메뉴 건너뛰기




Volumn 22, Issue 11, 2005, Pages 835-894

A history of research on yeasts 9: Regulation of sugar metabolism

Author keywords

[No Author keywords available]

Indexed keywords

6 PHOSPHOFRUCTOKINASE; HEXOKINASE; SUGAR;

EID: 25844501539     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/yea.1249     Document Type: Review
Times cited : (89)

References (402)
  • 1
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. 2003. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5: 417-421.
    • (2003) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 2
    • 0019346174 scopus 로고
    • IMP1/imp1: A gene involved in the nucleo-mitochondrial control of galactose fermentation in Saccharomyces cerevisiae
    • Algeri AA, Bianchi L, Viola AM, Puglisi PP, Marmiroli N. 1981. IMP1/imp1: a gene involved in the nucleo-mitochondrial control of galactose fermentation in Saccharomyces cerevisiae. Genetics 97: 27-44.
    • (1981) Genetics , vol.97 , pp. 27-44
    • Algeri, A.A.1    Bianchi, L.2    Viola, A.M.3    Puglisi, P.P.4    Marmiroli, N.5
  • 3
    • 0033517106 scopus 로고    scopus 로고
    • Reg1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cerevisiae characterizing the effects of a phosphatase subunit on the yeast proteome
    • Alms GR, Sanz P, Carlson M, Haystead TAJ. 1999. Reg1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cerevisiae characterizing the effects of a phosphatase subunit on the yeast proteome. EMBO Journal 18: 4157-4168.
    • (1999) EMBO Journal , vol.18 , pp. 4157-4168
    • Alms, G.R.1    Sanz, P.2    Carlson, M.3    Haystead, T.A.J.4
  • 4
    • 0002587184 scopus 로고
    • Anaerobic nutrition of Saccharomyces cerevisiae I. Ergosterol requirement for growth in a defined medium
    • Andreasen AA, Stier TJB. 1953. Anaerobic nutrition of Saccharomyces cerevisiae I. Ergosterol requirement for growth in a defined medium. Journal of Cellular and Comparative Physiology 41: 23-36.
    • (1953) Journal of Cellular and Comparative Physiology , vol.41 , pp. 23-36
    • Andreasen, A.A.1    Stier, T.J.B.2
  • 5
    • 0000493179 scopus 로고
    • Anaerobic nutrition of Saccharomyces cerevisiae II. Unsaturated fatty acid requirement for growth in a defined medium
    • Andreasen AA, Stier TJB. 1954. Anaerobic nutrition of Saccharomyces cerevisiae II. Unsaturated fatty acid requirement for growth in a defined medium. Journal of Cellular and Comparative Physiology 43: 271-281.
    • (1954) Journal of Cellular and Comparative Physiology , vol.43 , pp. 271-281
    • Andreasen, A.A.1    Stier, T.J.B.2
  • 6
    • 25844462324 scopus 로고
    • Crabtree, Herbert Grace
    • Anon
    • Anon 1967. Crabtree, Herbert Grace. Chemistry in Britain 3: 314.
    • (1967) Chemistry in Britain , vol.3 , pp. 314
  • 7
    • 25844483012 scopus 로고
    • Dr Hans Laser
    • Anon for 1980
    • Anon 1980. Dr Hans Laser. Lancet (vol. I for 1980): 270.
    • (1980) Lancet , vol.1 , pp. 270
  • 8
    • 25844527131 scopus 로고
    • Dean Burk, 84, chemist for Cancer Institute
    • Anon 10 October
    • Anon 1988. Dean Burk, 84, chemist for Cancer Institute. New York Times 10 October: 8.
    • (1988) New York Times , pp. 8
  • 10
    • 25844458174 scopus 로고
    • Professor Walter Bartley
    • Anon 2 September
    • Anon 1994. Professor Walter Bartley. The Times 2 September: 19.
    • (1994) The Times , pp. 19
  • 11
    • 0024285837 scopus 로고
    • Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome)
    • Arrigo A-P, Tanaka K, Goldberg AL, Welch WJ. 1988. Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature 331: 192-194.
    • (1988) Nature , vol.331 , pp. 192-194
    • Arrigo, A.-P.1    Tanaka, K.2    Goldberg, A.L.3    Welch, W.J.4
  • 12
    • 0032476052 scopus 로고    scopus 로고
    • A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase
    • Ashrafi K, Farazi TA, Gordon JI. 1998. A role for Saccharomyces cerevisiae fatty acid activation protein 4 in regulating protein N-myristoylation during entry into stationary phase. Journal of Biological Chemistry 273: 25864-25874.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 25864-25874
    • Ashrafi, K.1    Farazi, T.A.2    Gordon, J.I.3
  • 14
    • 0021288735 scopus 로고
    • Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae
    • Bailey RB, Woodword A. 1984. Isolation and characterization of a pleiotropic glucose repression resistant mutant of Saccharomyces cerevisiae. Molecular and General Genetics 193: 507-512.
    • (1984) Molecular and General Genetics , vol.193 , pp. 507-512
    • Bailey, R.B.1    Woodword, A.2
  • 15
    • 25844504175 scopus 로고
    • Walter Bartley - 1916-1994
    • Feb/Mar
    • Banks P. 1995. Walter Bartley - 1916-1994. The Biochemist Feb/Mar: 43-44.
    • (1995) The Biochemist , pp. 43-44
    • Banks, P.1
  • 16
    • 25844507027 scopus 로고
    • The biochemical differentiation of taxa, with special reference to the yeasts
    • Ainsworth GC, Sussman AS (eds). Academic Press: New York
    • Barnett JA. 1968. The biochemical differentiation of taxa, with special reference to the yeasts. In The Fungi, An Advanced Treatise, vol 3, Ainsworth GC, Sussman AS (eds). Academic Press: New York; 557-595.
    • (1968) The Fungi, an Advanced Treatise , vol.3 , pp. 557-595
    • Barnett, J.A.1
  • 17
    • 0017574593 scopus 로고
    • The nutritional tests in yeast systematics
    • Barnett JA. 1977. The nutritional tests in yeast systematics. Journal of General Microbiology 99: 183-190.
    • (1977) Journal of General Microbiology , vol.99 , pp. 183-190
    • Barnett, J.A.1
  • 20
    • 0027121368 scopus 로고
    • Some controls on oligosaccharide utilization by yeasts: The physiological basis of the Kluyver effect
    • Barnett JA. 1992. Some controls on oligosaccharide utilization by yeasts: the physiological basis of the Kluyver effect. FEMS Microbiology Letters 100: 371-378.
    • (1992) FEMS Microbiology Letters , vol.100 , pp. 371-378
    • Barnett, J.A.1
  • 21
    • 0032412707 scopus 로고    scopus 로고
    • A history of research on yeasts 1: Work by chemists and biologists 1789-1850
    • Barnett JA. 1998. A history of research on yeasts 1: work by chemists and biologists 1789-1850. Yeast 14: 1439-1451.
    • (1998) Yeast , vol.14 , pp. 1439-1451
    • Barnett, J.A.1
  • 22
    • 0034659726 scopus 로고    scopus 로고
    • A history of research on yeasts 2: Louis Pasteur and his contemporaries, 1850-1880
    • Barnett JA. 2000. A history of research on yeasts 2: Louis Pasteur and his contemporaries, 1850-1880. Yeast 16: 755-771.
    • (2000) Yeast , vol.16 , pp. 755-771
    • Barnett, J.A.1
  • 23
    • 0038366899 scopus 로고    scopus 로고
    • A history of research on yeasts 5: The fermentation pathway
    • Barnett JA. 2003. A history of research on yeasts 5: the fermentation pathway. Yeast 20: 509-543.
    • (2003) Yeast , vol.20 , pp. 509-543
    • Barnett, J.A.1
  • 24
    • 0141704327 scopus 로고    scopus 로고
    • A history of research on yeasts 6: The main respiratory pathway
    • Barnett JA. 2003. A history of research on yeasts 6: the main respiratory pathway. Yeast 20: 1015-1044.
    • (2003) Yeast , vol.20 , pp. 1015-1044
    • Barnett, J.A.1
  • 25
    • 4043181261 scopus 로고    scopus 로고
    • A history of research on yeasts 7: Enzymic adaptation and regulation
    • Barnett JA. 2004. A history of research on yeasts 7: enzymic adaptation and regulation. Yeast 21: 703-746.
    • (2004) Yeast , vol.21 , pp. 703-746
    • Barnett, J.A.1
  • 26
    • 9144272680 scopus 로고    scopus 로고
    • A history of research on yeasts 8: Taxonomy
    • Barnett JA. 2004. A history of research on yeasts 8: taxonomy. Yeast 21: 1141-1193.
    • (2004) Yeast , vol.21 , pp. 1141-1193
    • Barnett, J.A.1
  • 27
    • 0002625364 scopus 로고
    • The utilization by yeasts of acids of the tricarboxylic acid cycle
    • Barnett JA, Kornberg HL. 1960. The utilization by yeasts of acids of the tricarboxylic acid cycle. Journal of General Microbiology 23: 65-82.
    • (1960) Journal of General Microbiology , vol.23 , pp. 65-82
    • Barnett, J.A.1    Kornberg, H.L.2
  • 28
    • 0035869464 scopus 로고    scopus 로고
    • A history of research on yeasts 3: Emil Fischer, Eduard Buchner and their contemporaries, 1880-1900
    • Barnett JA, Lichtenthaler FW. 2001. A history of research on yeasts 3: Emil Fischer, Eduard Buchner and their contemporaries, 1880-1900. Yeast 18: 363-388.
    • (2001) Yeast , vol.18 , pp. 363-388
    • Barnett, J.A.1    Lichtenthaler, F.W.2
  • 30
    • 0036163430 scopus 로고    scopus 로고
    • A history of research on yeasts 4: Cytology part I, 1890-1950
    • Barnett JA, Robinow CF. 2002. A history of research on yeasts 4: cytology part I, 1890-1950. Yeast 19: 151-182.
    • (2002) Yeast , vol.19 , pp. 151-182
    • Barnett, J.A.1    Robinow, C.F.2
  • 31
    • 0036292556 scopus 로고    scopus 로고
    • A history of research on yeasts 4: Cytology part II, 1950-1990
    • Barnett JA, Robinow CF. 2002. A history of research on yeasts 4: cytology part II, 1950-1990. Yeast 19: 745-772.
    • (2002) Yeast , vol.19 , pp. 745-772
    • Barnett, J.A.1    Robinow, C.F.2
  • 32
    • 0020420386 scopus 로고
    • The requirement of oxygen for the active transport of sugars into yeasts
    • Barnett JA, Sims AP. 1982. The requirement of oxygen for the active transport of sugars into yeasts. Journal of General Microbiology 128: 2303-2312.
    • (1982) Journal of General Microbiology , vol.128 , pp. 2303-2312
    • Barnett, J.A.1    Sims, A.P.2
  • 33
    • 25844516337 scopus 로고
    • Isolation and characterization of Saccharomyces cerevisiae mutants with a defect in catabolite-inactivation
    • Thesis, University of Frankfurt
    • Bauer J. 1994. Isolation and characterization of Saccharomyces cerevisiae mutants with a defect in catabolite-inactivation. Thesis, University of Frankfurt.
    • (1994)
    • Bauer, J.1
  • 34
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zühl F, Seemüller E. 1998. The proteasome: paradigm of a self-compartmentalizing protease. Cell 92: 367-380.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zühl, F.3    Seemüller, E.4
  • 35
    • 0018180547 scopus 로고
    • Transformation of yeast by a replicating hybrid plasmid
    • Beggs JD. 1978. Transformation of yeast by a replicating hybrid plasmid. Nature 275: 104-109.
    • (1978) Nature , vol.275 , pp. 104-109
    • Beggs, J.D.1
  • 37
  • 39
    • 0001637471 scopus 로고
    • Allosteric properties of yeast pyruvate decarboxylase
    • Boiteux A, Hess B. 1970. Allosteric properties of yeast pyruvate decarboxylase. FEBS Letters 9: 293-296.
    • (1970) FEBS Letters , vol.9 , pp. 293-296
    • Boiteux, A.1    Hess, B.2
  • 40
    • 0002511728 scopus 로고    scopus 로고
    • Metabolic signals
    • Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn
    • Boles E, Zimmermann FK, Thevelein JM. 1997. Metabolic signals. In Yeast Sugar Metabolism, Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn; 379-407.
    • (1997) Yeast Sugar Metabolism , pp. 379-407
    • Boles, E.1    Zimmermann, F.K.2    Thevelein, J.M.3
  • 42
    • 3142750437 scopus 로고
    • Influence of oxygen and concentration on alcoholic fermentation
    • Brown AJ. 1892. Influence of oxygen and concentration on alcoholic fermentation. Journal of the Chemical Society 61: 369-385.
    • (1892) Journal of the Chemical Society , vol.61 , pp. 369-385
    • Brown, A.J.1
  • 43
    • 0035930607 scopus 로고    scopus 로고
    • Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles
    • Brown CR, Cui D-Y, Hung GG-C, Chiang H-L. 2001. Cyclophilin A mediates Vid22p function in the import of fructose-1,6-bisphosphatase into Vid vesicles. Journal of Biological Chemistry 276: 48017-48026.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 48017-48026
    • Brown, C.R.1    Cui, D.-Y.2    Hung, G.G.-C.3    Chiang, H.-L.4
  • 44
    • 0036473043 scopus 로고    scopus 로고
    • Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-bisphosphatase degradation pathway
    • Brown CR, McCann JA, Hung GG-C, Elco CP, Chiang H-L. 2002. Vid22p, a novel plasma membrane protein, is required for the fructose-1,6-bisphosphatase degradation pathway. Journal of Cell Science 115: 655-666.
    • (2002) Journal of Cell Science , vol.115 , pp. 655-666
    • Brown, C.R.1    McCann, J.A.2    Hung, G.G.-C.3    Elco, C.P.4    Chiang, H.-L.5
  • 45
    • 0016662623 scopus 로고
    • Biosynthesis of branched-chain amino acids in yeast: Effect of carbon source on leucine biosynthetic enzymes
    • Brown HD, Satyanarayana T, Umbarger HE. 1975. Biosynthesis of branched-chain amino acids in yeast: effect of carbon source on leucine biosynthetic enzymes. Journal of Bacteriology 121: 959-969.
    • (1975) Journal of Bacteriology , vol.121 , pp. 959-969
    • Brown, H.D.1    Satyanarayana, T.2    Umbarger, H.E.3
  • 46
    • 0038371638 scopus 로고
    • A colloquial consideration of the Pasteur and neo-Pasteur effects
    • Burk D. 1939. A colloquial consideration of the Pasteur and neo-Pasteur effects. Cold Spring Harbor Symposia on Quantitative Biology 7: 420-459.
    • (1939) Cold Spring Harbor Symposia on Quantitative Biology , vol.7 , pp. 420-459
    • Burk, D.1
  • 48
    • 0019566797 scopus 로고
    • Mutants of yeast defective in sucrose utilization
    • Carlson M, Osmond BC, Botstein D. 1981. Mutants of yeast defective in sucrose utilization. Genetics 98: 25-40.
    • (1981) Genetics , vol.98 , pp. 25-40
    • Carlson, M.1    Osmond, B.C.2    Botstein, D.3
  • 49
    • 0021432459 scopus 로고
    • A suppressor of SNF1 mutations causes constitutive high-level invertase synthesis in yeast
    • Carlson M, Osmond BC, Neigeborn L, Botstein D. 1984. A suppressor of SNF1 mutations causes constitutive high-level invertase synthesis in yeast. Genetics 107: 19-32.
    • (1984) Genetics , vol.107 , pp. 19-32
    • Carlson, M.1    Osmond, B.C.2    Neigeborn, L.3    Botstein, D.4
  • 52
    • 0022534202 scopus 로고
    • A yeast gene that is essential for release from glucose repression encodes a protein kinase
    • Celenza JL, Carlson M. 1986. A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science 233: 1175-1180.
    • (1986) Science , vol.233 , pp. 1175-1180
    • Celenza, J.L.1    Carlson, M.2
  • 53
    • 0024343258 scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein
    • Celenza JL, Carlson M. 1989. Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein. Molecular and Cellular Biology 9: 5034-5044.
    • (1989) Molecular and Cellular Biology , vol.9 , pp. 5034-5044
    • Celenza, J.L.1    Carlson, M.2
  • 54
    • 0024325465 scopus 로고
    • Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: Evidence for physical association of the SNF4 protein with the SNF1 piotein kinase
    • Celenza JL, Eng FJ, Carlson M. 1989. Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 piotein kinase. molecular and Cellular Biology 9: 5045-5054.
    • (1989) Molecular and Cellular Biology , vol.9 , pp. 5045-5054
    • Celenza, J.L.1    Eng, F.J.2    Carlson, M.3
  • 55
    • 0011205352 scopus 로고
    • On the control of metabolism in ascites tumor cell suspensions
    • Chance B, Hess B. 1956. On the control of metabolism in ascites tumor cell suspensions. Annals of the New York Academy of Sciences 63: 1008-1016.
    • (1956) Annals of the New York Academy of Sciences , vol.63 , pp. 1008-1016
    • Chance, B.1    Hess, B.2
  • 56
    • 0014026959 scopus 로고
    • Adenosine 3′,5′-phosphate and oscillations of DPNH in a cell-free extract of Saccharomyces carlsbergensis
    • Cheung WY. 1966. Adenosine 3′,5′-phosphate and oscillations of DPNH in a cell-free extract of Saccharomyces carlsbergensis. Biochimica et Biophysica Acta 115: 235-239.
    • (1966) Biochimica Et Biophysica Acta , vol.115 , pp. 235-239
    • Cheung, W.Y.1
  • 57
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang H-L, Schekman R. 1991. Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350: 313-318.
    • (1991) Nature , vol.350 , pp. 313-318
    • Chiang, H.-L.1    Schekman, R.2
  • 58
    • 0032559855 scopus 로고    scopus 로고
    • Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation
    • Chiang MC, Chiang H-L. 1998. Vid24p, a novel protein localized to the fructose-1,6-bisphosphatase-containing vesicles, regulates targeting of fructose-1,6-bisphosphatase from the vesicles to the vacuole for degradation. Journal of Cell Biology 140: 1347-1356.
    • (1998) Journal of Cell Biology , vol.140 , pp. 1347-1356
    • Chiang, M.C.1    Chiang, H.-L.2
  • 60
    • 0016826648 scopus 로고
    • Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae I. Isolation and genetic analysis of adh mutants
    • Ciriacy M. 1975. Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae I. Isolation and genetic analysis of adh mutants. Mutation Research 29: 315-326.
    • (1975) Mutation Research , vol.29 , pp. 315-326
    • Ciriacy, M.1
  • 61
    • 0016806745 scopus 로고
    • Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae II. Two loci controlling synthesis of the glucose-repressible ADH II
    • Ciriacy M. 1975. Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae II. Two loci controlling synthesis of the glucose-repressible ADH II. Molecular and General Genetics 138: 157-164.
    • (1975) Molecular and General Genetics , vol.138 , pp. 157-164
    • Ciriacy, M.1
  • 62
    • 0017140763 scopus 로고
    • cis-Dominant regulatory mutations affecting the formation of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae
    • Ciriacy M. 1976. cis-Dominant regulatory mutations affecting the formation of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae. Molecular and General Genetics 145: 327-333.
    • (1976) Molecular and General Genetics , vol.145 , pp. 327-333
    • Ciriacy, M.1
  • 63
    • 0017396028 scopus 로고
    • Isolation and characterization of yeast mutants defective in intermediary carbon metabolism and in carbon catabolite derepression
    • Ciriacy M. 1977. Isolation and characterization of yeast mutants defective in intermediary carbon metabolism and in carbon catabolite derepression. Molecular and General Genetics 154: 213-220.
    • (1977) Molecular and General Genetics , vol.154 , pp. 213-220
    • Ciriacy, M.1
  • 64
    • 0018391488 scopus 로고
    • Physiological effects of seven different blocks in glycolysis in Saccharomyces cerevisiae
    • Ciriacy M, Breitenbach I. 1979. Physiological effects of seven different blocks in glycolysis in Saccharomyces cerevisiae. Journal of Bacteriology 139: 152-160.
    • (1979) Journal of Bacteriology , vol.139 , pp. 152-160
    • Ciriacy, M.1    Breitenbach, I.2
  • 65
    • 0014248270 scopus 로고
    • Relationship between sugar structure and competition for the sugar transport system in bakers' yeast
    • Cirillo VP. 1968. Relationship between sugar structure and competition for the sugar transport system in bakers' yeast. Journal of Bacteriology 95: 603-611.
    • (1968) Journal of Bacteriology , vol.95 , pp. 603-611
    • Cirillo, V.P.1
  • 66
    • 0014287250 scopus 로고
    • Galactose transport in Saccharomyces cerevisiae I. Nonmetabolized sugars as substrates and inducers of the galactose transport system
    • Cirillo VP. 1968. Galactose transport in Saccharomyces cerevisiae I. Nonmetabolized sugars as substrates and inducers of the galactose transport system. Journal of Bacteriology 95: 1727-1731.
    • (1968) Journal of Bacteriology , vol.95 , pp. 1727-1731
    • Cirillo, V.P.1
  • 67
    • 0020481613 scopus 로고
    • Mutant studies of yeast phosphofructokinase
    • Clifton D, Fraenkel DG. 1982. Mutant studies of yeast phosphofructokinase. Biochemistry 21: 1935-1942.
    • (1982) Biochemistry , vol.21 , pp. 1935-1942
    • Clifton, D.1    Fraenkel, D.G.2
  • 68
    • 0038022092 scopus 로고
    • 2 compounds in micro-organisms 4. Synthesis of cell materials from acetate by Aspergillus niger
    • 2 compounds in micro-organisms 4. Synthesis of cell materials from acetate by Aspergillus niger. Biochemical Journal 77: 430-438.
    • (1960) Biochemical Journal , vol.77 , pp. 430-438
    • Collins, J.F.1    Kornberg, H.L.2
  • 69
    • 2242461686 scopus 로고
    • The hexokinases
    • 3rd edn, Boyer PD (ed.). Academic Press: New York
    • Colowick SP. 1973. The hexokinases. In The Enzymes, 3rd edn, vol. 9, Boyer PD (ed.). Academic Press: New York; 1-48.
    • (1973) The Enzymes , vol.9 , pp. 1-48
    • Colowick, S.P.1
  • 70
    • 25844438301 scopus 로고
    • Phosphorylation of carbohydrates
    • University of Wisconsin Press: Madison, WI
    • Cori CF. 1942. Phosphorylation of carbohydrates. In A Symposium on Respiratory Enzymes. University of Wisconsin Press: Madison, WI; 175-189.
    • (1942) A Symposium on Respiratory Enzymes , pp. 175-189
    • Cori, C.F.1
  • 71
    • 0000089325 scopus 로고
    • Observations on the carbohydrate metabolism of tumours
    • Crabtree HG. 1929. Observations on the carbohydrate metabolism of tumours. Biochemical Journal 23: 536-545.
    • (1929) Biochemical Journal , vol.23 , pp. 536-545
    • Crabtree, H.G.1
  • 72
    • 0014441132 scopus 로고
    • Promitochondria of anaerobically grown yeast. I. Isolation and biochemical properties
    • Criddle RS, Schatz G. 1968. Promitochondria of anaerobically grown yeast. I. Isolation and biochemical properties. Biochemistry 8: 322-334.
    • (1968) Biochemistry , vol.8 , pp. 322-334
    • Criddle, R.S.1    Schatz, G.2
  • 73
    • 0008878932 scopus 로고
    • Onderzoekingen over het gistgeslacht Brettanomyces
    • Thesis, De Technische Hoogeschool te Delft
    • Custers MTJ. 1940. Onderzoekingen over het gistgeslacht Brettanomyces. Thesis, De Technische Hoogeschool te Delft.
    • (1940)
    • Custers, M.T.J.1
  • 74
    • 0014592334 scopus 로고
    • Mitochondria in anaerobically-grown, lipid-limited brewer's yeast
    • Damsky CH, Nelson WM, Claude A. 1969. Mitochondria in anaerobically-grown, lipid-limited brewer's yeast. Journal of Cell Biology 43: 174-179.
    • (1969) Journal of Cell Biology , vol.43 , pp. 174-179
    • Damsky, C.H.1    Nelson, W.M.2    Claude, A.3
  • 75
    • 4043147643 scopus 로고
    • Invertase formation in Saccharomyces fragilis
    • Davies A. 1956. Invertase formation in Saccharomyces fragilis. Journal of General Microbiology 14: 109-121.
    • (1956) Journal of General Microbiology , vol.14 , pp. 109-121
    • Davies, A.1
  • 76
    • 0007820202 scopus 로고
    • Some factors affecting lactase formation and activity in Saccharomyces fragilis
    • Davies A. 1956. Some factors affecting lactase formation and activity in Saccharomyces fragilis. Journal of General Microbiology 14: 425-439.
    • (1956) Journal of General Microbiology , vol.14 , pp. 425-439
    • Davies, A.1
  • 77
    • 25844464101 scopus 로고    scopus 로고
    • A life-long quest for biochemical regulation (Helmut Holzer, 1921-1997)
    • Decker K. 2000. A life-long quest for biochemical regulation (Helmut Holzer, 1921-1997). Comprehensive Biochemistry 41: 531-561.
    • (2000) Comprehensive Biochemistry , vol.41 , pp. 531-561
    • Decker, K.1
  • 78
    • 0013936130 scopus 로고
    • The Crabtree effect: A regulatory system in yeast
    • De Deken RH. 1966. The Crabtree effect: a regulatory system in yeast. Journal of General Microbiology 44: 140-156.
    • (1966) Journal of General Microbiology , vol.44 , pp. 140-156
    • De Deken, R.H.1
  • 79
    • 0000095303 scopus 로고
    • The mechanism of the heterolactic fermentation: A new route of ethanol formation
    • DeMoss RD, Bard RC, Gunsalus IC. 1951. The mechanism of the heterolactic fermentation: a new route of ethanol formation. Journal of Bacteriology 62: 499-511.
    • (1951) Journal of Bacteriology , vol.62 , pp. 499-511
    • DeMoss, R.D.1    Bard, R.C.2    Gunsalus, I.C.3
  • 80
    • 0009633172 scopus 로고
    • Studien über die proteolytischen Enzyme der Hefe und ihre Beziehung zu der Autolyze
    • Dernby KG. 1917. Studien über die proteolytischen Enzyme der Hefe und ihre Beziehung zu der Autolyze. Biochemische Zeitschfift 81: 107-208.
    • (1917) Biochemische Zeitschfift , vol.81 , pp. 107-208
    • Dernby, K.G.1
  • 81
    • 0033523996 scopus 로고    scopus 로고
    • The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae
    • DeVit MJ, Johnston M. 1999. The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae. Current Biology 9: 1231-1241.
    • (1999) Current Biology , vol.9 , pp. 1231-1241
    • DeVit, M.J.1    Johnston, M.2
  • 83
    • 25844517804 scopus 로고
    • Anaerobic glycolysis, respiration, and the Pasteur effect
    • Sumner JB, Myrbäck K (eds). Academic Press: New York
    • Dickens F. 1951. Anaerobic glycolysis, respiration, and the Pasteur effect. In The Enzymes. Chemistry and Mechanism of Action, vol. 2, Sumner JB, Myrbäck K (eds). Academic Press: New York; 624-683.
    • (1951) The Enzymes. Chemistry and Mechanism of Action , vol.2 , pp. 624-683
    • Dickens, F.1
  • 84
    • 84932187367 scopus 로고
    • The Pasteur effect and its mechanism
    • Dixon KC. 1937. The Pasteur effect and its mechanism. Biological Reviews 12: 431-460.
    • (1937) Biological Reviews , vol.12 , pp. 431-460
    • Dixon, K.C.1
  • 85
    • 0013487953 scopus 로고
    • Factors influencing the appearance of invertase in Saccharomyces cerevisiae
    • Dodyk F, Rothstein A. 1964. Factors influencing the appearance of invertase in Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics 104: 478-486.
    • (1964) Archives of Biochemistry and Biophysics , vol.104 , pp. 478-486
    • Dodyk, F.1    Rothstein, A.2
  • 87
    • 0242624221 scopus 로고
    • The genetic control of galactose utilization in Saccharomyces
    • Douglas HC, Condie F. 1954. The genetic control of galactose utilization in Saccharomyces. Journal of Bacteriology 68: 662-670.
    • (1954) Journal of Bacteriology , vol.68 , pp. 662-670
    • Douglas, H.C.1    Condie, F.2
  • 88
    • 0014162215 scopus 로고
    • Glucose-dependent enzyme activities in different yeast species
    • Duntze W, Atzpodien W, Holzer H. 1967. Glucose-dependent enzyme activities in different yeast species. Archiv für Mikrobiologie 58: 296-301.
    • (1967) Archiv Für Mikrobiologie , vol.58 , pp. 296-301
    • Duntze, W.1    Atzpodien, W.2    Holzer, H.3
  • 89
  • 90
    • 0014240508 scopus 로고
    • Glucose induced inactivation of malate dehydrogenase in intact yeast cells
    • Duntze W, Neumann D, Holzer H. 1968. Glucose induced inactivation of malate dehydrogenase in intact yeast cells. European Journal of Biochemistry 3: 326-331.
    • (1968) European Journal of Biochemistry , vol.3 , pp. 326-331
    • Duntze, W.1    Neumann, D.2    Holzer, H.3
  • 91
    • 0020024144 scopus 로고
    • Mechanisms of solute transport in selected eukaryotic microorganisms
    • Eddy AA. 1982. Mechanisms of solute transport in selected eukaryotic microorganisms. Advances in Microbial Physiology 23: 1-78.
    • (1982) Advances in Microbial Physiology , vol.23 , pp. 1-78
    • Eddy, A.A.1
  • 92
    • 0030003051 scopus 로고    scopus 로고
    • Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4
    • Edmondson DG, Smith MM, Roth SY. 1996. Repression domain of the yeast global repressor Tup1 interacts directly with histones H3 and H4. Genes and Development 10: 1247-1259.
    • (1996) Genes and Development , vol.10 , pp. 1247-1259
    • Edmondson, D.G.1    Smith, M.M.2    Roth, S.Y.3
  • 95
    • 25844461266 scopus 로고
    • On the mechanism of the Pasteur effect
    • Engelhardt VA, Sakov NE. 1943. [On the mechanism of the Pasteur effect.] [Biokhimiya] 8: 9-36.
    • (1943) Biokhimiya , vol.8 , pp. 9-36
    • Engelhardt, V.A.1    Sakov, N.E.2
  • 96
    • 25844465725 scopus 로고
    • Genetik des Kohlenhydratstoffwechsels von Saccharomyces cerevisiae
    • Thesis, Technische Universität Darmstadt
    • Entian K-D. 1978. Genetik des Kohlenhydratstoffwechsels von Saccharomyces cerevisiae. Thesis, Technische Universität Darmstadt.
    • (1978)
    • Entian, K.-D.1
  • 97
    • 0018969294 scopus 로고
    • Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast
    • Entian K-D. 1980. Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Molecular and General Genetics 178: 633-637.
    • (1980) Molecular and General Genetics , vol.178 , pp. 633-637
    • Entian, K.-D.1
  • 98
    • 0018959685 scopus 로고
    • A defect in carbon catabolite repression associated with uncontrollable and excessive maltose uptake
    • Entian K-D. 1980. A defect in carbon catabolite repression associated with uncontrollable and excessive maltose uptake. Molecular and General Genetics 179: 169-175.
    • (1980) Molecular and General Genetics , vol.179 , pp. 169-175
    • Entian, K.-D.1
  • 99
    • 0002735864 scopus 로고    scopus 로고
    • Sugar phosphorylation in yeast
    • Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn
    • Entian K-D. 1997. Sugar phosphorylation in yeast. In Yeast Sugar Metabolism. Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn; 67-79.
    • (1997) Yeast Sugar Metabolism , pp. 67-79
    • Entian, K.-D.1
  • 100
    • 0007566614 scopus 로고
    • Some genetical and biochemical attempts to elucidate the energetics of sugar uptake and explain the Kluyver effect in the yeast, Kluyveromyces lactis
    • Entian K-D, Barnett JA. 1983. Some genetical and biochemical attempts to elucidate the energetics of sugar uptake and explain the Kluyver effect in the yeast, Kluyveromyces lactis. Current Genetics 7: 323-325.
    • (1983) Current Genetics , vol.7 , pp. 323-325
    • Entian, K.-D.1    Barnett, J.A.2
  • 101
    • 0026457028 scopus 로고
    • Regulation of sugar utilization by Saccharomyces cerevisiae
    • Entian K-D, Barnett JA. 1992. Regulation of sugar utilization by Saccharomyces cerevisiae. Trends in Biochemical Sciences 17: 506-510.
    • (1992) Trends in Biochemical Sciences , vol.17 , pp. 506-510
    • Entian, K.-D.1    Barnett, J.A.2
  • 102
    • 0020776397 scopus 로고
    • Studies on rapid reversible and non-reversible inactivation of fructose-1,6-bisphosphatase and malate dehydrogenase in wild-type and glycolytic block mutants of Saccharomyces cerevisiae
    • Entian K-D, Dröll L, Mecke D. 1983. Studies on rapid reversible and non-reversible inactivation of fructose-1,6-bisphosphatase and malate dehydrogenase in wild-type and glycolytic block mutants of Saccharomyces cerevisiae. Archives of Microbiology 134: 187-192.
    • (1983) Archives of Microbiology , vol.134 , pp. 187-192
    • Entian, K.-D.1    Dröll, L.2    Mecke, D.3
  • 103
    • 0021266044 scopus 로고
    • Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering carbon catabolite repression
    • Entian K-D, Fröhlich K-U. 1984. Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering carbon catabolite repression. Journal of Bacteriology 158: 29-35.
    • (1984) Journal of Bacteriology , vol.158 , pp. 29-35
    • Entian, K.-D.1    Fröhlich, K.-U.2
  • 104
    • 0022206328 scopus 로고
    • Cloning of hexokinase structural genes from Saccharomyces cerevisiae mutants with regulatory mutations responsible for glucose repression
    • Entian K-D, Hilberg F, Opitz H, Mecke D. 1985. Cloning of hexokinase structural genes from Saccharomyces cerevisiae mutants with regulatory mutations responsible for glucose repression. Molecular and Cellular Biology 5: 3035-3040.
    • (1985) Molecular and Cellular Biology , vol.5 , pp. 3035-3040
    • Entian, K.-D.1    Hilberg, F.2    Opitz, H.3    Mecke, D.4
  • 105
    • 0025356703 scopus 로고
    • Misregulation of maltose uptake in a glucose repression defective mutant of Saccharomyces cerevisiae leads to glucose poisoning
    • Entian K-D, Loureiro-Dias MC. 1990. Misregulation of maltose uptake in a glucose repression defective mutant of Saccharomyces cerevisiae leads to glucose poisoning. Journal of General Microbiology 136: 855-860.
    • (1990) Journal of General Microbiology , vol.136 , pp. 855-860
    • Entian, K.-D.1    Loureiro-Dias, M.C.2
  • 106
    • 0020028142 scopus 로고
    • Genetic evidence for a role of hexokinase isozyme PII in carbon catabolite repression in Saccharomyces cerevisiae
    • Entian K-D, Mecke D. 1982. Genetic evidence for a role of hexokinase isozyme PII in carbon catabolite repression in Saccharomyces cerevisiae. Journal of Biological Chemistry 257: 870-874.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 870-874
    • Entian, K.-D.1    Mecke, D.2
  • 107
    • 0018845565 scopus 로고
    • Glycolytic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae
    • Entian K-D, Zimmermann FK. 1980. Glycolytic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae. Molecular and General Genetics 177: 345-350.
    • (1980) Molecular and General Genetics , vol.177 , pp. 345-350
    • Entian, K.-D.1    Zimmermann, F.K.2
  • 108
    • 0020401969 scopus 로고
    • New genes involved in carbon catabolite repression and derepression in the yeast Saccharomyces cerevisiae
    • Entian K-D, Zimmermann FK. 1982. New genes involved in carbon catabolite repression and derepression in the yeast Saccharomyces cerevisiae. Journal of Bacteriology 151: 1123-1128.
    • (1982) Journal of Bacteriology , vol.151 , pp. 1123-1128
    • Entian, K.-D.1    Zimmermann, F.K.2
  • 109
    • 0017691984 scopus 로고
    • A partial defect in carbon catabolite repression in mutants of Saccharomyces cerevisiae with reduced hexose phosphorylation
    • Entian K-D, Zimmermann FK, Scheel I. 1977. A partial defect in carbon catabolite repression in mutants of Saccharomyces cerevisiae with reduced hexose phosphorylation. Molecular and General Genetics 156: 99-105.
    • (1977) Molecular and General Genetics , vol.156 , pp. 99-105
    • Entian, K.-D.1    Zimmermann, F.K.2    Scheel, I.3
  • 111
    • 0001073225 scopus 로고
    • The influence of the presence of glucose during growth on the enzymic activities of Escherichia coli: Comparison of the effect with that produced by fermentation acids
    • Epps HMR, Gale EF. 1942. The influence of the presence of glucose during growth on the enzymic activities of Escherichia coli: comparison of the effect with that produced by fermentation acids. Biochemical Journal 36: 619-623.
    • (1942) Biochemical Journal , vol.36 , pp. 619-623
    • Epps, H.M.R.1    Gale, E.F.2
  • 112
    • 0021763550 scopus 로고
    • Catabolite repression in yeasts is not associated with low levels of cAMP
    • Eraso P, Gancedo JM. 1984. Catabolite repression in yeasts is not associated with low levels of cAMP. European Journal of Biochemistry 141: 195-198.
    • (1984) European Journal of Biochemistry , vol.141 , pp. 195-198
    • Eraso, P.1    Gancedo, J.M.2
  • 113
    • 0025651676 scopus 로고
    • Increased dosage of the MSN1 gene restores invertase expression in yeast mutants defective in the SNF1 protein kinase
    • Estruch F, Carlson M. 1990. Increased dosage of the MSN1 gene restores invertase expression in yeast mutants defective in the SNF1 protein kinase. Nucleic Acids Research 18: 6959-6964.
    • (1990) Nucleic Acids Research , vol.18 , pp. 6959-6964
    • Estruch, F.1    Carlson, M.2
  • 115
    • 0014064552 scopus 로고
    • Yeast malate dehydrogenase: Enzyme inactivation in catabolite repression
    • Ferguson JJ, Boll M, Holzer H. 1967. Yeast malate dehydrogenase: enzyme inactivation in catabolite repression. European Journal of Biochemistry 1: 21-25.
    • (1967) European Journal of Biochemistry , vol.1 , pp. 21-25
    • Ferguson, J.J.1    Boll, M.2    Holzer, H.3
  • 116
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S, Song OK. 1989. A novel genetic system to detect protein-protein interactions. Nature 340: 245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.K.2
  • 118
    • 0025942492 scopus 로고
    • GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats
    • Flick JS, Johnston M. 1991. GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats. Molecular and Cellular Biology 11: 5101-5112.
    • (1991) Molecular and Cellular Biology , vol.11 , pp. 5101-5112
    • Flick, J.S.1    Johnston, M.2
  • 121
    • 0021802750 scopus 로고
    • The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression
    • Fröhlich K-U, Entian K-D, Mecke D. 1985. The primary structure of the yeast hexokinase PII gene (HXK2) which is responsible for glucose repression. Gene 36: 105-111.
    • (1985) Gene , vol.36 , pp. 105-111
    • Fröhlich, K.-U.1    Entian, K.-D.2    Mecke, D.3
  • 122
    • 0025353830 scopus 로고
    • Cloning of the yeast SFL2 gene: Its disruption results in pleiotropic phenotypes characteristic for tup1 mutants
    • Fujita A, Matsumoto S, Kuhara S, Misumi Y, Kobayashi H. 1990. Cloning of the yeast SFL2 gene: its disruption results in pleiotropic phenotypes characteristic for tup1 mutants. Gene 89: 93-99.
    • (1990) Gene , vol.89 , pp. 93-99
    • Fujita, A.1    Matsumoto, S.2    Kuhara, S.3    Misumi, Y.4    Kobayashi, H.5
  • 123
    • 0037878077 scopus 로고    scopus 로고
    • The Kluyver effect revisited
    • Fukuhara H. 2003. The Kluyver effect revisited. FEMS Yeast Research 3: 327-331.
    • (2003) FEMS Yeast Research , vol.3 , pp. 327-331
    • Fukuhara, H.1
  • 124
    • 0019166919 scopus 로고
    • Turnover of yeast fructose-bisphosphatase in different metabolic conditions
    • Funayama S, Gancedo JM, Gancedo C. 1980. Turnover of yeast fructose-bisphosphatase in different metabolic conditions. European Journal of Biochemistry 109: 61-66.
    • (1980) European Journal of Biochemistry , vol.109 , pp. 61-66
    • Funayama, S.1    Gancedo, J.M.2    Gancedo, C.3
  • 125
    • 0015100291 scopus 로고
    • Inactivation of fructose-1,6-diphosphatase by glucose in yeast
    • Gancedo C. 1971. Inactivation of fructose-1,6-diphosphatase by glucose in yeast. Journal of Bacteriology 107: 401-405.
    • (1971) Journal of Bacteriology , vol.107 , pp. 401-405
    • Gancedo, C.1
  • 126
    • 2642650376 scopus 로고
    • Reciprocal effects of carbon sources on the levels of the AMP-sensitive fructose-1,6-diphosphatase and phosphofructokinase in yeast
    • Gancedo C, Salas ML, Giner A, Sols A. 1965. Reciprocal effects of carbon sources on the levels of the AMP-sensitive fructose-1,6-diphosphatase and phosphofructokinase in yeast. Biochemical and Biophysical Research Communications 20: 15-20.
    • (1965) Biochemical and Biophysical Research Communications , vol.20 , pp. 15-20
    • Gancedo, C.1    Salas, M.L.2    Giner, A.3    Sols, A.4
  • 127
    • 0017178572 scopus 로고
    • Inactivation by glucose of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae
    • Gancedo C, Schwerzmann K. 1976. Inactivation by glucose of phosphoenolpyruvate carboxykinase from Saccharomyces cerevisiae. Archives of Microbiology 109: 221-225.
    • (1976) Archives of Microbiology , vol.109 , pp. 221-225
    • Gancedo, C.1    Schwerzmann, K.2
  • 128
  • 130
    • 0014977781 scopus 로고
    • Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeasts
    • Gancedo JM, Gancedo C. 1971. Fructose-1,6-diphosphatase, phosphofructokinase and glucose-6-phosphate dehydrogenase from fermenting and non-fermenting yeasts. Archives of Microbiology 76: 132-138.
    • (1971) Archives of Microbiology , vol.76 , pp. 132-138
    • Gancedo, J.M.1    Gancedo, C.2
  • 131
    • 0002594666 scopus 로고    scopus 로고
    • Gluconeogenesis and catabolite inactivation
    • Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn
    • Gancedo JM, Gancedo C. 1997. Gluconeogenesis and catabolite inactivation. In Yeast Sugar Metabolism, Zimmermann FK, Entian K-D (eds). Technomic: Lancaster, Penn; 359-377.
    • (1997) Yeast Sugar Metabolism , pp. 359-377
    • Gancedo, J.M.1    Gancedo, C.2
  • 132
    • 0020362744 scopus 로고
    • Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae
    • Gancedo JM, Mazón MJ, Gancedo C. 1982. Kinetic differences between two interconvertible forms of fructose-1,6-bisphosphatase from Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics 218: 478-482.
    • (1982) Archives of Biochemistry and Biophysics , vol.218 , pp. 478-482
    • Gancedo, J.M.1    Mazón, M.J.2    Gancedo, C.3
  • 133
    • 0021112036 scopus 로고
    • Fructose 2,6-bisphosphate activates the cAMP-dependent phosphorylation of yeast fructose-1,6-bisphosphatase in vitro
    • Gancedo JM, Mazón MJ, Gancedo C. 1983. Fructose 2,6-bisphosphate activates the cAMP-dependent phosphorylation of yeast fructose-1,6-bisphosphatase in vitro. Journal of Biological Chemistry 258: 5998-5999.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 5998-5999
    • Gancedo, J.M.1    Mazón, M.J.2    Gancedo, C.3
  • 134
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • and 37 others
    • Gavin AC and 37 others. 2002. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 136
    • 0005847351 scopus 로고
    • Zum Nachweis des im Hefepresssaft enthaltenen proteolytischen Enzyms
    • Geret L, Hahn M. 1898. Zum Nachweis des im Hefepresssaft enthaltenen proteolytischen Enzyms. Berichte der Deutschen Chemischen Gesellschaft 31: 202-205.
    • (1898) Berichte Der Deutschen Chemischen Gesellschaft , vol.31 , pp. 202-205
    • Geret, L.1    Hahn, M.2
  • 137
    • 0015823542 scopus 로고
    • Abnormal cell envelope ultrastructure of a Saccharomyces mutant with invertase formation resistant to hexoses
    • Ghosh BK, Montenecourt B, Lampen JO. 1973. Abnormal cell envelope ultrastructure of a Saccharomyces mutant with invertase formation resistant to hexoses. Journal of Bacteriology 116: 1412-1420.
    • (1973) Journal of Bacteriology , vol.116 , pp. 1412-1420
    • Ghosh, B.K.1    Montenecourt, B.2    Lampen, J.O.3
  • 138
    • 0036983124 scopus 로고    scopus 로고
    • The proteasome, a new target for cancer therapy
    • Gillessen S, Groettrup M, Cerny T. 2002. The proteasome, a new target for cancer therapy. Onkologie 25: 534-539.
    • (2002) Onkologie , vol.25 , pp. 534-539
    • Gillessen, S.1    Groettrup, M.2    Cerny, T.3
  • 139
    • 10244239321 scopus 로고    scopus 로고
    • Life with 6000 genes
    • and 15 others
    • Goffeau A and 15 others. 1996. Life with 6000 genes. Science 274: 546-567.
    • (1996) Science , vol.274 , pp. 546-567
    • Goffeau, A.1
  • 140
    • 0036134944 scopus 로고    scopus 로고
    • Respiration-dependent utilization of sugars in yeasts: A determinant role for sugar transporters
    • Goffrini P, Ferrero I, Donnini C. 2002. Respiration-dependent utilization of sugars in yeasts: a determinant role for sugar transporters. Journal of Bacteriology 184: 427-432.
    • (2002) Journal of Bacteriology , vol.184 , pp. 427-432
    • Goffrini, P.1    Ferrero, I.2    Donnini, C.3
  • 142
    • 25844523176 scopus 로고
    • Effect of different carbon sources on the regulation of carbohydrate metabolism in Saccharomyces cerevisiae
    • Görts CPM. 1967. Effect of different carbon sources on the regulation of carbohydrate metabolism in Saccharomyces cerevisiae. Antonie van Leeuwenhoek 33: 451-463.
    • (1967) Antonie Van Leeuwenhoek , vol.33 , pp. 451-463
    • Görts, C.P.M.1
  • 143
    • 0014695823 scopus 로고
    • Effect of glucose on the activity and the kinetics of the maltose-uptake system and of α-glucosidase in Saccharomyces cerevisiae
    • Görts CPM. 1969. Effect of glucose on the activity and the kinetics of the maltose-uptake system and of α-glucosidase in Saccharomyces cerevisiae. Biochimica et Biophysica Acta 184: 299-305.
    • (1969) Biochimica Et Biophysica Acta , vol.184 , pp. 299-305
    • Görts, C.P.M.1
  • 144
  • 145
    • 84942400590 scopus 로고
    • Über die Proteinase und die Polypeptidase der Hefe. 13. Abhandlung über Pflanzenproteasen in der von R. Willstätter und Mitarbeitern begonnenen Untersuchungsreihe
    • Grassmann W, Dyckerhoff H. 1928. Über die Proteinase und die Polypeptidase der Hefe. 13. Abhandlung über Pflanzenproteasen in der von R. Willstätter und Mitarbeitern begonnenen Untersuchungsreihe. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 179: 41-78.
    • (1928) Hoppe-Seyler's Zeitschrift Für Physiologische Chemie , vol.179 , pp. 41-78
    • Grassmann, W.1    Dyckerhoff, H.2
  • 146
    • 25844487648 scopus 로고
    • Effect of actidione (cycloheximide) on yeast fermentation
    • Greig ME, Walk RA, Gibbons AJ. 1958. Effect of actidione (cycloheximide) on yeast fermentation. Journal of Bacteriology 75: 489-491.
    • (1958) Journal of Bacteriology , vol.75 , pp. 489-491
    • Greig, M.E.1    Walk, R.A.2    Gibbons, A.J.3
  • 147
    • 0018929573 scopus 로고
    • The use of phenylmethylsulfonyl fluoride in the study of catabolite inactivation and repression in intact cells of Saccharomyces cerevisiae
    • Grossmann MK. 1980. The use of phenylmethylsulfonyl fluoride in the study of catabolite inactivation and repression in intact cells of Saccharomyces cerevisiae. Archives of Microbiology 124: 293-295.
    • (1980) Archives of Microbiology , vol.124 , pp. 293-295
    • Grossmann, M.K.1
  • 148
    • 9144233981 scopus 로고
    • Brewers Publications: Boulder, CO
    • Guinard J-X. 1990. Lambic. Brewers Publications: Boulder, CO.
    • (1990) Lambic
    • Guinard, J.-X.1
  • 149
    • 0016604850 scopus 로고
    • On the activity and regulation of anaplerotic and gluconeogenetic enzymes during the growth process of baker's yeast
    • Haarasilta S, Oura E. 1975. On the activity and regulation of anaplerotic and gluconeogenetic enzymes during the growth process of baker's yeast. European Journal of Biochemistry 52: 1-7.
    • (1975) European Journal of Biochemistry , vol.52 , pp. 1-7
    • Haarasilta, S.1    Oura, E.2
  • 150
    • 0017804537 scopus 로고
    • The malate dehydrogenase isoenzymes of Saccharomyces cerevisiae: Purification, characterisation and studies on their regulation
    • Hägele E, Neeff J, Mecke D. 1978. The malate dehydrogenase isoenzymes of Saccharomyces cerevisiae: purification, characterisation and studies on their regulation. European Journal of Biochemistry 83: 67-76.
    • (1978) European Journal of Biochemistry , vol.83 , pp. 67-76
    • Hägele, E.1    Neeff, J.2    Mecke, D.3
  • 151
    • 25844479738 scopus 로고
    • James Lorrain Smith
    • ['JSH']
    • Haldane JS ['JSH']. 1931. James Lorrain Smith. Biochemical Journal 25: 1849-1850.
    • (1931) Biochemical Journal , vol.25 , pp. 1849-1850
    • Haldane, J.S.1
  • 152
    • 84944483022 scopus 로고
    • The oxygen tension in arterial blood
    • [S]
    • Haldane J[S], Smith JL. 1896. The oxygen tension in arterial blood. Journal of Physiology 20: 497-520.
    • (1896) Journal of Physiology , vol.20 , pp. 497-520
    • Haldane, J.1    Smith, J.L.2
  • 153
    • 0032566737 scopus 로고    scopus 로고
    • Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae
    • Hämmerle M, Bauer J, Rose M, Szallies A, Thumm M, Düsterhus S, Mecke D, Entian K-D, Wolf DH. 1998. Proteins of newly isolated mutants and the amino-terminal proline are essential for ubiquitin-proteasome-catalyzed catabolite degradation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. Journal of Biological Chemistry 273: 25000-25005.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 25000-25005
    • Hämmerle, M.1    Bauer, J.2    Rose, M.3    Szallies, A.4    Thumm, M.5    Düsterhus, S.6    Mecke, D.7    Entian, K.-D.8    Wolf, D.H.9
  • 155
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase family: Metabolic sensors of the eukaryotic cell?
    • Hardie DG, Carling D, Carlson M. 1998. The AMP-activated/SNF1 protein kinase family: metabolic sensors of the eukaryotic cell? Annual Review of Biochemistry 67: 821-855.
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 821-855
    • Hardie, D.G.1    Carling, D.2    Carlson, M.3
  • 156
    • 0011762999 scopus 로고
    • Vacuolar (lysosomal) trehalase of Saccharomyces cerevisiae
    • Harris SD, Cotter DA. 1987. Vacuolar (lysosomal) trehalase of Saccharomyces cerevisiae. Current Microbiology 15: 247-249.
    • (1987) Current Microbiology , vol.15 , pp. 247-249
    • Harris, S.D.1    Cotter, D.A.2
  • 157
    • 0035808454 scopus 로고    scopus 로고
    • The transcriptional activator Cat8p provides a major contribution to the reprogramming of carbon metabolism during the diauxic shift in Saccharomyces cerevisiae
    • Haurie V, Perrot M, Mini T, Jenö P, Sagliocco F, 2001. The transcriptional activator Cat8p provides a major contribution to the reprogramming of carbon metabolism during the diauxic shift in Saccharomyces cerevisiae. Journal of Biological Chemistry 276: 76-85.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 76-85
    • Haurie, V.1    Perrot, M.2    Mini, T.3    Jenö, P.4    Sagliocco, F.5
  • 158
    • 4444311163 scopus 로고    scopus 로고
    • Pak1 protein kinase regulates activation and nuclear localization of Snf1-Ga183 protein kinase
    • Hedbacker K, Hong S-P, Carlson M. 2004. Pak1 protein kinase regulates activation and nuclear localization of Snf1-Ga183 protein kinase. Molecular and Cellular Biology 24: 8255-8263.
    • (2004) Molecular and Cellular Biology , vol.24 , pp. 8255-8263
    • Hedbacker, K.1    Hong, S.-P.2    Carlson, M.3
  • 159
    • 0028930777 scopus 로고
    • CAT8, a new zinc cluster-encoding gene necessary for derepression of gluconeogenic enzymes in the yeast Saccharomyces cerevisiae
    • Hedges D, Proft M, Entian K-D. 1995. CAT8, a new zinc cluster-encoding gene necessary for derepression of gluconeogenic enzymes in the yeast Saccharomyces cerevisiae. Molecular and Cellular Biology 15: 1915-1922.
    • (1995) Molecular and Cellular Biology , vol.15 , pp. 1915-1922
    • Hedges, D.1    Proft, M.2    Entian, K.-D.3
  • 160
    • 0022595650 scopus 로고
    • Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast
    • Heinisch J. 1986. Isolation and characterization of the two structural genes coding for phosphofructokinase in yeast. Molecular and General Genetics 202: 75-82.
    • (1986) Molecular and General Genetics , vol.202 , pp. 75-82
    • Heinisch, J.1
  • 163
    • 4243577799 scopus 로고
    • Metabolic studies with 2-deoxyhexoses I. Mechanisms of inhibition of growth and fermentation in baker's yeast
    • Heredia CF, De La Fuente G, Sols A. 1964. Metabolic studies with 2-deoxyhexoses I. Mechanisms of inhibition of growth and fermentation in baker's yeast. Biochimica et Biophysica Acta 86: 216-223.
    • (1964) Biochimica Et Biophysica Acta , vol.86 , pp. 216-223
    • Heredia, C.F.1    De La Fuente, G.2    Sols, A.3
  • 164
    • 0001097630 scopus 로고
    • Metabolic control mechanisms VI. Chemical events after glucose addition to ascites tumour cells
    • Hess B, Chance B. 1961. Metabolic control mechanisms VI. Chemical events after glucose addition to ascites tumour cells. Journal of Biological Chemistry 236: 239-246.
    • (1961) Journal of Biological Chemistry , vol.236 , pp. 239-246
    • Hess, B.1    Chance, B.2
  • 168
    • 0029844569 scopus 로고    scopus 로고
    • Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae
    • Hoffman M, Chiang H-L. 1996. Isolation of degradation-deficient mutants defective in the targeting of fructose-1,6-bisphosphatase into the vacuole for degradation in Saccharomyces cerevisiae. Genetics 143: 1555-1566.
    • (1996) Genetics , vol.143 , pp. 1555-1566
    • Hoffman, M.1    Chiang, H.-L.2
  • 169
    • 0017056930 scopus 로고
    • Catabolite inactivation in yeast
    • Holzer H. 1976. Catabolite inactivation in yeast. Trends in Biochemical Sciences 1: 178-181.
    • (1976) Trends in Biochemical Sciences , vol.1 , pp. 178-181
    • Holzer, H.1
  • 170
    • 0013363891 scopus 로고
    • Zusammenhang zwischen Wachstum und aerober Gärung. I. Versuche mit Hefezellen
    • Holzer H, Holzer E, Schultz G. 1955. Zusammenhang zwischen Wachstum und aerober Gärung. I. Versuche mit Hefezellen. Biochemische Zeitschrift 326: 385-404.
    • (1955) Biochemische Zeitschrift , vol.326 , pp. 385-404
    • Holzer, H.1    Holzer, E.2    Schultz, G.3
  • 172
    • 0037040938 scopus 로고    scopus 로고
    • Two distinct proteolytic systems responsible for glucose-induced degradation of fructose-1,6-bisphosphatase and the Ga12p transporter in the yeast Saccharomyces cerevisiae share the same protein components of the glucose signaling pathway
    • Horak J, Regelmann J, Wolf DH. 2002. Two distinct proteolytic systems responsible for glucose-induced degradation of fructose-1,6-bisphosphatase and the Ga12p transporter in the yeast Saccharomyces cerevisiae share the same protein components of the glucose signaling pathway. Journal of Biological Chemistry 277: 8248-8254.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 8248-8254
    • Horak, J.1    Regelmann, J.2    Wolf, D.H.3
  • 173
    • 0031047133 scopus 로고    scopus 로고
    • Catabolite inactivation of the galactose transporter in the yeast Saccharomyces cerevisiae: Ubiquitination, endocytosis, and degradation in the vacuole
    • Horak J, Wolf DH. 1997. Catabolite inactivation of the galactose transporter in the yeast Saccharomyces cerevisiae: ubiquitination, endocytosis, and degradation in the vacuole. Journal of Bacteriology 179: 1541-1549.
    • (1997) Journal of Bacteriology , vol.179 , pp. 1541-1549
    • Horak, J.1    Wolf, D.H.2
  • 174
    • 0035039154 scopus 로고    scopus 로고
    • Glucose-induced monoubiquitination of the Saccharomyces cerevisiae galactose transporter is sufficient to signal its internalization
    • Horak J, Wolf DH. 2001. Glucose-induced monoubiquitination of the Saccharomyces cerevisiae galactose transporter is sufficient to signal its internalization. Journal of Bacteriology 183: 3083-3088.
    • (2001) Journal of Bacteriology , vol.183 , pp. 3083-3088
    • Horak, J.1    Wolf, D.H.2
  • 175
    • 0018164695 scopus 로고
    • The mechanism of substrate activation of pyruvate decarboxylase: A first approach
    • Hübner G, Weidhase R, Schellenberger A. 1978. The mechanism of substrate activation of pyruvate decarboxylase: a first approach. European Journal of Biochemistry 92: 175-181.
    • (1978) European Journal of Biochemistry , vol.92 , pp. 175-181
    • Hübner, G.1    Weidhase, R.2    Schellenberger, A.3
  • 176
    • 0001007512 scopus 로고
    • The Crabtree effect: A review
    • Ibsen KH. 1961. The Crabtree effect: a review. Cancer Research 21: 829-841.
    • (1961) Cancer Research , vol.21 , pp. 829-841
    • Ibsen, K.H.1
  • 177
    • 0009575249 scopus 로고
    • Interrelationships of metabolic pathways in the Ehrlich ascites carcinoma cells I. Glycolysis and respiration (Crabtree effect)
    • Ibsen KH, Coe EL, McKee RW. 1958. Interrelationships of metabolic pathways in the Ehrlich ascites carcinoma cells I. Glycolysis and respiration (Crabtree effect). Biochimica et Biophysica Acta 30: 384-400.
    • (1958) Biochimica Et Biophysica Acta , vol.30 , pp. 384-400
    • Ibsen, K.H.1    Coe, E.L.2    McKee, R.W.3
  • 179
    • 0014667134 scopus 로고
    • The step sensitive to catabolite repression and its reversal by 3′-5′ cyclic AMP during induced synthesis of β-galactosidase in E. coli
    • Jacquet M, Kepes A. 1969. The step sensitive to catabolite repression and its reversal by 3′-5′ cyclic AMP during induced synthesis of β-galactosidase in E. coli. Biochemical and Biophysical Research Communications 36: 84-92.
    • (1969) Biochemical and Biophysical Research Communications , vol.36 , pp. 84-92
    • Jacquet, M.1    Kepes, A.2
  • 180
    • 25844525427 scopus 로고
    • Aldehyde oxidation I. Dehydrogenase from Pseudomonas fluorescens
    • Jakoby WB. 1958. Aldehyde oxidation I. Dehydrogenase from Pseudomonas fluorescens. Journal of Biological Chemistry 232: 75-87.
    • (1958) Journal of Biological Chemistry , vol.232 , pp. 75-87
    • Jakoby, W.B.1
  • 181
    • 0030468365 scopus 로고    scopus 로고
    • Glucose regulates protein interactions within the yeast SNF1 protein kinase complex
    • Jiang R, Carlson M. 1996. Glucose regulates protein interactions within the yeast SNF1 protein kinase complex. Genes and Development 10: 3105-3115.
    • (1996) Genes and Development , vol.10 , pp. 3105-3115
    • Jiang, R.1    Carlson, M.2
  • 182
    • 0014300661 scopus 로고
    • Dissolution of yeast glucan induced by 2-deoxyglucose
    • Johnson BF 1968. Dissolution of yeast glucan induced by 2-deoxyglucose. Experimental Cell Research 50: 692-694.
    • (1968) Experimental Cell Research , vol.50 , pp. 692-694
    • Johnson, B.F.1
  • 183
    • 0014259864 scopus 로고
    • Lysis of yeast cell walls induced by 2-deoxyglucose at their sites of glucan synthesis
    • Johnson BF 1968. Lysis of yeast cell walls induced by 2-deoxyglucose at their sites of glucan synthesis. Journal of Bacteriology 95: 1169-1172.
    • (1968) Journal of Bacteriology , vol.95 , pp. 1169-1172
    • Johnson, B.F.1
  • 184
    • 0017600514 scopus 로고
    • Proteinase mutants of Saccharomyces cerevisiae
    • Jones EW. 1977. Proteinase mutants of Saccharomyces cerevisiae. Genetics 85: 23-33.
    • (1977) Genetics , vol.85 , pp. 23-33
    • Jones, E.W.1
  • 185
    • 0020338057 scopus 로고
    • PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae
    • Jones EW, Zubenko GS, Parker RR. 1982. PEP4 gene function is required for expression of several vacuolar hydrolases in Saccharomyces cerevisiae. Genetics 102: 665-677.
    • (1982) Genetics , vol.102 , pp. 665-677
    • Jones, E.W.1    Zubenko, G.S.2    Parker, R.R.3
  • 188
    • 0022989417 scopus 로고
    • Regulation of carbon metabolism in Saccharomyces cerevisiae and related yeasts
    • Käppeli G. 1986. Regulation of carbon metabolism in Saccharomyces cerevisiae and related yeasts. Advances in Microbial Physiology 28: 181-209.
    • (1986) Advances in Microbial Physiology , vol.28 , pp. 181-209
    • Käppeli, G.1
  • 191
    • 0000402167 scopus 로고
    • Oxidation of fatty acids and tricarboxylic acid cycle intermediates by isolated rat liver mitochondria
    • Kennedy EP, Lehninger AL. 1949. Oxidation of fatty acids and tricarboxylic acid cycle intermediates by isolated rat liver mitochondria. Journal of Biological Chemistry 179: 957-972.
    • (1949) Journal of Biological Chemistry , vol.179 , pp. 957-972
    • Kennedy, E.P.1    Lehninger, A.L.2
  • 192
    • 4244087847 scopus 로고
    • Études cinétiques sur la galactoside-perméase d'Escherichia coli
    • Kepes A. 1960. Études cinétiques sur la galactoside-perméase d'Escherichia coli. Biochimica et Biophysica Acta 40: 70-84.
    • (1960) Biochimica Et Biophysica Acta , vol.40 , pp. 70-84
    • Kepes, A.1
  • 194
    • 77956807279 scopus 로고
    • Wladimir Engelhardt: The man and the scientist
    • Kisselev LL. 1990. Wladimir Engelhardt: the man and the scientist. Comprehensive Biochemistry 37: 67-99.
    • (1990) Comprehensive Biochemistry , vol.37 , pp. 67-99
    • Kisselev, L.L.1
  • 195
    • 0024295997 scopus 로고
    • Proteinase yscE of yeast shows homology with the 20 S cylinder particles of Xenopus laevis
    • Kleinschmidt JA, Escher C, Wolf DH. 1988. Proteinase yscE of yeast shows homology with the 20 S cylinder particles of Xenopus laevis. FEBS Letters 239: 35-40.
    • (1988) FEBS Letters , vol.239 , pp. 35-40
    • Kleinschmidt, J.A.1    Escher, C.2    Wolf, D.H.3
  • 196
    • 0037807217 scopus 로고
    • The suitability of disaccharides as respiration and assimilation substrates for yeasts which do not ferment these sugars
    • Kluyver AJ, Custers MTJ. 1940. The suitability of disaccharides as respiration and assimilation substrates for yeasts which do not ferment these sugars. Antonie van Leeuwenhoek 6: 121-162.
    • (1940) Antonie Van Leeuwenhoek , vol.6 , pp. 121-162
    • Kluyver, A.J.1    Custers, M.T.J.2
  • 198
    • 0038698464 scopus 로고
    • 14C]acetate by Pseudomonas fluorescens, and by a Corynebacterium, grown on ammonium acetate
    • 14C]acetate by Pseudomonas fluorescens, and by a Corynebacterium, grown on ammonium acetate. Biochemical Journal 68: 531-537.
    • (1958) Biochemical Journal , vol.68 , pp. 531-537
    • Kornberg, H.L.1
  • 200
    • 0000877111 scopus 로고
    • The glyoxylate cycle as a stage in the conversion of fat to carbohydrate in castor beans
    • Kornberg HL, Beevers H. 1957. The glyoxylate cycle as a stage in the conversion of fat to carbohydrate in castor beans. Biochimica et Biophysica Acta 26: 531-653.
    • (1957) Biochimica Et Biophysica Acta , vol.26 , pp. 531-653
    • Kornberg, H.L.1    Beevers, H.2
  • 201
    • 0000396226 scopus 로고
    • 4-dicarboxylic acids from acetate by a 'glyoxylate bypass' of the tricarboxylic acid cycle
    • 4-dicarboxylic acids from acetate by a 'glyoxylate bypass' of the tricarboxylic acid cycle. Biochimica et Biophysica Acta 24: 651-653.
    • (1957) Biochimica Et Biophysica Acta , vol.24 , pp. 651-653
    • Kornberg, H.L.1    Madsen, N.B.2
  • 202
    • 25844450054 scopus 로고
    • 2 compounds in micro-organisms 5. Biosynthesis of cell materials from acetate in Escherichia coli
    • 2 compounds in micro-organisms 5. Biosynthesis of cell materials from acetate in Escherichia coli. Biochemical Journal 77: 438-445.
    • (1960) Biochemical Journal , vol.77 , pp. 438-445
    • Kornberg, H.L.1    Phizackerley, P.J.R.2    Sadler, J.R.3
  • 203
    • 0014036735 scopus 로고
    • Properties of the sugar carrier in baker's yeast II. Specificity of transport
    • Kotyk A. 1967. Properties of the sugar carrier in baker's yeast II. Specificity of transport. Folia Microbiologica
    • (1967) Folia Microbiologica , vol.12 , pp. 121-131
    • Kotyk, A.1
  • 204
    • 0013852587 scopus 로고
    • Uphill transport of sugars in the yeast Rhodotorula gracilis
    • Kotyk A, Höfer M. 1965. Uphill transport of sugars in the yeast Rhodotorula gracilis. Biochimica et Biophysica Acta 101: 410-422.
    • (1965) Biochimica Et Biophysica Acta , vol.101 , pp. 410-422
    • Kotyk, A.1    Höfer, M.2
  • 205
    • 0015453103 scopus 로고
    • The Pasteur effect and the relations between respiration and fermentation
    • Krebs HA. 1972. The Pasteur effect and the relations between respiration and fermentation. Essays in Biochemistry 8: 1-34.
    • (1972) Essays in Biochemistry , vol.8 , pp. 1-34
    • Krebs, H.A.1
  • 208
  • 210
    • 0018692423 scopus 로고
    • Energetic irrelevance of aerobiosis for S. cerevisiae growing on sugars
    • Lagunas R. 1979. Energetic irrelevance of aerobiosis for S. cerevisiae growing on sugars. Molecular and Cellular Biochemistry 27: 139-146.
    • (1979) Molecular and Cellular Biochemistry , vol.27 , pp. 139-146
    • Lagunas, R.1
  • 211
    • 0022946405 scopus 로고
    • Misconceptions about the energy metabolism of Saccharomyces cerevisiae
    • Lagunas R. 1986. Misconceptions about the energy metabolism of Saccharomyces cerevisiae. Yeast 2: 221-228.
    • (1986) Yeast , vol.2 , pp. 221-228
    • Lagunas, R.1
  • 212
    • 0020356027 scopus 로고
    • Mechanisms of appearance of the Pasteur effect in Saccharomyces cerevisiae: Inactivation of sugar transport systems
    • Lagunas R, Dominguez C, Busturia A, Sáez MJ. 1982. Mechanisms of appearance of the Pasteur effect in Saccharomyces cerevisiae: inactivation of sugar transport systems. Journal of Bacteriology 152: 19-25.
    • (1982) Journal of Bacteriology , vol.152 , pp. 19-25
    • Lagunas, R.1    Dominguez, C.2    Busturia, A.3    Sáez, M.J.4
  • 213
    • 0021105641 scopus 로고
    • Role of phosphate in the regulation of the Pasteur effect in Saccharomyces cerevisiae
    • Lagunas R, Gancedo C. 1983. Role of phosphate in the regulation of the Pasteur effect in Saccharomyces cerevisiae. European Journal of Biochemistry 137: 479-483.
    • (1983) European Journal of Biochemistry , vol.137 , pp. 479-483
    • Lagunas, R.1    Gancedo, C.2
  • 214
    • 0014232086 scopus 로고
    • External enzymes of yeast: Their nature and formation
    • Lampen JO. 1968. External enzymes of yeast: their nature and formation. Antonie van Leeuwenhoek 34: 1-18.
    • (1968) Antonie Van Leeuwenhoek , vol.34 , pp. 1-18
    • Lampen, J.O.1
  • 215
    • 1642496024 scopus 로고
    • Tissue metabolism under the influence of carbon monoxide
    • Laser H. 1937. Tissue metabolism under the influence of carbon monoxide. Biochemical Journal 31: 1677-1682.
    • (1937) Biochemical Journal , vol.31 , pp. 1677-1682
    • Laser, H.1
  • 219
    • 4043146265 scopus 로고
    • The direct fermentation of maltose by yeast
    • Leibowitz J, Hestrin S. 1939. The direct fermentation of maltose by yeast. Enzymologia 6: 15-26.
    • (1939) Enzymologia , vol.6 , pp. 15-26
    • Leibowitz, J.1    Hestrin, S.2
  • 220
    • 0141481527 scopus 로고
    • Alcoholic fermentation of the oligosaccharides
    • Leibowitz J, Hestrin S. 1945. Alcoholic fermentation of the oligosaccharides. Advances in Enzymology 5: 87-127.
    • (1945) Advances in Enzymology , vol.5 , pp. 87-127
    • Leibowitz, J.1    Hestrin, S.2
  • 221
    • 0017343779 scopus 로고
    • Pathways of ultraviolet mutability in Saccharomyces cerevisiae. III. Genetic analysis and properties of mutants resistant to ultraviolet-induced forward mutation
    • Lemontt JF. 1977. Pathways of ultraviolet mutability in Saccharomyces cerevisiae. III. Genetic analysis and properties of mutants resistant to ultraviolet-induced forward mutation. Mutation Research 43: 179-204.
    • (1977) Mutation Research , vol.43 , pp. 179-204
    • Lemontt, J.F.1
  • 222
    • 0018870829 scopus 로고
    • Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerevisiae by glucose
    • Lenz A-G, Holzer H. 1980. Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerevisiae by glucose. FEBS Letters 109: 271-274.
    • (1980) FEBS Letters , vol.109 , pp. 271-274
    • Lenz, A.-G.1    Holzer, H.2
  • 223
    • 0029863284 scopus 로고    scopus 로고
    • 6 zinc cluster transcriptional activator: A new role for SNF1 in the glucose response
    • 6 zinc cluster transcriptional activator: a new role for SNF1 in the glucose response. Molecular and Cellular Biology 16: 1921-1928.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 1921-1928
    • Lesage, P.1    Yang, X.2    Carlson, M.3
  • 224
    • 0030874516 scopus 로고    scopus 로고
    • Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: Coupling glucose sensing to gene expression and the cell cycle
    • Li FN, Johnston M. 1997. Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle. EMBO Journal 16: 5629-5638.
    • (1997) EMBO Journal , vol.16 , pp. 5629-5638
    • Li, F.N.1    Johnston, M.2
  • 225
    • 0038644946 scopus 로고    scopus 로고
    • Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination of rDNA loci, and silencing
    • Lin SS, Manchester JK, Gordon JL. 2003. Sip2, an N-myristoylated beta subunit of Snf1 kinase, regulates aging in Saccharomyces cerevisiae by affecting cellular histone kinase activity, recombination of rDNA loci, and silencing. Journal of Biological Chemistry 278: 13390-13397.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 13390-13397
    • Lin, S.S.1    Manchester, J.K.2    Gordon, J.L.3
  • 226
    • 25844451075 scopus 로고
    • Über die oxydative Hemmbarkeit der Glykolyse und den Mechanismus der Pasteurschen Reaktion
    • Lipmann F. 1933. Über die oxydative Hemmbarkeit der Glykolyse und den Mechanismus der Pasteurschen Reaktion. Biochemische Zeitschrift 265: 133-140.
    • (1933) Biochemische Zeitschrift , vol.265 , pp. 133-140
    • Lipmann, F.1
  • 227
    • 25844485420 scopus 로고
    • Über die Hemmung der Mazerationssaftgärung durch Sauerstoff in Gegenwart positiver Oxydoreduktionssysteme
    • Lipmann F. 1934. Über die Hemmung der Mazerationssaftgärung durch Sauerstoff in Gegenwart positiver Oxydoreduktionssysteme. Biochemische Zeitschrift 268: 205-213.
    • (1934) Biochemische Zeitschrift , vol.268 , pp. 205-213
    • Lipmann, F.1
  • 228
    • 0343940524 scopus 로고
    • Pasteur effect
    • University of Wisconsin Press: Madison, WI
    • Lipmann F. 1942. Pasteur effect. In A Symposium on Respiratory Enzymes. University of Wisconsin Press: Madison, WI; 48-73.
    • (1942) A Symposium on Respiratory Enzymes , pp. 48-73
    • Lipmann, F.1
  • 229
    • 0021104261 scopus 로고
    • Glycolysis and respiration in yeasts. The Pasteur effect studied by mass spectrometry
    • Lloyd D, Kristensen B, Degn H. 1983. Glycolysis and respiration in yeasts. The Pasteur effect studied by mass spectrometry. Biochemical Journal 212: 749-754.
    • (1983) Biochemical Journal , vol.212 , pp. 749-754
    • Lloyd, D.1    Kristensen, B.2    Degn, H.3
  • 230
    • 0017382789 scopus 로고
    • Physiological role of glucose-phosphorylating enzymes in Saccharomyces cerevisiae
    • Lobo Z, Maitra PK. 1977. Physiological role of glucose-phosphorylating enzymes in Saccharomyces cerevisiae. Archives of Biochemistry and Biophysics 182: 639-645.
    • (1977) Archives of Biochemistry and Biophysics , vol.182 , pp. 639-645
    • Lobo, Z.1    Maitra, P.K.2
  • 231
    • 0017770845 scopus 로고
    • Resistance to 2-deoxyglucose in yeast: A direct selection of mutants lacking glucose-phosphorylating enzymes
    • Lobo Z, Maitra PK. 1977. Resistance to 2-deoxyglucose in yeast: a direct selection of mutants lacking glucose-phosphorylating enzymes. Molecular and General Genetics 157: 297-300.
    • (1977) Molecular and General Genetics , vol.157 , pp. 297-300
    • Lobo, Z.1    Maitra, P.K.2
  • 232
    • 0017650913 scopus 로고
    • Genetics of yeast hexokinase
    • Lobo Z, Maitra PK. 1977. Genetics of yeast hexokinase. Genetics 86: 727-744.
    • (1977) Genetics , vol.86 , pp. 727-744
    • Lobo, Z.1    Maitra, P.K.2
  • 234
    • 2242472523 scopus 로고
    • Inhibition of phosphorylation by azide in kidney homogenate
    • Loomis WF, Lipmann F. 1949. Inhibition of phosphorylation by azide in kidney homogenate. Journal of Biological Chemistry 179: 503-504.
    • (1949) Journal of Biological Chemistry , vol.179 , pp. 503-504
    • Loomis, W.F.1    Lipmann, F.2
  • 236
    • 0031761689 scopus 로고    scopus 로고
    • Characterization of three related glucose repressors and genes they regulate in Saccharomyces cerevisiae
    • Lutfiyya LL, Iyer VR, DeRisi J, DeVit MJ, Brown PO, Johnston M. 1998. Characterization of three related glucose repressors and genes they regulate in Saccharomyces cerevisiae. Genetics 150: 1377-1391.
    • (1998) Genetics , vol.150 , pp. 1377-1391
    • Lutfiyya, L.L.1    Iyer, V.R.2    DeRisi, J.3    DeVit, M.J.4    Brown, P.O.5    Johnston, M.6
  • 237
    • 0029783926 scopus 로고    scopus 로고
    • Two zinc-finger-containing repressors are responsible for glucose repression of SUC2 expression
    • Lutfiyya LL, Johnston M. 1996. Two zinc-finger-containing repressors are responsible for glucose repression of SUC2 expression. Molecular and Cellular Biology 16: 4790-4797.
    • (1996) Molecular and Cellular Biology , vol.16 , pp. 4790-4797
    • Lutfiyya, L.L.1    Johnston, M.2
  • 238
    • 0014409812 scopus 로고
    • Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae 1. Physiological control of ADH-2 and properties of ADH-2 and ADH-4
    • Lutstorf U, Megnet R. 1968. Multiple forms of alcohol dehydrogenase in Saccharomyces cerevisiae 1. Physiological control of ADH-2 and properties of ADH-2 and ADH-4. Archives of Biochemistry and Biophysics 126: 933-944.
    • (1968) Archives of Biochemistry and Biophysics , vol.126 , pp. 933-944
    • Lutstorf, U.1    Megnet, R.2
  • 240
    • 0024313495 scopus 로고
    • The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae
    • Ma H, Bloom LM, Walsh CT, Botstein D. 1989. The residual enzymatic phosphorylation activity of hexokinase II mutants is correlated with glucose repression in Saccharomyces cerevisiae. Molecular and Cellular Biology 9: 5643-5649.
    • (1989) Molecular and Cellular Biology , vol.9 , pp. 5643-5649
    • Ma, H.1    Bloom, L.M.2    Walsh, C.T.3    Botstein, D.4
  • 244
    • 0014939505 scopus 로고
    • A glucokinase from Saccharomyces cerevisiae
    • Maitra PK. 1970. A glucokinase from Saccharomyces cerevisiae. Journal of Biological Chemistry 245: 2423-2431.
    • (1970) Journal of Biological Chemistry , vol.245 , pp. 2423-2431
    • Maitra, P.K.1
  • 245
    • 25844454539 scopus 로고
    • Genetics of glucose phosphorylation in yeast
    • Stewart GG, Russell I (eds). Pergamon: Toronto
    • Maitra PK, Lobo Z. 1981. Genetics of glucose phosphorylation in yeast. In Current Developments in Yeast Research, Stewart GG, Russell I (eds). Pergamon: Toronto; 293-297.
    • (1981) Current Developments in Yeast Research , pp. 293-297
    • Maitra, P.K.1    Lobo, Z.2
  • 246
    • 0021088893 scopus 로고
    • Genetics of yeast glucokinase
    • Maitra PK, Lobo Z. 1983. Genetics of yeast glucokinase. Genetics 105: 501-515.
    • (1983) Genetics , vol.105 , pp. 501-515
    • Maitra, P.K.1    Lobo, Z.2
  • 247
    • 0017659917 scopus 로고
    • Catabolite inactivation of the galactose uptake system in yeast
    • Matern H, Holzer H. 1977. Catabolite inactivation of the galactose uptake system in yeast. Journal of Biological Chemistry 252: 6399-6402.
    • (1977) Journal of Biological Chemistry , vol.252 , pp. 6399-6402
    • Matern, H.1    Holzer, H.2
  • 248
    • 0021042207 scopus 로고
    • Cyclic AMP may not be involved in catabolite repression in Saccharomyces cerevisiae: Evidence from mutants unable to synthesize it
    • Matsumoto K, Uno I, Ishikawa T, Oshima Y. 1983. Cyclic AMP may not be involved in catabolite repression in Saccharomyces cerevisiae: evidence from mutants unable to synthesize it. Journal of Bacteriology 156: 898-900.
    • (1983) Journal of Bacteriology , vol.156 , pp. 898-900
    • Matsumoto, K.1    Uno, I.2    Ishikawa, T.3    Oshima, Y.4
  • 250
    • 0020200423 scopus 로고
    • Phosphorylation and inactivation of yeast fructose-bisphosphatase in vivo by glucose and by proton ionophores
    • Mazón MJ, Gancedo JM, Gancedo C. 1982. Phosphorylation and inactivation of yeast fructose-bisphosphatase in vivo by glucose and by proton ionophores. European Journal of Biochemistry 127: 605-608.
    • (1982) European Journal of Biochemistry , vol.127 , pp. 605-608
    • Mazón, M.J.1    Gancedo, J.M.2    Gancedo, C.3
  • 251
    • 0035965277 scopus 로고    scopus 로고
    • Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit
    • McCartney RR, Schmidt MC. 2001. Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit. Journal of Biological Chemistry 276: 36460-36466.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 36460-36466
    • McCartney, R.R.1    Schmidt, M.C.2
  • 252
    • 77957008409 scopus 로고
    • Fructose-1,6-diphosphatase from liver
    • McGilvery RW. 1955. Fructose-1,6-diphosphatase from liver. Methods in Enzymology 2: 543-546.
    • (1955) Methods in Enzymology , vol.2 , pp. 543-546
    • McGilvery, R.W.1
  • 254
    • 0026605247 scopus 로고
    • Genetic analysis of serine biosynthesis and glucose repression in yeast
    • Melcher K, Entian K-D. 1992. Genetic analysis of serine biosynthesis and glucose repression in yeast. Current Genetics 21: 295-300.
    • (1992) Current Genetics , vol.21 , pp. 295-300
    • Melcher, K.1    Entian, K.-D.2
  • 255
    • 1642496022 scopus 로고
    • The photochemical absorption spectra of the Pasteur enzyme and the respiratory ferment in yeast
    • Melnick JL. 1941. The photochemical absorption spectra of the Pasteur enzyme and the respiratory ferment in yeast. Journal of Biological Chemistry 141: 269-281.
    • (1941) Journal of Biological Chemistry , vol.141 , pp. 269-281
    • Melnick, J.L.1
  • 256
    • 0001674481 scopus 로고
    • The photochemical spectrum of cytochrome oxidase
    • Melnick JL. 1942. The photochemical spectrum of cytochrome oxidase. Journal of Biological Chemistry 146: 385-390.
    • (1942) Journal of Biological Chemistry , vol.146 , pp. 385-390
    • Melnick, J.L.1
  • 257
    • 0029823911 scopus 로고    scopus 로고
    • My role in the discovery and classification of the enteroviruses
    • Melnick JL. 1996. My role in the discovery and classification of the enteroviruses. Annual Review of Microbiology 50: 1-24.
    • (1996) Annual Review of Microbiology , vol.50 , pp. 1-24
    • Melnick, J.L.1
  • 260
    • 25844524632 scopus 로고
    • Über den Einfluß des Sauerstoffs auf die alkoholische Gärung der Hefe
    • Meyerhof O. 1925. Über den Einfluß des Sauerstoffs auf die alkoholische Gärung der Hefe. Biochemische Zeitschrift 162: 43-86.
    • (1925) Biochemische Zeitschrift , vol.162 , pp. 43-86
    • Meyerhof, O.1
  • 261
    • 0020611386 scopus 로고
    • Pleiotropic mutations regulating resistance to glucose repression in Saccharomyces carlsbergensis are allelic to the structural gene for hexokinase B
    • Michels CA, Hahnenberger KM, Sylvestre Y. 1983. Pleiotropic mutations regulating resistance to glucose repression in Saccharomyces carlsbergensis are allelic to the structural gene for hexokinase B. Journal of Bacteriology 153: 574-578.
    • (1983) Journal of Bacteriology , vol.153 , pp. 574-578
    • Michels, C.A.1    Hahnenberger, K.M.2    Sylvestre, Y.3
  • 262
    • 0038649638 scopus 로고    scopus 로고
    • The proteasome - An emerging therapeutic target in cancer
    • Mitchell BS. 2003. The proteasome - an emerging therapeutic target in cancer. New England Journal of Medicine 348: 2597-2598.
    • (2003) New England Journal of Medicine , vol.348 , pp. 2597-2598
    • Mitchell, B.S.1
  • 263
    • 0015610724 scopus 로고
    • Saccharomyces mutants with invertase formation resistant to repression by hexoses
    • Montenecourt BS, Kuo S-C, Lampen JO. 1973. Saccharomyces mutants with invertase formation resistant to repression by hexoses. Journal of Bacteriology 114: 233-238.
    • (1973) Journal of Bacteriology , vol.114 , pp. 233-238
    • Montenecourt, B.S.1    Kuo, S.-C.2    Lampen, J.O.3
  • 264
    • 0025822310 scopus 로고
    • AAR1/TUP1 protein, with a structure similar to that of the β subunit of G proteins, is required for a1-α2 and α2 repression in cell type control of Saccharomyces cerevisiae
    • Mukai Y, Harashima S, Oshima Y. 1991. AAR1/TUP1 protein, with a structure similar to that of the β subunit of G proteins, is required for a1-α2 and α2 repression in cell type control of Saccharomyces cerevisiae. Molecular and Cellular Biology 11: 3773-3779.
    • (1991) Molecular and Cellular Biology , vol.11 , pp. 3773-3779
    • Mukai, Y.1    Harashima, S.2    Oshima, Y.3
  • 265
    • 0019882147 scopus 로고
    • Regulation of fructose-1,6-bisphosphatase in yeast by phosphorylation/dephosphorylation
    • Müller D, Holzer H. 1981. Regulation of fructose-1,6-bisphosphatase in yeast by phosphorylation/dephosphorylation. Biochemical and Biophysical Research Communications 103: 926-933.
    • (1981) Biochemical and Biophysical Research Communications , vol.103 , pp. 926-933
    • Müller, D.1    Holzer, H.2
  • 266
    • 0019497190 scopus 로고
    • Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae
    • Müller M, Müller H, Holzer H. 1981. Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae. Journal of Biological Chemistry 256: 723-727.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 723-727
    • Müller, M.1    Müller, H.2    Holzer, H.3
  • 268
    • 0017814202 scopus 로고
    • Evidence for catabolite degradation in the glucose-dependent inactivation of yeast cytoplasmic malate dehydrogenase
    • Neeff J, Hägele E, Nauhaus J, Heer U, Mecke D. 1978. Evidence for catabolite degradation in the glucose-dependent inactivation of yeast cytoplasmic malate dehydrogenase. European Journal of Biochemistry 87: 489-495.
    • (1978) European Journal of Biochemistry , vol.87 , pp. 489-495
    • Neeff, J.1    Hägele, E.2    Nauhaus, J.3    Heer, U.4    Mecke, D.5
  • 269
    • 0017873762 scopus 로고
    • Catabolite inactivation of yeast cytoplasmic malate dehydrogenase. A process independent of protein synthesis
    • Neeff J, Heer U. 1978. Catabolite inactivation of yeast cytoplasmic malate dehydrogenase. A process independent of protein synthesis. FEBS Letters 85: 233-236.
    • (1978) FEBS Letters , vol.85 , pp. 233-236
    • Neeff, J.1    Heer, U.2
  • 270
    • 0017663782 scopus 로고
    • In vivo and in vitro studies on the glucose-dependent inactivation of yeast cytoplasmic malate dehydrogenase
    • Neeff J, Mecke D. 1977. In vivo and in vitro studies on the glucose-dependent inactivation of yeast cytoplasmic malate dehydrogenase. Archives of Microbiology 115: 55-60.
    • (1977) Archives of Microbiology , vol.115 , pp. 55-60
    • Neeff, J.1    Mecke, D.2
  • 271
    • 0025944734 scopus 로고
    • Control of yeast GAL genes by MIG1 repressor: A transcriptional cascade in the glucose response
    • Nehlin JO, Carlberg M, Ronne H. 1991. Control of yeast GAL genes by MIG1 repressor: a transcriptional cascade in the glucose response. EMBO Journal 10: 3373-3377.
    • (1991) EMBO Journal , vol.10 , pp. 3373-3377
    • Nehlin, J.O.1    Carlberg, M.2    Ronne, H.3
  • 272
    • 0025004155 scopus 로고
    • Yeast MIG1 repressor is related to the mammalian early growth response and Wilms' tumour finger proteins
    • Nehlin JO, Ronne H. 1990. Yeast MIG1 repressor is related to the mammalian early growth response and Wilms' tumour finger proteins. EMBO Journal 9: 2891-2898.
    • (1990) EMBO Journal , vol.9 , pp. 2891-2898
    • Nehlin, J.O.1    Ronne, H.2
  • 273
    • 0023140958 scopus 로고
    • Mutations causing constitutive invertase synthesis in yeast: Genetic interactions with snf mutations
    • Neigeborn L, Carlson M. 1987. Mutations causing constitutive invertase synthesis in yeast: genetic interactions with snf mutations. Genetics 115: 247-253.
    • (1987) Genetics , vol.115 , pp. 247-253
    • Neigeborn, L.1    Carlson, M.2
  • 274
    • 0000545927 scopus 로고
    • Die elektromotorische Wirksamkeit der Jonen
    • Nernst W. 1889. Die elektromotorische Wirksamkeit der Jonen. Zeitschrift für Physikalische Chemie 4: 129-181.
    • (1889) Zeitschrift Für Physikalische Chemie , vol.4 , pp. 129-181
    • Nernst, W.1
  • 275
    • 0025901117 scopus 로고
    • Characterization of the Hex2 protein, a negative regulatory element necessary for glucose repression in yeast
    • Niederacher D, Entian K-D. 1991. Characterization of the Hex2 protein, a negative regulatory element necessary for glucose repression in yeast. European Journal of Biochemistry 200: 311-319.
    • (1991) European Journal of Biochemistry , vol.200 , pp. 311-319
    • Niederacher, D.1    Entian, K.-D.2
  • 276
    • 0003450992 scopus 로고    scopus 로고
    • Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. (accessed 3 February 2005)
    • Nomenclature Committee of the International Union of Biochemistry and Molecular Biology. 2005. Enzyme Nomenclature; http://www.chem.qmul.ac.uk/iubmb/enzyme/EC3/intro (accessed 3 February 2005).
    • (2005) Enzyme Nomenclature
  • 277
    • 0038458670 scopus 로고
    • Über die Bildung des Hexose-monophosphorsäure-esters und dessen Umwandlung in Fructose-diphosphorsäure-ester im Muskel
    • Ostern P, Guthke JA, Terszakowee J. 1936. Über die Bildung des Hexose-monophosphorsäure-esters und dessen Umwandlung in Fructose-diphosphorsäure-ester im Muskel. Hoppe-Seyler's Zeitschrift für Physiologische Chemie 243: 9-37.
    • (1936) Hoppe-Seyler's Zeitschrift Für Physiologische Chemie , vol.243 , pp. 9-37
    • Ostern, P.1    Guthke, J.A.2    Terszakowee, J.3
  • 278
    • 0032519837 scopus 로고    scopus 로고
    • Negative control of the Migp repressor by Snf1p-dependent phosphorylation in the absence of glucose
    • Östling J, Ronne H. 1998. Negative control of the Migp repressor by Snf1p-dependent phosphorylation in the absence of glucose. European Journal of Biochemistry 252: 162-168.
    • (1998) European Journal of Biochemistry , vol.252 , pp. 162-168
    • Östling, J.1    Ronne, H.2
  • 279
    • 0001778610 scopus 로고
    • Reaction products of yeast fermentations
    • Oura E. 1977. Reaction products of yeast fermentations. Process Biochemistry 12: ,35 19-21.
    • (1977) Process Biochemistry , vol.12 , pp. 3519-3521
    • Oura, E.1
  • 280
    • 0017196989 scopus 로고
    • Biochemical studies on the cytosine permease of Saccharomyces cerevisiae
    • Parlebas N, Chevalier MR. 1976. Biochemical studies on the cytosine permease of Saccharomyces cerevisiae. FEBS Letters 65: 327-334.
    • (1976) FEBS Letters , vol.65 , pp. 327-334
    • Parlebas, N.1    Chevalier, M.R.2
  • 282
    • 0001430330 scopus 로고
    • Mémoire sur la fermentation alcoolique
    • Pasteur L. 1860. Mémoire sur la fermentation alcoolique. Annales de Chimie et de Physique 58: 323-426.
    • (1860) Annales De Chimie Et De Physique , vol.58 , pp. 323-426
    • Pasteur, L.1
  • 284
    • 0141479514 scopus 로고
    • Influence de l'oxygène sur le développement de la levûre et la fermentation alcoolique
    • Pasteur [L]. (Résumé Séance du 28 juin 1861)
    • Pasteur [L]. 1861. Influence de l'oxygène sur le développement de la levûre et la fermentation alcoolique. Bulletin de la Société de Paris (Résumé Séance du 28 juin 1861); 79-80.
    • (1861) Bulletin De La Société De Paris , pp. 79-80
  • 285
    • 0027432307 scopus 로고
    • Binding of acylated peptides and fatty acids to phospolipid vesicles: Pertinence to myristoylated proteins
    • Peitzsch RM, McLaughlin S. 1993. Binding of acylated peptides and fatty acids to phospolipid vesicles: pertinence to myristoylated proteins. Biochemistry 32: 10436-10443.
    • (1993) Biochemistry , vol.32 , pp. 10436-10443
    • Peitzsch, R.M.1    McLaughlin, S.2
  • 286
    • 0025160870 scopus 로고
    • Purification and characterization of glycogen synthase from a glycogen-deficient strain of Saccharomyces cerevisiae
    • Peng Z-Y, Trumbly RJ, Reimann EM. 1990. Purification and characterization of glycogen synthase from a glycogen-deficient strain of Saccharomyces cerevisiae. Journal of Biological Chemistry 265: 13871-13877.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 13871-13877
    • Peng, Z.-Y.1    Trumbly, R.J.2    Reimann, E.M.3
  • 287
    • 0014440704 scopus 로고
    • Promitochondria of anaerobically grown yeast. III. Morphology
    • Plattner H, Schatz G. 1969. Promitochondria of anaerobically grown yeast. III. Morphology. Biochemistry 8: 339-343.
    • (1969) Biochemistry , vol.8 , pp. 339-343
    • Plattner, H.1    Schatz, G.2
  • 288
    • 0023086699 scopus 로고
    • Isolation and characterization of a mutant of Schwanniomyces castellii with altered respiration
    • Poinsot C, Moulin G, Claisse M, Galzy P. 1987. Isolation and characterization of a mutant of Schwanniomyces castellii with altered respiration. Antonie van Leeuwenhoek 53: 65-75.
    • (1987) Antonie Van Leeuwenhoek , vol.53 , pp. 65-75
    • Poinsot, C.1    Moulin, G.2    Claisse, M.3    Galzy, P.4
  • 289
    • 0001363302 scopus 로고
    • Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources
    • Polakis ES, Bartley W. 1965. Changes in the enzyme activities of Saccharomyces cerevisiae during aerobic growth on different carbon sources. Biochemical Journal 97: 284-297.
    • (1965) Biochemical Journal , vol.97 , pp. 284-297
    • Polakis, E.S.1    Bartley, W.2
  • 290
    • 0001577283 scopus 로고
    • Changes in the structure and enzyme activity of Saccharomyces cerevisiae in response to changes in the environment
    • Polakis ES, Bartley W, Meek GA. 1964. Changes in the structure and enzyme activity of Saccharomyces cerevisiae in response to changes in the environment. Biochemical Journal 90: 369-374.
    • (1964) Biochemical Journal , vol.90 , pp. 369-374
    • Polakis, E.S.1    Bartley, W.2    Meek, G.A.3
  • 291
    • 0001363303 scopus 로고
    • Changes in the activities of respiratory enzymes during the aerobic growth of yeast on different carbon sources
    • Polakis ES, Bartley W, Meek GA. 1965. Changes in the activities of respiratory enzymes during the aerobic growth of yeast on different carbon sources. Biochemical Journal 97: 298-302.
    • (1965) Biochemical Journal , vol.97 , pp. 298-302
    • Polakis, E.S.1    Bartley, W.2    Meek, G.A.3
  • 292
    • 0029610003 scopus 로고
    • CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae
    • Proft M, Kötter P, Hedges D, Bojunga N, Entian K-D. 1995. CAT5, a new gene necessary for derepression of gluconeogenic enzymes in Saccharomyces cerevisiae. EMBO Journal 14: 6116-6126.
    • (1995) EMBO Journal , vol.14 , pp. 6116-6126
    • Proft, M.1    Kötter, P.2    Hedges, D.3    Bojunga, N.4    Entian, K.-D.5
  • 294
    • 1542688145 scopus 로고
    • Carbohydrate metabolism in ascites tumour cells
    • Racker E. 1956. Carbohydrate metabolism in ascites tumour cells. Annals of the New York Academy of Sciences 63: 1017-1021.
    • (1956) Annals of the New York Academy of Sciences , vol.63 , pp. 1017-1021
    • Racker, E.1
  • 295
    • 0016300146 scopus 로고
    • History of the Pasteur effect and its pathobiology
    • Racker E. 1974. History of the Pasteur effect and its pathobiology. Molecular and Cellular Biochemistry 5: 17-23.
    • (1974) Molecular and Cellular Biochemistry , vol.5 , pp. 17-23
    • Racker, E.1
  • 296
    • 0032870144 scopus 로고    scopus 로고
    • Deregulation of gluconeogenic structural genes by variants of the transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae
    • Rahner A, Hiesinger M, Schüller H-J. 1999. Deregulation of gluconeogenic structural genes by variants of the transcriptional activator Cat8p of the yeast Saccharomyces cerevisiae. Molecular Microbiology 34: 146-156.
    • (1999) Molecular Microbiology , vol.34 , pp. 146-156
    • Rahner, A.1    Hiesinger, M.2    Schüller, H.-J.3
  • 297
    • 0030015273 scopus 로고    scopus 로고
    • Dual influence of the yeast Cat1p (Snf1p) protein kinase on carbon source-dependent transcriptional activation of gluconeogenic genes by the regulatory gene CAT8
    • Rahner A, Schöler A, Martens E, Gollwitzer B, Schüller H-J. 1996. Dual influence of the yeast Cat1p (Snf1p) protein kinase on carbon source-dependent transcriptional activation of gluconeogenic genes by the regulatory gene CAT8. Nucleic Acids Research 24: 2331-2337.
    • (1996) Nucleic Acids Research , vol.24 , pp. 2331-2337
    • Rahner, A.1    Schöler, A.2    Martens, E.3    Gollwitzer, B.4    Schüller, H.-J.5
  • 298
    • 0030987084 scopus 로고    scopus 로고
    • Glucose derepression of gluconeogenic enzymes in Saccharomyces cerevisiae correlates with phosphorylation of the gene activator Cat8P
    • Randez-Gil F, Bojunga N, Proft M, Entian K-D. 1997. Glucose derepression of gluconeogenic enzymes in Saccharomyces cerevisiae correlates with phosphorylation of the gene activator Cat8P. Molecular and Cellular Biology 17: 2502-2510.
    • (1997) Molecular and Cellular Biology , vol.17 , pp. 2502-2510
    • Randez-Gil, F.1    Bojunga, N.2    Proft, M.3    Entian, K.-D.4
  • 299
    • 0032478569 scopus 로고    scopus 로고
    • Hexokinase PII has a double cytosolic-nuclear localisation in Saccharomyces cerevisiae
    • Randez-Gil F, Herrero P, Sanz P, Prieto JA, Moreno F. 1998. Hexokinase PII has a double cytosolic-nuclear localisation in Saccharomyces cerevisiae. FEBS Letters 425: 475-478.
    • (1998) FEBS Letters , vol.425 , pp. 475-478
    • Randez-Gil, F.1    Herrero, P.2    Sanz, P.3    Prieto, J.A.4    Moreno, F.5
  • 300
    • 0031897460 scopus 로고    scopus 로고
    • Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast
    • Randez-Gil F, Sanz P, Entian K-D, Prieto JA. 1998. Carbon source-dependent phosphorylation of hexokinase PII and its role in the glucose-signaling response in yeast. Molecular and Cellular Biology 18: 2940-2948.
    • (1998) Molecular and Cellular Biology , vol.18 , pp. 2940-2948
    • Randez-Gil, F.1    Sanz, P.2    Entian, K.-D.3    Prieto, J.A.4
  • 301
    • 0038709277 scopus 로고    scopus 로고
    • Catabolite degradation of fructose-1, 6-bisphosphatase in the yeast Saccharomyces cerevisiae: A genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways
    • Regelmann J, Schülle T, Josupeit FS, Horak J, Rose M, Entian K-D, Thumm M, Wolf DH. 2003. Catabolite degradation of fructose-1, 6-bisphosphatase in the yeast Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID genes and indicates the existence of two degradation pathways. Molecular Biology of the Cell 14: 1652-1663.
    • (2003) Molecular Biology of the Cell , vol.14 , pp. 1652-1663
    • Regelmann, J.1    Schülle, T.2    Josupeit, F.S.3    Horak, J.4    Rose, M.5    Entian, K.-D.6    Thumm, M.7    Wolf, D.H.8
  • 303
    • 0023664652 scopus 로고
    • Phosphorylation in vivo of yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase at the cyclic AMP-dependent site
    • Rittenhouse J, Moberly L, Marcus F. 1987. Phosphorylation in vivo of yeast (Saccharomyces cerevisiae) fructose-1,6-bisphosphatase at the cyclic AMP-dependent site. Journal of Biological Chemistry 262: 10114-10119.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10114-10119
    • Rittenhouse, J.1    Moberly, L.2    Marcus, F.3
  • 304
    • 0343280119 scopus 로고
    • The components of maltozymase in yeast, and their behavior during deadapation
    • Robertson JJ, Halvorson HO. 1957. The components of maltozymase in yeast, and their behavior during deadapation. Journal of Bacteriology 73: 186-198.
    • (1957) Journal of Bacteriology , vol.73 , pp. 186-198
    • Robertson, J.J.1    Halvorson, H.O.2
  • 306
    • 0028835605 scopus 로고
    • Glucose repression in fungi
    • Ronne H. 1995. Glucose repression in fungi. Trends in Genetics 11: 12-17.
    • (1995) Trends in Genetics , vol.11 , pp. 12-17
    • Ronne, H.1
  • 307
    • 0025772770 scopus 로고
    • Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinases PI and PII
    • Rose M, Albig W, Entian K-D. 1991. Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinases PI and PII. European Journal of Biochemistry 199: 511-518.
    • (1991) European Journal of Biochemistry , vol.199 , pp. 511-518
    • Rose, M.1    Albig, W.2    Entian, K.-D.3
  • 308
    • 0024204106 scopus 로고
    • Irreversible inactivation of Saccharomyces cerevisiae fructose-1,6-bisphosphatase independent of protein phosphorylation at Ser [11]
    • Rose M, Entian K-D, Hofmann L, Vogel RF, Mecke D. 1988. Irreversible inactivation of Saccharomyces cerevisiae fructose-1,6-bisphosphatase independent of protein phosphorylation at Ser [11]. FEBS Letters 241: 55-59.
    • (1988) FEBS Letters , vol.241 , pp. 55-59
    • Rose, M.1    Entian, K.-D.2    Hofmann, L.3    Vogel, R.F.4    Mecke, D.5
  • 309
    • 0018938640 scopus 로고
    • Genes affecting the expression of cytochrome c in yeast: Genetic mapping and genetic interactions
    • Rothstein RJ, Sherman F. 1980. Genes affecting the expression of cytochrome c in yeast: genetic mapping and genetic interactions. Genetics 94: 871-889.
    • (1980) Genetics , vol.94 , pp. 871-889
    • Rothstein, R.J.1    Sherman, F.2
  • 310
    • 0018563489 scopus 로고
    • The Pasteur effect and catabolite repression in an oxidative yeast, Kluyveromyces lactis
    • Royt PW, MacQuillan AM. 1979. The Pasteur effect and catabolite repression in an oxidative yeast, Kluyveromyces lactis. Antonie van Leeuwenhoek 45: 241-252.
    • (1979) Antonie Van Leeuwenhoek , vol.45 , pp. 241-252
    • Royt, P.W.1    MacQuillan, A.M.2
  • 312
    • 0016605838 scopus 로고
    • Isolation of a catabolite repression mutant of yeast as a revertant strain that is maltose negative in the respiratory-deficient state
    • Schamhart DHJ, Ten Berge AMA, van de Poll KW. 1975. Isolation of a catabolite repression mutant of yeast as a revertant strain that is maltose negative in the respiratory-deficient state. Journal of Bacteriology 121: 747-752.
    • (1975) Journal of Bacteriology , vol.121 , pp. 747-752
    • Schamhart, D.H.J.1    Ten Berge, A.M.A.2    van de Poll, K.W.3
  • 313
    • 25544480391 scopus 로고
    • Subcellular particles carrying mitochondrial enzymes in anaerobically grown cells of Saccharomyces cerevisiae
    • Schatz G. 1965. Subcellular particles carrying mitochondrial enzymes in anaerobically grown cells of Saccharomyces cerevisiae. Biochimica et Biophysica Acta 96: 342-345.
    • (1965) Biochimica Et Biophysica Acta , vol.96 , pp. 342-345
    • Schatz, G.1
  • 314
    • 0008899908 scopus 로고
    • On the inhibition of alcoholic fermentation in Brettanomyces yeasts under anaerobic conditions
    • Scheffers WA. 1961. On the inhibition of alcoholic fermentation in Brettanomyces yeasts under anaerobic conditions. Experientia 17: 40-42.
    • (1961) Experientia , vol.17 , pp. 40-42
    • Scheffers, W.A.1
  • 315
    • 0014031580 scopus 로고
    • Stimulation of fermentation in yeasts by acetoin and oxygen
    • Scheffers WA. 1966. Stimulation of fermentation in yeasts by acetoin and oxygen. Nature 210: 533-534.
    • (1966) Nature , vol.210 , pp. 533-534
    • Scheffers, W.A.1
  • 318
    • 0028108317 scopus 로고
    • Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome
    • Schork SM, Bee G, Thumm M, Wolf DH. 1994. Catabolite inactivation of fructose-1,6-bisphosphatase in yeast is mediated by the proteasome. FEBS Letters 349: 270-274.
    • (1994) FEBS Letters , vol.349 , pp. 270-274
    • Schork, S.M.1    Bee, G.2    Thumm, M.3    Wolf, D.H.4
  • 319
    • 0028815630 scopus 로고
    • Catabolite inactivation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae
    • Schork SM, Thumm M, Wolf DH. 1995. Catabolite inactivation of fructose-1,6-bisphosphatase of Saccharomyces cerevisiae. Journal of Biological Chemistry 270: 26446-26450.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 26446-26450
    • Schork, S.M.1    Thumm, M.2    Wolf, D.H.3
  • 320
    • 0343570543 scopus 로고    scopus 로고
    • Ubc8p functions in catabolite degradation of fructose-1,6-bisphosphatase in yeast
    • Schülle T, Rose M, Entian K-D, Thumm M, Wolf DH. 2000. Ubc8p functions in catabolite degradation of fructose-1,6-bisphosphatase in yeast. EMBO Journal 19: 2161-2167.
    • (2000) EMBO Journal , vol.19 , pp. 2161-2167
    • Schülle, T.1    Rose, M.2    Entian, K.-D.3    Thumm, M.4    Wolf, D.H.5
  • 321
    • 0023714501 scopus 로고
    • Molecular characterization of yeast regulatory gene CAT3 necessary for glucose derepression and nuclear localization of its product
    • Schüller H-J, Entian K-D. 1988. Molecular characterization of yeast regulatory gene CAT3 necessary for glucose derepression and nuclear localization of its product. Gene 67: 247-257.
    • (1988) Gene , vol.67 , pp. 247-257
    • Schüller, H.-J.1    Entian, K.-D.2
  • 322
    • 0026090455 scopus 로고
    • Extragenic suppressors of yeast glucose derepression mutants leading to constitutive synthesis of several glucose-repressible enzymes
    • Schüller H-J, Entian K-D. 1991. Extragenic suppressors of yeast glucose derepression mutants leading to constitutive synthesis of several glucose-repressible enzymes. Journal of Bacteriology 173: 2045-2052.
    • (1991) Journal of Bacteriology , vol.173 , pp. 2045-2052
    • Schüller, H.-J.1    Entian, K.-D.2
  • 323
    • 0022516930 scopus 로고
    • Utilization of lactose in non-respiring cells of the yeast Debaryomyces polymorphus
    • Schulz B, Höfer M. 1986. Utilization of lactose in non-respiring cells of the yeast Debaryomyces polymorphus. Archives of Microbiology 145: 367-371.
    • (1986) Archives of Microbiology , vol.145 , pp. 367-371
    • Schulz, B.1    Höfer, M.2
  • 324
    • 0014669944 scopus 로고
    • The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits
    • Schulze IT, Colowick SP. 1969. The modification of yeast hexokinases by proteases and its relationship to the dissociation of hexokinase into subunits. Journal of Biological Chemistry 244: 2306-2316.
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 2306-2316
    • Schulze, I.T.1    Colowick, S.P.2
  • 325
    • 0011812583 scopus 로고
    • Mutants missing a factor necessary for the expression of catabolite-sensitive operons in E. coli
    • Beckwith JR, Zipser D (eds). Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY
    • Schwartz D, Beckwith JR. 1970. Mutants missing a factor necessary for the expression of catabolite-sensitive operons in E. coli. In The Lactose Operon, Beckwith JR, Zipser D (eds). Cold Spring Harbor Laboratory Press: Cold Spring Harbor, NY; 417-422.
    • (1970) The Lactose Operon , pp. 417-422
    • Schwartz, D.1    Beckwith, J.R.2
  • 326
    • 0017895621 scopus 로고
    • The requirement of oxygen for the utilization of maltose, cellobiose and D-galactose by certain anaerobically-fermenting yeasts (Kluyver effect)
    • Sims AP, Barnett JA. 1978. The requirement of oxygen for the utilization of maltose, cellobiose and D-galactose by certain anaerobically-fermenting yeasts (Kluyver effect). Journal of General Microbiology 106: 277-288.
    • (1978) Journal of General Microbiology , vol.106 , pp. 277-288
    • Sims, A.P.1    Barnett, J.A.2
  • 327
    • 0026025773 scopus 로고
    • Levels of activity of enzymes involved in anaerobic utilization of sugars by six yeast species: Observations towards understanding the Kluyver effect
    • Sims AP, Barnett JA. 1991. Levels of activity of enzymes involved in anaerobic utilization of sugars by six yeast species: observations towards understanding the Kluyver effect. FEMS Microbiology Letters 77: 295-298.
    • (1991) FEMS Microbiology Letters , vol.77 , pp. 295-298
    • Sims, A.P.1    Barnett, J.A.2
  • 328
    • 25844497398 scopus 로고
    • Vladimir Alexandrovich Engelhardt 1894-1984
    • Slater EC. 1984. Vladimir Alexandrovich Engelhardt 1894-1984. Trends in Biochemical Sciences 9: 504-505.
    • (1984) Trends in Biochemical Sciences , vol.9 , pp. 504-505
    • Slater, E.C.1
  • 329
    • 0032768263 scopus 로고    scopus 로고
    • The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
    • Smith FC, Davies SP, Wilson WA, Carling D, Hardie DG. 1999. The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1. FEBS Letters 453: 219-223.
    • (1999) FEBS Letters , vol.453 , pp. 219-223
    • Smith, F.C.1    Davies, S.P.2    Wilson, W.A.3    Carling, D.4    Hardie, D.G.5
  • 330
    • 0034234638 scopus 로고    scopus 로고
    • Turning genes off by Ssn6-Tup1: A conserved system of transcriptional repression in eukaryotes
    • Smith RL, Johnson AD. 2000. Turning genes off by Ssn6-Tup1: a conserved system of transcriptional repression in eukaryotes. Trends in Biochemical Sciences 25: 325-330.
    • (2000) Trends in Biochemical Sciences , vol.25 , pp. 325-330
    • Smith, R.L.1    Johnson, A.D.2
  • 331
    • 0039295216 scopus 로고
    • The Pasteur effect in the allosteric era
    • Kornberg A (ed.). Pergamon: Oxford
    • Sols A. 1976. The Pasteur effect in the allosteric era. In Reflections on Biochemistry, Kornberg A (ed.). Pergamon: Oxford; 199-206.
    • (1976) Reflections on Biochemistry , pp. 199-206
    • Sols, A.1
  • 332
    • 0006900439 scopus 로고
    • Energy-yielding metabolism in yeasts
    • Rose AH, Harrison JS (eds). Academic Press: London
    • Sols A, Gancedo C, DelaFuente G. 1971. Energy-yielding metabolism in yeasts. In The Yeasts, vol. 2, Rose AH, Harrison JS (eds). Academic Press: London; 271-307.
    • (1971) The Yeasts , vol.2 , pp. 271-307
    • Sols, A.1    Gancedo, C.2    DelaFuente, G.3
  • 333
    • 25844480532 scopus 로고
    • The formation and stabilization of an adaptive enzyme in the absence of its substrate
    • Spiegelman S, Reiner JM. 1947. The formation and stabilization of an adaptive enzyme in the absence of its substrate. Journal of General Physiology 31: 175-193.
    • (1947) Journal of General Physiology , vol.31 , pp. 175-193
    • Spiegelman, S.1    Reiner, J.M.2
  • 334
    • 0018968487 scopus 로고
    • Pleiotropic properties of a yeast mutant insensitive to catabolite repression
    • Stark HC, Fugit D, Mowshowitz DB. 1980. Pleiotropic properties of a yeast mutant insensitive to catabolite repression. Genetics 94: 921-928.
    • (1980) Genetics , vol.94 , pp. 921-928
    • Stark, H.C.1    Fugit, D.2    Mowshowitz, D.B.3
  • 335
    • 25844436991 scopus 로고
    • The photochemical spectrum of the Pasteur enzyme in retina
    • Stern KG, Melnick JL. 1941. The photochemical spectrum of the Pasteur enzyme in retina. Journal of Biological Chemistry 139: 301-323.
    • (1941) Journal of Biological Chemistry , vol.139 , pp. 301-323
    • Stern, K.G.1    Melnick, J.L.2
  • 336
    • 0017407790 scopus 로고
    • Variation in number and volume of the mitochondria in yeast according to growth conditions. A study based on serial sectioning and computer graphics reconstruction
    • Stevens BJ. 1977. Variation in number and volume of the mitochondria in yeast according to growth conditions. A study based on serial sectioning and computer graphics reconstruction. Biologie Cellulaire 28: 37-56.
    • (1977) Biologie Cellulaire , vol.28 , pp. 37-56
    • Stevens, B.J.1
  • 338
    • 0010456369 scopus 로고
    • A re-evaluation of the Pasteur effect: New mechanisms in anaerobic metabolism
    • Storey KB. 1985. A re-evaluation of the Pasteur effect: new mechanisms in anaerobic metabolism. Molecular Physiology 8: 439-461.
    • (1985) Molecular Physiology , vol.8 , pp. 439-461
    • Storey, K.B.1
  • 339
    • 0037851486 scopus 로고
    • Adaptive variation in the level of oxidative activity in Saccharomyces cerevisiae
    • Strittmatter CF. 1957. Adaptive variation in the level of oxidative activity in Saccharomyces cerevisiae. Journal of General Microbiology 16: 169-183.
    • (1957) Journal of General Microbiology , vol.16 , pp. 169-183
    • Strittmatter, C.F.1
  • 343
    • 0342519156 scopus 로고
    • Localization of sucrose and maltose fermenting systems in Saccharomyces cerevisiae
    • Sutton DD, Lampen JO. 1962. Localization of sucrose and maltose fermenting systems in Saccharomyces cerevisiae. Biochimica et Biophysica Acta 56: 303-312.
    • (1962) Biochimica Et Biophysica Acta , vol.56 , pp. 303-312
    • Sutton, D.D.1    Lampen, J.O.2
  • 344
    • 0006339631 scopus 로고
    • Growth and assimilation in cultures of Saccharomyces cerevisiae
    • Swanson WH, Clifton CE. 1948. Growth and assimilation in cultures of Saccharomyces cerevisiae. Journal of Bacteriology 56: 115-124.
    • (1948) Journal of Bacteriology , vol.56 , pp. 115-124
    • Swanson, W.H.1    Clifton, C.E.2
  • 346
    • 0024459376 scopus 로고
    • Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival
    • Teichert U, Mechler B, Müller H, Wolf DH. 1989. Lysosomal (vacuolar) proteinases of yeast are essential catalysts for protein degradation, differentiation, and cell survival. Journal of Biological Chemistry 264: 16037-16045.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 16037-16045
    • Teichert, U.1    Mechler, B.2    Müller, H.3    Wolf, D.H.4
  • 347
    • 0024619078 scopus 로고
    • A yeast mutation that stabilizes a plasmid bearing a mutated ARS1 element
    • Thrash-Bingham C, Fangman WL. 1989. A yeast mutation that stabilizes a plasmid bearing a mutated ARS1 element. Molecular and Cellular Biology 9: 809-816.
    • (1989) Molecular and Cellular Biology , vol.9 , pp. 809-816
    • Thrash-Bingham, C.1    Fangman, W.L.2
  • 349
    • 0020381126 scopus 로고
    • Effect of caffeine on glucose-induced inactivation of gluconeogenic enzymes in Saccharomyces cerevisiae: Possible role of cyclic AMP
    • Tortora P, Burlini N, Hanozet GM, Guerritore A. 1982. Effect of caffeine on glucose-induced inactivation of gluconeogenic enzymes in Saccharomyces cerevisiae: possible role of cyclic AMP. European Journal of Biochemistry 126: 617-622.
    • (1982) European Journal of Biochemistry , vol.126 , pp. 617-622
    • Tortora, P.1    Burlini, N.2    Hanozet, G.M.3    Guerritore, A.4
  • 350
    • 0031740335 scopus 로고    scopus 로고
    • Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae
    • Treitel MA, Kuchin S, Carlson M. 1998. Snf1 protein kinase regulates phosphorylation of the Mig1 repressor in Saccharomyces cerevisiae. Molecular and Cellular Biology 18: 6273-6280.
    • (1998) Molecular and Cellular Biology , vol.18 , pp. 6273-6280
    • Treitel, M.A.1    Kuchin, S.2    Carlson, M.3
  • 351
    • 0022626969 scopus 로고
    • Isolation of Saccharomyces cerevisiae mutants constitutive for invertase synthesis
    • Trumbly RJ. 1986. Isolation of Saccharomyces cerevisiae mutants constitutive for invertase synthesis. Journal of Bacteriology 166: 1123-1127.
    • (1986) Journal of Bacteriology , vol.166 , pp. 1123-1127
    • Trumbly, R.J.1
  • 352
    • 0021073071 scopus 로고
    • Isolation and characerization of aminopeptidase mutants of Saccharomyces cerevisiae
    • Trumbly RJ, Bradley G. 1983. Isolation and characerization of aminopeptidase mutants of Saccharomyces cerevisiae. Journal of Bacteriology 156: 36-48.
    • (1983) Journal of Bacteriology , vol.156 , pp. 36-48
    • Trumbly, R.J.1    Bradley, G.2
  • 353
    • 0028102286 scopus 로고
    • The GLC7 type 1 protein phosphatase is required for glucose repression in Saccharomyces cerevisiae
    • Tu J, Carlson M. 1994. The GLC7 type 1 protein phosphatase is required for glucose repression in Saccharomyces cerevisiae. Molecular and Cellular Biology 14: 6789-6796.
    • (1994) Molecular and Cellular Biology , vol.14 , pp. 6789-6796
    • Tu, J.1    Carlson, M.2
  • 354
    • 0028894928 scopus 로고
    • REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae
    • Tu J, Carlson M. 1995. REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae. EMBO Journal 14: 5939-5946.
    • (1995) EMBO Journal , vol.14 , pp. 5939-5946
    • Tu, J.1    Carlson, M.2
  • 355
    • 0021947584 scopus 로고
    • Catabolite repression 1985
    • Ullmann A. 1985. Catabolite repression 1985. Biochemie 67: 29-34.
    • (1985) Biochemie , vol.67 , pp. 29-34
    • Ullmann, A.1
  • 357
    • 0028222062 scopus 로고
    • Synergistic release from glucose repression by mig1 and ssn mutations in Saccharomyces cerevisiae
    • Vallier LG, Carlson M. 1994. Synergistic release from glucose repression by mig1 and ssn mutations in Saccharomyces cerevisiae. Genetics 137: 49-54.
    • (1994) Genetics , vol.137 , pp. 49-54
    • Vallier, L.G.1    Carlson, M.2
  • 358
    • 0015952382 scopus 로고
    • Cyclic 3′, 5′-adenosine monophosphate stimulates trehalose degradation in baker's yeast
    • van der Plaat JB. 1974. Cyclic 3′, 5′-adenosine monophosphate stimulates trehalose degradation in baker's yeast. Biochemical and Biophysical Research Communications 56: 580-587.
    • (1974) Biochemical and Biophysical Research Communications , vol.56 , pp. 580-587
    • van der Plaat, J.B.1
  • 359
    • 0019130510 scopus 로고
    • Fructose 2,6-bisphosphate, the probable structure of the glucose- and glucagon-sensitive stimulator of phosphofructokinase
    • van Schaftingen E, Hue L, Hers H-G. 1980. Fructose 2,6-bisphosphate, the probable structure of the glucose- and glucagon-sensitive stimulator of phosphofructokinase. Biochemical Journal 192: 897-901.
    • (1980) Biochemical Journal , vol.192 , pp. 897-901
    • van Schaftingen, E.1    Hue, L.2    Hers, H.-G.3
  • 360
    • 0024340089 scopus 로고
    • Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621
    • van Urk H, Schipper D, Breedveld GV, Mak PR, Scheffers WA, van Dijken JP. 1989. Localization and kinetics of pyruvate-metabolizing enzymes in relation to aerobic alcoholic fermentation in Saccharomyces cerevisiae CBS 8066 and Candida utilis CBS 621. Biochimica et Biophysica Acta 992: 78-86.
    • (1989) Biochimica Et Biophysica Acta , vol.992 , pp. 78-86
    • van Urk, H.1    Schipper, D.2    Breedveld, G.V.3    Mak, P.R.4    Scheffers, W.A.5    van Dijken, J.P.6
  • 361
    • 0014687720 scopus 로고
    • Induction and catabolite repression of α-glucosidase synthesis in protoplasts of Saccharomyces carlsbergensis
    • van Wijk R, Ouwehand J, van den Bos T, Koningsberger VV. 1969. Induction and catabolite repression of α-glucosidase synthesis in protoplasts of Saccharomyces carlsbergensis. Biochimica et Biophysica Acta 186: 178-191.
    • (1969) Biochimica Et Biophysica Acta , vol.186 , pp. 178-191
    • van Wijk, R.1    Ouwehand, J.2    van den Bos, T.3    Koningsberger, V.V.4
  • 364
    • 0032403110 scopus 로고    scopus 로고
    • Sip4, a Snf1 kinase-dependent transcriptional activator, binds to the carbon source-responsive element of gluconeogenic genes
    • Vincent O, Carlson M. 1998. Sip4, a Snf1 kinase-dependent transcriptional activator, binds to the carbon source-responsive element of gluconeogenic genes. EMBO Journal 17: 7002-7008.
    • (1998) EMBO Journal , vol.17 , pp. 7002-7008
    • Vincent, O.1    Carlson, M.2
  • 365
    • 0035338114 scopus 로고    scopus 로고
    • Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism
    • Vincent O, Townley R, Kuchin S, Carlson M. 2001. Subcellular localization of the Snf1 kinase is regulated by specific beta subunits and a novel glucose signaling mechanism. Genes and Development 15: 1104-1114.
    • (2001) Genes and Development , vol.15 , pp. 1104-1114
    • Vincent, O.1    Townley, R.2    Kuchin, S.3    Carlson, M.4
  • 366
    • 0035554216 scopus 로고    scopus 로고
    • Professor Joseph Louis Melnick Dr. Med. honoris causa Univerzity Karlovy (1914-2001)
    • Vonka V. 2001. Professor Joseph Louis Melnick Dr. Med. honoris causa Univerzity Karlovy (1914-2001). Sborník Lékaoský 102: 547-554.
    • (2001) Sborník Lékaoský , vol.102 , pp. 547-554
    • Vonka, V.1
  • 367
    • 18844396507 scopus 로고
    • Oxidation and fermentation
    • Needham J, Green DE (eds). Cambridge University Press: Cambridge
    • von Szent-Györgyi A. 1937. Oxidation and fermentation. In Perspectives in Biochemistry, Needham J, Green DE (eds). Cambridge University Press: Cambridge; 165-174.
    • (1937) Perspectives in Biochemistry , pp. 165-174
    • von Szent-Györgyi, A.1
  • 368
    • 0001483173 scopus 로고
    • Versuche an überlebendem Carcinomgewebe
    • Warburg O. 1923. Versuche an überlebendem Carcinomgewebe. Biochemische Zeitschrift 142: 317-333.
    • (1923) Biochemische Zeitschrift , vol.142 , pp. 317-333
    • Warburg, O.1
  • 369
    • 0343550889 scopus 로고
    • Über die Wirkung von Blausäureäthylester (Äthylcarbylamin) auf die Pasteursche Reaktion
    • Warburg O. 1926. Über die Wirkung von Blausäureäthylester (Äthylcarbylamin) auf die Pasteursche Reaktion. Biochemische Zeitschrift 172: 432-441.
    • (1926) Biochemische Zeitschrift , vol.172 , pp. 432-441
    • Warburg, O.1
  • 371
    • 0001022291 scopus 로고
    • Über die Wirkung des Kohlenoxyds auf den Stoffwechsel der Hefen
    • Warburg O. 1926. Über die Wirkung des Kohlenoxyds auf den Stoffwechsel der Hefen. Biochemische Zeitschrift 177: 471-486.
    • (1926) Biochemische Zeitschrift , vol.177 , pp. 471-486
    • Warburg, O.1
  • 374
    • 0000906680 scopus 로고
    • Versuche an überlebendem Carcinomgewebe
    • Warburg O, Minami S. 1923. Versuche an überlebendem Carcinomgewebe. Klinische Wochenschrift 2: 776-777.
    • (1923) Klinische Wochenschrift , vol.2 , pp. 776-777
    • Warburg, O.1    Minami, S.2
  • 375
    • 0001638685 scopus 로고
    • Über die photochemische Dissoziation bei intermittierender Belichtung und das absolute Absorptionsspektrum des Atmungsferments
    • Warburg O, Negelein E. 1928. Über die photochemische Dissoziation bei intermittierender Belichtung und das absolute Absorptionsspektrum des Atmungsferments. Biochemische Zeitschrift 202: 202-228.
    • (1928) Biochemische Zeitschrift , vol.202 , pp. 202-228
    • Warburg, O.1    Negelein, E.2
  • 376
    • 25844526452 scopus 로고
    • Absolutes Absorptionsspektrum des Atmungsferments
    • Warburg O, Negelein E. 1929. Absolutes Absorptionsspektrum des Atmungsferments. Biochemische Zeitschrift 204: 495-499.
    • (1929) Biochemische Zeitschrift , vol.204 , pp. 495-499
    • Warburg, O.1    Negelein, E.2
  • 377
    • 0006518524 scopus 로고
    • Über das Absorptionsspektrum des Atmungsferments
    • Warburg O, Negelein E. 1929. Über das Absorptionsspektrum des Atmungsferments. Biochemische Zeitschrift 214: 64-100.
    • (1929) Biochemische Zeitschrift , vol.214 , pp. 64-100
    • Warburg, O.1    Negelein, E.2
  • 381
    • 0028314909 scopus 로고
    • Effects of oxygen limitation on sugar metabolism in yeasts: A continuous-culture study of the Kluyver effect
    • Weusthuis RA, Visser W, Pronk JT, Scheffers WA, van Dijken JP. 1994. Effects of oxygen limitation on sugar metabolism in yeasts: a continuous-culture study of the Kluyver effect. Microbiology 140: 703-715.
    • (1994) Microbiology , vol.140 , pp. 703-715
    • Weusthuis, R.A.1    Visser, W.2    Pronk, J.T.3    Scheffers, W.A.4    van Dijken, J.P.5
  • 383
    • 0015992687 scopus 로고
    • Mutants of Saccharomyces cerevisiae that incorporate deoxythymidine-5′-monophosphate into deoxyribonucleic acid in vivo
    • Wickner RB. 1974. Mutants of Saccharomyces cerevisiae that incorporate deoxythymidine-5′-monophosphate into deoxyribonucleic acid in vivo. Journal of Bacteriology 117: 252-260.
    • (1974) Journal of Bacteriology , vol.117 , pp. 252-260
    • Wickner, R.B.1
  • 384
    • 51249193822 scopus 로고
    • On the existence of a negative Pasteur effect in yeasts classified in the genus Brettanomyces Kufferath et van Laer
    • [O]
    • Wikén T[O], Scheffers WA, Verhaar AJM. 1961. On the existence of a negative Pasteur effect in yeasts classified in the genus Brettanomyces Kufferath et van Laer. Antonie van Leeuwenhoek 27: 401-433.
    • (1961) Antonie Van Leeuwenhoek , vol.27 , pp. 401-433
    • Wikén, T.1    Scheffers, W.A.2    Verhaar, A.J.M.3
  • 385
    • 0025804492 scopus 로고
    • The CYC8 and TUP1 proteins involved in glucose repression in Saccharomyces cerevisiae are associated in a protein complex
    • Williams FE, Varanasi U, Trumbly RJ. 1991. The CYC8 and TUP1 proteins involved in glucose repression in Saccharomyces cerevisiae are associated in a protein complex. Molecular and Cellular Biology 11: 3307-3316.
    • (1991) Molecular and Cellular Biology , vol.11 , pp. 3307-3316
    • Williams, F.E.1    Varanasi, U.2    Trumbly, R.J.3
  • 386
    • 0019486418 scopus 로고
    • Transposable elements associated with constitutive expression of yeast alcohol dehydrogenase II
    • Williamson VM, Young ET, Ciriacy M. 1981. Transposable elements associated with constitutive expression of yeast alcohol dehydrogenase II. Cell 23: 605-614.
    • (1981) Cell , vol.23 , pp. 605-614
    • Williamson, V.M.1    Young, E.T.2    Ciriacy, M.3
  • 389
    • 4043054144 scopus 로고
    • Complementary action of melibiase and galactozymase on raffinose fermentation
    • Winge Ö, Roberts C. 1956. Complementary action of melibiase and galactozymase on raffinose fermentation. Nature 177: 383-384.
    • (1956) Nature , vol.177 , pp. 383-384
    • Winge, Ö.1    Roberts, C.2
  • 391
    • 0014016745 scopus 로고
    • Repression von Alkoholdehydrogenase Malatdehydrogenase, Isocitratlyase und Malatsynthase in Hefe durch Glucose
    • Witt I, Kronau R, Holzer H. 1966. Repression von Alkoholdehydrogenase Malatdehydrogenase, Isocitratlyase und Malatsynthase in Hefe durch Glucose. Biochimica et Biophysica Acta 118: 522-537.
    • (1966) Biochimica Et Biophysica Acta , vol.118 , pp. 522-537
    • Witt, I.1    Kronau, R.2    Holzer, H.3
  • 392
    • 0014020598 scopus 로고
    • Isoenzyme der Malatdehydrogenase und ihre Regulation in Saccharomyces cerevisiae
    • Witt I, Kronau R, Holzer H. 1966. Isoenzyme der Malatdehydrogenase und ihre Regulation in Saccharomyces cerevisiae. Biochimica et Biophysica Acta 128: 63-73.
    • (1966) Biochimica Et Biophysica Acta , vol.128 , pp. 63-73
    • Witt, I.1    Kronau, R.2    Holzer, H.3
  • 393
    • 25844486440 scopus 로고    scopus 로고
    • Saccharopepsin
    • Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: London
    • Woessner JF. 1998. Saccharopepsin. In Handbook of Proteolytic Enzymes, Barrett AJ, Rawlings ND, Woessner JF (eds). Academic Press: London; 848-851.
    • (1998) Handbook of Proteolytic Enzymes , pp. 848-851
    • Woessner, J.F.1
  • 396
    • 0026758003 scopus 로고
    • A protein kinase substrate identified by the two-hybrid system
    • Yang X, Hubbard EJA, Carlson M. 1992. A protein kinase substrate identified by the two-hybrid system. Science 257: 680-682.
    • (1992) Science , vol.257 , pp. 680-682
    • Yang, X.1    Hubbard, E.J.A.2    Carlson, M.3
  • 397
    • 0028559507 scopus 로고
    • A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex
    • Yang X, Jiang R, Carlson M. 1994. A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex. EMBO Journal 13: 5878-5886.
    • (1994) EMBO Journal , vol.13 , pp. 5878-5886
    • Yang, X.1    Jiang, R.2    Carlson, M.3
  • 399
    • 0026022414 scopus 로고
    • A yeast protein with homology to the β-subunit of G proteins is involved in control of heme-regulated and catabolite-repressed genes
    • Zhang M, Rosenblum-Vos LS, Lowry CV, Boakye KA, Zitomer RS. 1991. A yeast protein with homology to the β-subunit of G proteins is involved in control of heme-regulated and catabolite-repressed genes. Gene 97: 153-161.
    • (1991) Gene , vol.97 , pp. 153-161
    • Zhang, M.1    Rosenblum-Vos, L.S.2    Lowry, C.V.3    Boakye, K.A.4    Zitomer, R.S.5
  • 400
    • 0017581540 scopus 로고
    • Genetics of carbon catabolite repression in Saccharomyces cerevisiae: Genes involved in the derepression process
    • Zimmermann FK, Kaufmann I, Rasenberger H, Haußmann P. 1977. Genetics of carbon catabolite repression in Saccharomyces cerevisiae: genes involved in the derepression process. Molecular and General Genetics 151: 95-103.
    • (1977) Molecular and General Genetics , vol.151 , pp. 95-103
    • Zimmermann, F.K.1    Kaufmann, I.2    Rasenberger, H.3    Haußmann, P.4
  • 401
    • 0017408123 scopus 로고
    • Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression
    • Zimmermann FK, Scheel I. 1977. Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. Molecular and General Genetics 154: 75-82.
    • (1977) Molecular and General Genetics , vol.154 , pp. 75-82
    • Zimmermann, F.K.1    Scheel, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.