메뉴 건너뛰기




Volumn 14, Issue , 2006, Pages 1-36

Molecular mechanisms of copper homeostasis in yeast

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33748913805     PISSN: 16102096     EISSN: 16106970     Source Type: Book Series    
DOI: 10.1007/4735_91     Document Type: Review
Times cited : (4)

References (177)
  • 2
    • 11144235539 scopus 로고    scopus 로고
    • Eukaryotic CTR Copper uptake transporters require two faces of the third transmembrane domain for helix packing, oligomerization, and function
    • Aller SG, Eng ET, De Feo CJ, Unger VM (2004) Eukaryotic CTR Copper uptake transporters require two faces of the third transmembrane domain for helix packing, oligomerization, and function. J Biol Chem 279:53435-53441
    • (2004) J Biol Chem , vol.279 , pp. 53435-53441
    • Aller, S.G.1    Eng, E.T.2    De Feo, C.J.3    Unger, V.M.4
  • 3
    • 0035852814 scopus 로고    scopus 로고
    • Solution structure of the Cu(I) and apo forms of the yeast metallochaperones Atx1
    • Arnesano F, Banci L, Bertini I, Huffman DL, O'Halloran TV (2001) Solution structure of the Cu(I) and apo forms of the yeast metallochaperones Atx1. Biochemistry 40:1528-1539
    • (2001) Biochemistry , vol.40 , pp. 1528-1539
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Huffman, D.L.4    O'Halloran, T.V.5
  • 4
    • 1842450290 scopus 로고    scopus 로고
    • A docking approach to the study of copper trafficking proteins: Interaction between metallochaperones and soluble domains of copper ATPases
    • Arnesano F, Banci L, Bertini I, Bonvin A (2004) A docking approach to the study of copper trafficking proteins: Interaction between metallochaperones and soluble domains of copper ATPases. Structure 12:669-676
    • (2004) Structure , vol.12 , pp. 669-676
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Bonvin, A.4
  • 5
    • 0033529926 scopus 로고    scopus 로고
    • Passage through stationary phase advances replicative aging in Saccharomyces cerevisiae
    • Ashrafi K, Sinclair D, Gordon JI, Guarente L (1999) Passage through stationary phase advances replicative aging in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 96:9100-9105
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9100-9105
    • Ashrafi, K.1    Sinclair, D.2    Gordon, J.I.3    Guarente, L.4
  • 7
    • 0035896548 scopus 로고    scopus 로고
    • Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states
    • Banci L, Bertini I, Ciofi-Baffoni S, Huffman DL, O'Halloran TV (2001) Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states. J Biol Chem 276:8415-8426
    • (2001) J Biol Chem , vol.276 , pp. 8415-8426
    • Banci, L.1    Bertini, I.2    Ciofi-Baffoni, S.3    Huffman, D.L.4    O'Halloran, T.V.5
  • 8
    • 3843110146 scopus 로고    scopus 로고
    • COX23, a homologue of COX17, is required for cytochrome oxidase assembly
    • Barros MH, Johnson A, Tzagoloff A (2004) COX23, a homologue of COX17, is required for cytochrome oxidase assembly. J Biol Chem 279:31943-31947
    • (2004) J Biol Chem , vol.279 , pp. 31943-31947
    • Barros, M.H.1    Johnson, A.2    Tzagoloff, A.3
  • 9
    • 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 (2001) The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1/Amt1-like recognition sequence. J Biol Chem 276:15472-15480
    • (2001) J Biol Chem , vol.276 , pp. 15472-15480
    • Beaudoin, J.1    Labbe, S.2
  • 10
    • 0038529682 scopus 로고    scopus 로고
    • The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors
    • Beaudoin J, Mercier A, Langlois R, Labbe S (2003) The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors. J Biol Chem 278:14565-14577
    • (2003) J Biol Chem , vol.278 , pp. 14565-14577
    • Beaudoin, J.1    Mercier, A.2    Langlois, R.3    Labbe, S.4
  • 11
    • 0031452147 scopus 로고    scopus 로고
    • Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle
    • Beers J, Glerum MD, Tzagoloff A (1997) Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle. J Biol Chem 272:33191-33196
    • (1997) J Biol Chem , vol.272 , pp. 33191-33196
    • Beers, J.1    Glerum, M.D.2    Tzagoloff, A.3
  • 13
    • 0028938278 scopus 로고
    • Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae
    • Bode HP, Dumschat M, Garotti S, Fuhrmann GF (1995) Iron sequestration by the yeast vacuole. A study with vacuolar mutants of Saccharomyces cerevisiae. Eur J Biochem 228:337-342
    • (1995) Eur J Biochem , vol.228 , pp. 337-342
    • Bode, H.P.1    Dumschat, M.2    Garotti, S.3    Fuhrmann, G.F.4
  • 14
    • 0037474301 scopus 로고    scopus 로고
    • The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur
    • Boer VM, de Winde JH, Pronk JT, Piper MD (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. J Biol Chem 278:3265-3274
    • (2003) J Biol Chem , vol.278 , pp. 3265-3274
    • Boer, V.M.1    de Winde, J.H.2    Pronk, J.T.3    Piper, M.D.4
  • 15
    • 1842782787 scopus 로고    scopus 로고
    • Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase
    • Brown NM, Torres AS, Doan PE, O'Halloran TV (2004) Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase. Proc Natl Acad Sci USA 101:5518-5523
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 5518-5523
    • Brown, N.M.1    Torres, A.S.2    Doan, P.E.3    O'Halloran, T.V.4
  • 16
    • 0024435602 scopus 로고
    • The CUP2 gene product, regulator of yeast metallothionein expression, is a copper-activated DNA-binding protein
    • Buchman C, Skroch P, Welch J, Fogel S, Karin M (1989) The CUP2 gene product, regulator of yeast metallothionein expression, is a copper-activated DNA-binding protein. Mol Cell Biol 9:4091-4095
    • (1989) Mol Cell Biol , vol.9 , pp. 4091-4095
    • Buchman, C.1    Skroch, P.2    Welch, J.3    Fogel, S.4    Karin, M.5
  • 17
    • 0038518286 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase within the mitochondrion
    • Carr HS, Winge DR (2003) Assembly of cytochrome c oxidase within the mitochondrion. Acc Chem Res 36:309-316
    • (2003) Acc Chem Res , vol.36 , pp. 309-316
    • Carr, H.S.1    Winge, D.R.2
  • 18
    • 0037163087 scopus 로고    scopus 로고
    • Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I) binding protein
    • Carr HS, George GN, Winge DR (2002) Yeast Cox11, a protein essential for cytochrome c oxidase assembly, is a Cu(I) binding protein. J Biol Chem 277:31237-31242
    • (2002) J Biol Chem , vol.277 , pp. 31237-31242
    • Carr, H.S.1    George, G.N.2    Winge, D.R.3
  • 19
    • 0026094746 scopus 로고
    • Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins
    • Cha JS, Cooksey DA (1991) Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc Natl Acad Sci USA 88:8915-8919
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8915-8919
    • Cha, J.S.1    Cooksey, D.A.2
  • 21
    • 1842739598 scopus 로고    scopus 로고
    • Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix
    • Cobine PA, Ojeda LD, Rigby KM, Winge DR (2004) Yeast contain a non-proteinaceous pool of copper in the mitochondrial matrix. J Biol Chem 279:14447-14455
    • (2004) J Biol Chem , vol.279 , pp. 14447-14455
    • Cobine, P.A.1    Ojeda, L.D.2    Rigby, K.M.3    Winge, D.R.4
  • 22
    • 0032711538 scopus 로고    scopus 로고
    • Disorders of copper transport
    • Cox DW (1999) Disorders of copper transport. Br Med Bull 55:544-555
    • (1999) Br Med Bull , vol.55 , pp. 544-555
    • Cox, D.W.1
  • 23
    • 0027946045 scopus 로고
    • CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae
    • Culotta VC, Howard WR, Liu XF (1994) CRS5 encodes a metallothionein-like protein in Saccharomyces cerevisiae. J Biol Chem 269:25295-25302
    • (1994) J Biol Chem , vol.269 , pp. 25295-25302
    • Culotta, V.C.1    Howard, W.R.2    Liu, X.F.3
  • 26
    • 0028010889 scopus 로고
    • Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport
    • Dancis A, Yuan DS, Haile D, Askwith C, Eide D, Moehle C, Kaplan J, Klausner RD (1994a) Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport. Cell 76:393-402
    • (1994) Cell , vol.76 , pp. 393-402
    • Dancis, A.1    Yuan, D.S.2    Haile, D.3    Askwith, C.4    Eide, D.5    Moehle, C.6    Kaplan, J.7    Klausner, R.D.8
  • 27
    • 0028152451 scopus 로고
    • The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake
    • Dancis A, Haile D, Yuan DS, Klausner RD (1994b) The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J Biol Chem 269:25660-25667
    • (1994) J Biol Chem , vol.269 , pp. 25660-25667
    • Dancis, A.1    Haile, D.2    Yuan, D.S.3    Klausner, R.D.4
  • 28
    • 0032506116 scopus 로고    scopus 로고
    • Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels
    • Davis-Kaplan SR, Askwith CC, Bengtzen AC, Radisky D, Kaplan J (1998) Chloride is an allosteric effector of copper assembly for the yeast multicopper oxidase Fet3p: An unexpected role for intracellular chloride channels. Proc Natl Acad Sci USA 95:13641-13645
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13641-13645
    • Davis-Kaplan, S.R.1    Askwith, C.C.2    Bengtzen, A.C.3    Radisky, D.4    Kaplan, J.5
  • 31
    • 0031050483 scopus 로고    scopus 로고
    • Copper transport and its alterations in Menkes and Wilson diseases
    • DiDonato M, Sarkar B (1997) Copper transport and its alterations in Menkes and Wilson diseases. Biochim Biophys Acta 1360:3-16
    • (1997) Biochim Biophys Acta , vol.1360 , pp. 3-16
    • DiDonato, M.1    Sarkar, B.2
  • 32
    • 0028053806 scopus 로고
    • The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae
    • Dix DR, Bridgham JT, Broderius MA, Byersdorfer CA, Eide DJ (1994) The FET4 gene encodes the low affinity Fe(II) transport protein of Saccharomyces cerevisiae. J Biol Chem 269:26092-260929
    • (1994) J Biol Chem , vol.269 , pp. 26092-260929
    • Dix, D.R.1    Bridgham, J.T.2    Broderius, M.A.3    Byersdorfer, C.A.4    Eide, D.J.5
  • 33
    • 0028911152 scopus 로고
    • Distinct regions of Cu(I) ACE1 contact two spatially resolved DNA major groove sites
    • Dobi A, Dameron CT, Hu S, Hamer D, Winge DR (1995) Distinct regions of Cu(I) ACE1 contact two spatially resolved DNA major groove sites. J Biol Chem 270:10171-10178
    • (1995) J Biol Chem , vol.270 , pp. 10171-10178
    • Dobi, A.1    Dameron, C.T.2    Hu, S.3    Hamer, D.4    Winge, D.R.5
  • 34
    • 0025099548 scopus 로고
    • ACE1 transcription factor produced in Escherichia coli binds multiple regions within yeast metallothionein upstream activation sequences
    • Evans CF, Engelke DR, Thiele DJ (1990) ACE1 transcription factor produced in Escherichia coli binds multiple regions within yeast metallothionein upstream activation sequences. Mol Cell Biol 10:426-429
    • (1990) Mol Cell Biol , vol.10 , pp. 426-429
    • Evans, C.F.1    Engelke, D.R.2    Thiele, D.J.3
  • 35
    • 0030050312 scopus 로고    scopus 로고
    • Identification of the Zn(II) site in the copper-responsive yeast transcription factor, AMT1: A conserved Zn module
    • Farrell RA, Thorvaldsen JL, Winge DR (1996) Identification of the Zn(II) site in the copper-responsive yeast transcription factor, AMT1: A conserved Zn module. Biochemistry 35:1571-1580
    • (1996) Biochemistry , vol.35 , pp. 1571-1580
    • Farrell, R.A.1    Thorvaldsen, J.L.2    Winge, D.R.3
  • 36
    • 0041344579 scopus 로고    scopus 로고
    • Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria
    • Field LS, Furukawa Y, O'Halloran TV, Culotta VC (2003) Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. J Biol Chem 278:28052-28059
    • (2003) J Biol Chem , vol.278 , pp. 28052-28059
    • Field, L.S.1    Furukawa, Y.2    O'Halloran, T.V.3    Culotta, V.C.4
  • 37
    • 0029969718 scopus 로고    scopus 로고
    • Intramembrane bisheme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase
    • Finegold AA, Shatwell KP, Segal AW, Klausner RD, Dancis A (1996) Intramembrane bisheme motif for transmembrane electron transport conserved in a yeast iron reductase and the human NADPH oxidase. J Biol Chem 271:31021-31024
    • (1996) J Biol Chem , vol.271 , pp. 31021-31024
    • Finegold, A.A.1    Shatwell, K.P.2    Segal, A.W.3    Klausner, R.D.4    Dancis, A.5
  • 38
    • 0343299702 scopus 로고
    • Tandem gene amplification mediates copper resistance in yeast
    • Fogel S, Welch JW (1982) Tandem gene amplification mediates copper resistance in yeast. Proc Natl Acad Sci USA 79:5342-5346
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5342-5346
    • Fogel, S.1    Welch, J.W.2
  • 39
    • 0005791294 scopus 로고
    • Cooperative activation of a eukaryotic transcription factor: Interaction between Cu(I) and yeast ACE1 protein
    • Furst P, Hamer D (1989) Cooperative activation of a eukaryotic transcription factor: Interaction between Cu(I) and yeast ACE1 protein. Proc Natl Acad Sci USA 86:5267-5271
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5267-5271
    • Furst, P.1    Hamer, D.2
  • 40
    • 0024291353 scopus 로고
    • Copper activates metallothionein gene transcription by altering the conformation of a specific DNA binding protein
    • Furst P, Hu S, Hackett R, Hamer D (1988) Copper activates metallothionein gene transcription by altering the conformation of a specific DNA binding protein. Cell 55:705-717
    • (1988) Cell , vol.55 , pp. 705-717
    • Furst, P.1    Hu, S.2    Hackett, R.3    Hamer, D.4
  • 41
    • 3543029884 scopus 로고    scopus 로고
    • Oxygen-induced maturation of SOD1: A key role for disulfide formation by the copper chaperone CCS
    • Furukawa Y, Torres AS, O'Halloran TV (2004) Oxygen-induced maturation of SOD1: A key role for disulfide formation by the copper chaperone CCS. EMBO J 23:2872-2881
    • (2004) EMBO J , vol.23 , pp. 2872-2881
    • Furukawa, Y.1    Torres, A.S.2    O'Halloran, T.V.3
  • 43
    • 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 LA, Fragiadakis GS, Alexandraki D (1997) The yeast Fre1p/Fre2p cupric reductases facilitate copper uptake and are regulated by the copper-modulated Mac1p activator. J Biol Chem 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
  • 44
    • 0034117603 scopus 로고    scopus 로고
    • Clinical perspectives on platinum resistance
    • Giaccone G (2000) Clinical perspectives on platinum resistance. Drugs 59 Suppl 4:9-17
    • (2000) Drugs , vol.59 , Issue.SUPPL. 4 , pp. 9-17
    • Giaccone, G.1
  • 45
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum MD, Shtanko A, Tzagoloff A (1996a) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem 271:14504-14509
    • (1996) J Biol Chem , vol.271 , pp. 14504-14509
    • Glerum, M.D.1    Shtanko, A.2    Tzagoloff, A.3
  • 46
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy supressors of mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum MD, Shtanko A, Tzagoloff A (1996b) SCO1 and SCO2 act as high copy supressors of mitochondrial copper recruitment defect in Saccharomyces cerevisiae J Biol Chem 271:20531-20535
    • (1996) J Biol Chem , vol.271 , pp. 20531-20535
    • Glerum, M.D.1    Shtanko, A.2    Tzagoloff, A.3
  • 47
    • 0026046097 scopus 로고
    • ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene
    • Gralla EB, Thiele DJ, Silar P, Valentine JS (1991) ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene. Proc Natl Acad Sci USA 88:8558-8562
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8558-8562
    • Gralla, E.B.1    Thiele, D.J.2    Silar, P.3    Valentine, J.S.4
  • 48
    • 0025098310 scopus 로고
    • Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae
    • Greco MA, Hrab DI, Magner W, Kosman DJ (1990) Cu,Zn superoxide dismutase and copper deprivation and toxicity in Saccharomyces cerevisiae. J Bacteriol 172:317-325
    • (1990) J Bacteriol , vol.172 , pp. 317-325
    • Greco, M.A.1    Hrab, D.I.2    Magner, W.3    Kosman, D.J.4
  • 49
    • 0034644739 scopus 로고    scopus 로고
    • Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays
    • Gross C, Kelleher M, Iyer VR, Brown PO, Winge DR (2000) Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays. J Biol Chem 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
  • 51
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B, Gutteridge JMC (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219:1-114
    • (1984) Biochem J , vol.219 , pp. 1-114
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 52
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • Halliwell B, Gutteridge JM (1990) Role of free radicals and catalytic metal ions in human disease: An overview. Methods Enzymol 186:1-85
    • (1990) Methods Enzymol , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.2
  • 53
    • 0022555879 scopus 로고
    • Metallothionein
    • Hamer DH (1986) Metallothionein. Annu Rev Biochem 55:913-951
    • (1986) Annu Rev Biochem , vol.55 , pp. 913-951
    • Hamer, D.H.1
  • 54
    • 0021839915 scopus 로고
    • Function and autoregulation of yeast copperthionein
    • Hamer DH, Thiele DJ, Lemontt JE (1985) Function and autoregulation of yeast copperthionein. Science 228:685-690
    • (1985) Science , vol.228 , pp. 685-690
    • Hamer, D.H.1    Thiele, D.J.2    Lemontt, J.E.3
  • 55
    • 0024294370 scopus 로고
    • Transcriptional activation by the SV40 AP-1 recognition element in yeast is mediated by a factor similar to AP-1 that is distinct from GCN4
    • Harshman KD, Moyle-Rowley WS, Parker CS (1988) Transcriptional activation by the SV40 AP-1 recognition element in yeast is mediated by a factor similar to AP-1 that is distinct from GCN4. Cell 53:321-330
    • (1988) Cell , vol.53 , pp. 321-330
    • Harshman, K.D.1    Moyle-Rowley, W.S.2    Parker, C.S.3
  • 56
    • 0028799741 scopus 로고
    • Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae
    • Hassett R, Kosman DJ (1995) Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae. J Biol Chem 270:128-134
    • (1995) J Biol Chem , vol.270 , pp. 128-134
    • Hassett, R.1    Kosman, D.J.2
  • 57
    • 0034667662 scopus 로고    scopus 로고
    • The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saccharomyces cerevisiae
    • Hassett R, Dix DR, Eide DJ, Kosman DJ (2000) The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saccharomyces cerevisiae. Biochem J 351:477-484
    • (2000) Biochem J , vol.351 , pp. 477-484
    • Hassett, R.1    Dix, D.R.2    Eide, D.J.3    Kosman, D.J.4
  • 58
    • 0034534913 scopus 로고    scopus 로고
    • Mutational analysis of the mitochondrial copper metallochaperone Cox17
    • Heaton D, Nittis T, Srinivasan C, Winge DR (2001) Mutational analysis of the mitochondrial copper metallochaperone Cox17. J Biol Chem 275:37582-37587
    • (2001) J Biol Chem , vol.275 , pp. 37582-37587
    • Heaton, D.1    Nittis, T.2    Srinivasan, C.3    Winge, D.R.4
  • 59
    • 0035937844 scopus 로고    scopus 로고
    • + coordination-dependent DNA binding of the transcription factor Mac1p in the regulation of copper transport
    • + coordination-dependent DNA binding of the transcription factor Mac1p in the regulation of copper transport. J Biol Chem 276:8793-8797
    • (2001) J Biol Chem , vol.276 , pp. 8793-8797
    • Heredia, J.1    Crooks, M.2    Zhu, Z.3
  • 60
    • 1942439642 scopus 로고    scopus 로고
    • Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins
    • Hettema EH, Valdez-Taubas J, Pelham HR (2004) Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins. EMBO J 23:1279-1288
    • (2004) EMBO J , vol.23 , pp. 1279-1288
    • Hettema, E.H.1    Valdez-Taubas, J.2    Pelham, H.R.3
  • 61
    • 0034614510 scopus 로고    scopus 로고
    • Cox11p is required for stable formation of the CuB and magnesium centers of cytochrome of cytochrome c oxidase
    • Hiser L, Di Valentin M, Hamer AG, Hosler JP (2000) Cox11p is required for stable formation of the CuB and magnesium centers of cytochrome of cytochrome c oxidase. J Biol Chem 275:619-623
    • (2000) J Biol Chem , vol.275 , pp. 619-623
    • Hiser, L.1    Di Valentin, M.2    Hamer, A.G.3    Hosler, J.P.4
  • 62
    • 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
    • Horng YC, Cobine PA, Maxfield AB, Carr HS, Winge DR (2004) Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome c oxidase. J Biol Chem 34:35334-35340
    • (2004) J Biol Chem , vol.34 , pp. 35334-35340
    • Horng, Y.C.1    Cobine, P.A.2    Maxfield, A.B.3    Carr, H.S.4    Winge, D.R.5
  • 63
    • 0025039823 scopus 로고
    • The DNA and Cu binding functions of ACE1 are interdigitated within a single domain
    • Hu S, Furst P, Hamer D (1990) The DNA and Cu binding functions of ACE1 are interdigitated within a single domain. New Biol 2:544-555
    • (1990) New Biol , vol.2 , pp. 544-555
    • Hu, S.1    Furst, P.2    Hamer, D.3
  • 64
    • 0034705616 scopus 로고    scopus 로고
    • Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2
    • Huffman DL, O'Halloran TV (2000) Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2. J Biol Chem 275:18611-18614
    • (2000) J Biol Chem , vol.275 , pp. 18611-18614
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 65
    • 0034913058 scopus 로고    scopus 로고
    • Function, structure, and mechanism of intracellular copper trafficking proteins
    • Huffman DL, O'Halloran TV (2001) Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem 70:677-701
    • (2001) Annu Rev Biochem , vol.70 , pp. 677-701
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 66
    • 2642591795 scopus 로고
    • Copper-induced binding of cellular factors to yeast metallothionein upstream activation sequences
    • Huibregtse JM, Engelke DR, Thiele DJ (1989) Copper-induced binding of cellular factors to yeast metallothionein upstream activation sequences. Proc Natl Acad Sci USA 86:65-69
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 65-69
    • Huibregtse, J.M.1    Engelke, D.R.2    Thiele, D.J.3
  • 67
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung I, Suzuki M, Yamaguchi Y, Yuan DS, Klausner RD, Gitlin JD (1997) Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem 272:21461-21466
    • (1997) J Biol Chem , vol.272 , pp. 21461-21466
    • Hung, I.1    Suzuki, M.2    Yamaguchi, Y.3    Yuan, D.S.4    Klausner, R.D.5    Gitlin, J.D.6
  • 68
    • 0037195066 scopus 로고    scopus 로고
    • Uptake of the anticancer drug cisplatin mediated by the copper transporter Ctr1 in yeast and mammals
    • Ishida S, Lee J, Thiele DJ, Herskowitz I (2002) Uptake of the anticancer drug cisplatin mediated by the copper transporter Ctr1 in yeast and mammals. Proc Natl Acad Sci USA 99:14298-14302
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14298-14302
    • Ishida, S.1    Lee, J.2    Thiele, D.J.3    Herskowitz, I.4
  • 69
    • 0028890031 scopus 로고
    • Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H (1995) Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376:660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 70
    • 0342858798 scopus 로고    scopus 로고
    • Oxidative stress during aging of stationary cultures of the yeast Saccharomyces cerevisiae
    • Jakubowski W, Bilinski T, Bartosz G (2000) Oxidative stress during aging of stationary cultures of the yeast Saccharomyces cerevisiae. Free Radic Biol Med 28:659-664
    • (2000) Free Radic Biol Med , vol.28 , pp. 659-664
    • Jakubowski, W.1    Bilinski, T.2    Bartosz, G.3
  • 72
    • 0032530720 scopus 로고    scopus 로고
    • Identification of a copper-induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae
    • Jensen LT, Winge DR (1998) Identification of a copper-induced intramolecular interaction in the transcription factor Mac1 from Saccharomyces cerevisiae. EMBO J 17:5400-5408
    • (1998) EMBO J , vol.17 , pp. 5400-5408
    • Jensen, L.T.1    Winge, D.R.2
  • 73
    • 0029767918 scopus 로고    scopus 로고
    • Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metallothionein in Saccharomyces cerevisiae
    • Jensen LT, Howard WR, Strain JJ, Winge DR, Culotta VC (1996) Enhanced effectiveness of copper ion buffering by CUP1 metallothionein compared with CRS5 metallothionein in Saccharomyces cerevisiae. J Biol Chem 271:18514-18519
    • (1996) J Biol Chem , vol.271 , pp. 18514-18519
    • Jensen, L.T.1    Howard, W.R.2    Strain, J.J.3    Winge, D.R.4    Culotta, V.C.5
  • 74
    • 0032508586 scopus 로고    scopus 로고
    • Mapping of the DNA binding domain of the copper-responsive transcription factor Mac1 from Saccharomyces cerevisiae
    • Jensen LT, Posewitz MC, Srinivasan C, Winge DR (1998) Mapping of the DNA binding domain of the copper-responsive transcription factor Mac1 from Saccharomyces cerevisiae. J Biol Chem 273:23805-23811
    • (1998) J Biol Chem , vol.273 , pp. 23805-23811
    • Jensen, L.T.1    Posewitz, M.C.2    Srinivasan, C.3    Winge, D.R.4
  • 75
    • 0142180122 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae high affinity phosphate transporter encoded by PHO84 also functions in manganese homeostasis
    • Jensen LT, Ajua-Alemanji M, Culotta VC (2003) The Saccharomyces cerevisiae high affinity phosphate transporter encoded by PHO84 also functions in manganese homeostasis. J Biol Chem 278:42036-42040
    • (2003) J Biol Chem , vol.278 , pp. 42036-42040
    • Jensen, L.T.1    Ajua-Alemanji, M.2    Culotta, V.C.3
  • 76
    • 0032957687 scopus 로고    scopus 로고
    • Evidence for (Mac1p) DNA ternary complex formation in Mac1p-dependent transactivation at the CTR1 promoter
    • Joshi A, Serpe M, Kosman DJ (1999) Evidence for (Mac1p) DNA ternary complex formation in Mac1p-dependent transactivation at the CTR1 promoter. J Biol Chem 274:218-226
    • (1999) J Biol Chem , vol.274 , pp. 218-226
    • Joshi, A.1    Serpe, M.2    Kosman, D.J.3
  • 77
    • 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 HA, Lee J, Romeo A, Hassett R, Kosman D, Jentsch S (1993) MAC1, a nuclear regulatory protein related to Cu-dependent transcription factors is involved in Cu/Fe utilization and stress resistance in yeast. EMBO J 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
  • 78
    • 0028818858 scopus 로고
    • Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue
    • Kampfenkel K, Kushnir S, Babiychuk E, Inze D, Van Montagu M (1995) Molecular characterization of a putative Arabidopsis thaliana copper transporter and its yeast homologue. J Biol Chem 270:28479-28486
    • (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
  • 79
    • 0035914449 scopus 로고    scopus 로고
    • Haa1, a protein homologous to the copper-regulated transcription factor Ace1, is a novel transcriptional activator
    • Keller G, Ray E, Brown PO, Winge DR (2001) Haa1, a protein homologous to the copper-regulated transcription factor Ace1, is a novel transcriptional activator. J Biol Chem 276:38697-38702
    • (2001) J Biol Chem , vol.276 , pp. 38697-38702
    • Keller, G.1    Ray, E.2    Brown, P.O.3    Winge, D.R.4
  • 80
    • 0016659863 scopus 로고
    • Cytochrome c oxidase biosynthesis and assembly in Candida utilis yeast cells. Function of copper in the assembly of active cytochrome c oxidase
    • Keyhani E, Keyhani J (1975) Cytochrome c oxidase biosynthesis and assembly in Candida utilis yeast cells. Function of copper in the assembly of active cytochrome c oxidase. Arch Biochem Biophys 167:596-602
    • (1975) Arch Biochem Biophys , vol.167 , pp. 596-602
    • Keyhani, E.1    Keyhani, J.2
  • 81
    • 0035834376 scopus 로고    scopus 로고
    • The role of PDR13 in tolerance to high copper stress in budding yeast
    • Kim DY, Song WY, Yang YY, Lee Y (2001) The role of PDR13 in tolerance to high copper stress in budding yeast. FEBS Lett 508:99-102
    • (2001) FEBS Lett , vol.508 , pp. 99-102
    • Kim, D.Y.1    Song, W.Y.2    Yang, Y.Y.3    Lee, Y.4
  • 82
    • 0030898098 scopus 로고    scopus 로고
    • Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis
    • Klomp LWJ, Lin SJ, Yuan D, Klausner RD, Culotta VC, Gitlin JD (1997) Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J Biol Chem 272:9221-9226
    • (1997) J Biol Chem , vol.272 , pp. 9221-9226
    • Klomp, L.W.J.1    Lin, S.J.2    Yuan, D.3    Klausner, R.D.4    Culotta, V.C.5    Gitlin, J.D.6
  • 83
    • 0029786735 scopus 로고    scopus 로고
    • A widespread transposable element masks expression of a yeast copper transport gene
    • Knight SA, Labbe S, Kwon LF, Kosman DJ, Thiele DJ (1996) A widespread transposable element masks expression of a yeast copper transport gene. Genes Dev 10:1917-1929
    • (1996) Genes Dev , vol.10 , pp. 1917-1929
    • Knight, S.A.1    Labbe, S.2    Kwon, L.F.3    Kosman, D.J.4    Thiele, D.J.5
  • 84
    • 0040437349 scopus 로고    scopus 로고
    • A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe
    • Labbe S, Pena MM, Fernandes AR, Thiele DJ (1999) A copper-sensing transcription factor regulates iron uptake genes in Schizosaccharomyces pombe. J Biol Chem 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
  • 85
    • 0033388950 scopus 로고    scopus 로고
    • Pipes and wiring: The regulation of copper uptake and distribution in yeast
    • Labbe S, Thiele DJ (1999) Pipes and wiring: The regulation of copper uptake and distribution in yeast. Trends Microbiol 7:500-505
    • (1999) Trends Microbiol , vol.7 , pp. 500-505
    • Labbe, S.1    Thiele, D.J.2
  • 86
    • 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 DJ (1997) Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway. J Biol Chem 272:15951-15958
    • (1997) J Biol Chem , vol.272 , pp. 15951-15958
    • Labbe, S.1    Zhu, Z.2    Thiele, D.J.3
  • 87
    • 0034610310 scopus 로고    scopus 로고
    • Heterodimer formation between superoxide dismutase and its copper chaperone
    • Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC (2000) Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry 39:14720-14727
    • (2000) Biochemistry , vol.39 , pp. 14720-14727
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 89
    • 0034878525 scopus 로고    scopus 로고
    • Heterodimeric structure of superoxide dismutase in complex with its metallochaperone
    • Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC (2001) Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nat Struct Biol 8:750-755
    • (2001) Nat Struct Biol , vol.8 , pp. 750-755
    • Lamb, A.L.1    Torres, A.S.2    O'Halloran, T.V.3    Rosenzweig, A.C.4
  • 90
    • 0037040252 scopus 로고    scopus 로고
    • Biochemical characterization of the human copper transporter Ctr1
    • Lee J, Pena MM, Nose Y, Thiele DJ (2002) Biochemical characterization of the human copper transporter Ctr1. J Biol Chem 277:4380-4387
    • (2002) J Biol Chem , vol.277 , pp. 4380-4387
    • Lee, J.1    Pena, M.M.2    Nose, Y.3    Thiele, D.J.4
  • 91
    • 0029946913 scopus 로고    scopus 로고
    • Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain
    • Lesuisse E, Casteras-Simon M, Labbe P (1996) Evidence for the Saccharomyces cerevisiae ferrireductase system being a multicomponent electron transport chain. J Biol Chem 271:13578-13583
    • (1996) J Biol Chem , vol.271 , pp. 13578-13583
    • Lesuisse, E.1    Casteras-Simon, M.2    Labbe, P.3
  • 92
    • 0035800856 scopus 로고    scopus 로고
    • Ccc1 is a transporter that mediates vacuolar iron storage in yeast
    • Li L, Chen OS, McVey Ward D, Kaplan J (2001) Ccc1 is a transporter that mediates vacuolar iron storage in yeast. J Biol Chem 276:29515-29519
    • (2001) J Biol Chem , vol.276 , pp. 29515-29519
    • Li, L.1    Chen, O.S.2    McVey Ward, D.3    Kaplan, J.4
  • 93
    • 0025363018 scopus 로고
    • Copper uptake in wild type and copper metallothionein-deficient Saccharomyces cerevisiae. Kinetics and mechanism
    • Lin CM, Kosman DJ (1990) Copper uptake in wild type and copper metallothionein-deficient Saccharomyces cerevisiae. Kinetics and mechanism. J Biol Chem 265:9194-9200
    • (1990) J Biol Chem , vol.265 , pp. 9194-9200
    • Lin, C.M.1    Kosman, D.J.2
  • 94
    • 0029039920 scopus 로고
    • The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity
    • Lin SJ, Culotta, VC (1995) The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc Natl Acad Sci USA 92:3784-3788
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3784-3788
    • Lin, S.J.1    Culotta, V.C.2
  • 95
    • 0030910597 scopus 로고    scopus 로고
    • A Role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport
    • Lin SJ, Pufahl RA, Dancis A, O'Halloran TV, Culotta VC (1997) A Role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J Biol Chem 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
  • 96
    • 0036840625 scopus 로고    scopus 로고
    • The copper transporter CTR1 regulates cisplatin uptake in Saccharomyces cerevisiae
    • Lin X, Okuda T, Holzer A, Howell SB (2002) The copper transporter CTR1 regulates cisplatin uptake in Saccharomyces cerevisiae. Mol Pharmacol 62:1154-1159
    • (2002) Mol Pharmacol , vol.62 , pp. 1154-1159
    • Lin, X.1    Okuda, T.2    Holzer, A.3    Howell, S.B.4
  • 97
    • 0001352978 scopus 로고    scopus 로고
    • Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene
    • Liu XF, Culotta VC (1999) Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene. J Biol Chem 274:4863-4868
    • (1999) J Biol Chem , vol.274 , pp. 4863-4868
    • Liu, X.F.1    Culotta, V.C.2
  • 98
    • 0001726322 scopus 로고    scopus 로고
    • Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene
    • Liu XF, Supek F, Nelson N, Culotta VC (1997) Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene. J Biol Chem 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
  • 99
    • 0036263267 scopus 로고    scopus 로고
    • The molecular basis of copper homeostasis copper-related disorders
    • Llanos RM, Mercer JF (2002) The molecular basis of copper homeostasis copper-related disorders. DNA Cell Biol 21:259-270
    • (2002) DNA Cell Biol , vol.21 , pp. 259-270
    • Llanos, R.M.1    Mercer, J.F.2
  • 100
    • 0034680823 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Interaction between Sco1p and Cox2p
    • Lode A, Kuschel M, Paret C, Rodel G (2000) Mitochondrial copper metabolism in yeast: Interaction between Sco1p and Cox2p. FEBS lett 448:1-6
    • (2000) FEBS Lett , vol.448 , pp. 1-6
    • Lode, A.1    Kuschel, M.2    Paret, C.3    Rodel, G.4
  • 101
    • 0036678264 scopus 로고    scopus 로고
    • Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p
    • Lode A, Paret C, Rodel G (2002) Molecular characterization of Saccharomyces cerevisiae Sco2p reveals a high degree of redundancy with Sco1p. Yeast 19:909-922
    • (2002) Yeast , vol.19 , pp. 909-922
    • Lode, A.1    Paret, C.2    Rodel, G.3
  • 102
    • 0021435857 scopus 로고
    • Drugs five years later. Cisplatin
    • Loehrer PJ, Einhorn LH (1984) Drugs five years later. Cisplatin. Ann Intern Med 100:704-713
    • (1984) Ann Intern Med , vol.100 , pp. 704-713
    • Loehrer, P.J.1    Einhorn, L.H.2
  • 104
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • Lutsenko S, Kaplan JH (1995) Organization of P-type ATPases: significance of structural diversity. Biochemistry 34:15607-15613
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 105
    • 0034660257 scopus 로고    scopus 로고
    • Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae
    • MacDiarmid CW, Gaither LA, Eide D (2000) Zinc transporters that regulate vacuolar zinc storage in Saccharomyces cerevisiae. EMBO J 19:2845-2855
    • (2000) EMBO J , vol.19 , pp. 2845-2855
    • MacDiarmid, C.W.1    Gaither, L.A.2    Eide, D.3
  • 106
    • 0032508637 scopus 로고    scopus 로고
    • Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae
    • Martins LJ, Jensen LT, Simon JR, Keller GL, Winge DR (1998) Metalloregulation of FRE1 and FRE2 homologs in Saccharomyces cerevisiae. J Biol Chem 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
  • 107
    • 0038818593 scopus 로고    scopus 로고
    • The Candida albicans CTR1 gene encodes a functional copper transporter
    • Marvin ME, Williams PH, Cashmore AM (2003) The Candida albicans CTR1 gene encodes a functional copper transporter. Microbiology 149:1461-1474
    • (2003) Microbiology , vol.149 , pp. 1461-1474
    • Marvin, M.E.1    Williams, P.H.2    Cashmore, A.M.3
  • 108
    • 1242294474 scopus 로고    scopus 로고
    • Cox17 is functional when tethered to the mitochondrial inner membrane
    • Maxfield AB, Heaton DN, Winge DR (2004) Cox17 is functional when tethered to the mitochondrial inner membrane. J Biol Chem 279:5072-5080
    • (2004) J Biol Chem , vol.279 , pp. 5072-5080
    • Maxfield, A.B.1    Heaton, D.N.2    Winge, D.R.3
  • 109
    • 0014691242 scopus 로고
    • The utility of superoxide dismutase in studying free radical reactions: Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen
    • McCord JM, Fridovich I (1969) The utility of superoxide dismutase in studying free radical reactions: Radicals generated by the interaction of sulfite, dimethyl sulfoxide, and oxygen. J Biol Chem 244:6049-6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 110
    • 0024316828 scopus 로고
    • Candida glabrata metallothioneins. Cloning and sequence of the genes and characterization of proteins
    • Mehra RK, Garey JR, Butt TR, Gray WR, Winge DR (1989) Candida glabrata metallothioneins. Cloning and sequence of the genes and characterization of proteins. J Biol Chem 264:19747-19753
    • (1989) J Biol Chem , vol.264 , pp. 19747-19753
    • Mehra, R.K.1    Garey, J.R.2    Butt, T.R.3    Gray, W.R.4    Winge, D.R.5
  • 111
    • 0025265525 scopus 로고
    • Selective and tandem amplification of a member of the metallothionein gene family in Candida glabrata
    • Mehra RK, Garey JR, Winge DR (1990) Selective and tandem amplification of a member of the metallothionein gene family in Candida glabrata. J Biol Chem 265:6369-6375
    • (1990) J Biol Chem , vol.265 , pp. 6369-6375
    • Mehra, R.K.1    Garey, J.R.2    Winge, D.R.3
  • 112
    • 0026519189 scopus 로고
    • Disruption analysis of metallothionein-encoding genes in Candida glabrata
    • Mehra RK, Thorvaldsen JL, Macreadie IG, Winge DR (1992) Disruption analysis of metallothionein-encoding genes in Candida glabrata. Gene 114:75-80
    • (1992) Gene , vol.114 , pp. 75-80
    • Mehra, R.K.1    Thorvaldsen, J.L.2    Macreadie, I.G.3    Winge, D.R.4
  • 113
    • 4143087157 scopus 로고    scopus 로고
    • Transcriptional control of multidrug resistance in the yeast Saccharomyces
    • Moye-Rowley WS (2003) Transcriptional control of multidrug resistance in the yeast Saccharomyces. Prog Nucleic Acid Res Mol Biol 73:251-279
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.73 , pp. 251-279
    • Moye-Rowley, W.S.1
  • 114
    • 0035834661 scopus 로고    scopus 로고
    • Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein
    • Nittis T, George GN, Winge DR (2001) Yeast Sco1, a protein essential for cytochrome c oxidase function is a Cu(I)-binding protein. J Biol Chem 276:42520-42526
    • (2001) J Biol Chem , vol.276 , pp. 42520-42526
    • Nittis, T.1    George, G.N.2    Winge, D.R.3
  • 115
    • 0037174842 scopus 로고    scopus 로고
    • Characterization of Cox19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase
    • Nobrega MP, Simone CB, Bandeira, Beers J, Tzagoloff A (2002) Characterization of Cox19, a widely distributed gene required for expression of mitochondrial cytochrome oxidase. J Biol Chem 277:40206-40211
    • (2002) J Biol Chem , vol.277 , pp. 40206-40211
    • Nobrega, M.P.1    Simone, C.B.2    Bandeira Beers, J.3    Tzagoloff, A.4
  • 116
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt A, Suter H, Krapf R, Solioz M (1993) Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J Biol Chem 268:12775-12779
    • (1993) J Biol Chem , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 117
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran TV, Culotta VC (2000) Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275:25057-25060
    • (2000) J Biol Chem , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 118
    • 0029994433 scopus 로고    scopus 로고
    • Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis
    • Ooi CE, Rabinovich E, Dancis A, Bonifacino JS, Klausner RD (1996) Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis. EMBO J 15:3515-3523
    • (1996) EMBO J , vol.15 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2    Dancis, A.3    Bonifacino, J.S.4    Klausner, R.D.5
  • 119
    • 0014691028 scopus 로고
    • Mobilization of liver iron by ferroxidase (ceruloplasmin)
    • Osaki S, Johnson DA (1969) Mobilization of liver iron by ferroxidase (ceruloplasmin). J Biol Chem 244:5757-5758
    • (1969) J Biol Chem , vol.244 , pp. 5757-5758
    • Osaki, S.1    Johnson, D.A.2
  • 120
    • 0031916243 scopus 로고    scopus 로고
    • 2+ homeostasis in the yeast Saccharomyces cerevisiae
    • 2+ homeostasis in the yeast Saccharomyces cerevisiae. Genetics 148:1787-1798
    • (1998) Genetics , vol.148 , pp. 1787-1798
    • Paidhungat, M.1    Garrett, S.2
  • 121
    • 0032488829 scopus 로고    scopus 로고
    • Functional expression of the Menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases
    • Payne AS, Gitlin JD (1998) Functional expression of the Menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases. J Biol Chem 273:3765-3770
    • (1998) J Biol Chem , vol.273 , pp. 3765-3770
    • Payne, A.S.1    Gitlin, J.D.2
  • 122
    • 0242666640 scopus 로고    scopus 로고
    • Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae
    • Pena MM, Koch KA, Thiele DJ (1998) Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae. Mol Cell Biol 18:2514-2523
    • (1998) Mol Cell Biol , vol.18 , pp. 2514-2523
    • Pena, M.M.1    Koch, K.A.2    Thiele, D.J.3
  • 123
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • Peña MM, Lee J, Thiele DJ (1999) A delicate balance: Homeostatic control of copper uptake and distribution. J Nutr 129:1251-1260
    • (1999) J Nutr , vol.129 , pp. 1251-1260
    • Peña, M.M.1    Lee, J.2    Thiele, D.J.3
  • 124
    • 0034721907 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3
    • Pena MM, Puig S, Thiele DJ (2000) Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3. J Biol Chem 275:33244-33251
    • (2000) J Biol Chem , vol.275 , pp. 33244-33251
    • Pena, M.M.1    Puig, S.2    Thiele, D.J.3
  • 125
    • 0038439210 scopus 로고    scopus 로고
    • Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1
    • Petris MJ, Smith K, Lee J, Thiele DJ (2003) Copper-stimulated endocytosis and degradation of the human copper transporter, hCtr1. J Biol Chem 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
  • 127
    • 0034893220 scopus 로고    scopus 로고
    • Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae
    • Portnoy ME, Schmidt PJ, Rogers RS, Culotta VC (2001) Metal transporters that contribute copper to metallochaperones in Saccharomyces cerevisiae. Mol Genet Genomics 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
  • 129
    • 0036525717 scopus 로고    scopus 로고
    • Molecular mechanisms of copper uptake and distribution
    • Puig S, Thiele DJ (2002) Molecular mechanisms of copper uptake and distribution. Curr Opin Chem Biol 6:171-180
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 171-180
    • Puig, S.1    Thiele, D.J.2
  • 130
    • 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 DJ (2002) Biochemical and genetic analyses of yeast and human high affinity copper transporters suggest a conserved mechanism for copper uptake. J Biol Chem 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
  • 131
    • 0028131545 scopus 로고
    • A putative P-type Cu (2+)-transporting ATPase gene on chromosome II of Saccharomyces cerevisiae
    • Rad MR, Kirchrath L, Hollenberg CP (1994) A putative P-type Cu (2+)-transporting ATPase gene on chromosome II of Saccharomyces cerevisiae. Yeast 10:1217-1225
    • (1994) Yeast , vol.10 , pp. 1217-1225
    • Rad, M.R.1    Kirchrath, L.2    Hollenberg, C.P.3
  • 132
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae TD, Schmidt PJ, Pufahl RA, Culotta VC, O'Halloran TV (1999) Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase. Science 284:805-807
    • (1999) Science , vol.284 , pp. 805-807
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 133
    • 0030788474 scopus 로고    scopus 로고
    • Mutants of Saccharomyces cerevisiae defective in vacuolar function confirm a role for the vacuole in toxic metal ion detoxification
    • Ramsay LM, Gadd GM (1997) Mutants of Saccharomyces cerevisiae defective in vacuolar function confirm a role for the vacuole in toxic metal ion detoxification. FEMS Microbiol Lett 152:293-298
    • (1997) FEMS Microbiol Lett , vol.152 , pp. 293-298
    • Ramsay, L.M.1    Gadd, G.M.2
  • 134
    • 11144247945 scopus 로고    scopus 로고
    • Mobilization of intracellular copper stores by the Ctr2 vacuolar copper transporter
    • (in press)
    • Rees EM, Lee J, Theile DJ (2004) Mobilization of intracellular copper stores by the Ctr2 vacuolar copper transporter. J Biol Chem (in press)
    • (2004) J Biol Chem
    • Rees, E.M.1    Lee, J.2    Theile, D.J.3
  • 135
    • 0033025125 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase
    • Rentzsch A, Krummeck-Weiss G, Hofer A, Bartuschka A, Ostermann K, Rodel G (1999) Mitochondrial copper metabolism in yeast: Mutational analysis of Sco1p involved in the biogenesis of cytochrome c oxidase. Curr Genet 35:103-108
    • (1999) Curr Genet , vol.35 , pp. 103-108
    • Rentzsch, A.1    Krummeck-Weiss, G.2    Hofer, A.3    Bartuschka, A.4    Ostermann, K.5    Rodel, G.6
  • 136
    • 0033901460 scopus 로고    scopus 로고
    • Role of a Candida albicans P1-type ATPase in resistance to copper and silver ion toxicity
    • Riggle PJ, Kumamoto CA (2000) Role of a Candida albicans P1-type ATPase in resistance to copper and silver ion toxicity. J Bacteriol 182:4899-4905
    • (2000) J Bacteriol , vol.182 , pp. 4899-4905
    • Riggle, P.J.1    Kumamoto, C.A.2
  • 137
    • 0027269739 scopus 로고
    • The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase
    • Roman DG, Dancis A, Anderson GJ, Klausner RD (1993) The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase. Mol Cell Biol 13:4342-4350
    • (1993) Mol Cell Biol , vol.13 , pp. 4342-4350
    • Roman, D.G.1    Dancis, A.2    Anderson, G.J.3    Klausner, R.D.4
  • 139
    • 0035117191 scopus 로고    scopus 로고
    • Copper delivery by metallochaperone proteins
    • Rosenzweig AC (2001) Copper delivery by metallochaperone proteins. Acc Chem Res 34:119-128
    • (2001) Acc Chem Res , vol.34 , pp. 119-128
    • Rosenzweig, A.C.1
  • 140
    • 0026613011 scopus 로고
    • Cytochrome b558: The flavin-binding component of the phagocyte NADPH oxidase
    • Rotrosen D, Yeung CL, Leto TL, Malech HL, Kwong CH (1992) Cytochrome b558: The flavin-binding component of the phagocyte NADPH oxidase. Science 256:1459-1462
    • (1992) Science , vol.256 , pp. 1459-1462
    • Rotrosen, D.1    Yeung, C.L.2    Leto, T.L.3    Malech, H.L.4    Kwong, C.H.5
  • 141
    • 0032932229 scopus 로고    scopus 로고
    • Genetic disorders of membrane transport. IV. Wilson's disease and Menkes disease
    • Schaefer M, Gitlin JD (1999) Genetic disorders of membrane transport. IV. Wilson's disease and Menkes disease. Am J Physiol 276:G311-314
    • (1999) Am J Physiol , vol.276
    • Schaefer, M.1    Gitlin, J.D.2
  • 143
    • 0034721928 scopus 로고    scopus 로고
    • Copper activation of superoxide dismutase 1 (SOD1) in vivo
    • Schmidt PJ, Kunst C, Culotta VC (2000) Copper activation of superoxide dismutase 1 (SOD1) in vivo. J Biol Chem 275:33771-33776
    • (2000) J Biol Chem , vol.275 , pp. 33771-33776
    • Schmidt, P.J.1    Kunst, C.2    Culotta, V.C.3
  • 144
    • 0036886546 scopus 로고    scopus 로고
    • The transcriptional response to alkaline pH in Saccharomyces cerevisiae: Evidence for calcium-mediated signaling
    • Serrano R, Ruiz A, Bernal D, Chambers JR, Arino J (2002) The transcriptional response to alkaline pH in Saccharomyces cerevisiae: evidence for calcium-mediated signaling. Mol Microbiol 46:1319-1333
    • (2002) Mol Microbiol , vol.46 , pp. 1319-1333
    • Serrano, R.1    Ruiz, A.2    Bernal, D.3    Chambers, J.R.4    Arino, J.5
  • 145
    • 2442500516 scopus 로고    scopus 로고
    • Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment
    • Serrano R, Bernal D, Simon E, Arino J (2004) Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment. J Biol Chem 279:19698-19704
    • (2004) J Biol Chem , vol.279 , pp. 19698-19704
    • Serrano, R.1    Bernal, D.2    Simon, E.3    Arino, J.4
  • 146
    • 15844366125 scopus 로고    scopus 로고
    • The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase
    • Shatwell KP, Dancis A, Cross AR, Klausner RD, Segal AW (1996) The FRE1 ferric reductase of Saccharomyces cerevisiae is a cytochrome b similar to that of NADPH oxidase. J Biol Chem 271:14240-14244
    • (1996) J Biol Chem , vol.271 , pp. 14240-14244
    • Shatwell, K.P.1    Dancis, A.2    Cross, A.R.3    Klausner, R.D.4    Segal, A.W.5
  • 147
    • 0034062984 scopus 로고    scopus 로고
    • The cadmium-resistant gene, CAD2, which is a mutated putative copper-transporter gene (PCA1), controls the intracellular cadmium-level in the yeast S. cerevisiae
    • Shiraishi E, Masahiro I, Masanori J, Hiroshi T (2000) The cadmium-resistant gene, CAD2, which is a mutated putative copper-transporter gene (PCA1), controls the intracellular cadmium-level in the yeast S. cerevisiae. Curr Genet 37:79-86
    • (2000) Curr Genet , vol.37 , pp. 79-86
    • Shiraishi, E.1    Masahiro, I.2    Masanori, J.3    Hiroshi, T.4
  • 148
    • 0032546539 scopus 로고    scopus 로고
    • Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae
    • Srinivasan C, Posewitz MC, George GN, Winge DR (1998) Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae. Biochemistry 37:7572-7577
    • (1998) Biochemistry , vol.37 , pp. 7572-7577
    • Srinivasan, C.1    Posewitz, M.C.2    George, G.N.3    Winge, D.R.4
  • 149
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Steaman R, Yuan D, Yamaguchi-Iwan Y, Klausner RD, Dancis A (1996) A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271:1552-1557
    • (1996) Science , vol.271 , pp. 1552-1557
    • Steaman, R.1    Yuan, D.2    Yamaguchi-Iwan, Y.3    Klausner, R.D.4    Dancis, A.5
  • 150
    • 0035851122 scopus 로고    scopus 로고
    • A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage
    • Sturtz LA, Diekert K, Jensen LT, Lill R, Culotta VC (2001) A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. J Biol Chem 276:38084-38089
    • (2001) J Biol Chem , vol.276 , pp. 38084-38089
    • Sturtz, L.A.1    Diekert, K.2    Jensen, L.T.3    Lill, R.4    Culotta, V.C.5
  • 151
    • 0029978512 scopus 로고    scopus 로고
    • A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria
    • Supek F, Supekova L, Nelson H, Nelson N (1996) A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria. Proc Natl Acad Sci USA 93:5105-5110
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5105-5110
    • Supek, F.1    Supekova, L.2    Nelson, H.3    Nelson, N.4
  • 152
    • 0030659440 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription
    • Szczypka MS, Zhu Z, Silar P, Thiele DJ (1997) Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription. Yeast 13:1423-35
    • (1997) Yeast , vol.13 , pp. 1423-1435
    • Szczypka, M.S.1    Zhu, Z.2    Silar, P.3    Thiele, D.J.4
  • 153
    • 0027169905 scopus 로고
    • Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase
    • Tamai KT, Gralla EB, Ellerby LM, Valentine JS, Thiele DJ (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proc Natl Acad Sci USA 90:8013-8017
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8013-8017
    • Tamai, K.T.1    Gralla, E.B.2    Ellerby, L.M.3    Valentine, J.S.4    Thiele, D.J.5
  • 154
    • 0024044018 scopus 로고
    • ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene
    • Thiele DJ (1988) ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol Cell Biol 8:2745-2752
    • (1988) Mol Cell Biol , vol.8 , pp. 2745-2752
    • Thiele, D.J.1
  • 155
    • 0026553931 scopus 로고
    • Metal-regulated transcription in eukaryotes
    • Thiele DJ (1992) Metal-regulated transcription in eukaryotes. Nucleic Acids Res 20:1183-1191
    • (1992) Nucleic Acids Res , vol.20 , pp. 1183-1191
    • Thiele, D.J.1
  • 158
    • 0037428410 scopus 로고    scopus 로고
    • A dominant allele of PDR1 alters transition metal resistance in yeast
    • Tuttle MS, Radisky D, Li L, Kaplan J (2003) A dominant allele of PDR1 alters transition metal resistance in yeast. J Biol Chem 278:1273-1280
    • (2003) J Biol Chem , vol.278 , pp. 1273-1280
    • Tuttle, M.S.1    Radisky, D.2    Li, L.3    Kaplan, J.4
  • 159
    • 0025071742 scopus 로고
    • Cytochrome oxidase assembly in yeast requires the product of COX11, a homologue of the P. denitrificans protein encoded by ORF3
    • Tzagoloff A, Capitanio N, Nobrega MP, Gatti D (1990) Cytochrome oxidase assembly in yeast requires the product of COX11, a homologue of the P. denitrificans protein encoded by ORF3 EMBO J 9:2759-2764
    • (1990) EMBO J , vol.9 , pp. 2759-2764
    • Tzagoloff, A.1    Capitanio, N.2    Nobrega, M.P.3    Gatti, D.4
  • 161
    • 0015694842 scopus 로고
    • Mitochondrial superoxide disimutase. Site of synthesis and intramitochondrial localization
    • Weisiger RA, Fridovich I (1973) Mitochondrial superoxide disimutase. Site of synthesis and intramitochondrial localization. J Biol Chem 248:4793-4796
    • (1973) J Biol Chem , vol.248 , pp. 4793-4796
    • Weisiger, R.A.1    Fridovich, I.2
  • 162
  • 163
    • 0024422809 scopus 로고
    • The CUP2 gene product regulates the expression of the CUP1 gene, coding for yeast metallothionein
    • Welch J, Fogel S, Buchman C, Karin M (1989) The CUP2 gene product regulates the expression of the CUP1 gene, coding for yeast metallothionein. EMBO J 8:255-260
    • (1989) EMBO J , vol.8 , pp. 255-260
    • Welch, J.1    Fogel, S.2    Buchman, C.3    Karin, M.4
  • 164
    • 0033278125 scopus 로고    scopus 로고
    • Copper-regulatory domain involved in gene expression
    • Winge DR (1999) Copper-regulatory domain involved in gene expression. Adv Exp Med Biol 448:237-246
    • (1999) Adv Exp Med Biol , vol.448 , pp. 237-246
    • Winge, D.R.1
  • 165
    • 0022432526 scopus 로고
    • Yeast metallothioneins: Sequence and metal-binding properties
    • Winge DR, Nielson KB, Gray WR, Hamer DH (1985) Yeast metallothioneins: Sequence and metal-binding properties. J Biol Chem 260:14464-14470
    • (1985) J Biol Chem , vol.260 , pp. 14464-14470
    • Winge, D.R.1    Nielson, K.B.2    Gray, W.R.3    Hamer, D.H.4
  • 166
    • 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 GN, Howlett GJ, Wedd AG (2004) 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 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
  • 167
    • 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, Wedd AG (2002) A C-terminal domain of the membrane copper pump Ctr1 exchanges copper(I) with the copper chaperone Atx1. Chem Commun (Camb) 6:588-589
    • (2002) Chem Commun (Camb) , vol.6 , pp. 588-589
    • Xiao, Z.1    Wedd, A.G.2
  • 168
    • 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 DJ, Klausner RD, Dancis A (1997) Homeostatic regulation of copper uptake in yeast via direct binding of MAC1 protein to upstream regulatory sequences of FRE1 and CTR1. J Biol Chem 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
  • 169
    • 0037025363 scopus 로고    scopus 로고
    • Copper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1p
    • Yonkovich J, McKenndry R, Shi X, Zhu Z (2002) Copper ion-sensing transcription factor Mac1p post-translationally controls the degradation of its target gene product Ctr1p. J Biol Chem 277:23981-23984
    • (2002) J Biol Chem , vol.277 , pp. 23981-23984
    • Yonkovich, J.1    McKenndry, R.2    Shi, X.3    Zhu, Z.4
  • 170
    • 0029863094 scopus 로고    scopus 로고
    • Identification of SLF1 as a new copper homeostasis gene involved in copper sulfide mineralization in Saccharomyces cerevisiae
    • Yu W, Farrell RA, Stillman DJ, Winge DR (1996) Identification of SLF1 as a new copper homeostasis gene involved in copper sulfide mineralization in Saccharomyces cerevisiae. Mol Cell Biol 16:2464-2472
    • (1996) Mol Cell Biol , vol.16 , pp. 2464-2472
    • Yu, W.1    Farrell, R.A.2    Stillman, D.J.3    Winge, D.R.4
  • 171
    • 0028916909 scopus 로고
    • The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake
    • Yuan DS, Stearman R, Dancis A, Dunn T, Beeler T, Klausner RD (1995) The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc Natl Acad Sci USA 92:2632-2636
    • (1995) Proc Natl Acad Sci USA , 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
  • 172
    • 0030820818 scopus 로고    scopus 로고
    • Restriction of copper export in Saccharomyces cerevisiae to a late golgi of post-golgi compartment in the secretory pathway
    • Yuan DS, Dancis A, Klausner RD (1997) Restriction of copper export in Saccharomyces cerevisiae to a late golgi of post-golgi compartment in the secretory pathway. J Biol Chem 272:25787-25793
    • (1997) J Biol Chem , vol.272 , pp. 25787-25793
    • Yuan, D.S.1    Dancis, A.2    Klausner, R.D.3
  • 173
    • 0025779301 scopus 로고
    • Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae
    • Zhou PB, Thiele DJ (1991) Isolation of a metal-activated transcription factor gene from Candida glabrata by complementation in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 88:6112-6116
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6112-6116
    • Zhou, P.B.1    Thiele, D.J.2
  • 174
    • 0027257306 scopus 로고
    • Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification
    • Zhou P, Thiele DJ (1993) Rapid transcriptional autoregulation of a yeast metalloregulatory transcription factor is essential for high-level copper detoxification. Genes Dev 7:1824-1835
    • (1993) Genes Dev , vol.7 , pp. 1824-1835
    • Zhou, P.1    Thiele, D.J.2
  • 175
    • 0030297549 scopus 로고    scopus 로고
    • A specialized nucleosome modulates transcription factor access to a C. glabrata metal responsive promoter
    • Zhu Z, Thiele DJ (1996) A specialized nucleosome modulates transcription factor access to a C. glabrata metal responsive promoter. Cell 87:459-470
    • (1996) Cell , vol.87 , pp. 459-470
    • Zhu, Z.1    Thiele, D.J.2
  • 176
    • 0035827610 scopus 로고    scopus 로고
    • Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe
    • Zhou H, Thiele DJ (2001) Identification of a novel high affinity copper transport complex in the fission yeast Schizosaccharomyces pombe. J Biol Chem 276:20529-20535
    • (2001) J Biol Chem , vol.276 , pp. 20529-20535
    • Zhou, H.1    Thiele, D.J.2
  • 177
    • 0031893254 scopus 로고    scopus 로고
    • Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor
    • Zhu Z, Labbe S, Pena MM, Thiele DJ (1998) Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor. J Biol Chem 273:1277-1280
    • (1998) J Biol Chem , vol.273 , pp. 1277-1280
    • Zhu, Z.1    Labbe, S.2    Pena, M.M.3    Thiele, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.