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Volumn 136, Issue 2, 1997, Pages 251-269

Biogenesis of the Saccharomyces cerevisiae mating pheromone a-factor

Author keywords

[No Author keywords available]

Indexed keywords

PHEROMONE;

EID: 0031055072     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.136.2.251     Document Type: Article
Times cited : (108)

References (71)
  • 1
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection
    • Adames, N., K. Blundell, M.N. Ashby, and C. Boone, 1995. Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science (Wash. DC). 270:464-467.
    • (1995) Science (Wash. DC) , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 2
    • 0024712405 scopus 로고
    • Multiple genes coding for precursors of rhodotorucine A, a farnesyl peptide mating pheromonc of the basidiomycetous yeast Rhodosporidium toruloides
    • Akada, R., K. Minomi, J. Kai, I. Yamashita, T. Miyakawa, and S. Fukui, 1989. Multiple genes coding for precursors of rhodotorucine A, a farnesyl peptide mating pheromonc of the basidiomycetous yeast Rhodosporidium toruloides. Mol. Cell. Biol. 9:3491-3498.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3491-3498
    • Akada, R.1    Minomi, K.2    Kai, J.3    Yamashita, I.4    Miyakawa, T.5    Fukui, S.6
  • 3
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • Alani, E., L. Cao, and N. Kleckner. 1987. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics. 116:541-545.
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 4
    • 0024279583 scopus 로고
    • Structure of Saccharomyces cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component
    • Anderegg, R.J., R. Setz, S.A. Carr, J.W. Crabb, and W. Duntze. 1988. Structure of Saccharomyces cerevisiae mating hormone a-factor. Identification of S-farnesyl cysteine as a structural component. J. Biol. Chem. 263:18236-18240.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18236-18240
    • Anderegg, R.J.1    Setz, R.2    Carr, S.A.3    Crabb, J.W.4    Duntze, W.5
  • 5
    • 0026521412 scopus 로고
    • Endoproleolytic processing of a farnesylated peptide in vitro
    • Ashby, M.N., D.S. King, and J. Rine. 1992. Endoproleolytic processing of a farnesylated peptide in vitro. Proc. Natl. Acad. Sci. USA. 89:4613-4617.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4613-4617
    • Ashby, M.N.1    King, D.S.2    Rine, J.3
  • 6
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin A precursor
    • Beck, L.A., T.J. Hosick, and M. Sinensky. 1990. Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol. 110:1489-1499.
    • (1990) J. Cell Biol. , vol.110 , pp. 1489-1499
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 7
    • 0029022718 scopus 로고
    • Insulysin and pitrilysin: Insulin-degrading enzymes of mammals and bacteria
    • Becker, A.B., and R.A. Roth. 1995. Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria. Methods Enzymol. 248:693-703.
    • (1995) Methods Enzymol. , vol.248 , pp. 693-703
    • Becker, A.B.1    Roth, R.A.2
  • 8
    • 0028117116 scopus 로고
    • Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae
    • Berkower, C., D. Loayza, and S. Michaelis. 1994. Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae. Mol. Biol. Cell. 5:1185-1198.
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 1185-1198
    • Berkower, C.1    Loayza, D.2    Michaelis, S.3
  • 9
    • 0026094617 scopus 로고
    • Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily
    • Berkower, C., and S. Michaelis. 1991. Mutational analysis of the yeast a-factor transporter STE6, a member of the ATP binding cassette (ABC) protein superfamily. EMBO (Eur. Mol. Biol. Organ.) J. 10:3777-3785.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 3777-3785
    • Berkower, C.1    Michaelis, S.2
  • 10
    • 0026500677 scopus 로고
    • The a mating type locus of U. maydis specifies cell signaling components
    • Bolker, M., M. Urban, and R. Kahmann. 1992. The a mating type locus of U. maydis specifies cell signaling components. Cell. 68:441-450.
    • (1992) Cell , vol.68 , pp. 441-450
    • Bolker, M.1    Urban, M.2    Kahmann, R.3
  • 11
    • 0003383950 scopus 로고
    • Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor
    • M. Gething, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Brake, A.J., C. Brenner, R. Najarian, P. Laybourn, and J. Merryweather. 1985. Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor. In Protein Transport and Secretion. M. Gething, editor. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York. 103-108.
    • (1985) Protein Transport and Secretion , pp. 103-108
    • Brake, A.J.1    Brenner, C.2    Najarian, R.3    Laybourn, P.4    Merryweather, J.5
  • 12
    • 0018566826 scopus 로고
    • Genetics and physiology of proline utilization in Saccharomyces cerevisiae: Enzyme induction by proline
    • Brandriss, M.C., and B. Magasanik. 1979. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: enzyme induction by proline. J. Bacteriol. 140:498-503.
    • (1979) J. Bacteriol. , vol.140 , pp. 498-503
    • Brandriss, M.C.1    Magasanik, B.2
  • 13
    • 0030479302 scopus 로고    scopus 로고
    • Cell fusion during yeast mating requires high levels of a-factor and α-factor mating pheromones
    • Brizzio, V., A.E. Gammie, G. Nijbroek, S. Michaelis, and M.D. Rose. 1996. Cell fusion during yeast mating requires high levels of a-factor and α-factor mating pheromones. J. Cell Biol. 135:1727-1739.
    • (1996) J. Cell Biol. , vol.135 , pp. 1727-1739
    • Brizzio, V.1    Gammie, A.E.2    Nijbroek, G.3    Michaelis, S.4    Rose, M.D.5
  • 14
    • 0029163024 scopus 로고
    • Fungal lipopeptidc mating pheromones: A model system for the study of protein prenylation
    • Caldwell, G.A., F. Naider, and J.M. Becker. 1995. Fungal lipopeptidc mating pheromones: a model system for the study of protein prenylation. Microbiol. Rev. 59:406-422.
    • (1995) Microbiol. Rev. , vol.59 , pp. 406-422
    • Caldwell, G.A.1    Naider, F.2    Becker, J.M.3
  • 15
    • 0020971317 scopus 로고
    • Beta-galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast
    • Casadaban, M.J., A.A. Martinez, S.K. Shapira, and J. Chou. 1983. Beta-galactosidase gene fusions for analyzing gene expression in Escherichia coli and yeast. Methods Enzymol. 100:293-308.
    • (1983) Methods Enzymol. , vol.100 , pp. 293-308
    • Casadaban, M.J.1    Martinez, A.A.2    Shapira, S.K.3    Chou, J.4
  • 16
    • 1842415257 scopus 로고
    • PhD thesis. Johns Hopkins University School of Medicine, Baltimore, MD
    • Chen, P. 1993. Biogenesis of yeast mating pheromone a-factor. PhD thesis. Johns Hopkins University School of Medicine, Baltimore, MD, 251 pp.
    • (1993) Biogenesis of Yeast Mating Pheromone A-factor , pp. 251
    • Chen, P.1
  • 18
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke, S. 1992. Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Anna. Rev. Biochem. 61:355-386.
    • (1992) Anna. Rev. Biochem. , vol.61 , pp. 355-386
    • Clarke, S.1
  • 20
    • 0026587548 scopus 로고
    • Mating pheromones of the fission yeast Schizosaccharomyces pombe: Purification and structural characterization of M-factor and isolation and analysis of two genes encoding the pheromone
    • Davey, J. 1992. Mating pheromones of the fission yeast Schizosaccharomyces pombe: purification and structural characterization of M-factor and isolation and analysis of two genes encoding the pheromone. EMBO (Eur. Mol. Biol. Organ.) J. 11:951-960.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 951-960
    • Davey, J.1
  • 21
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble, R. 1992. A simple and efficient procedure for transformation of yeasts. BioTechniqites. 13:18-20.
    • (1992) BioTechniqites , vol.13 , pp. 18-20
    • Elble, R.1
  • 22
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., A.L. Hubbard, S. Fowler, and P.B. Lazarow. 1982. Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93:97-102.
    • (1982) J. Cell Biol. , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 24
    • 0028151340 scopus 로고
    • A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes
    • Fujita, A., C. Oka, Y. Arikawa, T. Katagai, A. Tonouchi, S. Kuhara, and Y. Misumi. 1994. A yeast gene necessary for bud-site selection encodes a protein similar to insulin-degrading enzymes. Nature (Lond.). 372:567-570.
    • (1994) Nature (Lond.) , vol.372 , pp. 567-570
    • Fujita, A.1    Oka, C.2    Arikawa, Y.3    Katagai, T.4    Tonouchi, A.5    Kuhara, S.6    Misumi, Y.7
  • 25
    • 0023081809 scopus 로고
    • A novel yeast mutant defective in the processing of ras proteins: Assessment of the effect of the mutation on processing steps
    • Fujiyama, A., K. Matsumoto, and F. Tamanoi. 1987. A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. EMBO (Eur. Mol. Biol. Organ.) J. 6:223-228.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 223-228
    • Fujiyama, A.1    Matsumoto, K.2    Tamanoi, F.3
  • 26
    • 15144342541 scopus 로고
    • Post-translational processing events in the maturation of yeast pheromone precursors
    • J. Hicks, editor. Alan R. Liss, New York
    • Fuller, R., A. Brake, R. Sterne, R. Kunisawa, D. Barnes, M. Flessel, and J. Thorner. 1986. Post-translational processing events in the maturation of yeast pheromone precursors. In Yeast Cell Biology. J. Hicks, editor. Alan R. Liss, New York. 461-476.
    • (1986) Yeast Cell Biology , pp. 461-476
    • Fuller, R.1    Brake, A.2    Sterne, R.3    Kunisawa, R.4    Barnes, D.5    Flessel, M.6    Thorner, J.7
  • 27
    • 0027218689 scopus 로고
    • Biochemistry of multidrug resistance mediated by the multidrug transporter
    • Gottesman, M.M., and I. Pastan. 1993. Biochemistry of multidrug resistance mediated by the multidrug transporter. Annu. Rev. Biochem. 62:385-427.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 385-427
    • Gottesman, M.M.1    Pastan, I.2
  • 28
    • 0021167363 scopus 로고
    • Targeting of E. coli beta-galactosidase to the nucleus in yeast
    • Hall, M.N., L. Hereford, and I. Herskowitz. 1984. Targeting of E. coli beta-galactosidase to the nucleus in yeast. Cell. 36:1057-1065.
    • (1984) Cell , vol.36 , pp. 1057-1065
    • Hall, M.N.1    Hereford, L.2    Herskowitz, I.3
  • 29
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 30
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock, J.F., K. Cadwallader, and C.J. Marshall. 1991. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO (Eur. Mol. Biol. Organ.) J. 10:641-646.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 31
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock, J.F., H. Paterson, and C.J. Marshall. 1990. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell. 63:133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 32
    • 0026345033 scopus 로고
    • RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins
    • He, B., P. Chen, S.Y. Chen, K.L. Vancura, S. Michaelis, and S. Powers. 1991. RAM2, an essential gene of yeast, and RAM1 encode the two polypeptide components of the farnesyltransferase that prenylates a-factor and Ras proteins. Proc. Natl. Acad. Sci. USA. 88:11373-11377.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11373-11377
    • He, B.1    Chen, P.2    Chen, S.Y.3    Vancura, K.L.4    Michaelis, S.5    Powers, S.6
  • 33
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes, H., and E.A. Nigg. 1994. The role of isoprenylation in membrane attachment of nuclear lamins. A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J Cell Sci. 107:1019-1029.
    • (1994) J Cell Sci. , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 34
  • 35
    • 0025051169 scopus 로고
    • Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae
    • Hrycyna, C.A., and S. Clarke. 1990. Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:5071-5076.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5071-5076
    • Hrycyna, C.A.1    Clarke, S.2
  • 36
    • 0025764049 scopus 로고
    • The Sacchoromyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna, CA., S.K. Sapperstein, S. Clarke, and S. Michaelis. 1991. The Sacchoromyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO (Eur. Mol. Biol. Organ.) J. 10:1699-1709.
    • (1991) EMBO (Eur. Mol. Biol. Organ.) J. , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.4
  • 37
    • 0026779707 scopus 로고
    • Maturation of isoprenylated protiens in Saccharomyces cerevisiae. Multiple activities catalyze the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro
    • Hrycyna, C.A., and S. Clarke. 1992. Maturation of isoprenylated protiens in Saccharomyces cerevisiae. Multiple activities catalyze the cleavage of the three carboxyl-terminal amino acids from farnesylated substrates in vitro. J. Biol. Chem. 267:10457-10464.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10457-10464
    • Hrycyna, C.A.1    Clarke, S.2
  • 38
    • 0009680157 scopus 로고
    • Structures of Tremerogens A-9291-I and A-9291-VIII: Peptidyl sex hormones of Tremella drasiliensis
    • Ishibashi, Y., Y. Sakagami, A. Isogai, and A. Suzuki. 1984. Structures of Tremerogens A-9291-I and A-9291-VIII: peptidyl sex hormones of Tremella drasiliensis. Biochemistry. 23:1399-1404.
    • (1984) Biochemistry , vol.23 , pp. 1399-1404
    • Ishibashi, Y.1    Sakagami, Y.2    Isogai, A.3    Suzuki, A.4
  • 39
    • 0021282354 scopus 로고
    • Glycosylation and processing of prepro-α-factor through the yeast secretory pathway
    • Julius, D., R. Schekman, and J. Thorner. 1984. Glycosylation and processing of prepro-α-factor through the yeast secretory pathway. Cell. 36:309-318.
    • (1984) Cell , vol.36 , pp. 309-318
    • Julius, D.1    Schekman, R.2    Thorner, J.3
  • 40
    • 0018584369 scopus 로고
    • Structure of Rhodotorucine A, a peptidyl factor, inducing mating tube formation in Rhodosporidium toruloides
    • Kamiya, Y., A. Sakurai, S. Tamura, N. Takahashi, E. Tsuchiya, K. Abe, and S. Fukui. 1979. Structure of Rhodotorucine A, a peptidyl factor, inducing mating tube formation in Rhodosporidium toruloides. Agricult. Biol. Chem. 43:363-369.
    • (1979) Agricult. Biol. Chem. , vol.43 , pp. 363-369
    • Kamiya, Y.1    Sakurai, A.2    Tamura, S.3    Takahashi, N.4    Tsuchiya, E.5    Abe, K.6    Fukui, S.7
  • 41
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulate in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling, R., and C.P. Hollenberg. 1994. The ABC-transporter Ste6 accumulate in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO (Eur. Mol. Biol. Organ.) J. 13:3261-3271.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 42
    • 0024833061 scopus 로고
    • Saccharomyces cerevisiae STE6 gene product: A novel pathway for protein export in eukaryotic cells
    • Kuchler, K., R.E. Sterne, and J. Thorner. 1989. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO (Eur. Mol. Biol. Organ.) J. 8:3973-3984.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 3973-3984
    • Kuchler, K.1    Sterne, R.E.2    Thorner, J.3
  • 43
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., J.D. Roberts, and R.A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzvmol. 154:367-382.
    • (1987) Methods Enzvmol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 44
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 45
    • 0025860189 scopus 로고
    • Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone
    • Marcus, S., G.A. Caldwell, D. Miller, C.B. Xue, F. Naider, and J.M. Becker. 1991. Significance of C-terminal cysteine modifications to the biological activity of the Saccharomyces cerevisiae a-factor mating pheromone. Mol. Cell. Biol. 11:3603-3612.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3603-3612
    • Marcus, S.1    Caldwell, G.A.2    Miller, D.3    Xue, C.B.4    Naider, F.5    Becker, J.M.6
  • 46
    • 0025203977 scopus 로고
    • Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone
    • Marr, R.S., L.C. Blair, and J. Thorner. 1990. Saccharomyces cerevisiae STE14 gene is required for COOH-terminal methylation of a-factor mating pheromone. J. Biol. Chem. 265:20057-20060.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20057-20060
    • Marr, R.S.1    Blair, L.C.2    Thorner, J.3
  • 47
    • 0025885772 scopus 로고
    • Signal transduction during pheromone response in yeast
    • Marsh, L., A.M. Neiman, and I. Herskowitz. 1991. Signal transduction during pheromone response in yeast. Annu. Rev. Cell Biol. 7:699-728.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 699-728
    • Marsh, L.1    Neiman, A.M.2    Herskowitz, I.3
  • 48
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • McGrath, J.P., and A. Varshavsky. 1989. The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature (Lond.). 340:400-404.
    • (1989) Nature (Lond.) , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 49
    • 0027546252 scopus 로고
    • STE6, the yeast a-factor transporter
    • Michaelis, S. 1993. STE6, the yeast a-factor transporter. Semin. Cell Biol. 4:17-27.
    • (1993) Semin. Cell Biol. , vol.4 , pp. 17-27
    • Michaelis, S.1
  • 50
    • 0023974052 scopus 로고
    • The a-factor pheromone of Saccharomyces cerevisiae is essential for mating
    • Michaelis, S., and I. Herskowitz. 1988. The a-factor pheromone of Saccharomyces cerevisiae is essential for mating. Mol. Cell. Biol. 8:1309-1318.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 1309-1318
    • Michaelis, S.1    Herskowitz, I.2
  • 51
    • 0027479079 scopus 로고
    • The α-mating type locus of Cryptococcus neoformans contains a peptide pheromone gene
    • Moore, T.D.E., and J.C. Edman. 1993. The α-mating type locus of Cryptococcus neoformans contains a peptide pheromone gene. Mol. Cell. Biol. 13:1962-1970.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1962-1970
    • Moore, T.D.E.1    Edman, J.C.2
  • 52
    • 0022504637 scopus 로고
    • Genealogy of principal strains of the yeast genetic stock center
    • Mortimer, R.K., and J.R. Johnston. 1986. Genealogy of principal strains of the yeast genetic stock center. Genetics. 113:35-43.
    • (1986) Genetics , vol.113 , pp. 35-43
    • Mortimer, R.K.1    Johnston, J.R.2
  • 53
    • 0029976308 scopus 로고    scopus 로고
    • Analysis of the localization of STE6/CFTR chimeras in Saccharomyces cerevisiae model for the cystic fibrosis defect CFTR ΔF508
    • Paddon, C., D. Loayza, L. Vangelista, R. Solari, and S. Michaelis. 1996. Analysis of the localization of STE6/CFTR chimeras in Saccharomyces cerevisiae model for the cystic fibrosis defect CFTR ΔF508. Mol. Microbiol. 19:1007-1017.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1007-1017
    • Paddon, C.1    Loayza, D.2    Vangelista, L.3    Solari, R.4    Michaelis, S.5
  • 54
    • 0022994652 scopus 로고
    • RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor
    • Powers, S., S. Michaelis, D. Broek, A.S. Santa, J. Field, I. Herskowitz, and M. Wigler. 1986. RAM, a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Cell. 47:413-122.
    • (1986) Cell , vol.47 , pp. 413-1122
    • Powers, S.1    Michaelis, S.2    Broek, D.3    Santa, A.S.4    Field, J.5    Herskowitz, I.6    Wigler, M.7
  • 55
    • 0026471714 scopus 로고
    • Transport of proteins across the endoplasmic reticulum membrane
    • Rapoport, T.A. 1992, Transport of proteins across the endoplasmic reticulum membrane. Science (Wash. DC). 258:931-936.
    • (1992) Science (Wash. DC) , vol.258 , pp. 931-936
    • Rapoport, T.A.1
  • 56
    • 0026585065 scopus 로고
    • Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene
    • Raymond, M., P. Gros, M. Whiteway, and D.Y. Thomas. 1992. Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene. Science (Wash. DC). 256:232-234.
    • (1992) Science (Wash. DC) , vol.256 , pp. 232-234
    • Raymond, M.1    Gros, P.2    Whiteway, M.3    Thomas, D.Y.4
  • 57
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • Reutz, S., and P. Gros. 1994. Phosphatidylcholine translocase: a physiological role for the mdr2 gene. Cell. 77:1071-1081.
    • (1994) Cell , vol.77 , pp. 1071-1081
    • Reutz, S.1    Gros, P.2
  • 58
    • 0003361423 scopus 로고
    • Methods in Yeast Genetics
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Rose, M.D., F. Winston, and P. Hieter. 1990. Methods in Yeast Genetics. A Laboratory Course Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 198 pp.
    • (1990) A Laboratory Course Manual , pp. 198
    • Rose, M.D.1    Winston, F.2    Hieter, P.3
  • 59
    • 0019521320 scopus 로고
    • Peptidal sex hormones inducing conjugation tube formation in compatible mating-type cells of Tremella mesenterica
    • Sakagami, Y., M. Yoshida, A. Isogai, and A. Suzuki. 1981. Peptidal sex hormones inducing conjugation tube formation in compatible mating-type cells of Tremella mesenterica. Science (Wash. DC). 212:1525-1527.
    • (1981) Science (Wash. DC) , vol.212 , pp. 1525-1527
    • Sakagami, Y.1    Yoshida, M.2    Isogai, A.3    Suzuki, A.4
  • 61
    • 0028125792 scopus 로고
    • Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export
    • Sapperstein, S., C. Berkower, and S. Michaelis. 1994. Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyltransferase, and demonstration of its essential role in a-factor export. Mol. Cell. Biol. 14:1438-1449.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1438-1449
    • Sapperstein, S.1    Berkower, C.2    Michaelis, S.3
  • 63
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 64
    • 0021713895 scopus 로고
    • Transcription and regulatory signals at the mating type locus in yeast
    • Siliciano, P., and K. Tatchell. 1984. Transcription and regulatory signals at the mating type locus in yeast. Cell. 37:969-978.
    • (1984) Cell , vol.37 , pp. 969-978
    • Siliciano, P.1    Tatchell, K.2
  • 67
    • 0001134626 scopus 로고
    • Pheromone response and signal transduction during mating process of Saccharomyces cerevisiae
    • J.R. Broach, J.R. Pringle, and E.W. Jones, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • Sprague, G.F., Jr., and J. Thorner. 1992. Pheromone response and signal transduction during mating process of Saccharomyces cerevisiae. In The Molecular Biology of the Yeast Saccharomyces. 2nd ed. J.R. Broach, J.R. Pringle, and E.W. Jones, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 810 pp.
    • (1992) The Molecular Biology of the Yeast Saccharomyces. 2nd Ed. , pp. 810
    • Sprague Jr., G.F.1    Thorner, J.2
  • 69
    • 0025870323 scopus 로고
    • Identifying the recognition unit for G protein methylation
    • Tan, E.W., D. Perez-Sala, F.J. Canada, and R.R. Rando. 1991. Identifying the recognition unit for G protein methylation. J. Biol. Chem. 266:10719-10722.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10719-10722
    • Tan, E.W.1    Perez-Sala, D.2    Canada, F.J.3    Rando, R.R.4
  • 70
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: Molecular mechanisms and functional consequences
    • Zhang, F.L., and P.J. Casey. 1996. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 71
    • 0028206263 scopus 로고
    • Interaction of prenylcysteine methyl esters with the multidrug resistance transporter
    • Zhang, L., C.W. Sachs, R.L. Fine, and P.J. Casey. 1994. Interaction of prenylcysteine methyl esters with the multidrug resistance transporter. J. Biol. Chem. 269:15973-15976.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15973-15976
    • Zhang, L.1    Sachs, C.W.2    Fine, R.L.3    Casey, P.J.4


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