Oxygen toxicity, oxygen radicals, transition metals and disease

Halliwell, B; Gutteridge, J M C

doi:10.1042/bj2190001

Cited by 5,330Neutrophil, Myeloperoxidase and Oxidative MechanismsRedox biology and oxidative stressNitric Oxide and Endothelin Effects

Oxygen toxicity, oxygen radicals, transition metals and disease

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Halliwell, B, Gutteridge, J M C·1984·Biochemical Journal

DOI 10.1042/bj2190001PMC PMC1153442

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produce °2-include neutrophils, monocytes, macrophages and eosino- phils.

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Reactions of peroxide and superoxide with poorly liganded iron species can lead to catalytic production of the very reactive and dangerous hydroxyl radical, which is exceptionally damaging and a major cause of chronic inflammation.
“Possibly the commonest means by which such much more damaging species, in particular the hydroxyl radical, are created is by reaction with unliganded or incompletely liganded iron ions [61-63].”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [61]
The commonest means by which hydroxyl radical is created is reaction with unliganded or incompletely liganded iron ions.
“Possibly the commonest means by which such much more damaging species, in particular the hydroxyl radical, are created is by reaction with unliganded or incompletely liganded iron ions [61-63].”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [61]

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Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827 · see citing works
Untitled work
Fridovich (1978) · doi:10.1126/science.210504 · Cited by 3,329 · see citing works
Oxygen-Dependent Microbial Killing by Phagocytes
BABIOR, B. M. (1978) · New England Journal of Medicine · doi:10.1056/nejm197803232981205 · Cited by 2,483 · see citing works
Superoxide Dismutases
Fridovich, I. (1975) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.44.070175.001051 · Cited by 1,735 · see citing works
The Liver: Biology and Pathobiology
Carey, W., & Fleshler, B. (1983) · JAMA · doi:10.1001/jama.1983.03330310070041 · Cited by 1,479 · see citing works
Mechanisms of lipid peroxide formation in animal tissues
Wills, E. D. (1966) · Biochemical Journal · doi:10.1042/bj0990667 · Cited by 1,348 · see citing works
Iron and infection
Weinberg, E. D. (1978) · Microbiological Reviews · doi:10.1128/mmbr.42.1.45-66.1978 · Cited by 1,254 · see citing works
Iron Transport and Storage Proteins
Aisen, P., & Listowsky, I. (1980) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.49.070180.002041 · Cited by 1,179 · see citing works
Superoxide Radical: An Endogenous Toxicant
Fridovich, I. (1983) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.23.040183.001323 · Cited by 1,168 · see citing works
Free Radicals and Inflammation: Protection of Synovial Fluid by Superoxide Dismutase
McCord, J. M. (1974) · Science · doi:10.1126/science.185.4150.529 · Cited by 1,108 · see citing works
Role of superoxide dismutase in cancer: a review.
Oberley, L. W., & Buettner, G. R. (1979) · PubMed · Cited by 982 · see citing works
Superoxide‐dependent production of hydroxyl radical catalyzed by iron—EDTA complex
McCord, J. M., & Day, E. D. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80116-1 · Cited by 870 · see citing works
Formation of a thiobarbituric‐acid‐reactive substance from deoxyribose in the presence of iron salts
Halliwell, B. B., & Gutteridge, J. M. C. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80114-7 · Cited by 832 · see citing works
Self-citation
Oxidases and Related Redox Systems
(1982) · Elsevier eBooks · doi:10.1016/c2013-0-03176-3 · Cited by 768 · see citing works
Superoxide and Superoxide Dismutases
Sund, H. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)81216-2 · Cited by 755 · see citing works
Superoxide‐dependent formation of hydroxyl radicals in the presence of iron chelates
Halliwell, B. B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80779-0 · Cited by 743 · see citing works
Self-citation
A 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 · see citing works
Evidence that Peroxidation of Lysosomal Membranes Is Initiated by Hydroxyl Free Radicals Produced during Flavin Enzyme Activity
Fong, K.-L., McCay, P. B., Poyer, J. L., Keele, B. B., & Misra, H. P. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43258-4 · Cited by 650 · see citing works
Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine
Gutteridge, J. M. C., Richmond, R., & Halliwell, B. B. (1979) · Biochemical Journal · doi:10.1042/bj1840469 · Cited by 629 · see citing works
Self-citation
The significance of iron in infection
Bullen, J. J. (1981) · Clinical Infectious Diseases · doi:10.1093/clinids/3.6.1127 · Cited by 603 · see citing works
Oxidation of ascorbic acid with superoxide anion generated by the xanthine-xanthine oxidase system
Nishikimi, M. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90710-x · Cited by 567 · see citing works
A study of the reactivity of HO2/O2-with unsaturated fatty acids
Bielski, B. H., Arudi, R. L., & Sutherland, M. W. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32488-8 · Cited by 546 · see citing works
Free Radicals, Lipid Peroxidation and Cancer
Butler, J. (1982) · British Journal of Cancer · doi:10.1038/bjc.1982.283 · Cited by 514 · see citing works
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 · see citing works
Production of formaldehyde during metabolism of dimethyl sulfoxide by hydroxyl radical-generating systems
Klein, S. M., Cohen, G., & Cederbaum, A. I. (1981) · Biochemistry · doi:10.1021/bi00524a013 · Cited by 486 · see citing works
Copper- and zinc-containing superoxide dismutase, manganese-containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues.
Marklund, S. L., Westman, N. G., Lundgren, E., & Roos, G. (1982) · PubMed · Cited by 474 · see citing works
Superoxide-dependent formation of hydroxyl radicals in the presence of iron salts. Detection of ‘free’ iron in biological systems by using bleomycin-dependent degradation of DNA
Gutteridge, J. M. C., Rowley, D. A., & Halliwell, B. B. (1981) · Biochemical Journal · doi:10.1042/bj1990263 · Cited by 467 · see citing works
Self-citation
Spontaneous oxygen radical generation by sickle erythrocytes.
Hebbel, R. P., Eaton, J. W., Balasingam, M., & Steinberg, M. H. (1982) · Journal of Clinical Investigation · doi:10.1172/jci110724 · Cited by 441 · see citing works
Non‐Specific Serum Iron in Thalassaemia: an Abnormal Serum Iron Fraction of Potential Toxicity
Hershko, C., Graham, G. M., Bates, G. W., & Rachmilewitz, E. A. (1978) · British Journal of Haematology · doi:10.1111/j.1365-2141.1978.tb03662.x · Cited by 421 · see citing works
Hepatic lipid peroxidation in vivo in rats with chronic iron overload.
Bacon, B. R., Tavill, A. S., Brittenham, G. M., Park, C. H., & Recknagel, R. O. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110787 · Cited by 390 · see citing works
Spin Trapping of Superoxide
Finkelstein, E., Rosen, G. M., Rauckman, E. J., & Paxton, J. (1979) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)13797-8 · Cited by 372 · see citing works
Effect of oxygen‐derived free radicals on hyaluronic acid
Greenwald, R. A., & Moy, W. W. (1980) · Arthritis & Rheumatism · doi:10.1002/art.1780230408 · Cited by 363 · see citing works
Intracellular mechanisms for the decomposition of a lipid peroxide. I. Decomposition of a lipid peroxide by metal ions, heme compounds, and nucleophiles
O’Brien, P. J. (1969) · Canadian Journal of Biochemistry · doi:10.1139/o69-076 · Cited by 351 · see citing works
Evidence for role of hydroxyl radical in complement and neutrophil-dependent tissue injury.
Ward, P. A., Till, G. O., Kunkel, R., & Beauchamp, C. (1983) · Journal of Clinical Investigation · doi:10.1172/jci111050 · Cited by 336 · see citing works
Lactoferrin enhances hydroxyl radical production by human neutrophils, neutrophil particulate fractions, and an enzymatic generating system.
Ambruso, D. R., & Johnston, R. B. (1981) · Journal of Clinical Investigation · doi:10.1172/jci110042 · Cited by 334 · see citing works
Manganese, superoxide dismutase, and oxygen tolerance in some lactic acid bacteria
Archibald, F. S., & Fridovich, I. (1981) · Journal of Bacteriology · doi:10.1128/jb.146.3.928-936.1981 · Cited by 319 · see citing works
Superoxide‐dependent formation of hydroxyl radicals in the presence of iron salts
Halliwell, B. B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)80409-8 · Cited by 299 · see citing works
Self-citation
Interaction of Oxygen and Oxy-radicals With Carotenoids 1
Krinsky, N. I., & Deneke, S. M. (1982) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/69.1.205 · Cited by 298 · see citing works
Clinical Consequences of Acquired Transfusional Iron Overload in Adults
Schafer, A. I., Cheron, R. G., Dluhy, R., Cooper, B., Gleason, R. E., Soeldner, J. S., & Bunn, H. F. (1981) · New England Journal of Medicine · doi:10.1056/nejm198102053040603 · Cited by 293 · see citing works
Thiobarbituric acid‐reactivity following iron‐dependent free‐radical damage to amino acids and carbohydrates
Gutteridge, J. M. C. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80113-5 · Cited by 284 · see citing works
Self-citation
Lipid peroxide formation in microsomes. The role of non-haem iron
Wills, E. D. (1969) · Biochemical Journal · doi:10.1042/bj1130325 · Cited by 274 · see citing works
OCULAR TOXICITY OF HIGH-DOSE INTRAVENOUS DESFERRIOXAMINE
Davies, S., Hungerford, J. L., Arden, G. B., Marcus, R. E., Miller, M. H., & Huehns, E. R. (1983) · The Lancet · doi:10.1016/s0140-6736(83)90170-8 · Cited by 270 · see citing works
Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals
Winterbourn, C. C. (1979) · Biochemical Journal · doi:10.1042/bj1820625 · Cited by 266 · see citing works
Stimulated Human Phagocytes Produce Cytogenetic Changes in Cultured Mammalian Cells
Weitberg, A. B., Weitzman, S. A., Destrempes, M. M., Latt, S. A., & Stossel, T. P. (1983) · New England Journal of Medicine · doi:10.1056/nejm198301063080107 · Cited by 261 · see citing works
Lipid peroxidation: its measurement, occurrence, and significance in animal tissues.
Barber, A. A., & Bernheim, F. (1967) · PubMed · Cited by 253 · see citing works
Inhibition of lipid peroxidation by the iron-binding protein lactoferrin
Gutteridge, J. M. C., Paterson, S., Segal, A. W., & Halliwell, B. B. (1981) · Biochemical Journal · doi:10.1042/bj1990259 · Cited by 252 · see citing works
Self-citation
Hydroxyl radical production in body fluids Roles of metal ions, ascorbate and superoxide
Winterbourn, C. C. (1981) · Biochemical Journal · doi:10.1042/bj1980125 · Cited by 249 · see citing works
Oxygen Free Radicals and Tissue Damage
Halliwell, B. B. (1980) · FEBS Letters · doi:10.1016/0014-5793(80)81244-0 · Cited by 248 · see citing works
Self-citation
Copper salt-dependent hydroxyl radical formation
Gutteridge, J. M. C., & Wilkins, S. (1983) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(83)90186-1 · Cited by 243 · see citing works
Self-citation
Unusual copper-induced sensitization of the biological damage due to superoxide radicals.
Samuni, A. M., Chevion, M., & Czapski, G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42937-7 · Cited by 239 · see citing works
Superoxide-dependent formation of hydroxyl radicals: Detection of hydroxyl radicals by the hydroxylation of aromatic compounds
Richmond, R., Halliwell, B. B., Chauhan, J., & Darbre, A. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90590-x · Cited by 230 · see citing works
Self-citation
Superoxide-dependent formation of hydroxyl radicals and lipid peroxidation in the presence of iron salts. Detection of ‘catalytic’ iron and anti-oxidant activity in extracellular fluids
Gutteridge, J. M. C., Rowley, D. A., & Halliwell, B. B. (1982) · Biochemical Journal · doi:10.1042/bj2060605 · Cited by 217 · see citing works
Self-citation
Caeruloplasmin: Physiological and Pathological Perspectives
Gutteridge, J. M. C., & Stocks, J. (1981) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368109105866 · Cited by 217 · see citing works
Self-citation
Superoxide‐dependent formation of hydroxyl radicals in the presence of thiol compounds
Rowley, D. A., & Halliwell, B. B. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80388-8 · Cited by 213 · see citing works
Self-citation
Survival and desferrioxamine in thalassaemia major.
Modell, B., Letsky, E. A., Flynn, D. M., Peto, R., & Weatherall, D. J. (1982) · BMJ · doi:10.1136/bmj.284.6322.1081 · Cited by 205 · see citing works
Regulation of hydrogen peroxide in eye humors effect of 3-amino-1H-1,2,4-triazole on catalase and glutathione peroxidase of rabbit eye
Bhuyan, K. C., & Bhuyan, D. K. (1977) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(77)90284-7 · Cited by 201 · see citing works
Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals in the presence of copper salts: A physiologically significant reaction?
Rowley, D. A., & Halliwell, B. B. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90031-0 · Cited by 199 · see citing works
Self-citation
THE EFFECT OF IRON ON THE DISTRIBUTION OF SUPEROXIDE AND HYDROXYL RADICALS AS SEEN BY SPIN TRAPPING AND ON THE SUPEROXIDE DISMUTASE ASSAY
Buettner, G. R., Oberley, L. W., & Leuthauser, S. W. C. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb07001.x · Cited by 179 · see citing works
Free radicals and singlet oxygen scavengers: Reaction of a peroxy-radical with β-carotene, diphenyl furan and 1,4-diazobicyclo(2,2,2)-octane
Packer, J. E., Mahood, J. S., Mora-Arellano, V. O., Slater, T. F., WILLSON, R. L., & Wolfenden, B. S. (1981) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(81)91196-7 · Cited by 176 · see citing works
Superoxide dismutase activity of low molecular weight Cu2+‐chelates studied by pulse radiolysis
Brigelius, R., Spöttl, R., Bors, W., Lengfelder, E., Sarán, M., & Weser, U. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80428-x · Cited by 170 · see citing works
Vitamin C and Iron
Nienhuis, A. W. (1981) · New England Journal of Medicine · doi:10.1056/nejm198101153040311 · Cited by 163 · see citing works
Oxidation of arachidonic acid in micelles by superoxide and hydrogen peroxide.
Fridovich, S. E., & Porter, N. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)70128-8 · Cited by 162 · see citing works
Carotenoid pigments: their possible role in protecting against photooxidation in eyes and photoreceptor cells
Kirschfeld, K. (1982) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1982.0061 · Cited by 160 · see citing works
Reactions of ferrioxamine and desferrioxamine with the hydroxyl radical
Hoe, S. T., Rowley, D. A., & Halliwell, B. B. (1982) · Chemico-Biological Interactions · doi:10.1016/0009-2797(82)90018-7 · Cited by 149 · see citing works
Self-citation
Reaction of iron-EDTA chelates with the superoxide radical
Butler, J. A. V., & Halliwell, B. B. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90333-2 · Cited by 144 · see citing works
Self-citation
Thiol-dependent lipid peroxidation
Tien, M., Bucher, J. R., & Aust, S. D. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91701-6 · Cited by 144 · see citing works
Pathology of Oxygen Toxicity
Hasleton, P. S. (1983) · Journal of Clinical Pathology · doi:10.1136/jcp.36.12.1417-b · Cited by 136 · see citing works
The role of superoxide and hydroxyl radicals in phospholipid peroxidation catalysed by iron salts
Gutteridge, J. M. C. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80788-6 · Cited by 135 · see citing works
Self-citation
Oxygen and Living Processes: An Interdisciplinary Approach
Gilbert, D. L. (2011) · Medical Entomology and Zoology · Cited by 132 · see citing works
Production of Superoxide and Activity of Superoxide Dismutase in Rabbit Epididymal Spermatozoa
Holland, M. K., Álvarez, J. G., & Storey, B. T. (1982) · Biology of Reproduction · doi:10.1095/biolreprod27.5.1109 · Cited by 129 · see citing works
Effect of a specific iron chelating agent on animal models of inflammation.
Blake, D. R., Hall, N. D., BACON, P. A., Dieppe, P. A., Halliwell, B. B., & Gutteridge, J. M. C. (1983) · Annals of the Rheumatic Diseases · doi:10.1136/ard.42.1.89 · Cited by 125 · see citing works
Self-citation
Biochemical Mechanisms of Liver Injury.
(1979) · Annals of Internal Medicine · doi:10.7326/0003-4819-91-5-808_1 · Cited by 123 · see citing works
Role of iron and ethylenediaminetetraacetic acid in the bactericidal activity of a superoxide anion-generating system
Rosen, H., & Klebanoff, S. J. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90539-7 · Cited by 122 · see citing works
Direct demonstration that ferrous ion complexes of di- and triphosphate nucleotides catalyze hydroxyl free radical formation from hydrogen peroxide
Floyd, R. A. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90029-2 · Cited by 122 · see citing works
PHOTOSENSITIZED OXIDATION IN THE OCULAR LENS: EVIDENCE FOR PHOTOSENSITIZERS ENDOGENOUS TO THE HUMAN LENS
Zigler, J. S., & Goosey, J. D. (1981) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1981.tb05505.x · Cited by 121 · see citing works
Protection against Superoxide and Hydrogen Peroxide in Synovial Fluid from Rheumatoid Patients
Blake, D. R., Hall, N. D., Treby, D. A., Halliwell, B. B., & Gutteridge, J. M. C. (1981) · Clinical Science · doi:10.1042/cs0610483 · Cited by 119 · see citing works
Self-citation
Effects of antioxidant nutrient deficiency on the retina and retinal pigment epithelium of albino rats: a light and electron microscopic study
Katz, M. L., Parker, K. R., Handelman, G. J., Bramel, T. L., & Dratz, E. A. (1982) · Experimental Eye Research · doi:10.1016/0014-4835(82)90082-3 · Cited by 115 · see citing works
: Production of superoxide, hydrogen peroxide and hydroxyl radicals by phagocytic cells: A cause of chronic inflammatory disease?
Halliwell, B. B. (1982) · Cell Biology International Reports · doi:10.1016/0309-1651(82)90175-8 · Cited by 113 · see citing works
Self-citation
Effect of ferritin-containing fractions with different iron loading on lipid peroxidation
Gutteridge, J. M. C., Halliwell, B. B., Treffry, A., Harrison, P. M., & Blake, D. R. (1983) · Biochemical Journal · doi:10.1042/bj2090557 · Cited by 113 · see citing works
Self-citation
TREATMENT OF DIALYSIS OSTEOMALACIA WITH DESFERRIOXAMINE
Brown, D. J., Ham, K. N., Dawborn, J. K., & Xipell, J. M. (1982) · The Lancet · doi:10.1016/s0140-6736(82)90544-x · Cited by 110 · see citing works
Iron overload--clinical and pathologic aspects.
Jacobs, A. L. (1977) · PubMed · Cited by 108 · see citing works
Oxygen metabolism of Streptococcus mutans: uptake of oxygen and release of superoxide and hydrogen peroxide
Thomas, E. L., & Pera, K. (1983) · Journal of Bacteriology · doi:10.1128/jb.154.3.1236-1244.1983 · Cited by 106 · see citing works
Mitochondrial iron not bound in heme and iron-sulfur centers. Estimation, compartmentation and redox state
Tangerås, A., Flatmark, T., Bäckström, D., & Ehrenberg, A. (1980) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(80)90035-3 · Cited by 105 · see citing works
Formation of Hydroxyl Radicals from Hydrogen Peroxide and Iron Salts by Superoxide- and Ascorbate-Dependent Mechanisms: Relevance to the Pathology of Rheumatoid Disease
Rowley, D. A., & Halliwell, B. B. (1983) · Clinical Science · doi:10.1042/cs0640649 · Cited by 104 · see citing works
Self-citation
Lipid oxidation in biological membranes
Kaschnitz, R. M., & Hatefi, Y. (1975) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(75)90036-3 · Cited by 100 · see citing works
Transferrin binding and iron uptake in mouse hepatocytes
Cole, E. S., & Glass, J. (1983) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(83)90122-2 · Cited by 93 · see citing works
Lactoferrin-catalysed hydroxyl radical production. Additional requirement for a chelating agent
Winterbourn, C. C. (1983) · Biochemical Journal · doi:10.1042/bj2100015 · Cited by 93 · see citing works
A new method for the detection of hydroxyl radical production by phagocytic cells
Sagone, A. L., Decker, M. A., Wells, R. M., et al. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90354-2 · Cited by 89 · see citing works
Copper-induced generation of superoxide in human red cell membrane
Kumar, K. S., Rowse, C., & Hochstein, P. E. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91030-6 · Cited by 88 · see citing works
Enhanced production of hydroxyl radicals by the xanthine-xanthine oxidase reaction in the presence of lactoferrin
Bannister, J. V., BANNISTER, W. H., Hill, H. A. O., & Thornalley, P. J. (1982) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(82)90056-3 · Cited by 88 · see citing works
Superoxide‐dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts
Rowley, D. A., & Halliwell, B. B. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80214-7 · Cited by 87 · see citing works
Self-citation
Inhibition of microsomal oxidation of alcohols and of hydroxyl-radical-scavenging agents by the iron-chelating agent desferrioxamine
Cederbaum, A. I., & Dicker, E. (1983) · Biochemical Journal · doi:10.1042/bj2100107 · Cited by 86 · see citing works
The reticulocyte plasma membrane pathway of iron uptake as determined by the mechanism of alpha, alpha'-dipyridyl inhibition.
Núñez, M. T., Cole, E. S., & Glass, J. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33171-5 · Cited by 86 · see citing works
The protective action of superoxide dismutase on metal-ion catalysed peroxidation of phospholipids
Gutteridge, J. M. C. (1977) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(77)80208-8 · Cited by 86 · see citing works
Self-citation
Reactions of the Oxyform of Horseradish Peroxidase
Tamura, M., & Yamazaki, I. (1972) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a129768 · Cited by 83 · see citing works
Antitumor Effect of a Copper Coordination Compound With Superoxide Dismutase-Like Activity2
Leuthauser, S. W. C., Oberley, L. W., Oberley, T. D., et al. (1981) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/66.6.1077 · Cited by 82 · see citing works
Fifth Stenhouse‐Williams Memorial Lecture Oxygen and the Obligate Anaerobe
Morris, J. G. (1976) · Journal of Applied Bacteriology · doi:10.1111/j.1365-2672.1976.tb04171.x · Cited by 81 · see citing works
Hydroxyl radical production in a purified NADPH-cytochrome c (P-450) reductase system
Lai, C.-S., Grover, T. A., & Piette, L. H. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90042-0 · Cited by 76 · see citing works
Oxygen toxicity in Streptococcus sanguis. The relative importance of superoxide and hydroxyl radicals.
DiGuiseppi, J., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34683-0 · Cited by 71 · see citing works
Stimulation of microsomal lipid peroxidation by iron and cysteine. Characterization and the role of free radicals
Searle, A., & WILLSON, R. L. (1983) · Biochemical Journal · doi:10.1042/bj2120549 · Cited by 65 · see citing works
Iron-induced DNA damage and synthesis in isolated rat liver nuclei
Shires, T. K. (1982) · Biochemical Journal · doi:10.1042/bj2050321 · Cited by 62 · see citing works
The role of superoxide in xanthine oxidase-induced autooxidation of linoleic acid.
Thomas, M. J., Mehl, K. S., & PRYOR, W. A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34336-9 · Cited by 61 · see citing works
Growth‐modulating tripeptide (glycylhistidyllysine): Associaton with copper and iron in plasma, and stimulation of adhesiveness and growth of hepatoma cells in culture by tripeptide‐metal ion complexes
Pickart, L., & Thaler, M. (1980) · Journal of Cellular Physiology · doi:10.1002/jcp.1041020205 · Cited by 58 · see citing works
Collagen degradation in an experimental inflammatory lesion: studies on the role of the macrophage.
Etherington, D. J., Pugh, D., & Silver, I. A. (1981) · PubMed · Cited by 58 · see citing works
Superoxide‐dependent formation of hydroxyl radical catalyzed by transferrin
Motohashi, N., & Mori, I. (1983) · FEBS Letters · doi:10.1016/0014-5793(83)81144-2 · Cited by 54 · see citing works
The generation of hydroxyl radicals following superoxide production by neutrophil NADPH oxidase
Bannister, J. V., Bellavite, P., Davoli, A., et al. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80755-2 · Cited by 54 · see citing works
Factors which affect DNA strand breakage in human leukocytes exposed to a tumor promoter, phorbol myristate acetate
Birnboim, H. C. (1982) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y82-203 · Cited by 51 · see citing works
Ascorbate uptake by isolated rat alveolar macrophages and type II cells
Castranova, V., Wright, J. R., Colby, H. D., & Miles, P. R. (1983) · Journal of Applied Physiology · doi:10.1152/jappl.1983.54.1.208 · Cited by 48 · see citing works
Spontaneous chemiluminescence of human breath. Spectrum, lifetime, temporal distribution, and correlation with peroxide.
Williams, M. D., & Chance, B. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32711-x · Cited by 44 · see citing works
The Anaemia of Rheumatoid Arthritis: The Significance of Iron Deposits in the Synovial Membrane
Muirden, K. D. (1970) · Australasian Annals of Medicine · doi:10.1111/imj.1970.19.2.97 · Cited by 38 · see citing works
The effect of iron deficiency on experimental oral carcinogenesis in the rat
Prime, S. S., MacDonald, D. G., & Rennie, J. S. (1983) · British Journal of Cancer · doi:10.1038/bjc.1983.62 · Cited by 37 · see citing works
The incorporation of iron into apoferritin as mediated by ceruloplasmin
Boyer, R. F., & Schori, B. E. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)90407-2 · Cited by 36 · see citing works
Oxygen, oxidases, and the essential trace metals
Hill, H. A. O. (1981) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.1981.0093 · Cited by 30 · see citing works
Differential sensitivity of tumor cells to externally generated hydrogen peroxide. Role of glutathione and related enzymes.
Bozzi, A., Mavelli, I., Mondovı̀, B., et al. (1979) · PubMed · Cited by 29 · see citing works
Protection against free radical formation by protein bound iron
Maguire, J. J., KELLOGGIII, E., & Packer, L. (1982) · Toxicology Letters · doi:10.1016/0378-4274(82)90006-6 · Cited by 20 · see citing works
Studies on the properties of the singlet oxygen-like factor produced during lipid peroxidation
Lai, E. K., Kuo-Lan, P., & McCay, P. B. (1978) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(78)90040-1 · Cited by 19 · see citing works
Chromosome-damaging activity of ferritin and its relation to chelation and reduction of iron.
Whiting, R. F., Wei, L., & STICH, H. F. (1981) · PubMed · Cited by 19 · see citing works
IRON AND RHEUMATOID DISEASE
Blake, D. R., & Bacon, P. A. (1982) · The Lancet · doi:10.1016/s0140-6736(82)91779-2 · Cited by 13 · see citing works
Modification of superoxide dismutase in rat mammary carcinoma.
Petkau, A., Monasterski, L. G., Kelly, K. A., et al. (1977) · PubMed · Cited by 12 · see citing works
Non-protein-bound iron within bacterial cells and the action of bleomycin.
Gutteridge, J. M. C., & Wilkins, S. (1984) · PubMed · Cited by 9 · see citing works
Self-citation
Involvement of singlet oxygen in biochemical systems.
Singh, A., Singh, H., Kremers, W., et al. (1981) · PubMed · Cited by 6 · see citing works

Flagged first, then by citations

Research works printed but not linked: 21

Aust, S. D. & Svingen, B. A. (1982) in Free Radicals in Biology (Pryor, W. A., ed.), vol. 5, pp. 1-28, Academic Press, New York
Bannister, J. V., Bannister, W. H. & Thornalley, P. J. (1984) in Proc. EMBO Meet. Oxygen Radicals, in the press
Del Maestro, R. F., Bjork, J. & Arfors, K. E. (1982) in Pathology of Oxygen (Autor, A. P., ed.), pp. 157-173, Academic Press, New York
Foote, C. S. (1982) in Pathology ofOxygen (Autor, A. P., ed.), pp. 21-44, Academic Press, New York
Frimer, A. A. (1982) in Superoxide Dismutase, vol. 2 (Oberley, L, W., ed.), pp. 83-125, CRC Press, Boca Raton, FL
Haber, F. & Weiss, J. (1934) Proc. R. Soc. London Ser. A 147, 332-351
Halliwell, B. (1981a) Chloroplast Metabolism: the Stre- ture and Function of Chloroplasts in Green Leaf Cells, Oxford University Press, Oxford
Halliwell, B. (1981b) in Age Pigments (Sohal, R. S., ed.), pp. 1-62, Elsevier/North-Holland, Amsterdam
Halliwell, B. (1983) in Copper Proteins, vol. 2 (Lontie, R., ed.), CRC Press, Boca Raton, FL, in the press
Hill, H. A. 0. (1981) Philos. Trans. R. Soc. London Ser. B. 294, 119-128
Kirschfeld, K. (1982) Proc. R. Soc. London Ser. B. 216, 71-85
McBrien, D. C. H. & Slater, T. F. (eds.) (1982) Free Radicals, Lipid Peroxidation and Cancer, Academic Press, London
McCord, J. M., Wong, K., Stokes, S. H., Petrone, W. F. & English, D. (1982) in Pathology ofOxygen (Autor, A. P., ed.), pp. 75-83, Academic Press, New York
Michelson, A. M. (1982) in Pathology ofOxygen (Autor, A. P., ed.), pp. 277-302, Academic Press, New York
Oberley, L. W., Leuthauser, S. W. H. C., Buettner, G. R., Sorenson, J. R. J., Oberley, T. D. & Bize, I. B. (1982) in Pathology of Oxygen (Autor, A. P., ed.), pp. 207-221, Academic Press, New York
Petkau, A., Chelack, W. S., Kelly, K. & Friesen, H. G. (1982) in Pathology of Oxygen (Autor, A. P., ed.), pp. 223-243, Academic Press, New York
Richmond, R. (1983) Ph.D. Thesis, University of London King's College
Samuni, A., Aronovitch, J., Godinger, D., Chevion, M. & Czapski, G. (1984) Eur. J. Biochem., in the press
Walling, C. (1982) in Oxidases and Related Redox Systems (King, T. E., Mason, H. S. & Morrison, M., eds.), pp. 85-97, Pergamon Press, Oxford
Willson, R. L. (1977) New Sci. pp. 558-560
Willson, R. L. (1982) in Free Radicals, Lipid Peroxidation and Cancer (McBrien, D. C. H. & Slater, T. F., eds.), pp. 275-303, Academic Press, London

Sorted by citations

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Self-citation
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Self-citation
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Self-citation
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Increased peroxidation and reduced antioxidant enzyme activity in Alzheimer's disease
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Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497 · see citing works
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Self-citation
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Lipid peroxidation in erythrocytes
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Iron-dependent regulation of the divalent metal ion transporter
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A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage
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Iron–sulfur proteins with nonredox functions
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Hortschansky, P., Eisendle, M., Al‐Abdallah, Q., Schmidt, A. D., Bergmann, S., Thön, M., Kniemeyer, O., Abt, B., Seeber, B., Werner, E. R., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601752 · Cited by 232 · see citing works
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Long-lived reactive species on free-radical-damaged proteins
Simpson, J. A., Narita, S., Gieseg, S., Gebicki, S., Gebicki, J. M., & Dean, R. T. (1992) · Biochemical Journal · doi:10.1042/bj2820621 · Cited by 225 · see citing works
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What Is Responsible for the Initiating Chemistry of Iron-Mediated Lipid Peroxidation: An Update
Cheng, Z., & Li, Y. (2007) · Chemical Reviews · doi:10.1021/cr040077w · Cited by 211 · see citing works
Role of free radicals in viral pathogenesis and mutation
Akaike, T. (2001) · Reviews in Medical Virology · doi:10.1002/rmv.303 · Cited by 207 · see citing works
The Effects of Intravenous Antioxidants in Patients With Septic Shock
Galley, H. F., Howdle, P. D., Walker, B. E., & Webster, N. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00059-2 · Cited by 203 · see citing works
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Biemond, P., Swaak, A. J. G., Beindorff, C. M., & Koster, J. F. (1986) · Biochemical Journal · doi:10.1042/bj2390169 · Cited by 179 · see citing works
Superoxide dependent iron release from ferritin in inflammatory diseases
Biemond, P., Swaak, A. J. G., van Eijk, H. G., & Koster, J. F. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90026-3 · Cited by 182 · see citing works
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Iron-Chelating Therapy
Hershko, C., Weatherall, D. J., & Finch, C. (1988) · CRC Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408368809105894 · Cited by 141 · see citing works
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Eisendle, M., Schrettl, M., Kragl, C., Müller, D., Illmer, P., & Haas, H. (2006) · Eukaryotic Cell · doi:10.1128/ec.00057-06 · Cited by 141 · see citing works
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Schrettl, M., & Haas, H. (2011) · Current Opinion in Microbiology · doi:10.1016/j.mib.2011.06.002 · Cited by 139 · see citing works
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Ye, S., Liu, F., Wang, J., Wang, H., & Zhang, M. (2012) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2011.08.057 · Cited by 138 · see citing works
Cardiolipin Remodeling in the Heart
Sparagna, G. C., & Lesnefsky, E. J. (2009) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0b013e31819b5461 · Cited by 128 · see citing works
Molecular characterization of the ferric-uptake regulator, Fur, from Staphylococcus aureus The GenBank accession numbers for the S. aureus fur gene and fhu operon reported in this paper are AF118839 and AF132117, respectively.
Xiong, A., Singh, V. K., Cabrera, G., & Jayaswal, R. K. (2000) · Microbiology · doi:10.1099/00221287-146-3-659 · Cited by 122 · see citing works
A novel type of glutathione peroxidase: expression and regulation during wound repair
MUNZ, B., FRANK, S., HÜBNER, G., OLSEN, E., & WERNER, S. (1997) · Biochemical Journal · doi:10.1042/bj3260579 · Cited by 118 · see citing works
Oxidative Stress, Glucose Metabolism, and the Prevention of Type 2 Diabetes: Pathophysiological Insights
Shah, S., Iqbal, M., Karam, J., Salifu, M., & McFarlane, S. I. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.1629 · Cited by 115 · see citing works
Iron depletion or chelation reduces ischemia/reperfusion-induced edema in gerbil brains
Patt, A., Horesh, I. R., Berger, E. M., Harken, A. H., & Repine, J. E. (1990) · Journal of Pediatric Surgery · doi:10.1016/0022-3468(90)90407-z · Cited by 111 · see citing works
A role for iron and oxygen chemistry in preserving soft tissues, cells and molecules from deep time
Schweitzer, M. H., Zheng, W., Cleland, T. P., Goodwin, M. B., Boatman, E., Theil, E., Marcus, M. A., & Fakra, S. C. (2014) · Proceedings of the Royal Society B: Biological Sciences · doi:10.1098/rspb.2013.2741 · Cited by 112 · see citing works
Superoxide production by polymorphonuclear leucocytes in rheumatoid arthritis and osteoarthritis: in vivo inhibition by the antirheumatic drug piroxicam due to interference with the activation of the NADPH-oxidase.
Biemond, P., Swaak, A. J., Penders, J. M., Beindorff, C. M., & Koster, J. F. (1986) · Annals of the Rheumatic Diseases · doi:10.1136/ard.45.3.249 · Cited by 108 · see citing works
Oxygen Regulation in Development: Lessons from Embryogenesis towards Tissue Engineering
Fathollahipour, S., Patil, P. S., & Leipzig, N. D. (2018) · Cells Tissues Organs · doi:10.1159/000493162 · Cited by 101 · see citing works
Age-Associated Changes in Superoxide Dismutase Activity, Thiobarbituric Acid Reactivity and Reduced Glutathione Level in the Brain and Liver in Senescence Accelerated Mice (SAM): A Comparison with DdY Mice
Liu, J., & Mori, A. (1993) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(93)90032-m · Cited by 104 · see citing works
Optimization for the extraction of polysaccharides from Ganoderma lucidum and their antioxidant and antiproliferative activities
Ma, C.-W., Feng, M., Zhai, X., Hu, M., You, L., Luo, W., & Zhao, M. (2013) · Journal of the Taiwan Institute of Chemical Engineers · doi:10.1016/j.jtice.2013.01.032 · Cited by 102 · see citing works
Acidification of the intimal fluid: the perfect storm for atherogenesis
Öörni, K., Rajamäki, K., Nguyen, S. D., Lähdesmäki, K., Plihtari, R., Lee-Rueckert, M., & Kovanen, P. T. (2015) · Journal of Lipid Research · doi:10.1194/jlr.r050252 · Cited by 101 · see citing works
Isoleukotrienes are biologically active free radical products of lipid peroxidation
Harrison, K. A., & Murphy, R. C. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17273 · Cited by 98 · see citing works
Iron-Loaded Synthetic Chrysotile: A New Model Solid for Studying the Role of Iron in Asbestos Toxicity
Gazzano, E., Turci, F., Foresti, E., Putzu, M. G., Aldieri, E., Silvagno, F., Lesci, I. G., Tomatis, M., Riganti, C., Romano, C., et al. (2007) · Chemical Research in Toxicology · doi:10.1021/tx600354f · Cited by 88 · see citing works
Enhanced catabolism of mitochondrial superoxide/hydrogen peroxide and aging in transgenic Drosophila
Bayne, A.-C. V., Mockett, R. J., Orr, W. C., & Sohal, R. S. (2005) · Biochemical Journal · doi:10.1042/bj20041872 · Cited by 84 · see citing works
In vitro evaluation of antioxidant properties of Cocos nucifera Linn. water
Mantena, S. K., Jagadish, Badduri, S. R., Siripurapu, K. B., & Unnikrishnan, M. K. (2003) · Food / Nahrung · doi:10.1002/food.200390023 · Cited by 80 · see citing works
Desferrioxamine suppresses experimental allergic encephalomyelitis induced by MBP in SJL mice
Pedchenko, T. V., & LeVine, S. M. (1998) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(97)00256-7 · Cited by 78 · see citing works
Reflections of an aging free radical
Halliwell, B. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.10.010 · Cited by 75 · see citing works
Self-citation
The role of oxidative stress in postoperative delirium
Karlidag, R., Unal, S., Sezer, O. H., Bay Karabulut, A., Battaloğlu, B., But, A., & Ozcan, C. (2006) · General Hospital Psychiatry · doi:10.1016/j.genhosppsych.2006.06.002 · Cited by 72 · see citing works
Antioxidative Activities of Kefir
Liu, J.-R., Lin, Y.-Y., Chen, M.-J., Chen, L.-J., & Lin, C.-W. (2005) · Asian-Australasian Journal of Animal Sciences · doi:10.5713/ajas.2005.567 · Cited by 72 · see citing works
Induction of mesothelioma by intraperitoneal injections of ferric saccharate in male Wistar rats
Okada, S., Hamazaki, S., Toyokuni, S., & Midorikawa, O. (1989) · British Journal of Cancer · doi:10.1038/bjc.1989.344 · Cited by 65 · see citing works
Inhibition of iron absorption prolongs the life span of Drosophila
Massie, H. R., Aiello, V. R., & Williams, T. R. (1993) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(93)90001-8 · Cited by 61 · see citing works
Polyphenols of pseudostem of different banana cultivars and their antioxidant activities
Saravanan, K., & Aradhya, S. M. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103835z · Cited by 62 · see citing works
Amplification of the CUP1 gene is associated with evolution of copper tolerance in Saccharomyces cerevisiae
Adamo, G. M., Lotti, M., Tamás, M. J., & Brocca, S. (2012) · Microbiology · doi:10.1099/mic.0.058024-0 · Cited by 60 · see citing works
Fate of the sunscreen compound oxybenzone in Cyperus alternifolius based hydroponic culture: Uptake, biotransformation and phytotoxicity
Chen, F., Huber, C., & Schröder, P. (2017) · Chemosphere · doi:10.1016/j.chemosphere.2017.05.072 · Cited by 60 · see citing works
Hypothesis: Is lung disease after silicate inhalation caused by oxidant generation?
Ghio, A. J., Kennedy, T. P., Schapira, R. M., Crumbliss, A. L., & Hoidal, J. R. (1990) · The Lancet · doi:10.1016/0140-6736(90)92421-d · Cited by 56 · see citing works
Reduction of collagen degradation in experimental granulation tissue by vitamin E and selenium
Åsman, B., Wijkander, P., & Hjerpe, A. (1994) · Journal Of Clinical Periodontology · doi:10.1111/j.1600-051x.1994.tb00275.x · Cited by 49 · see citing works
Lipophilicity of analogs of pyridoxal isonicotinoyl hydrazone (PIH) determines the efflux of iron complexes and toxicity in K562 cells
Buss, J. L., Arduini, E., Shephard, K. C., & Ponka, P. (2003) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01551-4 · Cited by 41 · see citing works
Magnesium Deficiency Enhances Hydrogen Peroxide Production and Oxidative Damage in Chick Embryo Hepatocyte In Vitro
Yang, Y., Wu, Z., Chen, Y., Qiao, J., Gao, M., Yuan, J., Nie, W., & Guo, Y. (2006) · Biometals · doi:10.1007/s10534-005-6898-1 · Cited by 39 · see citing works
The role of iron in 2,3,7,8-tetrachlorodibenzo-p-dioxin-induced lipid peroxidation by rat liver microsomes
Al-Bayati, Z. A. F., & Stohs, S. J. (1987) · Toxicology Letters · doi:10.1016/0378-4274(87)90119-6 · Cited by 31 · see citing works

Authors: Halliwell, B., & Gutteridge, J. M. C.
Affiliations: University of London (GB)
ORCID: Halliwell, B
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1984-04-01
Volume: 219
Issue: 1
Pages: 1-14
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj2190001
PMC: PMC1153442
OpenAlex: W1879184430
Cited by: 5,330
References: 121
Citations by year: 2026: 43 · 2025: 78 · 2024: 80 · 2023: 102 · 2022: 96 · 2021: 127 · 2020: 144 · 2019: 151 · 2018: 140 · 2017: 143 · 2016: 156 · 2015: 154 · 2014: 183 · 2013: 177 · 2012: 188
FWCI: 14.23
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Wellcome Trust
Lister Institute of Preventive Medicine
Topics: Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
Keywords: oxygen toxicity, oxygen free radicals, reactive oxygen species, transition metals, oxidative stress, disease, neutrophils, monocytes, macrophages, eosinophils
MeSH terms: Animals, Arthritis, Rheumatoid, Copper, Free Radicals, Humans, Hydroxides, Iron, Lipid Peroxides, Neoplasms, Oxygen, Superoxides, Hydroxyl Radical

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Oxygen toxicity, oxygen radicals, transition metals and disease

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