메뉴 건너뛰기




Volumn 14, Issue 13, 2009, Pages 4878-4903

Molecular mechanisms of copper homeostasis

Author keywords

Chaperones; Copper; Cuproenzymes; Homeostasis; Menkes, review; Metallothioneins; Wilson

Indexed keywords

MAMMALIA;

EID: 69149095803     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/3575     Document Type: Article
Times cited : (53)

References (240)
  • 1
    • 0033826437 scopus 로고    scopus 로고
    • Cellular copper transport and metabolism
    • Harris, E. D.: Cellular copper transport and metabolism. Annu Rev Nutr, 20, 291-310(2000)
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 291-310
    • Harris, E.D.1
  • 4
    • 0025681888 scopus 로고
    • Phenotypic consequences of copper-zinc superoxide dismutase overexpression in Drosophila melanogaster
    • Staveley, B. E., J. P. Phillips & A. J. Hilliker: Phenotypic consequences of copper-zinc superoxide dismutase overexpression in Drosophila melanogaster. Genome, 33, 867-72(1990)
    • (1990) Genome , vol.33 , pp. 867-872
    • Staveley, B.E.1    Phillips, J.P.2    Hilliker, A.J.3
  • 5
    • 0018734969 scopus 로고
    • Changes in activity of the Cu-Zn superoxide dismutase enzyme in tissues of the rat with changes in dietary copper
    • Paynter, D. I., R. J. Moir & E. J. Underwood: Changes in activity of the Cu-Zn superoxide dismutase enzyme in tissues of the rat with changes in dietary copper. J Nutr, 109, 1570-6(1979) (Pubitemid 10229346)
    • (1979) Journal of Nutrition , vol.109 , Issue.9 , pp. 1570-1576
    • Paynter, D.I.1    Moir, R.J.2    Underwood, E.J.3
  • 6
    • 0034697370 scopus 로고    scopus 로고
    • Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism
    • DOI 10.1074/jbc.275.16.11645
    • De Freitas, J. M., A. Liba, R. Meneghini, J. S. Valentine & E. B. Gralla: Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism. J Biol Chem, 275, 11645-9(2000) (Pubitemid 30237724)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 11645-11649
    • De Freitas, J.M.1    Liba, A.2    Meneghini, R.3    Valentine, J.S.4    Gralla, E.B.5
  • 9
    • 0037354169 scopus 로고    scopus 로고
    • The copper-iron chronicles: The story of an intimate relationship
    • DOI 10.1023/A:1020799512190
    • Fox, P. L.: The copper-iron chronicles: the story of an intimate relationship. Biometals, 16, 9-40(2003) (Pubitemid 36140213)
    • (2003) BioMetals , vol.16 , Issue.1 , pp. 9-40
    • Fox, P.L.1
  • 11
    • 0034703872 scopus 로고    scopus 로고
    • The Menkes copper transporter is required for the activation of tyrosinase
    • Petris, M. J., D. Strausak & J. F. Mercer: The Menkes copper transporter is required for the activation of tyrosinase. Hum Mol Genet, 9, 2845-51(2000)
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2845-2851
    • Petris, M.J.1    Strausak, D.2    Mercer, J.F.3
  • 12
    • 0027937611 scopus 로고
    • Platelet thrombus formation and hemostasis are delayed in the microcirculation of copper-deficient rats
    • Schuschke, D. A., J. T. Saari, J. W. Nuss & F. N. Miller: Platelet thrombus formation and hemostasis are delayed in the microcirculation of copper-deficient rats. J Nutr, 124, 1258-64(1994) (Pubitemid 24270089)
    • (1994) Journal of Nutrition , vol.124 , Issue.8 , pp. 1258-1264
    • Schuschke, D.A.1    Saari, J.T.2    Nuss, J.W.3    Miller, F.N.4
  • 13
    • 0029367080 scopus 로고
    • Wilson's disease in personal material-disturbances in hemostasis
    • Jablonska-Kaszewska, I., E. Dabrowska & A. Ozieblowski: [Wilson's disease in personal material-disturbances in hemostasis]. Pol Tyg Lek, 50, 79-81(1995)
    • (1995) Pol. Tyg Lek , vol.50 , pp. 79-81
    • Jablonska-Kaszewska, I.1    Dabrowska, E.2    Ozieblowski, A.3
  • 14
    • 1642317603 scopus 로고    scopus 로고
    • A new proposal for the mechanism of glycine hydroxylation as catalyzed by peptidylglycine α-hydroxylating monooxygenase (PHM)
    • DOI 10.1016/j.mehy.2003.11.012
    • Owen, T. C. & D. J. Merkler: A new proposal for the mechanism of glycine hydroxylation as catalyzed by peptidylglycine alpha-hydroxylating monooxygenase (PHM). Med Hypotheses, 62, 392-400(2004) (Pubitemid 38388902)
    • (2004) Medical Hypotheses , vol.62 , Issue.3 , pp. 392-400
    • Owen, T.C.1    Merkler, D.J.2
  • 15
    • 0037409990 scopus 로고    scopus 로고
    • A mutation in the ATP7B copper transporter causes reduced dopamine β-hydroxylase and norepinephrine in mouse adrenal
    • DOI 10.1023/A:1023219308890
    • Gerbasi, V., S. Lutsenko & E. J. Lewis: A mutation in the ATP7B copper transporter causes reduced dopamine beta-hydroxylase and norepinephrine in mouse adrenal. Neurochem Res, 28, 867-73(2003) (Pubitemid 36438404)
    • (2003) Neurochemical Research , vol.28 , Issue.6 , pp. 867-873
    • Gerbasi, V.1    Lutsenko, S.2    Lewis, E.J.3
  • 16
    • 0027257306 scopus 로고
    • Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification
    • Zhou, P. & D. J. Thiele: Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification. Genes Dev, 7, 1824-35(1993) (Pubitemid 23269326)
    • (1993) Genes and Development , vol.7 , Issue.9 , pp. 1824-1835
    • Zhou, P.1    Thiele, D.J.2
  • 17
    • 0024044018 scopus 로고
    • ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene
    • Thiele, D. J.: ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol Cell Biol, 8, 2745-52(1988)
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2745-2752
    • Thiele, D.J.1
  • 18
    • 0029910647 scopus 로고    scopus 로고
    • Differential modulation by zinc and copper of amino acid receptors from rat olfactory bulb neurons
    • Trombley, P. Q. & G. M. Shepherd: Differential modulation by zinc and copper of amino acid receptors from rat olfactory bulb neurons. J Neurophysiol, 76, 2536-46(1996) (Pubitemid 26346427)
    • (1996) Journal of Neurophysiology , vol.76 , Issue.4 , pp. 2536-2546
    • Trombley, P.Q.1    Shepherd, G.M.2
  • 19
    • 0030661885 scopus 로고    scopus 로고
    • 7 receptor
    • DOI 10.1016/S0028-3908(97)00141-X, PII S002839089700141X
    • Virginio, C., D. Church, R. A. North & A. Surprenant: Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor. Neuropharmacology, 36, 1285-94(1997) (Pubitemid 27465616)
    • (1997) Neuropharmacology , vol.36 , Issue.9 , pp. 1285-1294
    • Virginio, C.1    Church, D.2    North, R.A.3    Surprenant, A.4
  • 21
    • 0017833890 scopus 로고
    • Superoxide dependent production of hydroxyl radical catalyzed by iron EDTA complex
    • DOI 10.1016/0014-5793(78)80116-1
    • McCord, J. M. & E. D. Day, Jr.: Superoxidedependent production of hydroxyl radical catalyzed by iron-EDTA complex. FEBS Lett, 86, 139-42(1978) (Pubitemid 8264454)
    • (1978) FEBS Letters , vol.86 , Issue.1 , pp. 139-142
    • McCord, J.M.1    Day Jr., E.D.2
  • 23
    • 0028152451 scopus 로고
    • The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake
    • Dancis, A., D. Haile, D. S. Yuan & R. D. Klausner: The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J Biol Chem, 269, 25660-7(1994)
    • (1994) J. Biol. Chem. , vol.269 , pp. 25660-25667
    • Dancis, A.1    Haile, D.2    Yuan, D.S.3    Klausner, R.D.4
  • 25
    • 0029786735 scopus 로고    scopus 로고
    • A widespread transposable element masks expression of a yeast copper transport gene
    • Knight, S. A., S. Labbe, L. F. Kwon, D. J. Kosman & D. J. Thiele: A widespread transposable element masks expression of a yeast copper transport gene. Genes Dev, 10, 1917-29(1996) (Pubitemid 26281686)
    • (1996) Genes and Development , vol.10 , Issue.15 , pp. 1917-1929
    • Knight, S.A.B.1    Labbe, S.2    Kwon, L.F.3    Kosman, D.J.4    Thiele, D.J.5
  • 26
    • 0028818858 scopus 로고
    • Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue
    • Kampfenkel, K., S. Kushnir, E. Babiychuk, D. Inze & M. Van Montagu: Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue. J Biol Chem, 270, 28479-86(1995)
    • (1995) J. Biol. Chem. , vol.270 , pp. 28479-28486
    • Kampfenkel, K.1    Kushnir, S.2    Babiychuk, E.3    Inze, D.4    Van Montagu, M.5
  • 28
    • 11144247945 scopus 로고    scopus 로고
    • Mobilization of intracellular copper stores by the Ctr2 vacuolar copper transporter
    • DOI 10.1074/jbc.M411669200
    • Rees, E. M., J. Lee & D. J. Thiele: Mobilization of intracellular copper stores by the ctr2 vacuolar copper transporter. J Biol Chem, 279, 54221-9(2004) (Pubitemid 40053159)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54221-54229
    • Rees, E.M.1    Lee, J.2    Thiele, D.J.3
  • 29
    • 0034893220 scopus 로고    scopus 로고
    • Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae
    • DOI 10.1007/s004380100482
    • Portnoy, M. E., P. J. Schmidt, R. S. Rogers & V. C. Culotta: Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae. Mol Genet Genomics, 265, 873-82(2001) (Pubitemid 32763301)
    • (2001) Molecular Genetics and Genomics , vol.265 , Issue.5 , pp. 873-882
    • Portnoy, M.E.1    Schmidt, P.J.2    Rogers, R.S.3    Culotta, V.C.4
  • 30
    • 8744280624 scopus 로고    scopus 로고
    • Cisplatin stabilizes a multimeric complex of the human Ctr1 copper transporter: Requirement for the extracellular methionine-rich clusters
    • DOI 10.1074/jbc.M407777200
    • Guo, Y., K. Smith & M. J. Petris: Cisplatin stabilizes a multimeric complex of the human Ctr1 copper transporter: requirement for the extracellular methionine-rich clusters. J Biol Chem, 279, 46393-9(2004) (Pubitemid 39518280)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 46393-46399
    • Guo, Y.1    Smith, K.2    Petris, M.J.3
  • 31
    • 0037135627 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake
    • DOI 10.1074/jbc.M202547200
    • Puig, S., J. Lee, M. Lau & D. J. Thiele: Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake. J Biol Chem, 277, 26021-30(2002) (Pubitemid 34967084)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26021-26030
    • Puig, S.1    Lee, J.2    Lau, M.3    Thiele, D.J.4
  • 32
    • 0037040252 scopus 로고    scopus 로고
    • Biochemical characterization of the human copper transporter Ctr1
    • DOI 10.1074/jbc.M104728200
    • Lee, J., M. M. Pena, Y. Nose & D. J. Thiele: Biochemical characterization of the human copper transporter Ctr1. J Biol Chem, 277, 4380-7(2002) (Pubitemid 34968704)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 4380-4387
    • Lee, J.1    Pena, M.M.O.2    Nose, Y.3    Thiele, D.J.4
  • 33
    • 27744526783 scopus 로고    scopus 로고
    • The mechanism of copper uptake mediated by human CTR1: A mutational analysis
    • DOI 10.1074/jbc.M508822200
    • Eisses, J. F. & J. H. Kaplan: The mechanism of copper uptake mediated by human CTR1: a mutational analysis. J Biol Chem, 280, 37159-68(2005) (Pubitemid 41587800)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.44 , pp. 37159-37168
    • Eisses, J.F.1    Kaplan, J.H.2
  • 34
    • 1642404510 scopus 로고    scopus 로고
    • C-Terminal Domain of the Membrane Copper Transporter Ctr1 from Saccharomyces cerevisiae Binds Four Cu(I) Ions as a Cuprous-Thiolate Polynuclear Cluster: Sub-femtomolar Cu(I) Affinity of Three Proteins Involved in Copper Trafficking
    • DOI 10.1021/ja0390350
    • Xiao, Z., F. Loughlin, G. N. George, G. J. Howlett & A. G. Wedd: C-terminal domain of the membrane copper transporter Ctr1 from Saccharomyces cerevisiae binds four Cu (I) ions as a cuprous-thiolate polynuclear cluster: subfemtomolar Cu (I) affinity of three proteins involved in copper trafficking. J Am Chem Soc, 126, 3081-90(2004) (Pubitemid 38380713)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.10 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 35
    • 0037149377 scopus 로고    scopus 로고
    • A C-terminal domain of the membrane copper pump Ctr1 exchanges copper (I) with the copper chaperone Atx1
    • Xiao, Z. & A. G. Wedd: A C-terminal domain of the membrane copper pump Ctr1 exchanges copper (I) with the copper chaperone Atx1. Chem Commun (Camb) 588-9 (2002)
    • Chem. Commun. (Camb) 588-9 (2002)
    • Xiao, Z.1    Wedd, A.G.2
  • 36
    • 2342444345 scopus 로고    scopus 로고
    • Identification of Methionine-rich Clusters That Regulate Copper-stimulated Endocytosis of the Human Ctr1 Copper Transporter
    • DOI 10.1074/jbc.M401493200
    • Guo, Y., K. Smith, J. Lee, D. J. Thiele & M. J. Petris: Identification of methionine-rich clusters that regulate copper-stimulated endocytosis of the human Ctr1 copper transporter. J Biol Chem, 279, 17428-33(2004) (Pubitemid 38560505)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.17 , pp. 17428-17433
    • Guo, Y.1    Smith, K.2    Lee, J.3    Thiele, D.J.4    Petris, M.J.5
  • 37
    • 0038439210 scopus 로고    scopus 로고
    • Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1
    • DOI 10.1074/jbc.M209455200
    • Petris, M. J., K. Smith, J. Lee & D. J. Thiele: Copperstimulated endocytosis and degradation of the human copper transporter, hCtr1. J Biol Chem, 278, 9639-46(2003) (Pubitemid 36800460)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9639-9646
    • Petris, M.J.1    Smith, K.2    Lee, J.3    Thiele, D.J.4
  • 38
    • 31544454133 scopus 로고    scopus 로고
    • Copper transport protein (Ctr1) levels in mice are tissue specific and dependent on copper status
    • Kuo, Y. M., A. A. Gybina, J. W. Pyatskowit, J. Gitschier & J. R. Prohaska: Copper transport protein (Ctr1) levels in mice are tissue specific and dependent on copper status. J Nutr, 136, 21-6(2006) (Pubitemid 43156479)
    • (2006) Journal of Nutrition , vol.136 , Issue.1 , pp. 21-26
    • Kuo, Y.-M.1    Gybina, A.A.2    Pyatskowit, J.W.3    Gitschier, J.4    Prohaska, J.R.5
  • 39
    • 0037174814 scopus 로고    scopus 로고
    • Characterization of mouse embryonic cells deficient in the Ctr1 high affinity copper transporter: Identification of a Ctr1-independent copper transport system
    • DOI 10.1074/jbc.M208002200
    • Lee, J., M. J. Petris & D. J. Thiele: Characterization of mouse embryonic cells deficient in the ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system. J Biol Chem, 277, 40253-9(2002) (Pubitemid 35215596)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 40253-40259
    • Lee, J.1    Petris, M.J.2    Thiele, D.J.3
  • 43
    • 0027978892 scopus 로고
    • Role of cytosolic copper, metallothionein and glutathione in copper toxicity in rat hepatoma tissue culture cells
    • DOI 10.1016/0300-483X(94)90168-6
    • Steinebach, O. M. & H. T. Wolterbeek: Role of cytosolic copper, metallothionein and glutathione in copper toxicity in rat hepatoma tissue culture cells. Toxicology, 92, 75-90(1994) (Pubitemid 24293216)
    • (1994) Toxicology , vol.92 , Issue.1-3 , pp. 75-90
    • Steinebach, O.M.1    Th Wolterbeek, H.2
  • 48
    • 0023087396 scopus 로고
    • Chemistry and biochemistry of metallothionein
    • Kagi, J. H. & Y. Kojima: Chemistry and biochemistry of metallothionein. Experientia Suppl, 52, 25-61(1987)
    • (1987) Experientia Suppl. , vol.52 , pp. 25-61
    • Kagi, J.H.1    Kojima, Y.2
  • 50
    • 0022971828 scopus 로고
    • Yeast metallothionein function in metal ion detoxification
    • Ecker, D. J., T. R. Butt, E. J. Sternberg, M. P. Neeper, C. Debouck, J. A. Gorman & S. T. Crooke: Yeast metallothionein function in metal ion detoxification. J Biol Chem, 261, 16895-900(1986) (Pubitemid 17210332)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.36 , pp. 16895-16900
    • Ecker, D.J.1    Butt, T.R.2    Sternberg, E.J.3
  • 51
    • 33847216851 scopus 로고    scopus 로고
    • Copper homeostasis in Drosophila by complex interplay of import, storage and behavioral avoidance
    • Balamurugan, K., D. Egli, H. Hua, R. Rajaram, G. Seisenbacher, O. Georgiev & W. Schaffner: Copper homeostasis in Drosophila by complex interplay of import, storage and behavioral avoidance. Embo J, 26, 1035-44(2007)
    • (2007) Embo J. , vol.26 , pp. 1035-1044
    • Balamurugan, K.1    Egli, D.2    Hua, H.3    Rajaram, R.4    Seisenbacher, G.5    Georgiev, O.6    Schaffner, W.7
  • 52
    • 0030665778 scopus 로고    scopus 로고
    • Primary structure of a copper-binding metallothionein from mantle tissue of the terrestrial gastropod Helix pomatia L
    • Berger, B., R. Dallinger, P. Gehrig & P. E. Hunziker: Primary structure of a copper-binding metallothionein from mantle tissue of the terrestrial gastropod Helix pomatia L. Biochem J, 328(Pt 1), 219-24(1997) (Pubitemid 27499462)
    • (1997) Biochemical Journal , vol.328 , Issue.1 , pp. 219-224
    • Berger, B.1    Dallinger, R.2    Gehrig, P.3    Hunziker, P.E.4
  • 54
    • 33750941551 scopus 로고    scopus 로고
    • Metal-dependent protein folding: Metallation of metallothionein
    • DOI 10.1016/j.jinorgbio.2006.09.005, PII S0162013406002571
    • Rigby Duncan, K. E. & M. J. Stillman: Metaldependent protein folding: metallation of metallothionein. J Inorg Biochem, 100, 2101-7(2006) (Pubitemid 44738050)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.12 , pp. 2101-2107
    • Rigby Duncan, K.E.1    Stillman, M.J.2
  • 55
    • 33747849534 scopus 로고    scopus 로고
    • Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function
    • DOI 10.1016/j.cmet.2006.08.009, PII S1550413106002798
    • Nose, Y., B. E. Kim & D. J. Thiele: Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function. Cell Metab, 4, 235-44(2006) (Pubitemid 44283961)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 235-244
    • Nose, Y.1    Kim, B.-E.2    Thiele, D.J.3
  • 58
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • DOI 10.1074/jbc.271.24.14504
    • Glerum, D. M., A. Shtanko & A. Tzagoloff: Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem, 271, 14504-9(1996) (Pubitemid 26190352)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.24 , pp. 14504-14509
    • Moira Glerum, D.1    Shtanko, A.2    Tzagoloff, A.3
  • 59
    • 0031045676 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment
    • DOI 10.1007/s004390050367
    • Amaravadi, R., D. M. Glerum & A. Tzagoloff: Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. Hum Genet, 99, 329-33(1997) (Pubitemid 27095793)
    • (1997) Human Genetics , vol.99 , Issue.3 , pp. 329-333
    • Amaravadi, R.1    Glerum, D.M.2    Tzagoloff, A.3
  • 60
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the Cu(B) and magnesium centers of cytochrome c oxidase
    • DOI 10.1074/jbc.275.1.619
    • Hiser, L., M. di Valentin, A. G. Hamer & J. P. Hosler: Cox11p is required for stable formation of the Cu (B) and magnesium centers of cytochrome c oxidase. J Biol Chem, 275, 619-23(2000) (Pubitemid 30039026)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.1 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 61
    • 0033539566 scopus 로고    scopus 로고
    • Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis
    • Hamza, I., M. Schaefer, L. W. Klomp & J. D. Gitlin: Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis. Proc Natl Acad Sci U S A, 96, 13363-8(1999)
    • (1999) Proc. Natl. Acad. Sci. U S A , vol.96 , pp. 13363-13368
    • Hamza, I.1    Schaefer, M.2    Klomp, L.W.3    Gitlin, J.D.4
  • 62
    • 0033214908 scopus 로고    scopus 로고
    • Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p
    • Larin, D., C. Mekios, K. Das, B. Ross, A. S. Yang & T. C. Gilliam: Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p. J Biol Chem, 274, 28497-504(1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 28497-28504
    • Larin, D.1    Mekios, C.2    Das, K.3    Ross, B.4    Yang, A.S.5    Gilliam, T.C.6
  • 63
    • 0037008692 scopus 로고    scopus 로고
    • 2-terminal domain of the Wilson's disease protein and regulates its catalytic activity
    • DOI 10.1074/jbc.M203845200
    • Walker, J. M., R. Tsivkovskii & S. Lutsenko: Metallochaperone Atox1 transfers copper to the NH2-terminal domain of the Wilson's disease protein and regulates its catalytic activity. J Biol Chem, 277, 27953-9(2002) (Pubitemid 34966743)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 27953-27959
    • Walker, J.M.1    Tsivkovskii, R.2    Lutsenko, S.3
  • 64
    • 0035936586 scopus 로고    scopus 로고
    • The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex
    • DOI 10.1021/bi002315x
    • Heaton, D. N., G. N. George, G. Garrison & D. R. Winge: The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry, 40, 743-51(2001) (Pubitemid 32096859)
    • (2001) Biochemistry , vol.40 , Issue.3 , pp. 743-751
    • Heaton, D.N.1    George, G.N.2    Garrison, G.3    Winge, D.R.4
  • 65
  • 67
    • 0024289334 scopus 로고
    • The resistance of transferrin, lactoferrin and caeruloplasmin to oxidative damage
    • Halliwell, B., O. I. Aruoma, M. Wasil & J. M. Gutteridge: The resistance of transferrin, lactoferrin and caeruloplasmin to oxidative damage. Biochem J, 256, 311-2(1988)
    • (1988) Biochem. J. , vol.256 , pp. 311-312
    • Halliwell, B.1    Aruoma, O.I.2    Wasil, M.3    Gutteridge, J.M.4
  • 68
    • 0030839796 scopus 로고    scopus 로고
    • N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes Disease Proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal- binding repeat
    • DOI 10.1074/jbc.272.30.18939
    • Lutsenko, S., K. Petrukhin, M. J. Cooper, C. T. Gilliam & J. H. Kaplan: N-terminal domains of human coppertransporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metalbinding repeat. J Biol Chem, 272, 18939-44(1997) (Pubitemid 27318247)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18939-18944
    • Lutsenko, S.1    Petrukhin, K.2    Cooper, M.J.3    Gilliam, C.T.4    Kaplan, J.H.5
  • 69
    • 0033003072 scopus 로고    scopus 로고
    • Characterisation of copper-binding to the second sub-domain of the Menkes protein ATPase (MNKr2)
    • DOI 10.1016/S0925-4439(98)00110-0, PII S0925443998001100
    • Harrison, M. D., S. Meier & C. T. Dameron: Characterisation of copper-binding to the second subdomain of the Menkes protein ATPase (MNKr2). Biochim Biophys Acta, 1453, 254-60(1999) (Pubitemid 29092763)
    • (1999) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1453 , Issue.2 , pp. 254-260
    • Harrison, M.D.1    Meier, S.2    Dameron, C.T.3
  • 70
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • DOI 10.1126/science.284.5415.805
    • Rae, T. D., P. J. Schmidt, R. A. Pufahl, V. C. Culotta & T. V. O'Halloran: Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science, 284, 805-8(1999) (Pubitemid 29291346)
    • (1999) Science , vol.284 , Issue.5415 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 71
    • 33744948516 scopus 로고    scopus 로고
    • Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase
    • DOI 10.1074/jbc.M601580200
    • Caruano-Yzermans, A. L., T. B. Bartnikas & J. D. Gitlin: Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase. J Biol Chem, 281, 13581-7(2006) (Pubitemid 43855272)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13581-13587
    • Caruano-Yzermans, A.L.1    Bartnikas, T.B.2    Gitlin, J.D.3
  • 73
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • DOI 10.1074/jbc.273.37.23625
    • Casareno, R. L., D. Waggoner & J. D. Gitlin: The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J Biol Chem, 273, 23625-8(1998) (Pubitemid 28435686)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 23625-23628
    • Casareno, R.L.B.1    Waggoner, D.2    Gitlin, J.D.3
  • 75
    • 29244480623 scopus 로고    scopus 로고
    • Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS
    • DOI 10.1074/jbc.M509142200
    • Jensen, L. T. & V. C. Culotta: Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS. J Biol Chem, 280, 41373-9(2005) (Pubitemid 41832195)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41373-41379
    • Jensen, L.T.1    Culotta, V.C.2
  • 78
    • 0028815433 scopus 로고
    • Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons
    • Pardo, C. A., Z. Xu, D. R. Borchelt, D. L. Price, S. S. Sisodia & D. W. Cleveland: Superoxide dismutase is an abundant component in cell bodies, dendrites, and axons of motor neurons and in a subset of other neurons. Proc Natl Acad Sci U S A, 92, 954-8(1995)
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 954-958
    • Pardo, C.A.1    Xu, Z.2    Borchelt, D.R.3    Price, D.L.4    Sisodia, S.S.5    Cleveland, D.W.6
  • 79
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord, J. M. & I. Fridovich: Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J Biol Chem, 244, 6049-55(1969)
    • (1969) J. Biol. Chem. , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 80
    • 0033566721 scopus 로고    scopus 로고
    • A model for the incorporation of metal from the copper chaperone CCS into Cu,Zn superoxide dismutase
    • DOI 10.1016/S0969-2126(99)80117-8
    • Falconi, M., M. Iovino & A. Desideri: A model for the incorporation of metal from the copper chaperone CCS into Cu, Zn superoxide dismutase. Structure, 7, 903-8(1999) (Pubitemid 29372512)
    • (1999) Structure , vol.7 , Issue.8 , pp. 903-908
    • Falconi, M.1    Iovino, M.2    Desideri, A.3
  • 81
    • 0042858163 scopus 로고    scopus 로고
    • Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase
    • DOI 10.1074/jbc.M305435200
    • Bartnikas, T. B. & J. D. Gitlin: Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase. J Biol Chem, 278, 33602-8(2003) (Pubitemid 37055814)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 33602-33608
    • Bartnikas, T.B.1    Gitlin, J.D.2
  • 82
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.34.20531
    • Glerum, D. M., A. Shtanko & A. Tzagoloff: SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J Biol Chem, 271, 20531-5(1996) (Pubitemid 26281827)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20531-20535
    • Moira Glerum, D.1    Shtanko, A.2    Tzagoloff, A.3
  • 83
    • 15844417719 scopus 로고    scopus 로고
    • Mammalian cytochrome c oxidase, a molecular monster subdued
    • DOI 10.1126/science.272.5265.1125
    • Ferguson-Miller, S.: Mammalian cytochrome c oxidase, a molecular monster subdued. Science, 272, 1125(1996) (Pubitemid 26169465)
    • (1996) Science , vol.272 , Issue.5265 , pp. 1125
    • Ferguson-Miller, S.1
  • 84
    • 0000021902 scopus 로고    scopus 로고
    • Heme/copper terminal oxidases
    • Ferguson-Miller, S. & G. T. Babcock: Heme/Copper Terminal Oxidases. Chem Rev, 96, 2889-2908(1996)
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.T.2
  • 85
    • 0037163087 scopus 로고    scopus 로고
    • Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I)-binding protein
    • DOI 10.1074/jbc.M204854200
    • Carr, H. S., G. N. George & D. R. Winge: Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu (I)-binding protein. J Biol Chem, 277, 31237-42(2002) (Pubitemid 34970831)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 86
    • 0026058705 scopus 로고
    • Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane
    • Buchwald, P., G. Krummeck & G. Rodel: Immunological identification of yeast SCO1 protein as a component of the inner mitochondrial membrane. Mol Gen Genet, 229, 413-20(1991)
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 413-420
    • Buchwald, P.1    Krummeck, G.2    Rodel, G.3
  • 87
    • 1842739598 scopus 로고    scopus 로고
    • Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix
    • DOI 10.1074/jbc.M312693200
    • Cobine, P. A., L. D. Ojeda, K. M. Rigby & D. R. Winge: Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. J Biol Chem, 279, 14447-55(2004) (Pubitemid 38468987)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14447-14455
    • Cobine, P.A.1    Ojeda, L.D.2    Rigby, K.M.3    Winge, D.R.4
  • 88
    • 1242294474 scopus 로고    scopus 로고
    • Cox17 is functional when tethered to the mitochondrial inner membrane
    • DOI 10.1074/jbc.M311772200
    • Maxfield, A. B., D. N. Heaton & D. R. Winge: Cox17 is functional when tethered to the mitochondrial inner membrane. J Biol Chem, 279, 5072-80(2004) (Pubitemid 38220523)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5072-5080
    • Maxfield, A.B.1    Heaton, D.N.2    Winge, D.R.3
  • 89
    • 4344560984 scopus 로고    scopus 로고
    • Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase
    • DOI 10.1042/BJ20040360
    • Palumaa, P., L. Kangur, A. Voronova & R. Sillard: Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Biochem J, 382, 307-14(2004) (Pubitemid 39141594)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 307-314
    • Palumaa, P.1    Kangur, L.2    Voronova, A.3    Sillard, R.4
  • 91
    • 0034534913 scopus 로고    scopus 로고
    • Mutational analysis of the mitochondrial copper metallochaperone Cox17
    • DOI 10.1074/jbc.M006639200
    • Heaton, D., T. Nittis, C. Srinivasan & D. R. Winge: Mutational analysis of the mitochondrial copper metallochaperone Cox17. J Biol Chem, 275, 37582-7(2000) (Pubitemid 32004868)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37582-37587
    • Heaton, D.1    Nittis, T.2    Srinivasan, C.3    Winge, D.R.4
  • 94
    • 4143074731 scopus 로고    scopus 로고
    • Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase
    • DOI 10.1074/jbc.M404747200
    • Horng, Y. C., P. A. Cobine, A. B. Maxfield, H. S. Carr & D. R. Winge: Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. J Biol Chem, 279, 35334-40(2004) (Pubitemid 39100532)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.34 , pp. 35334-35340
    • Horng, Y.-C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 97
    • 0033930194 scopus 로고    scopus 로고
    • Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes
    • Chinenov, Y. V.: Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes. J Mol Med, 78, 239-42(2000) (Pubitemid 30489706)
    • (2000) Journal of Molecular Medicine , vol.78 , Issue.5 , pp. 239-242
    • Chinenov, Y.V.1
  • 98
    • 34249849560 scopus 로고    scopus 로고
    • Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M610082200
    • Rigby, K., L. Zhang, P. A. Cobine, G. N. George & D. R. Winge: characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae. J Biol Chem, 282, 10233-42(2007) (Pubitemid 47093419)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10233-10242
    • Rigby, K.1    Zhang, L.2    Cobine, P.A.3    George, G.N.4    Winge, D.R.5
  • 99
    • 14844336406 scopus 로고    scopus 로고
    • Ortholog search of proteins involved in copper delivery to cytochrome c oxidase and functional analysis of paralogs and gene neighbors by genomic context
    • DOI 10.1021/pr049862f
    • Arnesano, F., L. Banci, I. Bertini & M. Martinelli: Ortholog search of proteins involved in copper delivery to cytochrome C oxidase and functional analysis of paralogs and gene neighbors by genomic context. J Proteome Res, 4, 63-70(2005) (Pubitemid 40344457)
    • (2005) Journal of Proteome Research , vol.4 , Issue.1 , pp. 63-70
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4
  • 101
    • 0025071742 scopus 로고
    • Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3
    • Tzagoloff, A., N. Capitanio, M. P. Nobrega & D. Gatti: Cytochrome oxidase assembly in yeast requires the product of COX11, a homolog of the P. denitrificans protein encoded by ORF3. Embo J, 9, 2759-64(1990)
    • (1990) Embo J. , vol.9 , pp. 2759-2764
    • Tzagoloff, A.1    Capitanio, N.2    Nobrega, M.P.3    Gatti, D.4
  • 103
    • 33645052707 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p
    • Banting, G. S. & D. M. Glerum: Mutational analysis of the Saccharomyces cerevisiae cytochrome c oxidase assembly protein Cox11p. Eukaryot Cell, 5, 568-78(2006)
    • (2006) Eukaryot Cell. , vol.5 , pp. 568-578
    • Banting, G.S.1    Glerum, D.M.2
  • 105
    • 0242600563 scopus 로고    scopus 로고
    • Proton transfer reactions associated with the reaction of the fully reduced, purified cytochrome c oxidase with molecular oxygen and ferricyanide
    • DOI 10.1021/bi0206208
    • Capitanio, N., G. Capitanio, E. de Nitto, D. Boffoli & S. Papa: Proton transfer reactions associated with the reaction of the fully reduced, purified cytochrome C oxidase with molecular oxygen and ferricyanide. Biochemistry, 42, 4607-12(2003) (Pubitemid 36506015)
    • (2003) Biochemistry , vol.42 , Issue.16 , pp. 4607-4612
    • Capitanio, N.1    Capitanio, G.2    De Nitto, E.3    Boffoli, D.4    Papa, S.5
  • 106
    • 0029039920 scopus 로고
    • The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity
    • Lin, S. J. & V. C. Culotta: The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci U S A, 92, 3784-8(1995)
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 3784-3788
    • Lin, S.J.1    Culotta, V.C.2
  • 107
    • 38649114700 scopus 로고    scopus 로고
    • Interplay between glutathione, Atx1 and copper. 1. Copper(I) glutathionate induced dimerization of Atx1
    • DOI 10.1007/s00775-007-0310-2
    • Miras, R., I. Morin, O. Jacquin, M. Cuillel, F. Guillain & E. Mintz: Interplay between glutathione, Atx1 and copper. 1. Copper (I) glutathionate induced dimerization of Atx1. J Biol Inorg Chem, 13, 195-205(2008) (Pubitemid 351172174)
    • (2008) Journal of Biological Inorganic Chemistry , vol.13 , Issue.2 , pp. 195-205
    • Miras, R.1    Morin, I.2    Jacquin, O.3    Cuillel, M.4    Guillain, F.5    Mintz, E.6
  • 108
    • 2442572209 scopus 로고    scopus 로고
    • The N-terminal Metal-binding Site 2 of the Wilson's Disease Protein Plays a Key Role in the Transfer of Copper from Atox1
    • DOI 10.1074/jbc.M400053200
    • Walker, J. M., D. Huster, M. Ralle, C. T. Morgan, N. J. Blackburn & S. Lutsenko: The N-terminal metal-binding site 2 of the Wilson's Disease Protein plays a key role in the transfer of copper from Atox1. J Biol Chem, 279, 15376-84(2004) (Pubitemid 38618936)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15376-15384
    • Walker, J.M.1    Huster, D.2    Ralle, M.3    Morgan, C.T.4    Blackburn, N.J.5    Lutsenko, S.6
  • 109
    • 0033813548 scopus 로고    scopus 로고
    • Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins
    • Wernimont, A. K., D. L. Huffman, A. L. Lamb, T. V. O'Halloran & A. C. Rosenzweig: Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat Struct Biol, 7, 766-71(2000)
    • (2000) Nat. Struct Biol. , vol.7 , pp. 766-771
    • Wernimont, A.K.1    Huffman, D.L.2    Lamb, A.L.3    O'Halloran, T.V.4    Rosenzweig, A.C.5
  • 112
    • 0028916909 scopus 로고
    • The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake
    • Yuan, D. S., R. Stearman, A. Dancis, T. Dunn, T. Beeler & R. D. Klausner: The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc Natl Acad Sci U S A, 92, 2632-6(1995)
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 2632-2636
    • Yuan, D.S.1    Stearman, R.2    Dancis, A.3    Dunn, T.4    Beeler, T.5    Klausner, R.D.6
  • 113
    • 0031055871 scopus 로고    scopus 로고
    • Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network
    • DOI 10.1093/hmg/6.3.409
    • Dierick, H. A., A. N. Adam, J. F. Escara-Wilke & T. W. Glover: Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network. Hum Mol Genet, 6, 409-16(1997) (Pubitemid 27116461)
    • (1997) Human Molecular Genetics , vol.6 , Issue.3 , pp. 409-416
    • Dierick, H.A.1    Adam, A.N.2    Escara-Wilke, J.F.3    Glover, T.W.4
  • 114
    • 0029847157 scopus 로고    scopus 로고
    • ATP-dependent copper transporter, in the Golgi apparatus of rat hepatocytes, transports Cu (II) not Cu (I)
    • Bingham, M. J., T. J. Ong, W. J. Ingledew & H. J. McArdle: ATP-dependent copper transporter, in the Golgi apparatus of rat hepatocytes, transports Cu (II) not Cu (I). Am J Physiol, 271, G741-6 (1996)
    • (1996) Am. J. Physiol. , vol.271
    • Bingham, M.J.1    Ong, T.J.2    Ingledew, W.J.3    McArdle, H.J.4
  • 115
    • 34447103789 scopus 로고    scopus 로고
    • Trafficking of the copper-ATPases, ATP7A and ATP7B: Role in copper homeostasis
    • DOI 10.1016/j.abb.2007.04.021, PII S000398610700210X
    • La Fontaine, S. & J. F. Mercer: Trafficking of the copper-ATPases, ATP7A and ATP7B: role in copper homeostasis. Arch Biochem Biophys, 463, 149-67(2007) (Pubitemid 47030343)
    • (2007) Archives of Biochemistry and Biophysics , vol.463 , Issue.2 , pp. 149-167
    • La Fontaine, S.1    Mercer, J.F.B.2
  • 116
    • 34248633103 scopus 로고    scopus 로고
    • 1B- ATPases
    • DOI 10.1007/s10534-006-9055-6, Biometals: function and transport in bacteria, fungi, and humans
    • Arguello, J. M., E. Eren & M. Gonzalez-Guerrero: The structure and function of heavy metal transport P1B-ATPases. Biometals, 20, 233-48(2007) (Pubitemid 46776570)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 233-248
    • Arguello, J.M.1    Eren, E.2    Gonzalez-Guerrero, M.3
  • 118
    • 0033617198 scopus 로고    scopus 로고
    • Role of the copper-binding domain in the copper transport function of ATP7B, the P-type ATPase defective in Wilson disease
    • Forbes, J. R., G. Hsi & D. W. Cox: Role of the copper-binding domain in the copper transport function of ATP7B, the P-type ATPase defective in Wilson disease. J Biol Chem, 274, 12408-13(1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 12408-12413
    • Forbes, J.R.1    Hsi, G.2    Cox, D.W.3
  • 119
    • 0034700982 scopus 로고    scopus 로고
    • Copper-induced conformational changes in the N-terminal domain of the Wilson disease copper-transporting ATPase
    • DOI 10.1021/bi992222j
    • DiDonato, M., H. F. Hsu, S. Narindrasorasak, L. Que, Jr. & B. Sarkar: Copper-induced conformational changes in the N-terminal domain of the Wilson disease coppertransporting ATPase. Biochemistry, 39, 1890-6(2000) (Pubitemid 30108982)
    • (2000) Biochemistry , vol.39 , Issue.7 , pp. 1890-1896
    • DiDonato, M.1    Hsu, H.-F.2    Narindrasorasak, S.3    Que Jr., L.4    Sarkar, B.5
  • 120
    • 0037354166 scopus 로고    scopus 로고
    • Copper-induced trafficking of the Cu-ATPases: A key mechanism for copper homeostasis
    • DOI 10.1023/A:1020719016675
    • Mercer, J. F., N. Barnes, J. Stevenson, D. Strausak & R. M. Llanos: Copper-induced trafficking of the cU-ATPases: a key mechanism for copper homeostasis. Biometals, 16, 175-84(2003) (Pubitemid 36140227)
    • (2003) BioMetals , vol.16 , Issue.1 , pp. 175-184
    • Mercer, J.F.B.1    Barnes, N.2    Stevenson, J.3    Strausak, D.4    Llanos, R.M.5
  • 122
    • 0035910261 scopus 로고    scopus 로고
    • 1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • DOI 10.1074/jbc.M003238200
    • Tsivkovskii, R., B. C. MacArthur & S. Lutsenko: The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner. J Biol Chem, 276, 2234-42(2001) (Pubitemid 32109707)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3
  • 123
    • 0041856098 scopus 로고    scopus 로고
    • The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein
    • DOI 10.1074/jbc.M305408200
    • Huster, D. & S. Lutsenko: The distinct roles of the N-terminal copper-binding sites in regulation of catalytic activity of the Wilson's disease protein. J Biol Chem, 278, 32212-8(2003) (Pubitemid 37048413)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 32212-32218
    • Huster, D.1    Lutsenko, S.2
  • 124
    • 0032471911 scopus 로고    scopus 로고
    • Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant?
    • DOI 10.1086/302163
    • Forbes, J. R. & D. W. Cox: Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant? Am J Hum Genet, 63, 1663-74(1998) (Pubitemid 30415729)
    • (1998) American Journal of Human Genetics , vol.63 , Issue.6 , pp. 1663-1674
    • Forbes, J.R.1    Cox, D.W.2
  • 125
    • 36448983237 scopus 로고    scopus 로고
    • Molecular pathogenesis of Wilson and Menkes disease: Correlation of mutations with molecular defects and disease phenotypes
    • DOI 10.1136/jmg.2007.052746
    • de Bie, P., P. Muller, C. Wijmenga & L. W. Klomp: Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes. J Med Genet, 44, 673-88(2007) (Pubitemid 350161581)
    • (2007) Journal of Medical Genetics , vol.44 , Issue.11 , pp. 673-688
    • De Bie, P.1    Muller, P.2    Wijmenga, C.3    Klomp, L.W.J.4
  • 126
    • 34447092712 scopus 로고    scopus 로고
    • Biochemical basis of regulation of human copper-transporting ATPases
    • DOI 10.1016/j.abb.2007.04.013, PII S0003986107002020
    • Lutsenko, S., E. S. LeShane & U. Shinde: Biochemical basis of regulation of human coppertransporting ATPases. Arch Biochem Biophys, 463, 134-48(2007) (Pubitemid 47030341)
    • (2007) Archives of Biochemistry and Biophysics , vol.463 , Issue.2 , pp. 134-148
    • Lutsenko, S.1    LeShane, E.S.2    Shinde, U.3
  • 128
    • 0035958909 scopus 로고    scopus 로고
    • The regulation of catalytic activity of the menkes coppertranslocating P-type ATPase. Role of high affinity copperbinding sites
    • Voskoboinik, I., J. Mar, D. Strausak & J. Camakaris: The regulation of catalytic activity of the menkes coppertranslocating P-type ATPase. Role of high affinity copperbinding sites. J Biol Chem, 276, 28620-7(2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 28620-28627
    • Voskoboinik, I.1    Mar, J.2    Strausak, D.3    Camakaris, J.4
  • 129
    • 33846311441 scopus 로고    scopus 로고
    • Copper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B)
    • DOI 10.1042/BJ20061055
    • Cater, M. A., S. la Fontaine & J. F. Mercer: Copper binding to the N-terminal metal-binding sites or the CPC motif is not essential for copper-induced trafficking of the human Wilson protein (ATP7B). Biochem J, 401, 143-53(2007) (Pubitemid 46114608)
    • (2007) Biochemical Journal , vol.401 , Issue.1 , pp. 143-153
    • Cater, M.A.1    La Fontaine, S.2    Mercer, J.F.B.3
  • 130
    • 4344703330 scopus 로고    scopus 로고
    • Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: Location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations
    • DOI 10.1042/BJ20040326
    • Efremov, R. G., Y. A. Kosinsky, D. E. Nolde, R. Tsivkovskii, A. S. Arseniev & S. Lutsenko: Molecular modelling of the nucleotide-binding domain of Wilson's disease protein: location of the ATP-binding site, domain dynamics and potential effects of the major disease mutations. Biochem J, 382, 293-305(2004) (Pubitemid 39141593)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 293-305
    • Efremov, R.G.1    Kosinsky, Y.A.2    Nolde, D.E.3    Tsivkovskii, R.4    Arseniev, A.S.5    Lutsenko, S.6
  • 131
    • 33645754710 scopus 로고    scopus 로고
    • Solution structure of the N-domain of Wilson disease protein: Distinct nucleotide-binding environment and effects of disease mutations
    • Dmitriev, O., R. Tsivkovskii, F. Abildgaard, C. T. Morgan, J. L. Markley & S. Lutsenko: Solution structure of the N-domain of Wilson disease protein: distinct nucleotide-binding environment and effects of disease mutations. Proc Natl Acad Sci U S A, 103, 5302-7(2006)
    • (2006) Proc. Natl. Acad. Sci. U S A , vol.103 , pp. 5302-5307
    • Dmitriev, O.1    Tsivkovskii, R.2    Abildgaard, F.3    Morgan, C.T.4    Markley, J.L.5    Lutsenko, S.6
  • 132
    • 0037059855 scopus 로고    scopus 로고
    • Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells
    • DOI 10.1074/jbc.M109368200
    • Tsivkovskii, R., J. F. Eisses, J. H. Kaplan & S. Lutsenko: Functional properties of the copper-transporting ATPase ATP7B (the Wilson's disease protein) expressed in insect cells. J Biol Chem, 277, 976-83(2002) (Pubitemid 34968842)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.2 , pp. 976-983
    • Tsivkovskii, R.1    Eisses, J.F.2    Kaplan, J.H.3    Lutsenko, S.4
  • 133
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • DOI 10.1152/physrev.00004.2006
    • Lutsenko, S., N. L. Barnes, M. Y. Bartee & O. Y. Dmitriev: Function and regulation of human coppertransporting ATPases. Physiol Rev, 87, 1011-46(2007) (Pubitemid 47084675)
    • (2007) Physiological Reviews , vol.87 , Issue.3 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 136
    • 0028916866 scopus 로고
    • Identification of an ATP-dependent copper transport system in endoplasmic reticulum vesicles isolated from rat liver
    • Bingham, M. J., A. Burchell & H. J. McArdle: Identification of an ATP-dependent copper transport system in endoplasmic reticulum vesicles isolated from rat liver. J Physiol, 482(Pt 3), 583-7(1995)
    • (1995) J. Physiol. , vol.482 , Issue.3 PART , pp. 583-587
    • Bingham, M.J.1    Burchell, A.2    McArdle, H.J.3
  • 137
    • 33846482550 scopus 로고    scopus 로고
    • Purification and membrane reconstitution of catalytically active Menkes copper-transporting P-type ATPase (MNK; ATP7A)
    • DOI 10.1042/BJ20060924
    • Hung, Y. H., M. J. Layton, I. Voskoboinik, J. F. Mercer & J. Camakaris: Purification and membrane reconstitution of catalytically active Menkes copper-transporting P-type ATPase (MNK; ATP7A). Biochem J, 401, 569-79(2007) (Pubitemid 46166438)
    • (2007) Biochemical Journal , vol.401 , Issue.2 , pp. 569-579
    • Hung, Y.H.1    Layton, M.J.2    Voskoboinik, I.3    Mercer, J.F.B.4    Camakaris, J.5
  • 138
    • 15744392287 scopus 로고    scopus 로고
    • The copper-transporting ATPases, Menkes and Wilson disease proteins, have distinct roles in adult and developing cerebellum
    • DOI 10.1074/jbc.M413840200
    • Barnes, N., R. Tsivkovskii, N. Tsivkovskaia & S. Lutsenko: The copper-transporting ATPases, menkes and wilson disease proteins, have distinct roles in adult and developing cerebellum. J Biol Chem, 280, 9640-5(2005) (Pubitemid 40409661)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9640-9645
    • Barnes, N.1    Tsivkovskii, R.2    Tsivkovskaia, N.3    Lutsenko, S.4
  • 139
    • 33644919107 scopus 로고    scopus 로고
    • Essential role for the Menkes ATPase in activation of extracellular superoxide dismutase: Implication for vascular oxidative stress
    • DOI 10.1096/fj.05-4564fje
    • Qin, Z., S. Itoh, V. Jeney, M. Ushio-Fukai & T. Fukai: Essential role for the Menkes ATPase in activation of extracellular superoxide dismutase: implication for vascular oxidative stress. Faseb J, 20, 334-6(2006) (Pubitemid 46671162)
    • (2006) FASEB Journal , vol.20 , Issue.2 , pp. 334-336
    • Qin, Z.1    Itoh, S.2    Jeney, V.3    Ushio-Fukai, M.4    Fukai, T.5
  • 140
    • 17644375510 scopus 로고    scopus 로고
    • Role of antioxidant-1 in extracellular superoxide dismutase function and expression
    • DOI 10.1161/01.RES.0000162001.57896.66
    • Jeney, V., S. Itoh, M. Wendt, Q. Gradek, M. Ushio-Fukai, D. G. Harrison & T. Fukai: Role of antioxidant-1 in extracellular superoxide dismutase function and expression. Circ Res, 96, 723-9(2005) (Pubitemid 40559511)
    • (2005) Circulation Research , vol.96 , Issue.7 , pp. 723-729
    • Jeney, V.1    Itoh, S.2    Wendt, M.3    Gradek, Q.4    Ushio-Fukai, M.5    Harrison, D.G.6    Fukai, T.7
  • 141
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris, M. J., J. F. Mercer, J. G. Culvenor, P. Lockhart, P. A. Gleeson & J. Camakaris: Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. Embo J, 15, 6084-95(1996) (Pubitemid 26397881)
    • (1996) EMBO Journal , vol.15 , Issue.22 , pp. 6084-6095
    • Petris, M.J.1    Mercer, J.F.B.2    Culvenor, J.G.3    Lockhart, P.4    Gleeson, P.A.5    Camakaris, J.6
  • 142
    • 0032920935 scopus 로고    scopus 로고
    • Hepatocyte-specific localization and copperdependent trafficking of the Wilson's disease protein in the liver
    • Schaefer, M., R. G. Hopkins, M. L. Failla & J. D. Gitlin: Hepatocyte-specific localization and copperdependent trafficking of the Wilson's disease protein in the liver. Am J Physiol, 276, G639-46 (1999)
    • (1999) Am. J. Physiol. , vol.276
    • Schaefer, M.1    Hopkins, R.G.2    Failla, M.L.3    Gitlin, J.D.4
  • 143
    • 0033862878 scopus 로고    scopus 로고
    • Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion
    • Roelofsen, H., H. Wolters, M. J. Van Luyn, N. Miura, F. Kuipers & R. J. Vonk: Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion. Gastroenterology, 119, 782-93(2000)
    • (2000) Gastroenterology , vol.119 , pp. 782-793
    • Roelofsen, H.1    Wolters, H.2    Van Luyn, M.J.3    Miura, N.4    Kuipers, F.5    Vonk, R.J.6
  • 144
    • 12144257164 scopus 로고    scopus 로고
    • NMDA receptor activation mediates copper homeostasis in hippocampal neurons
    • DOI 10.1523/JNEUROSCI.3699-04.2005
    • Schlief, M. L., A. M. Craig & J. D. Gitlin: NMDA receptor activation mediates copper homeostasis in hippocampal neurons. J Neurosci, 25, 239-46(2005) (Pubitemid 40110786)
    • (2005) Journal of Neuroscience , vol.25 , Issue.1 , pp. 239-246
    • Schlief, M.L.1    Craig, A.M.2    Gitlin, J.D.3
  • 145
    • 34249794279 scopus 로고    scopus 로고
    • New Insights into Membrane Trafficking and Protein Sorting
    • DOI 10.1016/S0074-7696(07)61002-X, PII S007476960761002X, A Survey of Cell Biology
    • Derby, M. C. & P. A. Gleeson: New insights into membrane trafficking and protein sorting. Int Rev Cytol, 261, 47-116(2007) (Pubitemid 46856617)
    • (2007) International Review of Cytology , vol.261 , pp. 47-116
    • Derby, M.C.1    Gleeson, P.A.2
  • 147
    • 0032816204 scopus 로고    scopus 로고
    • Characterization of the Menkes protein copper-binding domains and their role in copper-induced protein relocalization
    • DOI 10.1093/hmg/8.8.1473
    • Goodyer, I. D., E. E. Jones, A. P. Monaco & M. J. Francis: Characterization of the Menkes protein copperbinding domains and their role in copper-induced protein relocalization. Hum Mol Genet, 8, 1473-8(1999) (Pubitemid 29374080)
    • (1999) Human Molecular Genetics , vol.8 , Issue.8 , pp. 1473-1478
    • Goodyer, I.D.1    Jones, E.E.2    Monaco, A.P.3    Francis, M.J.4
  • 148
    • 0033574576 scopus 로고    scopus 로고
    • The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein
    • Strausak, D., S. la Fontaine, J. Hill, S. D. Firth, P. J. Lockhart & J. F. Mercer: The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein. J Biol Chem, 274, 11170-7(1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 11170-11177
    • Strausak, D.1    La Fontaine, S.2    Hill, J.3    Firth, S.D.4    Lockhart, P.J.5    Mercer, J.F.6
  • 149
    • 21344439799 scopus 로고    scopus 로고
    • Sortilin is essential and sufficient for the formation of glut4 storage vesicles in 3T3-L1 adipocytes
    • DOI 10.1016/j.devcel.2005.04.004, PII S1534580705001358
    • Shi, J. & K. V. Kandror: Sortilin is essential and sufficient for the formation of Glut4 storage vesicles in 3T3-L1 adipocytes. Dev Cell, 9, 99-108(2005) (Pubitemid 40903663)
    • (2005) Developmental Cell , vol.9 , Issue.1 , pp. 99-108
    • Shi, J.1    Kandror, K.V.2
  • 151
    • 27444439298 scopus 로고    scopus 로고
    • NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells
    • Guo, Y., L. Nyasae, L. T. Braiterman & A. L. Hubbard: NH2-terminal signals in ATP7B Cu-ATPase mediate its Cu-dependent anterograde traffic in polarized hepatic cells. Am J Physiol Gastrointest Liver Physiol, 289, G904-16 (2005)
    • (2005) Am. J. Physiol. Gastrointest Liver Physiol. , vol.289
    • Guo, Y.1    Nyasae, L.2    Braiterman, L.T.3    Hubbard, A.L.4
  • 152
    • 0031730641 scopus 로고    scopus 로고
    • A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network
    • Petris, M. J., J. Camakaris, M. Greenough, S. LaFontaine & J. F. Mercer: A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum Mol Genet, 7, 2063-71(1998) (Pubitemid 28546415)
    • (1998) Human Molecular Genetics , vol.7 , Issue.13 , pp. 2063-2071
    • Petris, M.J.1    Camakaris, J.2    Greenough, M.3    LaFontaine, S.4    Mercer, J.F.B.5
  • 153
    • 0742286873 scopus 로고    scopus 로고
    • Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK): Endocytosis of the Menkes protein
    • DOI 10.1023/A:1024413631537
    • Lane, C., M. J. Petris, A. Benmerah, M. Greenough & J. Camakaris: Studies on endocytic mechanisms of the Menkes copper-translocating P-type ATPase (ATP7A; MNK). Endocytosis of the Menkes protein. Biometals, 17, 87-98(2004) (Pubitemid 38161093)
    • (2004) BioMetals , vol.17 , Issue.1 , pp. 87-98
    • Lane, C.1    Petris, M.J.2    Benmerah, A.3    Greenough, M.4    Camakaris, J.5
  • 154
    • 0014861744 scopus 로고
    • The uptake of Hg203, Cu64, Mn52, and Pb212 by the intestinal wall of the duodenal and ileal segment in vitro
    • Cikrt, M.: The uptake of Hg203, Cu64, Mn52, and Pb212 by the intestinal wall of the duodenal and ileal segment in vitro. Int Z Klin Pharmakol Ther Toxikol, 4, 351-7(1970)
    • (1970) Int. Z. Klin. Pharmakol Ther. Toxikol , vol.4 , pp. 351-357
    • Cikrt, M.1
  • 155
    • 0016581495 scopus 로고
    • Studies on the nature of complexes formed by copper with human alimentary secretions and their influence on copper absorption in the rat
    • Gollan, G. L.: Studies on the nature of complexes formed by copper with human alimentary secretions and their influence on copper absorption in the rat. Clin Sci Mol Med, 49, 237-45(1975)
    • (1975) Clin. Sci. Mol. Med. , vol.49 , pp. 237-245
    • Gollan, G.L.1
  • 157
    • 0036525717 scopus 로고    scopus 로고
    • Molecular mechanisms of copper uptake and distribution
    • DOI 10.1016/S1367-5931(02)00298-3
    • Puig, S. & D. J. Thiele: Molecular mechanisms of copper uptake and distribution. Curr Opin Chem Biol, 6, 171-80(2002) (Pubitemid 34251372)
    • (2002) Current Opinion in Chemical Biology , vol.6 , Issue.2 , pp. 171-180
    • Puig, S.1    Thiele, D.J.2
  • 159
    • 33747179250 scopus 로고    scopus 로고
    • The Steap proteins are metalloreductases
    • DOI 10.1182/blood-2006-02-003681
    • Ohgami, R. S., D. R. Campagna, A. McDonald & M. D. Fleming: The Steap proteins are metalloreductases. Blood, 108, 1388-94(2006) (Pubitemid 44232042)
    • (2006) Blood , vol.108 , Issue.4 , pp. 1388-1394
    • Ohgami, R.S.1    Campagna, D.R.2    McDonald, A.3    Fleming, M.D.4
  • 162
    • 34548813087 scopus 로고    scopus 로고
    • Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: Implications for copper homeostasis
    • DOI 10.1074/jbc.M702653200
    • Zimnicka, A. M., E. B. Maryon & J. H. Kaplan: Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: implications for copper homeostasis. J Biol Chem, 282, 26471-80(2007) (Pubitemid 47443790)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.36 , pp. 26471-26480
    • Zimnicka, A.M.1    Maryon, E.B.2    Kaplan, J.H.3
  • 165
    • 33745807183 scopus 로고    scopus 로고
    • Gene chip analyses reveal differential genetic responses to iron deficiency in rat duodenum and jejunum
    • Collins, J. F.: Gene chip analyses reveal differential genetic responses to iron deficiency in rat duodenum and jejunum. Biol Res, 39, 25-37(2006) (Pubitemid 44027643)
    • (2006) Biological Research , vol.39 , Issue.1 , pp. 25-37
    • Collins, J.F.1
  • 167
    • 16244364384 scopus 로고    scopus 로고
    • ATP-driven copper transport across the intestinal brush border membrane
    • DOI 10.1016/j.bbrc.2005.03.023
    • Knopfel, M., C. Smith & M. Solioz: ATP-driven copper transport across the intestinal brush border membrane. Biochem Biophys Res Commun, 330, 645-52(2005) (Pubitemid 40462136)
    • (2005) Biochemical and Biophysical Research Communications , vol.330 , Issue.3 , pp. 645-652
    • Knopfel, M.1    Smith, C.2    Solioz, M.3
  • 168
    • 0014653410 scopus 로고
    • The absorption of ionic, biliary, and plasma radiocopper in neonatal rats
    • Mistilis, S. P. & P. T. Mearrick: The absorption of ionic, biliary, and plasma radiocopper in neonatal rats. Scand J Gastroenterol, 4, 691-6(1969)
    • (1969) Scand. J. Gastroenterol. , vol.4 , pp. 691-696
    • Mistilis, S.P.1    Mearrick, P.T.2
  • 169
    • 0018791656 scopus 로고
    • Copper metabolism in mottled mouse mutants: Distribution of 64Cu in brindled (Mobr) mice
    • Mann, J. R., J. Camakaris & D. M. Danks: Copper metabolism in mottled mouse mutants: distribution of 64Cu in brindled (Mobr) mice. Biochem J, 180, 613-9(1979)
    • (1979) Biochem. J. , vol.180 , pp. 613-619
    • Mann, J.R.1    Camakaris, J.2    Danks, D.M.3
  • 170
    • 0032909207 scopus 로고    scopus 로고
    • Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
    • DOI 10.1038/5979
    • Vulpe, C. D., Y. M. Kuo, T. L. Murphy, L. Cowley, C. Askwith, N. Libina, J. Gitschier & G. J. Anderson: Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse. Nat Genet, 21, 195-9(1999) (Pubitemid 29070366)
    • (1999) Nature Genetics , vol.21 , Issue.2 , pp. 195-199
    • Vulpe, C.D.1    Kuo, Y.-M.2    Murphy, T.L.3    Cowley, L.4    Askwith, C.5    Libina, N.6    Gitschier, J.7    Anderson, G.I.8
  • 171
    • 2942588454 scopus 로고    scopus 로고
    • Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin
    • DOI 10.1074/jbc.M401151200
    • Nittis, T. & J. D. Gitlin: Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin. J Biol Chem, 279, 25696-702(2004) (Pubitemid 38756833)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.24 , pp. 25696-25702
    • Nittis, T.1    Gitlin, J.D.2
  • 172
    • 27744473039 scopus 로고    scopus 로고
    • Menkes Copper ATPase (Atp7a) is a novel metal-responsive gene in rat duodenum, and immunoreactive protein is present on brush-border and basolateral membrane domains
    • DOI 10.1074/jbc.M506727200
    • Ravia, J. J., R. M. Stephen, F. K. Ghishan & J. F. Collins: Menkes Copper ATPase (Atp7a) is a novel metalresponsive gene in rat duodenum, and immunoreactive protein is present on brush-border and basolateral membrane domains. J Biol Chem, 280, 36221-7(2005) (Pubitemid 41633894)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 36221-36227
    • Ravia, J.J.1    Stephen, R.M.2    Ghishan, F.K.3    Collins, J.F.4
  • 173
    • 34147106917 scopus 로고    scopus 로고
    • Dynamics of endogenous ATP7A (Menkes protein) in intestinal epithelial cells: Copper-dependent redistribution between two intracellular sites
    • DOI 10.1152/ajpgi.00472.2006
    • Nyasae, L., R. Bustos, L. Braiterman, B. Eipper & A. Hubbard: Dynamics of endogenous ATP7A (Menkes protein) in intestinal epithelial cells: copper-dependent redistribution between two intracellular sites. Am J Physiol Gastrointest Liver Physiol, 292, G1181-94 (2007) (Pubitemid 46557793)
    • (2007) American Journal of Physiology - Gastrointestinal and Liver Physiology , vol.292 , Issue.4
    • Nyasae, L.1    Bustos, R.2    Braiterman, L.3    Eipper, B.4    Hubbard, A.5
  • 174
    • 0018650575 scopus 로고
    • Primary biochemical defect in copper metabolism in mice with a recessive X-linked mutation analogous to Menkes' disease in man
    • DOI 10.1016/S0162-0134(00)81002-8
    • Prins, H. W. & C. J. Van den Hamer: Primary biochemical defect in copper metabolism in mice with a recessive X-linked mutation analogous to Menkes' disease in man. J Inorg Biochem, 10, 19-27(1979) (Pubitemid 9247833)
    • (1979) Journal of Inorganic Biochemistry , vol.10 , Issue.1 , pp. 19-27
    • Prins, H.W.1    Van Den Hamer, C.J.A.2
  • 175
    • 0027452091 scopus 로고
    • The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
    • DOI 10.1038/ng1293-327
    • Bull, P. C., G. R. Thomas, J. M. Rommens, J. R. Forbes & D. W. Cox: The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nat Genet, 5, 327-37(1993) (Pubitemid 23351302)
    • (1993) Nature Genetics , vol.5 , Issue.4 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 176
    • 84960996051 scopus 로고
    • Localization of Cu64 in serum fractions following oral administration: An alteration in Wilson's disease
    • Bearn, A. G. & H. G. Kunkel: Localization of Cu64 in serum fractions following oral administration: an alteration in Wilson's disease. Proc Soc Exp Biol Med, 85, 44-8(1954)
    • (1954) Proc. Soc. Exp. Biol. Med. , vol.85 , pp. 44-48
    • Bearn, A.G.1    Kunkel, H.G.2
  • 177
    • 0014078090 scopus 로고
    • The state of copper in human serum: Evidence for an amino acidbound fraction
    • Neumann, P. Z. & A. Sass-Kortsak: The state of copper in human serum: evidence for an amino acidbound fraction. J Clin Invest, 46, 646-58(1967)
    • (1967) J. Clin. Invest. , vol.46 , pp. 646-658
    • Neumann, P.Z.1    Sass-Kortsak, A.2
  • 178
    • 0026610307 scopus 로고
    • 1H NMR studies of reactions of copper complexes with human blood plasma and urine
    • Bligh, S. W., H. A. Boyle, A. B. McEwen, P. J. Sadler & R. H. Woodham: 1H NMR studies of reactions of copper complexes with human blood plasma and urine. Biochem Pharmacol, 43, 137-45(1992)
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 137-145
    • Bligh, S.W.1    Boyle, H.A.2    McEwen, A.B.3    Sadler, P.J.4    Woodham, R.H.5
  • 181
    • 0027968625 scopus 로고
    • Copper transport in the Nagase analbuminemic rat
    • Vargas, E. J., A. R. Shoho & M. C. Linder: Copper transport in the Nagase analbuminemic rat. Am J Physiol, 267, G259-69 (1994)
    • (1994) Am. J. Physiol. , vol.267
    • Vargas, E.J.1    Shoho, A.R.2    Linder, M.C.3
  • 182
    • 0000016319 scopus 로고
    • Turnover of the copper and protein moieties of ceruloplasmin
    • Gitlin, D. & C. A. Janeway: Turnover of the copper and protein moieties of ceruloplasmin. Nature, 185, 693(1960)
    • (1960) Nature , vol.185 , pp. 693
    • Gitlin, D.1    Janeway, C.A.2
  • 184
    • 0021858066 scopus 로고
    • Absorption, transport, and hepatic metabolism of copper and zinc: Special reference to metallothionein and ceruloplasmin
    • Cousins, R. J.: Absorption, transport, and hepatic metabolism of copper and zinc: special reference to metallothionein and ceruloplasmin. Physiol Rev, 65, 238-309(1985) (Pubitemid 15081126)
    • (1985) Physiological Reviews , vol.65 , Issue.2 , pp. 238-309
    • Cousins, R.J.1
  • 185
    • 1242316275 scopus 로고    scopus 로고
    • Functional assessment of the carboxy-terminus of the Wilson disease copper-transporting ATPase, ATP7B
    • DOI 10.1016/j.ygeno.2003.08.022
    • Hsi, G., L. M. Cullen, D. Moira Glerum & D. W. Cox: Functional assessment of the carboxy-terminus of the Wilson disease copper-transporting ATPase, ATP7B. Genomics, 83, 473-81(2004) (Pubitemid 38220852)
    • (2004) Genomics , vol.83 , Issue.3 , pp. 473-481
    • Hsi, G.1    Cullen, L.M.2    Glerum, D.M.3    Cox, D.W.4
  • 186
    • 0242468697 scopus 로고    scopus 로고
    • Functional studies of hephaestin in yeast: Evidence for multicopper oxidase activity in the endocytic pathway
    • DOI 10.1042/BJ20030866
    • Li, L., C. D. Vulpe & J. Kaplan: Functional studies of hephaestin in yeast: evidence for multicopper oxidase activity in the endocytic pathway. Biochem J, 375, 793-8(2003) (Pubitemid 37433530)
    • (2003) Biochemical Journal , vol.375 , Issue.3 , pp. 793-798
    • Li, L.1    Vulpe, C.D.2    Kaplan, J.3
  • 187
    • 0001169569 scopus 로고    scopus 로고
    • The bilogy of human ceruloplasmin
    • A. Messerschmidt, ed. World Scientific Pub Co., Singapore
    • Harris, Z. L., H. Morita & J. D. Gitlin: The bilogy of human ceruloplasmin. In: Multicopper-oxidases (A. Messerschmidt, ed.) World Scientific Pub Co., Singapore 285-305 (1997)
    • (1997) Multicopper-oxidases , pp. 285-305
    • Harris, Z.L.1    Morita, H.2    Gitlin, J.D.3
  • 188
    • 0032758350 scopus 로고    scopus 로고
    • An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates to ceruloplasmin, a multi-copper oxidase in the plasma
    • DOI 10.1007/s007750050380
    • Zaitsev, V. N., I. Zaitseva, M. Papiz & P. F. Lindley: An X-ray crystallographic study of the binding sites of the azide inhibitor and organic substrates to ceruloplasmin, a multi-copper oxidase in the plasma. J Biol Inorg Chem, 4, 579-87(1999) (Pubitemid 29500842)
    • (1999) Journal of Biological Inorganic Chemistry , vol.4 , Issue.5 , pp. 579-587
    • Zaitsev, V.N.1    Zaitseva, I.2    Papiz, M.3    Lindley, P.F.4
  • 189
    • 0015217690 scopus 로고
    • The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase I
    • Osaki, S., D. A. Johnson & E. Frieden: The mobilization of iron from the perfused mammalian liver by a serum copper enzyme, ferroxidase I. J Biol Chem, 246, 3018-23(1971)
    • (1971) J. Biol. Chem. , vol.246 , pp. 3018-3023
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 191
    • 33748889489 scopus 로고    scopus 로고
    • Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice
    • DOI 10.1523/JNEUROSCI.2922-06.2006
    • Jeong, S. Y. & S. David: Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice. J Neurosci, 26, 9810-9(2006) (Pubitemid 44427720)
    • (2006) Journal of Neuroscience , vol.26 , Issue.38 , pp. 9810-9819
    • Suh, Y.J.1    David, S.2
  • 192
    • 0035965212 scopus 로고    scopus 로고
    • Copper transport and metabolism are normal in aceruloplasminemic mice
    • Meyer, L. A., A. P. Durley, J. R. Prohaska & Z. L. Harris: Copper transport and metabolism are normal in aceruloplasminemic mice. J Biol Chem, 276, 36857-61(2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 36857-36861
    • Meyer, L.A.1    Durley, A.P.2    Prohaska, J.R.3    Harris, Z.L.4
  • 193
    • 0037656489 scopus 로고    scopus 로고
    • Genetic defects in copper metabolism
    • Shim, H. & Z. L. Harris: Genetic defects in copper metabolism. J Nutr, 133, 1527S-31S (2003) (Pubitemid 36548740)
    • (2003) Journal of Nutrition , vol.133 , Issue.5 SUPPL. 2
    • Shim, H.1    Harris, Z.L.2
  • 195
    • 0035864917 scopus 로고    scopus 로고
    • Effect of the toxic milk mutation (tx) on the function and intracellular localization of Wnd, the murine homologue of the Wilson copper ATPase
    • La Fontaine, S., M. B. Theophilos, S. D. Firth, R. Gould, R. G. Parton & J. F. Mercer: Effect of the toxic milk mutation (tx) on the function and intracellular localization of Wnd, the murine homologue of the Wilson copper ATPase. Hum Mol Genet, 10, 361-70(2001) (Pubitemid 32166547)
    • (2001) Human Molecular Genetics , vol.10 , Issue.4 , pp. 361-370
    • La Fontaine, S.1    Theophilos, M.B.2    Firth, S.D.3    Gould, R.4    Parton, R.G.5    Mercer, J.F.B.6
  • 198
    • 3042542722 scopus 로고    scopus 로고
    • The subapical compartment: A traffic center in membrane polarity development
    • DOI 10.1242/jcs.01217
    • Hoekstra, D., D. Tyteca & I. S. C. van: The subapical compartment: a traffic center in membrane polarity development. J Cell Sci, 117, 2183-92(2004) (Pubitemid 38807487)
    • (2004) Journal of Cell Science , vol.117 , Issue.11 , pp. 2183-2192
    • Hoekstra, D.1    Tyteca, D.2    Van IJzendoorn, S.C.D.3
  • 199
    • 0028009419 scopus 로고
    • Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome
    • Barroso, M. & E. S. Sztul: Basolateral to apical transcytosis in polarized cells is indirect and involves BFA and trimeric G protein sensitive passage through the apical endosome. J Cell Biol, 124, 83-100(1994) (Pubitemid 24054612)
    • (1994) Journal of Cell Biology , vol.124 , Issue.1-2 , pp. 83-100
    • Barroso, M.1    Sztul, E.S.2
  • 201
    • 33744922690 scopus 로고    scopus 로고
    • Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A
    • DOI 10.1074/jbc.M512745200
    • Lim, C. M., M. A. Cater, J. F. Mercer & S. la Fontaine: Copper-dependent interaction of dynactin subunit p62 with the N terminus of ATP7B but not ATP7A. J Biol Chem, 281, 14006-14(2006) (Pubitemid 43848327)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.20 , pp. 14006-14014
    • Lim, C.M.1    Cater, M.A.2    Mercer, J.F.B.3    La Fontaine, S.4
  • 202
    • 84963072124 scopus 로고
    • Progressive lenticular degeneration: A familial nervous disease associated with cirrhosis of the liver
    • Wilson, S. A. K.: Progressive lenticular degeneration:a familial nervous disease associated with cirrhosis of the liver. Brain, 34, 295(1912)
    • (1912) Brain , vol.34 , pp. 295
    • Wilson, S.A.K.1
  • 203
    • 33846582913 scopus 로고    scopus 로고
    • Wilson's disease
    • DOI 10.1016/S0140-6736(07)60196-2, PII S0140673607601962
    • Ala, A., A. P. Walker, K. Ashkan, J. S. Dooley & M. L. Schilsky: Wilson's disease. Lancet, 369, 397-408(2007) (Pubitemid 46177228)
    • (2007) Lancet , vol.369 , Issue.9559 , pp. 397-408
    • Ala, A.1    Walker, A.P.2    Ashkan, K.3    Dooley, J.S.4    Schilsky, M.L.5
  • 204
    • 34347141569 scopus 로고
    • A histochemical contribution to metal deposition in the Kayser - Fleischer corneal ring
    • Schnabel, R. & G. Nisch: [A histochemical contribution to metal deposition in the Kayser - Fleischer corneal ring.]. Graefes Arch Clin Exp Ophthalmol, 164, 220-30(1961)
    • (1961) Graefes Arch. Clin. Exp. Ophthalmol. , vol.164 , pp. 220-230
    • Schnabel, R.1    Nisch, G.2
  • 205
    • 0005187972 scopus 로고    scopus 로고
    • Biochemical abnormalities in Wilson's disease
    • Bearn, A. G. & H. G. Kunkel: Biochemical abnormalities in Wilson's disease. J Clin Invest, ; 31, 616
    • J. Clin. Invest , vol.31 , pp. 616
    • Bearn, A.G.1    Kunkel, H.G.2
  • 206
    • 0000852301 scopus 로고
    • Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease)
    • Scheinberg, I. H. & D. Gitlin: Deficiency of ceruloplasmin in patients with hepatolenticular degeneration (Wilson's disease). Science, 116, 484-5(1952)
    • (1952) Science , vol.116 , pp. 484-485
    • Scheinberg, I.H.1    Gitlin, D.2
  • 207
    • 0035139204 scopus 로고    scopus 로고
    • The Wilson's disease gene and phenotypic diversity
    • DOI 10.1016/S0168-8278(00)00028-3, PII S0168827800000283
    • Riordan, S. M. & R. Williams: The Wilson's disease gene and phenotypic diversity. J Hepatol, 34, 165-71(2001) (Pubitemid 32102569)
    • (2001) Journal of Hepatology , vol.34 , Issue.1 , pp. 165-171
    • Riordan, S.M.1    Williams, R.2
  • 208
    • 0029353191 scopus 로고
    • Wilson's disease: A new gene and an animal model for an old disease
    • Cuthbert, J. A.: Wilson's disease: a new gene and an animal model for an old disease. J Investig Med, 43, 323-36(1995)
    • (1995) J. Investig Med. , vol.43 , pp. 323-336
    • Cuthbert, J.A.1
  • 210
    • 0014691028 scopus 로고
    • Mobilization of liver iron by ferroxidase (ceruloplasmin)
    • Osaki, S. & D. A. Johnson: Mobilization of liver iron by ferroxidase (ceruloplasmin). J Biol Chem, 244, 5757-8(1969)
    • (1969) J. Biol. Chem. , vol.244 , pp. 5757-5758
    • Osaki, S.1    Johnson, D.A.2
  • 211
  • 212
    • 37049036616 scopus 로고    scopus 로고
    • Sequence variation database for the Wilson disease copper transporter, ATP7B
    • Kenney, S. M. & D. W. Cox: Sequence variation database for the Wilson disease copper transporter, ATP7B. Hum Mutat (2007)
    • (2007) Hum. Mutat
    • Kenney, S.M.1    Cox, D.W.2
  • 214
    • 0034198684 scopus 로고    scopus 로고
    • Wilson's disease-early onset and lessons from a pediatric cohort in India
    • Kalra, V., D. Khurana & R. Mittal: Wilson's disease-early onset and lessons from a pediatric cohort in India. Indian Pediatr, 37, 595-601(2000)
    • (2000) Indian Pediatr. , vol.37 , pp. 595-601
    • Kalra, V.1    Khurana, D.2    Mittal, R.3
  • 215
    • 0038012541 scopus 로고    scopus 로고
    • Modifier genes and protective alleles in humans and mice
    • DOI 10.1016/S0959-437X(03)00061-3
    • Nadeau, J. H.: Modifier genes and protective alleles in humans and mice. Curr Opin Genet Dev, 13, 290-5(2003) (Pubitemid 36645093)
    • (2003) Current Opinion in Genetics and Development , vol.13 , Issue.3 , pp. 290-295
    • Nadeau, J.H.1
  • 216
    • 33747029284 scopus 로고    scopus 로고
    • Regional distribution of mutations of the ATP7B gene in patients with Wilson disease: Impact on genetic testing
    • DOI 10.1007/s00439-006-0202-5
    • Ferenci, P.: Regional distribution of mutations of the ATP7B gene in patients with Wilson disease: impact on genetic testing. Hum Genet, 120, 151-9(2006) (Pubitemid 44204003)
    • (2006) Human Genetics , vol.120 , Issue.2 , pp. 151-159
    • Ferenci, P.1
  • 217
    • 4344689863 scopus 로고    scopus 로고
    • The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: Analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F
    • DOI 10.1074/jbc.M404553200
    • Morgan, C. T., R. Tsivkovskii, Y. A. Kosinsky, R. G. Efremov & S. Lutsenko: The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F. J Biol Chem, 279, 36363-71(2004) (Pubitemid 39128974)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36363-36371
    • Morgan, C.T.1    Tsivkovskii, R.2    Kosinsky, Y.A.3    Efremov, R.G.4    Lutsenko, S.5
  • 218
    • 34548861803 scopus 로고    scopus 로고
    • Distinct Wilson's Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B
    • DOI 10.1053/j.gastro.2007.07.020, PII S001650850701400X
    • de Bie, P., B. van de Sluis, E. Burstein, P. V. van de Berghe, P. Muller, R. Berger, J. D. Gitlin, C. Wijmenga & L. W. Klomp: Distinct Wilson's Disease Mutations in ATP7B Are Associated With Enhanced Binding to COMMD1 and Reduced Stability of ATP7B. Gastroenterology, 133, 1316-26(2007) (Pubitemid 47494457)
    • (2007) Gastroenterology , vol.133 , Issue.4 , pp. 1316-1326
    • De Bie, P.1    Van De Sluis, B.2    Burstein, E.3    Van De Berghe, P.V.E.4    Muller, P.5    Berger, R.6    Gitlin, J.D.7    Wijmenga, C.8    Klomp, L.W.J.9
  • 219
    • 0034641603 scopus 로고    scopus 로고
    • Copper-dependent trafficking of Wilson disease mutant ATP7B proteins
    • Forbes, J. R. & D. W. Cox: Copper-dependent trafficking of Wilson disease mutant ATP7B proteins. Hum Mol Genet, 9, 1927-35(2000) (Pubitemid 30642656)
    • (2000) Human Molecular Genetics , vol.9 , Issue.13 , pp. 1927-1935
    • Forbes, J.R.1    Cox, D.W.2
  • 222
    • 0242690424 scopus 로고    scopus 로고
    • The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis
    • DOI 10.1016/S0168-8278(03)00380-5
    • Klomp, A. E., B. van de Sluis, L. W. Klomp & C. Wijmenga: The ubiquitously expressed MURR1 protein is absent in canine copper toxicosis. J Hepatol, 39, 703-9(2003) (Pubitemid 37372177)
    • (2003) Journal of Hepatology , vol.39 , Issue.5 , pp. 703-709
    • Klomp, A.E.M.1    Van De Sluis, B.2    Klomp, L.W.J.3    Wijmenga, C.4
  • 223
    • 9444288054 scopus 로고    scopus 로고
    • Evaluation of haplotypes associated with copper toxicosis in Bedlington Terriers in Australia
    • DOI 10.2460/ajvr.2004.65.1573
    • Hyun, C., L. T. Lavulo & L. J. Filippich: Evaluation of haplotypes associated with copper toxicosis in Bedlington Terriers in Australia. Am J Vet Res, 65, 1573-9(2004) (Pubitemid 39562002)
    • (2004) American Journal of Veterinary Research , vol.65 , Issue.11 , pp. 1573-1579
    • Hyun, C.1    Lavulo, L.T.2    Filippich, L.J.3
  • 224
    • 0038354720 scopus 로고    scopus 로고
    • New haplotypes in the Bedlington terrier indicate complexity in copper toxicosis
    • DOI 10.1007/s00335-002-2255-3
    • Coronado, V. A., D. Damaraju, R. Kohijoki & D. W. Cox: New haplotypes in the Bedlington terrier indicate complexity in copper toxicosis. Mamm Genome, 14, 483-91(2003) (Pubitemid 36801971)
    • (2003) Mammalian Genome , vol.14 , Issue.7 , pp. 483-491
    • Coronado, V.A.1    Damaraju, D.2    Kohijoki, R.3    Cox, D.W.4
  • 225
    • 0142149219 scopus 로고    scopus 로고
    • The copper toxicosis gene product murr1 directly interacts with the wilson disease protein
    • DOI 10.1074/jbc.C300391200
    • Tao, T. Y., F. Liu, L. Klomp, C. Wijmenga & J. D. Gitlin: The copper toxicosis gene product Murr1 directly interacts with the Wilson disease protein. J Biol Chem, 278, 41593-6(2003) (Pubitemid 37310414)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 41593-41596
    • Tao, T.Y.1    Liu, F.2    Klomp, L.3    Wijmenga, C.4    Gitlin, J.D.5
  • 227
    • 0032878550 scopus 로고    scopus 로고
    • Null mutation of the murine ATP7B (Wilson disease) gene results in intracellular copper accumulation and late-onset hepatic nodular transformation
    • DOI 10.1093/hmg/8.9.1665
    • Buiakova, O. I., J. Xu, S. Lutsenko, S. Zeitlin, K. Das, S. Das, B. M. Ross, C. Mekios, I. H. Scheinberg & T. C. Gilliam: Null mutation of the murine ATP7B (Wilson disease) gene results in intracellular copper accumulation and late-onset hepatic nodular transformation. Hum Mol Genet, 8, 1665-71(1999) (Pubitemid 29423875)
    • (1999) Human Molecular Genetics , vol.8 , Issue.9 , pp. 1665-1671
    • Buiakova, O.I.1    Xu, J.2    Lutsenko, S.3    Zeitlin, S.4    Das, K.5    Das, S.6    Ross, B.M.7    Mekios, C.8    Scheinberg, I.H.9    Gilliam, T.C.10
  • 228
    • 33746497951 scopus 로고    scopus 로고
    • Iron removal by phlebotomy for the prophylaxis of fulminant hepatitis in a Wilson disease model of Long-Evans Cinnamon Rats
    • DOI 10.1016/j.hepres.2006.04.008, PII S1386634606001562
    • Hayashi, H., S. Wakusawa & M. Yano: Iron removal by phlebotomy for the prophylaxis of fulminant hepatitis in a Wilson disease model of Long-Evans Cinnamon Rats. Hepatol Res, 35, 276-80(2006) (Pubitemid 44138485)
    • (2006) Hepatology Research , vol.35 , Issue.4 , pp. 276-280
    • Hayashi, H.1    Wakusawa, S.2    Yano, M.3
  • 229
    • 79959563681 scopus 로고    scopus 로고
    • Withdrawal of penicillamine from zinc sulphate-penicillamine maintenance therapy in Wilson's disease: Promising, safe and cheap
    • Sinha, S. & A. B. Taly: Withdrawal of penicillamine from zinc sulphate-penicillamine maintenance therapy in Wilson's disease: Promising, safe and cheap. J Neurol Sci (2007)
    • (2007) J. Neurol. Sci.
    • Sinha, S.1    Taly, A.B.2
  • 230
    • 34249994839 scopus 로고    scopus 로고
    • Wilson disease-A practical approach to diagnosis, treatment and follow-up
    • DOI 10.1016/j.dld.2006.12.095, PII S1590865807000035
    • Medici, V., L. Rossaro & G. C. Sturniolo: Wilson disease - a practical approach to diagnosis, treatment and follow-up. Dig Liver Dis, 39, 601-9(2007) (Pubitemid 46888204)
    • (2007) Digestive and Liver Disease , vol.39 , Issue.7 , pp. 601-609
    • Medici, V.1    Rossaro, L.2    Sturniolo, G.C.3
  • 231
    • 0015385968 scopus 로고
    • Kinky hair disease
    • Menkes, J. H.: Kinky hair disease. Pediatrics, 50, 181-3(1972)
    • (1972) Pediatrics , vol.50 , pp. 181-183
    • Menkes, J.H.1
  • 233
    • 1042281034 scopus 로고    scopus 로고
    • A comparison of the mutation spectra of Menkes disease and Wilson disease
    • DOI 10.1007/s00439-003-1045-y
    • Hsi, G. & D. W. Cox: A comparison of the mutation spectra of Menkes disease and Wilson disease. Hum Genet, 114, 165-72(2004) (Pubitemid 38195343)
    • (2004) Human Genetics , vol.114 , Issue.2 , pp. 165-172
    • Hsi, G.1    Cox, D.W.2
  • 234
    • 0032917818 scopus 로고    scopus 로고
    • Identification of three novel mutations in the MNK gene in three unrelated Japanese patients with classical Menkes disease
    • DOI 10.1007/s100380050144
    • Ogawa, A., S. Yamamoto, M. Takayanagi, T. Kogo, M. Kanazawa & Y. Kohno: Identification of three novel mutations in the MNK gene in three unrelated Japanese patients with classical Menkes disease. J Hum Genet, 44, 206-9(1999) (Pubitemid 29219910)
    • (1999) Journal of Human Genetics , vol.44 , Issue.3 , pp. 206-209
    • Ogawa, A.1    Yamamoto, S.2    Takayanagi, M.3    Kogo, T.4    Kanazawa, M.5    Kohno, Y.6
  • 235
    • 0019366779 scopus 로고
    • A mild form of Menkes steely hair syndrome
    • DOI 10.1016/S0022-3476(81)80551-3
    • Procopis, P., J. Camakaris & D. M. Danks: A mild form of Menkes steely hair syndrome. J Pediatr, 98, 97-9(1981) (Pubitemid 11184073)
    • (1981) Journal of Pediatrics , vol.98 , Issue.1 , pp. 97-99
    • Procopis, P.1    Camakaris, J.2    Danks, D.M.3
  • 236
    • 0037374848 scopus 로고    scopus 로고
    • A copper treatable Menkes disease mutation associated with defective trafficking of a functional Menkes copper ATPase [1]
    • Kim, B. E., K. Smith & M. J. Petris: A copper treatable Menkes disease mutation associated with defective trafficking of a functional Menkes copper ATPase. J Med Genet, 40, 290-5(2003) (Pubitemid 36506444)
    • (2003) Journal of Medical Genetics , vol.40 , Issue.4 , pp. 290-295
    • Kim, B.-E.1    Smith, K.2    Petris, M.J.3
  • 237
    • 0028017998 scopus 로고
    • Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus
    • DOI 10.1038/ng1094-195
    • Kaler, S. G., L. K. Gallo, V. K. Proud, A. K. Percy, Y. Mark, N. A. Segal, D. S. Goldstein, C. S. Holmes & W. A. Gahl: Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus. Nat Genet, 8, 195-202(1994) (Pubitemid 24308369)
    • (1994) Nature Genetics , vol.8 , Issue.2 , pp. 195-202
    • Kaler, S.G.1    Gallo, L.K.2    Proud, V.K.3    Percy, A.K.4    Mark, Y.5    Segal, N.A.6    Goldstein, D.S.7    Holmes, C.S.8    Gahl, W.A.9
  • 240
    • 0030752983 scopus 로고    scopus 로고
    • Molecular basis of the brindled mouse mutant (Mo(br)): A murine model of Menkes disease
    • DOI 10.1093/hmg/6.7.1037
    • Grimes, A., C. J. Hearn, P. Lockhart, D. F. Newgreen & J. F. Mercer: Molecular basis of the brindled mouse mutant (Mo (br)): a murine model of Menkes disease. Hum Mol Genet, 6, 1037-42(1997) (Pubitemid 27308387)
    • (1997) Human Molecular Genetics , vol.6 , Issue.7 , pp. 1037-1042
    • Grimes, A.1    Hearn, C.J.2    Lockhart, P.3    Newgreen, D.F.4    Mercer, J.F.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.