Ferritin as a source of iron for oxidative damage

Free radicals in biology and medicine

Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works

Free radicals in biology and medicine

Halliwell, B. B., & Gutteridge, J. M. C. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90140-0 · Cited by 2,931 · see citing works

Macrophage oxidation of L-arginine to nitrite and nitrate: nitric oxide is an intermediate

Marletta, M. A., Yoon, P. S., Iyengar, R., Leaf, C. D., & Wishnok, J. S. (1988) · Biochemistry · doi:10.1021/bi00424a003 · Cited by 1,601 · see citing works

Biosynthesis And Metabolism Of Endothelium-Derived Nitric Oxide

Ignarro, L. J. (1990) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.30.040190.002535 · Cited by 1,300 · see citing works

The Reduction of Cytochrome c by Milk Xanthine Oxidase

McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,205 · 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

Role of metals in oxygen radical reactions

Aust, S. D., Morehouse, L. A., & Thomas, C. E. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90025-x · Cited by 1,150 · see citing works

The Generation of Hydrogen Peroxide, Superoxide Radical, and Hydroxyl Radical by 6-Hydroxydopamine, Dialuric Acid, and Related Cytotoxic Agents

Cohen, G., Heikkila, R. E., & MacNamee, W. T. T. A. O. D. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42751-8 · Cited by 898 · see citing works

Transition metals as catalysts of “autoxidation” reactions

Miller, D. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90148-c · Cited by 739 · see citing works

Iron transport and storage

Crichton, R. R., & CHARLOTEAUX‐WAUTERS, M. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb11155.x · Cited by 682 · see citing works

Calmodulin-dependent endothelium-derived relaxing factor/nitric oxide synthase activity is present in the particulate and cytosolic fractions of bovine aortic endothelial cells.

Förstermann, U., Pollock, J. S., Schmidt, H. H. H. W., Heller, M., & Murad, F. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.5.1788 · Cited by 592 · see citing works

Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity

Bus, J. S., Aust, S. D., & Gibson, J. E. (1974) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(74)80481-x · Cited by 539 · see citing works

Ferritin and superoxide-dependent lipid peroxidation.

Thomas, C. E., Morehouse, L. A., & Aust, S. D. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83617-7 · Cited by 530 · see citing works

Reaction of superoxide with nitric oxide to form peroxonitrite in alkaline aqueous solution

Blough, N. V., & Zafiriou, O. C. (1985) · Inorganic Chemistry · doi:10.1021/ic00216a003 · Cited by 525 · see citing works

Synthesis of nitric oxide from l -arginine by neutrophils. Release and interaction with superoxide anion

McCall, T., Boughton-Smith, N. K., Palmer, R. M. J., Whittle, B. J. R., & Moncada, S. (1989) · Biochemical Journal · doi:10.1042/bj2610293 · Cited by 518 · see citing works

EPR demonstration of iron-nitrosyl complex formation by cytotoxic activated macrophages

Lancaster, J. R., & Hibbs, J. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1223 · Cited by 507 · see citing works

Copper Proteins and Copper Enzymes

Lontie, R. (2018) · CRC Press eBooks · doi:10.1201/9781351070898 · Cited by 487 · see citing works

The double-edged role of nitric oxide in brain function and superoxide-mediated injury.

Beckman, J. S. (1991) · PubMed · Cited by 463 · see citing works

Iron carriers and iron proteins

Loehr, T. M. (1989) · Medical Entomology and Zoology · Cited by 436 · see citing works

Nitric oxide as an antioxidant

Kanner, J., Harel, S., & Rina, G. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90452-o · Cited by 429 · see citing works

Murine cytotoxic activated macrophages inhibit aconitase in tumor cells. Inhibition involves the iron-sulfur prosthetic group and is reversible.

Drapier, J., & Hibbs, J. B. (1986) · Journal of Clinical Investigation · doi:10.1172/jci112642 · Cited by 415 · see citing works

Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.

Biemond, P., van Eijk, H. G., Swaak, A. J., & Koster, J. F. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111364 · Cited by 380 · see citing works

Ceruloplasmin. A scavenger of superoxide anion radicals.

Goldstein, I. M., Kaplan, H. B., Edelson, H. S., & Weissmann, G. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50692-x · Cited by 365 · see citing works

Sites of inhibition of mitochondrial electron transport in macrophage-injured neoplastic cells.

Granger, D. L., & Lehninger, A. L. (1982) · The Journal of Cell Biology · doi:10.1083/jcb.95.2.527 · Cited by 348 · see citing works

Lipid Peroxidation and Mechanisms of Toxicity

Horton, A. A., Fairhurst, S., & Bus, J. S. (1987) · Critical Reviews in Toxicology · doi:10.3109/10408448709089856 · Cited by 340 · see citing works

The one-electron transfer redox potentials of free radicals. I. The oxygen/superoxide system

Ilan, Y. A., Czapski, G., & Meisel, D. (1976) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(76)90080-3 · Cited by 304 · see citing works

Energetics of interconversion reactions of oxyradicals

Koppenol, W. H., & Butler, J. (1985) · Advances in free radical biology and medicine · doi:10.1016/8755-9668(85)90005-5 · Cited by 292 · see citing works

Nitric oxide mediates iron release from ferritin

Reif, D. W., & Simmons, R. D. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90680-w · Cited by 280 · see citing works

Generation of EPR-detectable nitrosyl-iron complexes in tumor target cells cocultured with activated macrophages

Drapier, J., Pellat‐Deceunynck, C., & Henry, Y. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99204-5 · Cited by 279 · see citing works

The role of iron in the initiation of lipid peroxidation

Minotti, G., & Aust, S. D. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90050-8 · Cited by 272 · see citing works

Studies of ascorbate-dependent, iron-catalyzed lipid peroxidation

Miller, D. M., & Aust, S. D. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90261-0 · Cited by 264 · see citing works

Alloxan-induced diabetes—evidence for hydroxyl radical as a cytotoxic intermediate

Heikkila, R. E., Winston, B., Cohen, G., & Barden, H. (1976) · Biochemical Pharmacology · doi:10.1016/0006-2952(76)90502-5 · Cited by 243 · see citing works

Antioxidants in Therapy and Preventive Medicine

Emerit, I., Packer, L., & Auclair, C. (1990) · Advances in experimental medicine and biology · doi:10.1007/978-1-4684-5730-8 · Cited by 213 · see citing works

Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogs

Jones, T. T., Spencer, R. W., & Walsh, C. (1978) · Biochemistry · doi:10.1021/bi00612a021 · Cited by 198 · see citing works

Some Reactions and Properties of Nitro Radical-Anions Important in Biology and Medicine

Wardman, P. (1985) · Environmental Health Perspectives · doi:10.1289/ehp.8564309 · Cited by 184 · see citing works

Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation

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

Iron depletion: Possible cause of tumor cell cytotoxicity induced by activated macrophages

Hibbs, J. B., Taintor, R. R., & Vavrin, Z. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)90288-2 · Cited by 178 · see citing works

Reductive release of iron from ferritin by cation free radicals of paraquat and other bipyridyls.

Thomas, C. E., & Aust, S. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69271-3 · Cited by 167 · see citing works

Inhibition of superoxide and ferritin-dependent lipid peroxidation by ceruloplasmin

Samokyszyn, V. M., Miller, D. M., Reif, D. W., & Aust, S. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31218-8 · Cited by 166 · see citing works

Reduction of mammalian ferritin.

Watt, G. D., Frankel, R. B., & Papaefthymiou, G. C. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.11.3640 · Cited by 161 · see citing works

Alloxan toxicity to the pancreatic B-cell

Malaisse, W. J. (1982) · Biochemical Pharmacology · doi:10.1016/0006-2952(82)90571-8 · Cited by 160 · see citing works

Inhibition of Alloxan Action in Isolated Pancreatic Islets by Superoxide Dismutase, Catalase, and a Metal Chelator

Fischer, L. J., & Hamburger, S. A. (1980) · Diabetes · doi:10.2337/diab.29.3.213 · Cited by 159 · see citing works

Superoxide ion as a primary reductant in ascorbate-mediated ferretin iron release

Boyer, R. F., & McCleary, C. J. (1987) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(87)90017-7 · Cited by 156 · see citing works

THE MECHANISM OF IRON RELEASE FROM FERRITIN AS RELATED TO ITS BIOLOGICAL PROPERTIES

Mazur, A., Baez, S., & Shorr, E. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71052-1 · Cited by 152 · see citing works

Developments in inorganic nitrogen chemistry

Colburn, C. B. (1966) · Medical Entomology and Zoology · Cited by 147 · see citing works

Ferritin iron uptake and release. Structure–function relationships

Harrison, P. M., Hoy, T. G., Macara, I. G., & Hoare, R. J. (1974) · Biochemical Journal · doi:10.1042/bj1430445 · Cited by 133 · see citing works

Release of iron from ferritin by cardiotoxic anthracycline antibiotics

Thomas, C. E., & Aust, S. D. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90523-0 · Cited by 116 · see citing works

Reduction and Release of Ferritin Iron By Plant Phenolics

Boyer, R. F., Clark, H. M., & LaRoche, A. P. (1988) · Journal of Inorganic Biochemistry · doi:10.1016/0162-0134(88)80025-4 · Cited by 115 · see citing works

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

Glutathione-mediated redox cycling of alloxan

Winterbourn, C. C., & Munday, R. (1989) · Biochemical Pharmacology · doi:10.1016/0006-2952(89)90037-3 · Cited by 112 · see citing works

On the limited ability of superoxide to release iron from ferritin

Bolann, B. J., & Ulvik, R. J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19415.x · Cited by 111 · see citing works

Cytochrome c reduction by semiquinone radicals can be indirectly inhibited by superoxide dismutase

Winterbourn, C. C. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90268-x · Cited by 106 · see citing works

Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release?

Watt, G. D., Jacobs, D., & Frankel, R. B. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.20.7457 · 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

Versatility and low-temperature synthetic potential of ammonium halides

Meyer, G., Staffel, T., Doetsch, S., & Schleid, T. (1985) · Inorganic Chemistry · doi:10.1021/ic00216a004 · Cited by 93 · see citing works

Hydroxyl radical is not a product of the reaction of xanthine oxidase and xanthine. The confounding problem of adventitious iron bound to xanthine oxidase.

Britigan, B. E., Pou, S., Rosen, G. M., Lilleg, D. M., & Buettner, G. R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)38197-3 · Cited by 89 · see citing works

Mitochondrial iron loss from leukemia cells injured by macrophages. A possible mechanism for electron transport chain defects.

Wharton, M., Granger, D. L., & Durack, D. T. (1988) · The Journal of Immunology · doi:10.4049/jimmunol.141.4.1311 · Cited by 84 · see citing works

Rat liver microsomal NADPH-dependent release of iron from ferritin and lipid peroxidation

Thomas, C. E., & Aust, S. D. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90134-5 · Cited by 84 · see citing works

One-electron reduction of adriamycin: Properties of the semiquinone

Land, E. J., Mukherjee, T., Swallow, A. J., & Bruce, J. M. (1983) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(83)90013-9 · Cited by 76 · see citing works

Bipyridylium quaternary salts and related compounds. Part 6.—Pulse radiolysis studies of the reaction of paraquat radical analogues with oxygen

Farrington, J. A., Ebert, M., & Land, E. J. (1978) · Journal of the Chemical Society Faraday Transactions 1 Physical Chemistry in Condensed Phases · doi:10.1039/f19787400665 · Cited by 76 · see citing works

Mobilisation of iron from ferritin fractions of defined iron content by biological reductants

Dognin, J., & Crichton, R. R. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80081-0 · Cited by 67 · see citing works

Iron mobilization from ferritin using α-oxohydroxy heteroaromatic chelators

Kontoghiorghes, G. J. (1986) · Biochemical Journal · doi:10.1042/bj2330299 · Cited by 65 · see citing works

Inhibition of alloxan action in isolated pancreatic islets by superoxide dismutase, catalase, and a metal chelator

Fischer, L. J., & Hamburger, S. A. (1980) · Diabetes · doi:10.2337/diabetes.29.3.213 · Cited by 64 · see citing works

The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin

Monteiro, H. P., & Winterbourn, C. C. (1988) · Biochemical Journal · doi:10.1042/bj2560923 · Cited by 62 · see citing works

Protective effect of ICRF-187 on doxorubicin-induced cardiac and renal toxicity in spontaneously hypertensive (SHR) and normotensive (WKY) rats

Herman, E. H., El-Hage, A. N., & Ferrans, V. J. (1988) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(88)90226-8 · Cited by 61 · see citing works

Release of iron from ferritin by aqueous extracts of cigarette smoke

Moreno, J. J., Foroozesh, M. B., Church, D. F., & Pryor, W. A. (1992) · Chemical Research in Toxicology · doi:10.1021/tx00025a020 · Cited by 60 · see citing works

Plasma ceruloplasmin Evidence for its presence in and uptake by heart and other organs of the rat

Linder, M. C., & Moor, J. R. (1977) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(77)90064-2 · Cited by 60 · see citing works

Paraquat and ferritin-dependent lipid peroxidation

Saito, M., Thomas, C. E., & Aust, S. D. (1985) · Journal of Free Radicals in Biology & Medicine · doi:10.1016/0748-5514(85)90116-3 · Cited by 60 · see citing works

Release of iron from ferritin by semiquinone, anthracycline, bipyridyl, and nitroaromatic radicals

Montiero, H. P., Vile, G. F., & Winterbourn, C. C. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90065-8 · Cited by 58 · see citing works

Redox reactions associated with iron release from mammalian ferritin

Jacobs, D., Watt, G. D., Frankel, R. B., & Papaefthymiou, G. C. (1989) · Biochemistry · doi:10.1021/bi00430a033 · Cited by 58 · see citing works

[28] Biological activity of human plasma copper-binding growth factor glycyl-l-histidyl-l-lysine

Pickart, L., & Lovejoy, S. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)47121-8 · Cited by 57 · see citing works

Iron release from ferritin and lipid peroxidation by radiolytically generated reducing radicals

Reif, D. W., Schubert, J., & Aust, S. D. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90590-5 · Cited by 50 · see citing works

Ferritin: structure, function, and regulation.

Ec, T. (1983) · PubMed · Cited by 50 · see citing works

Redox activities of antitumor anthracyclines determined by microsomal oxygen consumption and assays for superoxide anion and hydroxyl radical generation

Peters, J. H., Gordon, G. R., Kashiwase, D., Lown, J. W., Shau-Fung, Y., & Plambeck, J. A. (1986) · Biochemical Pharmacology · doi:10.1016/0006-2952(86)90276-5 · Cited by 46 · see citing works

Metabolism of cu-64-labeled copper by the isolated rat liver

Owen, C. A., & Hazelrig, J. (1966) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1966.210.5.1059 · Cited by 46 · see citing works

Iron binding proteins without cofactors or sulfur clusters.

Theil, E. C., Eichhorn, G. L., & Marzilli, L. G. (1983) · PubMed · Cited by 45 · see citing works

Free radicals and environmental toxins

Thomas, C. E., & Aust, S. D. (1986) · Annals of Emergency Medicine · doi:10.1016/s0196-0644(86)80132-9 · Cited by 44 · see citing works

The role of superoxide anion radical in the reduction of ferritin iron by xanthine oxidase.

Williams, D., LEE, G. R., & Cartwright, G. E. (1974) · Journal of Clinical Investigation · doi:10.1172/jci107603 · Cited by 43 · see citing works

Ferritin, Lipid Peroxidation and Redox-Cycling Xenobiotics

Winterbourn, C. C., Vile, G. F., & Monteiro, H. P. (1991) · Free Radical Research Communications · doi:10.3109/10715769109145774 · Cited by 40 · see citing works

Hydroxyl radical is not a product of the reaction of xanthine oxidase and xanthine

Britigan, B. E., Pou, S., Rosen, G. M., Lilleg, D. M., & Buettner, G. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90807-u · Cited by 38 · 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

Effect of diquat on the distribution of iron in rat liver

Reif, D. W., Beales, I., Thomas, C. E., & Ausi, S. D. (1988) · Toxicology and Applied Pharmacology · doi:10.1016/0041-008x(88)90054-3 · Cited by 36 · see citing works

Free Radicals in the Reaction of Alloxan with Glutathione and Ascorbic Acid.

Lagercrantz, C., Yhland, M., Hegge, E., Reistad, R., & Munch‐Petersen, J. (1963) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.17-0904 · Cited by 35 · see citing works

Microsomal reduction of low-molecular-weight Fe3+ chelates and ferritin: Enhancement by adriamycin, paraquat, menadione, and anthraquinone 2-sulfonate and inhibition by oxygen

Vile, G. F., & Winterbourn, C. C. (1988) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(88)90068-9 · Cited by 35 · see citing works

Free Radicals in the Reaction of Alloxan with Glutathione and Ascorbic Acid.

Lagercrantz, C., Yhland, M., Førland, T., von Euler, U. S., & Munch‐Petersen, J. (1963) · Acta chemica Scandinavica/Acta chemica Scandinavica. B, Organic chemistry and biochemistry/Acta chemica Scandinavica. A, Physical and inorganic chemistry/Acta chemica Scandinavica. Series B. Organic chemistry and biochemistry/Acta chemica Scandinavica. Series A, Physical and inorganic chemistry · doi:10.3891/acta.chem.scand.17-1677 · Cited by 34 · see citing works

Effects of Ceruloplasmin on Superoxide-Dependent Iron Release from Ferritin and Lipid Peroxidation

Samokyszyn, V. M., Reif, D. W., Miller, D. M., & Aust, S. D. (1991) · Free Radical Research Communications · doi:10.3109/10715769109145780 · Cited by 33 · see citing works

Release of iron from ferritin by divicine, isouramil, acid-hydrolyzed vicine, and dialuric acid and initiation of lipid peroxidation

Monteiro, H. P., & Winterbourn, C. C. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90305-6 · Cited by 29 · see citing works

Reactions of Nitrogen(II) Oxide

Drago, R. S. (1962) · Advances in chemistry series · doi:10.1021/ba-1962-0036.ch015 · Cited by 29 · see citing works

Rapid reduction of iron in horse spleen ferritin by thioglycolic acid measured by dispersive X-ray absorption spectroscopy

Joo, M., Tourillon, G., Sayers, D. E., & Theil, E. C. (1990) · BioMetals · doi:10.1007/bf01140575 · Cited by 28 · see citing works

Reactivity of semiquinone radicals and its relation to the biochemical role of superoxide

Sutton, H. C., & Sangster, D. F. (1982) · Journal of the Chemical Society Faraday Transactions 1 Physical Chemistry in Condensed Phases · doi:10.1039/f19827800695 · Cited by 25 · see citing works

Role of free radicals in biological systems

Fehér, J., Blázovics, A., Matkovics, B., & Mézes, M. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90047-x · Cited by 24 · see citing works

Alloxan- and glutathione-dependent ferritin iron release and lipid peroxidation

Reif, D. W., Samokyszyn, V. M., Miller, D. M., & Aust, S. D. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90124-0 · Cited by 18 · see citing works

Radical chemistry of alloxan-dialuric acid: role of the superoxide radical.

Houée‐Levin, C., Gardès-Albert, M., Pucheault, J., & Ferradini, C. (1981) · PubMed · Cited by 12 · see citing works

Role of free radicals in biological systems

Bisby, R. H. (1993) · Endeavour · doi:10.1016/0160-9327(93)90080-m · Cited by 11 · see citing works

Effects of (+)-1,2-bis(3,5-dioxopiperazin-1-yl)propane (ADR-529) on iron-catalyzed lipid peroxidation

Ryan, T. P., Samokyszyn, V. M., Dellis, S., & Aust, S. D. (1990) · Chemical Research in Toxicology · doi:10.1021/tx00016a018 · Cited by 8 · see citing works

Iron release from ferritin and generation of hydroxyl radical in the reaction system of alloxan with reduced glutathione; A role of ferritin in alloxan toxicity.

Sakurai, K., & Miura, T. (1988) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.36.4534 · Cited by 7 · see citing works

The ferritins: molecular properties, iron storage function and cellular regulation

Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667 · see citing works

Toxicity of iron and hydrogen peroxide: the Fenton reaction

Winterbourn, C. C. (1995) · Toxicology Letters · doi:10.1016/0378-4274(95)03532-x · Cited by 1,415 · see citing works

Potential toxicity of superparamagnetic iron oxide nanoparticles (SPION)

Singh, N., Jenkins, G. J. S., Asadi, R., & Doak, S. H. (2010) · Nano Reviews · doi:10.3402/nano.v1i0.5358 · Cited by 1,112 · see citing works

Ascorbic acid: Chemistry, biology and the treatment of cancer

Du, J., Cullen, J. J., & Buettner, G. R. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.06.003 · Cited by 1,071 · see citing works

Catalytic Metals, Ascorbate and Free Radicals: Combinations to Avoid

Buettner, G. R., & Jurkiewicz, B. A. (1996) · Radiation Research · doi:10.2307/3579271 · Cited by 884 · see citing works

The heme synthesis and degradation pathways: role in oxidant sensitivity

Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 822 · see citing works

Cross-Talk Between Iron Metabolism and Diabetes

Fernández-Real, J. M., López-Bermejo, A., & Ricart, W. (2002) · Diabetes · doi:10.2337/diabetes.51.8.2348 · Cited by 704 · see citing works

Formation, Prevention, and Repair of DNA Damage by Iron/Hydrogen Peroxide

Henle, E. S., & Linn, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.31.19095 · Cited by 582 · see citing works

Biomarkers of Oxidative Stress and Antioxidant Defense

Çekiç, S. D., Özkan, G., Avan, A. N., Uzunboy, S., Çapanoğlu, E., & Apak, R. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114477 · Cited by 601 · see citing works

Iron Homeostasis, Oxidative Stress, and DNA Damage

Meneghini, R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00016-6 · Cited by 578 · see citing works

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works

Oxidative stress: Free radical production in neural degeneration

Götz, M. E., Künig, G., Riederer, P. F., & Youdim, M. B. H. (1994) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(94)90055-8 · Cited by 479 · see citing works

Mechanism of Lipid Peroxidation in Meat and Meat Products -A Review

Min, B. R., & Ahn, D. U. (2005) · Food Science and Biotechnology · Cited by 460 · see citing works

Aging and oxidative stress: Modulation by dietary restriction

Yu, B. P. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(96)00162-1 · Cited by 443 · see citing works

Reversal of HO‐1 related cytoprotection with increased expression is due to reactive iron

Suttner, D. M., & Dennery, P. A. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.13.1800 · Cited by 426 · see citing works

Body Iron Stores and the Risk of Carotid Atherosclerosis: Prospective Results From the Bruneck Study

Kiechl, S., Willeit, J., Egger, G., Poewe, W., & Oberhollenzer, F. (1997) · Circulation · doi:10.1161/01.cir.96.10.3300 · Cited by 390 · see citing works

EPR characterization of molecular targets for NO in mammalian cells and organelles

Henry, Y. A., Lepoivre, M., Drapier, J., Ducrocq, C., Boucher, J., & Guissani, A. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.12.8397130 · Cited by 367 · see citing works

Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples

Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works

Serum Ferritin as a Component of the Insulin Resistance Syndrome

Fernández-Real, J.-M., Ricart-Engel, W., Arroyo, E., Balançá, R., Casamitjana-Abella, R., Cabrero, D., Fernández-Castañer, M., & Soler, J. (1998) · Diabetes Care · doi:10.2337/diacare.21.1.62 · Cited by 328 · see citing works

Induction of Ferritin Synthesis by Oxidative Stress

Cairo, G., Tacchini, L., Pogliaghi, G., Anzon, E., Tomasi, A., & Bernelli‐Zazzera, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.700 · Cited by 322 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., Yoshimasu, F., & Kitamoto, T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.t01-1-01061.x · Cited by 313 · see citing works

Iron-dependent oxygen free radical generation in plants subjected to environmental stress: toxicity and antioxidant protection

Becana, M., Morán, J. F., & Iturbe‐Ormaetxe, I. (1998) · Plant and Soil · doi:10.1023/a:1004375732137 · Cited by 312 · see citing works

Citrate – new functions for an old metabolite

Iacobazzi, V., & Infantino, V. (2014) · Biological Chemistry · doi:10.1515/hsz-2013-0271 · Cited by 285 · see citing works

Apoptosis induced by exposure to a low steady-state concentration of H2O2 is a consequence of lysosomal rupture

Antunes, F., Cadenas, E., & Brunk, U. T. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560549 · Cited by 286 · see citing works

Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Yamamoto, A., Shin, R., Hasegawa, K., Naiki, H., Sato, H., YOSHIMASU, F., & Kitamoto, T. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01061.x · Cited by 246 · see citing works

Chapter 1: Developmental, Cellular, and Molecular Basis of Human Breast Cancer

Russo, J., Hu, Y.-F., Yang, X., & Russo, I. H. (2000) · JNCI Monographs · doi:10.1093/oxfordjournals.jncimonographs.a024241 · Cited by 241 · see citing works

Brain iron metabolism: Neurobiology and neurochemistry

Ke, Y., & Qian, Z. (2007) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2007.07.009 · Cited by 236 · see citing works

Increased excretion of a lipid peroxidation biomarker in autism

Ming, X., Stein, T. P., Brimacombe, M., Johnson, W. G., Lambert, G. H., & Wagner, G. C. (2005) · Prostaglandins, Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2005.06.002 · Cited by 236 · see citing works

Iron and neurodegenerative disorders

Thompson, K. J., Shoham, S., & Connor, J. R. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00510-x · Cited by 235 · see citing works

Iron, Free Radicals, and Oxidative Injury

McCord, J. M. (2004) · Journal of Nutrition · doi:10.1093/jn/134.11.3171s · Cited by 232 · see citing works

Prooxidant effects of phenolic acids on the generalist herbivore Helicoverpa zea (Lepidoptera: Noctuidae): Potential mode of action for phenolic compounds in plant anti-herbivore chemistry

Summers, C. B., & Felton, G. W. (1994) · Insect Biochemistry and Molecular Biology · doi:10.1016/0965-1748(94)90023-x · Cited by 225 · see citing works

Arsenic Species That Cause Release of Iron from Ferritin and Generation of Activated Oxygen

Ahmad, S., Kitchin, K. T., & Cullen, W. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2023 · Cited by 215 · see citing works

Heme, Heme Oxygenase, and Ferritin: How the Vascular Endothelium Survives (and Dies) in an Iron-Rich Environment

Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Jacob, H. S., Eaton, J. W., & Balla, G. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1787 · Cited by 212 · see citing works

Deleterious iron-mediated oxidation of biomolecules1 1This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal. 6 6Guest Editor: Mario Comporti

Welch, K. D., Davis, T. Z., Van Eden, M. E., & Aust, S. D. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00760-8 · Cited by 205 · see citing works

Are iron oxide nanoparticles safe? Current knowledge and future perspectives

Valdiglesias, V., Fernández‐Bertólez, N., Kılıç, G., Costa, C., Costa, S., Fraga, S., Bessa, M. J., Pásaro, E., Teixeira, J. P., & Laffón, B. (2016) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.03.017 · Cited by 204 · see citing works

Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions

Boutet, I., Tanguy, A., & Moraga, D. (2004) · Gene · doi:10.1016/j.gene.2003.12.027 · Cited by 203 · see citing works

Iron release, oxidative stress and erythrocyte ageing2 2Guest Editor: Mario Comporti 3 3This article is part of a series of reviews on “Iron and Cellular Redox Status.” The full list of papers may be found on the homepage of the journal.

Comporti, M., Signorini, C., Buonocore, G., & Ciccoli, L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00759-1 · Cited by 200 · see citing works

Protective effects of tea polyphenols against oxidative damage to red blood cells

Grinberg, L. N., Newmark, H., Kitrossky, N., Rahamim, E., Chevion, M., & Rachmilewitz, E. A. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00155-x · Cited by 187 · see citing works

Brain Iron Metabolism Dysfunction in Parkinson’s Disease

Jiang, H. F., Wang, J., Rogers, J. T., & Xie, J. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9879-1 · Cited by 183 · see citing works

Anticarcinogenic Factors in Plant Foods: A New Class of Nutrients?

Johnson, I. T., Williamson, G., & Musk, S. R. R. (1994) · Nutrition Research Reviews · doi:10.1079/nrr19940011 · Cited by 181 · see citing works

Ultraviolet A radiation induces immediate release of iron in human primary skin fibroblasts: The role of ferritin

Pourzand, C., Watkin, R. D., Brown, J. E., & Tyrrell, R. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6751 · Cited by 176 · see citing works

Intralysosomal iron chelation protects against oxidative stress‐induced cellular damage

Kurz, T., Gustafsson, B., & Brunk, U. T. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05321.x · Cited by 175 · see citing works

The neglected significance of “antioxidative stress”

Poljsak, B., & Milisav, I. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/480895 · Cited by 177 · see citing works

Oxidative Stress Induced in Microorganisms by Zero-valent Iron Nanoparticles

Ševců, A., El-Temsah, Y. S., Joner, E. J., & Černík, M. (2011) · Microbes and Environments · doi:10.1264/jsme2.me11126 · Cited by 175 · see citing works

Hepcidin Is Down‐regulated in Alcoholic Liver Injury: Implications for the Pathogenesis of Alcoholic Liver Disease

Bridle, K. R., Cheung, T., Murphy, T. L., Walters, M. M., Anderson, G. J., Crawford, D. H., & Fletcher, L. M. (2006) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2006.00002.x · Cited by 165 · see citing works

Does low meat consumption increase life expectancy in humans?

Singh, P. N., Sabaté, J., & Fraser, G. E. (2003) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/78.3.526s · Cited by 158 · see citing works

Increased ferritin gene expression in atherosclerotic lesions.

Pang, J. H., Jiang, M. J., Chen, Y., Wang, F. W., Wang, D. L., Chu, S., & Chau, L. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118661 · Cited by 162 · see citing works

Mammary epithelial stem cells

Smith, G. H., & Chepko, G. (2001) · Microscopy Research and Technique · doi:10.1002/1097-0029(20010115)52:2 · Cited by 173 · see citing works

Bacillus subtilis aconitase is an RNA-binding protein

Amaro, C. A., & Sonenshein, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10412 · Cited by 159 · see citing works

The Role of Iron in the Pathogenesis of Experimental Allergic Encephalomyelitis and Multiple Sclerosis

Levine, S. M., & Chakrabarty, A. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.021 · Cited by 183 · see citing works

The role of iron neurotoxicity in ischemic stroke

Selim, M. H., & Ratan, R. R. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.04.001 · Cited by 158 · see citing works

c-Jun NH2-Terminal Kinase Signaling Axis Regulates Diallyl Trisulfide–Induced Generation of Reactive Oxygen Species and Cell Cycle Arrest in Human Prostate Cancer Cells

Antosiewicz, J., Herman-Antosiewicz, A., Marynowski, S. W., & Singh, S. V. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0356 · Cited by 156 · see citing works

Potentiation of hydrogen peroxide toxicity: From catalase inhibition to stable DNA-iron complexes

Mahaseth, T., & Kuzminov, A. (2016) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2016.08.006 · Cited by 151 · see citing works

Effects of Positive Iron Status at a Cellular Level

McCord, J. M. (2009) · Nutrition Reviews · doi:10.1111/j.1753-4887.1996.tb03876.x · Cited by 150 · see citing works

Dietary iron intake and Type 2 diabetes incidence in postmenopausal women: the Iowa Women’s Health Study

Lee, D.-H., Folsom, A. R., & Jacobs, D. R. (2004) · Diabetologia · doi:10.1007/s00125-003-1307-1 · Cited by 146 · see citing works

The Relationship between Intracellular Free Iron and Cell Injury in Cultured Neurons, Astrocytes, and Oligodendrocytes

Kress, G. J., Dineley, K. E., & Reynolds, I. J. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-14-05848.2002 · Cited by 143 · see citing works

Iron supplementation generates hydroxyl radical in vivo. An ESR spin-trapping investigation.

Kadiiska, M. B., Burkitt, M. J., Xiang, Q.-H., & Mason, R. P. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118205 · Cited by 140 · see citing works

Body iron stores and early neurologic deterioration in acute cerebral infarction

Dávalos, A., Castillo, J., Marrugat, J., Fernández‐Real, J. M., Armengou, A., Cacabelos, P., & Rama, R. (2000) · Neurology · doi:10.1212/wnl.54.8.1568 · Cited by 140 · see citing works

Ferritin protects endothelial cells from oxidized low density lipoprotein in vitro.

Juckett, M., Balla, J., Balla, G., Jessurun, J., Jacob, H. S., & Vercellotti, G. M. (1995) · Europe PMC (PubMed Central) · Cited by 139 · see citing works

Ferritin in atherosclerosis

You, S.-A., & Wang, Q. K. (2005) · Clinica Chimica Acta · doi:10.1016/j.cccn.2005.02.001 · Cited by 135 · see citing works

Reduced oxidative and nitrosative damage in murine experimental colitis in the absence of inducible nitric oxide synthase

Zingarelli, B., Szabó, C., & Salzman, A. L. (1999) · Gut · doi:10.1136/gut.45.2.199 · Cited by 136 · see citing works

Serum ferritin and risk of myocardial infarction in the elderly: the Rotterdam Study

Klipstein‐Grobusch, K., Koster, J. F., Grobbee, D. E., Lindemans, J. W., Boeing, H., Albert Hofman, D., & Witteman, J. C. M. (1999) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/69.6.1231 · Cited by 135 · see citing works

Heme Oxygenase-mediated Resistance to Oxygen Toxicity in Hamster Fibroblasts

Dennery, P. A., Sridhar, K. J., Lee, C. S., Wong, H. E., Shokoohi, V., Rodgers, P. A., & Spitz, D. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14937 · Cited by 135 · see citing works

Proteomic approach to coronary atherosclerosis shows ferritin light chain as a significant marker: evidence consistent with iron hypothesis in atherosclerosis

You, S.-A., Archacki, S. R., Angheloiu, G. O., Moravec, C. S., Rao, S., Kinter, M. T., Topol, E. J., & Wang, Q. K. (2003) · Physiological Genomics · doi:10.1152/physiolgenomics.00124.2002 · Cited by 134 · see citing works

Iron and 8-isoprostane levels in acute and chronic wounds

Yeoh-Ellerton, S., & Stacey, M. C. (2003) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2003.12471.x · Cited by 125 · see citing works

Cytochrome P-450 mediates tissue-damaging hydroxyl radical formation during reoxygenation of the kidney.

Paller, M. S., & Jacob, H. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.7002 · Cited by 125 · see citing works

Heme, heme oxygenase and ferritin in vascular endothelial cell injury

Balla, J., Vercellotti, G. M., Jeney, V., Yachie, A., Varga, Z., Eaton, J. W., & Balla, G. (2005) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200500076 · Cited by 123 · see citing works

Protein hydroperoxides as new reactive oxygen species

Gebicki, J. M. (1997) · Redox Report · doi:10.1080/13510002.1997.11747096 · Cited by 121 · see citing works

The dark side of gamma-glutamyltransferase (GGT): Pathogenic effects of an ‘antioxidant’ enzyme

Corti, A., Belcastro, E., Dominici, S., Maellaro, E., & Alfonso Pompella, C. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.09.005 · Cited by 120 · see citing works

Antioxidative and Metal-Chelating Effects of Polyamines

Løvaas, E. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60982-5 · Cited by 116 · see citing works

Gestational Diabetes Mellitus in Relation to Maternal Dietary Heme Iron and Nonheme Iron Intake

Qiu, C., Zhang, C., Gelaye, B., Enquobahrie, D. A., Frederick, I. O., & Williams, M. A. (2011) · Diabetes Care · doi:10.2337/dc11-0135 · Cited by 115 · see citing works

Nrf2 Activator PB125® as a Potential Therapeutic Agent against COVID-19

McCord, J. M., Hybertson, B. M., Cota‐Gomez, A., Geraci, K. P., & Gao, B. (2020) · Antioxidants · doi:10.3390/antiox9060518 · Cited by 114 · see citing works

Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei

Thompson, K. J., Fried, M. G., Ye, Z., Boyer, P., & Connor, J. R. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.10.2165 · Cited by 110 · see citing works

Patterns of 8-hydroxydeoxyguanosine formation in DNA and indications of oxidative stress in rat and human pleural mesothelial cells after exposure to crocidolite asbestos

Fung, H. (1997) · Carcinogenesis · doi:10.1093/carcin/18.4.825 · Cited by 110 · see citing works

Commentary: The Role of Iron-Sulfur Clusters inin vivoHydroxyl Radical Production

Liochev, S. I. (1996) · Free Radical Research · doi:10.3109/10715769609149059 · Cited by 112 · see citing works

Increased concentrations of iron and isoferritins in the lower respiratory tract of patients with stable cystic fibrosis

STITES, S. W., PLAUTZ, M. W., BAILEY, K., O'BRIEN-LADNER, A. R., & WESSELIUS, L. J. (1999) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm.160.3.9811018 · Cited by 109 · see citing works

The importance of eukaryotic ferritins in iron handling and cytoprotection

Arosio, P., Carmona, F., Gozzelino, R., Maccarinelli, F., & Poli, M. (2015) · Biochemical Journal · doi:10.1042/bj20150787 · Cited by 104 · see citing works

Egg Yolk Phosvitin Inhibits Hydroxyl Radical Formation from the Fenton Reaction

ISHIKAWA, S.-I., Yano, Y., Arihara, K., & Makoto, I. T. O. H. (2004) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.68.1324 · Cited by 108 · see citing works

Increased Iron and Ferritin Content of Sputum From Patients With Cystic Fibrosis or Chronic Bronchitis

Stites, S. W., Walters, B., O'Brien-Ladner, A. R., Bailey, K., & Wesselius, L. (1998) · CHEST Journal · doi:10.1378/chest.114.3.814 · Cited by 95 · see citing works

Quantitative structure–activity relationships in prooxidant cytotoxicity of polyphenols: Role of potential of phenoxyl radical/phenol redox couple

Nemeikaitė-Čėnienė, A., Imbrasaitė, A., Sergedienė, E., & Čėnas, N. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.07.002 · Cited by 93 · see citing works

Increased Body Iron Stores Are Associated With Poor Outcome After Thrombolytic Treatment in Acute Stroke

Millan, M., Sobrino, T., Castellanos, M., Nombela, F., Arenillas, J. F., Riva, E., Cristobo, I., García, M. M., Vivancos, J., Serena, J., et al. (2007) · Stroke · doi:10.1161/01.str.0000251798.25803.e0 · Cited by 92 · see citing works

SIH—a novel lipophilic iron chelator—protects H9c2 cardiomyoblasts from oxidative stress-induced mitochondrial injury and cell death

Šimůnek, T., Boer, C., Bouwman, R. A., VLASBLOM, R., Versteilen, A. M. G., Štěrba, M., Geršl, V., Hrdina, R., Poňka, P., & DELANGE, J. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.05.008 · Cited by 91 · see citing works

Exposure to Metal Fume and Infectious Pneumonia

Palmer, K. T. (2003) · American Journal of Epidemiology · doi:10.1093/aje/kwf188 · Cited by 88 · see citing works

The Protective Role of Endogenous Estrogens in Carrageenan-Induced Lung Injury in the Rat

Cuzzocrea, S., Mazzon, E., Sautebin, L., Serraino, I., Dugo, L., Calabrò, G., Caputi, A. P., & Maggi, A. C. (2001) · Molecular Medicine · doi:10.1007/bf03401853 · Cited by 87 · see citing works

Formation of DNA-protein cross-links in cultured mammalian cells upon treatment with iron ions

Altman, S. A., Zastawny, T. H., Randers‐Eichhorn, L., Cacciuttolo, M. A., Akman, S. A., Dizdaroğlu, M., & Rao, G. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)00095-f · Cited by 86 · see citing works

Effects of iron and iron chelation in vitro on mucosal oxidant activity in ulcerative colitis

Millar, Rampton, D. S., & Blake (2000) · Alimentary Pharmacology & Therapeutics · doi:10.1046/j.1365-2036.2000.00828.x · Cited by 86 · see citing works

Interrelationships of alcohol and iron in liver disease with particular reference to the iron‐binding proteins, ferritin and transferrin

Fletcher, L. M., Halliday, J. W., & Powell, L. W. (1999) · Journal of Gastroenterology and Hepatology · doi:10.1046/j.1440-1746.1999.01836.x · Cited by 84 · see citing works

Oxidation-induced ferritin turnover in microglial cells: role of proteasome

Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84 · see citing works

Polyunsaturated fatty acids increase lipid radical formation induced by oxidant stress in endothelial cells

Alexander-North, L. S., North, J. A., Kiminyo, K. P., Buettner, G. R., & Spector, A. A. (1994) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39772-8 · Cited by 85 · see citing works

Ferritin levels predict severe dengue

Soundravally, R., Agieshkumar, B., Samadanam, D. M., Sherin, J., & Cherupanakkal, C. (2014) · Infection · doi:10.1007/s15010-014-0683-4 · Cited by 84 · see citing works

A re-evaluation of the tissue distribution and physiology of xanthine oxidoreductase

Kooij, A. (1994) · The Histochemical Journal · doi:10.1007/bf00174006 · Cited by 84 · see citing works

Interdependence of tetrapyrrole metabolism, the generation of oxidative stress and the mitigative oxidative stress response

Busch, A. W. U., & Montgomery, B. L. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.010 · Cited by 82 · see citing works

DNA base modifications and membrane damage in cultured mammalian cells treated with iron ions

Zastawny, T. H., Altman, S. A., Randers‐Eichhorn, L., Madurawe, R. D., Lumpkin, J. A., Dizdaroğlu, M., & Rao, G. (1995) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)00241-b · Cited by 81 · see citing works

Secondary alcohol metabolites mediate iron delocalization in cytosolic fractions of myocardial biopsies exposed to anticancer anthracyclines. Novel linkage between anthracycline metabolism and iron-induced cardiotoxicity.

Minotti, G., Cavaliere, A. F., Mordente, A., Rossi, M., Schiavello, R., Zamparelli, R., & Possati, G. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117833 · Cited by 81 · see citing works

Potential Use of Iron Chelators against Oxidative Damage

Galey, J.-B. (1996) · Advances in pharmacology · doi:10.1016/s1054-3589(08)60984-9 · Cited by 80 · see citing works

Ebselen inhibits iron-induced tau phosphorylation by attenuating DMT1 up-regulation and cellular iron uptake

Xie, L., Zheng, W. H., Xin, N., Xie, J., Wang, T., & Wang, Z. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.05.016 · Cited by 79 · see citing works

Airway iron and iron-regulatory cytokines in cystic fibrosis

Reid, D. W., Lam, Q. T., Schneider, H. G., & Walters, E. H. (2004) · European Respiratory Journal · doi:10.1183/09031936.04.00104803 · 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

Melatonin controls oxidative stress and modulates iron, ferritin, and transferrin levels in adriamycin treated rats

Othman, A. I., El-Missiry, M. A., Amer, M. A., & Arafa, M. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.08.004 · Cited by 78 · see citing works

Antioxidant properties of omeprazole

Lapenna, D., de Gioia, S., Ciofani, G., Festi, D., & Cuccurullo, F. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00155-x · Cited by 78 · see citing works

On the limited ability of superoxide to release iron from ferritin

Bolann, B. J., & Ulvik, R. J. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19415.x · Cited by 111 · see citing works

Effect of a Prolonged Superoxide Flux on Transferrin and Ferritin

Paul, T. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.2027 · Cited by 30 · see citing works

Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.

Biemond, P., van Eijk, H. G., Swaak, A. J., & Koster, J. F. (1984) · Journal of Clinical Investigation · doi:10.1172/jci111364 · Cited by 380 · see citing works

Iron release from ferritin and its sensitivity to superoxide ions differs among vertebrates

Harris, L. R., Cake, M. H., & Macey, D. J. (1994) · Biochemical Journal · doi:10.1042/bj3010385 · Cited by 43 · see citing works

Reductive release of iron from ferritin by cation free radicals of paraquat and other bipyridyls.

Thomas, C. E., & Aust, S. D. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69271-3 · Cited by 167 · see citing works