{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T16:00:36Z","timestamp":1791216036287,"version":"4.1.0"},"reference-count":57,"publisher":"Elsevier BV","issue":"4-5","license":[{"start":{"date-parts":[[2005,8,1]],"date-time":"2005-08-01T00:00:00Z","timestamp":1122854400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Aspects of Medicine"],"published-print":{"date-parts":[[2005,8]]},"DOI":"10.1016\/j.mam.2005.07.006","type":"journal-article","created":{"date-parts":[[2005,8,16]],"date-time":"2005-08-16T11:12:51Z","timestamp":1124190771000},"page":"340-352","source":"Crossref","is-referenced-by-count":364,"title":["Superoxide dismutases and their impact upon human health"],"prefix":"10.1016","volume":"26","author":[{"given":"Felicity","family":"Johnson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cecilia","family":"Giulivi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"10","key":"10.1016\/j.mam.2005.07.006_bib1","doi-asserted-by":"crossref","first-page":"9640","DOI":"10.1074\/jbc.M413840200","article-title":"The copper-transporting ATPases, Menkes and Wilson disease proteins, have distinct roles in adult and developing cerebellum","volume":"280","author":"Barnes","year":"2005","journal-title":"J Biol Chem"},{"issue":"10","key":"10.1016\/j.mam.2005.07.006_bib2","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/S0891-5849(02)01092-4","article-title":"CCS knockout mice establish an alternative source of copper for SOD in ALS","volume":"33","author":"Beckman","year":"2002","journal-title":"Free Radic Biol Med"},{"issue":"3","key":"10.1016\/j.mam.2005.07.006_bib3","doi-asserted-by":"crossref","first-page":"676","DOI":"10.1152\/ajpgi.00049.2004","article-title":"Chimeric SOD2\/3 inhibits at the endothelial\u2013neutrophil interface to limit vascular dysfunction in ischemia-reperfusion","volume":"287","author":"Bonder","year":"2004","journal-title":"Am J Physiol Gastrointest Liver Physiol"},{"issue":"Suppl 1","key":"10.1016\/j.mam.2005.07.006_bib4","doi-asserted-by":"crossref","first-page":"S13","DOI":"10.1016\/j.jhep.2004.11.013","article-title":"Wilson\u2019s disease: clinical management and therapy","volume":"42","author":"Brewer","year":"2005","journal-title":"J Hepatol"},{"issue":"11","key":"10.1016\/j.mam.2005.07.006_bib5","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.freeradbiomed.2005.01.019","article-title":"Reactive oxygen species and the modulation of stroke","volume":"38","author":"Crack","year":"2005","journal-title":"Free Radic Biol Med"},{"issue":"5","key":"10.1016\/j.mam.2005.07.006_bib6","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1046\/j.1471-4159.1997.69051936.x","article-title":"Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite","volume":"69","author":"Crow","year":"1997","journal-title":"J Neurochem"},{"issue":"1","key":"10.1016\/j.mam.2005.07.006_bib7","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/S0165-0173(02)00219-9","article-title":"Zinc takes the center stage: its paradoxical role in Alzheimer\u2019s disease","volume":"41","author":"Cuajungco","year":"2003","journal-title":"Brain Res Brain Res Rev"},{"issue":"2","key":"10.1016\/j.mam.2005.07.006_bib8","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1074\/jbc.M106589200","article-title":"Diffusion of nitric oxide into low density lipoprotein","volume":"277","author":"Denicola","year":"2002","journal-title":"J Biol Chem"},{"issue":"7","key":"10.1016\/j.mam.2005.07.006_bib9","doi-asserted-by":"crossref","first-page":"3566","DOI":"10.1073\/pnas.95.7.3566","article-title":"Diffusion of peroxynitrite across erythrocyte membranes","volume":"95","author":"Denicola","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"10.1016\/j.mam.2005.07.006_bib10","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1038\/sj.onc.1208207","article-title":"Cu, Zn-SOD deficiency leads to persistent and widespread oxidative damage and hepatocarcinogenesis later in life","volume":"24","author":"Elchuri","year":"2005","journal-title":"Oncogene"},{"issue":"1","key":"10.1016\/j.mam.2005.07.006_bib11","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.neulet.2004.12.045","article-title":"Protection by dietary zinc in ALS mutant G93A SOD transgenic mice","volume":"379","author":"Ermilova","year":"2005","journal-title":"Neurosci Lett"},{"issue":"5449","key":"10.1016\/j.mam.2005.07.006_bib12","doi-asserted-by":"crossref","first-page":"2498","DOI":"10.1126\/science.286.5449.2498","article-title":"Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase","volume":"286","author":"Estevez","year":"1999","journal-title":"Science"},{"issue":"30","key":"10.1016\/j.mam.2005.07.006_bib13","doi-asserted-by":"crossref","first-page":"28052","DOI":"10.1074\/jbc.M304296200","article-title":"Factors controlling the uptake of yeast copper\/zinc superoxide dismutase into mitochondria","volume":"278","author":"Field","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.mam.2005.07.006_bib14","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1146\/annurev.bi.64.070195.000525","article-title":"Superoxide radical and superoxide dismutases","volume":"64","author":"Fridovich","year":"1995","journal-title":"Annu Rev Biochem"},{"issue":"17","key":"10.1016\/j.mam.2005.07.006_bib15","doi-asserted-by":"crossref","first-page":"17266","DOI":"10.1074\/jbc.M500482200","article-title":"Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation","volume":"280","author":"Furukawa","year":"2005","journal-title":"J Biol Chem"},{"issue":"6","key":"10.1016\/j.mam.2005.07.006_bib16","doi-asserted-by":"crossref","first-page":"L917","DOI":"10.1152\/ajplung.00374.2002","article-title":"Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2\/3","volume":"284","author":"Gao","year":"2003","journal-title":"Am J Physiol Lung Cell Mol Physiol"},{"key":"10.1016\/j.mam.2005.07.006_bib17","series-title":"Reactive Oxygen Species","article-title":"The steady-state concentrations of oxygen radicals in mitochondria","author":"Giulivi","year":"1999"},{"issue":"5166","key":"10.1016\/j.mam.2005.07.006_bib18","doi-asserted-by":"crossref","first-page":"1772","DOI":"10.1126\/science.8209258","article-title":"Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation","volume":"264","author":"Gurney","year":"1994","journal-title":"Science"},{"issue":"4","key":"10.1016\/j.mam.2005.07.006_bib19","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/j.biopha.2005.03.001","article-title":"Anti-inflammatory properties of a chimeric recombinant superoxide dismutase: SOD2\/3","volume":"59","author":"Hernandez-Saavedra","year":"2005","journal-title":"Biomed Pharmacother"},{"issue":"3","key":"10.1016\/j.mam.2005.07.006_bib20","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1097\/00024382-200209000-00005","article-title":"Superoxide dismutase mimetics with catalase activity reduce the organ injury in hemorrhagic shock","volume":"18","author":"Izumi","year":"2002","journal-title":"Shock"},{"issue":"20","key":"10.1016\/j.mam.2005.07.006_bib21","doi-asserted-by":"crossref","first-page":"7133","DOI":"10.1073\/pnas.0502594102","article-title":"Perinatal {omega}-3 polyunsaturated fatty acid supply modifies brain zinc homeostasis during adulthood","volume":"102","author":"Jayasooriya","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"10.1016\/j.mam.2005.07.006_bib22","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/S0891-5849(02)00741-4","article-title":"Aggregation of alpha-synuclein induced by the Cu, Zn-superoxide dismutase and hydrogen peroxide system","volume":"32","author":"Kim","year":"2002","journal-title":"Free Radic Biol Med"},{"issue":"11","key":"10.1016\/j.mam.2005.07.006_bib23","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1021\/tx970160x","article-title":"Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis","volume":"10","author":"Kissner","year":"1998","journal-title":"Chem Res Toxicol"},{"issue":"5","key":"10.1016\/j.mam.2005.07.006_bib24","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/0891-5849(94)90061-2","article-title":"Differential regulation of superoxide dismutase in copper-deficient rat organs","volume":"16","author":"Lai","year":"1994","journal-title":"Free Radic Biol Med"},{"issue":"3","key":"10.1016\/j.mam.2005.07.006_bib25","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.mad.2004.08.012","article-title":"Superoxide dismutase evolution and life span regulation","volume":"126","author":"Landis","year":"2005","journal-title":"Mech Ageing Dev"},{"issue":"12","key":"10.1016\/j.mam.2005.07.006_bib26","first-page":"2260","article-title":"Zinc, copper, and superoxide dismutase in hepatocellular carcinoma","volume":"92","author":"Liaw","year":"1997","journal-title":"Am J Gastroenterol"},{"key":"10.1016\/j.mam.2005.07.006_bib27","doi-asserted-by":"crossref","unstructured":"Luk, E., Yang, M., Jensen, L.T., Bourbonnais, Y., Culotta, V.C., 2005. Manganese activation of superoxide dismutase 2 in the mitochondria of Saccharomyces cerevisiae. J Biol Chem. Apr 25; [Epub ahead of print].","DOI":"10.1074\/jbc.M504257200"},{"issue":"18","key":"10.1016\/j.mam.2005.07.006_bib28","doi-asserted-by":"crossref","first-page":"10353","DOI":"10.1073\/pnas.1632471100","article-title":"Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1, a member of the mitochondrial carrier family","volume":"100","author":"Luk","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"10.1016\/j.mam.2005.07.006_bib29","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/bj2200269","article-title":"Properties of extracellular superoxide dismutase from human lung","volume":"220","author":"Marklund","year":"1984","journal-title":"Biochem J"},{"issue":"24","key":"10.1016\/j.mam.2005.07.006_bib30","doi-asserted-by":"crossref","first-page":"7634","DOI":"10.1073\/pnas.79.24.7634","article-title":"Human copper-containing superoxide dismutase of high molecular weight","volume":"79","author":"Marklund","year":"1982","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.mam.2005.07.006_bib31","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1007\/978-1-4684-3270-1_45","article-title":"Iron- and manganese-containing superoxide dismutases: structure, distribution, and evolutionary relationships","volume":"74","author":"McCord","year":"1976","journal-title":"Adv Exp Med Biol"},{"issue":"22","key":"10.1016\/j.mam.2005.07.006_bib32","doi-asserted-by":"crossref","first-page":"6049","DOI":"10.1016\/S0021-9258(18)63504-5","article-title":"Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)","volume":"244","author":"McCord","year":"1969","journal-title":"J Biol Chem"},{"issue":"11","key":"10.1016\/j.mam.2005.07.006_bib33","doi-asserted-by":"crossref","first-page":"2249","DOI":"10.1016\/j.bcp.2004.08.003","article-title":"A gene expression signature for oxidant stress\/reactive metabolites in rat liver","volume":"68","author":"McMillian","year":"2004","journal-title":"Biochem Pharmacol"},{"issue":"2","key":"10.1016\/j.mam.2005.07.006_bib34","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/S1471-4914(01)01920-7","article-title":"The molecular basis of copper-transport diseases","volume":"7","author":"Mercer","year":"2001","journal-title":"Trends Mol Med"},{"issue":"2","key":"10.1016\/j.mam.2005.07.006_bib35","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.cbpa.2004.02.011","article-title":"Superoxide dismutases: active sites that save, but a protein that kills","volume":"8","author":"Miller","year":"2004","journal-title":"Curr Opin Chem Biol"},{"issue":"10","key":"10.1016\/j.mam.2005.07.006_bib36","doi-asserted-by":"crossref","first-page":"8850","DOI":"10.1074\/jbc.M413699200","article-title":"Direct measurement of nitric oxide and oxygen partitioning into liposomes and low density lipoprotein","volume":"280","author":"Moller","year":"2005","journal-title":"J Biol Chem"},{"issue":"1","key":"10.1016\/j.mam.2005.07.006_bib37","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1139\/o04-100","article-title":"Rose (Rosa rugosa)-flower extract increases the activities of antioxidant enzymes and their gene expression and reduces lipid peroxidation","volume":"83","author":"Ng","year":"2005","journal-title":"Biochem Cell Biol"},{"issue":"1\u20132","key":"10.1016\/j.mam.2005.07.006_bib38","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/s11010-005-3639-2","article-title":"Hierarchical change in antioxidant enzyme gene expression and activity in acute cardiac rejection: role of inducible nitric oxide synthase","volume":"270","author":"Nilakantan","year":"2005","journal-title":"Mol Cell Biochem"},{"issue":"2","key":"10.1016\/j.mam.2005.07.006_bib39","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0891-5849(88)90036-6","article-title":"Free radicals and diabetes","volume":"5","author":"Oberley","year":"1988","journal-title":"Free Radic Biol Med"},{"issue":"3","key":"10.1016\/j.mam.2005.07.006_bib40","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1089\/152308604773934242","article-title":"Mitochondria, manganese superoxide dismutase, and cancer","volume":"6","author":"Oberley","year":"2004","journal-title":"Antioxid Redox Signal"},{"issue":"1","key":"10.1016\/j.mam.2005.07.006_bib41","doi-asserted-by":"crossref","first-page":"85","DOI":"10.3181\/00379727-213-44040","article-title":"Oxidant defense systems in testes from zinc-deficient rats","volume":"213","author":"Oteiza","year":"1996","journal-title":"Proc Soc Exp Biol Med"},{"issue":"8","key":"10.1016\/j.mam.2005.07.006_bib42","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/S0009-9120(02)00363-6","article-title":"Increased oxidative stress and hypozincemia in male obesity","volume":"35","author":"Ozata","year":"2002","journal-title":"Clin Biochem"},{"issue":"6122","key":"10.1016\/j.mam.2005.07.006_bib43","doi-asserted-by":"crossref","first-page":"524","DOI":"10.1038\/327524a0","article-title":"Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor","volume":"327","author":"Palmer","year":"1987","journal-title":"Nature"},{"issue":"1\u20132","key":"10.1016\/j.mam.2005.07.006_bib44","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0006-8993(02)03040-8","article-title":"Attenuation of zinc-induced intracellular dysfunction and neurotoxicity by a synthetic superoxide dismutase\/catalase mimetic, in cultured cortical neurons","volume":"950","author":"Pong","year":"2002","journal-title":"Brain Res"},{"issue":"2","key":"10.1016\/j.mam.2005.07.006_bib45","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1093\/jn\/134.2.416","article-title":"Contrasting and cooperative effects of copper and iron deficiencies in male rats fed different concentrations of manganese and different sources of sulfur amino acids in an AIN-93G-based diet","volume":"134","author":"Reeves","year":"2004","journal-title":"J Nutr"},{"issue":"43","key":"10.1016\/j.mam.2005.07.006_bib46","doi-asserted-by":"crossref","first-page":"33771","DOI":"10.1074\/jbc.M006254200","article-title":"Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein\u2013protein interactions with the copper chaperone for SOD1","volume":"275","author":"Schmidt","year":"2000","journal-title":"J Biol Chem"},{"issue":"52","key":"10.1016\/j.mam.2005.07.006_bib47","doi-asserted-by":"crossref","first-page":"36952","DOI":"10.1074\/jbc.274.52.36952","article-title":"A gain of superoxide dismutase (SOD) activity obtained with CCS, the copper metallochaperone for SOD1","volume":"274","author":"Schmidt","year":"1999","journal-title":"J Biol Chem"},{"issue":"34","key":"10.1016\/j.mam.2005.07.006_bib48","doi-asserted-by":"crossref","first-page":"23719","DOI":"10.1074\/jbc.274.34.23719","article-title":"Multiple protein domains contribute to the action of the copper chaperone for superoxide dismutase","volume":"274","author":"Schmidt","year":"1999","journal-title":"J Biol Chem"},{"issue":"4","key":"10.1016\/j.mam.2005.07.006_bib49","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.biopha.2005.03.004","article-title":"Modulation of skin tumorigenesis by SOD","volume":"59","author":"St Clair","year":"2005","journal-title":"Biomed Pharmacother"},{"issue":"41","key":"10.1016\/j.mam.2005.07.006_bib50","doi-asserted-by":"crossref","first-page":"38084","DOI":"10.1074\/jbc.M105296200","article-title":"A fraction of yeast Cu, Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage","volume":"276","author":"Sturtz","year":"2001","journal-title":"J Biol Chem"},{"issue":"11","key":"10.1016\/j.mam.2005.07.006_bib51","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1291\/hypres.27.877","article-title":"Calcium antagonist reduces oxidative stress by upregulating Cu\/Zn superoxide dismutase in stroke-prone spontaneously hypertensive rats","volume":"27","author":"Umemoto","year":"2004","journal-title":"Hypertens Res"},{"issue":"5","key":"10.1016\/j.mam.2005.07.006_bib52","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.jnutbio.2005.01.007","article-title":"Diabetes and dietary copper alter 67Cu metabolism and oxidant defense in the rat","volume":"16","author":"Uriu-Adams","year":"2005","journal-title":"J Nutr Biochem"},{"issue":"6","key":"10.1016\/j.mam.2005.07.006_bib53","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1006\/nbdi.2001.0443","article-title":"Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues","volume":"8","author":"Watanabe","year":"2001","journal-title":"Neurobiol Dis"},{"issue":"5465","key":"10.1016\/j.mam.2005.07.006_bib54","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1126\/science.288.5465.399a","article-title":"Toxicity of ALS-linked SOD1 mutants","volume":"288","author":"Williamson","year":"2000","journal-title":"Science"},{"issue":"6","key":"10.1016\/j.mam.2005.07.006_bib55","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1073\/pnas.040461197","article-title":"Copper chaperone for superoxide dismutase is essential to activate mammalian Cu\/Zn superoxide dismutase","volume":"97","author":"Wong","year":"2000","journal-title":"Proc Natl Acad Sci USA"},{"issue":"Pt 3","key":"10.1016\/j.mam.2005.07.006_bib56","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1042\/bj3180889","article-title":"A novel nickel-containing superoxide dismutase from Streptomyces spp.","volume":"318","author":"Youn","year":"1996","journal-title":"Biochem J"},{"issue":"13","key":"10.1016\/j.mam.2005.07.006_bib57","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1096\/fj.04-1629fje","article-title":"Redox modulation of the liver with chronic antioxidant enzyme mimetic treatment prevents age-related oxidative damage associated with environmental stress","volume":"18","author":"Zhang","year":"2004","journal-title":"FASEB J"}],"container-title":["Molecular Aspects of Medicine"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299705000361?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0098299705000361?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,7,15]],"date-time":"2021-07-15T21:17:10Z","timestamp":1626383830000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0098299705000361"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,8]]},"references-count":57,"journal-issue":{"issue":"4-5","published-print":{"date-parts":[[2005,8]]}},"alternative-id":["S0098299705000361"],"URL":"https:\/\/doi.org\/10.1016\/j.mam.2005.07.006","relation":{},"ISSN":["0098-2997"],"issn-type":[{"value":"0098-2997","type":"print"}],"subject":[],"published":{"date-parts":[[2005,8]]}}}