메뉴 건너뛰기




Volumn 20, Issue 11, 2000, Pages 3918-3927

Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; GLUTAMIC ACID; IRON; LYSINE; MITOCHONDRIAL DNA; SUCCINATE DEHYDROGENASE;

EID: 0034107324     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.20.11.3918-3927.2000     Document Type: Article
Times cited : (160)

References (57)
  • 1
    • 0028058038 scopus 로고
    • The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
    • Askwith, C., D. Eide, A. Van Ho, P. S. Bernard, L. Li, S. Davis-Kaplan, D. M. Sipe, and J. Kaplan. 1994. The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76:403-410.
    • (1994) Cell , vol.76 , pp. 403-410
    • Askwith, C.1    Eide, D.2    Van Ho, A.3    Bernard, P.S.4    Li, L.5    Davis-Kaplan, S.6    Sipe, D.M.7    Kaplan, J.8
  • 3
    • 0031452147 scopus 로고    scopus 로고
    • Purification, characterization, and localization of yeast Cox17p, a mitochondrial copper shuttle
    • Beers, J., D. M. Glerum, and A. Tzagoloff. 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, D.M.2    Tzagoloff, A.3
  • 4
    • 0027141376 scopus 로고
    • Aconitase, a two-faced protein: Enzyme and iron regulatory factor
    • Beinert, H., and M. C. Kennedy. 1993. Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB J. 7:1442-1449.
    • (1993) FASEB J. , vol.7 , pp. 1442-1449
    • Beinert, H.1    Kennedy, M.C.2
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 0032508609 scopus 로고    scopus 로고
    • The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase
    • Casareno, R. L., D. Waggoner, and J. D. Gitlin. 1998. The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase. J. Biol. Chem. 273:23625-23628.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23625-23628
    • Casareno, R.L.1    Waggoner, D.2    Gitlin, J.D.3
  • 7
    • 0027953554 scopus 로고
    • Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins
    • Cullin, C., and L. Minvielle-Sebastia. 1994. Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins. Yeast 10:105-112.
    • (1994) Yeast , vol.10 , pp. 105-112
    • Cullin, C.1    Minvielle-Sebastia, L.2
  • 8
    • 0020479807 scopus 로고
    • Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria
    • Daum, G., P. C. Bohni, and G. Schatz. 1982. Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermembrane space of yeast mitochondria. J. Biol. Chem. 257:13028-13033.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13028-13033
    • Daum, G.1    Bohni, P.C.2    Schatz, G.3
  • 9
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint, D. H. 1996. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J. Biol. Chem. 271:16068-16074.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 10
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury, F., and O. Cazzalini. 1997. Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. 411:373-377.
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 11
    • 0027959635 scopus 로고
    • nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters
    • Fu, W., R. F. Jack, T. V. Morgan, D. R. Dean, and M. K. Johnson. 1994. nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters. Biochemistry 33:13455-13463.
    • (1994) Biochemistry , vol.33 , pp. 13455-13463
    • Fu, W.1    Jack, R.F.2    Morgan, T.V.3    Dean, D.R.4    Johnson, M.K.5
  • 12
    • 0025336743 scopus 로고
    • Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate
    • Gangloff, S. P., D. Marguet, and G. J.-M. Lauquin. 1990. Molecular cloning of the yeast mitochondrial aconitase gene (ACO1) and evidence of a synergistic regulation of expression by glucose plus glutamate. Mol. Cell. Biol. 10:3551-3561.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3551-3561
    • Gangloff, S.P.1    Marguet, D.2    Lauquin, G.J.-M.3
  • 13
    • 0033544704 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae ISU1 and ISU2: Members of a well-conserved gene family for iron-sulfur cluster assembly
    • Garland, S., K. Hoff, L. Vickery, and V. Culotta. 1999. Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly. J. Mol. Biol. 294:897-907.
    • (1999) J. Mol. Biol. , vol.294 , pp. 897-907
    • Garland, S.1    Hoff, K.2    Vickery, L.3    Culotta, V.4
  • 14
    • 0025903857 scopus 로고
    • Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier
    • Gietz, R. D., and R. H. Schiestl. 1991. Applications of high efficiency lithium acetate transformation of intact yeast cells using single-stranded nucleic acids as carrier. Yeast 7:253-263.
    • (1991) Yeast , vol.7 , pp. 253-263
    • Gietz, R.D.1    Schiestl, R.H.2
  • 15
    • 0022376231 scopus 로고
    • NADP+-dependent glutamate dehydrogenase activity is impaired in mutants of Saccharomyces cerevisiae that lack aconitase
    • Gonzalez, A., L. Rodriguez, H. Olivera, and M. Soberon. 1985. NADP+-dependent glutamate dehydrogenase activity is impaired in mutants of Saccharomyces cerevisiae that lack aconitase. J. Gen. Microbiol. 131:2565-2571.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2565-2571
    • Gonzalez, A.1    Rodriguez, L.2    Olivera, H.3    Soberon, M.4
  • 16
    • 0023663892 scopus 로고
    • Successive translocation into and out of the mitochondrial matrix: Targeting of proteins to the intermembrane space by a bipartite signal peptide
    • Hartl, F. U., J. Ostermann, B. Guiard, and W. Neupert. 1987 Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell 51:1027-1037.
    • (1987) Cell , vol.51 , pp. 1027-1037
    • Hartl, F.U.1    Ostermann, J.2    Guiard, B.3    Neupert, W.4
  • 17
    • 0029993477 scopus 로고    scopus 로고
    • Activation of SoxR-dependent transcription in vitro by noncatalytic or NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR
    • Hidalgo, E., and B. Demple. 1996. Activation of SoxR-dependent transcription in vitro by noncatalytic or NifS-mediated assembly of [2Fe-2S] clusters into apo-SoxR. J. Biol. Chem. 271:7269-7272.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7269-7272
    • Hidalgo, E.1    Demple, B.2
  • 18
    • 0031960184 scopus 로고    scopus 로고
    • A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms
    • Irvin, S. D., and J. K. Bhattacharjee. 1998. A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms. J. Mol. Evol. 46: 401-408.
    • (1998) J. Mol. Evol. , vol.46 , pp. 401-408
    • Irvin, S.D.1    Bhattacharjee, J.K.2
  • 19
    • 0024743814 scopus 로고
    • Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii
    • Jacobson, M. R., V. L. Cash, M. C. Weiss, N. F. Laird, W. E. Newton, and D. R. Dean. 1989. Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii. Mol. Gen. Genet. 219:49-57.
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 49-57
    • Jacobson, M.R.1    Cash, V.L.2    Weiss, M.C.3    Laird, N.F.4    Newton, W.E.5    Dean, D.R.6
  • 20
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal, G., P. Csere, B. Guiard, and R. Lill. 1997. The ABC transporter Atm1p is required for mitochondrial iron homeostasis. FEBS Lett. 418:346-350.
    • (1997) FEBS Lett. , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 21
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal, G., P. Csere, C. Prohl, and R. Lill. 1999. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18:3981-3989.
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 22
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., T. A. Rouault, and J. B. Harford. 1993. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 23
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight, S. A., N. B. Sepuri, D. Pain, and A. Dancis. 1998. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273:18389-18393.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 24
    • 0032245425 scopus 로고    scopus 로고
    • Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization
    • Land, T., and T. A. Rouault. 1998. Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization. Mol. Cell 2:807-815.
    • (1998) Mol. Cell , vol.2 , pp. 807-815
    • Land, T.1    Rouault, T.A.2
  • 25
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange, H., A. Kaut, G. Kispal, and R. Lill. 2000. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. USA 97:1050-1055.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1050-1055
    • Lange, H.1    Kaut, A.2    Kispal, G.3    Lill, R.4
  • 26
    • 0032722872 scopus 로고    scopus 로고
    • Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution
    • Li, J., M. Kogan, S. A. Knight, D. Pain, and A. Dancis. 1999. Yeast mitochondrial protein, Nfs1p, coordinately regulates iron-sulfur cluster proteins, cellular iron uptake, and iron distribution. J. Biol. Chem. 274:33025-33034.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33025-33034
    • Li, J.1    Kogan, M.2    Knight, S.A.3    Pain, D.4    Dancis, A.5
  • 27
    • 0001352978 scopus 로고    scopus 로고
    • Post-translation control of Nramp metal transport in yeast. Role of metal ions and the BSD2 gene
    • Liu, X. F., and V. C. Culotta. 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
  • 28
    • 0025299986 scopus 로고
    • Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae
    • Lombardo, A., K. Carine, and I. E. Scheffler. 1990. Cloning and characterization of the iron-sulfur subunit gene of succinate dehydrogenase from Saccharomyces cerevisiae. J. Biol. Chem. 265:10419-10423.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10419-10423
    • Lombardo, A.1    Carine, K.2    Scheffler, I.E.3
  • 29
    • 0023448936 scopus 로고
    • Isolation and expression of the gene encoding yeast mitochondrial malate dehydrogenase
    • McAlister-Henn, L., and L. M. Thompson. 1987. Isolation and expression of the gene encoding yeast mitochondrial malate dehydrogenase. J. Bacteriol. 169:5157-5166.
    • (1987) J. Bacteriol. , vol.169 , pp. 5157-5166
    • McAlister-Henn, L.1    Thompson, L.M.2
  • 30
    • 0028953840 scopus 로고
    • Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds
    • Mumberg, D., R. Muller, and M. Funk. 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119-122.
    • (1995) Gene , vol.156 , pp. 119-122
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 31
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai, K., and P. Horton. 1999. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24:34-36.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 32
    • 0029770047 scopus 로고    scopus 로고
    • Expression and biochemical characterization of iron regulatory proteins 1 and 2 in Saccharomyces cerevisiae
    • Phillips, J. D., B. Guo, Y. Yu, F. M. Brown, and E. A. Leibold. 1996. Expression and biochemical characterization of iron regulatory proteins 1 and 2 in Saccharomyces cerevisiae. Biochemistry 35:15704-15714.
    • (1996) Biochemistry , vol.35 , pp. 15704-15714
    • Phillips, J.D.1    Guo, B.2    Yu, Y.3    Brown, F.M.4    Leibold, E.A.5
  • 34
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable irtracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • Rae, T. D., P. J. Schmidt, R. A. Pufahl, V. C. Culotta, and T. V. O'Halloran. 1999. Undetectable irtracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284:805-808.
    • (1999) Science , vol.284 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 36
    • 0030624029 scopus 로고    scopus 로고
    • Regulation of iron metabolism in eukaryotes
    • Rouault, T., and R. Klausner. 1997. Regulation of iron metabolism in eukaryotes. Curr. Top. Cell. Regul. 35:1-19.
    • (1997) Curr. Top. Cell. Regul. , vol.35 , pp. 1-19
    • Rouault, T.1    Klausner, R.2
  • 38
    • 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., J. Forster, J. Davis, P. James, W. Walter, S. Laloraya, J. Johnson, B. Miao, and E. Craig. 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. 134:603-613.
    • (1996) J. Cell Biol. , vol.134 , pp. 603-613
    • Schilke, B.1    Forster, J.2    Davis, J.3    James, P.4    Walter, W.5    Laloraya, S.6    Johnson, J.7    Miao, B.8    Craig, E.9
  • 39
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke, B., C. Voisine, H. Beinert, and E. Craig. 1999. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 96:10206-10211.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 40
    • 0027322148 scopus 로고
    • Targeting of cytochrome b2 into the mitochondrial intermembrane space: Specific recognition of the sorting signal
    • Schwarz, E., T. Seytter, B. Guiard, and W. Neupert. 1993. Targeting of cytochrome b2 into the mitochondrial intermembrane space: specific recognition of the sorting signal. EMBO J. 12:2295-2302.
    • (1993) EMBO J. , vol.12 , pp. 2295-2302
    • Schwarz, E.1    Seytter, T.2    Guiard, B.3    Neupert, W.4
  • 41
    • 0028293312 scopus 로고
    • A gene encoding a DnaK/hsp70 homolog in Escherichia coli
    • Seaton, B. L., and L. E. Vickery. 1994. A gene encoding a DnaK/hsp70 homolog in Escherichia coli. Proc. Natl. Acad. Sci. USA 91:2066-2070.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2066-2070
    • Seaton, B.L.1    Vickery, L.E.2
  • 43
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 44
    • 0032414399 scopus 로고    scopus 로고
    • The Hsc66-Hsc20 chaperone system in Escherichia coli: Chaperone activity and interactions with the DnaK-DnaJ-GrpE system
    • Silberg, J. J., K. G. Hoff, and L. E. Vickery. 1998. The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-GrpE system. J. Bacteriol. 180:6617-6624.
    • (1998) J. Bacteriol. , vol.180 , pp. 6617-6624
    • Silberg, J.J.1    Hoff, K.G.2    Vickery, L.E.3
  • 45
    • 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., C. R. Lorenz, J. Bode, S. Garland, G. A. Smolen, D. T. Ta, L. E. Vickery, and V. C. Culotta. 1998. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J. Biol. Chem. 273:31138-31144.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31138-31144
    • Strain, J.1    Lorenz, C.R.2    Bode, J.3    Garland, S.4    Smolen, G.A.5    Ta, D.T.6    Vickery, L.E.7    Culotta, V.C.8
  • 46
    • 0018787277 scopus 로고
    • Purification of a reconstitutively active iron-sulfur protein (oxidation factor) from succinate · cytochrome c reductase complex of bovine heart mitochondria
    • Trumpower, B. L., and C. A. Edwards. 1979. Purification of a reconstitutively active iron-sulfur protein (oxidation factor) from succinate · cytochrome c reductase complex of bovine heart mitochondria. J. Biol. Chem. 254:8697-8706.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8697-8706
    • Trumpower, B.L.1    Edwards, C.A.2
  • 47
    • 0021949856 scopus 로고
    • General and specific controls of lysine biosynthesis in Saccharomyces cerevisiae
    • Urrestarazu, L. A., C. W. Borell, and J. K. Bhattacharjee. 1985. General and specific controls of lysine biosynthesis in Saccharomyces cerevisiae. Curr. Genet. 9:341-344.
    • (1985) Curr. Genet. , vol.9 , pp. 341-344
    • Urrestarazu, L.A.1    Borell, C.W.2    Bhattacharjee, J.K.3
  • 48
    • 0030671295 scopus 로고    scopus 로고
    • Delivering copper inside yeast and human cells
    • Valentine, J. S., and E. B. Gralla. 1997. Delivering copper inside yeast and human cells. Science 278:817-818.
    • (1997) Science , vol.278 , pp. 817-818
    • Valentine, J.S.1    Gralla, E.B.2
  • 49
    • 0030903131 scopus 로고    scopus 로고
    • Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • Vickery, L. E., J. J. Silberg, and D. T. Ta. 1997. Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Protein Sci. 6:1047-1056.
    • (1997) Protein Sci. , vol.6 , pp. 1047-1056
    • Vickery, L.E.1    Silberg, J.J.2    Ta, D.T.3
  • 50
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat. R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 51
    • 0030758003 scopus 로고    scopus 로고
    • The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme involved in the fungus-specific lysine biosynthesis pathway
    • Weidner, G., B. Steffan, and A. A. Brakhage. 1997. The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme involved in the fungus-specific lysine biosynthesis pathway. Mol. Gen. Genet. 255:237-247.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 237-247
    • Weidner, G.1    Steffan, B.2    Brakhage, A.A.3
  • 53
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A., J. Yang, P. Cavadini, C. Gellera, B. Lonnerdal. F. Taroni, and G. Cortopassi. 1999. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8:425-430.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 55
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng, L., V. L. Cash, D. H. Flint, and D. R. Dean. 1998. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:13264-13272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 56
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng, L., and D. R. Dean. 1994. Catalytic formation of a nitrogenase iron-sulfur cluster. J. Biol. Chem. 269:18723-18726.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2
  • 57
    • 0027450059 scopus 로고
    • Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis
    • Zheng, L., R. H. White, V. L. Cash, R. F. Jack, and D. R. Dean. 1993. Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis. Proc. Natl. Acad. Sci. USA 90:2754-2758.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2754-2758
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Jack, R.F.4    Dean, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.