메뉴 건너뛰기




Volumn 14, Issue 5, 2010, Pages 541-552

Adaptive changes of the yeast mitochondrial proteome in response to salt stress

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DEHYDROGENASE; COQ6 ENZYME; COQ7 ENZYME; DELTA(24) STEROL C METHYLTRANSFERASE; FRUCTOSE BISPHOSPHATE ALDOLASE; FUNGAL PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE ISOZYME 1; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE ISOZYME 2; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE ISOZYME 3; HEAT SHOCK PROTEIN 78; HYDROGEN PEROXIDE; MITOCHONDRIAL PROTEIN; PEROXIREDOXIN; PHOSPHOGLYCERATE KINASE; PROTEIN ATP4; PROTEIN CPR5; PROTEIN ECM40; PROTEIN GCV3; PROTEIN ILV2; PROTEIN ILV6; PROTEIN KAR2; PROTEIN LEU4; PROTEIN LEU9; PROTEIN LSP1; PROTEIN PDI1; PROTEIN RIP1; PYRUVATE DECARBOXYLASE ISOZYME 1; SODIUM CHLORIDE; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 77958155905     PISSN: 15362310     EISSN: None     Source Type: Journal    
DOI: 10.1089/omi.2010.0020     Document Type: Article
Times cited : (15)

References (58)
  • 1
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner, G., Gaigg, B., Krasser, A., Kainersdorfer, E., Kohlwein, S. D., Perktold, A., et al. (1999). Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur J Biochem 264, 545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1    Gaigg, B.2    Krasser, A.3    Kainersdorfer, E.4    Kohlwein, S.D.5    Perktold, A.6
  • 3
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban, R. S., Nemoto, S., and Finkel, T. (2005). Mitochondria, oxidants, and aging. Cell 120, 483-495.
    • (2005) Cell. , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 4
    • 34248194299 scopus 로고    scopus 로고
    • The antioxidant role of coenzyme Q
    • Bentinger, M., Brismar, K., and Dallner, G. (2007). The antioxidant role of coenzyme Q. Mitochondrion 7 (Suppl), S41-S50.
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Bentinger, M.1    Brismar, K.2    Dallner, G.3
  • 5
    • 0033118209 scopus 로고    scopus 로고
    • Glucose repression in yeast
    • Carlson, M. (1999). Glucose repression in yeast. Curr Opin Microbiol 2, 202-207.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 202-207
    • Carlson, M.1
  • 6
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic organelles in disease, aging, and development
    • Chan, D. C. (2006). Mitochondria: dynamic organelles in disease, aging, and development. Cell 125, 1241-1252.
    • (2006) Cell. , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 7
    • 33644674439 scopus 로고    scopus 로고
    • The organization and inheritance of the mitochondrial genome
    • Chen, X. J., and Butow, R. A. (2005). The organization and inheritance of the mitochondrial genome. Nat Rev Genet 6, 815-825.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 815-825
    • Chen, X.J.1    Butow, R.A.2
  • 8
    • 33749022800 scopus 로고    scopus 로고
    • Structural and functional features and significance of the physical linkage between ER and mitochondria
    • Csordas, G., Renken, C., Varnai, P., Walter, L., Weaver, D., Buttle, K. F., et al. (2006). Structural and functional features and significance of the physical linkage between ER and mitochondria. J Cell Biol 174, 915-921.
    • (2006) J. Cell. Biol. , vol.174 , pp. 915-921
    • Csordas, G.1    Renken, C.2    Varnai, P.3    Walter, L.4    Weaver, D.5    Buttle, K.F.6
  • 9
    • 35448960851 scopus 로고    scopus 로고
    • Functions and dysfunctions of mitochondrial dynamics
    • Detmer, S. A., and Chan, D. C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nat Rev Mol Cell Biol 8, 870-879.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 870-879
    • Detmer, S.A.1    Chan, D.C.2
  • 10
    • 0028206309 scopus 로고
    • Regulation of mitochondrial gene expression in Saccharomyces cerevisiae
    • Dieckmann, C. L., and Staples, R. R. (1994). Regulation of mitochondrial gene expression in Saccharomyces cerevisiae. Int Rev Cytol 152, 145-181.
    • (1994) Int. Rev. Cytol , vol.152 , pp. 145-181
    • Dieckmann, C.L.1    Staples, R.R.2
  • 11
    • 0024348798 scopus 로고
    • The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol
    • Gaber, R. F., Copple, D. M., Kennedy, B. K., Vidal, M., and Bard, M. (1989). The yeast gene ERG6 is required for normal membrane function but is not essential for biosynthesis of the cell-cycle-sparking sterol. Mol Cell Biol 9, 3447-3456.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3447-3456
    • Gaber, R.F.1    Copple, D.M.2    Kennedy, B.K.3    Vidal, M.4    Bard, M.5
  • 12
    • 0028916511 scopus 로고
    • Characterization of a microsomal subfraction associated with mitochondria of the yeast, Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria
    • Gaigg, B., Simbeni, R., Hrastnik, C., Paltauf, F., and Daum, G. (1995). Characterization of a microsomal subfraction associated with mitochondria of the yeast, Saccharomyces cerevisiae. Involvement in synthesis and import of phospholipids into mitochondria. Biochim Biophys Acta 1234, 214-220.
    • (1995) Biochim. Biophys. Acta , vol.1234 , pp. 214-220
    • Gaigg, B.1    Simbeni, R.2    Hrastnik, C.3    Paltauf, F.4    Daum, G.5
  • 13
    • 0033637153 scopus 로고    scopus 로고
    • Genomic expression programs in the response of yeast cells to environmental changes
    • Gasch, A. P., Spellman, P. T., Kao, C. M., Carmel-Harel, O., Eisen, M. B., Storz, G., et al. (2000). Genomic expression programs in the response of yeast cells to environmental changes. Mol Biol Cell 11, 4241-4257.
    • (2000) Mol. Biol. Cell. , vol.11 , pp. 4241-4257
    • Gasch, A.P.1    Spellman, P.T.2    Kao, C.M.3    Carmel-Harel, O.4    Eisen, M.B.5    Storz, G.6
  • 15
    • 71849095133 scopus 로고    scopus 로고
    • Cause and consequence: Mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases
    • Gibson, G. E., Starkov, A., Blass, J. P., Ratan, R. R., and Beal, M. F. (2010). Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases. Biochim Biophys Acta 1802, 122-134.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 122-134
    • Gibson, G.E.1    Starkov, A.2    Blass, J.P.3    Ratan, R.R.4    Beal, M.F.5
  • 16
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi, C., De Stefani, D., Bononi, A., Rizzuto, R., and Pinton, P. (2009). Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int J Biochem Cell Biol 41, 1817-1827.
    • (2009) Int. J. Biochem. Cell. Biol. , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 17
    • 0030739963 scopus 로고    scopus 로고
    • Mitochondrial function is required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae
    • Grant, C. M., Maciver, F. H., and Dawes, I. W. (1997). Mitochondrial function is required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. FEBS Lett 410, 219-222.
    • (1997) FEBS Lett. , vol.410 , pp. 219-222
    • Grant, C.M.1    Maciver, F.H.2    Dawes, I.W.3
  • 18
    • 66349105304 scopus 로고    scopus 로고
    • Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
    • Greetham, D., and Grant, C. M. (2009). Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol Cell Biol 29, 3229-3240.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3229-3240
    • Greetham, D.1    Grant, C.M.2
  • 21
    • 0036211334 scopus 로고    scopus 로고
    • Osmotic adaptation in yeast-control of the yeast osmolyte system
    • Hohmann, S. (2002). Osmotic adaptation in yeast-control of the yeast osmolyte system. Int Rev Cytol 215, 149-187.
    • (2002) Int. Rev. Cytol , vol.215 , pp. 149-187
    • Hohmann, S.1
  • 22
    • 0034083942 scopus 로고    scopus 로고
    • Direct Blue 71 staining of proteins bound to blotting membranes
    • Hong, H. Y., Yoo, G. S., and Choi, J. K. (2000). Direct Blue 71 staining of proteins bound to blotting membranes. Electrophoresis 21, 841-845.
    • (2000) Electrophoresis , vol.21 , pp. 841-845
    • Hong, H.Y.1    Yoo, G.S.2    Choi, J.K.3
  • 25
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., et al. (2009). An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325, 477-481.
    • (2009) Science , vol.325 , pp. 477-481
    • Kornmann, B.1    Currie, E.2    Collins, S.R.3    Schuldiner, M.4    Nunnari, J.5    Weissman, J.S.6
  • 26
    • 18144367355 scopus 로고    scopus 로고
    • Antioxidants protect the yeast Saccharomyces cerevisiae against hypertonic stress
    • Koziol, S., Zagulski, M., Bilinski, T., and Bartosz, G. (2005). Antioxidants protect the yeast Saccharomyces cerevisiae against hypertonic stress. Free Radic Res 39, 365-371.
    • (2005) Free Radic Res. , vol.39 , pp. 365-371
    • Koziol, S.1    Zagulski, M.2    Bilinski, T.3    Bartosz, G.4
  • 27
    • 46749110071 scopus 로고    scopus 로고
    • Mitochondrial nucleoids undergo remodeling in response to metabolic cues
    • Kucej, M., Kucejova, B., Subramanian, R., Chen, X. J., and Butow, R. A. (2008). Mitochondrial nucleoids undergo remodeling in response to metabolic cues. J Cell Sci 121, 1861-1868.
    • (2008) J. Cell. Sci. , vol.121 , pp. 1861-1868
    • Kucej, M.1    Kucejova, B.2    Subramanian, R.3    Chen, X.J.4    Butow, R.A.5
  • 28
    • 0032750635 scopus 로고    scopus 로고
    • Biodiversity of the P450 catalytic cycle: Yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction
    • Lamb, D. C., Kelly, D. E., Manning, N. J., Kaderbhai, M. A., and Kelly, S. L. (1999). Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. FEBS Lett 462, 283-288.
    • (1999) FEBS Lett. , vol.462 , pp. 283-288
    • Lamb, D.C.1    Kelly, D.E.2    Manning, N.J.3    Kaderbhai, M.A.4    Kelly, S.L.5
  • 29
    • 0027445711 scopus 로고
    • HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases
    • Leonhardt, S. A., Fearson, K., Danese, P. N., and Mason, T. L. (1993). HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases. Mol Cell Biol 13, 6304-6313.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6304-6313
    • Leonhardt, S.A.1    Fearson, K.2    Danese, P.N.3    Mason, T.L.4
  • 30
    • 33845656956 scopus 로고    scopus 로고
    • Mitochondrial retrograde signaling
    • Liu, Z., and Butow, R. A. (2006). Mitochondrial retrograde signaling. Annu Rev Genet 40, 159-185.
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 159-185
    • Liu, Z.1    Butow, R.A.2
  • 31
    • 0022385984 scopus 로고
    • Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes
    • McAlister, L., and Holland, M. J. (1985). Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260, 15019-15027.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15019-15027
    • McAlister, L.1    Holland, M.J.2
  • 32
    • 33746016268 scopus 로고    scopus 로고
    • Mitochondria: More than just a powerhouse
    • McBride, H. M., Neuspiel, M., and Wasiak, S. (2006). Mitochondria: more than just a powerhouse. Curr Biol 16, R551-R560.
    • (2006) Curr. Biol. , vol.16
    • McBride, H.M.1    Neuspiel, M.2    Wasiak, S.3
  • 33
    • 0034672334 scopus 로고    scopus 로고
    • Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations
    • Meisinger, C., Sommer, T., and Pfanner, N. (2000). Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations. Anal Biochem 287, 339-342.
    • (2000) Anal. Biochem. , vol.287 , pp. 339-342
    • Meisinger, C.1    Sommer, T.2    Pfanner, N.3
  • 34
    • 65549106475 scopus 로고    scopus 로고
    • Two sources of mitochondrial NADPH in the yeast Saccharomyces cerevisiae
    • Miyagi, H., Kawai, S., and Murata, K. (2009). Two sources of mitochondrial NADPH in the yeast Saccharomyces cerevisiae. J Biol Chem 284, 7553-7560.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7553-7560
    • Miyagi, H.1    Kawai, S.2    Murata, K.3
  • 35
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P. (2009). How mitochondria produce reactive oxygen species. Biochem J 417, 1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 36
    • 0031040998 scopus 로고    scopus 로고
    • Molecular characterization of GCV3, the Saccharomyces cerevisiae gene coding for the glycine cleavage system hydrogen carrier protein
    • Nagarajan, L., and Storms, R. K. (1997). Molecular characterization of GCV3, the Saccharomyces cerevisiae gene coding for the glycine cleavage system hydrogen carrier protein. J Biol Chem 272, 4444-4450.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4444-4450
    • Nagarajan, L.1    Storms, R.K.2
  • 37
    • 66149163332 scopus 로고    scopus 로고
    • Dynamic and complex transcription factor binding during an inducible response in yeast
    • Ni, L., Bruce, C., Hart, C., Leigh-Bell, J., Gelperin, D., Umansky, L., et al. (2009). Dynamic and complex transcription factor binding during an inducible response in yeast. Genes Dev 23, 1351-1363.
    • (2009) Genes Dev. , vol.23 , pp. 1351-1363
    • Ni, L.B.C.1    Hart, C.2    Leigh-Bell, J.3    Gelperin, D.4    Umansky, L.5
  • 38
    • 0031952124 scopus 로고    scopus 로고
    • Amino acid uptake is strongly affected during exponential growth of Saccharomyces cerevisiae in 0.7M NaCl medium
    • Norbeck, J., and Blomberg, A. (1998). Amino acid uptake is strongly affected during exponential growth of Saccharomyces cerevisiae in 0.7M NaCl medium. FEMS Microbiol Lett 158, 121-126.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 121-126
    • Norbeck, J.1    Blomberg, A.2
  • 39
    • 67349113204 scopus 로고    scopus 로고
    • Pathophysiology of mitochondrial volume homeostasis: Potassium transport and permeability transition
    • Nowikovsky, K., Schweyen, R. J., and Bernardi, P. (2009). Pathophysiology of mitochondrial volume homeostasis: potassium transport and permeability transition. Biochim Biophys Acta 1787, 345-350.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 345-350
    • Nowikovsky, K.1    Schweyen, R.J.2    Bernardi, P.3
  • 40
    • 34249865334 scopus 로고    scopus 로고
    • Extracting the hidden features in saline osmotic tolerance in Saccharomyces cerevisiae from DNA microarray data using the self-organizing map: Biosynthesis of amino acids
    • Pandey, G., Yoshikawa, K., Hirasawa, T., Nagahisa, K., Katakura, Y., Furusawa, C., et al. (2007). Extracting the hidden features in saline osmotic tolerance in Saccharomyces cerevisiae from DNA microarray data using the self-organizing map: biosynthesis of amino acids. Appl Microbiol Biotechnol 75, 415-426.
    • (2007) Appl. Microbiol. Biotechnol. , vol.75 , pp. 415-426
    • Pandey, G.1    Yoshikawa, K.2    Hirasawa, T.3    Nagahisa, K.4    Katakura, Y.5    Furusawa, C.6
  • 41
    • 0034747684 scopus 로고    scopus 로고
    • The Sko1p repressor and Gcn4p activator antagonistically modulate stress-regulated transcription in Saccharomyces cerevisiae
    • Pascual-Ahuir, A., Serrano, R., and Proft, M. (2001). The Sko1p repressor and Gcn4p activator antagonistically modulate stress-regulated transcription in Saccharomyces cerevisiae. Mol Cell Biol 21, 16-25.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 16-25
    • Pascual-Ahuir, A.1    Serrano, R.2    Proft, M.3
  • 42
    • 71049129777 scopus 로고    scopus 로고
    • Mitochondrial function is an inducible determinant of osmotic stress adaptation in yeast
    • Pastor, M. M., Proft, M., and Pascual-Ahuir, A. (2009). Mitochondrial function is an inducible determinant of osmotic stress adaptation in yeast. J Biol Chem 284, 30307-30317.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30307-30317
    • Pastor, M.M.1    Proft, M.2    Pascual-Ahuir, A.3
  • 43
    • 0034717135 scopus 로고    scopus 로고
    • Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity
    • Pedrajas, J. R., Miranda-Vizuete, A., Javanmardy, N., Gustafsson, J. A., and Spyrou, G. (2000). Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J Biol Chem 275, 16296-16301.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16296-16301
    • Pedrajas, J.R.1    Miranda-Vizuete, A.2    Javanmardy, N.3    Gustafsson, J.A.4    Spyrou, G.5
  • 44
    • 46549088173 scopus 로고    scopus 로고
    • Reactive oxygen species and yeast apoptosis
    • Perrone, G. G., Tan, S. X., and Dawes, I. W. (2008). Reactive oxygen species and yeast apoptosis. Biochim Biophys Acta 1783, 1354-1368.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1354-1368
    • Perrone, G.G.1    Tan, S.X.2    Dawes, I.W.3
  • 45
    • 35248824214 scopus 로고    scopus 로고
    • Mitochondria-endoplasmic reticulum choreography: Structure and signaling dynamics
    • Pizzo, P., and Pozzan, T. (2007). Mitochondria-endoplasmic reticulum choreography: structure and signaling dynamics. Trends Cell Biol 17, 511-517.
    • (2007) Trends Cell. Biol. , vol.17 , pp. 511-517
    • Pizzo, P.1    Pozzan, T.2
  • 47
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • Reinders, J., Zahedi, R. P., Pfanner, N., Meisinger, C., and Sickmann, A. (2006). Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5, 1543-1554.
    • (2006) J. Proteome Res. , vol.5 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 48
    • 36749053957 scopus 로고    scopus 로고
    • Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase
    • Reinders, J., Wagner, K., Zahedi, R. P., Stojanovski, D., Eyrich, B., van der Laan, M., et al. (2007). Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6, 1896-1906.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1896-1906
    • Reinders, J.1    Wagner, K.2    Zahedi, R.P.3    Stojanovski, D.4    Eyrich, B.5    Van Der Laan, M.6
  • 49
    • 0034708436 scopus 로고    scopus 로고
    • The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathwaydependent genes
    • Rep, M., Krantz, M., Thevelein, J. M., and Hohmann, S. (2000). The transcriptional response of Saccharomyces cerevisiae to osmotic shock. Hot1p and Msn2p/Msn4p are required for the induction of subsets of high osmolarity glycerol pathwaydependent genes. J Biol Chem 275, 8290-8300.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8290-8300
    • Rep, M.1    Krantz, M.2    Thevelein, J.M.3    Hohmann, S.4
  • 50
    • 0029045002 scopus 로고
    • Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70
    • Schmitt, M., Neupert, W., and Langer, T. (1995). Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70. EMBO J 14, 3434-3444.
    • (1995) EMBO J. , vol.14 , pp. 3434-3444
    • Schmitt, M.1    Neupert, W.2    Langer, T.3
  • 51
    • 0037774738 scopus 로고    scopus 로고
    • Transcriptional control of nonfermentative metabolism in the yeast Saccharomyces cerevisiae
    • Schuller, H. J. (2003). Transcriptional control of nonfermentative metabolism in the yeast Saccharomyces cerevisiae. Curr Genet 43, 139-160.
    • (2003) Curr. Genet. , vol.43 , pp. 139-160
    • Schuller, H.J.1
  • 52
    • 33644959683 scopus 로고    scopus 로고
    • Mitochondrial respiration and reactive oxygen species in mitochondrial aging mutants
    • Sedensky, M. M., and Morgan, P. G. (2006). Mitochondrial respiration and reactive oxygen species in mitochondrial aging mutants. Exp Gerontol 41, 237-245.
    • (2006) Exp. Gerontol. , vol.41 , pp. 237-245
    • Sedensky, M.M.1    Morgan, P.G.2
  • 53
    • 0018951988 scopus 로고
    • The amino acid sequence of copper-zinc superoxide dismutase from bakers' yeast
    • Steinman, H. M. (1980). The amino acid sequence of copper-zinc superoxide dismutase from bakers' yeast. J Biol Chem 255, 6758-6765.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6758-6765
    • Steinman, H.M.1
  • 54
    • 2342487990 scopus 로고    scopus 로고
    • Cells have distinct mechanisms to maintain protection against different reactive oxygen species: Oxidativestress-response genes
    • Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004). Cells have distinct mechanisms to maintain protection against different reactive oxygen species: oxidativestress-response genes. Proc Natl Acad Sci USA 101, 6564-6569.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6564-6569
    • Thorpe, G.W.1    Fong, C.S.2    Alic, N.3    Higgins, V.J.4    Dawes, I.W.5
  • 55
    • 34248195476 scopus 로고    scopus 로고
    • Endogenous synthesis of coenzyme Q in eukaryotes
    • Tran, U. C., and Clarke, C. F. (2007). Endogenous synthesis of coenzyme Q in eukaryotes. Mitochondrion 7 (Suppl), S62-S71.
    • (2007) Mitochondrion , vol.7 , Issue.SUPPL.
    • Tran, U.C.1    Clarke, C.F.2
  • 57
    • 0033529707 scopus 로고    scopus 로고
    • Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis
    • Winzeler, E. A., Shoemaker, D. D., Astromoff, A., Liang, H., Anderson, K., Andre, B., et al. (1999). Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285, 901-906.
    • (1999) Science , vol.285 , pp. 901-906
    • Winzeler, E.A.1    Shoemaker, D.D.2    Astromoff, A.3    Liang, H.4    Anderson, K.5    Andre, B.6
  • 58
    • 33644912080 scopus 로고    scopus 로고
    • Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins
    • Zahedi, R. P., Sickmann, A., Boehm, A. M., Winkler, C., Zufall, N., Schonfisch, B., et al. (2006). Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins. Mol Biol Cell 17, 1436-1450.
    • (2006) Mol. Biol. Cell. , vol.17 , pp. 1436-1450
    • Zahedi, R.P.1    Sickmann, A.2    Boehm, A.M.3    Winkler, C.4    Zufall, N.5    Schonfisch, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.