{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T15:53:07Z","timestamp":1793116387426,"version":"4.5.0"},"reference-count":109,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[1996,5,1]],"date-time":"1996-05-01T00:00:00Z","timestamp":830908800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,2,25]],"date-time":"2023-02-25T00:00:00Z","timestamp":1677283200000},"content-version":"vor","delay-in-days":9796,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The American Journal of Clinical Nutrition"],"published-print":{"date-parts":[[1996,5]]},"DOI":"10.1093\/ajcn\/63.5.797","type":"journal-article","created":{"date-parts":[[2024,6,7]],"date-time":"2024-06-07T16:01:04Z","timestamp":1717776064000},"page":"797S-811S","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1156,"title":["Copper biochemistry and molecular biology"],"prefix":"10.1016","volume":"63","author":[{"given":"Maria C","family":"Linder","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maryam","family":"Hazegh-Azam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1093\/ajcn\/63.5.797_bib1","series-title":"The biochemistry of copper.","author":"Linder","year":"1991"},{"key":"10.1093\/ajcn\/63.5.797_bib2","series-title":"Nutritional biochemistry and metabolism.","first-page":"215","article-title":"Nutrition and metabolism of trace elements.","author":"Linder","year":"1991"},{"key":"10.1093\/ajcn\/63.5.797_bib3","first-page":"301","article-title":"Copper.","volume":"1","author":"Davis","year":"1987"},{"key":"10.1093\/ajcn\/63.5.797_bib4","doi-asserted-by":"crossref","first-page":"130","DOI":"10.3181\/00379727-196-43171B","article-title":"Copper transport: an overview.","author":"Harris","year":"1991","journal-title":"Soc Exp Biol Med"},{"key":"10.1093\/ajcn\/63.5.797_bib5","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1016\/0955-2863(94)90064-7","article-title":"Compartment model of copper metabolism in adult men.","volume":"5","author":"Scott","year":"1994","journal-title":"J Nutr Biochem"},{"key":"10.1093\/ajcn\/63.5.797_bib6","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1093\/ajcn\/56.5.917","article-title":"Effect of age and sex on copper absorption, biological half-life, and status in humans.","volume":"56","author":"Johnson","year":"1992","journal-title":"J Clin Nutr"},{"key":"10.1093\/ajcn\/63.5.797_bib7","first-page":"341","article-title":"Lead and copper\u2014a model home approach.","author":"Dunham","year":"1992","journal-title":"Proc Water Qual Technol Conf"},{"key":"10.1093\/ajcn\/63.5.797_bib8","series-title":"The biochemistry of copper.","first-page":"331","article-title":"Copper and disease.","author":"Goode","year":"1991"},{"key":"10.1093\/ajcn\/63.5.797_bib9","series-title":"Inflammatory diseases and copper.","first-page":"469","article-title":"The results of a copper bracelet clinical trial and subsequent studies.","author":"Walker","year":"1982"},{"key":"10.1093\/ajcn\/63.5.797_bib10","first-page":"93","article-title":"Studies on solubilization and transformation of species of Cu, Pb, Zn and Cr in simulant acid rain.","volume":"5","author":"He","year":"1994","journal-title":"Chin Chem Lett"},{"key":"10.1093\/ajcn\/63.5.797_bib11","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0043-1354(94)90117-1","article-title":"The contribution of complexed copper to the meta bolic inhibition of algae and bacteria in synthetic media and river water.","volume":"28","author":"Tubbing","year":"1994","journal-title":"Water Res"},{"key":"10.1093\/ajcn\/63.5.797_bib12","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1093\/ajcn\/49.5.870","article-title":"Copper absorption and retention in young men at three levels of dietary copper using the stable isotope, 65Cu.","volume":"49","author":"Turnlund","year":"1989","journal-title":"Am J Clin Nutr"},{"key":"10.1093\/ajcn\/63.5.797_bib13","series-title":"Recommended dietary allowances.","year":"1989"},{"key":"10.1093\/ajcn\/63.5.797_bib14","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1080\/07315724.1993.10718364","article-title":"Dietary regulation of copper absorption and storage in rats: effects of sodium, zinc and histidine-zinc.","volume":"12","author":"Wapnir","year":"1993","journal-title":"J Am Coll Nutr"},{"key":"10.1093\/ajcn\/63.5.797_bib15","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1079\/BJN19940194","article-title":"Increasing intakes of iron reduce status, absorption and biliary excretion of copper in rats.","volume":"71","author":"Yu","year":"1994","journal-title":"Br J Nutr"},{"key":"10.1093\/ajcn\/63.5.797_bib16","first-page":"E309","article-title":"Altered copper absorption in tumor bearing and estrogen treated rats.","volume":"236","author":"Cohen","year":"1979","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib17","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1007\/BF00140112","article-title":"Intestinal administration of copper and its transient release into venous blood serum concomitantly with metallothionein.","volume":"6","author":"Hartmann","year":"1993","journal-title":"Biometals"},{"key":"10.1093\/ajcn\/63.5.797_bib18","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1111\/j.1365-2958.1994.tb00430.x","article-title":"A copper transporting P-type ATPase found in the thylakoid membrane of the cyanobacterium Synechococcus species PCC7942.","volume":"13","author":"Kanamura","year":"1994","journal-title":"Mol Microbiol"},{"key":"10.1093\/ajcn\/63.5.797_bib19","series-title":"Trace elements in man and animals (TEMA-6).","first-page":"141","article-title":"Structure and function of transcuprein in transport of copper by mammalian blood plasma.","author":"Linder","year":"1987"},{"key":"10.1093\/ajcn\/63.5.797_bib20","series-title":"Copper deficiency and toxicity. Physiological aspects of copper.","article-title":"Biochemical aspects of copper.","author":"Owen","year":"1982"},{"key":"10.1093\/ajcn\/63.5.797_bib21","first-page":"E77","article-title":"Copper transport in rats involving a new plasma protein.","volume":"249","author":"Weiss","year":"1985","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib22","first-page":"277","article-title":"Distribution of copper among multiple components of human serum.","volume":"75","author":"Wirth","year":"1985","journal-title":"J Natl Cancer Inst"},{"key":"10.1093\/ajcn\/63.5.797_bib23","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1111\/j.1365-2362.1988.tb01267.x","article-title":"Copper distribution among serum proteins in paediatric liver disorders and malignancies.","volume":"18","author":"Barrow","year":"1988","journal-title":"Eur J Clin Invest"},{"key":"10.1093\/ajcn\/63.5.797_bib24","first-page":"A1095","article-title":"Interactions of transcuprein and albumin in copper transport.","volume":"6","author":"Tsai","year":"1992","journal-title":"FASEB J"},{"key":"10.1093\/ajcn\/63.5.797_bib25","first-page":"G259","article-title":"Copper transport in the Nagase analbuminemic rat.","volume":"267","author":"Vargas","year":"1994","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib26","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1139\/o84-061","article-title":"Comparative studies of manganese(II)-, nickel(II)-, zinc(II)-, copper(II)-cadmium(II)-, and iron(III)-binding components in human cord and adult sera.","volume":"62","author":"Lau","year":"1984","journal-title":"Can J Biochem Cell Biol"},{"key":"10.1093\/ajcn\/63.5.797_bib27","doi-asserted-by":"crossref","first-page":"321","DOI":"10.3181\/00379727-200-43437","article-title":"Comparison of copper binding proteins in dog serum with those in other species.","volume":"200","author":"Montaser","year":"1992","journal-title":"Proc Soc Exp Biol Med"},{"key":"10.1093\/ajcn\/63.5.797_bib28","first-page":"2800","article-title":"Mechanism of copper transport from plasma to hepatocytes.","volume":"45","author":"Ettinger","year":"1986","journal-title":"Fed Proc"},{"key":"10.1093\/ajcn\/63.5.797_bib29","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0162-0134(87)80057-0","article-title":"Albumin has no role in the uptake of copper by human fibroblasts.","volume":"31","author":"McArdle","year":"1987","journal-title":"J Inorg Biochem"},{"key":"10.1093\/ajcn\/63.5.797_bib30","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/0092-8674(94)90345-X","article-title":"Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport.","volume":"76","author":"Dancis","year":"1994","journal-title":"Cell"},{"key":"10.1093\/ajcn\/63.5.797_bib31","doi-asserted-by":"crossref","first-page":"8915","DOI":"10.1073\/pnas.88.20.8915","article-title":"Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membtane proteins.","volume":"88","author":"Cha","year":"1991","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1093\/ajcn\/63.5.797_bib32","doi-asserted-by":"crossref","first-page":"12775","DOI":"10.1016\/S0021-9258(18)31455-8","article-title":"Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae.","volume":"268","author":"Odermatt","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1093\/ajcn\/63.5.797_bib33","first-page":"25660","article-title":"The Saccharomyces cerevisiae copper transport protein (Ctrlp).","volume":"269","author":"Dancis","year":"1994","journal-title":"Biochemical characteriation, regulation by copper, and physiologic role in copper uptake. J Biol Chem"},{"key":"10.1093\/ajcn\/63.5.797_bib34","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/0304-4165(81)90044-1","article-title":"Circulating ceruloplasmin is an important source of copper for normal and malignant cells.","volume":"678","author":"Campbell","year":"1981","journal-title":"Biochim Biophys Acta"},{"key":"10.1093\/ajcn\/63.5.797_bib35","doi-asserted-by":"crossref","first-page":"428","DOI":"10.3181\/00379727-203-43619","article-title":"Ceruloplasmin and copper transport during the latter part of gestation in the rat.","volume":"203","author":"Lee","year":"1993","journal-title":"Proc Soc Exp Biol Med"},{"key":"10.1093\/ajcn\/63.5.797_bib36","doi-asserted-by":"crossref","first-page":"2539","DOI":"10.1073\/pnas.92.7.2539","article-title":"Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.","volume":"92","author":"Harris","year":"1995","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1093\/ajcn\/63.5.797_bib37","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1038\/ng0395-267","article-title":"A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans.","volume":"9","author":"Yoshida","year":"1995","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib38","first-page":"151","article-title":"Interaction of bovine ceruloplasmin with erythrocytes.","volume":"24","author":"Fischer","year":"1994","journal-title":"Prep Biochem"},{"key":"10.1093\/ajcn\/63.5.797_bib39","doi-asserted-by":"crossref","first-page":"C140","DOI":"10.1152\/ajpcell.1990.258.1.C140","article-title":"Copper transport from ceruloplasmin: characterization of the cellular uptake mechanism.","volume":"258","author":"Percival","year":"1990","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib40","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0167-4889(94)90208-9","article-title":"Characterization of a particulate pathway for copper in K562 cells.","volume":"1221","author":"Davidson","year":"1994","journal-title":"Biochim Biophys Acta"},{"key":"10.1093\/ajcn\/63.5.797_bib41","first-page":"E551","article-title":"Turnover and excretion of copper in rats as measured with 67Cu.","author":"Linder","year":"1986","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib42","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1002\/hep.1840170120","article-title":"Biliary copper excretion in acutely and chronically copper-loaded rats.","volume":"17","author":"Harada","year":"1993","journal-title":"Hepatology"},{"key":"10.1093\/ajcn\/63.5.797_bib43","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.ph.28.030166.002251","article-title":"Functions of lysosomes.","volume":"28","author":"DeDuve","year":"1966","journal-title":"Annu Rev Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib44","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1172\/JCI113873","article-title":"Biliary copper excretion by hepatocyte lysosomes in the rat.","volume":"83","author":"Gross","year":"1989","journal-title":"J Clin Invest"},{"key":"10.1093\/ajcn\/63.5.797_bib45","series-title":"Trace elements in man and animal 7.","first-page":"2\/8","article-title":"The protective role of metallothionein in copper overload.","author":"Evering","year":"1991"},{"key":"10.1093\/ajcn\/63.5.797_bib46","doi-asserted-by":"crossref","first-page":"3399","DOI":"10.1016\/0006-2952(89)90107-X","article-title":"Effect of the glutathione-depleting agents diethylmaleate, phorone and buthionine sulfoxamine on biliary copper excretion in rats.","volume":"38","author":"Nederbragt","year":"1989","journal-title":"Biochem Pharmacol"},{"key":"10.1093\/ajcn\/63.5.797_bib47","first-page":"751","article-title":"The role of glutathione in bile secretion of endogenous trace elements in rats.","volume":"121","author":"Dijkstra","year":"1993","journal-title":"J Lab Clin Med"},{"key":"10.1093\/ajcn\/63.5.797_bib48","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1002\/hep.1840040512","article-title":"Origins of biliary copper.","volume":"4","author":"Kressner","year":"1984","journal-title":"Hepatology"},{"key":"10.1093\/ajcn\/63.5.797_bib49","first-page":"267","article-title":"Studies of cholecysto-kinin-stimulated biliary secretions reveal a high molecular weight copper binding substance in normal subjects that is absent in patients with Wilson\u2019s disease.","volume":"111","author":"Iyengar","year":"1988","journal-title":"J Lab Clin Med"},{"key":"10.1093\/ajcn\/63.5.797_bib50","doi-asserted-by":"crossref","first-page":"190S","DOI":"10.1042\/bst022190s","article-title":"The role of caeruloplasmin in copper excretion.","volume":"22","author":"Chowrimootoo","year":"1994","journal-title":"Biochem Soc Trans"},{"key":"10.1093\/ajcn\/63.5.797_bib51","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1083\/jcb.102.4.1298","article-title":"Liver endothelium mediates the hepatocyte\u2019s uptake of ceruloplasmin.","volume":"102","author":"Tavassoli","year":"1986","journal-title":"J Cell Biol"},{"key":"10.1093\/ajcn\/63.5.797_bib52","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/0955-2863(92)90088-Z","article-title":"Mitochondrial respiration in heart, liver, and kidney of copper deficient rats.","volume":"3","author":"Bode","year":"1992","journal-title":"J Nutr Biochem"},{"key":"10.1093\/ajcn\/63.5.797_bib53","doi-asserted-by":"crossref","first-page":"4789","DOI":"10.1073\/pnas.85.13.4789","article-title":"The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity.","volume":"85","author":"Bermingham-McDonogh","year":"1988","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1093\/ajcn\/63.5.797_bib54","first-page":"L636","article-title":"Effects of inhibition of catalase and superoxide dismutase activity on antioxidant enzyme mRNA levels.","volume":"265","author":"Ma\u00eetre","year":"1993","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib55","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1161\/01.STR.25.1.165","article-title":"Human copper-zinc superoxide dismutase transgenic mice are highly resistant to reperfusion injury after focal cerebral ischemia.","volume":"25","author":"Yang","year":"1994","journal-title":"Stroke"},{"key":"10.1093\/ajcn\/63.5.797_bib56","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1038\/362059a0","article-title":"Mutations in Cu\/Zn superoxide dismutase gene are associated with familial amyotropic lateral sclerosis.","volume":"362","author":"Rosen","year":"1993","journal-title":"Nature"},{"key":"10.1093\/ajcn\/63.5.797_bib57","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/0003-9861(82)90010-8","article-title":"Differences in the polymorphic forms of metallothionein.","volume":"214","author":"Winge","year":"1982","journal-title":"Arch Biochem Biophys"},{"key":"10.1093\/ajcn\/63.5.797_bib58","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/0167-4838(93)90042-P","article-title":"A pulse radiolytic study on the reaction of hydroxyl and superoxide radicals with yeast Cu(I) thionein.","volume":"1203","author":"Felix","year":"1993","journal-title":"Biochim Biophys Acta"},{"key":"10.1093\/ajcn\/63.5.797_bib59","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/BF02342510","article-title":"Effect of preinduction of metallothionein on paraquat toxicity in mice.","volume":"66","author":"Satoh","year":"1992","journal-title":"Arch Toxicol"},{"key":"10.1093\/ajcn\/63.5.797_bib60","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1007\/BF00914269","article-title":"Antiinflammatory reactivity of copper(I)-thionein.","volume":"14","author":"Miesel","year":"1990","journal-title":"Inflammation"},{"key":"10.1093\/ajcn\/63.5.797_bib61","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1248\/bpb.16.664","article-title":"Adriamycin-induced lipid peroxidation of erythrocyte membranes in the presence of ferritin and the inhibitory effect of ceruloplasmin.","volume":"16","author":"Miura","year":"1993","journal-title":"Biol Pharm Bull"},{"key":"10.1093\/ajcn\/63.5.797_bib62","series-title":"Metal-metal interactions.","first-page":"11","article-title":"Interactions between copper and iron in mammalian metabolism.","author":"Linder","year":"1994"},{"key":"10.1093\/ajcn\/63.5.797_bib63","first-page":"117","article-title":"Ceruloplasmin; a multifunctional metalloprotein of vertebrate plasma.","volume":"13","author":"Frieden","year":"1981"},{"key":"10.1093\/ajcn\/63.5.797_bib64","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1139\/y93-107","article-title":"Ferritin and ceruloplasmin in oxidative damage: review and recent findings.","volume":"71","author":"De Silva","year":"1993","journal-title":"Can J Physiol Pharmacol"},{"key":"10.1093\/ajcn\/63.5.797_bib65","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/0092-8674(94)90346-8","article-title":"The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.","volume":"76","author":"Askwith","year":"1994","journal-title":"Cell"},{"key":"10.1093\/ajcn\/63.5.797_bib66","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/0092-8674(94)90345-X","article-title":"Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport.","volume":"76","author":"Dancis","year":"1994","journal-title":"Cell"},{"key":"10.1093\/ajcn\/63.5.797_bib67","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1172\/JCI117127","article-title":"Intact human ceruloplasmin oxidatively modifies low density lipoprotein.","volume":"93","author":"Ehrenwald","year":"1994","journal-title":"J Clin Invest"},{"key":"10.1093\/ajcn\/63.5.797_bib68","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0014-5793(94)80582-2","article-title":"Peroxynitrite releases copper from caeruloplasmin: implications for atherosclerosis.","volume":"342","author":"Swain","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1093\/ajcn\/63.5.797_bib69","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/0021-9150(92)90128-4","article-title":"Low density lipoprotein oxidation by stimulated neutrophils and ferritin.","volume":"97","author":"Abdalla","year":"1992","journal-title":"Atherosclerosis"},{"key":"10.1093\/ajcn\/63.5.797_bib70","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/0014-5793(94)80348-X","article-title":"Acidic pH enables caeruloplasmin to catalyse the modification of low-density lipoprotein.","volume":"338","author":"Lamb","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1093\/ajcn\/63.5.797_bib71","first-page":"A71l","article-title":"Ceruloplasmin in milk and amniotic fluid.","volume":"8","author":"Linder","year":"1994","journal-title":"FASEB J"},{"key":"10.1093\/ajcn\/63.5.797_bib72","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1006\/abbi.1993.1224","article-title":"Synthesis and turnover of ceruloplasmin in rats treated with 17-\/3-estradiol.","volume":"302","author":"Middleton","year":"1993","journal-title":"Arch Biochem Biophys"},{"key":"10.1093\/ajcn\/63.5.797_bib73","first-page":"47","article-title":"Regulation of ceruloplasmin and copper turnover, by estrogens and tumors, in the rat.","volume":"3","author":"Karp","year":"1986","journal-title":"J Nutr Growth Cancer"},{"key":"10.1093\/ajcn\/63.5.797_bib74","first-page":"263","article-title":"Ceruloplasmin assays in diagnosis and treatment of human lung, breast and gastrointestinal cancer.","volume":"67","author":"Linder","year":"1981","journal-title":"J Natl Cancer Inst"},{"key":"10.1093\/ajcn\/63.5.797_bib75","doi-asserted-by":"crossref","first-page":"4407","DOI":"10.1016\/S0021-9258(18)53624-3","article-title":"Evidence that a 550,000 dalton cartilage matrix glycoprotein is a chondrocyte membrane associated protein closely related to ceruloplasmin.","volume":"268","author":"Fife","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1093\/ajcn\/63.5.797_bib76","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0304-4165(94)90145-7","article-title":"Studies of copper transport in cultured bovine chondrocytes.","volume":"1201","author":"Fife","year":"1994","journal-title":"Biochim Biophys Acta"},{"key":"10.1093\/ajcn\/63.5.797_bib77","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1126\/science.2111581","article-title":"A new redox cofactor in eukaryotic enzymes: 6-hydroxy dopa at the active site of bovine serum amine oxidase.","volume":"248","author":"Janes","year":"1990","journal-title":"Science"},{"key":"10.1093\/ajcn\/63.5.797_bib78","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1093\/jn\/123.7.1226","article-title":"Persistent regional changes in brain copper, cuproenzymes and catecholamines following perinatal copper deficiency in mice.","volume":"123","author":"Prohaska","year":"1993","journal-title":"J Nutr"},{"key":"10.1093\/ajcn\/63.5.797_bib79","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1046\/j.1471-4159.1994.63041551.x","article-title":"Regional specificity in alterations of rat brain copper and catecholamines following perinatal copper deficiency.","volume":"63","author":"Prohaska","year":"1994","journal-title":"J Neurochem"},{"key":"10.1093\/ajcn\/63.5.797_bib80","first-page":"27","article-title":"Changes in the distribution and metabolism of copper in cancer: a review.","volume":"1","author":"Linder","year":"1983","journal-title":"J Nutr Growth Cancer"},{"key":"10.1093\/ajcn\/63.5.797_bib81","first-page":"223","article-title":"Ischemic heart disease: toward a unified theory.","author":"Klevay","year":"1990"},{"key":"10.1093\/ajcn\/63.5.797_bib82","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/ng1094-195","article-title":"Occipital horn syndrome and a mild Menkes phenotype associate with splice site mutations at the MNK locus.","volume":"8","author":"Kaler","year":"1994","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib83","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1038\/ng0494-374","article-title":"Mutation in the murine homologue of the Menkes gene in dappled and blotchy mice.","volume":"6","author":"Mercer","year":"1994","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib84","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1006\/bbrc.1993.2471","article-title":"Isolation and characterization of a human liver cDNA as a candidate gene for Wilson disease.","volume":"197","author":"Yamaguchi","year":"1993","journal-title":"Biochem Biophys Res Comm"},{"key":"10.1093\/ajcn\/63.5.797_bib85","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1097\/00005792-199205000-00004","article-title":"Wilson disease.","volume":"71","author":"Brewer","year":"1992","journal-title":"Medicine"},{"key":"10.1093\/ajcn\/63.5.797_bib86","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/ng1293-327","article-title":"The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene.","volume":"5","author":"Bull","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib87","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/ng1293-344","article-title":"The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene.","volume":"5","author":"Tanzi","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib88","first-page":"864","article-title":"Polymorphic microsatellites and Wilson Disease (WD).","volume":"53","author":"Stewart","year":"1993","journal-title":"Am J Hum Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib89","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1038\/ng1293-338","article-title":"Mapping, cloning and genetic characterization of the region containing the Wilson disease gene.","volume":"5","author":"Petrukhin","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib90","first-page":"71","article-title":"Haplotype studies in Wilson disease.","volume":"54","author":"Thomas","year":"1994","journal-title":"Am J Hum Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib91","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-510X(93)90145-O","article-title":"Geographic variations in Wilson\u2019s disease.","volume":"117","author":"Chu","year":"1993","journal-title":"J Neurol Sci"},{"key":"10.1093\/ajcn\/63.5.797_bib92","first-page":"458","article-title":"Diagnosis and characterization of presymptomatic patients with Wilson\u2019s disease and the use of molecular genetics to aid in the diagnosis.","volume":"118","author":"Yuzbasian-Gurkian","year":"1991","journal-title":"J Lab Clin Med"},{"key":"10.1093\/ajcn\/63.5.797_bib93","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1038\/ng0295-210","article-title":"The Wilson disease gene: spectrum of mutations and their consequences.","volume":"9","author":"Thomas","year":"1995","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib94","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3010001","article-title":"Expression of the Wilson disease gene is deficient in the Long-Evans Cinnamon rat.","volume":"301","author":"Yukitoshi","year":"1994","journal-title":"Biochem J"},{"key":"10.1093\/ajcn\/63.5.797_bib95","doi-asserted-by":"crossref","first-page":"8965","DOI":"10.1016\/S0021-9258(18)52966-5","article-title":"Inhibition of the copper incorporation into ceruloplasmin leads to the deficiency in serum ceruloplasmin activity in Long-Evans Cinnamon mutant rat.","volume":"268","author":"Yamada","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1093\/ajcn\/63.5.797_bib96","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1203\/00006450-199405000-00012","article-title":"Impaired hepatic copper homeostasis in Long-Evans Cinnamon rats: reduced biliary excretion of copper.","volume":"35","author":"Suzuki","year":"1994","journal-title":"Pediatr Res"},{"key":"10.1093\/ajcn\/63.5.797_bib97","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1007\/BF00484913","article-title":"On the defect of synthesis of ceruloplasmin in the liver polyribosomes in Wilson\u2019s disease.","volume":"13","author":"Gaitskhoki","year":"1975","journal-title":"Biochem Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib98","first-page":"G907","article-title":"Pleiotropic effect of LEC mutation: a rodent model of Wilson\u2019s disease.","volume":"266","author":"Schilsky","year":"1994","journal-title":"Am J Physiol"},{"key":"10.1093\/ajcn\/63.5.797_bib99","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/0168-9525(94)90172-4","article-title":"Wilson disease and Menkes disease: new handles on heavy-metal transport.","volume":"10","author":"Bull","year":"1994","journal-title":"Trends Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib100","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/0014-5793(94)00316-5","article-title":"Copper pumping ATPase: common concepts in bacteria and man.","volume":"346","author":"Solioz","year":"1994","journal-title":"FEBS Lett"},{"key":"10.1093\/ajcn\/63.5.797_bib101","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1038\/ng0193-20","article-title":"Isolation of a partial candidate gene for Menkes disease by positional cloning.","volume":"3","author":"Mercer","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib102","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/ng0193-7","article-title":"Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase.","volume":"3","author":"Vulpe","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib103","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/ng0193-14","article-title":"Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein.","volume":"3","author":"Chelly","year":"1993","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib104","first-page":"97","article-title":"Clinical and pathological studies of swine copper intoxication.","volume":"18","author":"Chang","year":"1992","journal-title":"Zhonghua Minguo Shouyi Xuehui Zazhi"},{"key":"10.1093\/ajcn\/63.5.797_bib105","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/ng0494-369","article-title":"The mottled gene is the mouse homologue of the Menkes disease gene.","volume":"6","author":"Levinson","year":"1994","journal-title":"Nature Genet"},{"key":"10.1093\/ajcn\/63.5.797_bib106","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1006\/taap.1993.1236","article-title":"In vivo ESR spin trapping evidence for hydroxyl radical-mediated toxicity of paraquat and copper in rats.","volume":"123","author":"Kadiiska","year":"1993","journal-title":"Toxicol Appl Pharmacol"},{"key":"10.1093\/ajcn\/63.5.797_bib107","doi-asserted-by":"crossref","first-page":"1522","DOI":"10.1182\/blood.V82.5.1522.1522","article-title":"Oxidative inactivation of plasmin and other serine proteases by copper and ascorbate.","volume":"82","author":"Lind","year":"1993","journal-title":"Blood"},{"key":"10.1093\/ajcn\/63.5.797_bib108","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/0167-4838(92)90061-H","article-title":"Oxidation of peptidyl lysine by copper complexes of pyrroloquinoline quinone and other quinones.","volume":"1159","author":"Shah","year":"1992","journal-title":"A model for oxidative pathochemistry. Biochim Biophys Acta"},{"key":"10.1093\/ajcn\/63.5.797_bib109","first-page":"222","article-title":"Electron spin resonance evidence for free radical generation in copper-treated vitamin E-and selenium-deficient rats: in vivo spin-trapping investigation.","volume":"44","author":"Kadiiska","year":"1993","journal-title":"Mol Pharmacol"}],"container-title":["The American Journal of Clinical Nutrition"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002916523193038?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002916523193038?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,7]],"date-time":"2024-06-07T16:08:52Z","timestamp":1717776532000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0002916523193038"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1996,5]]},"references-count":109,"journal-issue":{"issue":"5","published-print":{"date-parts":[[1996,5]]}},"alternative-id":["S0002916523193038"],"URL":"https:\/\/doi.org\/10.1093\/ajcn\/63.5.797","relation":{},"ISSN":["0002-9165"],"issn-type":[{"value":"0002-9165","type":"print"}],"subject":[],"published":{"date-parts":[[1996,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Copper biochemistry and molecular biology","name":"articletitle","label":"Article Title"},{"value":"The American Journal of Clinical Nutrition","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1093\/ajcn\/63.5.797","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 1996 American Society for Nutrition. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}