메뉴 건너뛰기




Volumn 163, Issue 1, 2003, Pages 35-46

SOD2 functions downstream of Sch9 to extend longevity in yeast

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; COPPER ZINC SUPEROXIDE DISMUTASE; MANGANESE SUPEROXIDE DISMUTASE; SUPEROXIDE DISMUTASE;

EID: 0037280096     PISSN: 00166731     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (303)

References (59)
  • 1
    • 0033529926 scopus 로고    scopus 로고
    • Passage through stationary phase advances replicative aging in Saccharomyces cerevisae
    • ASHRAFI,K., D. SINCLAIR, J. I. and L. GUARENTE, 1999. Passage through stationary phase advances replicative aging in Saccharomyces cerevisae. Proc. Natl. Acad. Sci. USA 96:9100-9105.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9100-9105
    • Ashrafi, K.1    Sinclair, D.J.I.2    Guarente, L.3
  • 2
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide
    • BOVERIS, A., and B. CHANCE, 1973 The mitochondrial generation of hydrogen peroxide. Biochem. J. 134: 707-716.
    • (1973) Biochem. J. , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 3
    • 0031910875 scopus 로고    scopus 로고
    • Msn2p and Msn4p control a large number of genes induced at the diauxic transition which are repressed by cyclic AMP in Saccharomyces cerevisiae
    • BOY-MARCOTTE, E., M. PERROT, F. BUSSEREAU, H. BOUCHERIE and M. JACQUET, 1998 Msn2p and Msn4p control a large number of genes induced at the diauxic transition which are repressed by cyclic AMP in Saccharomyces cerevisiae. J. Bacteriol. 180: 1044-1052.
    • (1998) J. Bacteriol. , vol.180 , pp. 1044-1052
    • Boy-Marcotte, E.1    Perrot, M.2    Bussereau, F.3    Boucherie, H.4    Jacquet, M.5
  • 4
    • 0034647439 scopus 로고    scopus 로고
    • Diverse Caenorhabditis elegans genes that are upregulated in dauer larvae also show elevated transcript levels in long-lived, aged, or starved adults
    • CHERKASOVA, V., S. AYYADEVARA, N. EGILMEZ and R. S. REIS, 2000 Diverse Caenorhabditis elegans genes that are upregulated in dauer larvae also show elevated transcript levels in long-lived, aged, or starved adults. J. Mol. Biol. 300: 433-448.
    • (2000) J. Mol. Biol. , vol.300 , pp. 433-448
    • Cherkasova, V.1    Ayyadevara, S.2    Egilmez, N.3    Reis, R.S.4
  • 5
    • 0029799910 scopus 로고    scopus 로고
    • Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids
    • DO, T. Q., J. R. SCHULTZ and C. F. CLARKE, 1996 Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids. Proc. Natl. Acad. Sci. USA 93: 7534-7539.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7534-7539
    • Do, T.Q.1    Schultz, J.R.2    Clarke, C.F.3
  • 6
    • 0027253092 scopus 로고
    • Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae
    • ESTRUCH, F., and M. CARLSON, 1993 Two homologous zinc finger genes identified by multicopy suppression in a SNF1 protein kinase mutant of Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 3872-3881.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3872-3881
    • Estruch, F.1    Carlson, M.2
  • 7
    • 0035853552 scopus 로고    scopus 로고
    • Regulation of longevity and stress resistance by Sch9 in yeast
    • FABRIZIO, P., F. POZZA, S. D. PLETCHER, C. M. GENDRON and V. D. LONGO, 2001 Regulation of longevity and stress resistance by Sch9 in yeast. Science 292: 288-290.
    • (2001) Science , vol.292 , pp. 288-290
    • Fabrizio, P.1    Pozza, F.2    Pletcher, S.D.3    Gendron, C.M.4    Longo, V.D.5
  • 8
    • 0031032296 scopus 로고    scopus 로고
    • Stationary-phase regulation of the Saccharomyces cerevisiae SOD2 gene is dependent on additive effects of HAP2/3/4/5- and STRE-binding elements
    • FLATTERY-O'BRIEN, J. A., C. M. GRANT and I. W. DAWES, 1997 Stationary-phase regulation of the Saccharomyces cerevisiae SOD2 gene is dependent on additive effects of HAP2/3/4/5- and STRE-binding elements. Mol. Microbiol. 23: 303-312.
    • (1997) Mol. Microbiol. , vol.23 , pp. 303-312
    • Flattery-O'Brien, J.A.1    Grant, C.M.2    Dawes, I.W.3
  • 9
    • 0001531847 scopus 로고    scopus 로고
    • Iron-sulfur proteins with nonredox functions
    • FLINT, D. H., and R. M. ALLEN, 1996 Iron-sulfur proteins with nonredox functions. Chem. Rev. 96: 2315-2334.
    • (1996) Chem. Rev. , vol.96 , pp. 2315-2334
    • Flint, D.H.1    Allen, R.M.2
  • 10
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • FLINT, D. H., J. F. TUMINELLO and M. H. EMPTAGE., 1993 The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J. Biol. Chem. 268: 22369-22376.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 11
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • FRIDOVICH, I., 1995 Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64: 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 12
    • 0029064257 scopus 로고
    • Superoxide radical and iron modulate aconitase activity in mammalian cells
    • GARDNER, P. R., I. RAINERI, L. B. EPSTEIN and C. W. WHITE, 1995 Superoxide radical and iron modulate aconitase activity in mammalian cells. J. Biol. Chem. 270: 13399-13405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13399-13405
    • Gardner, P.R.1    Raineri, I.2    Epstein, L.B.3    White, C.W.4
  • 13
    • 0021288819 scopus 로고
    • Subcellular distribution of superoxide dismutases in rat liver
    • GELLER, B. L., and D. R. WINGE, 1984 Subcellular distribution of superoxide dismutases in rat liver. Methods Enzymol. 105: 105-114.
    • (1984) Methods Enzymol. , vol.105 , pp. 105-114
    • Geller, B.L.1    Winge, D.R.2
  • 14
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • GIETZ, D., A. ST. JEAN, R. A. WOODS and R. H. SCHIESTL, 1992 Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20: 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 15
    • 0025938799 scopus 로고
    • Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: Characterization and spontaneous mutation rates
    • GRALLA, E. B., and J. S. VALENTINE, 1991 Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: characterization and spontaneous mutation rates. J. Bacteriol. 173: 5918-5920.
    • (1991) J. Bacteriol. , vol.173 , pp. 5918-5920
    • Gralla, E.B.1    Valentine, J.S.2
  • 16
    • 0025953705 scopus 로고
    • Glucose induces cAMP-independent growth-related changes in stationary-phase cells of Saccharomyces cerevisiae
    • GRANOT, D., and M. SNYDER, 1991 Glucose induces cAMP-independent growth-related changes in stationary-phase cells of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88: 5724-5728.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5724-5728
    • Granot, D.1    Snyder, M.2
  • 17
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • HAN, D., E. WILLIAMS and E. CADENAS, 2001 Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 353: 411-416.
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 18
    • 0017139230 scopus 로고
    • A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine
    • HEIKKILA, R. E., and C. FELICITAS, 1976 A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine. Anal. Biochem. 75: 356-362.
    • (1976) Anal. Biochem. , vol.75 , pp. 356-362
    • Heikkila, R.E.1    Felicitas, C.2
  • 19
    • 0032782364 scopus 로고    scopus 로고
    • The daf-2 gene network for longevity regulates oxidative stress resistance and Mn-superoxide dismutase gene expression in Caenorhabditis elegans
    • HONDA, Y., and S. HONDA, 1999 The daf-2 gene network for longevity regulates oxidative stress resistance and Mn-superoxide dismutase gene expression in Caenorhabditis elegans. FASEB J. 13:1385-1393.
    • (1999) FASEB J. , vol.13 , pp. 1385-1393
    • Honda, Y.1    Honda, S.2
  • 20
    • 0030016821 scopus 로고    scopus 로고
    • Longevity, genes, and aging
    • JAZWINSKI, S. M., 1996 Longevity, genes, and aging. Science 273: 54-59.
    • (1996) Science , vol.273 , pp. 54-59
    • Jazwinski, S.M.1
  • 21
    • 0025004091 scopus 로고
    • Increased life-span of age-1 mutants in Caenorhabditis elegans and lower Gompertz rate of aging
    • JOHNSON, T. E., 1990 Increased life-span of age-1 mutants in Caenorhabditis elegans and lower Gompertz rate of aging. Science 249: 908-912.
    • (1990) Science , vol.249 , pp. 908-912
    • Johnson, T.E.1
  • 22
    • 0027717968 scopus 로고
    • Bcl-2 inhibition of neural death: Decreased generation of reactive oxygen species
    • KANE, D. J., T. A. SARAFIAN, R. ANTON, H. HAHN, E. B. GRALLA et al., 1993 Bcl-2 inhibition of neural death: decreased generation of reactive oxygen species. Science 262: 1274-1277.
    • (1993) Science , vol.262 , pp. 1274-1277
    • Kane, D.J.1    Sarafian, T.A.2    Anton, R.3    Hahn, H.4    Gralla, E.B.5
  • 24
    • 0035917440 scopus 로고    scopus 로고
    • A conserved regulatory system for aging
    • KENYON, C., 2001 A conserved regulatory system for aging. Cell 105: 165-168.
    • (2001) Cell , vol.105 , pp. 165-168
    • Kenyon, C.1
  • 25
    • 0027771804 scopus 로고
    • A C. elegans mutant that lives twice as long as wild type
    • KENYON, C., J. CHANG, E. GENSCH, A. RUDNER and R. TABTIANG, 1993 A C. elegans mutant that lives twice as long as wild type. Nature 366: 461-464.
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 26
    • 0030813398 scopus 로고    scopus 로고
    • daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans
    • KIMURA, K. D., H. A. TISSENBAUM, Y. LIU and G. RUVKUN, 1997 daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans. Science 277: 942-946.
    • (1997) Science , vol.277 , pp. 942-946
    • Kimura, K.D.1    Tissenbaum, H.A.2    Liu, Y.3    Ruvkun, G.4
  • 27
    • 0027515616 scopus 로고
    • Aging and resistance to oxidative damage in Caenorhabditis elegans
    • LARSEN, P. L., 1993 Aging and resistance to oxidative damage in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 90: 8905-8909.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8905-8909
    • Larsen, P.L.1
  • 28
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • LI, Y., T. T. HUANG, E. J. CARLSON, S. MELOV, P. C. URSELL et al., 1995 Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat. Genet. 11: 376-381.
    • (1995) Nat. Genet. , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3    Melov, S.4    Ursell, P.C.5
  • 29
    • 0019187844 scopus 로고
    • Reserve carbohydrate metabolism in Saccharomyces cerevisiae: Response to nutrient limitation
    • LILLIE, S. H., and J. R. PRINGLE, 1980 Reserve carbohydrate metabolism in Saccharomyces cerevisiae: response to nutrient limitation. J. Bacteriol. 143: 1384-1394.
    • (1980) J. Bacteriol. , vol.143 , pp. 1384-1394
    • Lillie, S.H.1    Pringle, J.R.2
  • 30
    • 0030657540 scopus 로고    scopus 로고
    • daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans
    • LIN, K., J. B. DORMAN, A. RODAN and C. KENYON, 1997 daf-16: an HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans. Science 278: 1319-1322.
    • (1997) Science , vol.278 , pp. 1319-1322
    • Lin, K.1    Dorman, J.B.2    Rodan, A.3    Kenyon, C.4
  • 31
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and S/R2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • LIN, S. J., P. A. DEFOSSEZ and L. GUARENTE, 2000 Requirement of NAD and S/R2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science 289: 2126-2128.
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 32
    • 0029123058 scopus 로고
    • Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress
    • LITHGOW, G. J., T. M. WHITE, S. MELOV and T. E. JOHNSON, 1995 Thermotolerance and extended life-span conferred by single-gene mutations and induced by thermal stress. Proc. Natl. Acad. Sci. USA 92: 7540-7544.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7540-7544
    • Lithgow, G.J.1    White, T.M.2    Melov, S.3    Johnson, T.E.4
  • 33
  • 34
    • 0033405860 scopus 로고    scopus 로고
    • Mutations in signal transduction proteins increase stress resistance and longevity in yeast, nematodes, fruit flies, and mammalian neuronal cells
    • LONGO, V. D., 1999 Mutations in signal transduction proteins increase stress resistance and longevity in yeast, nematodes, fruit flies, and mammalian neuronal cells. Neurobiol. Aging 20: 479-486.
    • (1999) Neurobiol. Aging , vol.20 , pp. 479-486
    • Longo, V.D.1
  • 35
    • 0036306657 scopus 로고    scopus 로고
    • Regulation of longevity and stress resistance: A molecular strategy conserved from yeast to humans?
    • LONGO, V. D., and P. FABRIZIO, 2002 Regulation of longevity and stress resistance: A molecular strategy conserved from yeast to humans? Cell. Mol. Life Sci. 59: 903-908.
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 903-908
    • Longo, V.D.1    Fabrizio, P.2
  • 36
    • 15844429977 scopus 로고    scopus 로고
    • Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo
    • LONGO, V. D., E. B. GRALLA and J. S. VALENTINE, 1996 Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo. J. Biol. Chem. 271: 12275-12280.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12275-12280
    • Longo, V.D.1    Gralla, E.B.2    Valentine, J.S.3
  • 37
    • 0031009829 scopus 로고    scopus 로고
    • Human Bcl-2 reverses survival defects in yeast lacking superoxide dismutase and delays death of wild-type yeast
    • LONGO, V. D., L. M. ELLERBY, D. E. BREDESEN, J. S. VALENTINE and E. B. GRALLA, 1997 Human Bcl-2 reverses survival defects in yeast lacking superoxide dismutase and delays death of wild-type yeast. J. Cell Biol. 137: 1581-1588.
    • (1997) J. Cell Biol. , vol.137 , pp. 1581-1588
    • Longo, V.D.1    Ellerby, L.M.2    Bredesen, D.E.3    Valentine, J.S.4    Gralla, E.B.5
  • 38
    • 0033134233 scopus 로고    scopus 로고
    • Mitochondrial superoxide decreases yeast survival in stationary phase
    • LONGO, V. D., L. L. LIOU, J. S. VALENTINE and E. B. GRALLA, 1999 Mitochondrial superoxide decreases yeast survival in stationary phase. Arch. Biochem. Biophys. 365: 131-142.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 131-142
    • Longo, V.D.1    Liou, L.L.2    Valentine, J.S.3    Gralla, E.B.4
  • 39
    • 0029879360 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress-response element (STRE)
    • MARTINEZ-PASTOR, M. T., G. MARCHLER, C. SCHULLER, A. MARCHLER-BAUER, H. RUIS et al, 1996 The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress-response element (STRE). EMBO J. 15: 2227-2235.
    • (1996) EMBO J. , vol.15 , pp. 2227-2235
    • Martinez-Pastor, M.T.1    Marchler, G.2    Schuller, C.3    Marchler-Bauer, A.4    Ruis, H.5
  • 40
    • 0020429672 scopus 로고
    • Recombination between genes located on nonhomologous chromosomes in Saccharomyces cerevisiae
    • MIKUS, M. D. and T. D. PETES, 1982 Recombination between genes located on nonhomologous chromosomes in Saccharomyces cerevisiae. Genetics 101: 369-404.
    • (1982) Genetics , vol.101 , pp. 369-404
    • Mikus, M.D.1    Petes, T.D.2
  • 41
    • 0033230459 scopus 로고    scopus 로고
    • The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo
    • MORANO, K. A., and D. J. THIELE, 1999 The Sch9 protein kinase regulates Hsp90 chaperone complex signal transduction activity in vivo. EMBO J. 18: 5953-5962.
    • (1999) EMBO J. , vol.18 , pp. 5953-5962
    • Morano, K.A.1    Thiele, D.J.2
  • 42
    • 0029768753 scopus 로고    scopus 로고
    • A phospatidyl-inositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans
    • MORRIS, J. Z., H. A. TISSENBAUM and G. RUVKUN, 1996 A phospatidyl-inositol-3-OH kinase family member regulating longevity and diapause in Caenorhabditis elegans. Nature 382: 536-539.
    • (1996) Nature , vol.382 , pp. 536-539
    • Morris, J.Z.1    Tissenbaum, H.A.2    Ruvkun, G.3
  • 43
    • 0023906045 scopus 로고
    • Arginine 328 of the beta-subunit of the mitochondrial ATPase in yeast is essential for protein stability
    • MUELLER, D. M., 1988 Arginine 328 of the beta-subunit of the mitochondrial ATPase in yeast is essential for protein stability. J. Biol. Chem. 263: 5634-5639.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5634-5639
    • Mueller, D.M.1
  • 44
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • OKADO-MATSUMOTO, A., and I. FRIDOVICH, 2001 Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J. Biol. Chem. 276: 38388-38393.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 45
    • 0342657757 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ras/cAMP pathway controls post-diauxic shift element-dependent transcription through the zinc finger protein Gisl
    • PEDRUZZI, I., N. BURCKERT, P. EGGER and C. DE VIRGILIO, 2000 Saccharomyces cerevisiae Ras/cAMP pathway controls post-diauxic shift element-dependent transcription through the zinc finger protein Gisl. EMBO J. 19: 2569-2579.
    • (2000) EMBO J. , vol.19 , pp. 2569-2579
    • Pedruzzi, I.1    Burckert, N.2    Egger, P.3    De Virgilio, C.4
  • 46
    • 0033618376 scopus 로고    scopus 로고
    • Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis
    • POON, W. W., R. J. BARKOVICH, A. Y. HSU, A. FRANKEL, P. T. LEE et al., 1999 Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis. J. Biol. Chem. 274: 21665-21672.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21665-21672
    • Poon, W.W.1    Barkovich, R.J.2    Hsu, A.Y.3    Frankel, A.4    Lee, P.T.5
  • 47
    • 0000342177 scopus 로고
    • Spectrophotometric measurements of the enzymatic formation of fumaric acid and cis-aconitic acid
    • RACKER, E., 1950 Spectrophotometric measurements of the enzymatic formation of fumaric acid and cis-aconitic acid. Biochim. Biophys. Acta 4: 211-214.
    • (1950) Biochim. Biophys. Acta , vol.4 , pp. 211-214
    • Racker, E.1
  • 48
    • 0031587849 scopus 로고    scopus 로고
    • 14-3-3 Proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae
    • ROBERTS, R. L., H. U. MOSCH and G. R. FINK, 1997 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Cell 89: 1055-1065.
    • (1997) Cell , vol.89 , pp. 1055-1065
    • Roberts, R.L.1    Mosch, H.U.2    Fink, G.R.3
  • 49
    • 0029395010 scopus 로고
    • Stress signaling in yeast
    • RUIS, H., and C. SCHULLER, 1995 Stress signaling in yeast. Bioessays 17: 959-965.
    • (1995) Bioessays , vol.17 , pp. 959-965
    • Ruis, H.1    Schuller, C.2
  • 50
    • 0030820491 scopus 로고    scopus 로고
    • Accelerated aging and nucleolar fragmentation in yeast sgs1 mutants
    • SINCLAIR, D. A., K. MILLS and L. GUARENTE, 1997 Accelerated aging and nucleolar fragmentation in yeast sgs1 mutants. Science 277: 1313-1316.
    • (1997) Science , vol.277 , pp. 1313-1316
    • Sinclair, D.A.1    Mills, K.2    Guarente, L.3
  • 52
    • 0032127462 scopus 로고    scopus 로고
    • Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation
    • SMITH, A., M. P. WARD and S. GARRETT, 1998 Yeast PKA represses Msn2p/Msn4p-dependent gene expression to regulate growth, stress response and glycogen accumulation. EMBO J. 17: 3556-3564.
    • (1998) EMBO J. , vol.17 , pp. 3556-3564
    • Smith, A.1    Ward, M.P.2    Garrett, S.3
  • 53
    • 0032835137 scopus 로고    scopus 로고
    • Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae
    • THEVELEIN, J. M., and J. H. DE WINDE, 1999 Novel sensing mechanisms and targets for the cAMP-protein kinase A pathway in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 33: 904-918.
    • (1999) Mol. Microbiol. , vol.33 , pp. 904-918
    • Thevelein, J.M.1    De Winde, J.H.2
  • 54
    • 0021967321 scopus 로고
    • In yeast, RAS proteins are controlling elements of adenylate cyclase
    • TODA, T., I. UNO, T. ISHIKAWA, S. POWERS, T. KATAOKA et al., 1985 In yeast, RAS proteins are controlling elements of adenylate cyclase. Cell 40: 27-36.
    • (1985) Cell , vol.40 , pp. 27-36
    • Toda, T.1    Uno, I.2    Ishikawa, T.3    Powers, S.4    Kataoka, T.5
  • 55
    • 0024009008 scopus 로고
    • SCH9, a gene of Saccharomyces cerevisiae that encodes a protein distinct from, but functionally and structurally related to, cAMP-dependent protein kinase catalytic subunits
    • TODA, T., S. CAMERON, P. SASS and M. WIGLER, 1988 SCH9, a gene of Saccharomyces cerevisiae that encodes a protein distinct from, but functionally and structurally related to, cAMP-dependent protein kinase catalytic subunits. Genes Dev. 2: 517-527.
    • (1988) Genes Dev. , vol.2 , pp. 517-527
    • Toda, T.1    Cameron, S.2    Sass, P.3    Wigler, M.4
  • 56
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • TURRENS, J. F., A. ALEXANDER, and A. L. LEHNINGER, 1985 Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237: 408-414.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexander, A.2    Lehninger, A.L.3
  • 59
    • 0030602818 scopus 로고    scopus 로고
    • GASPing for life in stationary phase
    • ZAMBRANO, M. M., and R. KOLTER, 1996 GASPing for life in stationary phase. Cell 86: 181-184.
    • (1996) Cell , vol.86 , pp. 181-184
    • Zambrano, M.M.1    Kolter, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.