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Volumn 67, Issue 5 SUPPL., 1998, Pages

Essentiality of copper in humans

Author keywords

Copper; Copper deficiency; Copper nutrition; Copper requirements; Humans; Metal responsive elements; Oxidoreductase enzymes; Superoxide dismutase; Toxicity; Transcription factors

Indexed keywords

COPPER;

EID: 0031971570     PISSN: 00029165     EISSN: None     Source Type: Journal    
DOI: 10.1093/ajcn/67.5.952S     Document Type: Conference Paper
Times cited : (884)

References (85)
  • 1
    • 0001284487 scopus 로고
    • Iron nutrition. VII. Copper is a supplement to iron for hemoglobin building in the rat
    • Hart EB, Steenbock H, Waddell J, Elvehjem CA. Iron nutrition. VII. Copper is a supplement to iron for hemoglobin building in the rat. J Biol Chem 1928;77:797-812.
    • (1928) J Biol Chem , vol.77 , pp. 797-812
    • Hart, E.B.1    Steenbock, H.2    Waddell, J.3    Elvehjem, C.A.4
  • 2
    • 0000493781 scopus 로고
    • The treatment of idiopathic (hypochromic) anemia with iron and copper
    • Mills ES. The treatment of idiopathic (hypochromic) anemia with iron and copper. Can Med Assoc J 1930;22:175-8.
    • (1930) Can Med Assoc J , vol.22 , pp. 175-178
    • Mills, E.S.1
  • 3
    • 0000818049 scopus 로고
    • Treatment of anemia of infancy with iron and copper
    • Josephs HW. Treatment of anemia of infancy with iron and copper. Bull Johns Hopkins Hosp 1931;49:246-58.
    • (1931) Bull Johns Hopkins Hosp , vol.49 , pp. 246-258
    • Josephs, H.W.1
  • 4
    • 0025093088 scopus 로고
    • Structural and catalytic properties of copper in lysyl oxidase
    • Gacheru N, Trackman PC, Shah MA, et al. Structural and catalytic properties of copper in lysyl oxidase. J Biol Chem 1990;265:19022-7.
    • (1990) J Biol Chem , vol.265 , pp. 19022-19027
    • Gacheru, N.1    Trackman, P.C.2    Shah, M.A.3
  • 5
    • 0027202019 scopus 로고
    • Lysyl oxidase copper-talon complex: A model
    • Krebs CJ, Krawetz SA. Lysyl oxidase copper-talon complex: a model. Biochim Biophys Acta 1993;1202:7-12.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 7-12
    • Krebs, C.J.1    Krawetz, S.A.2
  • 9
    • 0028924256 scopus 로고
    • Effects of overall oxidation state on infrared spectra of heme a3 cyanide in bovine heart cytochrome c oxidase. Evidence of novel mechanistic roles for CuB
    • Yoshikawa S, Mochizuki M, Zhao XJ, Caughey WS. Effects of overall oxidation state on infrared spectra of heme a3 cyanide in bovine heart cytochrome c oxidase. Evidence of novel mechanistic roles for CuB. J Biol Chem 1995;270:4270-9.
    • (1995) J Biol Chem , vol.270 , pp. 4270-4279
    • Yoshikawa, S.1    Mochizuki, M.2    Zhao, X.J.3    Caughey, W.S.4
  • 10
    • 0029942862 scopus 로고    scopus 로고
    • The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å
    • Tsukihara T, Aoyama H, Yamashita E, et al. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å. Science 1996;272:1136-44.
    • (1996) Science , vol.272 , pp. 1136-1144
    • Tsukihara, T.1    Aoyama, H.2    Yamashita, E.3
  • 11
    • 0030584404 scopus 로고    scopus 로고
    • Iron metabolism in eukaryotes: Mars and Venus at it again
    • Kaplan J, O'Halloran TV. Iron metabolism in eukaryotes: Mars and Venus at it again. Science 1996;271:1510-2.
    • (1996) Science , vol.271 , pp. 1510-1512
    • Kaplan, J.1    O'Halloran, T.V.2
  • 12
    • 0023654636 scopus 로고
    • Cytochrome c oxidase is a three-copper, two-heme-A protein
    • Steffens GC, Biewald R, Buse G. Cytochrome c oxidase is a three-copper, two-heme-A protein. Eur J Biochem 1987;164:295-300.
    • (1987) Eur J Biochem , vol.164 , pp. 295-300
    • Steffens, G.C.1    Biewald, R.2    Buse, G.3
  • 13
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B. Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 1995;376:660-9.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 14
    • 0028978455 scopus 로고
    • The CuA center of cytochrome-c oxidase: Electronic structure and spectra of models compared to the properties of CuA domains
    • Larsson S, Kallebring B, Wittung P, Malmstrom BG. The CuA center of cytochrome-c oxidase: electronic structure and spectra of models compared to the properties of CuA domains. Proc Natl Acad Sci U S A 1995;92:7167-71.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 7167-7171
    • Larsson, S.1    Kallebring, B.2    Wittung, P.3    Malmstrom, B.G.4
  • 15
    • 0029120507 scopus 로고
    • Structure of cytochrome c oxidase, energy generator of aerobic life
    • Gennis R, Ferguson-Miller S. Structure of cytochrome c oxidase, energy generator of aerobic life. Science 1995;269:1063-4.
    • (1995) Science , vol.269 , pp. 1063-1064
    • Gennis, R.1    Ferguson-Miller, S.2
  • 16
    • 15844384254 scopus 로고    scopus 로고
    • Genetic and molecular basis for copper toxicity
    • Harris ZL, Gitlin JD. Genetic and molecular basis for copper toxicity. Am J Clin Nutr 1996;63(suppl):836S-41S.
    • (1996) Am J Clin Nutr , vol.63 , Issue.SUPPL.
    • Harris, Z.L.1    Gitlin, J.D.2
  • 17
    • 0026506667 scopus 로고
    • Copper as a cofactor and regulator of copper, zinc superoxide dismutase
    • Harris ED. Copper as a cofactor and regulator of copper, zinc superoxide dismutase. J Nutr 1992;122:636-40.
    • (1992) J Nutr , vol.122 , pp. 636-640
    • Harris, E.D.1
  • 18
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymatic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I. Superoxide dismutase: an enzymatic function for erythrocuprein (hemocuprein). J Biol Chem 1969;244:6049-55.
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 19
    • 0030052114 scopus 로고    scopus 로고
    • Mutant enzyme provides new insights into the cause of ALS
    • Marx J. Mutant enzyme provides new insights into the cause of ALS. Science 1996;271:446-7.
    • (1996) Science , vol.271 , pp. 446-447
    • Marx, J.1
  • 20
    • 0028149084 scopus 로고
    • Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis
    • Nishida CR, Gralla EB, Valentine JS. Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis. Proc Natl Acad Sci U S A 1994;91:9906-10.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9906-9910
    • Nishida, C.R.1    Gralla, E.B.2    Valentine, J.S.3
  • 21
    • 0028915976 scopus 로고
    • Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast and neuronal cells
    • Rabizadeh S, Gralla EB, Borchelt D, et al. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neuronal cells. Proc Natl Acad Sci U S A 1995;92:3024-8.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3024-3028
    • Rabizadeh, S.1    Gralla, E.B.2    Borchelt, D.3
  • 22
    • 0029010496 scopus 로고
    • Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase
    • Andersen PM, Nilsson P, Ala-Hurula V, et al. Amyotrophic lateral sclerosis associated with homozygosity for an Asp90Ala mutation in CuZn-superoxide dismutase. Nat Genet 1995;10:61-6.
    • (1995) Nat Genet , vol.10 , pp. 61-66
    • Andersen, P.M.1    Nilsson, P.2    Ala-Hurula, V.3
  • 23
    • 0016816804 scopus 로고
    • The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: Inactivation of the enzyme
    • Hodgson EK, Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 1975;14:5294-8.
    • (1975) Biochemistry , vol.14 , pp. 5294-5298
    • Hodgson, E.K.1    Fridovich, I.2
  • 24
    • 0029671220 scopus 로고    scopus 로고
    • Altered reactivity of superoxide in familial amyotrophic lateral sclerosis
    • Wiedau-Pazos M, Goto JJ, Rabizadeh S, et al. Altered reactivity of superoxide in familial amyotrophic lateral sclerosis. Nature 1996;271:515-8.
    • (1996) Nature , vol.271 , pp. 515-518
    • Wiedau-Pazos, M.1    Goto, J.J.2    Rabizadeh, S.3
  • 25
    • 0027250458 scopus 로고
    • Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase
    • Turowski PN, McGuirl MA, Dooley DM. Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase. J Biol Chem 1993;268:17680-2.
    • (1993) J Biol Chem , vol.268 , pp. 17680-17682
    • Turowski, P.N.1    McGuirl, M.A.2    Dooley, D.M.3
  • 26
    • 0028360735 scopus 로고
    • Primary structures for a mammalian cellular and serum copper oxidase
    • Mu D, Medzihradszky KF, Adams GW, et al. Primary structures for a mammalian cellular and serum copper oxidase. J Biol Chem 1994;269:9926-32.
    • (1994) J Biol Chem , vol.269 , pp. 9926-9932
    • Mu, D.1    Medzihradszky, K.F.2    Adams, G.W.3
  • 27
    • 0028964417 scopus 로고
    • Copper/topa quinone-containing histamine oxidase from Arthobacter globiformis
    • Choi Y-H, Matsuzaki R, Fukui T, et al. Copper/topa quinone-containing histamine oxidase from Arthobacter globiformis. J Biol Chem 1995;270:4712-20.
    • (1995) J Biol Chem , vol.270 , pp. 4712-4720
    • Choi, Y.-H.1    Matsuzaki, R.2    Fukui, T.3
  • 28
  • 29
    • 0026553931 scopus 로고
    • Metal-regulated transcription in eukaryotes
    • Thiele DJ. Metal-regulated transcription in eukaryotes. Nucleic Acids Res 1992;20:1183-91.
    • (1992) Nucleic Acids Res , vol.20 , pp. 1183-1191
    • Thiele, D.J.1
  • 30
    • 0025779301 scopus 로고
    • Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae
    • Zhou P, Thiele DJ. Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 1991;88:6112-6.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6112-6116
    • Zhou, P.1    Thiele, D.J.2
  • 31
    • 0027247483 scopus 로고
    • Regulation of metallothionein genes by Ace1 and Amt1 transcription factors
    • Thorvaldsen JL, Sewell AK, McCowen CL, Winge DR. Regulation of metallothionein genes by Ace1 and Amt1 transcription factors. J Biol Chem 1993;268:12512-8.
    • (1993) J Biol Chem , vol.268 , pp. 12512-12518
    • Thorvaldsen, J.L.1    Sewell, A.K.2    McCowen, C.L.3    Winge, D.R.4
  • 32
    • 0024291353 scopus 로고
    • Copper activates metallothionein gene transcription by altering the conformation of specific DNA binding protein
    • Fúrst P, Hu S, Hackett R, Hamer D. Copper activates metallothionein gene transcription by altering the conformation of specific DNA binding protein. Cell 1988;55:1219-23.
    • (1988) Cell , vol.55 , pp. 1219-1223
    • Fúrst, P.1    Hu, S.2    Hackett, R.3    Hamer, D.4
  • 33
    • 0027183546 scopus 로고
    • Transition metals in the control of gene expression
    • O'Halloran TV. Transition metals in the control of gene expression. Science 1993;261:715-25.
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 34
    • 0028171037 scopus 로고
    • Identification and analysis of a Saccharomyces cerevisiae copper homeostasis gene encoding a homeodomain protein
    • Knight SA, Tamai KT, Kosman DJ, Thiele DJ. Identification and analysis of a Saccharomyces cerevisiae copper homeostasis gene encoding a homeodomain protein. Mol Cell Biol 1994;14:7792-804.
    • (1994) Mol Cell Biol , vol.14 , pp. 7792-7804
    • Knight, S.A.1    Tamai, K.T.2    Kosman, D.J.3    Thiele, D.J.4
  • 35
    • 0026046097 scopus 로고
    • ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene
    • Gralla EB, Thiele DJ, Silar P, Valentine JS. ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci U S A 1991;88:8558-62.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 8558-8562
    • Gralla, E.B.1    Thiele, D.J.2    Silar, P.3    Valentine, J.S.4
  • 36
    • 0025957551 scopus 로고
    • Evidence for co-regulation of Cu, Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE1 factor
    • Carri MT, Galiazzo F, Ciriolo MR, Rotilio G. Evidence for co-regulation of Cu, Zn superoxide dismutase and metallothionein gene expression in yeast through transcriptional control by copper via the ACE1 factor. FEBS Lett 1991;2278:263-6.
    • (1991) FEBS Lett , vol.2278 , pp. 263-266
    • Carri, M.T.1    Galiazzo, F.2    Ciriolo, M.R.3    Rotilio, G.4
  • 37
    • 0027500845 scopus 로고
    • MAC1, is a nuclear regulatory protein related to Cu-dependent transcription factors involved in Cu/Fe utilization and stress resistance in yeast
    • Jungmann J, Reins H-A, Lee J, et al. MAC1, is a nuclear regulatory protein related to Cu-dependent transcription factors involved in Cu/Fe utilization and stress resistance in yeast. EMBO J 1993;12:5051-6.
    • (1993) EMBO J , vol.12 , pp. 5051-5056
    • Jungmann, J.1    Reins, H.-A.2    Lee, J.3
  • 38
    • 0023652466 scopus 로고
    • Regulation in vitro of metallothionein gene binding factors
    • Seguin C, Hamer DH. Regulation in vitro of metallothionein gene binding factors. Science 1987;235:1383-6.
    • (1987) Science , vol.235 , pp. 1383-1386
    • Seguin, C.1    Hamer, D.H.2
  • 39
    • 0027414642 scopus 로고
    • Cloned transcription factor MTF-I activates the mouse metallothionein I promoter
    • Radtke F, Heuchel R, Georgiev O, et al. Cloned transcription factor MTF-I activates the mouse metallothionein I promoter. EMBO J 1993;12:1355-62.
    • (1993) EMBO J , vol.12 , pp. 1355-1362
    • Radtke, F.1    Heuchel, R.2    Georgiev, O.3
  • 40
    • 0028125990 scopus 로고
    • Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-I
    • Palmiter RD. Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-I. Proc Natl Acad Sci U S A 1994;91:1219-23.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1219-1223
    • Palmiter, R.D.1
  • 42
  • 44
    • 78651124591 scopus 로고
    • A sex-linked recessive disorder with retardation of growth, peculiar hair, and focal cerebral and cerebellar degeneration
    • Menkes JH, Alter M, Steigleder GK, Weakley DR, Sung JH. A sex-linked recessive disorder with retardation of growth, peculiar hair, and focal cerebral and cerebellar degeneration. Pediatrics 1962;29:764-79.
    • (1962) Pediatrics , vol.29 , pp. 764-779
    • Menkes, J.H.1    Alter, M.2    Steigleder, G.K.3    Weakley, D.R.4    Sung, J.H.5
  • 45
    • 0029883794 scopus 로고    scopus 로고
    • Copper as an essential element
    • Olivares M, Uauy R. Copper as an essential element. Am J Clin Nutr 1996;63(suppl):791S-6S.
    • (1996) Am J Clin Nutr , vol.63 , Issue.SUPPL.
    • Olivares, M.1    Uauy, R.2
  • 46
    • 0002144448 scopus 로고
    • Chemical composition of the body
    • Comar CL, Bronner F, eds. New York: Academic Press
    • Widdowson EM, Dickerson JWT. Chemical composition of the body. In: Comar CL, Bronner F, eds. Mineral metabolism. Vol 2. New York: Academic Press, 1964:1-247.
    • (1964) Mineral Metabolism , vol.2 , pp. 1-247
    • Widdowson, E.M.1    Dickerson, J.W.T.2
  • 47
    • 0016227179 scopus 로고
    • Trace elements in foetal and early post-natal development
    • Widdowson EM, Dauncey J, Shaw JCL. Trace elements in foetal and early post-natal development. Proc Nutr Soc 1974;33:275-84.
    • (1974) Proc Nutr Soc , vol.33 , pp. 275-284
    • Widdowson, E.M.1    Dauncey, J.2    Shaw, J.C.L.3
  • 48
    • 0017657738 scopus 로고
    • The absorption and retention of magnesium, zinc and copper by low birth weight infants fed pasteurized human breast milk
    • Dauncey MJ, Shaw JCL, Urman J. The absorption and retention of magnesium, zinc and copper by low birth weight infants fed pasteurized human breast milk. Pediatr Res 1977;11:991-7.
    • (1977) Pediatr Res , vol.11 , pp. 991-997
    • Dauncey, M.J.1    Shaw, J.C.L.2    Urman, J.3
  • 49
    • 0022257131 scopus 로고
    • Copper deficiency in the preterm infant of very low birthweight: Four cases and a reference range for plasma copper
    • Sutton AM, Harvie A, Cockburn A, et al. Copper deficiency in the preterm infant of very low birthweight: four cases and a reference range for plasma copper. Arch Dis Child 1985;60:644-51.
    • (1985) Arch Dis Child , vol.60 , pp. 644-651
    • Sutton, A.M.1    Harvie, A.2    Cockburn, A.3
  • 50
    • 0024392464 scopus 로고
    • Longitudinal manganese and copper balances in young infants and preterm infants fed on breast-milk and adapted cow's milk formulas
    • Dörner K, Dziadzka S, Hohn A, et al. Longitudinal manganese and copper balances in young infants and preterm infants fed on breast-milk and adapted cow's milk formulas. Br J Nutr 1989;61:559-72.
    • (1989) Br J Nutr , vol.61 , pp. 559-572
    • Dörner, K.1    Dziadzka, S.2    Hohn, A.3
  • 51
    • 0024422576 scopus 로고
    • Zinc and copper nutritional studies in very low birth weight infants: Comparison of stable isotopic extrinsic tag and chemical balance methods
    • Ehrenkranz RA, Gettner PA, Nelli CM, et al. Zinc and copper nutritional studies in very low birth weight infants: comparison of stable isotopic extrinsic tag and chemical balance methods. Pediatr Res 1989;26:298-307.
    • (1989) Pediatr Res , vol.26 , pp. 298-307
    • Ehrenkranz, R.A.1    Gettner, P.A.2    Nelli, C.M.3
  • 52
    • 0019427005 scopus 로고
    • Copper deficiency with cow's milk diet
    • Naveh Y, Haqzani A, Berant M. Copper deficiency with cow's milk diet. Pediatrics 1981;68:397-400.
    • (1981) Pediatrics , vol.68 , pp. 397-400
    • Naveh, Y.1    Haqzani, A.2    Berant, M.3
  • 53
    • 0022357795 scopus 로고
    • Copper absorption from human milk, cow's milk, and infant formulas using suckling rat model
    • Lönnerdal B, Bell JG, Keen CL. Copper absorption from human milk, cow's milk, and infant formulas using suckling rat model. Am J Clin Nutr 1985;42:836-44.
    • (1985) Am J Clin Nutr , vol.42 , pp. 836-844
    • Lönnerdal, B.1    Bell, J.G.2    Keen, C.L.3
  • 54
    • 0020740549 scopus 로고
    • Copper deficiency in humans
    • Williams DM. Copper deficiency in humans. Semin Hematol 1983;20:118-28.
    • (1983) Semin Hematol , vol.20 , pp. 118-128
    • Williams, D.M.1
  • 56
    • 0023800128 scopus 로고
    • Trace mineral balance during acute diarrhea in infants
    • Castillo-Duran C, Vial P, Uauy R. Trace mineral balance during acute diarrhea in infants. J Pediatr 1988;113:452-7.
    • (1988) J Pediatr , vol.113 , pp. 452-457
    • Castillo-Duran, C.1    Vial, P.2    Uauy, R.3
  • 58
    • 0017975751 scopus 로고
    • Skeletal changes of copper deficiency in infants receiving prolonged total parenteral nutrition
    • Heller RM, Kirchner SG, O'Neill JA Jr, et al. Skeletal changes of copper deficiency in infants receiving prolonged total parenteral nutrition. J Pediatr 1978;92:947-9.
    • (1978) J Pediatr , vol.92 , pp. 947-949
    • Heller, R.M.1    Kirchner, S.G.2    O'Neill Jr., J.A.3
  • 60
    • 0024506048 scopus 로고
    • Trace element metabolism in adult patients requiring total parenteral nutrition
    • Fleming CR. Trace element metabolism in adult patients requiring total parenteral nutrition. Am J Clin Nutr 1989;49:573-9.
    • (1989) Am J Clin Nutr , vol.49 , pp. 573-579
    • Fleming, C.R.1
  • 61
    • 0028205174 scopus 로고
    • Anemia and neutropenia due to copper deficiency in enteral nutrition
    • Tamura H, Hirose S, Watanabe O, et al. Anemia and neutropenia due to copper deficiency in enteral nutrition. JPEN J Parenter Enteral Nutr 1994;18:185-9.
    • (1994) JPEN J Parenter Enteral Nutr , vol.18 , pp. 185-189
    • Tamura, H.1    Hirose, S.2    Watanabe, O.3
  • 62
    • 0001188027 scopus 로고
    • Rules and regulations. Nutrient requirements for infant formulas
    • Food and Drug Administration. Rules and regulations. Nutrient requirements for infant formulas. Fed Regist 1985;50:45106-8.
    • (1985) Fed Regist , vol.50 , pp. 45106-45108
  • 63
    • 0018600076 scopus 로고
    • A conspectus of research on copper metabolism and requirements of man
    • Mason KE. A conspectus of research on copper metabolism and requirements of man. J Nutr 1979;109:1979-2066.
    • (1979) J Nutr , vol.109 , pp. 1979-2066
    • Mason, K.E.1
  • 64
    • 0024149135 scopus 로고
    • Copper deficiency in humans
    • Danks DM. Copper deficiency in humans. Annu Rev Nutr 1988;8:235-57.
    • (1988) Annu Rev Nutr , vol.8 , pp. 235-257
    • Danks, D.M.1
  • 66
    • 0002695932 scopus 로고
    • Failure of iron injection to reverse copper dependent anemia in mice
    • Mills CF, Bremner I, Chesters JK, eds. Bucks, United Kingdom: Commonwealth Agricultural Bureau
    • Prohaska JR, Bailey WR, Cox DA. Failure of iron injection to reverse copper dependent anemia in mice. In: Mills CF, Bremner I, Chesters JK, eds. Trace elements in man and animals. Bucks, United Kingdom: Commonwealth Agricultural Bureau, 1985:27-32
    • (1985) Trace Elements in Man and Animals , pp. 27-32
    • Prohaska, J.R.1    Bailey, W.R.2    Cox, D.A.3
  • 67
    • 2642633565 scopus 로고
    • Copper and protein depletion complicating hypoferric anemia of infancy
    • Schubert WK, Lahey ME. Copper and protein depletion complicating hypoferric anemia of infancy. Pediatrics 1959;24:710-33.
    • (1959) Pediatrics , vol.24 , pp. 710-733
    • Schubert, W.K.1    Lahey, M.E.2
  • 68
    • 2642661253 scopus 로고
    • Role of copper in iron metabolism and heme biosynthesis
    • Prasad AS, Oberleas D, eds. New York: Academic Press
    • Lee GE, Williams DM, Cartwright GE. Role of copper in iron metabolism and heme biosynthesis. In: Prasad AS, Oberleas D, eds. Trace elements in human health and disease. Vol 1. New York: Academic Press, 1976:373-90.
    • (1976) Trace Elements in Human Health and Disease , vol.1 , pp. 373-390
    • Lee, G.E.1    Williams, D.M.2    Cartwright, G.E.3
  • 69
    • 0023883524 scopus 로고
    • Copper deficiency impairs growth of infants recovering from malnutrition
    • Castillo-Duran C, Uauy R. Copper deficiency impairs growth of infants recovering from malnutrition. Am J Clin Nutr 1988;47:710-4.
    • (1988) Am J Clin Nutr , vol.47 , pp. 710-714
    • Castillo-Duran, C.1    Uauy, R.2
  • 72
    • 0021744133 scopus 로고
    • Increased cholesterol in plasma in a young man during experimental copper depletion
    • Klevay LM, Inman L, Johnson LK, et al. Increased cholesterol in plasma in a young man during experimental copper depletion. Metabolism 1984;33:1112-8.
    • (1984) Metabolism , vol.33 , pp. 1112-1118
    • Klevay, L.M.1    Inman, L.2    Johnson, L.K.3
  • 73
    • 0001081969 scopus 로고
    • Effect of copper intake on blood cholesterol and its lipoprotein distribution in men
    • Reiser S, Powell A, Yang CY, Canary JJ. Effect of copper intake on blood cholesterol and its lipoprotein distribution in men. Nutr Rep Int 1987;36:641-9.
    • (1987) Nutr Rep Int , vol.36 , pp. 641-649
    • Reiser, S.1    Powell, A.2    Yang, C.Y.3    Canary, J.J.4
  • 74
    • 0022620092 scopus 로고
    • Decreased glucose tolerance in two men during experimental copper depletion
    • Klevay LM, Canfield WK, Gallagher SK, et al. Decreased glucose tolerance in two men during experimental copper depletion. Nutr Rep Int 1986;33:371-82.
    • (1986) Nutr Rep Int , vol.33 , pp. 371-382
    • Klevay, L.M.1    Canfield, W.K.2    Gallagher, S.K.3
  • 75
    • 0023754406 scopus 로고
    • Effects of copper on human autonomic cardiovascular function
    • Lukaski HC, Klevay LM, Milne DB. Effects of copper on human autonomic cardiovascular function. Eur J Appl Physiol 1988;58:74-80.
    • (1988) Eur J Appl Physiol , vol.58 , pp. 74-80
    • Lukaski, H.C.1    Klevay, L.M.2    Milne, D.B.3
  • 78
    • 0028997219 scopus 로고
    • The metabolism of copper during pregnancy - A review
    • McArdle HJ. The metabolism of copper during pregnancy - a review. Food Chem 1995;54:79-84.
    • (1995) Food Chem , vol.54 , pp. 79-84
    • McArdle, H.J.1
  • 79
    • 0027272944 scopus 로고
    • Ceruloplasmin and copper transport during the latter part of gestation in the rat
    • Lee SH, Lancey R, Montaser A, Madani N, Linder MC. Ceruloplasmin and copper transport during the latter part of gestation in the rat. Proc Soc Exp Biol Med 1993;203:428-39.
    • (1993) Proc Soc Exp Biol Med , vol.203 , pp. 428-439
    • Lee, S.H.1    Lancey, R.2    Montaser, A.3    Madani, N.4    Linder, M.C.5
  • 80
    • 0025777805 scopus 로고
    • Copper uptake and transfer to the mouse fetus during pregnancy
    • McArdle HJ, Erlich R. Copper uptake and transfer to the mouse fetus during pregnancy. J Nutr 1991;121:208-14.
    • (1991) J Nutr , vol.121 , pp. 208-214
    • McArdle, H.J.1    Erlich, R.2
  • 81
    • 0021925472 scopus 로고
    • Distribution of copper among multiple components of human serum
    • Wirth PL, Linder MC. Distribution of copper among multiple components of human serum. J Natl Cancer Inst 1985;75:277-84
    • (1985) J Natl Cancer Inst , vol.75 , pp. 277-284
    • Wirth, P.L.1    Linder, M.C.2
  • 82
    • 0015622184 scopus 로고
    • Changes in total, nondiffusible, and diffusible plasma zinc and copper during infancy
    • Henkin RI, Schulman JD, Schulman CD, Bronzert DA. Changes in total, nondiffusible, and diffusible plasma zinc and copper during infancy. J Pediatr 1973;82:831-7.
    • (1973) J Pediatr , vol.82 , pp. 831-837
    • Henkin, R.I.1    Schulman, J.D.2    Schulman, C.D.3    Bronzert, D.A.4
  • 83
    • 0026638004 scopus 로고
    • Copper status of very low birth weight infants during the first 12 months of infancy
    • L'Abbé MR, Friel JK. Copper status of very low birth weight infants during the first 12 months of infancy. Pediatr Res 1992;32:183-8.
    • (1992) Pediatr Res , vol.32 , pp. 183-188
    • L'Abbé, M.R.1    Friel, J.K.2
  • 84
    • 0001567870 scopus 로고
    • Intakes and excretions of iron, copper, and zinc in the neonatal period
    • Cavell PA, Widdowson EM. Intakes and excretions of iron, copper, and zinc in the neonatal period. Arch Dis Child 1964;39:496-501.
    • (1964) Arch Dis Child , vol.39 , pp. 496-501
    • Cavell, P.A.1    Widdowson, E.M.2
  • 85
    • 0019366006 scopus 로고
    • Effect of oral copper supplementation on serum copper and ceruloplasmin concentrations in premature infants
    • Hillman LS, Martin L, Fiore B. Effect of oral copper supplementation on serum copper and ceruloplasmin concentrations in premature infants. J Pediatr 1981;98:311-3.
    • (1981) J Pediatr , vol.98 , pp. 311-313
    • Hillman, L.S.1    Martin, L.2    Fiore, B.3


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