The DOI matches its Crossref record, with a small difference in title or year; 38 of the 38 references it cites were found in a registry or an index.
Superoxide Dismutase
Open accessAbstract
Abstract Fresh chicken liver contains two types of superoxide dismutase, one of which is localized in the mitochondria while the other is found in the cytosol. The mitochondrial superoxide dismutase was inactivated by treatment with mixtures of chloroform and ethanol whereas the cytosol superoxide dismutase was not. The cytosol superoxide dismutase was inhibited by cyanide, whereas the mitochondrial enzyme was not. The cytosol superoxide dismutase was purified to homogeneity and was found to contain copper and zinc and to be similar to the other cupro-zinc superoxide dismutases which have been isolated from diverse eukaryotes. In contrast, the superoxide dismutase present in chicken liver mitochondria, when isolated, was found to a manganoprotein which has a molecular weight of 80,000. It is composed of four subunits of equal size, which are not covalently joined. It contains 2.3 atoms of manganese per molecule and is strikingly similar to the superoxide dismutase previously isolated from bacteria (Keele, B. B., Jr., McCord, J. M., and Fridovich, I. (1970) J. Biol. Chem. 245, 6176–6181; Vance, P. G., Keele, B. B., Jr., and Rajagopalan, K. V. (1972) J. Biol. Chem. 247, 4782–4786). Avimanganin which was isolated from chicken liver mitochondria (Scrutton, M. C. (1971) Biochemistry 10, 3897–3905) appears to be an inactive form of mitochondrial superoxide dismutase. The similarity between the mitochondrial superoxide dismutase and the corresponding enzymes from Escherichia coli and from Streptococcus mutans and the marked dissimilarity to the superoxide dismutase found in the cytosols of eukaryotes lends support to the theory that mitochondria have evolved from aerobic prokaryotes, which entered into an endocellular symbiosis with a protoeukaryote. Chicken liver was not unique in possessing distinct superoxide dismutases in cytosol and in mitochondrial compartments, since the same situation was shown to occur in pig heart. The chicken liver cytosol superoxide dismutase exhibited two peculiar properties. Thus when stored in deep, concentrated solutions it underwent autoreduction to a yellow cuprous form which retained enzymatic activity, and it polymerized to forms which likewise retained activity. Both of these changes were reversible and appeared to be due to reactive sulfhydryl groups which could act as the endogenous reductant and could form intermolecular disulfide bridges. The cytosol superoxide dismutase consisted of a family of electrophoretically distinct forms which could readily be separated on a preparative scale by isoelectric focusing. These multiple forms were indistinguishable in size and in specific activity. The chemical basis of these differences in charge was not explored.
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
“The second enzyme is located near the mitochondrial inner membrane. This is a SOD that binds manganese in its catalytic centre (SOD2 or Mn-SOD) [71,72].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [72]
Citations
Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688
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-citationSuperoxide 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
Self-citationSpectroscopic Determination of Tryptophan and Tyrosine in Proteins *
Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438
Equilibrium Ultracentrifugation of Dilute Solutions*
Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,386
High resolution acrylamide gel electrophoresis of histones
Panyim, S., & Chalkley, R. G. (1969) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(69)90042-3 · Cited by 2,459
THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID
Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,862
Raven, P. H., & Margulis, L. (1971) · Evolution · doi:10.1111/j.1558-5646.1971.tb01930.x · Cited by 1,483
An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase
McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 976
Self-citation
Research works printed but not linked: 4
- Tsuchihashi, 1923, Biochem. Z., 140, 63
- Cohen, 1970, Amer. Sci., 58, 281
- Schnepf, 1972, 2, 299
- Dixon, 1935, Proc. Roy. Soc. Ser. B Biol. Sci., 119, 159
Cited by
Sorted by citations
Items 301–400 of 895
Dryer, S. E., Dryer, R. L., & Autor, A. P. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86140-9 · Cited by 60
Extracellular Superoxide Dismutase: Growth Promoter or Tumor Suppressor?
Laukkanen, M. O. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3612589 · Cited by 61
Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase
Iñarrea, P., Moini, H., Rettori, D., Han, D., MARTÍNEZ, J., García‐Rubio, I., Fernández‐Vizarra, E., Iturralde, M., & Cadenas, E. (2005) · Biochemical Journal · doi:10.1042/bj20041683 · Cited by 59
Lee, S. J., Choi, M. G., Kim, D. S., & Kim, T. W. (2005) · Metabolism · doi:10.1016/j.metabol.2005.04.030 · Cited by 59
Nakano, M., Kimura, H., Hara, M., Kuroiwa, M., Katô, M., Totsune, K., & Yoshikawa, T. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90457-k · Cited by 59
Hurt, J. D., Hsu, J.-L., Dougall, W. C., Visner, G. A., Burr, I. M., & Nick, H. S. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.12.2985 · Cited by 59
Evolutionary relationships in superoxide dismutase
Bridgen, J., Harris, J. I., & Northrop, F. D. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80793-9 · Cited by 59
Babo, S., & Vasseur, P. (1992) · Aquatic Toxicology · doi:10.1016/0166-445x(92)90036-m · Cited by 58
Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1
Fetherolf, M. M., Boyd, S. D., Winkler, D. D., & Winge, D. R. (2017) · Metallomics · doi:10.1039/c6mt00298f · Cited by 60
Ureta, T. (1978) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152813-3.50011-2 · Cited by 58
The biology and pathology of hypoxia-ischemia: an update.
Clarkson, A. N., Sutherland, B. A., & Appleton, I. (2005) · PubMed · Cited by 57
Manganese scavenges superoxide and hydroxyl radicals: an in vitro study in rats
Hussain, S. M., & Ali, S. F. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(98)01005-2 · Cited by 57
Matsumoto, H., Silverton, S. F., Debolt, K. M., & Shapiro, I. M. (1991) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650060607 · Cited by 57
Secretion of extracellular superoxide dismutase in neonatal lungs
Nozik‐Grayck, E., Dieterle, C. S., Piantadosi, C. A., Enghild, J. J., & Oury, T. D. (2000) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.2000.279.5.l977 · Cited by 57
Duke, M. V., & Salin, M. L. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90800-8 · Cited by 57
Piqueras, A., Hern�ndez, J. A., Olmos, E., Hell�n, E., & Sevilla, F. (1996) · Plant Cell Tissue and Organ Culture (PCTOC) · doi:10.1007/bf00043428 · Cited by 57
cDNA and deduced amino acid sequence of rat copper-zinc-containing superoxide dismutase
Ho, Y., & Crapo, J. D. (1987) · Nucleic Acids Research · doi:10.1093/nar/15.16.6746 · Cited by 57
Davis, C. D., & Feng, Y. (1999) · Journal of Nutrition · doi:10.1093/jn/129.5.1060 · Cited by 55
Lee, I. K., Kang, K. A., Zhang, R., Kim, B., Kang, S. S., & Hyun, J. W. (2010) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2010.11.002 · Cited by 54
Datkhile, K. D., Mukhopadhyaya, R., Dongre, T. K., & Nath, B. B. (2008) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2008.11.003 · Cited by 55
In Vivo Imaging of Hydrogen Peroxide with HyPer Probes
Bilan, D. S., & Belousov, V. V. (2018) · Antioxidants and Redox Signaling · doi:10.1089/ars.2018.7540 · Cited by 56
Manganese stimulates calcium flux through the mitochondrial uniporter
Allshire, A., Bernardi, P., & Saris, N.-E. L. (1985) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(85)90123-9 · Cited by 55
Altered Levels of Scavenging Enzymes in Embryos Subjected to a Diabetic Environment
Forsberg, H., Borg, H. L. A., Cagliero, E., & Eriksson, L. J. (1996) · Free Radical Research · doi:10.3109/10715769609088044 · Cited by 56
Magnetic Resonance Studies of Manganese (III) and Iron(III) Superoxide Dismutases
Villafranca, J. J., Yost, F. J., & Fridovich, I. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42604-5 · Cited by 55
Self-citationOxidative Stress and Antioxidant Status in Hypo- and Hyperthyroidism
Petrulea, M. S., Mureșan, A., & Dunce, I. (2012) · InTech eBooks · doi:10.5772/51018 · Cited by 56
Mohamed, H. I. (2011) · Biological Trace Element Research · doi:10.1007/s12011-011-9058-1 · Cited by 54
McCord, J. M. (1976) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-3270-1_45 · Cited by 54
Kim, S. C., Kim, I. K., Seo, K. K., Baek, K. J., & Lee, M. Y. (1997) · Urological Research · doi:10.1007/bf01294663 · Cited by 54
Prakash, O., Teng, S., Ali, M., Zhu, X., Coleman, R., Dabdoub, R., Chambers, R. B., Aw, T. Y., Flores, S. C., & Joshi, B. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0168 · Cited by 52
Isoherranen, K., Peltola, V. T., Laurikainen, L., Punnonen, J., Laihia, J. K., Ahotupa, M. O., & Punnonen, K. R. A. (1997) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(97)00071-7 · Cited by 54
Julicher, R. H. M., Sterrenberg, L., Bast, A., Riksen, R. O. W. M., Koomen, J. M., & Noordhoek, J. (1986) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.1986.tb04566.x · Cited by 54
Borders, C. L., & Fridovich, I. (1985) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(85)90572-7 · Cited by 54
Self-citationCarrillo, M.-C., Kitani, K., Kanai, S., Sato, Y., & Ivy, G. O. (1992) · Life Sciences · doi:10.1016/0024-3205(92)90528-w · Cited by 54
Bakthavatchalu, V., Dey, S., Xu, Y., Noel, T. J., Jungsuwadee, P., Holley, A. K., Dhar, S. K., Batinic-Haberle, I., & Clair, D. K. S. (2011) · Oncogene · doi:10.1038/onc.2011.407 · Cited by 54
Castillo‐Martín, M., Bonet, S., Morató, R., & Yeste, M. (2014) · Cryobiology · doi:10.1016/j.cryobiol.2014.03.001 · Cited by 53
Free Radicals and Oxygen Toxicity
Buechter, D. D. (1988) · Pharmaceutical Research · doi:10.1023/a:1015914418014 · Cited by 53
Superoxide Radical and the Bactericidal Action of Phagocytes
Fridovich, I. (1974) · New England Journal of Medicine · doi:10.1056/nejm197403142901112 · Cited by 53
Self-citationFee, J. A., Shapiro, E. R., & Moss, T. H. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33074-0 · Cited by 53
A MYCOPLASMA-LIKE ARCHAEBACTERIUM POSSIBLY RELATED TO THE NUCLEUS AND CYTOPLASM OF EUKARYOTIC CELLS
Searcy, D. G., Stein, D. B., & Searcy, K. B. (1981) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1981.tb54373.x · Cited by 53
Molecular and functional aspects of superoxide dismutases
Gärtner, A., & Weser, U. (2005) · Springer eBooks · doi:10.1007/bfb0018063 · Cited by 52
Basu, S., Kumari, S., Kumar, P., Kumar, G., & Rajwanshi, R. (2021) · Physiologia Plantarum · doi:10.1111/ppl.13387 · Cited by 51
Pérez‐Jiménez, A., Hidalgo, M. C., Morales, A. E., Arizcún, M., Abellán, E., & Cardenete, G. (2009) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2009.07.011 · Cited by 51
Cardioprotective effects of nitrite during exercise
Calvert, J. W. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq307 · Cited by 51
Martí, J. I., Martı́, E., Cebrián-Pérez, J. Á., & Muiño-Blanco, T. (2003) · Theriogenology · doi:10.1016/s0093-691x(03)00105-5 · Cited by 51
Roche, H., & Bogé, G. (1993) · Toxicology in Vitro · doi:10.1016/0887-2333(93)90096-n · Cited by 51
The trail to superoxide dismutase
Fridovich, I. (1998) · Protein Science · doi:10.1002/pro.5560071225 · Cited by 51
Self-citationMaestro, R. F. D., & McDonald, W. (1989) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(89)90022-5 · Cited by 51
Physiological Responses of Bacteroides and Clostridium Strains to Environmental Stress Factors
Woods, D., & Jones, D. T. (1987) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60236-2 · Cited by 50
Palma, J. M., Sandalio, L. M., & del Río, L. A. (1986) · Journal of Plant Physiology · doi:10.1016/s0176-1617(86)80006-2 · Cited by 51
Yang, X., Zhuang, J., Rao, K., Xiao, L., & Zhao, R. (2010) · Research in Veterinary Science · doi:10.1016/j.rvsc.2010.04.003 · Cited by 50
Manganese superoxide dismutase from a higher plant
Sevilla, F., Lopez-Gorge, J., Gómez, M., & del Río, L. A. (1980) · Planta · doi:10.1007/bf00582359 · Cited by 50
Chloroplast manganese and superoxide
Lumsden, J., & Hall, D. O. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90363-0 · Cited by 50
Analysis of Superoxide Dismutase Activity
McCord, J. M. (1999) · Current Protocols in Toxicology · doi:10.1002/0471140856.tx0703s00 · Cited by 49
Genther, O., & Hansen, S. L. (2014) · Journal of Animal Science · doi:10.2527/jas.2013-7066 · Cited by 49
Lucigenin and linoleate enhanced chemiluminescent assay for superoxide dismutase activity
Laihia, J. K., Jansén, C. T., & Ahotupa, M. O. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90102-z · Cited by 49
Zhang, Q., Shen, M., Ding, M., Shen, D., & Ding, F. (2011) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2011.02.006 · Cited by 49
Quercetin in Hypoxia-Induced Oxidative Stress: Novel Target for Neuroprotection
Pandey, A. K., Patnaik, R., Muresanu, D. F., Sharma, A., & Sharma, H. S. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00005-3 · Cited by 49
Schininà, M. E., Carlini, P., Polticelli, F., Zappacosta, F., Bossa, F., & Calabrese, L. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0433k.x · Cited by 49
Manganese superoxide dismutase content and localization in human thyroid tumours
Nishida, S., Akai, F., Iwasaki, H., Hosokawa, K., Kusunoki, T., Suzuki, K., Taniguchl, N., Hashimoto, S., & Tamura, T. T. (1993) · The Journal of Pathology · doi:10.1002/path.1711690311 · Cited by 49
Hydroxylation of p‐Coumaric Acid by Illuminated Chloroplasts
Halliwell, B. B. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb02169.x · Cited by 49
Cross-tolerance to hyperoxia following cadmium aerosol pretreatment
Hart, B. A. (1990) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(90)90228-m · Cited by 49
Paine, A. J. (1978) · Biochemical Pharmacology · doi:10.1016/0006-2952(78)90023-0 · Cited by 49
Hernández, J. A., Díaz‐Vivancos, P., Martínez-Sánchez, G., Alburquerque, N., Martínez‐Romero, D., Barba‐Espín, G., Acosta‐Motos, J. R., Carrera, E., & Brunton, J. G. (2021) · Scientia Horticulturae · doi:10.1016/j.scienta.2021.109957 · Cited by 48
Suzuki, K. A. O., Ito, Y., Ochiai, J., Aoki, K., Wakai, K., Tamakoshi, A., Ando, M., Watanabe, Y., Ozasa, K., Seki, N., et al. (2003) · Journal of Epidemiology · doi:10.2188/jea.13.29 · Cited by 49
Becana, M., Paris, F. J., Sandalio, L. M., & del Río, L. A. (1989) · PLANT PHYSIOLOGY · doi:10.1104/pp.90.4.1286 · Cited by 48
Massie, H. R., Aiello, V. R., & Williams, T. R. (1980) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(80)90051-2 · Cited by 48
Tamari, Y., Nawata, H., Inoue, E., Yoshimura, A., Yoshii, H., Kashino, G., Seki, M., Enomoto, T., Watanabe, M., & Tano, K. (2012) · Free Radical Research · doi:10.3109/10715762.2012.734916 · Cited by 47
Domogauer, J., de Toledo, S. M., Howell, R. W., & Azzam, E. I. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00711-4 · Cited by 48
Signal Generation, Acquisition, and Processing in Brain Machine Interfaces: A Unified Review
Salahuddin, U., & Gao, P. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.728178 · Cited by 50
Mitochondrial Transplantation: A Novel Therapeutic Approach for Treating Diseases
Miao, X., Jiang, P., Wang, Z., Kong, W., & Feng, L. (2025) · MedComm · doi:10.1002/mco2.70253 · Cited by 54
Sehmer, L., Alaoui-Sossé, B., & Dizengremel, P. (1995) · Journal of Plant Physiology · doi:10.1016/s0176-1617(11)81427-6 · Cited by 46
Intracellular distribution of manganese and ferric superoxide dismutases in blue‐green algae
Okada, S., Kanematsu, S., & Asada, K. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81260-0 · Cited by 46
Julicher, R. H. M., Sterrenberg, L., Haenen, G. R. M. M., Bast, A., & Noordhoek, J. (1984) · Archives of Toxicology · doi:10.1007/bf00349076 · Cited by 45
Effects 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
Austin, F. E., Barbieri, J. T., Corin, R. E., Grigas, K. E., & Cox, C. D. (1981) · Infection and Immunity · doi:10.1128/iai.33.2.372-379.1981 · Cited by 45
Identification of superoxide dismutase in rat liver peroxisomes
Wanders, R. J. A., & Denis, S. W. (1992) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(92)90063-z · Cited by 45
Phillips, M., Camakaris, J., & Danks, D. M. (1986) · Biochemical Journal · doi:10.1042/bj2380177 · Cited by 45
Distribution of superoxide dismutase in rat brain
Thomas, T. N., Priest, D. G., & Zemp, J. W. (1976) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1976.tb01585.x · Cited by 45
Study of biochemical redox processes by the technique of pulse radiolysis
Avigdor Shafferman, C., & Stein, G. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(75)90002-6 · Cited by 45
Brown, C. O., Salem, K., Wagner, B. A., Bera, S., Singh, N., Tiwari, A., Choudhury, A., Buettner, G. R., & Goel, A. (2012) · Biochemical Journal · doi:10.1042/bj20112019 · Cited by 45
El-Naggar, M. M., El-Waseef, A., El-Halafawy, K. M., & Elsayed, I. (1998) · Cancer Letters · doi:10.1016/s0304-3835(98)00213-4 · Cited by 44
Sárközi, L., Horváth, E., Kónya, Z., Kiricsi, I., Szalay, B., Vezér, T., & Papp, A. (2009) · Inhalation Toxicology · doi:10.1080/08958370902939406 · Cited by 44
Pouyatos, B., Gearhart, C. A., & Fechter, L. D. (2004) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2004.08.015 · Cited by 44
Activities of free oxygen radical scavenger enzymes in human liver
Togashi, H., Shinzawa, H., Wakabayashi, H., Nakamura, T., Yamada, N., Takahashi, T. A., & Ishikawa, M. (1990) · Journal of Hepatology · doi:10.1016/0168-8278(90)90114-7 · Cited by 44
Shatzman, A. R., & Kosman, D. J. (1978) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(78)90220-9 · Cited by 44
Shibata, N., Hirano, A., Kobayashi, M., Canto, M. C. D., Gurney, M. E., Komori, T., Umahara, T., & Asayama, K. (1998) · Acta Neuropathologica · doi:10.1007/s004010050777 · Cited by 44
Superoxide constitutes a major signal of mitochondrial superoxide flash
Zhang, X., Huang, Z., Hou, T., Xu, J., Wang, Y., Shang, W. H., Ye, T., Cheng, H., Gao, F., & Wang, X. (2013) · Life Sciences · doi:10.1016/j.lfs.2013.06.012 · Cited by 43
L-Citrulline Supplementation and Exercise in the Management of Sarcopenia
Caballero-García, A., Pascual-Fernández, J., Noriega, D. C., Bello, H. J., Pons, A., Roche, E., & Córdova, A. (2021) · Nutrients · doi:10.3390/nu13093133 · Cited by 45
Localization of corneal superoxide dismutase by biochemical and histocytochemical techniques
Redmond, T. M., Duke, E. J., Coles, W. H., Simson, J. A. V., & Crouch, R. K. (1984) · Experimental Eye Research · doi:10.1016/0014-4835(84)90192-1 · Cited by 43
Superoxide anion production and superoxide dismutase and catalase activities in Coxiella burnetii
Akporiaye, E. T., & Baca, O. G. (1983) · Journal of Bacteriology · doi:10.1128/jb.154.1.520-523.1983 · Cited by 43
Henry, L. E. A., Cammack, R., Schwitzguébel, J., Palmer, J. M., & Hall, D. O. (1980) · Biochemical Journal · doi:10.1042/bj1870321 · Cited by 43
Kim, A. D., Kang, K. A., Piao, M. J., Kim, K. C., Zheng, J., Yao, C., Cha, J. W., Hyun, C. L., Kang, H. K., Lee, N. H., et al. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24790 · Cited by 42
Basu, S., Kumar, G., Kumari, N., Kumari, S., Shekhar, S., Kumar, S., & Rajwanshi, R. (2020) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2020.104118 · Cited by 42
The purification and properties of superoxide dismutase from a blue-green alga
Misra, H. P., & Keele, B. B. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90148-8 · Cited by 42
Ukeda, H., Sarker, A. K., Kawana, D., & Sawamura, M. (1999) · Analytical Sciences · doi:10.2116/analsci.15.353 · Cited by 41
The Evolutionary Origin of the Mitochondrion: A Nonsymbiotic Model
Mahler, H. R., & Raff, R. A. (1976) · International review of cytology · doi:10.1016/s0074-7696(08)60067-4 · Cited by 41
Walters, M. N., Papadimitriou, J. M., & Spector, W. G. (1978) · Critical Reviews in Toxicology · doi:10.3109/10408447809081012 · Cited by 43
A MYCOPLASMA-LIKE ARCHAEBACTERIUM POSSIBLY RELATED TO THE NUCLEUS AND CYTOPLASM OF EUKARYOTIC CELLS
Searcy, D. G., Stein, D. B., & Searcy, K. B. (1981) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1981.tb46527.x · Cited by 41
Genther, O., & Hansen, S. L. (2014) · Journal of Animal Science · doi:10.2527/jas.2013-7426 · Cited by 40
Purification and characterization of superoxide dismutase from chicken liver
Ürek, R. Ö., & Tarhan, L. (2001) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(00)00300-6 · Cited by 41
Metadata
- Authors
- Weisiger, R. A., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1973-05
- Volume
- 248
- Issue
- 10
- Pages
- 3582-3592
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1580575515
- Cited by
- 895
- References
- 37
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 11 · 2021: 19 · 2020: 20 · 2019: 18 · 2018: 15 · 2017: 13 · 2016: 9 · 2015: 12 · 2014: 25 · 2013: 13 · 2012: 23
- FWCI
- 35.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- 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
- Keywords
- superoxide dismutase, chicken liver, mitochondrial superoxide dismutase, cytosolic superoxide dismutase, manganese superoxide dismutase, copper-zinc superoxide dismutase, enzyme purification, enzyme inactivation, cyanide inhibition, endosymbiotic origin of mitochondria, autoreduction, porcine heart
- MeSH terms
- Amino Acids, Animals, Chickens, Copper, Cytoplasm, Cytosol, Electrophoresis, Disc, Isoelectric Focusing, Liver, Manganese, Mitochondria, Liver, Molecular Weight, Myocardium, Oxidation-Reduction, Oxidoreductases, Species Specificity, Superoxide Dismutase, Swine, Ultracentrifugation, Zinc
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