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Volumn 16, Issue 1, 2003, Pages 185-197

Yeast, a model organism for iron and copper metabolism studies

Author keywords

Copper; Iron; Metabolism; Metal; Yeast

Indexed keywords

CARRIER PROTEIN; COPPER INTRAUTERINE DEVICE; IRON; SIDEROPHORE; TRANSITION ELEMENT;

EID: 0037353864     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1020771000746     Document Type: Conference Paper
Times cited : (135)

References (99)
  • 1
    • 0034896427 scopus 로고    scopus 로고
    • Chemistry and biology of eukaryotic iron metabolism
    • Aisen P, Enns C et al. 2001 Chemistry and biology of eukaryotic iron metabolism. Intern J Biochem Cell Biol 33(10), 940-959.
    • (2001) Intern J Biochem Cell Biol , vol.33 , Issue.10 , pp. 940-959
    • Aisen, P.1    Enns, C.2
  • 2
    • 0032838080 scopus 로고    scopus 로고
    • Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease
    • Ambrosini L, Mercer JFB. 1999 Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease. Hum Mol Gen 8(8), 1547-1555.
    • (1999) Hum Mol Gen , vol.8 , Issue.8 , pp. 1547-1555
    • Ambrosini, L.1    Mercer, J.F.B.2
  • 3
    • 0033990794 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression by oxidative stress and metal ions
    • Andrews GK. 2000 Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem Pharmacol 59(1), 95-104.
    • (2000) Biochem Pharmacol , vol.59 , Issue.1 , pp. 95-104
    • Andrews, G.K.1
  • 4
    • 0033044583 scopus 로고    scopus 로고
    • Iron transport across biologic membranes
    • Andrews NC, Fleming MD et al. 1999 Iron transport across biologic membranes. Nutri Rev 57(4), 114-123.
    • (1999) Nutri Rev , vol.57 , Issue.4 , pp. 114-123
    • Andrews, N.C.1    Fleming, M.D.2
  • 5
    • 0030846021 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin
    • Babcock M, deSilva D et al. 1997 Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin. Science 276(5319), 1709-1712.
    • (1997) Science , vol.276 , Issue.5319 , pp. 1709-1712
    • Babcock, M.1    DeSilva, D.2
  • 6
    • 0031452147 scopus 로고    scopus 로고
    • Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle
    • Beers J, Glerum DM et al. 1997 Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle. J Biol Chem 272(52), 33191-33196.
    • (1997) J Biol Chem , vol.272 , Issue.52 , pp. 33191-33196
    • Beers, J.1    Glerum, D.M.2
  • 7
    • 0029112931 scopus 로고
    • DNA strand breaks produced by oxidative stress in mammalian cells exhibit 3′-phosphoglycolate termini
    • Bertoncini CRA, Meneghini R. 1995 DNA strand breaks produced by oxidative stress in mammalian cells exhibit 3′-phosphoglycolate termini. Nucl Acids Res 23(15), 2995-3002.
    • (1995) Nucl Acids Res , vol.23 , Issue.15 , pp. 2995-3002
    • Bertoncini, C.R.A.1    Meneghini, R.2
  • 8
    • 0035823615 scopus 로고    scopus 로고
    • Aft2p, a novel iron-regulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast
    • Blaiseau PL, Lesuisse E et al. 2001 Aft2p, a novel iron-regulated transcription activator that modulates, with Aft1p, intracellular iron use and resistance to oxidative stress in yeast. J Biol Chem 276(36), 34221-34226.
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 34221-34226
    • Blaiseau, P.L.1    Lesuisse, E.2
  • 9
    • 0033214513 scopus 로고    scopus 로고
    • Regulation of plant ferritin synthesis: How and why
    • Briat JF, Lobreaux S et al. 1999 Regulation of plant ferritin synthesis: how and why. Cell Mol Life Sci 56(1-2), 155-166.
    • (1999) Cell Mol Life Sci , vol.56 , Issue.1-2 , pp. 155-166
    • Briat, J.F.1    Lobreaux, S.2
  • 10
    • 0028242939 scopus 로고
    • Wilson disease and menkes disease - New handles on Heavy-metal transport
    • Bull PC, Cox DW. 1994 Wilson Disease and Menkes Disease - New Handles on Heavy-Metal Transport. Trends Gen 10(7), 246-252.
    • (1994) Trends Gen , vol.10 , Issue.7 , pp. 246-252
    • Bull, P.C.1    Cox, D.W.2
  • 11
    • 0030920037 scopus 로고    scopus 로고
    • The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae
    • Casas C, Aldea M et al. 1997 The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae. Yeast 13(7), 621-637.
    • (1997) Yeast , vol.13 , Issue.7 , pp. 621-637
    • Casas, C.1    Aldea, M.2
  • 12
    • 0034677901 scopus 로고    scopus 로고
    • CCC1 suppresses mitochondrial damage in the yeast model of Friedreich's ataxia by limiting mitochondrial iron accumulation
    • Chen OS, Kaplan J. 2000 CCC1 suppresses mitochondrial damage in the yeast model of Friedreich's ataxia by limiting mitochondrial iron accumulation. J Biol Chem 275(11), 7626-7632.
    • (2000) J Biol Chem , vol.275 , Issue.11 , pp. 7626-7632
    • Chen, O.S.1    Kaplan, J.2
  • 13
    • 0034721927 scopus 로고    scopus 로고
    • The family of SMF metal ion transporters in yeast cells
    • Cohen A, Nelson H et al. 2000 The family of SMF metal ion transporters in yeast cells. J Biol Chem 275(43), 33388-33394.
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33388-33394
    • Cohen, A.1    Nelson, H.2
  • 14
    • 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
    • DavisKaplan SR, Askwith CC et al. 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(23), 13641-13645.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.23 , pp. 13641-13645
    • DavisKaplan, S.R.1    Askwith, C.C.2
  • 16
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi JL, Iyer VR et al. 1997 Exploring the metabolic and genetic control of gene expression on a genomic scale. Science 278(5338), 680-686.
    • (1997) Science , vol.278 , Issue.5338 , pp. 680-686
    • DeRisi, J.L.1    Iyer, V.R.2
  • 17
    • 0030923008 scopus 로고    scopus 로고
    • Characterization of the FET4 protein of yeast - Evidence for a direct role in the transport of iron
    • Dix D, Bridgham J et al. 1997 Characterization of the FET4 protein of yeast - Evidence for a direct role in the transport of iron. J Biol Chem 272(18), 11770-11777.
    • (1997) J Biol Chem , vol.272 , Issue.18 , pp. 11770-11777
    • Dix, D.1    Bridgham, J.2
  • 18
    • 0031845660 scopus 로고    scopus 로고
    • The molecular biology of metal ion transport in Saccharomyces cerevisiae
    • Eide DJ. 1998 The molecular biology of metal ion transport in Saccharomyces cerevisiae. Ann Rev Nutri 18, 441-469.
    • (1998) Ann Rev Nutri , vol.18 , pp. 441-469
    • Eide, D.J.1
  • 19
    • 0027508062 scopus 로고
    • The vacuolar H+-Atpase of Saccharomyces-Cerevisiae is required for efficient copper detoxification, mitochondrial function, and iron metabolism
    • Eide DJ, Bridgham JT et al. 1993 The vacuolar H+-Atpase of Saccharomyces-Cerevisiae is required for efficient copper detoxification, Mitochondrial Function, and Iron Metabolism. Mol General Gen 241(3-4), 447-456.
    • (1993) Mol General Gen , vol.241 , Issue.3-4 , pp. 447-456
    • Eide, D.J.1    Bridgham, J.T.2
  • 20
    • 0035896520 scopus 로고    scopus 로고
    • Mitochondrial control of iron homeostasis - A genome wide analysis of gene expression in a yeast frataxin-deficient strain
    • Foury F, Talibi D. 2001 Mitochondrial control of iron homeostasis - A genome wide analysis of gene expression in a yeast frataxin-deficient strain. J Biol Chem 276(11), 7762-7768.
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 7762-7768
    • Foury, F.1    Talibi, D.2
  • 22
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. 1995 Superoxide Radical and Superoxide Dismutases. Ann Rev Biochem 64, 97-112.
    • (1995) Ann Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 23
    • 0033396970 scopus 로고    scopus 로고
    • Fundamental aspects of reactive oxygen species, or what's the matter with oxygen?
    • Blass JP and McDowell FH (eds) New York, Academy of Sciences; New York
    • Fridovich I. 1999 Fundamental aspects of reactive oxygen species, or what's the matter with oxygen? Annals of the New York Academy of Sciences; Oxidative/energy metabolism in neurodegenerative disorders. In Blass JP and McDowell FH (eds) New York, Academy of Sciences; New York: 13-18.
    • (1999) Annals of the New York Academy of Sciences; Oxidative/Energy Metabolism in Neurodegenerative Disorders , pp. 13-18
    • Fridovich, I.1
  • 24
    • 0035800874 scopus 로고    scopus 로고
    • Reflections of a fortunate biochemist
    • Fridovich I. 2001 Reflections of a fortunate biochemist. J Biol Chem 276(31), 28629-28636.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 28629-28636
    • Fridovich, I.1
  • 25
    • 0033544704 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae ISU1 and ISU2: Members of a well-conserved gene family for iron-sulfur cluster assembly
    • Garland SA, Hoff K et al. 1999 Saccharomyces cerevisiae ISU1 and ISU2: Members of a well-conserved gene family for iron-sulfur cluster assembly. J Mol Biol 294(4), 897-907.
    • (1999) J Mol Biol , vol.294 , Issue.4 , pp. 897-907
    • Garland, S.A.1    Hoff, K.2
  • 26
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of Cox17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum DM, Shtanko A et al. 1996 Characterization of Cox17, a Yeast Gene Involved in Copper Metabolism and Assembly of Cytochrome Oxidase. J Biol Chem 271(24), 14504-14509.
    • (1996) J Biol Chem , vol.271 , Issue.24 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2
  • 27
    • 9444296498 scopus 로고    scopus 로고
    • Sco1 and Sco2 act as high copy suppressors of a mitochondrial copper recruitment defect Saccharomyces Cerevisiae
    • Glerum DM, Shtanko A et al. 1996 Sco1 and Sco2 Act as High Copy Suppressors of a Mitochondrial Copper Recruitment Defect Saccharomyces Cerevisiae. J Biol Chem 271(34), 20531-20535.
    • (1996) J Biol Chem , vol.271 , Issue.34 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2
  • 28
    • 0034644739 scopus 로고    scopus 로고
    • Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays
    • Gross C, Kelleher M et al. 2000 Identification of the copper regulon in Saccharomyces cerevisiae by DNA microarrays. J Biol Chem 275(41), 32310-32316.
    • (2000) J Biol Chem , vol.275 , Issue.41 , pp. 32310-32316
    • Gross, C.1    Kelleher, M.2
  • 29
    • 0034667662 scopus 로고    scopus 로고
    • The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saecharomyces cerevisiae
    • Hassett R, Dix DR et al. 2000 The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saecharomyces cerevisiae. Biochem J 351(PT2), 477-484.
    • (2000) Biochem J , vol.351 , Issue.PART 2 , pp. 477-484
    • Hassett, R.1    Dix, D.R.2
  • 30
    • 0032571374 scopus 로고    scopus 로고
    • Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae - Role of dioxygen and Fe(II)
    • Hassett RF, Romeo AM et al. (1998). Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae - Role of dioxygen and Fe(II). J Biol Chem 273(13), 7628-7636.
    • (1998) J Biol Chem , vol.273 , Issue.13 , pp. 7628-7636
    • Hassett, R.F.1    Romeo, A.M.2
  • 31
    • 0034534913 scopus 로고    scopus 로고
    • Mutational analysis of the mitochondrial copper metallochaperone Cox17
    • Heaton D, Nittis T et al. 2000 Mutational analysis of the mitochondrial copper metallochaperone Cox17. J Biol Chem 275(48), 37582-37587.
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 37582-37587
    • Heaton, D.1    Nittis, T.2
  • 32
    • 0035936586 scopus 로고    scopus 로고
    • The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex
    • Heaton DN, George GN et al. 2001 The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. Biochemistry 40(3), 743-751.
    • (2001) Biochemistry , vol.40 , Issue.3 , pp. 743-751
    • Heaton, D.N.1    George, G.N.2
  • 33
    • 0034607615 scopus 로고    scopus 로고
    • Identification and substrate specificity of a ferrichrome-type siderophore transporter (Arn1p) in Saccharomyces cerevisiae
    • Heymann P, Ernst JF et al. 2000 Identification and substrate specificity of a ferrichrome-type siderophore transporter (Arn1p) in Saccharomyces cerevisiae. Fems Microbiol Lett 186(2), 221-227.
    • (2000) Fems Microbiol Lett , vol.186 , Issue.2 , pp. 221-227
    • Heymann, P.1    Ernst, J.F.2
  • 34
    • 0034019371 scopus 로고    scopus 로고
    • Delivering copper within plant cells
    • Himelblau E, Amasino RM. 2000 Delivering copper within plant cells. Curr Opin Plant Biol 3(3), 205-210.
    • (2000) Curr Opin Plant Biol , vol.3 , Issue.3 , pp. 205-210
    • Himelblau, E.1    Amasino, R.M.2
  • 35
    • 0034616930 scopus 로고    scopus 로고
    • Functional discovery via a compendium of expression profiles
    • Hughes TR, Marion MJ et al. 2000 Functional discovery via a compendium of expression profiles. Cell 102(1), 109-126.
    • (2000) Cell , vol.102 , Issue.1 , pp. 109-126
    • Hughes, T.R.1    Marion, M.J.2
  • 36
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen LT, Culotta VC. 2000 Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol Cell Biol 20(11), 3918-3927.
    • (2000) Mol Cell Biol , vol.20 , Issue.11 , pp. 3918-3927
    • Jensen, L.T.1    Culotta, V.C.2
  • 37
    • 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 et al. 1996 Enhanced effectiveness of copper ion buffering by Cup1 metallothionein compared with Crs5 metallothionein in Saccharomyces Cerevisiae. J Biol Chem 271(31), 18514-18519.
    • (1996) J Biol Chem , vol.271 , Issue.31 , pp. 18514-18519
    • Jensen, L.T.1    Howard, W.R.2
  • 38
    • 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 et al. 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(13), 5051-5056.
    • (1993) Embo J , vol.12 , Issue.13 , pp. 5051-5056
    • Jungmann, J.1    Reins, H.A.2
  • 39
    • 0030584404 scopus 로고    scopus 로고
    • Iron metabolism in eukaryotes - Mars and Venus at it again
    • Kaplan J, Ohalloran TV 1996 Iron metabolism in eukaryotes - Mars and Venus at it again. Science 271(5255), 1510-1512.
    • (1996) Science , vol.271 , Issue.5255 , pp. 1510-1512
    • Kaplan, J.1    Ohalloran, T.V.2
  • 40
    • 0034717132 scopus 로고    scopus 로고
    • Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function
    • Kaut A, Lange H et al. 2000 Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function. J Biol Chem 275(21), 15955-15961.
    • (2000) J Biol Chem , vol.275 , Issue.21 , pp. 15955-15961
    • Kaut, A.1    Lange, H.2
  • 41
    • 0035907297 scopus 로고    scopus 로고
    • J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins
    • Kim R, Saxena S et al. 2001 J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J Biol Chem 276(20), 17524-17532.
    • (2001) J Biol Chem , vol.276 , Issue.20 , pp. 17524-17532
    • Kim, R.1    Saxena, S.2
  • 42
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal G, Csere P et al. 1997 The ABC transporter Atm1p is required for mitochondrial iron homeostasis. Febs Lett 418(3), 346-350.
    • (1997) Febs Lett , vol.418 , Issue.3 , pp. 346-350
    • Kispal, G.1    Csere, P.2
  • 43
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G, Csere P et al. 1999 The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. Embo J 18(14), 3981-3989.
    • (1999) Embo J , vol.18 , Issue.14 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2
  • 44
    • 0029786735 scopus 로고    scopus 로고
    • A widespread transposable element masks expression of a yeast copper transport gene
    • Knight SAB, Labbe S et al. 1996 A widespread transposable element masks expression of a yeast copper transport gene. Genes Develop 10(15), 1917-1929.
    • (1996) Genes Develop , vol.10 , Issue.15 , pp. 1917-1929
    • Knight, S.A.B.1    Labbe, S.2
  • 45
    • 0034793688 scopus 로고    scopus 로고
    • The Haber-Weiss cycle-70 years later
    • Koppenol WH. 2001 The Haber-Weiss cycle-70 years later. Redox Rep 6(4), 229-34.
    • (2001) Redox Rep , vol.6 , Issue.4 , pp. 229-234
    • Koppenol, W.H.1
  • 46
    • 0030941339 scopus 로고    scopus 로고
    • Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway
    • Labbe S, Zhu ZW et al. 1997 Copper-specific transcriptional repression of yeast genes encoding critical components in the copper transport pathway. J Biol Chem 272(25), 15951-15958.
    • (1997) J Biol Chem , vol.272 , Issue.25 , pp. 15951-15958
    • Labbe, S.1    Zhu, Z.W.2
  • 47
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange H, Kaut A et al. 2000 A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc Natl Acad Sci USA 97(3), 1050-1055.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.3 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2
  • 48
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange H, Kispal G et al. 1999 Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J Biol Chem 274(27), 18989-18996.
    • (1999) J Biol Chem , vol.274 , Issue.27 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2
  • 49
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange H, Lisowsky T et al. 2001 An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. Embo Rep 2(8), 715-720.
    • (2001) Embo Rep , vol.2 , Issue.8 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2
  • 50
    • 0035134461 scopus 로고    scopus 로고
    • Siderophore uptake and use by the yeast Saccharomyces cerevisiae
    • Lesuisse E, Blaiseau PL et al. 2001 Siderophore uptake and use by the yeast Saccharomyces cerevisiae. Microbiol-Uk 147(PT2), 289-298.
    • (2001) Microbiol-Uk , vol.147 , Issue.PART 2 , pp. 289-298
    • Lesuisse, E.1    Blaiseau, P.L.2
  • 51
    • 0035846961 scopus 로고    scopus 로고
    • Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis
    • Li J, Saxena S et al. 2001 Adrenodoxin reductase homolog (Arh1p) of yeast mitochondria required for iron homeostasis. J Biol Chem 276(2), 1503-1509.
    • (2001) J Biol Chem , vol.276 , Issue.2 , pp. 1503-1509
    • Li, J.1    Saxena, S.2
  • 52
    • 0035800856 scopus 로고    scopus 로고
    • CCC1 is a transporter that mediates vacuolar iron storage in yeast
    • Li LT, Chen OS et al. 2001 CCC1 is a transporter that mediates vacuolar iron storage in yeast. J Biol Chem 276(31), 29515-29519.
    • (2001) J Biol Chem , vol.276 , Issue.31 , pp. 29515-29519
    • Li, L.T.1    Chen, O.S.2
  • 53
    • 0030014654 scopus 로고    scopus 로고
    • Characterization of yeast methyl sterol oxidase (Erg25) and identification of a human homologue
    • Li LT, Kaplan J. 1996 Characterization of yeast methyl sterol oxidase (Erg25) and identification of a human homologue. J Biol Chem 271(28), 16927-16933.
    • (1996) J Biol Chem , vol.271 , Issue.28 , pp. 16927-16933
    • Li, L.T.1    Kaplan, J.2
  • 54
    • 0030662261 scopus 로고    scopus 로고
    • Characterization of two homologous yeast genes that encode mitochondrial iron transporters
    • Li LT, Kaplan J 1997 Characterization of two homologous yeast genes that encode mitochondrial iron transporters. J Biol Chem 272(45), 28485-28493.
    • (1997) J Biol Chem , vol.272 , Issue.45 , pp. 28485-28493
    • Li, L.T.1    Kaplan, J.2
  • 55
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R, Kispal G. 2000 Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci 25(8), 352-356.
    • (2000) Trends Biochem Sci , vol.25 , Issue.8 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 56
    • 0035002973 scopus 로고    scopus 로고
    • Mitochondrial ABC transporters
    • Lill R and Kispal G. 2001 Mitochondrial ABC transporters. Res Microbiol 152(3-4), 331-340.
    • (2001) Res Microbiol , vol.152 , Issue.3-4 , pp. 331-340
    • Lill, R.1    Kispal, G.2
  • 57
    • 0030910597 scopus 로고    scopus 로고
    • A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport
    • Lin SJ, Pufahl RA et al. 1997 A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J Biol Chem 272(14), 9215-9220.
    • (1997) J Biol Chem , vol.272 , Issue.14 , pp. 9215-9220
    • Lin, S.J.1    Pufahl, R.A.2
  • 58
    • 0028177211 scopus 로고
    • The role of O-2-center-dot- in the production of Ho-center-dot - In vitro and in vivo
    • Liochev SI, Fridovich I. 1994 The role of O-2-center-dot- in the production of Ho-center-dot - in vitro and in vivo. Free Rad Biol Med 16(1), 29-33.
    • (1994) Free Rad Biol Med , vol.16 , Issue.1 , pp. 29-33
    • Liochev, S.I.1    Fridovich, I.2
  • 59
    • 0032732998 scopus 로고    scopus 로고
    • Superoxide and iron: Partners in crime
    • Liochev SI, Fridovich I. 1999 Superoxide and iron: partners in crime. Iubmb Life 48(2), 157-161.
    • (1999) Iubmb Life , vol.48 , Issue.2 , pp. 157-161
    • Liochev, S.I.1    Fridovich, I.2
  • 60
    • 0034680823 scopus 로고    scopus 로고
    • Mitochondrial copper metabolism in yeast: Interaction between Sco1p and Cox2p
    • Lode A, Kuschel M et al. 2000 Mitochondrial copper metabolism in yeast: interaction between Sco1p and Cox2p. FEBS Lett 485(1), 19-24.
    • (2000) FEBS Lett , vol.485 , Issue.1 , pp. 19-24
    • Lode, A.1    Kuschel, M.2
  • 61
    • 0035025935 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in friedreich's ataxia
    • Lodi R, Taylor DJ et al. 2001 Mitochondrial dysfunction in friedreich's ataxia. Biol Signals Recept 10(3-4), 263-270.
    • (2001) Biol Signals Recept , vol.10 , Issue.3-4 , pp. 263-270
    • Lodi, R.1    Taylor, D.J.2
  • 62
    • 0035970292 scopus 로고    scopus 로고
    • The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
    • Lutz T, Westermann B et al. 2001 The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J Mol Biol 307(3), 815-825.
    • (2001) J Mol Biol , vol.307 , Issue.3 , pp. 815-825
    • Lutz, T.1    Westermann, B.2
  • 63
    • 0032604157 scopus 로고    scopus 로고
    • Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis
    • Lyons TJ, Gralla EB et al. 1999 Biological chemistry of copper-zinc superoxide dismutase and its link to amyotrophic lateral sclerosis. Met Ions Biol Syst 36, 125-177.
    • (1999) Met Ions Biol Syst , vol.36 , pp. 125-177
    • Lyons, T.J.1    Gralla, E.B.2
  • 64
    • 0035937770 scopus 로고    scopus 로고
    • The neuronal adaptor protein X11 alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity
    • McLoughlin DM, Standen CL et al. 2001 The neuronal adaptor protein X11 alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity. J Biol Chem 276(12), 9303-9307.
    • (2001) J Biol Chem , vol.276 , Issue.12 , pp. 9303-9307
    • McLoughlin, D.M.1    Standen, C.L.2
  • 65
    • 0026014738 scopus 로고
    • Iron is the intracellular metal involved in the production of DNA damage by oxygen radicals
    • Mello AC, Meneghini R. 1991 Iron is the intracellular metal involved in the production of DNA damage by oxygen radicals. Mutat Res 251(1), 109-113.
    • (1991) Mutat Res , vol.251 , Issue.1 , pp. 109-113
    • Mello, A.C.1    Meneghini, R.2
  • 66
    • 0030857377 scopus 로고    scopus 로고
    • Iron homeostasis, oxidative stress, and DNA damage
    • Meneghini R. 1997 Iron homeostasis, oxidative stress, and DNA damage. Free Rad Biol Med 23(5), 783-792.
    • (1997) Free Rad Biol Med , vol.23 , Issue.5 , pp. 783-792
    • Meneghini, R.1
  • 67
    • 0041893905 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
    • Muhlenhoff U, Lill R. 2000 Biogenesis of iron-sulfur proteins in eukaryotes: a novel task of mitochondria that is inherited from bacteria. Biochim Biophys ActaBioenerg 1459(2-3), 370-382.
    • (2000) Biochim Biophys ActaBioenerg , vol.1459 , Issue.2-3 , pp. 370-382
    • Muhlenhoff, U.1    Lill, R.2
  • 68
    • 0035117173 scopus 로고    scopus 로고
    • Iron-induced oxidative damage in colon carcinoma (Caco-2) cells
    • U17,U18
    • Nunez MT, Tapia V et al. 2001 Iron-induced oxidative damage in colon carcinoma (Caco-2) cells. Free Rad Res 34(1), 57-68,U17,U18.
    • (2001) Free Rad Res , vol.34 , Issue.1 , pp. 57-68
    • Nunez, M.T.1    Tapia, V.2
  • 69
    • 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(33), 25057-25060.
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 70
    • 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 et al. 1996 Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctr1p in the apparent absence of endocytosis. Embo J 15(14), 3515-3523.
    • (1996) Embo J , vol.15 , Issue.14 , pp. 3515-3523
    • Ooi, C.E.1    Rabinovich, E.2
  • 71
    • 0035380105 scopus 로고    scopus 로고
    • Friedreich's ataxia and frataxin: Molecular genetics, evolution and pathogenesis
    • Palau F, 2001 Friedreich's ataxia and frataxin: molecular genetics, evolution and pathogenesis (Review). Interl J Mol Med 7(6), 581-589.
    • (2001) Interl J Mol Med , vol.7 , Issue.6 , pp. 581-589
    • Palau, F.1
  • 72
    • 0343628833 scopus 로고    scopus 로고
    • Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins
    • Pelzer W, Muhlenhoff U et al. 2000 Mitochondrial Isa2p plays a crucial role in the maturation of cellular iron-sulfur proteins. FEBS Lett 476(3), 134-139.
    • (2000) FEBS Lett , vol.476 , Issue.3 , pp. 134-139
    • Pelzer, W.1    Muhlenhoff, U.2
  • 73
    • 0242666640 scopus 로고    scopus 로고
    • Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae
    • Pena MMO, Koch KA et al. 1998 Dynamic regulation of copper uptake and detoxification genes in Saccharomyces cerevisiae. Mol Cell Biol 18(5), 2514-2523.
    • (1998) Mol Cell Biol , vol.18 , Issue.5 , pp. 2514-2523
    • Pena, M.M.O.1    Koch, K.A.2
  • 74
    • 0037477740 scopus 로고    scopus 로고
    • A delicate balance: Homeostatic control of copper uptake and distribution
    • Pena MMO, Lee J et al. 1999 A delicate balance: homeostatic control of copper uptake and distribution. J Nutrit 129(7), 1251-1260.
    • (1999) J Nutrit , vol.129 , Issue.7 , pp. 1251-1260
    • Pena, M.M.O.1    Lee, J.2
  • 75
    • 0034721907 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3
    • Pena MMO, Puig S et al. 2000 Characterization of the Saccharomyces cerevisiae high affinity copper transporter Ctr3. J Biol Chem 275(43), 33244-33251.
    • (2000) J Biol Chem , vol.275 , Issue.43 , pp. 33244-33251
    • Pena, M.M.O.1    Puig, S.2
  • 76
    • 0030684012 scopus 로고    scopus 로고
    • Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family
    • Pinner E, Gruenheid S et al. 1997 Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family. J Biol Chem 272(46), 28933-28938.
    • (1997) J Biol Chem , vol.272 , Issue.46 , pp. 28933-28938
    • Pinner, E.1    Gruenheid, S.2
  • 77
    • 0033873904 scopus 로고    scopus 로고
    • Characterization and localization of human COX17, a gene involved in mitochondrial copper transport
    • Punter FA, Adams DL et al. 2000 Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. Hum Gen 107(1), 69-74.
    • (2000) Hum Gen , vol.107 , Issue.1 , pp. 69-74
    • Punter, F.A.1    Adams, D.L.2
  • 78
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux - Evidence for a mitochondrial, iron cycle
    • Radisky DC, Babcock MC et al. 1999 The yeast frataxin homologue mediates mitochondrial iron efflux - Evidence for a mitochondrial, iron cycle. J Biol Chem 274(8), 4497-4499.
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2
  • 79
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae TD, Schmidt PJ et al. 1999 Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284(5415), 805-808.
    • (1999) Science , vol.284 , Issue.5415 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2
  • 80
    • 0343717915 scopus 로고    scopus 로고
    • Frataxin activates mitochondrial energy conversion and oxidative phosphorylation
    • Ristow M, Pfister MF et al. 2000 Frataxin activates mitochondrial energy conversion and oxidative phosphorylation. Proc Natl Acad Sci USA 97(22), 12239-12243.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.22 , pp. 12239-12243
    • Ristow, M.1    Pfister, M.F.2
  • 81
    • 0029757416 scopus 로고    scopus 로고
    • The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 Is Suppressed by Loss of Mitochondrial DNA
    • Schilke B, Forster J et al. 1996 The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 Is Suppressed by Loss of Mitochondrial DNA. J Cell Biol 134(3), 603-613.
    • (1996) J Cell Biol , vol.134 , Issue.3 , pp. 603-613
    • Schilke, B.1    Forster, J.2
  • 82
    • 0032546539 scopus 로고    scopus 로고
    • Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae
    • Srinivasan C, Posewitz MC et al. 1998 Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae. Biochemistry 37(20), 7572-7577.
    • (1998) Biochemistry , vol.37 , Issue.20 , pp. 7572-7577
    • Srinivasan, C.1    Posewitz, M.C.2
  • 83
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • Stearman R, Yuan DS et al. 1996 A permease-oxidase complex involved in high-affinity iron uptake in yeast. Science 271(5255), 1552-1557.
    • (1996) Science , vol.271 , Issue.5255 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.S.2
  • 84
    • 0029977674 scopus 로고    scopus 로고
    • Copper ions anti the regulation of Saccharomyces Cerevisiae metallothionein genes under aerobic and anaerobic conditions
    • Strain J, Culotta VC. 1996 Copper ions anti the regulation of Saccharomyces Cerevisiae metallothionein genes under aerobic and anaerobic conditions. Mol Gen Gen 251(2), 139-145.
    • (1996) Mol Gen Gen , vol.251 , Issue.2 , pp. 139-145
    • Strain, J.1    Culotta, V.C.2
  • 85
    • 0032553445 scopus 로고    scopus 로고
    • Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae - Identification of proteins predicted to mediate iron-sulfur cluster assembly
    • Strain J, Lorenz CR et al. 1998 Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae - Identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem 273(47), 31138-31144.
    • (1998) J Biol Chem , vol.273 , Issue.47 , pp. 31138-31144
    • Strain, J.1    Lorenz, C.R.2
  • 86
    • 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 ZW et al. 1997 Saccharomyces cerevisiae mutants altered in vacuole function are defective in copper detoxification and iron-responsive gene transcription. Yeast 13(15), 1423-1435.
    • (1997) Yeast , vol.13 , Issue.15 , pp. 1423-1435
    • Szczypka, M.S.1    Zhu, Z.W.2
  • 87
    • 0033621395 scopus 로고    scopus 로고
    • The iron transporter fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane
    • Urbanowski JL, Piper RC. 1999 The iron transporter fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane. J Biol Chem 274(53), 38061-38070.
    • (1999) J Biol Chem , vol.274 , Issue.53 , pp. 38061-38070
    • Urbanowski, J.L.1    Piper, R.C.2
  • 88
    • 0030671295 scopus 로고    scopus 로고
    • Delivering copper inside yeast and human cells
    • Valentine JS, Gralla EB. 1997 Delivering copper inside yeast and human cells. Science 278(5339), 817-818.
    • (1997) Science , vol.278 , Issue.5339 , pp. 817-818
    • Valentine, J.S.1    Gralla, E.B.2
  • 89
    • 0032042992 scopus 로고    scopus 로고
    • The dark side of dioxygen biochemistry
    • Valentine JS, Wertz DL et al. 1998 The dark side of dioxygen biochemistry. Curr Opin Chem Biol 2(2), 253-262.
    • (1998) Curr Opin Chem Biol , vol.2 , Issue.2 , pp. 253-262
    • Valentine, J.S.1    Wertz, D.L.2
  • 90
    • 0035852737 scopus 로고    scopus 로고
    • Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae
    • Voisine C, Cheng YC et al. 2001 Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 98(4), 1483-1488.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.4 , pp. 1483-1488
    • Voisine, C.1    Cheng, Y.C.2
  • 91
    • 0029134884 scopus 로고
    • Cellular copper transport
    • Vulpe CD, Packman S. 1995 Cellular copper transport. Ann Rev Nutrit 15, 293-322.
    • (1995) Ann Rev Nutrit , vol.15 , pp. 293-322
    • Vulpe, C.D.1    Packman, S.2
  • 92
    • 0032887626 scopus 로고    scopus 로고
    • The role of copper in neurodegenerative disease
    • Waggoner DJ, Bartnikas TB et al. 1999 The role of copper in neurodegenerative disease. Neurobiol Dis 6(4), 221-230.
    • (1999) Neurobiol Dis , vol.6 , Issue.4 , pp. 221-230
    • Waggoner, D.J.1    Bartnikas, T.B.2
  • 93
    • 0030467256 scopus 로고    scopus 로고
    • Biochemical characterization and intracellular localization of the Menkes disease protein
    • Yamaguchi Y, Heiny Me et al. 1996 Biochemical characterization and intracellular localization of the Menkes disease protein. Proc Natl Acad Sci USA 93(24), 14030-14035.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.24 , pp. 14030-14035
    • Yamaguchi, Y.1    Heiny, M.E.2
  • 94
    • 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 et al. 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(28), 17711-17718.
    • (1997) J Biol Chem , vol.272 , Issue.28 , pp. 17711-17718
    • Yamaguchi-Iwai, Y.1    Serpe, M.2
  • 95
    • 0030054971 scopus 로고    scopus 로고
    • Iron-regulated DNA binding by the Aft1 protein controls the iron regulon in yeast
    • Yamaguchi-Iwai Y, Steannan R et al. 1996 Iron-regulated DNA binding by the Aft1 protein controls the iron regulon in yeast. Embo J 15(13), 3377-3384.
    • (1996) Embo J , vol.15 , Issue.13 , pp. 3377-3384
    • Yamaguchi-Iwai, Y.1    Steannan, R.2
  • 96
    • 0028961739 scopus 로고
    • Aft1 - A mediator of iron regulated transcriptional control in Saccharomyces cerevisiae
    • Yamaguchiiwai Y, Dancis A et al. 1995 Aft1 - a mediator of iron regulated transcriptional control in Saccharomyces cerevisiae. Embo J 14(6), 1231-1239.
    • (1995) Embo J , vol.14 , Issue.6 , pp. 1231-1239
    • Yamaguchiiwai, Y.1    Dancis, A.2
  • 97
    • 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 et al. 1996 Identification of Slf1 as a new copper homeostasis gene involved in copper sulfide mineralization in Saccharomyces Cerevisiae. Mol Cell Biol 16(5), 2464-2472.
    • (1996) Mol Cell Biol , vol.16 , Issue.5 , pp. 2464-2472
    • Yu, W.1    Farrell, R.A.2
  • 98
    • 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 et al. 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(7), 2632-2636.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.7 , pp. 2632-2636
    • Yuan, D.S.1    Stearman, R.2
  • 99
    • 0031893254 scopus 로고    scopus 로고
    • Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor
    • Zhu ZW, Labbe S et al. 1998 Copper differentially regulates the activity and degradation of yeast Mac1 transcription factor. J Biol Chem 273(3), 1277-1280.
    • (1998) J Biol Chem , vol.273 , Issue.3 , pp. 1277-1280
    • Zhu, Z.W.1    Labbe, S.2


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