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Volumn 14, Issue , 2006, Pages 37-58

Zinc in yeast: Mechanisms involved in homeostasis

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EID: 33748908864     PISSN: 16102096     EISSN: 16106970     Source Type: Book Series    
DOI: 10.1007/4735_98     Document Type: Article
Times cited : (13)

References (74)
  • 2
    • 0035696187 scopus 로고    scopus 로고
    • Cellular zinc sensors: MTF-1 regulation of gene expression
    • Andrews GK (2001) Cellular zinc sensors: MTF-1 regulation of gene expression. Biometals 14:223-237
    • (2001) Biometals , vol.14 , pp. 223-237
    • Andrews, G.K.1
  • 3
    • 0003161553 scopus 로고    scopus 로고
    • Zinc sites in metalloenzymes and related proteins
    • In: I. Bertini, A. Sigel and H. Sigel, Editors, Marcell Dekker, New York
    • Auld DS (2001) Zinc sites in metalloenzymes and related proteins. In: I. Bertini, A. Sigel and H. Sigel, Editors, Handbook on Metalloproteins, Marcell Dekker, New York, pp. 881-959
    • (2001) Handbook on Metalloproteins , pp. 881-959
    • Auld, D.S.1
  • 4
  • 5
    • 0002370274 scopus 로고
    • The reaction pathways of zinc enzymes and related biological catalysts
    • In: Bertini I, Gray H, Lippard S, Valentine JS (eds) University Science Books Mill Valley, CA
    • Bertini I, Luchinat C (1994) The reaction pathways of zinc enzymes and related biological catalysts. In: Bertini I, Gray H, Lippard S, Valentine JS (eds) Bioinorganic Chemistry. University Science Books, Mill Valley, CA, pp 37-106
    • (1994) Bioinorganic Chemistry , pp. 37-106
    • Bertini, I.1    Luchinat, C.2
  • 6
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • Beyersmann D, Haase H (2001) Functions of zinc in signaling, proliferation and differentiation of mammalian cells. Biometals 14:331-341
    • (2001) Biometals , vol.14 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 7
    • 1842524183 scopus 로고    scopus 로고
    • The Zap1 transcriptional activator also acts as a repressor by binding downstream of the TATA box in ZRT2
    • Bird AJ, Blankman E, Stillman DJ, Eide DJ, Winge DR (2004) The Zap1 transcriptional activator also acts as a repressor by binding downstream of the TATA box in ZRT2. EMBO J 23:1123-1132
    • (2004) EMBO J , vol.23 , pp. 1123-1132
    • Bird, A.J.1    Blankman, E.2    Stillman, D.J.3    Eide, D.J.4    Winge, D.R.5
  • 8
    • 0141864674 scopus 로고    scopus 로고
    • Zinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function
    • Bird AJ, McCall K, Kramer M, Blankman E, Winge DR, Eide DJ (2003) Zinc fingers can act as Zn2+ sensors to regulate transcriptional activation domain function. EMBO J 22:5137-5146
    • (2003) EMBO J , vol.22 , pp. 5137-5146
    • Bird, A.J.1    McCall, K.2    Kramer, M.3    Blankman, E.4    Winge, D.R.5    Eide, D.J.6
  • 9
  • 10
    • 0037119369 scopus 로고    scopus 로고
    • Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe
    • Borrelly GP, Harrison MD, Robinson AK, Cox SG, Robinson NJ, Whitehall SK (2002) Surplus zinc is handled by Zym1 metallothionein and Zhf endoplasmic reticulum transporter in Schizosaccharomyces pombe. J Biol Chem 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
  • 13
    • 0026766977 scopus 로고
    • Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins
    • Coleman JE (1992) Zinc proteins: Enzymes, storage proteins, transcription factors, and replication proteins. Annu Rev Biochem 61:897-946
    • (1992) Annu Rev Biochem , vol.61 , pp. 897-946
    • Coleman, J.E.1
  • 15
    • 0026707878 scopus 로고
    • COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae
    • Conklin DS, McMaster JA, Culbertson MR, Kung C (1992) COT1, a gene involved in cobalt accumulation in Saccharomyces cerevisiae. Mol Cell Biol 12:3678-3688
    • (1992) Mol Cell Biol , vol.12 , pp. 3678-3688
    • Conklin, D.S.1    McMaster, J.A.2    Culbertson, M.R.3    Kung, C.4
  • 16
    • 0035499392 scopus 로고    scopus 로고
    • Transcriptional repression: The long and the short of it
    • Courey AJ, Jia S (2001) Transcriptional repression: The long and the short of it. Genes Dev 15:2786-2796
    • (2001) Genes Dev , vol.15 , pp. 2786-2796
    • Courey, A.J.1    Jia, S.2
  • 17
    • 0034069249 scopus 로고    scopus 로고
    • Zinc-dependent protein folding
    • Cox EH, McLendon GL (2000) Zinc-dependent protein folding. Curr Opin Chem Biol 4(2):162-5
    • (2000) Curr Opin Chem Biol , vol.4 , Issue.2 , pp. 162-165
    • Cox, E.H.1    McLendon, G.L.2
  • 18
    • 0033564189 scopus 로고    scopus 로고
    • Genome-wide transcriptional analysis in S. cerevisiae by mini-array membrane hybridization
    • Cox KH, Pinchak AB, Cooper TG (1999) Genome-wide transcriptional analysis in S. cerevisiae by mini-array membrane hybridization. Yeast 15:703-713
    • (1999) Yeast , vol.15 , pp. 703-713
    • Cox, K.H.1    Pinchak, A.B.2    Cooper, T.G.3
  • 19
    • 0030725838 scopus 로고    scopus 로고
    • Zinc metabolism in the brain: Relevance to human neurodegenerative disorders
    • Cuajungco MP, Lees GJ (1997) Zinc metabolism in the brain: Relevance to human neurodegenerative disorders. Neurobiol Dis 4:137-169
    • (1997) Neurobiol Dis , vol.4 , pp. 137-169
    • Cuajungco, M.P.1    Lees, G.J.2
  • 20
    • 4444316699 scopus 로고    scopus 로고
    • Exchangeable zinc ions transiently accumulate in a vesicular compartment in the yeast Saccharomyces cerevisiae
    • Devirgiliis C, Murgia C, Danscher G, Perozzi G (2004) Exchangeable zinc ions transiently accumulate in a vesicular compartment in the yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun 323:58-64
    • (2004) Biochem Biophys Res Commun , vol.323 , pp. 58-64
    • Devirgiliis, C.1    Murgia, C.2    Danscher, G.3    Perozzi, G.4
  • 21
    • 0017234843 scopus 로고
    • Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc
    • Dickenson CJ, Dickinson FM (1976) Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc. Biochem J 153:309-319
    • (1976) Biochem J , vol.153 , pp. 309-319
    • Dickenson, C.J.1    Dickinson, F.M.2
  • 22
    • 0038637993 scopus 로고    scopus 로고
    • Zinc inhibition of cellular energy production: Implications for mitochondria and neurodegeneration
    • Dineley KE, Votyakova TV, Reynolds IJ (2003) Zinc inhibition of cellular energy production: Implications for mitochondria and neurodegeneration. J Neurochem 85:563-570
    • (2003) J Neurochem , vol.85 , pp. 563-570
    • Dineley, K.E.1    Votyakova, T.V.2    Reynolds, I.J.3
  • 23
    • 0037656480 scopus 로고    scopus 로고
    • Multiple regulatory mechanisms maintain zinc homeostasis in Saccharomyces cerevisiae
    • Eide DJ (2003) Multiple regulatory mechanisms maintain zinc homeostasis in Saccharomyces cerevisiae. J Nutr 133:1532S-1535S
    • (2003) J Nutr , vol.133
    • Eide, D.J.1
  • 24
    • 1342344814 scopus 로고    scopus 로고
    • The SLC39 family of metal ion transporters
    • Eide DJ (2004) The SLC39 family of metal ion transporters. Pflugers Arch 447:796-800
    • (2004) Pflugers Arch , vol.447 , pp. 796-800
    • Eide, D.J.1
  • 26
    • 3543109122 scopus 로고    scopus 로고
    • Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function
    • Ellis CD, Wang F, MacDiarmid CW, Clark S, Lyons T, Eide DJ (2004) Zinc and the Msc2 zinc transporter protein are required for endoplasmic reticulum function. J Cell Biol 166:325-335
    • (2004) J Cell Biol , vol.166 , pp. 325-335
    • Ellis, C.D.1    Wang, F.2    MacDiarmid, C.W.3    Clark, S.4    Lyons, T.5    Eide, D.J.6
  • 27
    • 23344440858 scopus 로고    scopus 로고
    • Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells
    • in press
    • Ellis CD, MacDiarmid CW and Eide DJ (2005) Heteromeric protein complexes mediate zinc transport into the secretory pathway of eukaryotic cells. J Biol Chem, in press
    • (2005) J Biol Chem
    • Ellis, C.D.1    MacDiarmid, C.W.2    Eide, D.J.3
  • 28
    • 0037417769 scopus 로고    scopus 로고
    • Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding
    • Evans-Galea MV, Blankman E, Myszka DG, Bird AJ, Eide DJ, Winge DR (2003) Two of the five zinc fingers in the Zap1 transcription factor DNA binding domain dominate site-specific DNA binding. Biochemistry 42:1053-1061
    • (2003) Biochemistry , vol.42 , pp. 1053-1061
    • Evans-Galea, M.V.1    Blankman, E.2    Myszka, D.G.3    Bird, A.J.4    Eide, D.J.5    Winge, D.R.6
  • 29
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • Finney LA, O'Halloran TV (2003) Transition metal speciation in the cell: insights from the chemistry of metal ion receptors. Science 300:931-936
    • (2003) Science , vol.300 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 30
    • 0032582814 scopus 로고    scopus 로고
    • Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation
    • Gitan RS, Luo H, Rodgers J, Broderius M, Eide D (1998) Zinc-induced inactivation of the yeast ZRT1 zinc transporter occurs through endocytosis and vacuolar degradation. J Biol Chem 273:28617-28624
    • (1998) J Biol Chem , vol.273 , pp. 28617-28624
    • Gitan, R.S.1    Luo, H.2    Rodgers, J.3    Broderius, M.4    Eide, D.5
  • 31
    • 0141994845 scopus 로고    scopus 로고
    • A cytosolic domain of the yeast Zrt1 zinc transporter is required for its post-translational inactivation in response to zinc and cadmium
    • Gitan RS, Shababi M, Kramer M, Eide DJ (2003) A cytosolic domain of the yeast Zrt1 zinc transporter is required for its post-translational inactivation in response to zinc and cadmium. J Biol Chem 278:39558-39564
    • (2003) J Biol Chem , vol.278 , pp. 39558-39564
    • Gitan, R.S.1    Shababi, M.2    Kramer, M.3    Eide, D.J.4
  • 33
    • 0035870760 scopus 로고    scopus 로고
    • Treble clef finger - A functionally diverse zinc-binding structural motif
    • Grishin NV (2001) Treble clef finger--a functionally diverse zinc-binding structural motif. Nucleic Acids Res 29:1703-1714
    • (2001) Nucleic Acids Res , vol.29 , pp. 1703-1714
    • Grishin, N.V.1
  • 34
    • 0035971250 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
    • Han GS, Johnston CN, Chen X, Athenstaedt K, Daum G, Carman GM (2001) Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J Biol Chem 276:10126-10133
    • (2001) J Biol Chem , vol.276 , pp. 10126-10133
    • Han, G.S.1    Johnston, C.N.2    Chen, X.3    Athenstaedt, K.4    Daum, G.5    Carman, G.M.6
  • 36
    • 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
  • 37
    • 0024741152 scopus 로고
    • Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae
    • Kamizono A, Nishizawa M, Teranishi Y, Murata K, Kimura A (1989) Identification of a gene conferring resistance to zinc and cadmium ions in the yeast Saccharomyces cerevisiae. Mol Gen Genet 219:161-167
    • (1989) Mol Gen Genet , vol.219 , pp. 161-167
    • Kamizono, A.1    Nishizawa, M.2    Teranishi, Y.3    Murata, K.4    Kimura, A.5
  • 38
    • 0023007605 scopus 로고
    • Yeast preparations enriched with trace elements
    • Korhola M, Edelmann K (1986) Yeast preparations enriched with trace elements. Acta Pharmacol Toxicol (Copenh) 59 Suppl 7:148-151
    • (1986) Acta Pharmacol Toxicol (Copenh) , vol.59 , Issue.SUPPL. 7 , pp. 148-151
    • Korhola, M.1    Edelmann, K.2
  • 39
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva I, Hoyos B, Chua R, Levi E, Hammerling U (2002) Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J Biol Chem 277:44327-44331
    • (2002) J Biol Chem , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 40
    • 0037439997 scopus 로고    scopus 로고
    • Structural classification of zinc fingers: Survey and summary
    • Krishna SS, Majumdar I, Grishin NV (2003) Structural classification of zinc fingers: Survey and summary. Nucleic Acids Res 31:532-550
    • (2003) Nucleic Acids Res , vol.31 , pp. 532-550
    • Krishna, S.S.1    Majumdar, I.2    Grishin, N.V.3
  • 41
    • 0032710987 scopus 로고    scopus 로고
    • Zinc protoporphyrin: A metabolite with a mission
    • Labbe RF, Vreman HJ, Stevenson DK (1999) Zinc protoporphyrin: A metabolite with a mission. Clin Chem 45:2060-2072
    • (1999) Clin Chem , vol.45 , pp. 2060-2072
    • Labbe, R.F.1    Vreman, H.J.2    Stevenson, D.K.3
  • 42
    • 0035253047 scopus 로고    scopus 로고
    • Zinc finger proteins: New insights into structural and functional diversity
    • Laity JH, Lee BM, Wright PE (2001) Zinc finger proteins: New insights into structural and functional diversity. Curr Opin Struct Biol 11:39-46
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 39-46
    • Laity, J.H.1    Lee, B.M.2    Wright, P.E.3
  • 43
    • 0035910457 scopus 로고    scopus 로고
    • Alkaline response genes of Saccharomyces cerevisiae and their relationship to the RIM101 pathway
    • Lamb TM, Xu W, Diamond A, Mitchell AP (2001) Alkaline response genes of Saccharomyces cerevisiae and their relationship to the RIM101 pathway. J Biol Chem 276:1850-1856
    • (2001) J Biol Chem , vol.276 , pp. 1850-1856
    • Lamb, T.M.1    Xu, W.2    Diamond, A.3    Mitchell, A.P.4
  • 44
    • 0030662261 scopus 로고    scopus 로고
    • Characterization of two homologous yeast genes that encode mitochondrial iron transporters
    • Li L, Kaplan J (1997) Characterization of two homologous yeast genes that encode mitochondrial iron transporters. J Biol Chem 272:28485-28493
    • (1997) J Biol Chem , vol.272 , pp. 28485-28493
    • Li, L.1    Kaplan, J.2
  • 45
    • 0029806025 scopus 로고    scopus 로고
    • Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles
    • Lin SJ, Culotta VC (1996) Suppression of oxidative damage by Saccharomyces cerevisiae ATX2, which encodes a manganese-trafficking protein that localizes to Golgi-like vesicles. Mol Cell Biol 16:6303-6312
    • (1996) Mol Cell Biol , vol.16 , pp. 6303-6312
    • Lin, S.J.1    Culotta, V.C.2
  • 46
    • 0028808109 scopus 로고
    • Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group
    • Link TA, von Jagow G (1995) Zinc ions inhibit the QP center of bovine heart mitochondrial bc1 complex by blocking a protonatable group. J Biol Chem 270:25001-25006
    • (1995) J Biol Chem , vol.270 , pp. 25001-25006
    • Link, T.A.1    von Jagow, G.2
  • 49
    • 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
  • 50
    • 0037131363 scopus 로고    scopus 로고
    • Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae
    • MacDiarmid CW, Milanick MA, Eide DJ (2002) Biochemical properties of vacuolar zinc transport systems of Saccharomyces cerevisiae. J Biol Chem 277:39187-39194
    • (2002) J Biol Chem , vol.277 , pp. 39187-39194
    • MacDiarmid, C.W.1    Milanick, M.A.2    Eide, D.J.3
  • 51
    • 0037674978 scopus 로고    scopus 로고
    • Induction of the ZRC1 metal tolerance gene in zinc-limited yeast confers resistance to zinc shock
    • MacDiarmid CW, Milanick MA, Eide DJ (2003) Induction of the ZRC1 metal tolerance gene in zinc-limited yeast confers resistance to zinc shock. J Biol Chem 278:15065-15072
    • (2003) J Biol Chem , vol.278 , pp. 15065-15072
    • MacDiarmid, C.W.1    Milanick, M.A.2    Eide, D.J.3
  • 52
    • 2942516407 scopus 로고    scopus 로고
    • Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein
    • Mason AZ, Perico N, Moeller R, Thrippleton K, Potter T, Lloyd D (2004) Metal donation and apo-metalloenzyme activation by stable isotopically labeled metallothionein. Mar Environ Res 58:371-375
    • (2004) Mar Environ Res , vol.58 , pp. 371-375
    • Mason, A.Z.1    Perico, N.2    Moeller, R.3    Thrippleton, K.4    Potter, T.5    Lloyd, D.6
  • 53
    • 0036931270 scopus 로고    scopus 로고
    • Zinc fingers - Folds for many occasions
    • Matthews JM, Sunde M (2002) Zinc fingers--folds for many occasions. IUBMB Life 54:351-355
    • (2002) IUBMB Life , vol.54 , pp. 351-355
    • Matthews, J.M.1    Sunde, M.2
  • 54
    • 0037369564 scopus 로고    scopus 로고
    • Pyrrolidine dithiocarbamate-induced neuronal cell death is mediated by Akt, casein kinase 2, c-Jun N-terminal kinase, and IkappaB kinase in embryonic hippocampal progenitor cells
    • Min YK, Park JH, Chong SA, Kim YS, Ahn YS, Seo JT, Bae YS, Chung KC (2003) Pyrrolidine dithiocarbamate-induced neuronal cell death is mediated by Akt, casein kinase 2, c-Jun N-terminal kinase, and IkappaB kinase in embryonic hippocampal progenitor cells. J Neurosci Res 71:689-700
    • (2003) J Neurosci Res , vol.71 , pp. 689-700
    • Min, Y.K.1    Park, J.H.2    Chong, S.A.3    Kim, Y.S.4    Ahn, Y.S.5    Seo, J.T.6    Bae, Y.S.7    Chung, K.C.8
  • 57
    • 0000502799 scopus 로고    scopus 로고
    • Effects of zinc deficiency on the growth, proteins and other constituents of yeast, Saccharomyces cerevisiae, cells
    • Obata H, Hayashi A, Toda T, Umebayashi M (1996) Effects of zinc deficiency on the growth, proteins and other constituents of yeast, Saccharomyces cerevisiae, cells. Soil Sci Plant Nutr 42:147-154
    • (1996) Soil Sci Plant Nutr , vol.42 , pp. 147-154
    • Obata, H.1    Hayashi, A.2    Toda, T.3    Umebayashi, M.4
  • 58
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten CE, O'Halloran TV (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis. Science 292:2488-2492
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 60
    • 1242295160 scopus 로고    scopus 로고
    • Efflux and compartmentalization of zinc by members of the SLC30 family of solute carriers
    • Palmiter RD, Huang L (2004) Efflux and compartmentalization of zinc by members of the SLC30 family of solute carriers. Pflugers Arch 447:744-751
    • (2004) Pflugers Arch , vol.447 , pp. 744-751
    • Palmiter, R.D.1    Huang, L.2
  • 61
    • 0043193943 scopus 로고    scopus 로고
    • Comparative genomics of bacterial zinc regulons: Enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins
    • Panina EM, Mironov AA, Gelfand MS (2003) Comparative genomics of bacterial zinc regulons: Enhanced ion transport, pathogenesis, and rearrangement of ribosomal proteins. Proc Natl Acad Sci USA 100:9912-9917
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 9912-9917
    • Panina, E.M.1    Mironov, A.A.2    Gelfand, M.S.3
  • 62
    • 1542304635 scopus 로고    scopus 로고
    • Synthetic analogues relevant to the structure and function of zinc enzymes
    • Parkin G (2004) Synthetic analogues relevant to the structure and function of zinc enzymes. Chem Rev 104:699-767
    • (2004) Chem Rev , vol.104 , pp. 699-767
    • Parkin, G.1
  • 63
    • 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
  • 64
    • 0009843443 scopus 로고
    • Crystalline alcohol dehydrogenase from baker's yeast
    • Racker E (1950) Crystalline alcohol dehydrogenase from baker's yeast. J Biol Chem 184:313-319
    • (1950) J Biol Chem , vol.184 , pp. 313-319
    • Racker, E.1
  • 65
    • 0033544726 scopus 로고    scopus 로고
    • The contribution of a zinc finger motif to the function of yeast ribosomal protein YL37a
    • Rivlin AA, Chan YL, Wool IG (1999) The contribution of a zinc finger motif to the function of yeast ribosomal protein YL37a. J Mol Biol 294:909-919
    • (1999) J Mol Biol , vol.294 , pp. 909-919
    • Rivlin, A.A.1    Chan, Y.L.2    Wool, I.G.3
  • 68
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee BL, Falchuk KH (1993) The biochemical basis of zinc physiology. Physiol Rev 73:79-118
    • (1993) Physiol Rev , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 69
    • 0035875663 scopus 로고    scopus 로고
    • Structure of Golgi alpha-mannosidase II: A target for inhibition of growth and metastasis of cancer cells
    • van den Elsen JM, Kuntz DA, Rose DR (2001) Structure of Golgi alpha-mannosidase II: A target for inhibition of growth and metastasis of cancer cells. EMBO J 20(12):3008-17
    • (2001) EMBO J , vol.20 , Issue.12 , pp. 3008-3017
    • van den Elsen, J.M.1    Kuntz, D.A.2    Rose, D.R.3
  • 70
    • 0033229970 scopus 로고    scopus 로고
    • The economics of ribosome biosynthesis in yeast
    • Warner JR (1999) The economics of ribosome biosynthesis in yeast. Trends Biochem Sci 24:437-440
    • (1999) Trends Biochem Sci , vol.24 , pp. 437-440
    • Warner, J.R.1
  • 71
    • 0037072773 scopus 로고    scopus 로고
    • Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen
    • Waters BM, Eide DJ (2002) Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen. J Biol Chem 277:33749-33757
    • (2002) J Biol Chem , vol.277 , pp. 33749-33757
    • Waters, B.M.1    Eide, D.J.2
  • 72
    • 0032582651 scopus 로고    scopus 로고
    • Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements
    • Zhao H, Butler E, Rodgers J, Spizzo T, Duesterhoeft S, Eide D (1998) Regulation of zinc homeostasis in yeast by binding of the ZAP1 transcriptional activator to zinc-responsive promoter elements. J Biol Chem 273:28713-28720
    • (1998) J Biol Chem , vol.273 , pp. 28713-28720
    • Zhao, H.1    Butler, E.2    Rodgers, J.3    Spizzo, T.4    Duesterhoeft, S.5    Eide, D.6
  • 73
    • 0030794279 scopus 로고    scopus 로고
    • Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae
    • Zhao H, Eide DJ (1997) Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae. Mol Cell Biol 17:5044-5052
    • (1997) Mol Cell Biol , vol.17 , pp. 5044-5052
    • Zhao, H.1    Eide, D.J.2
  • 74
    • 0036428393 scopus 로고    scopus 로고
    • Amino acid residue specific stable isotope labeling for quantitative proteomics
    • Zhu H, Pan S, Gu S, Bradbury EM, Chen X (2002) Amino acid residue specific stable isotope labeling for quantitative proteomics. Rapid Commun Mass Spectrom 16:2115-2123
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 2115-2123
    • Zhu, H.1    Pan, S.2    Gu, S.3    Bradbury, E.M.4    Chen, X.5


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