide dismutase during exposure to O2− and H2O2
Sinet, P.-M., & Garber, P. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90382-9 · Cited by 167
[3] Basic methods for the study of phagocytosis
Absolom, D. R. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(86)32005-6 · Cited by 166
Sumithra, K., Jutur, P. P., Carmel, B. D., & Reddy, A. R. (2006) · Plant Growth Regulation · doi:10.1007/s10725-006-9121-7 · Cited by 167
Antioxidant responses to water deficit by drought‐tolerant and ‐sensitive sugarcane varieties
Cia, M. C., Guimarães, A. C. R., Médici, L. O., Chabregas, S. M., & Azevedo, R. A. (2012) · Annals of Applied Biology · doi:10.1111/j.1744-7348.2012.00575.x · Cited by 165
Kaya, C., Şenbayram, M., Akram, N. A., Ashraf, M., Alyemeni, M. N., & Ahmad, P. (2020) · Scientific Reports · doi:10.1038/s41598-020-62669-6 · Cited by 166
Superoxide Dismutases of Escherichia coli : Intracellular Localization and Functions
Gregory, E. M., Yost, F. J., & Fridovich, I. (1973) · Journal of Bacteriology · doi:10.1128/jb.115.3.987-991.1973 · Cited by 166
Self-citationTewari, R. K., Kumar, P., & Sharma, P. N. (2005) · Planta · doi:10.1007/s00425-005-0160-5 · Cited by 163
Xie, Y., Ling, T., Han, Y., Liu, K., Zheng, Q., Huang, L., Yuan, X., He, Z., Hu, B., Fang, L., et al. (2008) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2008.01888.x · Cited by 166
Allen, M. D., Kropat, J., Tottey, S., Campo, J. A. D., & Merchant, S. (2006) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.088609 · Cited by 166
H 2 S Protects Against Methionine–Induced Oxidative Stress in Brain Endothelial Cells
Tyagi, N., Moshal, K. S., Sen, U., Vacek, T. P., Kumar, M., Hughes, W. M., Kundu, S., & Tyagi, S. C. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2008.2073 · Cited by 165
Nitric oxide interferes with plant photo‐oxidative stress by detoxifying reactive oxygen species
Beligni, M. V., & Lamattina, L. (2002) · Plant Cell & Environment · doi:10.1046/j.1365-3040.2002.00857.x · Cited by 165
Khan, Z., Khan, M. N., Zhang, K., Luo, T., Zhu, K., & Hu, L. (2021) · Industrial Crops and Products · doi:10.1016/j.indcrop.2021.113878 · Cited by 169
Liu, R., Althaus, J. S., Ellerbrock, B. R., Becker, D. A., & Gurney, M. E. (1998) · Annals of Neurology · doi:10.1002/ana.410440510 · Cited by 165
Diaz-Ochoa, V. E., Lam, D., Lee, C. S., Klaus, S., Behnsen, J., Liu, J. Z., Chim, N., Nuccio, S.-P., Rathi, S. G., Mastroianni, J. R., et al. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.05.005 · Cited by 164
Phytostabilization Potential of Jatropha Curcas L. in Polymetallic Acid Mine Tailings
Wu, Q., Wang, S., Thangavel, P., Li, Q., Zheng, H., Bai, J., & Qiu, R. (2011) · International Journal of Phytoremediation · doi:10.1080/15226514.2010.525562 · Cited by 164
Effects of Cadmium on Antioxidant Enzyme Activities in Sugar Cane
Fornazier, R. F., Ferreira, R. R., Vitória, Â. P., Molina, S., Lea, P. J., & Azevedo, R. A. (2002) · Biologia Plantarum · doi:10.1023/a:1015100624229 · Cited by 164
�d�m, A. L., Bestwick, C. S., Barna, B., & Mansfıeld, J. W. (1995) · Planta · doi:10.1007/bf00202643 · Cited by 164
Pedrajas, J. R., Peinado, J., & López‐Barea, J. (1995) · Chemico-Biological Interactions · doi:10.1016/0009-2797(95)03651-2 · Cited by 164
Israr, M., Jewell, A., Kumar, D., & Sahi, S. V. (2010) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2010.12.021 · Cited by 163
Umar, S., Umar, K., Sarwar, A. H. M. G., Khan, A., Ahmad, N., Ahmad, S., Katiyar, C. K., Husain, S. A., & Khan, H. A. (2014) · Phytomedicine · doi:10.1016/j.phymed.2014.02.001 · Cited by 163
Gülçın, İ., Tel, A. Z., & Kıreçcı, E. (2008) · International Journal of Food Properties · doi:10.1080/10942910701567364 · Cited by 163
Prussian Blue: A Nanozyme with Versatile Catalytic Properties
Estelrich, J., & Busquets, M. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115993 · Cited by 163
Christensen, A. B., Thordal‐Christensen, H., Zimmermann, G., Gjetting, T., Lyngkjær, M. F., Dudler, R., & Schweizer, P. (2004) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi.2004.17.1.109 · Cited by 163
Blocking NMDA receptors prevents the oxidative stress induced by acute ammonia intoxication
Kosenko, E. A., Kaminski, Y., Lopata, O., Muravyov, N., & Felipo, V. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00339-6 · Cited by 163
Effect of hydrogen peroxide on somatic embryogenesis of Lycium barbarum L.
Kairong, C., Gengsheng, X., Xinmin, L., Gengmei, X., & Yafu, W. (1999) · Plant Science · doi:10.1016/s0168-9452(99)00087-4 · Cited by 163
Jaleel, C. A., Sankar, B., Murali, P. V., Gomathinayagam, M., Lakshmanan, G. M. A., & Panneerselvam, R. (2007) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2007.09.026 · Cited by 163
Tseng, H., Srikhanta, Y. N., McEwan, A. G., & Jennings, M. P. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02460.x · Cited by 164
Sun, J., You, X., Li, L., HongXiang, P., Su, W., Li, C., He, Q., & Liao, F. (2011) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2011.07.001 · Cited by 161
Malanga, G., & Puntarulo, S. (1995) · Physiologia Plantarum · doi:10.1111/j.1399-3054.1995.tb00983.x · Cited by 162
Poyart, C., Pellegrini, E., Gaillot, O., Boumaila, C., Baptista, M., & Trieu‐Cuot, P. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.5098-5106.2001 · Cited by 162
Yeşilkaya, H., Kadioglu, A., Gingles, N. A., Alexander, J. E., Mitchell, T. J., & Andrew, P. W. (2000) · Infection and Immunity · doi:10.1128/iai.68.5.2819-2826.2000 · Cited by 162
Höferl, M., Стоилова, И., Schmidt, E., Wanner, J., Jirovetz, L., Trifonova, D., Krastev, L., & Krastanov, A. I. (2014) · Antioxidants · doi:10.3390/antiox3010081 · Cited by 161
Oxidative events during programmed cell death of daylily (Hemerocallis hybrid) petals
Panavas, T., & Rubinstein, B. (1998) · Plant Science · doi:10.1016/s0168-9452(98)00034-x · Cited by 161
de Campos, M. K. F., de Carvalho, K., de Souza, F. S., Marur, C. J., Pereira, L. F. P., Filho, J. C. B., & Vieira, L. G. E. (2011) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2011.03.009 · Cited by 161
Kaur, N., Dhawan, M. K., Sharma, I., & Pati, P. K. (2016) · BMC Plant Biology · doi:10.1186/s12870-016-0824-2 · Cited by 157
Abdelaziz, M. E., Abdelsattar, M., Abdeldaym, E. A., Atia, M. A. M., Mahmoud, A. W. M., Saad, M. M., & Hirt, H. (2019) · Scientia Horticulturae · doi:10.1016/j.scienta.2019.05.059 · Cited by 165
Light-Induced Production of Singlet Oxygen and Superoxide by the Fungal Toxin, Cercosporin
Daub, M. E., & Hangarter, R. P. (1983) · PLANT PHYSIOLOGY · doi:10.1104/pp.73.3.855 · Cited by 161
Antioxidative enzymes in wheat subjected to increasing water deficit and rewatering
Sgherri, C. L. M., Maffei, M., & Navari‐Izzo, F. (2000) · Journal of Plant Physiology · doi:10.1016/s0176-1617(00)80048-6 · Cited by 161
Superoxide production and reducing activity in human platelets.
Marcus, A. J., Silk, S. T., Safier, L. B., & ULLMAN, H. L. (1977) · Journal of Clinical Investigation · doi:10.1172/jci108613 · Cited by 161
Meier, B., Barra, D., Bossa, F., Calabrese, L., & Rotilio, G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45329-5 · Cited by 161
Yen, F., Wu, T.-H., Lin, L., & Lin, C. (2006) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2006.11.003 · Cited by 160
Zong, X., Li, D., Gu, L., Liu, L., Liu, L., & Hu, X. (2008) · Planta · doi:10.1007/s00425-008-0848-4 · Cited by 160
Melatonin combined with ascorbic acid provides salt adaptation in Citrus aurantium L. seedlings
Kostopoulou, Z., Therios, I. N., Roumeliotis, E., Kanellis, A. K., & Molassiotis, A. N. (2014) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2014.11.021 · Cited by 161
Chaki, M., Valderrama, R., Fernández-Ocaña, A. M., Carreras, A., Gómez-Rodríguez, M. V., Pedrajas, J. R., Begara-Morales, J. C., Sánchez-Calvo, B., Luque, F., Leterrier, M., et al. (2010) · Journal of Experimental Botany · doi:10.1093/jxb/erq358 · Cited by 166
Tognetti, V. B., Palatnik, J. F., Fillat, M. F., Melzer, M., Hajirezaei, M., Valle, E. M., & Carrillo, N. J. (2006) · The Plant Cell · doi:10.1105/tpc.106.042424 · Cited by 160
Srivastava, S., Bist, V., Srivastava, S., Singh, P. C., Trivedi, P. K., Asif, M. H., Chauhan, P. S., & Nautiyal, C. S. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.00587 · Cited by 162
Vesković, M. N., Mladenović, D. R., Milenkovic, M. M., Tasić, J., Borozan, S. Z., Gopčević, K., Labudović‐Borović, M., Dragutinović, V. V., Vučević, D. B., Jorgačević, B. Z., et al. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.01.043 · Cited by 162
Bar‐Or, D., Rael, L. T., Lau, E. P., Rao, N. K. R., Thomas, G. W., Winkler, J. V., Yukl, R. L., Kingston, R. G., & Curtis, C. G. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5042 · Cited by 160
Superoxide dismutase as modulator of immune function in American white shrimp (Litopenaeus vannamei)
Campa‐Córdova, Á. I., Hernández-Saavedra, N. Y., & Ascencio, F. (2002) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/s1532-0456(02)00125-4 · Cited by 160
Modulation of antioxidant responses by arsenic in maize
Mylona, P. V., Polidoros, A. N., & Scandalios, J. G. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00090-2 · Cited by 160
Handelman, G. J., & Dratz, E. A. (1986) · Advances in free radical biology and medicine · doi:10.1016/s8755-9668(86)80024-2 · Cited by 158
Synthesis and antiviral activity of novel pyrazole derivatives containing oxime esters group
Ouyang, G., Chen, Z., Cai, X.-J., Song, B.-A., Bhadury, P. S., Yang, S., Jin, L., Xue, W., Hu, D., & Zeng, S. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.09.070 · Cited by 159
Buonanno, M., de Toledo, S. M., Pain, D., & Azzam, E. I. (2011) · Radiation Research · doi:10.1667/rr2461.1 · Cited by 159
Changes in antioxidative metabolism accompanying pitting development in stored blueberry fruit
Zhou, Q., Ma, C., Cheng, S., Wei, B., Liu, X., & Ji, S. (2013) · Postharvest Biology and Technology · doi:10.1016/j.postharvbio.2013.10.003 · Cited by 160
Bioaccumulation and catabolism of prometryne in green algae
Jin, Z. P., Luo, K., Zhang, S., Zheng, Q., & Yang, H. (2012) · Chemosphere · doi:10.1016/j.chemosphere.2011.12.071 · Cited by 156
Fukami, J., de la Osa, C., Ollero, F. J., Megı́as, M., & Hungría, M. (2017) · Functional Plant Biology · doi:10.1071/fp17167 · Cited by 159
Zahedi, S. M., Hosseini, M. S., Abadı́a, J., & Marjani, M. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.02.021 · Cited by 159
Superoxide anion scavenging effect and superoxide dismutase activity ofGinkgo biloba extract
Pincemail, J., Dupuis, M., Nasr, C., Hans, P., Haag-Berrurier, M., Anton, R., & Deby, C. M. T. (1989) · Cellular and Molecular Life Sciences · doi:10.1007/bf01974564 · Cited by 159
Alonso, R., Elvira, S., Castillo, F. J., & Gimeno, B. (2001) · Plant Cell & Environment · doi:10.1046/j.0016-8025.2001.00738.x · Cited by 158
Bajguz, A. (2009) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2009.11.003 · Cited by 157
Tu, Y., Sun, Y.-Z., Tian, Y., Xie, M., & Chen, J. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.11.015 · Cited by 158
Misra, S., & Chauhan, P. S. (2020) · 3 Biotech · doi:10.1007/s13205-020-2104-y · Cited by 161
Alleviation of cadmium toxicity in Medicago sativa by hydrogen-rich water
Cui, W., Gao, C., Fang, P., Lin, G., & Shen, W. (2013) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2013.06.032 · Cited by 155
Jiang, J. X., Mikami, K., Venugopal, S. K., Li, Y., & Torok, N. J. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2009.03.024 · Cited by 159
Tkalec, M., Štefanić, P. P., Cvjetko, P., Šikić, S., Pavlica, M., & Balen, B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087582 · Cited by 156
Noreen, S., Sultan, M., Akhter, M. S., Shah, K. H., Ummara, U., Manzoor, H., Ulfat, M., Alyemeni, M. N., & Ahmad, P. (2020) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2020.11.007 · Cited by 160
Chu, Y., Iida, S., Lund, D. D., Weiss, R. M., DiBona, G. F., Watanabe, Y., Faraci, F. M., & Heistad, D. D. (2003) · Circulation Research · doi:10.1161/01.res.0000057755.02845.f9 · Cited by 157
Rai, A., Tripathi, P., Dwivedi, S., Dubey, S., Shri, M., Kumar, S., Tripathi, P. K., Dave, R., Kumar, A., Singh, R., et al. (2011) · Chemosphere · doi:10.1016/j.chemosphere.2010.10.070 · Cited by 156
Oliveira, M. W. S., Minotto, J. B., de Oliveira, M. R., Zanotto‐Filho, A., Behr, G. A., da Rocha, R. F., Moreira, J. C. F., & Klamt, F. (2010) · Pharmacological Reports · doi:10.1016/s1734-1140(10)70256-5 · Cited by 156
Uddin, I., Bano, A., & Masood, S. (2014) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2014.12.014 · Cited by 156
Zhang, M., Zhai, Z.-X., Tian, X., Duan, L., & Li, Z. (2008) · Plant Growth Regulation · doi:10.1007/s10725-008-9305-4 · Cited by 156
Soon, C. P. W., Donnelly, P. S., Turner, B. J., Hung, L. W., Crouch, P. J., Sherratt, N. A., Tan, J., Lim, N. K.-H., Lam, L. Q., Bica, L., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.274407 · Cited by 158
Singh, A. P., Awasthi, G., Kumar, A., Mishra, S., Singh, P. K., Dwivedi, S., Trivedi, P. K., Chakrabarty, D., Mallick, S., Pandey, V., et al. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2015.01272 · Cited by 158
Melatonin attenuates postharvest physiological deterioration of cassava storage roots
Ma, Q., Zhang, T., Zhang, P., & Wang, Z. (2016) · Journal of Pineal Research · doi:10.1111/jpi.12325 · Cited by 157
Venkataraman, S., Jiang, X., Weydert, C. J. D., Zhang, Y., Zhang, H. J., Goswami, P. C., Ritchie, J. M., Oberley, L. W., & Buettner, G. R. (2004) · Oncogene · doi:10.1038/sj.onc.1208145 · Cited by 156
Seyler, R. W., Olson, J. W., & Maier, R. J. (2001) · Infection and Immunity · doi:10.1128/iai.69.6.4034-4040.2001 · Cited by 155
Distribution of Iron-Containing Superoxide Dismutase in Vascular Plants
Bridges, S. M., & Salin, M. L. (1981) · PLANT PHYSIOLOGY · doi:10.1104/pp.68.2.275 · Cited by 156
Allen, R. C., Yevich, S. J., Orth, R. W., & Steele, R. H. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(74)90401-x · Cited by 156
Liposomal Delivery System Enhances Anti-Inflammatory Properties of Curcumin
Basnet, P., Hussain, H., Tho, I., & Škalko‐Basnet, N. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22785 · Cited by 155
Kim, Y., Kim, C. Y., Song, W., Park, D., Kwon, S., Haeng-Soon, L. E. E., Bang, J.-W., & Kwak, S. (2007) · Planta · doi:10.1007/s00425-007-0663-3 · Cited by 155
Liu, D., Zou, J., Wang, M., & Jiang, W. (2007) · Bioresource Technology · doi:10.1016/j.biortech.2007.04.045 · Cited by 155
Zinc alleviates growth inhibition and oxidative stress caused by cadmium in rice
Hassan, M. J., Zhang, G., Wu, F., Wei, K., & Chen, Z. (2005) · Journal of Plant Nutrition and Soil Science · doi:10.1002/jpln.200420403 · Cited by 155
Polarographic determination of superoxide dismutase
Rigo, A., Viglino, P., & Rotilio, G. (1975) · Analytical Biochemistry · doi:10.1016/0003-2697(75)90672-7 · Cited by 155
Malm, T., Iivonen, H., Goldsteins, G., Keksa-Goldsteine, V., Ahtoniemi, T., Kanninen, K. M., Salminen, A., Auriola, S. O. K., van Groen, T., Tanila, H., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0059-07.2007 · Cited by 157
Ansari, F. A., Jabeen, M., & Ahmad, I. (2021) · International Journal of Environmental Science and Technology · doi:10.1007/s13762-020-03045-9 · Cited by 154
Inhibition of glutathione reductase by flavonoids
Elliott, A. J., Scheiber, S. A., Thomas, C., & Pardini, R. S. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90478-2 · Cited by 154
Srivalli, B., Sharma, G., & Khanna‐Chopra, R. (2003) · Physiologia Plantarum · doi:10.1046/j.1399-3054.2003.00125.x · Cited by 154
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