메뉴 건너뛰기




Volumn 1823, Issue 9, 2012, Pages 1580-1593

Charting the travels of copper in eukaryotes from yeast to mammals

Author keywords

Chaperone; Copper; Homeostasis; Mammal; Transporter; Yeast

Indexed keywords

ATX1 PROTEIN; BACTERIAL PROTEIN; CARRIER PROTEIN; CCC2 PROTEIN; CHAPERONE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; COX17 PROTEIN; CTR PROTEIN; CUPRIC ION; CYTOCHROME C OXIDASE; FERREDOXIN; FRE PROTEIN; GLUTATHIONE; HISTIDINE; IRON; METHIONINE; PLACENTA PROTEIN; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84864300450     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.02.011     Document Type: Review
Times cited : (240)

References (150)
  • 1
    • 27744494790 scopus 로고    scopus 로고
    • Independent metalloregulation of Ace1 and Mac1 in Saccharomyces cerevisiae
    • Keller G., Bird A., Winge D.R. Independent metalloregulation of Ace1 and Mac1 in Saccharomyces cerevisiae. Eukaryot. Cell 2005, 4:1863-1871.
    • (2005) Eukaryot. Cell , vol.4 , pp. 1863-1871
    • Keller, G.1    Bird, A.2    Winge, D.R.3
  • 2
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: homeostatic control of copper uptake and distribution
    • Pena M.M., Lee J., Thiele D.J. A delicate balance: homeostatic control of copper uptake and distribution. J. Nutr. 1999, 129:1251-1260.
    • (1999) J. Nutr. , vol.129 , pp. 1251-1260
    • Pena, M.M.1    Lee, J.2    Thiele, D.J.3
  • 3
    • 1242277806 scopus 로고    scopus 로고
    • Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells
    • Rutherford J.C., Bird A.J. Metal-responsive transcription factors that regulate iron, zinc, and copper homeostasis in eukaryotic cells. Eukaryot. Cell 2004, 3:1-13.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1-13
    • Rutherford, J.C.1    Bird, A.J.2
  • 4
    • 80053303115 scopus 로고    scopus 로고
    • Hammering out details: regulating metal levels in eukaryotes
    • Ehrensberger K.M., Bird A.J. Hammering out details: regulating metal levels in eukaryotes. Trends Biochem. Sci. 2011, 36:524-531.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 524-531
    • Ehrensberger, K.M.1    Bird, A.J.2
  • 5
    • 0038153078 scopus 로고
    • A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering
    • Culotta V.C., Joh H.D., Lin S.J., Slekar K.H., Strain J. A physiological role for Saccharomyces cerevisiae copper/zinc superoxide dismutase in copper buffering. J. Biol. Chem. 1995, 270:29991-29997.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29991-29997
    • Culotta, V.C.1    Joh, H.D.2    Lin, S.J.3    Slekar, K.H.4    Strain, J.5
  • 6
    • 0034644739 scopus 로고    scopus 로고
    • Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays
    • Gross C., Kelleher M., Iyer V.R., Brown P.O., Winge D.R. Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays. J. Biol. Chem. 2000, 275:32310-32316.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32310-32316
    • Gross, C.1    Kelleher, M.2    Iyer, V.R.3    Brown, P.O.4    Winge, D.R.5
  • 7
    • 0030967609 scopus 로고    scopus 로고
    • Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor
    • Graden J.A., Winge D.R. Copper-mediated repression of the activation domain in the yeast Mac1p transcription factor. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:5550-5555.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5550-5555
    • Graden, J.A.1    Winge, D.R.2
  • 8
    • 0032530720 scopus 로고    scopus 로고
    • Identification of a copper-induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae
    • Jensen L.T., Winge D.R. Identification of a copper-induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae. EMBO J. 1998, 17:5400-5408.
    • (1998) EMBO J. , vol.17 , pp. 5400-5408
    • Jensen, L.T.1    Winge, D.R.2
  • 9
    • 0030941339 scopus 로고    scopus 로고
    • Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway
    • Labbe S., Zhu Z., Thiele D.J. Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway. J. Biol. Chem. 1997, 272:15951-15958.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15951-15958
    • Labbe, S.1    Zhu, Z.2    Thiele, D.J.3
  • 10
    • 0032508637 scopus 로고    scopus 로고
    • Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae
    • Martins L.J., Jensen L.T., Simon J.R., Keller G.L., Winge D.R. Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae. J. Biol. Chem. 1998, 273:23716-23721.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23716-23721
    • Martins, L.J.1    Jensen, L.T.2    Simon, J.R.3    Keller, G.L.4    Winge, D.R.5
  • 11
    • 0030757298 scopus 로고    scopus 로고
    • Homeostatic regulation of copper uptake in yeast via direct binding of MAC1 protein to upstream regulatory sequences of FRE1 and CTR1
    • Yamaguchi-Iwai Y., Serpe M., Haile D., Yang W., Kosman D.J., Klausner R.D., Dancis A. Homeostatic regulation of copper uptake in yeast via direct binding of MAC1 protein to upstream regulatory sequences of FRE1 and CTR1. J. Biol. Chem. 1997, 272:17711-17718.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17711-17718
    • Yamaguchi-Iwai, Y.1    Serpe, M.2    Haile, D.3    Yang, W.4    Kosman, D.J.5    Klausner, R.D.6    Dancis, A.7
  • 12
    • 0030924805 scopus 로고    scopus 로고
    • The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator
    • Georgatsou E., Mavrogiannis L.A., Fragiadakis G.S., Alexandraki D. The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator. J. Biol. Chem. 1997, 272:13786-13792.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13786-13792
    • Georgatsou, E.1    Mavrogiannis, L.A.2    Fragiadakis, G.S.3    Alexandraki, D.4
  • 13
    • 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
    • Xiao Z., Loughlin F., George G.N., Howlett G.J., Wedd A.G. 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. J. Am. Chem. Soc. 2004, 126:3081-3090.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3081-3090
    • Xiao, Z.1    Loughlin, F.2    George, G.N.3    Howlett, G.J.4    Wedd, A.G.5
  • 14
    • 79952270577 scopus 로고    scopus 로고
    • The tightly regulated copper window in yeast
    • Wegner S.V., Sun F., Hernandez N., He C. The tightly regulated copper window in yeast. Chem. Commun. 2011, 47:2571-2573.
    • (2011) Chem. Commun. , vol.47 , pp. 2571-2573
    • Wegner, S.V.1    Sun, F.2    Hernandez, N.3    He, C.4
  • 16
    • 58649108110 scopus 로고    scopus 로고
    • Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutase
    • Wood L.K., Thiele D.J. Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutase. J. Biol. Chem. 2009, 284:404-413.
    • (2009) J. Biol. Chem. , vol.284 , pp. 404-413
    • Wood, L.K.1    Thiele, D.J.2
  • 18
    • 0025779301 scopus 로고
    • Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae
    • Zhou P.B., Thiele D.J. Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1991, 88:6112-6116.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 6112-6116
    • Zhou, P.B.1    Thiele, D.J.2
  • 19
    • 0026743186 scopus 로고
    • Expression of a yeast metallothionein gene family is activated by a single metalloregulatory transcription factor
    • Zhou P., Szczypka M.S., Sosinowski T., Thiele D.J. Expression of a yeast metallothionein gene family is activated by a single metalloregulatory transcription factor. Mol. Cell. Biol. 1992, 12:3766-3775.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3766-3775
    • Zhou, P.1    Szczypka, M.S.2    Sosinowski, T.3    Thiele, D.J.4
  • 20
    • 0024615582 scopus 로고
    • A cysteine-rich nuclear protein activates yeast metallothionein gene transcription
    • Szczypka M.S., Thiele D.J. A cysteine-rich nuclear protein activates yeast metallothionein gene transcription. Mol. Cell. Biol. 1989, 9:421-429.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 421-429
    • Szczypka, M.S.1    Thiele, D.J.2
  • 21
    • 0027257306 scopus 로고
    • Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification
    • Zhou P., Thiele D.J. Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification. Genes Dev. 1993, 7:1824-1835.
    • (1993) Genes Dev. , vol.7 , pp. 1824-1835
    • Zhou, P.1    Thiele, D.J.2
  • 22
    • 71749115454 scopus 로고    scopus 로고
    • A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity
    • White C., Lee J., Kambe T., Fritsche K., Petris M.J. A role for the ATP7A copper-transporting ATPase in macrophage bactericidal activity. J. Biol. Chem. 2009, 284:33949-33956.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33949-33956
    • White, C.1    Lee, J.2    Kambe, T.3    Fritsche, K.4    Petris, M.J.5
  • 24
    • 0040437349 scopus 로고    scopus 로고
    • A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe
    • Labbe S., Pena M.M., Fernandes A.R., Thiele D.J. A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe. J. Biol. Chem. 1999, 274:36252-36260.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36252-36260
    • Labbe, S.1    Pena, M.M.2    Fernandes, A.R.3    Thiele, D.J.4
  • 25
    • 0035805543 scopus 로고    scopus 로고
    • The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence
    • Beaudoin J., Labbe S. The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence. J. Biol. Chem. 2001, 276:15472-15480.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15472-15480
    • Beaudoin, J.1    Labbe, S.2
  • 26
    • 11144247945 scopus 로고    scopus 로고
    • Mobilization of intracellular copper stores by the ctr2 vacuolar copper transporter
    • Rees E.M., Lee J., Thiele D.J. Mobilization of intracellular copper stores by the ctr2 vacuolar copper transporter. J. Biol. Chem. 2004, 279:54221-54229.
    • (2004) J. Biol. Chem. , vol.279 , pp. 54221-54229
    • Rees, E.M.1    Lee, J.2    Thiele, D.J.3
  • 29
    • 79960244792 scopus 로고    scopus 로고
    • Regulation of copper homeostasis by Cuf1 associates with its subcellular localization in the pathogenic yeast Cryptococcus neoformans H99
    • Jiang N., Liu X., Yang J., Li Z., Pan J., Zhu X. Regulation of copper homeostasis by Cuf1 associates with its subcellular localization in the pathogenic yeast Cryptococcus neoformans H99. FEMS Yeast Res. 2011, 11:440-448.
    • (2011) FEMS Yeast Res. , vol.11 , pp. 440-448
    • Jiang, N.1    Liu, X.2    Yang, J.3    Li, Z.4    Pan, J.5    Zhu, X.6
  • 30
    • 56549119570 scopus 로고    scopus 로고
    • Turning a hobby into a job: how duplicated genes find new functions
    • Conant G.C., Wolfe K.H. Turning a hobby into a job: how duplicated genes find new functions. Nat. Rev. Genet. 2008, 9:938-950.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 938-950
    • Conant, G.C.1    Wolfe, K.H.2
  • 31
    • 25844471721 scopus 로고    scopus 로고
    • The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species
    • Byrne K.P., Wolfe K.H. The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res. 2005, 15:1456-1461.
    • (2005) Genome Res. , vol.15 , pp. 1456-1461
    • Byrne, K.P.1    Wolfe, K.H.2
  • 32
    • 0030923008 scopus 로고    scopus 로고
    • Characterization of the FET4 protein of yeast. Evidence for a direct role in the transport of iron
    • Dix D., Bridgham J., Broderius M., Eide D. Characterization of the FET4 protein of yeast. Evidence for a direct role in the transport of iron. J. Biol. Chem. 1997, 272:11770-11777.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11770-11777
    • Dix, D.1    Bridgham, J.2    Broderius, M.3    Eide, D.4
  • 33
    • 0001726322 scopus 로고    scopus 로고
    • Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene
    • Liu X.F., Supek F., Nelson N., Culotta V.C. Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene. J. Biol. Chem. 1997, 272:11763-11769.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11763-11769
    • Liu, X.F.1    Supek, F.2    Nelson, N.3    Culotta, V.C.4
  • 34
    • 0027500845 scopus 로고
    • MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast
    • Jungmann J., Reins H.A., Lee J., Romeo A., Hassett R., Kosman D., Jentsch S. MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. EMBO J. 1993, 12:5051-5056.
    • (1993) EMBO J. , vol.12 , pp. 5051-5056
    • Jungmann, J.1    Reins, H.A.2    Lee, J.3    Romeo, A.4    Hassett, R.5    Kosman, D.6    Jentsch, S.7
  • 35
    • 34548827087 scopus 로고    scopus 로고
    • Global transcriptional responses of fission and budding yeast to changes in copper and iron levels: a comparative study
    • Rustici G., van Bakel H., Lackner D.H., Holstege F.C., Wijmenga C., Bahler J., Brazma A. Global transcriptional responses of fission and budding yeast to changes in copper and iron levels: a comparative study. Genome Biol. 2007, 8:R73.
    • (2007) Genome Biol. , vol.8
    • Rustici, G.1    van Bakel, H.2    Lackner, D.H.3    Holstege, F.C.4    Wijmenga, C.5    Bahler, J.6    Brazma, A.7
  • 36
    • 0037135627 scopus 로고    scopus 로고
    • Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake
    • Puig S., Lee J., Lau M., Thiele D.J. Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake. J. Biol. Chem. 2002, 277:26021-26030.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26021-26030
    • Puig, S.1    Lee, J.2    Lau, M.3    Thiele, D.J.4
  • 38
    • 0030844529 scopus 로고    scopus 로고
    • HCTR1: a human gene for copper uptake identified by complementation in yeast
    • Zhou B., Gitschier J. hCTR1: a human gene for copper uptake identified by complementation in yeast. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:7481-7486.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 7481-7486
    • Zhou, B.1    Gitschier, J.2
  • 39
    • 77952238147 scopus 로고    scopus 로고
    • Tryptophan scanning analysis of the membrane domain of CTR-copper transporters
    • De Feo C.J., Mootien S., Unger V.M. Tryptophan scanning analysis of the membrane domain of CTR-copper transporters. J. Membr. Biol. 2010, 234:113-123.
    • (2010) J. Membr. Biol. , vol.234 , pp. 113-123
    • De Feo, C.J.1    Mootien, S.2    Unger, V.M.3
  • 40
    • 77957757099 scopus 로고    scopus 로고
    • Copper-dependent trafficking of the Ctr4-Ctr5 copper transporting complex
    • Ioannoni R., Beaudoin J., Mercier A., Labbe S. Copper-dependent trafficking of the Ctr4-Ctr5 copper transporting complex. PLoS One 2010, 5:e11964.
    • (2010) PLoS One , vol.5
    • Ioannoni, R.1    Beaudoin, J.2    Mercier, A.3    Labbe, S.4
  • 41
    • 79953718474 scopus 로고    scopus 로고
    • Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery functions
    • Beaudoin J., Thiele D.J., Labbe S., Puig S. Dissection of the relative contribution of the Schizosaccharomyces pombe Ctr4 and Ctr5 proteins to the copper transport and cell surface delivery functions. Microbiology 2011, 157:1021-1031.
    • (2011) Microbiology , vol.157 , pp. 1021-1031
    • Beaudoin, J.1    Thiele, D.J.2    Labbe, S.3    Puig, S.4
  • 43
    • 0037119369 scopus 로고    scopus 로고
    • Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe
    • Borrelly G.P., Harrison M.D., Robinson A.K., Cox S.G., Robinson N.J., Whitehall S.K. Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe. J. Biol. Chem. 2002, 277:30394-30400.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30394-30400
    • Borrelly, G.P.1    Harrison, M.D.2    Robinson, A.K.3    Cox, S.G.4    Robinson, N.J.5    Whitehall, S.K.6
  • 44
    • 80054711990 scopus 로고    scopus 로고
    • Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system
    • Gross D.P., Burgard C.A., Reddehase S., Leitch J.M., Culotta V.C., Hell K. Mitochondrial Ccs1 contains a structural disulfide bond crucial for the import of this unconventional substrate by the disulfide relay system. Mol. Biol. Cell 2011, 22:3758-3767.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3758-3767
    • Gross, D.P.1    Burgard, C.A.2    Reddehase, S.3    Leitch, J.M.4    Culotta, V.C.5    Hell, K.6
  • 45
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum D.M., Shtanko A., Tzagoloff A. Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J. Biol. Chem. 1996, 271:14504-14509.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 46
    • 1242294474 scopus 로고    scopus 로고
    • Cox17 is functional when tethered to the mitochondrial inner membrane
    • Maxfield A.B., Heaton D.N., Winge D.R. Cox17 is functional when tethered to the mitochondrial inner membrane. J. Biol. Chem. 2004, 279:5072-5080.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5072-5080
    • Maxfield, A.B.1    Heaton, D.N.2    Winge, D.R.3
  • 48
    • 80052403741 scopus 로고    scopus 로고
    • Transition metal homeostasis: from yeast to human disease
    • Bleackley M.R., Macgillivray R.T. Transition metal homeostasis: from yeast to human disease. Biometals 2011, 24:785-809.
    • (2011) Biometals , vol.24 , pp. 785-809
    • Bleackley, M.R.1    Macgillivray, R.T.2
  • 49
    • 0030910597 scopus 로고    scopus 로고
    • A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport
    • Lin S.J., Pufahl R.A., Dancis A., O'Halloran T.V., Culotta V.C. A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 1997, 272:9215-9220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9215-9220
    • Lin, S.J.1    Pufahl, R.A.2    Dancis, A.3    O'Halloran, T.V.4    Culotta, V.C.5
  • 50
    • 69949113909 scopus 로고    scopus 로고
    • The right to choose: multiple pathways for activating copper, zinc superoxide dismutase
    • Leitch J.M., Yick P.J., Culotta V.C. The right to choose: multiple pathways for activating copper, zinc superoxide dismutase. J. Biol. Chem. 2009, 284:24679-24683.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24679-24683
    • Leitch, J.M.1    Yick, P.J.2    Culotta, V.C.3
  • 51
    • 0036052119 scopus 로고    scopus 로고
    • An overview on glutathione in Saccharomyces versus non-conventional yeasts
    • Penninckx M.J. An overview on glutathione in Saccharomyces versus non-conventional yeasts. FEMS Yeast Res. 2002, 2:295-305.
    • (2002) FEMS Yeast Res. , vol.2 , pp. 295-305
    • Penninckx, M.J.1
  • 53
    • 55949105820 scopus 로고    scopus 로고
    • Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer
    • Poger D., Fillaux C., Miras R., Crouzy S., Delangle P., Mintz E., Den Auwer C., Ferrand M. Interplay between glutathione, Atx1 and copper: X-ray absorption spectroscopy determination of Cu(I) environment in an Atx1 dimer. J. Biol. Inorg. Chem. 2008, 13:1239-1248.
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 1239-1248
    • Poger, D.1    Fillaux, C.2    Miras, R.3    Crouzy, S.4    Delangle, P.5    Mintz, E.6    Den Auwer, C.7    Ferrand, M.8
  • 54
    • 0030659440 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription
    • Szczypka M.S., Zhu Z., Silar P., Thiele D.J. Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription. Yeast 1997, 13:1423-1435.
    • (1997) Yeast , vol.13 , pp. 1423-1435
    • Szczypka, M.S.1    Zhu, Z.2    Silar, P.3    Thiele, D.J.4
  • 55
    • 4043084194 scopus 로고    scopus 로고
    • A mitochondrial-vacuolar signaling pathway in yeast that affects iron and copper metabolism
    • Li L., Kaplan J. A mitochondrial-vacuolar signaling pathway in yeast that affects iron and copper metabolism. J. Biol. Chem. 2004, 279:33653-33661.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33653-33661
    • Li, L.1    Kaplan, J.2
  • 56
    • 25144499969 scopus 로고    scopus 로고
    • Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism
    • van Bakel H., Strengman E., Wijmenga C., Holstege F.C. Gene expression profiling and phenotype analyses of S. cerevisiae in response to changing copper reveals six genes with new roles in copper and iron metabolism. Physiol. Genomics 2005, 22:356-367.
    • (2005) Physiol. Genomics , vol.22 , pp. 356-367
    • van Bakel, H.1    Strengman, E.2    Wijmenga, C.3    Holstege, F.C.4
  • 57
    • 0034893220 scopus 로고    scopus 로고
    • Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae
    • Portnoy M.E., Schmidt P.J., Rogers R.S., Culotta V.C. Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae. Mol. Genet. Genomics 2001, 265:873-882.
    • (2001) Mol. Genet. Genomics , vol.265 , pp. 873-882
    • Portnoy, M.E.1    Schmidt, P.J.2    Rogers, R.S.3    Culotta, V.C.4
  • 58
    • 0015878963 scopus 로고
    • Copper homeostasis in the mammalian system
    • Evans G.W. Copper homeostasis in the mammalian system. Physiol. Rev. 1973, 53:535-570.
    • (1973) Physiol. Rev. , vol.53 , pp. 535-570
    • Evans, G.W.1
  • 60
    • 0035811069 scopus 로고    scopus 로고
    • The copper transporter CTR1 provides an essential function in mammalian embryonic development
    • Kuo Y.M., Zhou B., Cosco D., Gitschier J. The copper transporter CTR1 provides an essential function in mammalian embryonic development. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:6836-6841.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6836-6841
    • Kuo, Y.M.1    Zhou, B.2    Cosco, D.3    Gitschier, J.4
  • 61
    • 0035811053 scopus 로고    scopus 로고
    • Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development
    • Lee J., Prohaska J.R., Thiele D.J. Essential role for mammalian copper transporter Ctr1 in copper homeostasis and embryonic development. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:6842-6847.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6842-6847
    • Lee, J.1    Prohaska, J.R.2    Thiele, D.J.3
  • 62
    • 0038439210 scopus 로고    scopus 로고
    • Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1
    • Petris M.J., Smith K., Lee J., Thiele D.J. Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1. J. Biol. Chem. 2003, 278:9639-9646.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9639-9646
    • Petris, M.J.1    Smith, K.2    Lee, J.3    Thiele, D.J.4
  • 63
    • 2342444345 scopus 로고    scopus 로고
    • Identification of methionine-rich clusters that regulate copper-stimulated endocytosis of the human Ctr1 copper transporter
    • Guo Y., Smith K., Lee J., Thiele D.J., Petris M.J. Identification of methionine-rich clusters that regulate copper-stimulated endocytosis of the human Ctr1 copper transporter. J. Biol. Chem. 2004, 279:17428-17433.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17428-17433
    • Guo, Y.1    Smith, K.2    Lee, J.3    Thiele, D.J.4    Petris, M.J.5
  • 64
    • 77957771488 scopus 로고    scopus 로고
    • Ctr1 is an apical copper transporter in mammalian intestinal epithelial cells in vivo that is controlled at the level of protein stability
    • Nose Y., Wood L.K., Kim B.E., Prohaska J.R., Fry R.S., Spears J.W., Thiele D.J. Ctr1 is an apical copper transporter in mammalian intestinal epithelial cells in vivo that is controlled at the level of protein stability. J. Biol. Chem. 2010, 285:32385-32392.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32385-32392
    • Nose, Y.1    Wood, L.K.2    Kim, B.E.3    Prohaska, J.R.4    Fry, R.S.5    Spears, J.W.6    Thiele, D.J.7
  • 65
    • 79952157828 scopus 로고    scopus 로고
    • Acquisition of dietary copper: a role for anion transporters in intestinal apical copper uptake
    • Zimnicka A.M., Ivy K., Kaplan J.H. Acquisition of dietary copper: a role for anion transporters in intestinal apical copper uptake. Am. J. Physiol. Cell Physiol. 2011, 300:C588-C599.
    • (2011) Am. J. Physiol. Cell Physiol. , vol.300
    • Zimnicka, A.M.1    Ivy, K.2    Kaplan, J.H.3
  • 66
    • 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
    • Lee J., Petris M.J., Thiele D.J. Characterization of mouse embryonic cells deficient in the ctr1 high affinity copper transporter. Identification of a Ctr1-independent copper transport system. J. Biol. Chem. 2002, 277:40253-40259.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40253-40259
    • Lee, J.1    Petris, M.J.2    Thiele, D.J.3
  • 67
    • 84856731679 scopus 로고    scopus 로고
    • The Human ZIP4 Transporter Has Two Distinct Binding Affinities and Mediates Transport of Multiple Transition Metals
    • Antala S., Dempski R.E. The Human ZIP4 Transporter Has Two Distinct Binding Affinities and Mediates Transport of Multiple Transition Metals. Biochemistry 2012, 51:963-973.
    • (2012) Biochemistry , vol.51 , pp. 963-973
    • Antala, S.1    Dempski, R.E.2
  • 69
    • 38949145276 scopus 로고    scopus 로고
    • M, Ctr2 is partially localized to the plasma membrane and stimulates copper uptake in COS-7 cells
    • Bertinato J., Swist E., Plouffe L.J., Brooks S.P., L'Abbe R. M, Ctr2 is partially localized to the plasma membrane and stimulates copper uptake in COS-7 cells. Biochem. J. 2008, 409:731-740.
    • (2008) Biochem. J. , vol.409 , pp. 731-740
    • Bertinato, J.1    Swist, E.2    Plouffe, L.J.3    Brooks, S.P.4    L'Abbe, R.5
  • 70
    • 78650988648 scopus 로고    scopus 로고
    • M, Copper transporter 2 content is lower in liver and heart of copper-deficient rats
    • Bertinato J., Duval S., L'Abbe R. M, Copper transporter 2 content is lower in liver and heart of copper-deficient rats. Int. J. Mol. Sci. 2010, 11:4741-4749.
    • (2010) Int. J. Mol. Sci. , vol.11 , pp. 4741-4749
    • Bertinato, J.1    Duval, S.2    L'Abbe, R.3
  • 71
    • 78650972288 scopus 로고    scopus 로고
    • Copper transporter 2 regulates endocytosis and controls tumor growth and sensitivity to cisplatin in vivo
    • Blair B.G., Larson C.A., Adams P.L., Abada P.B., Pesce C.E., Safaei R., Howell S.B. Copper transporter 2 regulates endocytosis and controls tumor growth and sensitivity to cisplatin in vivo. Mol. Pharmacol. 2011, 79:157-166.
    • (2011) Mol. Pharmacol. , vol.79 , pp. 157-166
    • Blair, B.G.1    Larson, C.A.2    Adams, P.L.3    Abada, P.B.4    Pesce, C.E.5    Safaei, R.6    Howell, S.B.7
  • 72
    • 0043164959 scopus 로고    scopus 로고
    • Metallochaperone for Cu, Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats
    • Prohaska J.R., Broderius M., Brokate B. Metallochaperone for Cu, Zn-superoxide dismutase (CCS) protein but not mRNA is higher in organs from copper-deficient mice and rats. Arch. Biochem. Biophys. 2003, 417:227-234.
    • (2003) Arch. Biochem. Biophys. , vol.417 , pp. 227-234
    • Prohaska, J.R.1    Broderius, M.2    Brokate, B.3
  • 73
    • 0042317107 scopus 로고    scopus 로고
    • Copper modulates the degradation of copper chaperone for Cu, Zn superoxide dismutase by the 26 S proteosome
    • Bertinato J., L'Abbe M.R. Copper modulates the degradation of copper chaperone for Cu, Zn superoxide dismutase by the 26 S proteosome. J. Biol. Chem. 2003, 278:35071-35078.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35071-35078
    • Bertinato, J.1    L'Abbe, M.R.2
  • 74
    • 33744948516 scopus 로고    scopus 로고
    • Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase
    • Caruano-Yzermans A.L., Bartnikas T.B., Gitlin J.D. Mechanisms of the copper-dependent turnover of the copper chaperone for superoxide dismutase. J. Biol. Chem. 2006, 281:13581-13587.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13581-13587
    • Caruano-Yzermans, A.L.1    Bartnikas, T.B.2    Gitlin, J.D.3
  • 76
    • 0141736847 scopus 로고    scopus 로고
    • Copper, zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase
    • Prohaska J.R., Geissler J., Brokate B., Broderius M. Copper, zinc-superoxide dismutase protein but not mRNA is lower in copper-deficient mice and mice lacking the copper chaperone for superoxide dismutase. Exp. Biol. Med. (Maywood) 2003, 228:959-966.
    • (2003) Exp. Biol. Med. (Maywood) , vol.228 , pp. 959-966
    • Prohaska, J.R.1    Geissler, J.2    Brokate, B.3    Broderius, M.4
  • 78
    • 29244480623 scopus 로고    scopus 로고
    • Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS
    • Jensen L.T., Culotta V.C. Activation of CuZn superoxide dismutases from Caenorhabditis elegans does not require the copper chaperone CCS. J. Biol. Chem. 2005, 280:41373-41379.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41373-41379
    • Jensen, L.T.1    Culotta, V.C.2
  • 83
    • 65649111565 scopus 로고    scopus 로고
    • Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase
    • Oswald C., Krause-Buchholz U., Rodel G. Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase. J. Mol. Biol. 2009, 389:470-479.
    • (2009) J. Mol. Biol. , vol.389 , pp. 470-479
    • Oswald, C.1    Krause-Buchholz, U.2    Rodel, G.3
  • 88
    • 0028358324 scopus 로고
    • The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression
    • Heuchel R., Radtke F., Georgiev O., Stark G., Aguet M., Schaffner W. The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression. EMBO J. 1994, 13:2870-2875.
    • (1994) EMBO J. , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 89
    • 0035927936 scopus 로고    scopus 로고
    • Protective effect of metallothionein against the toxicity of cadmium and other metals(1)
    • Park J.D., Liu Y., Klaassen C.D. Protective effect of metallothionein against the toxicity of cadmium and other metals(1). Toxicology 2001, 163:93-100.
    • (2001) Toxicology , vol.163 , pp. 93-100
    • Park, J.D.1    Liu, Y.2    Klaassen, C.D.3
  • 90
    • 0037081470 scopus 로고    scopus 로고
    • Roles of metallothionein in copper homeostasis: responses to Cu-deficient diets in mice
    • Suzuki K.T., Someya A., Komada Y., Ogra Y. Roles of metallothionein in copper homeostasis: responses to Cu-deficient diets in mice. J. Inorg. Biochem. 2002, 88:173-182.
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 173-182
    • Suzuki, K.T.1    Someya, A.2    Komada, Y.3    Ogra, Y.4
  • 91
    • 33745727740 scopus 로고    scopus 로고
    • Protective role of metallothionein against copper depletion
    • Ogra Y., Aoyama M., Suzuki K.T. Protective role of metallothionein against copper depletion. Arch. Biochem. Biophys. 2006, 451:112-118.
    • (2006) Arch. Biochem. Biophys. , vol.451 , pp. 112-118
    • Ogra, Y.1    Aoyama, M.2    Suzuki, K.T.3
  • 92
    • 79960196460 scopus 로고    scopus 로고
    • Roles of copper chaperone for superoxide dismutase 1 and metallothionein in copper homeostasis
    • Miyayama T., Ishizuka Y., Iijima T., Hiraoka D., Ogra Y. Roles of copper chaperone for superoxide dismutase 1 and metallothionein in copper homeostasis. Metallomics 2011, 3:693-701.
    • (2011) Metallomics , vol.3 , pp. 693-701
    • Miyayama, T.1    Ishizuka, Y.2    Iijima, T.3    Hiraoka, D.4    Ogra, Y.5
  • 93
    • 0031956122 scopus 로고    scopus 로고
    • Association of copper to metallothionein in hepatic lysosomes of Long-Evans cinnamon (LEC) rats during the development of hepatitis [se e comments]
    • Klein D., Lichtmannegger J., Heinzmann U., Muller-Hocker J., Michaelsen S., Summer K.H. Association of copper to metallothionein in hepatic lysosomes of Long-Evans cinnamon (LEC) rats during the development of hepatitis [se e comments]. Eur. J. Clin. Invest. 1998, 28:302-310.
    • (1998) Eur. J. Clin. Invest. , vol.28 , pp. 302-310
    • Klein, D.1    Lichtmannegger, J.2    Heinzmann, U.3    Muller-Hocker, J.4    Michaelsen, S.5    Summer, K.H.6
  • 95
    • 33747849534 scopus 로고    scopus 로고
    • Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function
    • Nose Y., Kim B.E., Thiele D.J. Ctr1 drives intestinal copper absorption and is essential for growth, iron metabolism, and neonatal cardiac function. Cell Metab. 2006, 4:235-244.
    • (2006) Cell Metab. , vol.4 , pp. 235-244
    • Nose, Y.1    Kim, B.E.2    Thiele, D.J.3
  • 96
    • 77953605055 scopus 로고    scopus 로고
    • Effect of glutathione depletion on removal of copper from LEC rat livers by tetrathiomolybdate
    • Ogra Y., Miyayama T., Anan Y. Effect of glutathione depletion on removal of copper from LEC rat livers by tetrathiomolybdate. J. Inorg. Biochem. 2010, 104:858-862.
    • (2010) J. Inorg. Biochem. , vol.104 , pp. 858-862
    • Ogra, Y.1    Miyayama, T.2    Anan, Y.3
  • 98
    • 0035965212 scopus 로고    scopus 로고
    • Copper transport and metabolism are normal in aceruloplasminemic mice
    • Meyer L.A., Durley A.P., Prohaska J.R., Harris Z.L. Copper transport and metabolism are normal in aceruloplasminemic mice. J. Biol. Chem. 2001, 276:36857-36861.
    • (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
  • 99
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris Z.L., Durley A.P., Man T.K., Gitlin J.D. Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:10812-10817.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 100
    • 0014939521 scopus 로고
    • Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma
    • Holtzman N.A., Gaumnitz B.M. Studies on the rate of release and turnover of ceruloplasmin and apoceruloplasmin in rat plasma. J. Biol. Chem. 1970, 245:2354-2358.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2354-2358
    • Holtzman, N.A.1    Gaumnitz, B.M.2
  • 101
    • 79953187664 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-linked ceruloplasmin is expressed in multiple rodent organs and is lower following dietary copper deficiency
    • Mostad E.J., Prohaska J.R. Glycosylphosphatidylinositol-linked ceruloplasmin is expressed in multiple rodent organs and is lower following dietary copper deficiency. Exp. Biol. Med. (Maywood) 2011, 236:298-308.
    • (2011) Exp. Biol. Med. (Maywood) , vol.236 , pp. 298-308
    • Mostad, E.J.1    Prohaska, J.R.2
  • 104
    • 2942588454 scopus 로고    scopus 로고
    • Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin
    • Nittis T., Gitlin J.D. Role of copper in the proteosome-mediated degradation of the multicopper oxidase hephaestin. J. Biol. Chem. 2004, 279:25696-25702.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25696-25702
    • Nittis, T.1    Gitlin, J.D.2
  • 105
    • 11844282820 scopus 로고    scopus 로고
    • Dietary copper deficiency reduces iron absorption and duodenal enterocyte hephaestin protein in male and female rats
    • Reeves P.G., Demars L.C., Johnson W.T., Lukaski H.C. Dietary copper deficiency reduces iron absorption and duodenal enterocyte hephaestin protein in male and female rats. J. Nutr. 2005, 135:92-98.
    • (2005) J. Nutr. , vol.135 , pp. 92-98
    • Reeves, P.G.1    Demars, L.C.2    Johnson, W.T.3    Lukaski, H.C.4
  • 108
  • 109
    • 34147106917 scopus 로고    scopus 로고
    • Dynamics of endogenous ATP7A (Menkes protein) in intestinal epithelial cells: copper-dependent redistribution between two intracellular sites
    • Nyasae L., Bustos R., Braiterman L., Eipper B., Hubbard A. Dynamics of endogenous ATP7A (Menkes protein) in intestinal epithelial cells: copper-dependent redistribution between two intracellular sites. Am. J. Physiol. Gastrointest. Liver Physiol. 2007, 292:G1181-G1194.
    • (2007) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.292
    • Nyasae, L.1    Bustos, R.2    Braiterman, L.3    Eipper, B.4    Hubbard, A.5
  • 110
    • 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
    • Ravia J.J., Stephen R.M., Ghishan F.K., Collins J.F. 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. J. Biol. Chem. 2005, 280:36221-36227.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36221-36227
    • Ravia, J.J.1    Stephen, R.M.2    Ghishan, F.K.3    Collins, J.F.4
  • 111
    • 31544454133 scopus 로고    scopus 로고
    • Copper transport protein (Ctr1) levels in mice are tissue specific and dependent on copper status
    • Kuo Y.M., Gybina A.A., Pyatskowit J.W., Gitschier J., Prohaska J.R. Copper transport protein (Ctr1) levels in mice are tissue specific and dependent on copper status. J. Nutr. 2006, 136:21-26.
    • (2006) J. Nutr. , vol.136 , pp. 21-26
    • Kuo, Y.M.1    Gybina, A.A.2    Pyatskowit, J.W.3    Gitschier, J.4    Prohaska, J.R.5
  • 112
    • 0037063360 scopus 로고    scopus 로고
    • Effects of copper on the expression of metal transporters in human intestinal Caco-2 cells
    • Tennant J., Stansfield M., Yamaji S., Srai S.K., Sharp P. Effects of copper on the expression of metal transporters in human intestinal Caco-2 cells. FEBS Lett. 2002, 527:239-244.
    • (2002) FEBS Lett. , vol.527 , pp. 239-244
    • Tennant, J.1    Stansfield, M.2    Yamaji, S.3    Srai, S.K.4    Sharp, P.5
  • 113
    • 1542618128 scopus 로고    scopus 로고
    • Functional and molecular responses of suckling rat pups and human intestinal Caco-2 cells to copper treatment
    • Bauerly K.A., Kelleher S.L., Lonnerdal B. Functional and molecular responses of suckling rat pups and human intestinal Caco-2 cells to copper treatment. J. Nutr. Biochem. 2004, 15:155-162.
    • (2004) J. Nutr. Biochem. , vol.15 , pp. 155-162
    • Bauerly, K.A.1    Kelleher, S.L.2    Lonnerdal, B.3
  • 114
    • 34548813087 scopus 로고    scopus 로고
    • Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: implications for copper homeostasis
    • Zimnicka A.M., Maryon E.B., Kaplan J.H. Human copper transporter hCTR1 mediates basolateral uptake of copper into enterocytes: implications for copper homeostasis. J. Biol. Chem. 2007, 282:26471-26480.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26471-26480
    • Zimnicka, A.M.1    Maryon, E.B.2    Kaplan, J.H.3
  • 116
    • 84862511003 scopus 로고    scopus 로고
    • Iron, copper, and zinc transport: inhibition of divalent metal transporter 1 (DMT1) and human copper transporter 1 (hCTR1) by shRNA
    • DOI:10.1007/S 12011-011-9243-2 (Electronic publication ahead of print)
    • Espinoza A., Le Blanc S., Olivares M., Pizarro F., Ruz M., Arredondo M. Iron, copper, and zinc transport: inhibition of divalent metal transporter 1 (DMT1) and human copper transporter 1 (hCTR1) by shRNA. Biol. Trace Elem. Res. 2011, DOI:10.1007/S 12011-011-9243-2 (Electronic publication ahead of print).
    • (2011) Biol. Trace Elem. Res.
    • Espinoza, A.1    Le Blanc, S.2    Olivares, M.3    Pizarro, F.4    Ruz, M.5    Arredondo, M.6
  • 119
    • 59449094867 scopus 로고    scopus 로고
    • Deletion of hepatic Ctr1 reveals its function in copper acquisition and compensatory mechanisms for copper homeostasis
    • Kim H., Son H.Y., Bailey S.M., Lee J. Deletion of hepatic Ctr1 reveals its function in copper acquisition and compensatory mechanisms for copper homeostasis. Am. J. Physiol. Gastrointest. Liver Physiol. 2009, 296:G356-G364.
    • (2009) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.296
    • Kim, H.1    Son, H.Y.2    Bailey, S.M.3    Lee, J.4
  • 120
    • 77953851473 scopus 로고    scopus 로고
    • Cardiac copper deficiency activates a systemic signaling mechanism that communicates with the copper acquisition and storage organs
    • Kim B.E., Turski M.L., Nose Y., Casad M., Rockman H.A., Thiele D.J. Cardiac copper deficiency activates a systemic signaling mechanism that communicates with the copper acquisition and storage organs. Cell Metab. 2010, 11:353-363.
    • (2010) Cell Metab. , vol.11 , pp. 353-363
    • Kim, B.E.1    Turski, M.L.2    Nose, Y.3    Casad, M.4    Rockman, H.A.5    Thiele, D.J.6
  • 122
    • 39749157811 scopus 로고    scopus 로고
    • Copper deficient rats and mice both develop anemia but only rats have lower plasma and brain iron levels
    • Pyatskowit J.W., Prohaska J.R. Copper deficient rats and mice both develop anemia but only rats have lower plasma and brain iron levels. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2008, 147:316-323.
    • (2008) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.147 , pp. 316-323
    • Pyatskowit, J.W.1    Prohaska, J.R.2
  • 123
    • 33747891843 scopus 로고    scopus 로고
    • Chronological changes in tissue copper, zinc and iron in the toxic milk mouse and effects of copper loading
    • Allen K.J., Buck N.E., Cheah D.M., Gazeas S., Bhathal P., Mercer J.F. Chronological changes in tissue copper, zinc and iron in the toxic milk mouse and effects of copper loading. Biometals 2006, 19:555-564.
    • (2006) Biometals , vol.19 , pp. 555-564
    • Allen, K.J.1    Buck, N.E.2    Cheah, D.M.3    Gazeas, S.4    Bhathal, P.5    Mercer, J.F.6
  • 124
    • 0014702532 scopus 로고
    • Age-dependent alterations in hepatic subcellular copper distribution and plasma ceruloplasmin
    • Evans G.W., Myron D.R., Cornatzer N.F., Cornatzer W.E. Age-dependent alterations in hepatic subcellular copper distribution and plasma ceruloplasmin. Am. J. Physiol. 1970, 218:298-300.
    • (1970) Am. J. Physiol. , vol.218 , pp. 298-300
    • Evans, G.W.1    Myron, D.R.2    Cornatzer, N.F.3    Cornatzer, W.E.4
  • 125
    • 0037081771 scopus 로고    scopus 로고
    • Identification of a new copper metabolism gene by positional cloning in a purebred dog population
    • van De Sluis B., Rothuizen J., Pearson P.L., van Oost B.A., Wijmenga C. Identification of a new copper metabolism gene by positional cloning in a purebred dog population. Hum. Mol. Genet. 2002, 11:165-173.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 165-173
    • van De Sluis, B.1    Rothuizen, J.2    Pearson, P.L.3    van Oost, B.A.4    Wijmenga, C.5
  • 126
    • 77956507263 scopus 로고    scopus 로고
    • Cu, Zn superoxide dismutase maturation and activity are regulated by COMMD1
    • Vonk W.I., Wijmenga C., Berger R., van de Sluis B., Klomp L.W. Cu, Zn superoxide dismutase maturation and activity are regulated by COMMD1. J. Biol. Chem. 2010, 285:28991-29000.
    • (2010) J. Biol. Chem. , vol.285 , pp. 28991-29000
    • Vonk, W.I.1    Wijmenga, C.2    Berger, R.3    van de Sluis, B.4    Klomp, L.W.5
  • 132
    • 34547782810 scopus 로고    scopus 로고
    • Copper and iron disorders of the brain
    • Madsen E., Gitlin J.D. Copper and iron disorders of the brain. Annu. Rev. Neurosci. 2007, 30:317-337.
    • (2007) Annu. Rev. Neurosci. , vol.30 , pp. 317-337
    • Madsen, E.1    Gitlin, J.D.2
  • 133
    • 41549119144 scopus 로고    scopus 로고
    • Variable response of selected cuproproteins in rat choroid plexus and cerebellum following perinatal copper deficiency
    • Gybina A.A., Prohaska J.R. Variable response of selected cuproproteins in rat choroid plexus and cerebellum following perinatal copper deficiency. Genes Nutr. 2006, 1:51-59.
    • (2006) Genes Nutr. , vol.1 , pp. 51-59
    • Gybina, A.A.1    Prohaska, J.R.2
  • 134
    • 0029930329 scopus 로고    scopus 로고
    • Localization of Menkes gene expression in the mouse brain; its association with neurological manifestations in Menkes model mice
    • Iwase T., Nishimura M., Sugimura H., Igarashi H., Ozawa F., Shinmura K., Suzuki M., Tanaka M., Kino I. Localization of Menkes gene expression in the mouse brain; its association with neurological manifestations in Menkes model mice. Acta Neuropathol. 1996, 91:482-488.
    • (1996) Acta Neuropathol. , vol.91 , pp. 482-488
    • Iwase, T.1    Nishimura, M.2    Sugimura, H.3    Igarashi, H.4    Ozawa, F.5    Shinmura, K.6    Suzuki, M.7    Tanaka, M.8    Kino, I.9
  • 135
    • 33746727678 scopus 로고    scopus 로고
    • Developmental changes in the expression of ATP7A during a critical period in postnatal neurodevelopment
    • Niciu M.J., Ma X.M., El Meskini R., Ronnett G.V., Mains R.E., Eipper B.A. Developmental changes in the expression of ATP7A during a critical period in postnatal neurodevelopment. Neuroscience 2006, 139:947-964.
    • (2006) Neuroscience , vol.139 , pp. 947-964
    • Niciu, M.J.1    Ma, X.M.2    El Meskini, R.3    Ronnett, G.V.4    Mains, R.E.5    Eipper, B.A.6
  • 136
    • 15744392287 scopus 로고    scopus 로고
    • The copper-transporting ATPases, menkes and wilson disease proteins, have distinct roles in adult and developing cerebellum
    • Barnes N., Tsivkovskii R., Tsivkovskaia N., Lutsenko S. The copper-transporting ATPases, menkes and wilson disease proteins, have distinct roles in adult and developing cerebellum. J. Biol. Chem. 2005, 280:9640-9645.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9640-9645
    • Barnes, N.1    Tsivkovskii, R.2    Tsivkovskaia, N.3    Lutsenko, S.4
  • 139
    • 33847410167 scopus 로고    scopus 로고
    • Rodent brain and heart catecholamine levels are altered by different models of copper deficiency
    • Pyatskowit J.W., Prohaska J.R. Rodent brain and heart catecholamine levels are altered by different models of copper deficiency. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 2007, 145:275-281.
    • (2007) Comp. Biochem. Physiol. C Toxicol. Pharmacol. , vol.145 , pp. 275-281
    • Pyatskowit, J.W.1    Prohaska, J.R.2
  • 140
    • 41549159468 scopus 로고    scopus 로고
    • ATP7A transgenic and nontransgenic mice are resistant to high copper exposure
    • Ke B.X., Llanos R.M., Mercer J.F. ATP7A transgenic and nontransgenic mice are resistant to high copper exposure. J. Nutr. 2008, 138:693-697.
    • (2008) J. Nutr. , vol.138 , pp. 693-697
    • Ke, B.X.1    Llanos, R.M.2    Mercer, J.F.3
  • 141
    • 35348953339 scopus 로고    scopus 로고
    • Changes in copper and zinc status and response to dietary copper deficiency in metallothionein-overexpressing transgenic mouse heart
    • Kang Y.J., Jiang Y., Saari J.T. Changes in copper and zinc status and response to dietary copper deficiency in metallothionein-overexpressing transgenic mouse heart. J. Nutr. Biochem. 2007, 18:714-718.
    • (2007) J. Nutr. Biochem. , vol.18 , pp. 714-718
    • Kang, Y.J.1    Jiang, Y.2    Saari, J.T.3
  • 142
    • 33746935661 scopus 로고    scopus 로고
    • Expression, localisation and hormone regulation of the human copper transporter hCTR1 in placenta and choriocarcinoma Jeg-3 cells
    • Hardman B., Manuelpillai U., Wallace E.M., Monty J.F., Kramer D.R., Kuo Y.M., Mercer J.F., Ackland M.L. Expression, localisation and hormone regulation of the human copper transporter hCTR1 in placenta and choriocarcinoma Jeg-3 cells. Placenta 2006, 27:968-977.
    • (2006) Placenta , vol.27 , pp. 968-977
    • Hardman, B.1    Manuelpillai, U.2    Wallace, E.M.3    Monty, J.F.4    Kramer, D.R.5    Kuo, Y.M.6    Mercer, J.F.7    Ackland, M.L.8
  • 145
    • 78650511738 scopus 로고    scopus 로고
    • Differential intracellular localisation of the Menkes and Wilson copper transporting ATPases in the third trimester human placenta
    • Hardman B., Luff S., Ackland M.L. Differential intracellular localisation of the Menkes and Wilson copper transporting ATPases in the third trimester human placenta. Placenta 2011, 32:79-85.
    • (2011) Placenta , vol.32 , pp. 79-85
    • Hardman, B.1    Luff, S.2    Ackland, M.L.3
  • 146
    • 35848954099 scopus 로고    scopus 로고
    • Distinct functional roles for the Menkes and Wilson copper translocating P-type ATPases in human placental cells
    • Hardman B., Michalczyk A., Greenough M., Camakaris J., Mercer J., Ackland L. Distinct functional roles for the Menkes and Wilson copper translocating P-type ATPases in human placental cells. Cell. Physiol. Biochem. 2007, 20:1073-1084.
    • (2007) Cell. Physiol. Biochem. , vol.20 , pp. 1073-1084
    • Hardman, B.1    Michalczyk, A.2    Greenough, M.3    Camakaris, J.4    Mercer, J.5    Ackland, L.6
  • 147
    • 82855172097 scopus 로고    scopus 로고
    • Is the Western diet adequate in copper?
    • Klevay L.M. Is the Western diet adequate in copper?. J. Trace Elem. Med. Biol. 2011, 25:204-212.
    • (2011) J. Trace Elem. Med. Biol. , vol.25 , pp. 204-212
    • Klevay, L.M.1
  • 148
    • 0041672570 scopus 로고    scopus 로고
    • Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation
    • Ganz T. Hepcidin, a key regulator of iron metabolism and mediator of anemia of inflammation. Blood 2003, 102:783-788.
    • (2003) Blood , vol.102 , pp. 783-788
    • Ganz, T.1
  • 149
    • 0038662619 scopus 로고    scopus 로고
    • Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
    • Nemeth E., Valore E.V., Territo M., Schiller G., Lichtenstein A., Ganz T. Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein. Blood 2003, 101:2461-2463.
    • (2003) Blood , vol.101 , pp. 2461-2463
    • Nemeth, E.1    Valore, E.V.2    Territo, M.3    Schiller, G.4    Lichtenstein, A.5    Ganz, T.6
  • 150
    • 2342510407 scopus 로고    scopus 로고
    • IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin
    • Nemeth E., Rivera S., Gabayan V., Keller C., Taudorf S., Pedersen B.K., Ganz T. IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin. J. Clin. Invest. 2004, 113:1271-1276.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1271-1276
    • Nemeth, E.1    Rivera, S.2    Gabayan, V.3    Keller, C.4    Taudorf, S.5    Pedersen, B.K.6    Ganz, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.