Cited by 895Metal-Catalyzed Oxygenation MechanismsGlutathione Transferases and PolymorphismsRedox biology and oxidative stress

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 access

Weisiger, Richard A., Fridovich, Irwin·1973·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)43969-0

Open this paper in CoChat — free account

Abstract

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.

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(19)43969-0

Cites

38 of 38 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.
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
Superoxide Dismutase
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Self-citation
Superoxide 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-citation
Spectroscopic 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
ORIGIN OF EUKARYOTIC CELLS
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

Show all 37 references

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

Sorted by citations

Items 801–895 of 895

Dietary Fatty Acids, Redox Signaling, and the Heart
Beam, J., Botta, A. M., Barendregt, R., & Ghosh, S. (2014) · Springer eBooks · doi:10.1007/978-3-642-30018-9_44 · Cited by 3
Intracellular Oxygen Concentration Determined By Mitochondrial Respiration Regulates Production of Reactive Oxygen Species.
Wiese, A. K., Prior, S., Chambers, T. C., & Higuchi, M. (2017) · PubMed · Cited by 3
Measuring Activities of the Enzymes Superoxide Dismutase and Glutathione Reductase in Lichens
Thomas, M. A. (2002) · Springer eBooks · doi:10.1007/978-3-642-56359-1_12 · Cited by 3
The Role of Nitric Oxide in the Peripheral Nervous System
Martin, W. (2000) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-57077-3_13 · Cited by 3
Purification and characterization of canine manganese superoxide dismutase and its immunohistochemical localization in canine heart compared with that of copper-zinc superoxide dismutase
Ikeda, K., Matsumi, S., Magara, T., & Nakagawa, S. (1995) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/1357-2725(95)00108-2 · Cited by 3
The Effect of Vitamin E-Deficiency in Isolated Rat Heart on the Cellular Defence System Against Free Radicals During Normal Reperfusion After Hypoxic, Ischemic and Ca2+-Free Perfusion
Julicher, R. H. M., Sterrenberg, L., Walenbergh, L. H., Bast, A., & Noordhoek, J. (1986) · Free Radical Research Communications · doi:10.3109/10715768609083153 · Cited by 3
Mitochondrial Function and Neurodegenerative Diseases
Wilkins, H. M., Weidling, I., Koppel, S., Wang, X., von Schulze, A., & Swerdlow, R. H. (2018) · The Molecular and Cellular Basis of Neurodegenerative Diseases · doi:10.1016/b978-0-12-811304-2.00013-4 · Cited by 2
Zinc Oxide Nanoparticles Affect the Genomic and Redox Status of Chicken Embryo—Influence of Shape
Dominiak, B., Rosowska, J., Wal, A., Majewska, A., Witkowski, B. S., Wachnicki, Ł., Kaszewski, J., Słońska, A., Cymerys, J., Gralak, M. A., et al. (2025) · Nanomaterials · doi:10.3390/nano15181412 · Cited by 2
Biological and Biochemical Studies on the Effect of Gamma Radiation on Post-Mating Changes in the Honeybee Queen (Apis mellifera)
Sawires, S. G., Elbassiouny, A., Abdel-Monsef, M. M., & Darwish, D. A. (2025) · Entomological News · doi:10.3157/021.132.0510 · Cited by 2
Altered Phenotypes in Saccharomyces cerevisiae by Heterologous Expression of Basidiomycete Moniliophthora perniciosa SOD2 Gene
Melo, S. C. O., Santos, R. X., Melgaço, A. C. C., Pereira, A., Pungartnik, C., & Brendel, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160612324 · Cited by 2
Purification and Characterization of Cu, Zn Superoxide Dismutase from Ark ShellScapharca broughtonii
Kim, Y., Park, S., & Kim, S. (1998) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.62.2211 · Cited by 2
An improved method for the separation of CuZn-superoxide dismutase from human erythrocytes by gel electrophoresis
Lickl, E. (1987) · Chromatographia · doi:10.1007/bf02324872 · Cited by 2
Insilico docking for validation of drug leads on Superoxide dismutase of Homo sapiens and Plasmodium falciparum.
Bernhardt, V. G., Pinto, J. R. T., & Pai, V. R. (2010) · Biomedical Research-tokyo · Cited by 2
Oxidative Stress
Madamanchi, N. R., & Runge, M. S. (2007) · Humana Press eBooks · doi:10.1007/978-1-59259-878-6_30 · Cited by 2
The Efficacy and Safety of GF101 and Its Antioxidant Effect on In Vitro Fertilization Outcomes: A Double-Blind, Non-Inferiority, Randomized, Controlled Trial with Coenzyme Q10
Shin, S. Y., Yoon, H. K., Kim, J. H., Kim, J. H., Park, C., Choi, D. H., Yu, Y. D., Shin, J. E., & Kwon, H. (2024) · Antioxidants · doi:10.3390/antiox13030321 · Cited by 2
Phlorotannins and their biological significances.
Pullaiah, C. P., Kedam, T., Nelson, V., Kumar, G., Babu, B. G. B., & Reddy, D. V. L. (2018) · Cited by 2
The inhibition of manganese superoxide dismutase by cacodylate
Thornalley, P. J., Sarchet, A. W., Hill, H. A. O., Bannister, J. V., & BANNISTER, W. H. (1982) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)85043-4 · Cited by 2
Post-Embedding Immuno-Electron Microscopy with Rapid Freezing and Freeze-Substitution Techniques for the Localization of Manganese Superoxide Dismutase.
Tatsumi, H., Suzuki, K., Senda, T., SATOH, S., Fujita, H., & Taniguchi, N. (1991) · Archivum histologicum japonicum · doi:10.1679/aohc.54.465 · Cited by 2
Cardiac Defense Mechanisms against Oxidative Damage: The Role of Superoxide Dismutase and Glutathione-Related Enzymes
Ishikawa, T. (1988) · Developments in cardiovascular medicine · doi:10.1007/978-1-4613-1743-2_7 · Cited by 2
Copper deficiency in Blesbok (aliscus pygargus phillipsi) from the Karoo Nature Reserve
Quan, M. (2001) · Cited by 2
Trace Elements in Total Parenteral Nutrition
Jeejeebhoy, K. N. (1990) · Springer eBooks · doi:10.1007/978-4-431-68120-5_27 · Cited by 2
GENETICS OF HUMAN SUPEROXIDE DISMUTASE ISOZYMES
Beckman, G., & Beckman, L. E. (1975) · Elsevier eBooks · doi:10.1016/b978-0-12-472704-5.50053-7 · Cited by 2
Synaptic and Neuroglial Pathobiology in Acute and Chronic Neurological Disorders
Martin, L. J. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-105-3_25 · Cited by 1
Field evaluation of Trichoderma harzianum grown on different media for the management of potato root-knot nematode and enhancement of enzymatic antioxidant activities
Elkelany, U. S., Masoud, H. M. M., El-Mougy, N. S., & Abdel-Kader, M. M. (2026) · Journal of the Saudi Society of Agricultural Sciences · doi:10.1007/s44447-026-00140-0 · Cited by 1
Preparation of bacoside A encapsulated PLGA-PEG nanoparticles for neuroprotection against kainic acid-induced excitotoxicity
Sekhar, V. C., Baby, S., & Viswanathan, G. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02315-1 · Cited by 1
Effect of Dietary Krill Meal on the Performance of Broiler Chicks During the Acute Phase Response
Koh, T. S. (2004) · Journal of Animal Science and Technology · doi:10.5187/jast.2004.46.2.173 · Cited by 1
Copper metabolism and copper-mediated alterations in the metabolism of cultured astrocytes
Scheiber, I. F. (2012) · State and University Library Bremen · Cited by 1
The kinetic substitution reactions and structural analysis of manganese(I) acetylacetonato complexes
Mokolokolo, P., Alexander, O. T., Brink, A., & Visser, H. G. (2021) · Polyhedron · doi:10.1016/j.poly.2021.115121 · Cited by 1
Role of Mitochondria and Oxidative Stress in Parkinson’s Disease
Santos, R. X., Correia, S. C., Cardoso, S., Carvalho, C., Candeias, E., Plácido, A. I., Duarte, A. I., Santos, M. S., & Moreira, P. I. (2014) · CRC Press eBooks · doi:10.1201/b16653-26 · Cited by 1
Role of Oxidized Lipids in Atherosclerosis
Garelnabi, M., Kakumanu, S., & Litvinov, D. Y. (2012) · InTech eBooks · doi:10.5772/32999 · Cited by 2
Superoxide, superoxide dismutases, and cardiovascular dysfunction
Cole, M. P., Chaiswing, L., Oberley, T. D., Kiningham, K. K., & Clair, D. K. S. (2002) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(02)11033-9 · Cited by 1
Activity and electrophoretic multiplicity of molecular forms of superoxide dismutase in human blood cells
Гусев, В. А., Lamchingiĭn, T., & Gerasimov, A. M. (1977) · Bulletin of Experimental Biology and Medicine · doi:10.1007/bf00799193 · Cited by 1
Immunohistochemical localization of CuZn-superoxide dismutase in human uterine cervix and cervical cancer.
Shiotani, M., Noda, Y., Narimoto, K., Mori, T., & Ogawa, K. (1993) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.26.57 · Cited by 1
Ageing transition of superoxide dismutase in rat retina
Ogawa, T., Ohira, A., & Amemiya, T. (1998) · The Histochemical Journal · doi:10.1023/a:1003228326884 · Cited by 1
Subcellular Localization and Identification of Superoxide Dismutase Isoenzymes from Pennisetum typhoideum Seedlings
Reddy, S. V. K., & Venkaiah, B. (1984) · Journal of Plant Physiology · doi:10.1016/s0176-1617(84)80018-8 · Cited by 1
Protective effect of copper against pancreatic insult in streptozotocin-induced diabetogenic rat
Kim, H., Jhoo, W. K., Kim, K. H., Kim, J. T., Lee, S. J., & Hur, I. H. (1990) · Archives of Pharmacal Research · doi:10.1007/bf02857787 · Cited by 1
Effect of manganese on the hepatic microsomal mixed function oxidase enzyme system in the rat
Deimling, M. J. (1984) · Fundamental and Applied Toxicology · doi:10.1016/0272-0590(84)90240-9 · Cited by 1
O papel do fator de transcrição mitocondrial A (TFAM) na proteção do DNA mitocondrial contra lesões oxidadas
Tonolli, P. N. (2014) · doi:10.11606/d.46.2014.tde-29042014-144505 · Cited by 1
El pulmón como órgano diana del estrés oxidativo. radicales libres y especies activas del oxígeno
Alvira, D. R., Ariño, A. S., Lamban, F. C., Villacampa, M. M., & Martin, M. P. V. (1990) · Archivos de Bronconeumología · doi:10.1016/s0300-2896(15)31560-x · Cited by 1
Copper-Manganese Interactions Concerning Red-Cell and Plasma Lipid Peroxidation
Fernandes, A. C., & Manso, C. (1988) · Free Radical Research Communications · doi:10.3109/10715768809066927 · Cited by 1
Using patient-derived cell models to investigate the role of misfolded SOD1 in ALS
Forsgren, E. (2017) · DiVA at Umeå University (Umeå University) · Cited by 1
Developmental Regulation of Mitochondrial Function in Ovine Fetal Skeletal Muscle
Davies, K. (2018) · Apollo (University of Cambridge) · doi:10.17863/cam.22845 · Cited by 1
The SOD-2 protein is the single active SOD enzyme in C. elegansPreprint
Fernando, L. M., Adeel, S., Basar, M. A., Allen, A. K., & Duttaroy, A. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.08.12.247973 · Cited by 1
Molecular evolution and the fate of the mitochondrion in microsporidia parasites
Williams, B. A. P. (2003) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 1
Reactive Oxygen Species-Toxicity, Metabolism, and Reactions in the Eye
Buckley, B., & Freeman, B. Α. (1987) · Cell and developmental biology of the eye · doi:10.1007/978-1-4612-4784-5_6 · Cited by 1
Misfolded superoxide dismutase-1 in sporadic and familial Amyotrophic Lateral Sclerosis
Forsberg, K. (2011) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1
Mecanismos de proliferación dependientes del estado redox celular: rol de AKT y otras kinasas involucradas en la progresión del ciclo celular
Arciuch, A., & Gabriela, V. (2009)
The antioxidant properties of 4–quinolones compared to structurally related flavonoids
Greeff, J. (2009)
Age-Specific Difference in Pulmonary Cellular Injury and Mitochondrial Damage
Tuggle, K. L., & Fanucchi, M. V. (2014) · Respiratory medicine · doi:10.1007/978-1-4939-0829-5_9
The role of MnSOD and sirtuin 3 in thymocyte responses to radiation and lymphomagenesis
Mao, G. (2013) · doi:10.17077/etd.xlb9pe09
METHODS DEVELOPMENT AND APPLICATION OF TWO-DIMENSIONAL GEL ELECTROPHORESIS AND MASS SPECTROMETRY IN PROTEOMICS
Rajagopal, M. U. (2006) · UKnowledge (University of Kentucky)
TARGETING THE METAL CHELATOR D-PENICILLAMINE TO EXPLOIT THE ELEVATED COPPER AND OXIDATIVE STRESS ASSOCIATED WITH CANCER
Gupte, A. (2008)
DIFFERENTIATION-INDUCED CHANGES IN ANTIOXIDANT CAPACITY AND ANTIOXIDANT RESPONSE IN SH-SY5Y CELLS: ROLE OF NRF2
Karikari, A. A. (2013) · The Mathematics Enthusiast
Listing of Protein Spectra
Kirschenbaüm, D. M. (1984) · Springer eBooks · doi:10.1007/978-1-4684-8836-4_1
ALS and the Copper Chaperone CCS
Son, M., & Elliott, J. L. (2011) · Wiley eBooks · doi:10.1002/9781118063903.ch10
Extracellular Superoxide Dismutase and Matrix Metalloproteinases in Pulmonary Fibrosis
Tan, R. J. (2005) · D-Scholarship@Pitt (University of Pittsburgh)
The NO-cytochrome C Oxidase Signaling Pathway; Mechanisms and Biological Implications
Shiva, S., Levonen, A., Barone, M. C., & Darley-Usmar, V. M. (2003) · Springer eBooks · doi:10.1007/0-306-48412-9_15
Experimental study on the effect of superoxide dismutase and peplomycin on implanted VX2 tongue carcinoma of the domestic rabbits.
Imamura, H. (1994) · Japanese Journal of Oral & Maxillofacial Surgery · doi:10.5794/jjoms.40.870
S.W.A.T.--SOD Weapons and Tactics
Sampayo, J. N., & Lithgow, G. J. (2004) · Science of Aging Knowledge Environment · doi:10.1126/sageke.2004.25.pe27
This student paper was written as an assignment in the graduate course Free Radicals in Biology and Medicine
Buettner, G. R., Oberley, L. W., Spitz, D. R., & Domann, F. E. (2003)
EFECTOS ANTICANCEROSOS DE POLIFENOLES NATURALES: PETEROSTILBENO Y QUERCETINA
Pastor, P. F. (2008) · TDX (Tesis Doctorals en Xarxa)
Mutant Superoxide Dismutase-1-caused pathogenesis in Amyotrophic Lateral Sclerosis
Bergemalm, D. (2010) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Nitrotyrosine immunoreactivity in gerbil hippocampal CA1 region after transient forebrain ischemia
Asai, S., Murata, A., Tamagaki, C., Sakata, T., Gonno, K., Takase, K., & Kinoshita, T. (1999) · Neuropathology · doi:10.1046/j.1440-1789.1999.00249.x
Urinary 1,4-dihydroxynonene mercapturic acid (DHN- MA) and 8-hydroxy-2'-deoxyguanosine (8-OHdG) as markers of oxidative damage: The SABPA study
Steenkamp, L. (2010) · Boloka Institutional Repository (North-west University)
Superoxide dismutase and pulm ,on ary oxygen toxicity
Crap, J. D., & Tierney, D. F. (1974)
The Effects of Two Modes of Exercise Training on Plasma Biomarkers of Inflammation and Oxidative Stress in Patients with Symptomatic Peripheral Artery Disease
Salisbury, D. L. (2014) · University of Minnesota Digital Conservancy (University of Minnesota)
REGULATION OF THE OXIDATIVE STRESS RESPONSE BY ARID1A
Kwan, S. Y. (2015) · Digital Commons-TMC (Texas Medical Center)
Superoxide Dismutase Activity of Heart and Liver Tissue from Copper Deficient Rats
Mylroie, A. A., Umbles, C., & Kyle, J. (1987) · Humana Press eBooks · doi:10.1007/978-1-4612-4584-1_41
Efeitos do tratamento oncológico no estado nutricional, nos marcadores de estresse oxidativo e na qualidade de vida de pacientes com câncer de estômago e de esôfago
Knack, R. A. (2016) · doi:10.11606/d.17.2016.tde-06012016-154601
Disruption Characteristics of Bakers' Yeast with High-pressure Homogenizer.
YOSHIKAWA, Y., Anh Dao Thi, D. O. N. G., Xing, X., & Matsumoto, K. (1999) · Journal of the Society of Powder Technology Japan · doi:10.4164/sptj.36.534
Oxidative stress induced in tobacco leaves by chloroplast over-expression of maize plastidial transglutaminase
Pintó‐Marijuan, M. (2010)
Resistance Loading and Signaling Assays for Oxidative Stress in Rodent Skeletal Muscle
Alway, S. E., & Cutlip, R. G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-343-1_11
Superoxide AnionProduction andSuperoxide Dismutase and Catalase Activities inCoxiella burnetii
Akporiayeandoswaldg, E. T. (1983)
Metabolism of Superoxide Radicals and Hydrogen Peroxide in Mitochondria
Marinho, H. S., & Antunes, F. (2015) · Oxidative stress and disease · doi:10.1201/b19420-3
Folding and Stability Studies on Amyotrophic Lateral Sclerosis-Associated apo Cu, Zn Superoxide dismutases
Vassall, K. A. (2009) · UWSpace (University of Waterloo)
THE RADIOSENSITIZATION EFFECT OF PARTHENOLIDE IN PROSTATE CANCER: IMPLICATIONS FOR SELECTIVE CANCER KILLING BY MODULATION OF INTRACELLULAR REDOX STATE
Sun, Y. (2010) · UKnowledge (University of Kentucky)
Development Of Chemical Tools To Investigate Protein S-Glutathionylation In Response To Metabolic Alteration
Samarasinghe, K. T. G. (2017) · Human Biology
Photosensitization of Lipofuscin in Skin Keratinocytes: Effect of Visible Light on Human Skin
Tonolli, P. N. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.46.2018.tde-12122018-114252 · Cited by 1
Catecholamine metabolism via monoamine oxidase (MAO) within myocardium of individuals with type 2 diabetes
Nelson, M. A. M. (2019) · The Scholarship East Carolina University's Institutional Repository (East Carolina University)
PERCEPTION ON MARINE NATURAL PRODUCTS FROM BROWN ALGAE AND ITS PHARMACOLOGICAL REVIEW
Rajan, H., Selva Kumari, E., & Arumugam (2020) · Journal of Emerging Technologies and Innovative Research
EFFECT OF ACTIVITY AND ENVIRONMENTAL IMPACTS ON THE ANTIOXIDANT DEFENCES OF VARIOUS AIR-BREATHING TELEOST FISHES
Singh, S. K., & Bhat, R. A. (2020) · UTTAR PRADESH JOURNAL OF ZOOLOGY
ENDOGENOUS ANTIOXIDANT COMPLEX AND SUPEROXIDE DISMUTASE PERFORMED IN SOME NON-AIRBREATHING FISHES
Singh, S. K., & Bhat, R. A. (2020) · UTTAR PRADESH JOURNAL OF ZOOLOGY
Protective effects of N-acetylcysteine on myocardial injury induced by acute fluctuations in blood glucosePreprint
Zhang, W., Peng, G., Zhao, S., Li, Y., Han, P., & Li, Y. (2020) · doi:10.21203/rs.3.rs-30269/v1
Chapter 1 Antioxidant systems in animal body
Surai, P. F. (2018) · Wageningen Academic Publishers eBooks · doi:10.3920/978-90-8686-865-0_1
Chapter 4: Superoxide dismutases (SODs)
Surai, P. F. (2020) · Wageningen Academic Publishers eBooks · doi:10.3920/978-90-8686-906-0_4
Bibliography
(1978) · Elsevier eBooks · doi:10.1016/b978-0-12-575550-4.50019-6
Aging
Sun, A. Y., Sun, G. Y., & Foudin, L. L. (1985) · Springer eBooks · doi:10.1007/978-1-4757-6740-7_7
Succinate Dehydrogenase in Mitochondrial Disorders
Tripathi, S., Sharma, Y., & Kumar, D. (2025) · Springer eBooks · doi:10.1007/978-981-96-6831-1_5
Redox processes in male Drosophila with the cd mutation
Zhuravlev, A. V., Vetrovoy, O. V., Potapova, S., & Savvateeva-Popova, E. V. (2025) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2025.104871
Stimulus response coupling in the carotid body: a role for metabolic signalling
Holmes, A. P. (2013) · University of Birmingham Institutional Research Archive (University of Birmingham)
Oxygen Utilization and Toxicity in the Lungs
Fisher, A. B., & Forman, H. J. (1985) · Comprehensive physiology · doi:10.1002/j.2040-4603.1985.tb01035.x
Récepteurs cutanés à la mélanocortine de type 1 (MC1R) et réponses oxydatives aux UVA dans des kératinocytes humains HaCaT
Henri, P. (2010) · theses.fr (ABES) · doi:10.70675/3d9b68e3z3ff2z4f0czae15z1e7b3d7b9f58
Attenuation of oxidative phosporylation and induction of hypoxic celle response : [alpha]-tocopherolacetate and miR-210 effects on mesenchymal stromal cells
Loncaric, D. (2019) · theses.fr (ABES) · doi:10.70675/688931baz6abdz4f1czb8adzdbf8c07ba500
Blood SOD1 Activity in ALS Patients Receiving Tofersen Treatment
Goehring, K., Abler, E., Vavra, J., Mayer, K., Dorst, J., Elmas, Z., Wiesenfarth, M., Richter, L., Petri, S., Regensburger, M., et al. (2026) · Annals of Neurology · doi:10.1002/ana.78328
Mitochondrion: A Novel Center for Cancer Cell Signaling
Miriyala, S., Holley, A. K., & Clair, D. K. S. (2014) · Springer eBooks · doi:10.1007/978-94-017-8984-4_1

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)
DOI: 10.1016/s0021-9258(19)43969-0
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 17333 d)
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

Superoxide Dismutase

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks