메뉴 건너뛰기




Volumn 69, Issue 2, 2005, Pages 262-291

Cell wall integrity signaling in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CELL SURFACE PROTEIN; CHITIN SYNTHASE; CHITIN SYNTHASE 3; CYTIDINE TRIPHOSPHATE SYNTHASE; GLUCAN SYNTHASE; MEMBRANE PROTEIN; METHENAMINE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 2; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE 1; OLIGOSACCHARYLTRANSFERASE; PHOSPHATASE; PHOSPHATIDYLINOSITIDE; PHOSPHOLIPID; PROTEIN BNI1; PROTEIN BNR1; PROTEIN CDC42; PROTEIN HISTIDINE KINASE; PROTEIN HISTIDINE KINASE 1; PROTEIN HISTIDINE KINASE 2; PROTEIN MID2; PROTEIN MTL1; PROTEIN SEC3; PROTEIN SERINE THREONINE KINASE; PROTEIN SERINE THREONINE KINASE 1; PROTEIN SERINE THREONINE KINASE 2; PROTEIN SWI; PROTEIN WSC1; PROTEIN WSC2; PROTEIN WSC3; RHO FACTOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; STAUROSPORINE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RLM1; TRANSCRIPTION FACTOR SBF; TRANSFERASE; TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 20544432791     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.69.2.262-291.2005     Document Type: Review
Times cited : (955)

References (373)
  • 1
    • 0032740682 scopus 로고    scopus 로고
    • The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity
    • Adamo, J. E., G. Rossi, and P. Brennwald. 1999. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Mol. Biol. Cell 10:4121-4133.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4121-4133
    • Adamo, J.E.1    Rossi, G.2    Brennwald, P.3
  • 2
    • 0032802378 scopus 로고    scopus 로고
    • Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast
    • Alarcon, C. M., J. Heitman, and M. E. Cardenas. 1999. Protein kinase activity and identification of a toxic effector domain of the target of rapamycin TOR proteins in yeast. Mol. Biol. Cell 10:2531-2546.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2531-2546
    • Alarcon, C.M.1    Heitman, J.2    Cardenas, M.E.3
  • 3
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts, A. S. 2001. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276:2824-2830.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 4
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7
    • Alberts, A. S., N. Bouquin, L. H. Johnston, and R. Treisman. 1998. Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J. Biol. Chem. 273:8616-8622.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 5
    • 0028302033 scopus 로고
    • GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway
    • Albertyn, J., S. Hohmann, J. M. Thevelein, and B. A. Prior. 1994. GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway. Mol. Cell. Biol. 14:4135-4144.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4135-4144
    • Albertyn, J.1    Hohmann, S.2    Thevelein, J.M.3    Prior, B.A.4
  • 6
    • 0142242242 scopus 로고    scopus 로고
    • Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p in Saccharomyces cerevisiae
    • Alic, N., V. J. Higgins, A. Pichova, M. Breitenbach, and I. W. Dawes. 2003. Lipid hydroperoxides activate the mitogen-activated protein kinase Mpk1p in Saccharomyces cerevisiae. J. Biol. Chem. 278:41849-41855.
    • (2003) J. Biol. Chem. , vol.278 , pp. 41849-41855
    • Alic, N.1    Higgins, V.J.2    Pichova, A.3    Breitenbach, M.4    Dawes, I.W.5
  • 7
    • 0024550203 scopus 로고
    • Identification of a DNA binding factor involved in cell cycle-control of the yeast HO gene
    • Andrews, B. J., and I. Herskowitz. 1989. Identification of a DNA binding factor involved in cell cycle-control of the yeast HO gene. Cell 57:21-29.
    • (1989) Cell , vol.57 , pp. 21-29
    • Andrews, B.J.1    Herskowitz, I.2
  • 8
    • 0033837037 scopus 로고    scopus 로고
    • Dynamic, Rho1p-dependent localization of Pkc1p to sites of polarized growth
    • Andrews, P. D., and M. J. Stark. 2000. Dynamic, Rho1p-dependent localization of Pkc1p to sites of polarized growth. J. Cell Sci. 113:2685-2693.
    • (2000) J. Cell Sci. , vol.113 , pp. 2685-2693
    • Andrews, P.D.1    Stark, M.J.2
  • 9
    • 0028301447 scopus 로고
    • Protein kinase C in yeast. Characteristics of the Saccharomyces cerevisiae PKC1 gene product
    • Antonsson, B., S. Montessuit, L. Friedli, M. A. Payton, and G. Paravicini. 1994. Protein kinase C in yeast. Characteristics of the Saccharomyces cerevisiae PKC1 gene product. J. Biol. Chem. 269:16821-16828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16821-16828
    • Antonsson, B.1    Montessuit, S.2    Friedli, L.3    Payton, M.A.4    Paravicini, G.5
  • 11
    • 0036001334 scopus 로고    scopus 로고
    • Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade
    • Audhya, A., and S. D. Emr. 2002. Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade. Dev. Cell 2:593-605.
    • (2002) Dev. Cell , vol.2 , pp. 593-605
    • Audhya, A.1    Emr, S.D.2
  • 12
    • 0042967817 scopus 로고    scopus 로고
    • 2 synthesis by nuclear-cytoplasmic shuttling of the Mss4 lipid kinase
    • 2 synthesis by nuclear-cytoplasmic shuttling of the Mss4 lipid kinase. EMBO J. 22:4223-4236.
    • (2003) EMBO J. , vol.22 , pp. 4223-4236
    • Audhya, A.1    Emr, S.D.2
  • 13
    • 0033840656 scopus 로고    scopus 로고
    • Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics
    • Audhya, A., M. Foti, and S. D. Emr. 2000. Distinct roles for the yeast phosphatidylinositol 4-kinases, Stt4p and Pik1p, in secretion, cell growth, and organelle membrane dynamics. Mol. Biol. Cell 11:2673-2689.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2673-2689
    • Audhya, A.1    Foti, M.2    Emr, S.D.3
  • 15
    • 13144302852 scopus 로고    scopus 로고
    • A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling
    • Ayscough, K. R., and D. G. Drubin. 1998. A role for the yeast actin cytoskeleton in pheromone receptor clustering and signalling. Curr. Biol. 8: 927-930.
    • (1998) Curr. Biol. , vol.8 , pp. 927-930
    • Ayscough, K.R.1    Drubin, D.G.2
  • 16
    • 0032934806 scopus 로고    scopus 로고
    • Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology
    • Ayscough, K. R., J. J. Eby, T. Lila, H. Dewar, K. G. Kozminski, and D. G. Drubin. 1999. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Mol. Biol. Cell 10:1061-1075.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1061-1075
    • Ayscough, K.R.1    Eby, J.J.2    Lila, T.3    Dewar, H.4    Kozminski, K.G.5    Drubin, D.G.6
  • 17
    • 0032875465 scopus 로고    scopus 로고
    • Regulation of the cell cycle transcription factor Swi4 through auto-inhibition of DNA binding
    • Baetz, K., and B. Andrews. 1999. Regulation of the cell cycle transcription factor Swi4 through auto-inhibition of DNA binding. Mol. Cell. Biol. 19: 6729-6741.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6729-6741
    • Baetz, K.1    Andrews, B.2
  • 18
    • 0034804391 scopus 로고    scopus 로고
    • Transcriptional coregulation by the cell integrity mitogen-activated protein kinase Slt2 and the cell cycle regulator Swi4
    • Baetz, K., J. Moffat, J. Haynes, M. Chang, and B. Andrews. 2001. Transcriptional coregulation by the cell integrity mitogen-activated protein kinase Slt2 and the cell cycle regulator Swi4. Mol. Cell. Biol. 21:6515-6528.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6515-6528
    • Baetz, K.1    Moffat, J.2    Haynes, J.3    Chang, M.4    Andrews, B.5
  • 19
    • 1642499365 scopus 로고    scopus 로고
    • The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesion
    • Baetz, K. K., N. J. Krogan, A. Emili, J. Greenblatt, and P. Hieter. 2004. The ctf13-30/CTF13 genomic haploinsufficiency modifier screen identifies the yeast chromatin remodeling complex RSC, which is required for the establishment of sister chromatid cohesion. Mol. Cell. Biol. 24:1232-1244.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1232-1244
    • Baetz, K.K.1    Krogan, N.J.2    Emili, A.3    Greenblatt, J.4    Hieter, P.5
  • 20
    • 0034724182 scopus 로고    scopus 로고
    • Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
    • Bagnat, M., S. Keranen, A. Shevchenko, K., and Simons. 2000. Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc. Natl. Acad. Sci. USA 97:3254-3259.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3254-3259
    • Bagnat, M.1    Keranen, S.2    Shevchenko, A.K.3    Simons4
  • 21
    • 0037484259 scopus 로고    scopus 로고
    • Gβγ recruits Rho1 to the site of polarized growth during mating in budding yeast
    • Bar, E. E., A. T. Ellicott, and D. E. Stone. 2003. Gβγ recruits Rho1 to the site of polarized growth during mating in budding yeast. J. Biol. Chem. 278: 21798-21804.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21798-21804
    • Bar, E.E.1    Ellicott, A.T.2    Stone, D.E.3
  • 23
    • 0029789334 scopus 로고    scopus 로고
    • Yeast respond to hypotonic shock with a calcium pulse
    • Batiza, A. F., T. Schulz, and P. H. Masson. 1996. Yeast respond to hypotonic shock with a calcium pulse. J. Biol. Chem. 271:23357-23362.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23357-23362
    • Batiza, A.F.1    Schulz, T.2    Masson, P.H.3
  • 24
    • 0025170867 scopus 로고
    • Protein kinase C interaction with calcium: A phospholipid-dependent process
    • Bazzi, M. D., and G. L. Nelsestuen. 1990. Protein kinase C interaction with calcium: a phospholipid-dependent process. Biochemistry 29:7624-7630.
    • (1990) Biochemistry , vol.29 , pp. 7624-7630
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 25
    • 15844384186 scopus 로고    scopus 로고
    • Associations among PH and SH3 domain-containins proteins and Rho-type GTPases in yeast
    • Bender, L., H. S. Lo, H. Lee, V. Kokojan, V. Peterson, and A. Bender. 1996. Associations among PH and SH3 domain-containins proteins and Rho-type GTPases in Yeast. J. Cell Biol. 133:879-894.
    • (1996) J. Cell Biol. , vol.133 , pp. 879-894
    • Bender, L.1    Lo, H.S.2    Lee, H.3    Kokojan, V.4    Peterson, V.5    Bender, A.6
  • 26
    • 0032522723 scopus 로고    scopus 로고
    • Cell wall integrity modulates RHO1 activity via the exchange factor ROM2
    • Bickle, M., P. A. Delley, A. Schmidt, and M. N. Hall. 1998. Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J. 17:2235-2245.
    • (1998) EMBO J. , vol.17 , pp. 2235-2245
    • Bickle, M.1    Delley, P.A.2    Schmidt, A.3    Hall, M.N.4
  • 27
    • 0034202612 scopus 로고    scopus 로고
    • It's a kar9ochore to capture microtubules
    • Bloom, K. 2000. It's a kar9ochore to capture microtubules. Nat. Cell Biol. 2:96-98.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 96-98
    • Bloom, K.1
  • 28
    • 0141764710 scopus 로고    scopus 로고
    • 2+ signaling is required for survival of endoplasmic reticulum stress in yeast
    • 2+ signaling is required for survival of endoplasmic reticulum stress in yeast. Mol. Biol. Cell 14:4296-4305.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4296-4305
    • Bonilla, M.1    Cunningham, K.W.2
  • 29
    • 0037093384 scopus 로고    scopus 로고
    • Essential role of calcineurin in response to endoplasmic reticulum stress
    • Bonilla, M., K. K. Nastase, and K. W. Cunningham. 2002. Essential role of calcineurin in response to endoplasmic reticulum stress. EMBO J. 21: 2343-2353.
    • (2002) EMBO J. , vol.21 , pp. 2343-2353
    • Bonilla, M.1    Nastase, K.K.2    Cunningham, K.W.3
  • 30
    • 1942539985 scopus 로고    scopus 로고
    • Characterization of the transcriptional response to cell wall stress in Saccharomyces cerevisiae
    • Boorsma, A., H. de Nobel, B. ter Riet, B. Bargmann, S. Brul, K. J. Hellingwerf, and F. M. Klis. 2004. Characterization of the transcriptional response to cell wall stress in Saccharomyces cerevisiae. Yeast 21:413-427.
    • (2004) Yeast , vol.21 , pp. 413-427
    • Boorsma, A.1    De Nobel, H.2    Ter Riet, B.3    Bargmann, B.4    Brul, S.5    Hellingwerf, K.J.6    Klis, F.M.7
  • 31
    • 0032831938 scopus 로고    scopus 로고
    • Association of the cell cycle transcription factor Mbp1 with the Skn7 response regulator in budding yeast
    • Bouquin, N., A. L. Johnson, B. A. Morgan, and L. H. Johnston. 1999. Association of the cell cycle transcription factor Mbp1 with the Skn7 response regulator in budding yeast. Mol. Biol. Cell 10:3389-3400.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3389-3400
    • Bouquin, N.1    Johnson, A.L.2    Morgan, B.A.3    Johnston, L.H.4
  • 32
    • 0037425623 scopus 로고    scopus 로고
    • Periodic transcription: A cycle within a cycle
    • Breeden, L. L. 2003. Periodic transcription: a cycle within a cycle. Curr. Biol. 13:R31-38.
    • (2003) Curr. Biol. , vol.13
    • Breeden, L.L.1
  • 33
    • 0028076328 scopus 로고
    • Yeast Skn7p functions in a eukaryotic two-component regulatory pathway
    • Brown, J. L., H. Bussey, and R. C. Stewart. 1994. Yeast Skn7p functions in a eukaryotic two-component regulatory pathway. EMBO J. 13:5186-5194.
    • (1994) EMBO J. , vol.13 , pp. 5186-5194
    • Brown, J.L.1    Bussey, H.2    Stewart, R.C.3
  • 34
    • 0027501822 scopus 로고
    • SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-glucan assembly, encodes a product with domains homologous to prokaryotic two-component regulators and to heat shock transcription factors
    • Brown, J. L., S. North, and H. Bussey. 1993. SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-glucan assembly, encodes a product with domains homologous to prokaryotic two-component regulators and to heat shock transcription factors. J. Bacteriol. 175:6908-6915.
    • (1993) J. Bacteriol. , vol.175 , pp. 6908-6915
    • Brown, J.L.1    North, S.2    Bussey, H.3
  • 35
    • 0030799126 scopus 로고    scopus 로고
    • Coordination of the mating and cell integrity mitogen-activated protein kinase pathways in Saccharomyces cerevisiae
    • Buehrer, B. M., and B. Errede. 1997. Coordination of the mating and cell integrity mitogen-activated protein kinase pathways in Saccharomyces cerevisiae. Mol. Cell. Biol. 17:6517-6525.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6517-6525
    • Buehrer, B.M.1    Errede, B.2
  • 36
    • 0142184966 scopus 로고    scopus 로고
    • Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress
    • Bulik, D. A., M. Olczak, H. A. Lucero, B. C. Osmond, P. W. Robbins, and C. A. Specht. 2003. Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress. Eukaryot. Cell 2:886-900.
    • (2003) Eukaryot. Cell , vol.2 , pp. 886-900
    • Bulik, D.A.1    Olczak, M.2    Lucero, H.A.3    Osmond, B.C.4    Robbins, P.W.5    Specht, C.A.6
  • 37
    • 0031663368 scopus 로고    scopus 로고
    • Role of small G proteins in yeast cell polarization and wall biosynthesis
    • Cabib, E., J. Drgonova, and T. Drgon. 1998. Role of small G proteins in yeast cell polarization and wall biosynthesis. Annu. Rev. Biochem. 67: 307-333.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 307-333
    • Cabib, E.1    Drgonova, J.2    Drgon, T.3
  • 38
    • 0035827639 scopus 로고    scopus 로고
    • The yeast cell wall and septum as paradigms of cell growth and morphogenesis
    • Cabib, E., D-H. Roh, M. Schmidt, L. B. Crotti, and A. Varma. 2001. The yeast cell wall and septum as paradigms of cell growth and morphogenesis. J. Biol. Chem. 276:19678-19682.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19678-19682
    • Cabib, E.1    Roh, D.-H.2    Schmidt, M.3    Crotti, L.B.4    Varma, A.5
  • 40
    • 0028110116 scopus 로고
    • Mating type-specific cell-cell recognition of Saccharomyces cerevisiae: Cell wall attachment and active sites of a- and alpha-agglutinin
    • Cappellaro, C., C. Baldermann, R. Rachel, and W. Tanner. 1994. Mating type-specific cell-cell recognition of Saccharomyces cerevisiae: cell wall attachment and active sites of a- and alpha-agglutinin. EMBO J. 13:4737-4744.
    • (1994) EMBO J. , vol.13 , pp. 4737-4744
    • Cappellaro, C.1    Baldermann, C.2    Rachel, R.3    Tanner, W.4
  • 41
    • 15444346372 scopus 로고    scopus 로고
    • In silicio identification glycosyl-phosphatidylinositol-anchored plasma membrane and cell wall proteins of Saccharomyces cerevisiae
    • Caro, H. P., H. Tettelin, J. H. Vossen, A. F. J. Ram, H. Van den Ende, and F. Klis. 1997. In silicio identification glycosyl-phosphatidylinositol- anchored plasma membrane and cell wall proteins of Saccharomyces cerevisiae. Yeast 13:1477-1489.
    • (1997) Yeast , vol.13 , pp. 1477-1489
    • Caro, H.P.1    Tettelin, H.2    Vossen, J.H.3    Ram, A.F.J.4    Van Den Ende, H.5    Klis, F.6
  • 42
    • 0033602281 scopus 로고    scopus 로고
    • Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast
    • Cassamayor, A., P. D. Torrance, T. Kobayashi, J. Thorner, and D. R. Alessi. 1999. Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast. Curr. Biol. 9:186-197.
    • (1999) Curr. Biol. , vol.9 , pp. 186-197
    • Cassamayor, A.1    Torrance, P.D.2    Kobayashi, T.3    Thorner, J.4    Alessi, D.R.5
  • 43
    • 0035989364 scopus 로고    scopus 로고
    • Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway
    • Chai, B., J. M. Hsu, J. Du, and B. C. Laurent. 2002. Yeast RSC function is required for organization of the cellular cytoskeleton via an alternative PKC1 pathway. Genetics 161:575-584.
    • (2002) Genetics , vol.161 , pp. 575-584
    • Chai, B.1    Hsu, J.M.2    Du, J.3    Laurent, B.C.4
  • 44
    • 0037178414 scopus 로고    scopus 로고
    • Formins set the record straight
    • Chang, F., and M. Peter. 2002. Formins set the record straight. Science 297: 531-532.
    • (2002) Science , vol.297 , pp. 531-532
    • Chang, F.1    Peter, M.2
  • 45
    • 0346435091 scopus 로고    scopus 로고
    • Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase
    • Chavan, M., M. Rekowicz, and W. Lennarz. 2003. Insight into functional aspects of Stt3p, a subunit of the oligosaccharyl transferase. J. Biol. Chem. 278:51441-51447.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51441-51447
    • Chavan, M.1    Rekowicz, M.2    Lennarz, W.3
  • 46
    • 0027476071 scopus 로고
    • A pair of putative protein kinase genes (YPK1 and YPK2) is required for cell growth in Saccharomyces cerevisiae
    • Chen, P., K. S. Lee, and D. E. Levin. 1993. A pair of putative protein kinase genes (YPK1 and YPK2) is required for cell growth in Saccharomyces cerevisiae. Mol. Gen. Genet. 236:443-447.
    • (1993) Mol. Gen. Genet. , vol.236 , pp. 443-447
    • Chen, P.1    Lee, K.S.2    Levin, D.E.3
  • 47
    • 0038607442 scopus 로고    scopus 로고
    • Phosphorylation of Saccharomyces cerevisiae CTP synthetase at Ser424 by protein kinases A and C regulates phosphatidylcholine synthesis by the CDP-choline pathway
    • Choi, M-G., T-S. Park, and G. M. Carman. 2003. Phosphorylation of Saccharomyces cerevisiae CTP synthetase at Ser424 by protein kinases A and C regulates phosphatidylcholine synthesis by the CDP-choline pathway. J. Biol. Chem. 278:23610-23616.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23610-23616
    • Choi, M.-G.1    Park, T.-S.2    Carman, G.M.3
  • 48
    • 0027937981 scopus 로고
    • Are yeast chitin synthases regulated at the transcriptional or the posttranslational level?
    • Choi, W. J., B. Santos, A. Duran, and E. Cabib. 1994. Are yeast chitin synthases regulated at the transcriptional or the posttranslational level? Mol. Cell. Biol. 14:7685-7694.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7685-7694
    • Choi, W.J.1    Santos, B.2    Duran, A.3    Cabib, E.4
  • 49
    • 0031962930 scopus 로고    scopus 로고
    • A mutation in the Rho1-GAP-encoding gene BEM2 of Saccharomyces cerevisiae affects morphogenesis and cell wall functionality
    • Cid, V. J., R. Cenamor, M. Sanchez, and C. Nombela. 1998. A mutation in the Rho1-GAP-encoding gene BEM2 of Saccharomyces cerevisiae affects morphogenesis and cell wall functionality. Microbiology 1:25-36.
    • (1998) Microbiology , vol.1 , pp. 25-36
    • Cid, V.J.1    Cenamor, R.2    Sanchez, M.3    Nombela, C.4
  • 50
    • 0029094218 scopus 로고
    • Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae
    • Cid, V. J., A. Duran, F. Rey, M. P. Snyder, C. Nombela, and M. Sanchez. 1995. Molecular basis of cell integrity and morphogenesis in Saccharomyces cerevisiae. Microbiol. Rev. 59:345-386.
    • (1995) Microbiol. Rev. , vol.59 , pp. 345-386
    • Cid, V.J.1    Duran, A.2    Rey, F.3    Snyder, M.P.4    Nombela, C.5    Sanchez, M.6
  • 51
    • 0142216123 scopus 로고    scopus 로고
    • Ask10p mediates the oxidative stress-induced destruction of the Saccharomyces cerevisiae C-type cyclin Une3p/Srb11p
    • Cohen, T. J., K. Lee, L. H. Rutkowski, and R. Strich. 2003. Ask10p mediates the oxidative stress-induced destruction of the Saccharomyces cerevisiae C-type cyclin Une3p/Srb11p. Eukaryot. Cell 2:962-970.
    • (2003) Eukaryot. Cell , vol.2 , pp. 962-970
    • Cohen, T.J.1    Lee, K.2    Rutkowski, L.H.3    Strich, R.4
  • 52
    • 0033590589 scopus 로고    scopus 로고
    • Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum
    • Cohen-Kupiec, R., K. E. Broglie, D. Friesem, R. M. Broglie, and I. Chet. 1999. Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum. Gene 226:147-154.
    • (1999) Gene , vol.226 , pp. 147-154
    • Cohen-Kupiec, R.1    Broglie, K.E.2    Friesem, D.3    Broglie, R.M.4    Chet, I.5
  • 53
    • 0037063353 scopus 로고    scopus 로고
    • YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae
    • Collister, M., M. P. Didmon, F. MacIsaac, M. J. Stark, N. Q. MacDonald, and S. M. Keyes. 2002. YIL113w encodes a functional dual-specificity protein phosphatase which specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S. cerevisiae. FEBS Lett. 527:186-192.
    • (2002) FEBS Lett. , vol.527 , pp. 186-192
    • Collister, M.1    Didmon, M.P.2    MacIsaac, F.3    Stark, M.J.4    MacDonald, N.Q.5    Keyes, S.M.6
  • 55
    • 0026600968 scopus 로고
    • A synthetic lethal screen identifies SLK1, a novel protein kinase homolog implicated in yeast cell morphogenesis and cell growth
    • Costigan, C., S. Gehrung, and M. Snyder. 1992. A synthetic lethal screen identifies SLK1, a novel protein kinase homolog implicated in yeast cell morphogenesis and cell growth. Mol. Cell. Biol. 12:1162-1178.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1162-1178
    • Costigan, C.1    Gehrung, S.2    Snyder, M.3
  • 56
    • 0030783253 scopus 로고    scopus 로고
    • STT4 is an essential phosphatidylinositol 4-kinase that is a target of wartmannin in Saccharomyces cerevisiae
    • Cutler, N. S., J. Heitman, and M. E. Cardenas. 1997. STT4 is an essential phosphatidylinositol 4-kinase that is a target of wartmannin in Saccharomyces cerevisiae. J. Biol. Chem. 272:27671-27677.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27671-27677
    • Cutler, N.S.1    Heitman, J.2    Cardenas, M.E.3
  • 57
    • 0026637095 scopus 로고
    • 2+/ calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone
    • 2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone. Mol. Cell. Biol. 12:3460-3469.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3460-3469
    • Cyert, M.S.1    Thorner, J.2
  • 58
    • 0031689591 scopus 로고    scopus 로고
    • A new method for quantitative determination of polysaccharides in the yeast cell wall. Application to the cell wall defective mutants of Saccharomyces cerevisiae
    • Dallies, N., J. Francois, and V. Paquet. 1998. A new method for quantitative determination of polysaccharides in the yeast cell wall. Application to the cell wall defective mutants of Saccharomyces cerevisiae. Yeast 14:1297-1306.
    • (1998) Yeast , vol.14 , pp. 1297-1306
    • Dallies, N.1    Francois, J.2    Paquet, V.3
  • 59
    • 0027250485 scopus 로고
    • Potentially rapid walking in cellular regulatory networks using the gene-gene interference method in yeast
    • Daniel, J. 1993. Potentially rapid walking in cellular regulatory networks using the gene-gene interference method in yeast. Mol. Gen. Genet. 240: 245-257.
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 245-257
    • Daniel, J.1
  • 60
    • 0029561101 scopus 로고
    • A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway
    • Davenport, K. R., M. Sohaskey, Y. Kamada, D. E. Levin, and M. C. Gustin. 1995. A second osmosensing signal transduction pathway in yeast. Hypotonic shock activates the PKC1 protein kinase-regulated cell integrity pathway. J. Biol. Chem. 270:30157-30161.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30157-30161
    • Davenport, K.R.1    Sohaskey, M.2    Kamada, Y.3    Levin, D.E.4    Gustin, M.C.5
  • 61
    • 2942755857 scopus 로고    scopus 로고
    • Cln3 activates G1-specific transcription via phosphorylation of the SBF bound repressor Whi5
    • de Bruin, R. A., W. H. McDonald, T. I. Kalashnikova, J. Yates 3rd, and C. Wittenberg. 2004. Cln3 activates G1-specific transcription via phosphorylation of the SBF bound repressor Whi5. Cell 117:887-898.
    • (2004) Cell , vol.117 , pp. 887-898
    • De Bruin, R.A.1    McDonald, W.H.2    Kalashnikova, T.I.3    Yates III, J.4    Wittenberg, C.5
  • 62
    • 0037148529 scopus 로고    scopus 로고
    • The conserved Pkh-Ypk kinase cascade is required for endocytosis in yeast
    • de Hart, A. K., J. D. Schnell, D. A. Allen, and L. Hicke. 2002. The conserved Pkh-Ypk kinase cascade is required for endocytosis in yeast. J. Cell Biol. 156:241-248.
    • (2002) J. Cell Biol. , vol.156 , pp. 241-248
    • De Hart, A.K.1    Schnell, J.D.2    Allen, D.A.3    Hicke, L.4
  • 63
    • 0033523764 scopus 로고    scopus 로고
    • Cell wall stress depolarizes cell growth via hyperactivation of RHO1
    • Delley, P. A., and M. N. Hall. 1999. Cell wall stress depolarizes cell growth via hyperactivation of RHO1. J. Cell Biol. 147:163-174.
    • (1999) J. Cell Biol. , vol.147 , pp. 163-174
    • Delley, P.A.1    Hall, M.N.2
  • 64
    • 13744251877 scopus 로고    scopus 로고
    • Molecular analysis reveals localization of Saccharomyces cerevisiae protein kinase C to sites of polarized growth and Pkc1p targeting to the nucleus and mitotic spindle
    • Denis, V., and M. S. Cyert. 2005. Molecular analysis reveals localization of Saccharomyces cerevisiae protein kinase C to sites of polarized growth and Pkc1p targeting to the nucleus and mitotic spindle. Eukaryot. Cell 4:36-45.
    • (2005) Eukaryot. Cell , vol.4 , pp. 36-45
    • Denis, V.1    Cyert, M.S.2
  • 65
    • 0037214352 scopus 로고    scopus 로고
    • Targeting the MEF2-like transcription factor Smp1 by the stress-activated Hog1 mitogen-activated protein kinase
    • de Nadal, E., L. Casadomé, and F. Posas. 2003. Targeting the MEF2-like transcription factor Smp1 by the stress-activated Hog1 mitogen-activated protein kinase. Mol. Cell. Biol. 23:229-237.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 229-237
    • De Nadal, E.1    Casadomé, L.2    Posas, F.3
  • 66
    • 0033832763 scopus 로고    scopus 로고
    • Cell wall perturbation in yeast results in dual phosphorylation of the Slt2/Mpk1 MAP kinase and in an Slt2-mediated increase in FKS2-lacZ expression, glucanase resistance and thermotolerance
    • de Nobel, H., C. Ruiz, H. Martin, W. Morris, S. Brul, M. Molina, and F. M. Klis. 2000. Cell wall perturbation in yeast results in dual phosphorylation of the Slt2/Mpk1 MAP kinase and in an Slt2-mediated increase in FKS2-lacZ expression, glucanase resistance and thermotolerance. Microbiology 146: 2121-2132.
    • (2000) Microbiology , vol.146 , pp. 2121-2132
    • De Nobel, H.1    Ruiz, C.2    Martin, H.3    Morris, W.4    Brul, S.5    Molina, M.6    Klis, F.M.7
  • 68
    • 0025809077 scopus 로고
    • Passage of molecules through yeast cell walls: A brief essay-review
    • de Nobel, J. G., and J. A. Barnett. 1991. Passage of molecules through yeast cell walls: a brief essay-review. Yeast 7:313-323.
    • (1991) Yeast , vol.7 , pp. 313-323
    • De Nobel, J.G.1    Barnett, J.A.2
  • 69
    • 0025517598 scopus 로고
    • The glucanase-soluble mannoproteins limit cell wall porosity in Saccharomyces cerevisiae
    • de Nobel, J. G., F. M. Klis, J. Priem, T. Munnik, and H. van den Ende. 1990. The glucanase-soluble mannoproteins limit cell wall porosity in Saccharomyces cerevisiae. Yeast 6:491-499.
    • (1990) Yeast , vol.6 , pp. 491-499
    • De Nobel, J.G.1    Klis, F.M.2    Priem, J.3    Munnik, T.4    Van Den Ende, H.5
  • 70
    • 0032546798 scopus 로고    scopus 로고
    • MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Desrivieres, S., F. T. Cooke, P. J. Parker, and M. N. Hall. 1998. MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae. J. Biol. Chem. 273:15787-15793.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15787-15793
    • Desrivieres, S.1    Cooke, F.T.2    Parker, P.J.3    Hall, M.N.4
  • 72
    • 0030988939 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae MADS-box transcription factor Rlm1 is a target for the Mpk1 mitogen-activated protein kinase pathway
    • Dodou, E., and R. Treisman. 1997. The Saccharomyces cerevisiae MADS-box transcription factor Rlm1 is a target for the Mpk1 mitogen-activated protein kinase pathway. Mol. Cell. Biol. 17:1848-1859.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1848-1859
    • Dodou, E.1    Treisman, R.2
  • 73
    • 0028157519 scopus 로고
    • MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae
    • Doi, K., A. Gartner, G. Ammerer, B. Errede, H. Shinkawa, K. Sugimoto, and K. Matsumoto. 1994. MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. EMBO J. 13:61-70.
    • (1994) EMBO J. , vol.13 , pp. 61-70
    • Doi, K.1    Gartner, A.2    Ammerer, G.3    Errede, B.4    Shinkawa, H.5    Sugimoto, K.6    Matsumoto, K.7
  • 74
    • 0037815488 scopus 로고    scopus 로고
    • Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast
    • Dong, Y., D. Pruyne, and A. Bretscher. 2003. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J. Cell Biol. 161:1081-1092.
    • (2003) J. Cell Biol. , vol.161 , pp. 1081-1092
    • Dong, Y.1    Pruyne, D.2    Bretscher, A.3
  • 77
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D. G., and W. J. Nelson. 1996. Origins of cell polarity. Cell 84: 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 79
    • 0033647489 scopus 로고    scopus 로고
    • Pheromone response, mating and cell biology
    • Elion, E. A. 2000. Pheromone response, mating and cell biology. Curr. Opin. Microbiol. 3:573-581.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 573-581
    • Elion, E.A.1
  • 80
    • 0028268281 scopus 로고
    • Genes that can bypass the CLN requirement for Saccharomyces cerevisiae cell cycle START
    • Epstein, C. B., and F. R. Cross. 1994. Genes that can bypass the CLN requirement for Saccharomyces cerevisiae cell cycle START. Mol. Cell. Biol. 14:2041-2047.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2041-2047
    • Epstein, C.B.1    Cross, F.R.2
  • 83
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • Evangelista, M., S. Zigmond, and C. Boone. 2003. Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116: 2603-2611.
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 84
    • 0030445778 scopus 로고    scopus 로고
    • Tripping the switch fantastic: How a protein kinase cascade can convert graded inputs into switch-like outputs
    • Ferrell, J. E. Jr. 1996. Tripping the switch fantastic: how a protein kinase cascade can convert graded inputs into switch-like outputs. Trends Biochem. Sci. 21:460-466.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 460-466
    • Ferrell Jr., J.E.1
  • 85
    • 0032548828 scopus 로고    scopus 로고
    • Sec3 is a spatial landmark for polarized secretion in budding yeast
    • Finger, F. P., T. E. Hughes, and P. Novick. 1998. Sec3 is a spatial landmark for polarized secretion in budding yeast. Cell 92:559-571.
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 86
    • 0031451748 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae CCH1 gene is involved in calcium influx and mating
    • Fischer, M., N. Schnell, J. Chattaway, P. Davies, G. Dixon, and D. Sanders. 1997. The Saccharomyces cerevisiae CCH1 gene is involved in calcium influx and mating. FEBS Lett. 419:259-262.
    • (1997) FEBS Lett. , vol.419 , pp. 259-262
    • Fischer, M.1    Schnell, N.2    Chattaway, J.3    Davies, P.4    Dixon, G.5    Sanders, D.6
  • 87
    • 1642524418 scopus 로고    scopus 로고
    • Reciprocal regulation between Slt2 MAPK and isoforms of Msg5 dual-specificity protein phosphatase modulates the yeast cell integrity pathway
    • Flandez, M., I. C. Cosano, C. Nombela, H. Martin, and M. Molina. 2004. Reciprocal regulation between Slt2 MAPK and isoforms of Msg5 dual-specificity protein phosphatase modulates the yeast cell integrity pathway. J. Biol. Chem. 279:11027-11034.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11027-11034
    • Flandez, M.1    Cosano, I.C.2    Nombela, C.3    Martin, H.4    Molina, M.5
  • 88
    • 0032579489 scopus 로고    scopus 로고
    • Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif
    • Flynn, P., H. Mellor, R. Palmer, G. Panayotou, and P. J. Parker. 1998. Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif. J. Biol. Chem. 273:2698-2705.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2698-2705
    • Flynn, P.1    Mellor, H.2    Palmer, R.3    Panayotou, G.4    Parker, P.J.5
  • 89
    • 0026619467 scopus 로고
    • Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from alpha-factor arrest in yeast
    • Poor, F., S. A. Parent, N. Morin, A. M. Dahl, N. Ramadan, G. Chrebet, K. A. Bostian, and J. B. Nielsen. 1992. Calcineurin mediates inhibition by FK506 and cyclosporin of recovery from alpha-factor arrest in yeast. Nature 360:682-684.
    • (1992) Nature , vol.360 , pp. 682-684
    • Poor, F.1    Parent, S.A.2    Morin, N.3    Dahl, A.M.4    Ramadan, N.5    Chrebet, G.6    Bostian, K.A.7    Nielsen, J.B.8
  • 90
    • 0033977772 scopus 로고    scopus 로고
    • Emerging novel antifungal agents
    • Fostel, J. M., and P. A. Lartey. 2000. Emerging novel antifungal agents. Drug Disc. Today 5:25-32.
    • (2000) Drug Disc. Today , vol.5 , pp. 25-32
    • Fostel, J.M.1    Lartey, P.A.2
  • 91
    • 0035172107 scopus 로고    scopus 로고
    • Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology
    • Foti, M., A. Audhya, and S. D. Emr. 2001. Sac1 lipid phosphatase and Stt4 phosphatidylinositol 4-kinase regulate a pool of phosphatidylinositol 4-phosphate that functions in the control of the actin cytoskeleton and vacuole morphology. Mol. Biol. Cell 12:2396-2411.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2396-2411
    • Foti, M.1    Audhya, A.2    Emr, S.D.3
  • 92
    • 0035803482 scopus 로고    scopus 로고
    • Sphingoid base signaling via Pkh kinases is required for endocytosis in yeast
    • Friant, S., R. Lombardi, T. Schmelzle, M. N. Hall, and H. Riezman. 2001. Sphingoid base signaling via Pkh kinases is required for endocytosis in yeast. EMBO J. 20:6783-6792.
    • (2001) EMBO J. , vol.20 , pp. 6783-6792
    • Friant, S.1    Lombardi, R.2    Schmelzle, T.3    Hall, M.N.4    Riezman, H.5
  • 93
    • 0034660458 scopus 로고    scopus 로고
    • Increased protein kinase or decreased PP2A activity bypasses the sphingoid base requirement in endocytosis
    • Friant, S., B. Zanolari, and H. Riezman. 2000. Increased protein kinase or decreased PP2A activity bypasses the sphingoid base requirement in endocytosis. EMBO J. 19:2834-2844.
    • (2000) EMBO J. , vol.19 , pp. 2834-2844
    • Friant, S.1    Zanolari, B.2    Riezman, H.3
  • 94
    • 0031665143 scopus 로고    scopus 로고
    • Rho1p-Bni1p-Spa2p interactions: Implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae
    • Fujiwara, T., K. Tanaka, A. Mino, M. Kikyo, K. Takahashi, K. Shimizu, and Y. Takai. 1998. Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 9:1221-1233.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1221-1233
    • Fujiwara, T.1    Tanaka, K.2    Mino, A.3    Kikyo, M.4    Takahashi, K.5    Shimizu, K.6    Takai, Y.7
  • 95
    • 2442477661 scopus 로고    scopus 로고
    • The global transcriptional response to transient cell wall damage in Saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway
    • Garcia, R., C. Bermejo, C. Grau, R. Perez, J. M. Rodriquez-Pena, J. Francois, C. Nombela, and J. Arroyo. 2004. The global transcriptional response to transient cell wall damage in Saccharomyces cerevisiae and its regulation by the cell integrity signaling pathway. J. Biol. Chem. 279:15183-15195.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15183-15195
    • Garcia, R.1    Bermejo, C.2    Grau, C.3    Perez, R.4    Rodriquez-Pena, J.M.5    Francois, J.6    Nombela, C.7    Arroyo, J.8
  • 97
    • 0029954105 scopus 로고    scopus 로고
    • The PMT gene family: Protein O-glycosylation in Saccharomyces cerevisiae is vital
    • Gentzsch, M., and W. Tanner. 1996. The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. EMBO J. 15:5752-5759.
    • (1996) EMBO J. , vol.15 , pp. 5752-5759
    • Gentzsch, M.1    Tanner, W.2
  • 98
    • 0030033020 scopus 로고    scopus 로고
    • Antifungal agents: Chemotherapeutic targets and immunologic strategies
    • Geogopapadakou, N. H., and T. J. Walsh. 1996. Antifungal agents: chemotherapeutic targets and immunologic strategies. Antimicrob. Agents Chemother. 40:279-291.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 279-291
    • Geogopapadakou, N.H.1    Walsh, T.J.2
  • 99
    • 2942705969 scopus 로고    scopus 로고
    • Candida and candidiasis: The cell wall as a potential target for antifungal therapy
    • Gozalbo, D., P. Roig, E. Villamon, and M. L. Gill. 2004. Candida and candidiasis: the cell wall as a potential target for antifungal therapy. Curr. Drug Targets Infect. Disord. 4:117-135.
    • (2004) Curr. Drug Targets Infect. Disord. , vol.4 , pp. 117-135
    • Gozalbo, D.1    Roig, P.2    Villamon, E.3    Gill, M.L.4
  • 100
    • 0030789480 scopus 로고    scopus 로고
    • A role for the Pkc1 MAP kinase pathway of Saccharomyces cerevisiae in bud emergence and identification of a putative upstream regulator
    • Gray, J. V., J. P. Ogas, Y. Kamada, M. Stone, D. E. Levin, and I. Herskowitz. 1997. A role for the Pkc1 MAP kinase pathway of Saccharomyces cerevisiae in bud emergence and identification of a putative upstream regulator. EMBO J. 16:4924-4937.
    • (1997) EMBO J. , vol.16 , pp. 4924-4937
    • Gray, J.V.1    Ogas, J.P.2    Kamada, Y.3    Stone, M.4    Levin, D.E.5    Herskowitz, I.6
  • 101
    • 0141591661 scopus 로고    scopus 로고
    • A synthetic analysis of the Saccharomyces cerevisiae stress sensor Mid2p, and indentification of a Mid2p-interacting protein, Zeo1, that modulates the PKC1-MPK1 cell integrity pathway
    • Green, R., G. Lesage, A-M. Sdicu, P. Menard, and H. Bussey. 2003. A synthetic analysis of the Saccharomyces cerevisiae stress sensor Mid2p, and indentification of a Mid2p-interacting protein, Zeo1, that modulates the PKC1-MPK1 cell integrity pathway. Microbiology 149:2487-2499.
    • (2003) Microbiology , vol.149 , pp. 2487-2499
    • Green, R.1    Lesage, G.2    Sdicu, A.-M.3    Menard, P.4    Bussey, H.5
  • 102
    • 0035747143 scopus 로고    scopus 로고
    • Uncommon opportunistic fungi: New nosocomial threats
    • Groll, A. H., and T. J. Walsh. 2001. Uncommon opportunistic fungi: new nosocomial threats. Clin. Microbiol. Infect. Dis. 7:8-24.
    • (2001) Clin. Microbiol. Infect. Dis. , vol.7 , pp. 8-24
    • Groll, A.H.1    Walsh, T.J.2
  • 103
    • 0035067186 scopus 로고    scopus 로고
    • Spatial regulation of the exocyst complex by Rho1 GTPase
    • Guo, W., F. Tamanoi, and P. Novick. 2001. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat. Cell Biol. 3:353-360.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 353-360
    • Guo, W.1    Tamanoi, F.2    Novick, P.3
  • 105
    • 0037077207 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase
    • Hahn, J-S., and D. J. Thiele. 2002. Regulation of the Saccharomyces cerevisiae Slt2 kinase pathway by the stress-inducible Sdp1 dual specificity phosphatase. J. Biol. Chem. 277:21278-21284.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21278-21284
    • Hahn, J.-S.1    Thiele, D.J.2
  • 106
    • 2342609778 scopus 로고    scopus 로고
    • Probing the importance of potential roles of the binding of the PH-domain protein Boi1 to acidic phospholipids
    • Hallett, M. A., H. S. Lo, and A. Bender. 2002. Probing the importance of potential roles of the binding of the PH-domain protein Boi1 to acidic phospholipids. BMC Cell Biol. 3:16-29.
    • (2002) BMC Cell Biol. , vol.3 , pp. 16-29
    • Hallett, M.A.1    Lo, H.S.2    Bender, A.3
  • 107
    • 0347091261 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae LSB6 gene encodes phosphatidylinositol 4-kinase activity
    • Han, G-S., A. Audhya, D. J. Markley, S. D. Emr, and G. M. Carman. 2002. The Saccharomyces cerevisiae LSB6 gene encodes phosphatidylinositol 4-kinase activity. J. Biol. Chem. 277:47709-47718.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47709-47718
    • Han, G.-S.1    Audhya, A.2    Markley, D.J.3    Emr, S.D.4    Carman, G.M.5
  • 108
    • 0030590881 scopus 로고    scopus 로고
    • Interaction of G protein Gbetagamma dimers with small GTP-binding proteins of the Rho family
    • Harhammer, R., A. Gohla, and G. Schultz. 1996. Interaction of G protein Gbetagamma dimers with small GTP-binding proteins of the Rho family. FEBS Lett. 399:211-214.
    • (1996) FEBS Lett. , vol.399 , pp. 211-214
    • Harhammer, R.1    Gohla, A.2    Schultz, G.3
  • 109
    • 0036440952 scopus 로고    scopus 로고
    • Force and compliance: Rethinking morphogenesis in walled cells
    • Harold, F. M. 2002. Force and compliance: rethinking morphogenesis in walled cells. Fungal Genet. Biol. 37:271-282.
    • (2002) Fungal Genet. Biol. , vol.37 , pp. 271-282
    • Harold, F.M.1
  • 110
    • 0029939201 scopus 로고    scopus 로고
    • Binding to the yeast Swi4,6-dependent cell cycle box, CACGAAA, is cell cycle regulated in vivo
    • Harrington, L. A., and B. J. Andrews. 1996. Binding to the yeast Swi4,6-dependent cell cycle box, CACGAAA, is cell cycle regulated in vivo. Nucleic Acids Res. 24:558-565.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 558-565
    • Harrington, L.A.1    Andrews, B.J.2
  • 111
    • 0035066932 scopus 로고    scopus 로고
    • A role for the Pkc1p/Mpk1p kinase cascade in the morphogenesis checkpoint
    • Harrison, J. C., E. S. Bardes, Y. Ohya, and D. J. Lew. 2001. A role for the Pkc1p/Mpk1p kinase cascade in the morphogenesis checkpoint. Nat. Cell Biol. 3:417-420.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 417-420
    • Harrison, J.C.1    Bardes, E.S.2    Ohya, Y.3    Lew, D.J.4
  • 112
    • 1642576083 scopus 로고    scopus 로고
    • Stress-activation mechanisms for the "cell integrity" MAPK pathway
    • Harrison, J. C., T. R. Zyla, E. S. G. Bardes, and D. J. Lew. 2004. Stress-activation mechanisms for the "cell integrity" MAPK pathway. J. Biol. Chem. 279:2616-2622.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2616-2622
    • Harrison, J.C.1    Zyla, T.R.2    Bardes, E.S.G.3    Lew, D.J.4
  • 113
    • 0026496258 scopus 로고
    • A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs
    • Hart, M. J., Y. Maru, D. Leonard, O. N. Witte, T. Evans, and R. A. Cerione. 1992. A GDP dissociation inhibitor that serves as a GTPase inhibitor for the Ras-like protein CDC42Hs. Science 258:812-815.
    • (1992) Science , vol.258 , pp. 812-815
    • Hart, M.J.1    Maru, Y.2    Leonard, D.3    Witte, O.N.4    Evans, T.5    Cerione, R.A.6
  • 114
    • 0033009538 scopus 로고    scopus 로고
    • The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae
    • Heinisch, J. J., A. Lorberg, H. P. Schmitz, and J. J. Jacoby. 1999. The protein kinase C-mediated MAP kinase pathway involved in the maintenance of cellular integrity in Saccharomyces cerevisiae. Mol. Microbiol. 32: 671-680.
    • (1999) Mol. Microbiol. , vol.32 , pp. 671-680
    • Heinisch, J.J.1    Lorberg, A.2    Schmitz, H.P.3    Jacoby, J.J.4
  • 115
    • 0025776523 scopus 로고
    • Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast
    • Heitman, J., N. R. Movva, and M. N. Hall. 1991. Targets for cell cycle arrest by the immunosuppressant rapamycin in yeast. Science 253:905-909.
    • (1991) Science , vol.253 , pp. 905-909
    • Heitman, J.1    Movva, N.R.2    Hall, M.N.3
  • 116
    • 0031882240 scopus 로고    scopus 로고
    • TOR2 is part of two related signaling pathways coordinating cell growth in Saccharomyces cerevisiae
    • Helliwell, S. B., I. Howald, N. Barbet, and M. N. Hall. 1998. TOR2 is part of two related signaling pathways coordinating cell growth in Saccharomyces cerevisiae. Genetics 148:99-112.
    • (1998) Genetics , vol.148 , pp. 99-112
    • Helliwell, S.B.1    Howald, I.2    Barbet, N.3    Hall, M.N.4
  • 117
    • 0032488042 scopus 로고    scopus 로고
    • The Rho1 effector Pkc1, but not Bni1, mediates signalling from Tor2 to the actin cytoskeleton
    • Helliwell, S. B., A. Schmidt, Y. Ohya, and M. N. Hall. 1998. The Rho1 effector Pkc1, but not Bni1, mediates signalling from Tor2 to the actin cytoskeleton. Curr. Biol. 8:1211-1214.
    • (1998) Curr. Biol. , vol.8 , pp. 1211-1214
    • Helliwell, S.B.1    Schmidt, A.2    Ohya, Y.3    Hall, M.N.4
  • 118
    • 0028137771 scopus 로고
    • TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast
    • Helliwell, S. B., P. Wagner, J. Kunz, M. Deuter-Reinhard, R. Henriquez, and M. N. Hall. 1994. TOR1 and TOR2 are structurally and functionally similar but not identical phosphatidylinositol kinase homologues in yeast. Mol. Biol. Cell 5:105-118.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 105-118
    • Helliwell, S.B.1    Wagner, P.2    Kunz, J.3    Deuter-Reinhard, M.4    Henriquez, R.5    Hall, M.N.6
  • 119
    • 0028985079 scopus 로고
    • MAP kinase pathways in yeast: For mating and more
    • Herskowitz, I. 1995. MAP kinase pathways in yeast: for mating and more. Cell 80:187-197.
    • (1995) Cell , vol.80 , pp. 187-197
    • Herskowitz, I.1
  • 120
    • 0032550179 scopus 로고    scopus 로고
    • Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization
    • Hicke, L., B. Zanolari, and H. Riezman. 1998. Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 141:349-358.
    • (1998) J. Cell Biol. , vol.141 , pp. 349-358
    • Hicke, L.1    Zanolari, B.2    Riezman, H.3
  • 121
    • 0036282743 scopus 로고    scopus 로고
    • Osmotic stress signaling and osmoadaptation in yeasts
    • Hohmann, S. 2002. Osmotic stress signaling and osmoadaptation in yeasts. Microbiol. Mol. Biol. Rev. 66:300-372.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 300-372
    • Hohmann, S.1
  • 122
    • 0032546932 scopus 로고    scopus 로고
    • Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis
    • Homma, K., S. Terui, M. Minemura, H. Qadota, Y. Anraku, Y. Kanaho, Y. Ohya. 1998. Phosphatidylinositol-4-phosphate 5-kinase localized on the plasma membrane is essential for yeast cell morphogenesis. J. Biol. Chem. 273:15779-15786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15779-15786
    • Homma, K.1    Terui, S.2    Minemura, M.3    Qadota, H.4    Anraku, Y.5    Kanaho, Y.6    Ohya, Y.7
  • 123
    • 0025906597 scopus 로고
    • Post-translational modifications of the C-terminal region of rho are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins
    • Hori, Y., A. Kikuchi, M. Isomura, M. Katayama, Y. Miura, H. Fujioka, K. Kaibuchi, and Y. Takai. 1991. Post-translational modifications of the C-terminal region of rho are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 6: 515-522.
    • (1991) Oncogene , vol.6 , pp. 515-522
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 124
    • 0034827609 scopus 로고    scopus 로고
    • PKC1, a protein kinase C homologue of Saccharomyces cerevisiae, participates in microtubule function through the yeast EB1 homologue, BIM1
    • Hosotani, T., H. Koyama, M. Uchino, T. Miyakawa, and E. Tsuchiya. 2001. PKC1, a protein kinase C homologue of Saccharomyces cerevisiae, participates in microtubule function through the yeast EB1 homologue, BIM1. Genes Cells 6:775-788.
    • (2001) Genes Cells , vol.6 , pp. 775-788
    • Hosotani, T.1    Koyama, H.2    Uchino, M.3    Miyakawa, T.4    Tsuchiya, E.5
  • 125
    • 0028054926 scopus 로고
    • The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro
    • Hottiger, T., C. de Virgilio, M. N. Hall, T. Boller, and A. Wiemken. 1994. The role of trehalose synthesis for the acquisition of thermotolerance in yeast. II. Physiological concentrations of trehalose increase the thermal stability of proteins in vitro. Eur. J. Biochem. 219:187-193.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 187-193
    • Hottiger, T.1    De Virgilio, C.2    Hall, M.N.3    Boller, T.4    Wiemken, A.5
  • 126
    • 0036295684 scopus 로고    scopus 로고
    • Dissection of a complex phenotype by functional genomics reveals roles for the yeast cyclin-dependent protein kinase Pho85 in stress adaptation and cell integrity
    • Huang, D., J. Moffat, and B. Andrews. 2002. Dissection of a complex phenotype by functional genomics reveals roles for the yeast cyclin-dependent protein kinase Pho85 in stress adaptation and cell integrity. Mol. Cell. Biol. 22:5076-5088.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5076-5088
    • Huang, D.1    Moffat, J.2    Andrews, B.3
  • 127
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang, C-Y., and J. E. Ferrell, Jr. 1996. Ultrasensitivity in the mitogen-activated protein kinase cascade. Proc. Natl. Acad. Sci. USA 93:10078-10083.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10078-10083
    • Huang, C.-Y.1    Ferrell Jr., J.E.2
  • 128
    • 0027999205 scopus 로고
    • Mutation of the gene encoding protein kinase C 1 stimulates mitotic recombination in Saccharomyces cerevisiae
    • Huang, K. N., and L. S. Symington. 1994. Mutation of the gene encoding protein kinase C 1 stimulates mitotic recombination in Saccharomyces cerevisiae. Mol. Cell. Biol. 14:6039-6045.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6039-6045
    • Huang, K.N.1    Symington, L.S.2
  • 130
    • 0029792380 scopus 로고    scopus 로고
    • Coordinated regulation of gene expression by the cell cycle transcription factor SWI4 and the protein kinase C MAP kinase pathway for yeast cell integrity
    • Igual, J. C., A. L. Johnson, and L. H. Johnston. 1996. Coordinated regulation of gene expression by the cell cycle transcription factor SWI4 and the protein kinase C MAP kinase pathway for yeast cell integrity. EMBO J. 15: 5001-5013.
    • (1996) EMBO J. , vol.15 , pp. 5001-5013
    • Igual, J.C.1    Johnson, A.L.2    Johnston, L.H.3
  • 132
    • 0030044425 scopus 로고    scopus 로고
    • Genetic analysis of the Saccharomyces cerevisiae RHO3 gene, encoding a Rho-type small GTPase, provides evidence for a role in bud formation
    • Imai, J., A. Toh-e, and Y. Matsui. 1996. Genetic analysis of the Saccharomyces cerevisiae RHO3 gene, encoding a Rho-type small GTPase, provides evidence for a role in bud formation. Genetics 142:359-369.
    • (1996) Genetics , vol.142 , pp. 359-369
    • Imai, J.1    Toh-e, A.2    Matsui, Y.3
  • 133
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura, H., K. Tanaka, T. Hihara, M. Umikawa, T. Kamei, K. Takahashi, T. Sasaki, and Y. Takai. 1997. Bni1p and Bnr1p: downstream targets of the rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16:2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Kamei, T.5    Takahashi, K.6    Sasaki, T.7    Takai, Y.8
  • 135
    • 0033621467 scopus 로고    scopus 로고
    • Prenylation of Rho1p is required for activation of yeast 1,3-beta-glucan synthase
    • Inoue, S. B., H. Qadota, M. Arisawa, T. Watanabe, and Y. Ohya. 1999. Prenylation of Rho1p is required for activation of yeast 1,3-beta-glucan synthase. J. Biol. Chem. 274:38119-38124.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38119-38124
    • Inoue, S.B.1    Qadota, H.2    Arisawa, M.3    Watanabe, T.4    Ohya, Y.5
  • 137
    • 0027192944 scopus 로고
    • MKK1 and MKK2, which encode Saccharomyces cerevisiae mitogen-activated protein kinase kinase homologs, function in the pathway mediated by protein kinase C
    • Irie, K., M. Takase, K. S. Lee, D. E. Levin, H. Araki, K. Matsumoto, and Y. Oshima. 1993. MKK1 and MKK2, which encode Saccharomyces cerevisiae mitogen-activated protein kinase kinase homologs, function in the pathway mediated by protein kinase C. Mol. Cell. Biol. 13:3076-3083.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3076-3083
    • Irie, K.1    Takase, M.2    Lee, K.S.3    Levin, D.E.4    Araki, H.5    Matsumoto, K.6    Oshima, Y.7
  • 139
    • 0031900935 scopus 로고    scopus 로고
    • A screen for upstream components of the yeast protein kinase C signal transduction pathway identifies the product of the SLG1 gene
    • Jacoby, J. J., S. M. Nilius, and J. J. Heinisch. 1998. A screen for upstream components of the yeast protein kinase C signal transduction pathway identifies the product of the SLG1 gene. Mol. Gen. Genet. 258:148-155.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 148-155
    • Jacoby, J.J.1    Nilius, S.M.2    Heinisch, J.J.3
  • 140
    • 0030728256 scopus 로고    scopus 로고
    • Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C
    • Jacoby, J. J., H. P. Schmitz, and J. J. Heinisch. 1997. Mutants affected in the putative diacylglycerol binding site of yeast protein kinase C. FEBS Lett. 417:219-222.
    • (1997) FEBS Lett. , vol.417 , pp. 219-222
    • Jacoby, J.J.1    Schmitz, H.P.2    Heinisch, J.J.3
  • 141
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential rho-type GTPase controlling eukaryotic cell polarity
    • Johnson, D. I. 1999. Cdc42: an essential rho-type GTPase controlling eukaryotic cell polarity. Microbiol. Mol. Biol. Rev. 63:54-105.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 142
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D. I., and J. Pringle. 1990. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 111:143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.I.1    Pringle, J.2
  • 143
    • 0036440853 scopus 로고    scopus 로고
    • Regulation of the yeast Rlm1 transcription factor by the Mpk1 cell wall integrity MAP kinase
    • Jung, U. S., A. K. Sobering, M. J. Romeo, and D. E. Levin. 2002. Regulation of the yeast Rlm1 transcription factor by the Mpk1 cell wall integrity MAP kinase. Mol. Microbiol. 46:781-789.
    • (2002) Mol. Microbiol. , vol.46 , pp. 781-789
    • Jung, U.S.1    Sobering, A.K.2    Romeo, M.J.3    Levin, D.E.4
  • 144
    • 0033452784 scopus 로고    scopus 로고
    • Genome-wide analysis of gene expression regulated by the yeast cell wall integrity signalling pathway
    • Jung, U. S., and D. E. Levin. 1999. Genome-wide analysis of gene expression regulated by the yeast cell wall integrity signalling pathway. Mol. Microbiol. 34:1049-1057.
    • (1999) Mol. Microbiol. , vol.34 , pp. 1049-1057
    • Jung, U.S.1    Levin, D.E.2
  • 145
    • 0030609126 scopus 로고    scopus 로고
    • SRO9, a multicopy suppressor of the bud growth defect in the Saccharomyces cerevisiae rho3-deficient cells, shows strong genetic interactions with tropomyosin genes, suggesting its role in organization of the actin cytoskeleton
    • Kagami, M., A. Toh-e, and Y. Matsui. 1997. SRO9, a multicopy suppressor of the bud growth defect in the Saccharomyces cerevisiae rho3-deficient cells, shows strong genetic interactions with tropomyosin genes, suggesting its role in organization of the actin cytoskeleton. Genetics 147:1003-1016.
    • (1997) Genetics , vol.147 , pp. 1003-1016
    • Kagami, M.1    Toh-e, A.2    Matsui, Y.3
  • 146
    • 0024320079 scopus 로고
    • Molecular genetic analysis of the regulatory and catalytic domains of protein kinase C
    • Kaibuchi, K., Y. Fukumoto, N. Oku, Y. Takai, K. Arai, and M. Muramatsu. 1989. Molecular genetic analysis of the regulatory and catalytic domains of protein kinase C. J. Biol. Chem. 264:13489-13496.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13489-13496
    • Kaibuchi, K.1    Fukumoto, Y.2    Oku, N.3    Takai, Y.4    Arai, K.5    Muramatsu, M.6
  • 148
    • 11944273348 scopus 로고
    • The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response
    • Kamada, Y., U. S. Jung, J. Piotrowski, and D. E. Levin. 1995. The protein kinase C-activated MAP kinase pathway of Saccharomyces cerevisiae mediates a novel aspect of the heat shock response. Genes Dev. 9:1559-1571.
    • (1995) Genes Dev. , vol.9 , pp. 1559-1571
    • Kamada, Y.1    Jung, U.S.2    Piotrowski, J.3    Levin, D.E.4
  • 150
    • 0033529578 scopus 로고    scopus 로고
    • Molecular identification of a eukaryotic, stretch-activated nonselective cation channel
    • Kanzaki, M., M. Nagasawa, I. Kojima, C. Sato, K. Naruse, M. Sokabe, and H. Iida. 1999. Molecular identification of a eukaryotic, stretch-activated nonselective cation channel. Science 285:882-886.
    • (1999) Science , vol.285 , pp. 882-886
    • Kanzaki, M.1    Nagasawa, M.2    Kojima, I.3    Sato, C.4    Naruse, K.5    Sokabe, M.6    Iida, H.7
  • 152
    • 0033038844 scopus 로고    scopus 로고
    • The contribution of the O-glycosylated protein Pir2/ Hsp150 to the construction of the yeast cell wall in wild type cells and β1,6-glucan- deficient mutants
    • Kapteyn, J. C., P. van Egmond, E. Sievi, H. van den Ende, M. Makarow, and F. M. Klis. 1999. The contribution of the O-glycosylated protein Pir2/ Hsp150 to the construction of the yeast cell wall in wild type cells and β1,6-glucan-deficient mutants. Mol. Microbiol. 31:1835-1844.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1835-1844
    • Kapteyn, J.C.1    Van Egmond, P.2    Sievi, E.3    Van Den Ende, H.4    Makarow, M.5    Klis, F.M.6
  • 153
    • 0038294237 scopus 로고    scopus 로고
    • Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties
    • Kelleher, D., D. Karaoglu, E. Mandon, and R. Gilmore. 2003. Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties. Mol. Cell 12:101-111.
    • (2003) Mol. Cell , vol.12 , pp. 101-111
    • Kelleher, D.1    Karaoglu, D.2    Mandon, E.3    Gilmore, R.4
  • 155
    • 0031660370 scopus 로고    scopus 로고
    • Yeast Skn7p activity is modulated by the Sln1p-Ypd1p osmosensor and contributes to regulation of the HOG pathway
    • Ketela, T., J. L. Brown, R. C. Stewart, and H. Bussey. 1998. Yeast Skn7p activity is modulated by the Sln1p-Ypd1p osmosensor and contributes to regulation of the HOG pathway. Mol. Gen. Genet. 259:372-378.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 372-378
    • Ketela, T.1    Brown, J.L.2    Stewart, R.C.3    Bussey, H.4
  • 156
    • 0033000927 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Mid2p is a potential cell wall stress sensor and upstream activator of the PKC1-MPK1 cell integrity pathway
    • Ketela, T., R. Green, and H. Bussey. 1999. Saccharomyces cerevisiae Mid2p is a potential cell wall stress sensor and upstream activator of the PKC1-MPK1 cell integrity pathway. J. Bacteriol. 181:3330-3340.
    • (1999) J. Bacteriol. , vol.181 , pp. 3330-3340
    • Ketela, T.1    Green, R.2    Bussey, H.3
  • 157
    • 0033869314 scopus 로고    scopus 로고
    • Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes
    • Khalfan, W., I. Ivanovska, and M. D. Rose. 2000. Functional interaction between the PKC1 pathway and CDC31 network of SPB duplication genes. Genetics 155:1543-1559.
    • (2000) Genetics , vol.155 , pp. 1543-1559
    • Khalfan, W.1    Ivanovska, I.2    Rose, M.D.3
  • 159
    • 0027981822 scopus 로고
    • Review: Cell wall assembly in yeast
    • Klis, F. M. 1994. Review: cell wall assembly in yeast. Yeast 10:851-869.
    • (1994) Yeast , vol.10 , pp. 851-869
    • Klis, F.M.1
  • 160
    • 0036024578 scopus 로고    scopus 로고
    • Dynamics of cell wall structure in Saccharomyces cerevisiae
    • Klis, F. M., P. Mol, K. Hellingwerf, and S. Brul. 2002. Dynamics of cell wall structure in Saccharomyces cerevisiae. FEMS Microbiol. Rev. 26:239-256.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 239-256
    • Klis, F.M.1    Mol, P.2    Hellingwerf, K.3    Brul, S.4
  • 162
    • 0030799904 scopus 로고    scopus 로고
    • Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae
    • Koch, G., K. Tanaka, T. Masuda, W. Yamochi, H. Nonaka, Y. Takai. 1997. Association of the Rho family small GTP-binding proteins with Rho GDP dissociation inhibitor (Rho GDI) in Saccharomyces cerevisiae. Oncogene 15: 417-422.
    • (1997) Oncogene , vol.15 , pp. 417-422
    • Koch, G.1    Tanaka, K.2    Masuda, T.3    Yamochi, W.4    Nonaka, H.5    Takai, Y.6
  • 165
    • 0026681302 scopus 로고
    • The influence of congo red on the cell wall and 1,3-β-D-glucan microfibril biogenesis in Saccharomyces cerevisiae
    • Kopecka, M., and M. Gabriel. 1992. The influence of congo red on the cell wall and 1,3-β-D-glucan microfibril biogenesis in Saccharomyces cerevisiae. Arch. Microbiol. 158:115-126.
    • (1992) Arch. Microbiol. , vol.158 , pp. 115-126
    • Kopecka, M.1    Gabriel, M.2
  • 166
    • 0037006802 scopus 로고    scopus 로고
    • The protein kinase C pathway is required for viability in quiescence in Saccharomyces cerevisiae
    • Krause, S. A., and J. V. Gray. 2002. The protein kinase C pathway is required for viability in quiescence in Saccharomyces cerevisiae. Curr. Biol.
    • (2002) Curr. Biol. , vol.12 , pp. 588-593
    • Krause, S.A.1    Gray, J.V.2
  • 167
    • 0029922049 scopus 로고    scopus 로고
    • The response regulator-like protein Pos9/Skn7 of Saccharomyces cerevisiae is involved in oxidative stress resistance
    • Krems, B., C. Charizanis, and K-D. Entian. 1996. The response regulator-like protein Pos9/Skn7 of Saccharomyces cerevisiae is involved in oxidative stress resistance. Curr. Genet. 29:327-334.
    • (1996) Curr. Genet. , vol.29 , pp. 327-334
    • Krems, B.1    Charizanis, C.2    Entian, K.-D.3
  • 170
    • 0036226050 scopus 로고    scopus 로고
    • Involvement of GFA1, which encodes glutamine-fructose-6-phosphate amidotransferase, in the activation of chitin synthesis pathway in response to cell-wall defects in Saccharomyces cerevisiae
    • Lagorce, A., V. le Berre-Anton, B. Aguilar-Uscanga, H. Martin-Yken, A. Dagkessamanskaia, and J. Francois. 2002. Involvement of GFA1, which encodes glutamine-fructose-6-phosphate amidotransferase, in the activation of chitin synthesis pathway in response to cell-wall defects in Saccharomyces cerevisiae. Eur. J. Biochem. 269:1697-1707.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1697-1707
    • Lagorce, A.1    Le Berre-Anton, V.2    Aguilar-Uscanga, B.3    Martin-Yken, H.4    Dagkessamanskaia, A.5    Francois, J.6
  • 171
  • 172
    • 0027219432 scopus 로고
    • A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway
    • Lee, K. S., L. K. Hines, and D. E. Levin. 1993. A pair of functionally redundant yeast genes (PPZ1 and PPZ2) encoding type 1-related protein phosphatases function within the PKC1-mediated pathway. Mol. Cell. Biol. 13:5843-5853.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5843-5853
    • Lee, K.S.1    Hines, L.K.2    Levin, D.E.3
  • 174
    • 0026584373 scopus 로고
    • Dominant mutations in a gene encoding a putative protein kinase (BCK1) bypass the requirement for a Saccharomyces cerevisiae protein kinase C homolog
    • Lee, K. S., and D. E. Levin. 1992. Dominant mutations in a gene encoding a putative protein kinase (BCK1) bypass the requirement for a Saccharomyces cerevisiae protein kinase C homolog. Mol. Cell. Biol. 12:172-182.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 172-182
    • Lee, K.S.1    Levin, D.E.2
  • 175
    • 0028605709 scopus 로고
    • Protein kinase C zeta is associated with the mitotic apparatus in primary cell cultures of the shark rectal gland
    • Lehrich, R. W., and J. N. Forrest, Jr. 1994. Protein kinase C zeta is associated with the mitotic apparatus in primary cell cultures of the shark rectal gland. J. Biol. Chem. 269:32446-32450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32446-32450
    • Lehrich, R.W.1    Forrest Jr., J.N.2
  • 176
    • 0032031556 scopus 로고    scopus 로고
    • Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei
    • Lendenfeld, T., and C. P. Kubicek. 1998. Characterization and properties of protein kinase C from the filamentous fungus Trichoderma reesei. Biochem. J. 330:689-694.
    • (1998) Biochem. J. , vol.330 , pp. 689-694
    • Lendenfeld, T.1    Kubicek, C.P.2
  • 177
    • 0026511056 scopus 로고
    • Mutants in the S. cerevisiae PKC1 gene display a cell cycle-specific osmotic stability defect
    • Levin, D. E., and E. Bartlett-Heubusch. 1992. Mutants in the S. cerevisiae PKC1 gene display a cell cycle-specific osmotic stability defect. J. Cell Biol. 116:1221-1229.
    • (1992) J. Cell Biol. , vol.116 , pp. 1221-1229
    • Levin, D.E.1    Bartlett-Heubusch, E.2
  • 178
    • 0028154801 scopus 로고
    • Dissecting the protein kinase C/MAP kinase signalling pathway of Saccharomyces cerevisiae
    • Levin, D. E., B. Bowers, C. Y. Chen, Y. Kamada, and M. Watanabe. 1994. Dissecting the protein kinase C/MAP kinase signalling pathway of Saccharomyces cerevisiae. Cell. Mol. Biol. Res. 40:229-239.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 229-239
    • Levin, D.E.1    Bowers, B.2    Chen, C.Y.3    Kamada, Y.4    Watanabe, M.5
  • 179
    • 0028920365 scopus 로고
    • The proliferation of MAP kinase signaling pathways in yeast
    • Levin, D. E., and Errede. 1995. The proliferation of MAP kinase signaling pathways in yeast. Curr. Biol. 7:197-202.
    • (1995) Curr. Biol. , vol.7 , pp. 197-202
    • Levin, D.E.1    Errede2
  • 180
    • 0025300349 scopus 로고
    • A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle
    • Levin, D. E., F. O. Fields, R. Kunisawa, J. M. Bishop, and J. Thorner. 1990. A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle. Cell 62:213-224.
    • (1990) Cell , vol.62 , pp. 213-224
    • Levin, D.E.1    Fields, F.O.2    Kunisawa, R.3    Bishop, J.M.4    Thorner, J.5
  • 181
    • 0344309014 scopus 로고    scopus 로고
    • The morphogenesis checkpoint: How yeast cells watch their figures
    • Lew, D. J. 2003. The morphogenesis checkpoint: how yeast cells watch their figures. Curr. Opin. Cell Biol. 15:648-653.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 648-653
    • Lew, D.J.1
  • 182
    • 0028915943 scopus 로고
    • A cell cycle checkpoint monitors cell morphogenesis in budding yeast
    • Lew, D. J., and S. I. Reed. 1995. A cell cycle checkpoint monitors cell morphogenesis in budding yeast. J. Cell Biol. 129:739-749.
    • (1995) J. Cell Biol. , vol.129 , pp. 739-749
    • Lew, D.J.1    Reed, S.I.2
  • 183
    • 0032401739 scopus 로고    scopus 로고
    • The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p
    • Li, S., A. Ault, C. L. Malone, D. Raitt, S. Dean, L. H. Johnston, R. J. Besehenes, and J. S. Fassler. 1998. The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p. EMBO J. 17:6952-6962.
    • (1998) EMBO J. , vol.17 , pp. 6952-6962
    • Li, S.1    Ault, A.2    Malone, C.L.3    Raitt, D.4    Dean, S.5    Johnston, L.H.6    Besehenes, R.J.7    Fassler, J.S.8
  • 184
    • 0036179410 scopus 로고    scopus 로고
    • The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p
    • Li, S., S. Dean, Z. Li, J. Horecka, R. J. Deschenes, and J. J. Fassler. 2002. The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p. Mol. Biol. Cell 13:412-424.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 412-424
    • Li, S.1    Dean, S.2    Li, Z.3    Horecka, J.4    Deschenes, R.J.5    Fassler, J.J.6
  • 185
    • 0034064974 scopus 로고    scopus 로고
    • Repression of ribosome and tRNA synthesis in secretion-defective cells is signaled by a novel branch of the cell integrity pathway
    • Li, Y., R. Moir, I. Sethy-Coraci, J. Warner, and I. Willis. 2000. Repression of ribosome and tRNA synthesis in secretion-defective cells is signaled by a novel branch of the cell integrity pathway. Mol. Cell. Biol. 20:3843-3851.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3843-3851
    • Li, Y.1    Moir, R.2    Sethy-Coraci, I.3    Warner, J.4    Willis, I.5
  • 186
    • 0026574205 scopus 로고
    • Sexual agglutination in budding yeasts: Structure, function, and regulation of adhesion glycoproteins
    • Lipke, P. N., and J. Kurjan. 1992. Sexual agglutination in budding yeasts: structure, function, and regulation of adhesion glycoproteins. Microbiol. Rev. 56:180-194.
    • (1992) Microbiol. Rev. , vol.56 , pp. 180-194
    • Lipke, P.N.1    Kurjan, J.2
  • 187
    • 0027245483 scopus 로고
    • FK506 and cyclosporine, molecular probes for studying intracellular signal transduction
    • Liu, J. 1993. FK506 and cyclosporine, molecular probes for studying intracellular signal transduction. Immunol. Today 14:290-295.
    • (1993) Immunol. Today , vol.14 , pp. 290-295
    • Liu, J.1
  • 189
    • 0344721493 scopus 로고    scopus 로고
    • Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae
    • Lodder, A. L., T. K. Lee, and R. Ballester. 1999. Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae. Genetics 152:1487-1499.
    • (1999) Genetics , vol.152 , pp. 1487-1499
    • Lodder, A.L.1    Lee, T.K.2    Ballester, R.3
  • 191
    • 0346993670 scopus 로고    scopus 로고
    • Aberrant processing of the WSC family and Mid2p cell surface sensors results in death of Saccharomyces cerevisiae O-mannosylation mutants
    • Lommel, M., M. Bagnat, and S. Strahl. 2004. Aberrant processing of the WSC family and Mid2p cell surface sensors results in death of Saccharomyces cerevisiae O-mannosylation mutants. Mol. Cell. Biol. 24:46-57.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 46-57
    • Lommel, M.1    Bagnat, M.2    Strahl, S.3
  • 192
    • 0346433720 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p
    • Lu, J. M. H., R. J. Deschenes, and J. S. Fassler. 2003. Saccharomyces cerevisiae histidine phosphotransferase Ypd1p shuttles between the nucleus and cytoplasm for SLN1-dependent phosphorylation of Ssk1p and Skn7p. Eukaryot. Cell 2:1304-1314.
    • (2003) Eukaryot. Cell , vol.2 , pp. 1304-1314
    • Lu, J.M.H.1    Deschenes, R.J.2    Fassler, J.S.3
  • 194
    • 0028947362 scopus 로고
    • Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress
    • Luyten, K., J. Albertyn, W. F. Skibbe, B. A. Prior, J. Ramos, J. M. Thevelein, and S. Hohmann. 1995. Fps1, a yeast member of the MIP family of channel proteins, is a facilitator for glycerol uptake and efflux and is inactive under osmotic stress. EMBO J. 14:1360-1371.
    • (1995) EMBO J. , vol.14 , pp. 1360-1371
    • Luyten, K.1    Albertyn, J.2    Skibbe, W.F.3    Prior, B.A.4    Ramos, J.5    Thevelein, J.M.6    Hohmann, S.7
  • 195
    • 0023293818 scopus 로고
    • Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae
    • Madaule, P., R. Axel, and A. M. Myers. 1987. Characterization of two members of the rho gene family from the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 84:779-783.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 779-783
    • Madaule, P.1    Axel, R.2    Myers, A.M.3
  • 196
    • 0031004235 scopus 로고    scopus 로고
    • SBF cell cycle regulator as a target of the yeast PKC-MAP kinase pathway
    • Madden, K., Y. J. Sheu, K. Baetz, B. Andrews, and M. Snyder. 1997. SBF cell cycle regulator as a target of the yeast PKC-MAP kinase pathway. Science 275:1781-1784.
    • (1997) Science , vol.275 , pp. 1781-1784
    • Madden, K.1    Sheu, Y.J.2    Baetz, K.3    Andrews, B.4    Snyder, M.5
  • 197
    • 0031782969 scopus 로고    scopus 로고
    • Cell polarity and morphogenesis in budding yeast
    • Madden, K., and M. Snyder. 1998. Cell polarity and morphogenesis in budding yeast. Annu. Rev. Microbiol. 52:687-744.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 687-744
    • Madden, K.1    Snyder, M.2
  • 198
  • 199
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • Maeda, T., S. M. Wurgler-Murphy, and H. Saito. 1994. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369:242-245.
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 200
    • 0033594117 scopus 로고    scopus 로고
    • Differential regulation of Kar3p kinesin-related protein by two associated proteins, Cik1 and Vik1
    • Manning, B. D., J. G. Barrett, J. A. Wallace, H. Granok, and M. Snyder. 1999. Differential regulation of Kar3p kinesin-related protein by two associated proteins, Cik1 and Vik1. J. Cell Biol. 144:1219-1233.
    • (1999) J. Cell Biol. , vol.144 , pp. 1219-1233
    • Manning, B.D.1    Barrett, J.G.2    Wallace, J.A.3    Granok, H.4    Snyder, M.5
  • 201
    • 0030868676 scopus 로고    scopus 로고
    • The rho-GEF Rom2p localizes to sites of polarized cell growth and participates in cytoskeletal functions in Saccharomyces cerevisiae
    • Manning, B. D., R. Padmanabha, and M. Snyder. 1997. The rho-GEF Rom2p localizes to sites of polarized cell growth and participates in cytoskeletal functions in Saccharomyces cerevisiae. Mol. Biol. Cell 8:1829-1844.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1829-1844
    • Manning, B.D.1    Padmanabha, R.2    Snyder, M.3
  • 202
    • 0036153176 scopus 로고    scopus 로고
    • Casein kinase I controls a late step in the endocytic trafficking of yeast uracil permease
    • Marchal, C., S. Dupre, and D. Urban-Grimal. 2002. Casein kinase I controls a late step in the endocytic trafficking of yeast uracil permease. J. Cell Sci. 115:217-226.
    • (2002) J. Cell Sci. , vol.115 , pp. 217-226
    • Marchal, C.1    Dupre, S.2    Urban-Grimal, D.3
  • 203
    • 0031871868 scopus 로고    scopus 로고
    • Overexpression of M1D2 suppresses the profilin-deficient phenotype of yeast cells
    • Marcoux, N., Y. Bourbonnais, P-M. Charest, and D. Pallotta. 1998. Overexpression of M1D2 suppresses the profilin-deficient phenotype of yeast cells. Mol. Microbiol. 29:515-526.
    • (1998) Mol. Microbiol. , vol.29 , pp. 515-526
    • Marcoux, N.1    Bourbonnais, Y.2    Charest, P.-M.3    Pallotta, D.4
  • 204
    • 0027433380 scopus 로고
    • Activity of the yeast MAP kinase homologue Slt2 is critically required for cell integrity at 37 degrees C
    • Martin, H., J. Arroyo, M. Sanchez, M. Molina, and C. Nombela. 1993. Activity of the yeast MAP kinase homologue Slt2 is critically required for cell integrity at 37 degrees C. Mol. Gen. Genet. 241:177-184.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 177-184
    • Martin, H.1    Arroyo, J.2    Sanchez, M.3    Molina, M.4    Nombela, C.5
  • 205
    • 0343415650 scopus 로고    scopus 로고
    • Regulatory mechanisms for modulation of signaling through the cell integrity Slt2-mediated pathway in Saccharomyces cerevisiae
    • Martin, H., J. M. Rodriguez-Pachon, C. Ruiz, C. Nombela, and M. Molina. 2000. Regulatory mechanisms for modulation of signaling through the cell integrity Slt2-mediated pathway in Saccharomyces cerevisiae. J. Biol. Chem. 275:1511-1519.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1511-1519
    • Martin, H.1    Rodriguez-Pachon, J.M.2    Ruiz, C.3    Nombela, C.4    Molina, M.5
  • 206
    • 0027992663 scopus 로고
    • Molecular cloning and characterization of yeast rho GDP dissociation inhibitor
    • Masuda, T., K. Tanaka, H. Nonaka, W. Yamochi, A. Maeda, and Y. Takai. 1994. Molecular cloning and characterization of yeast rho GDP dissociation inhibitor. J. Biol. Chem. 269:19713-19718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19713-19718
    • Masuda, T.1    Tanaka, K.2    Nonaka, H.3    Yamochi, W.4    Maeda, A.5    Takai, Y.6
  • 207
    • 0031451194 scopus 로고    scopus 로고
    • Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae
    • Matheos, D. P., T. J. Kingsbury, U. S. Ahsan, and K. W. Cunningham. 1997. Tcn1p/Crz1p, a calcineurin-dependent transcription factor that differentially regulates gene expression in Saccharomyces cerevisiae. Genes Dev. 11:3445-3458.
    • (1997) Genes Dev. , vol.11 , pp. 3445-3458
    • Matheos, D.P.1    Kingsbury, T.J.2    Ahsan, U.S.3    Cunningham, K.W.4
  • 208
    • 0026484397 scopus 로고
    • Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and BEM1
    • Matsui, Y., and A. Toh-e. 1992. Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and BEM1. Mol. Cell. Biol. 12:5690-5699.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5690-5699
    • Matsui, Y.1    Toh-e, A.2
  • 209
    • 0032718779 scopus 로고    scopus 로고
    • Differential regulation of the cell wall integrity mitogen-activated protein kinase pathway in budding yeast by the protein tyrosine phosphatases Ptp2 and Ptp3
    • Mattison, C. P., S. S. Spencer, K. A. Kresge, J. Lee, and I. M. Ota. 1999. Differential regulation of the cell wall integrity mitogen-activated protein kinase pathway in budding yeast by the protein tyrosine phosphatases Ptp2 and Ptp3. Mol. Cell. Biol. 19:7651-7660.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7651-7660
    • Mattison, C.P.1    Spencer, S.S.2    Kresge, K.A.3    Lee, J.4    Ota, I.M.5
  • 210
    • 15844412765 scopus 로고    scopus 로고
    • In vitro activity of 1,3-β-D-glucan synthase requires the GTP-binding protein Rho1
    • Mazur, P., and W. Baginsky. 1996. In vitro activity of 1,3-β-D-glucan synthase requires the GTP-binding protein Rho1. J. Biol. Chem. 271:14604-14609.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14604-14609
    • Mazur, P.1    Baginsky, W.2
  • 211
  • 212
    • 0027761005 scopus 로고
    • The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae
    • Mazzoni, C., P. Zarov, A. Rambourg, and C. Mann. 1993. The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae. J. Cell Biol. 123:1821-1833.
    • (1993) J. Cell Biol. , vol.123 , pp. 1821-1833
    • Mazzoni, C.1    Zarov, P.2    Rambourg, A.3    Mann, C.4
  • 213
    • 0032874877 scopus 로고    scopus 로고
    • The morphogenesis checkpoint in Saccharomyces cerevisiae: Cell cycle control of Swe1p degradation by Hsl1p and Hsl7p
    • McMillan, J. N., M. S. Longtine, R. A. Sia, C. L. Theesfeld, E. S. Bardes, J. R. Pringle, and D. J. Lew. 1999. The morphogenesis checkpoint in Saccharomyces cerevisiae: cell cycle control of Swe1p degradation by Hsl1p and Hsl7p. Mol. Cell. Biol. 19:6929-6939.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6929-6939
    • McMillan, J.N.1    Longtine, M.S.2    Sia, R.A.3    Theesfeld, C.L.4    Bardes, E.S.5    Pringle, J.R.6    Lew, D.J.7
  • 214
    • 0028589197 scopus 로고
    • The PCL2(ORFD)-PHO85 cyclin-dependent kinase complex: A cell cycle regulator in yeast
    • Measday, V., L. Moore, J. Ogas, M. Tyers, and B. Andrews. 1994. The PCL2(ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle regulator in yeast. Science 266:1391-1395.
    • (1994) Science , vol.266 , pp. 1391-1395
    • Measday, V.1    Moore, L.2    Ogas, J.3    Tyers, M.4    Andrews, B.5
  • 215
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor, H., and P. J. Parker. 1998. The extended protein kinase C superfamily. Biochem. J. 332:281-292.
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 216
    • 0028286249 scopus 로고
    • The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae
    • Mendoza, I., F. Rubio, A. Rodriguez-Navarro, and J. M. Pardo. 1994. The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae. J. Biol. Chem. 269:8792-8796.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8792-8796
    • Mendoza, I.1    Rubio, F.2    Rodriguez-Navarro, A.3    Pardo, J.M.4
  • 217
    • 1242277786 scopus 로고    scopus 로고
    • Response of the Saccharomyces cerevisiae Mpk1 mitogen-activated protein kinase pathway to increases in internal turgor pressure caused by loss of Ppz protein phosphatases
    • Merchan, S. D. Bernal, R. Serrano, and L. Yenush. 2004. Response of the Saccharomyces cerevisiae Mpk1 mitogen-activated protein kinase pathway to increases in internal turgor pressure caused by loss of Ppz protein phosphatases. Eukaryot. Cell 3:100-107.
    • (2004) Eukaryot. Cell , vol.3 , pp. 100-107
    • Merchan1    Bernal, S.D.2    Serrano, R.3    Yenush, L.4
  • 218
    • 0028215997 scopus 로고
    • Continued functioning of the secretory pathway is essential for ribosome synthesis
    • Mizuta, K., and J. R. Warner. 1994. Continued functioning of the secretory pathway is essential for ribosome synthesis. Mol. Cell. Biol. 14:2493-2502.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2493-2502
    • Mizuta, K.1    Warner, J.R.2
  • 219
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen, D. 1995. Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 268:247-251.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 220
    • 1342310741 scopus 로고    scopus 로고
    • Late-G1 cyclin-CDK activity is essential for control of cell morphogenesis in budding yeast
    • Moffat, J., and B. Andrews. 2004. Late-G1 cyclin-CDK activity is essential for control of cell morphogenesis in budding yeast. Nat. Cell Biol. 6:59-66.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 59-66
    • Moffat, J.1    Andrews, B.2
  • 222
    • 0031048280 scopus 로고    scopus 로고
    • The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae
    • Morgan, B. A., G. R. Banks, W. M. Toone, D. Raitt, S. Kuge, and L. H. Johnston. 1997. The Skn7 response regulator controls gene expression in the oxidative stress response of the budding yeast Saccharomyces cerevisiae. EMBO J. 16:1035-1044.
    • (1997) EMBO J. , vol.16 , pp. 1035-1044
    • Morgan, B.A.1    Banks, G.R.2    Toone, W.M.3    Raitt, D.4    Kuge, S.5    Johnston, L.H.6
  • 223
    • 0028805253 scopus 로고
    • A yeast transcription factor bypassing the requirement for SBF and DSC1/MBF in budding yeast has homology to bacterial signal transduction proteins
    • Morgan, B. A., N. Bouquin, G. F. Merrill, and L. H. Johnston. 1995. A yeast transcription factor bypassing the requirement for SBF and DSC1/MBF in budding yeast has homology to bacterial signal transduction proteins. EMBO J. 14:5679-5689.
    • (1995) EMBO J. , vol.14 , pp. 5679-5689
    • Morgan, B.A.1    Bouquin, N.2    Merrill, G.F.3    Johnston, L.H.4
  • 224
    • 1242274644 scopus 로고    scopus 로고
    • Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I
    • Moriya, H., and M. Johnston. 2004. Glucose sensing and signaling in Saccharomyces cerevisiae through the Rgt2 glucose sensor and casein kinase I. Proc. Natl. Acad. Sci. USA 101:1572-1577.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1572-1577
    • Moriya, H.1    Johnston, M.2
  • 225
    • 0033775855 scopus 로고    scopus 로고
    • Latrunculin alters the actin-monomer subunit interface to prevent polymerization
    • Morton, W. M., K. R. Ayscough, and P. J. McLaughlin. 2000. Latrunculin alters the actin-monomer subunit interface to prevent polymerization. Nat. Cell Biol. 2:376-378.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 376-378
    • Morton, W.M.1    Ayscough, K.R.2    McLaughlin, P.J.3
  • 227
    • 0035695061 scopus 로고    scopus 로고
    • 2+ influx systems by pheromone signaling in Saccharomyces cerevisiae
    • 2+ influx systems by pheromone signaling in Saccharomyces cerevisiae. Genetics 159:1527-1538.
    • (2001) Genetics , vol.159 , pp. 1527-1538
    • Muller, E.M.1    Locke, E.G.2    Cunningham, K.W.3
  • 228
    • 0345621646 scopus 로고    scopus 로고
    • Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall
    • Mrsa, V., and W. Tanner. 1999. Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p (members of the Pir protein family) in stability of the Saccharomyces cerevisiae cell wall. Yeast 15:813-820.
    • (1999) Yeast , vol.15 , pp. 813-820
    • Mrsa, V.1    Tanner, W.2
  • 229
    • 0026625118 scopus 로고
    • Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae deficient in mannose outer chain elongation
    • Nagasu, T., Y. Shimma, Y. Nakanishi, J. Kuromitsu, K. Iwama, K. Nakayama, K. Suzuki, and Y. Jigami. 1992. Isolation of new temperature-sensitive mutants of Saccharomyces cerevisiae deficient in mannose outer chain elongation. Yeast 8:535-547.
    • (1992) Yeast , vol.8 , pp. 535-547
    • Nagasu, T.1    Shimma, Y.2    Nakanishi, Y.3    Kuromitsu, J.4    Iwama, K.5    Nakayama, K.6    Suzuki, K.7    Jigami, Y.8
  • 230
    • 0027385382 scopus 로고
    • Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions
    • Nakamura, T., Y. Liu, D. Hirata, H. Namba, S. Harada, T. Hirokawa, and T. Miyakawa. 1993. Protein phosphatase type 2B (calcineurin)-mediated, FK506-sensitive regulation of intracellular ions in yeast is an important determinant for adaptation to high salt stress conditions. EMBO J. 12: 4063-4071.
    • (1993) EMBO J. , vol.12 , pp. 4063-4071
    • Nakamura, T.1    Liu, Y.2    Hirata, D.3    Namba, H.4    Harada, S.5    Hirokawa, T.6    Miyakawa, T.7
  • 231
    • 0037175011 scopus 로고    scopus 로고
    • Protein kinase C isoforms are translocated to microtubules in neurons
    • Nakhost, A., N. Kabir, P. Forscher, and W. S. Sossin. 2002. Protein kinase C isoforms are translocated to microtubules in neurons. J. Biol. Chem. 277: 40633-40639.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40633-40639
    • Nakhost, A.1    Kabir, N.2    Forscher, P.3    Sossin, W.S.4
  • 232
    • 0034846391 scopus 로고    scopus 로고
    • The arrest of secretion response in yeast: Signaling from the secretory path to the nucleus via Wsc proteins and Pkc1p
    • Nanduri, J., and A. M. Tartakoff. 2001. The arrest of secretion response in yeast: signaling from the secretory path to the nucleus via Wsc proteins and Pkc1p. Mol. Cell 8:281-289.
    • (2001) Mol. Cell , vol.8 , pp. 281-289
    • Nanduri, J.1    Tartakoff, A.M.2
  • 233
    • 0033584859 scopus 로고    scopus 로고
    • An unexpected link between the secretory path and the organization of the nucleus
    • Nanduri, J., S. Mitra, C. Andrei, Y. Liu, Y. Yu, M. Hitomi, and A. Tartakoff. 1999. An unexpected link between the secretory path and the organization of the nucleus. J. Biol. Chem. 274:33785-33789.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33785-33789
    • Nanduri, J.1    Mitra, S.2    Andrei, C.3    Liu, Y.4    Yu, Y.5    Hitomi, M.6    Tartakoff, A.7
  • 234
    • 0031888386 scopus 로고    scopus 로고
    • A role for the MAP kinase gene MKC1 in cell wall construction and morphological transitions in Candida albicans
    • Navarro-Garcia, F., R. Alonso-Monge, H. Rico, J. Pla, R. Sentandreu, and C. Nombela. 1998. A role for the MAP kinase gene MKC1 in cell wall construction and morphological transitions in Candida albicans. Microbiology 144:411-424.
    • (1998) Microbiology , vol.144 , pp. 411-424
    • Navarro-Garcia, F.1    Alonso-Monge, R.2    Rico, H.3    Pla, J.4    Sentandreu, R.5    Nombela, C.6
  • 235
    • 0027051833 scopus 로고
    • On the mechanism by which a heat shock induces trehalose accumulation in Saccharomyces cerevisiae
    • Neves, M. J., and J. Francois. 1992. On the mechanism by which a heat shock induces trehalose accumulation in Saccharomyces cerevisiae. Biochem. J. 288:859-864.
    • (1992) Biochem. J. , vol.288 , pp. 859-864
    • Neves, M.J.1    Francois, J.2
  • 236
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton, A. C. 1995. Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270:28495-28498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 237
    • 0033532045 scopus 로고    scopus 로고
    • Protein kinase C enables the regulatory circuit that connects membrane synthesis to ribosome synthesis in Saccharomyces cerevisiae
    • Nierras, C. R., and J. R. Warner. 1999. Protein kinase C enables the regulatory circuit that connects membrane synthesis to ribosome synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 274:13235-13241.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13235-13241
    • Nierras, C.R.1    Warner, J.R.2
  • 238
    • 0030001665 scopus 로고    scopus 로고
    • Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy
    • Nomanbhoy, T. K., and R. A. Cerione. 1996. Characterization of the interaction between RhoGDI and Cdc42Hs using fluorescence spectroscopy. J. Biol. Chem. 271:10004-10009.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10004-10009
    • Nomanbhoy, T.K.1    Cerione, R.A.2
  • 240
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae
    • Nonaka, H., K. Tanaka, H. Hirano, T. Fujiwara, H. Kohno, M. Umikawa, A. Mino, and Y. Takai. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J. 14:5931-5938.
    • (1995) EMBO J. , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 241
    • 0026049598 scopus 로고
    • Transcriptional activation of CLN1, CLN2 and a putative new G1 cyclin (HCS26) by Swi4, a positive regulator of G1 specific transcription
    • Ogas, J., B. J. Andrews, and I. Herskowitz. 1991. Transcriptional activation of CLN1, CLN2 and a putative new G1 cyclin (HCS26) by Swi4, a positive regulator of G1 specific transcription. Cell 66:1015-1026.
    • (1991) Cell , vol.66 , pp. 1015-1026
    • Ogas, J.1    Andrews, B.J.2    Herskowitz, I.3
  • 242
    • 0028601345 scopus 로고
    • 2+-binding domain and shows mating pheromone-stimulated expression in Saccharomyces cerevisiae
    • 2+-binding domain and shows mating pheromone-stimulated expression in Saccharomyces cerevisiae. Gene 151:203-208.
    • (1994) Gene , vol.151 , pp. 203-208
    • Ono, T.1    Suzuki, T.2    Anraku, Y.3    Iida, H.4
  • 243
    • 0000912342 scopus 로고    scopus 로고
    • Biogenesis of yeast wall and surface components
    • J. R. Pringle et al. (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Orlean, P. 1997. Biogenesis of yeast wall and surface components, p. 229-362. In J. R. Pringle et al. (ed.), The molecular biology of the yeast Saccharomyces, vol. 3. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) The Molecular Biology of the Yeast Saccharomyces , vol.3 , pp. 229-362
    • Orlean, P.1
  • 244
    • 0032053318 scopus 로고    scopus 로고
    • The ultrastucture of yeast: Cell wall structure and formation
    • Osumi, M. 1998. The ultrastucture of yeast: Cell wall structure and formation. Micron 29:207-233.
    • (1998) Micron , vol.29 , pp. 207-233
    • Osumi, M.1
  • 245
    • 0027507956 scopus 로고
    • A yeast protein similar to bacterial two-component regulators
    • Ota, I. M., and A. Varshavsky. 1993. A yeast protein similar to bacterial two-component regulators. Science 262:566-569.
    • (1993) Science , vol.262 , pp. 566-569
    • Ota, I.M.1    Varshavsky, A.2
  • 246
    • 0029920783 scopus 로고    scopus 로고
    • Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Ozaki, K., K. Tanaka, H. Imamura, T. Hihara, T. Kameyama, H. Nonaka, H. Hirano, Y. Matsuura, and Y. Takai. 1996. Rom1p and Rom2p are GDP/GTP exchange proteins (GEPs) for the Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15:2196-2207.
    • (1996) EMBO J. , vol.15 , pp. 2196-2207
    • Ozaki, K.1    Tanaka, K.2    Imamura, H.3    Hihara, T.4    Kameyama, T.5    Nonaka, H.6    Hirano, H.7    Matsuura, Y.8    Takai, Y.9
  • 247
  • 248
    • 0028158129 scopus 로고
    • Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein
    • Page, B. D., L. L. Satterwhite, M. D. Rose, and M. Snyder. 1994. Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein. J. Cell Biol. 124:507-519.
    • (1994) J. Cell Biol. , vol.124 , pp. 507-519
    • Page, B.D.1    Satterwhite, L.L.2    Rose, M.D.3    Snyder, M.4
  • 250
    • 0029872224 scopus 로고    scopus 로고
    • Identification of ASK10 as a multicopy activator of Skn7p-dependent transcription of a HIS3 reporter gene
    • Page, N., J. Sheraton, J. L. Brown, R. C. Stewart, and H. Bussey. 1996. Identification of ASK10 as a multicopy activator of Skn7p-dependent transcription of a HIS3 reporter gene. Yeast 12:267-272.
    • (1996) Yeast , vol.12 , pp. 267-272
    • Page, N.1    Sheraton, J.2    Brown, J.L.3    Stewart, R.C.4    Bussey, H.5
  • 251
    • 0030803799 scopus 로고    scopus 로고
    • 2+ uptake and exacerbates the cdc1(Ts) growth defect
    • 2+ uptake and exacerbates the cdc1(Ts) growth defect. Mol. Cell. Biol. 17:6339-6347.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6339-6347
    • Paidhungat, M.1    Garrett, S.2
  • 252
    • 0034907213 scopus 로고    scopus 로고
    • mDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A. F., T. A. Cook, A. S. Alberts, and G. G. Gundersen. 2001. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3:723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 254
    • 0029832176 scopus 로고    scopus 로고
    • Protein-protein interactions in the yeast PKC1 pathway: Pkc1p interacts with a component of the MAP kinase cascade
    • Paravicini, G., and L. Friedli. 1996. Protein-protein interactions in the yeast PKC1 pathway: Pkc1p interacts with a component of the MAP kinase cascade. Mol. Gen. Genet. 251:682-691.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 682-691
    • Paravicini, G.1    Friedli, L.2
  • 255
    • 0033860694 scopus 로고    scopus 로고
    • Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase
    • Park, H., and W. J. Lennarz. 2000. Evidence for interaction of yeast protein kinase C with several subunits of oligosaccharyl transferase. Glycobiology 10:737-744.
    • (2000) Glycobiology , vol.10 , pp. 737-744
    • Park, H.1    Lennarz, W.J.2
  • 256
    • 0028148453 scopus 로고
    • Interactions between the bud emergence proteins Bem1p and Bem2p and rho-type GTPases in yeast
    • Peterson, J., Y. Zheng, L. Bender, A. Myers, R. Cerione, and A. Bender. 1994. Interactions between the bud emergence proteins Bem1p and Bem2p and rho-type GTPases in yeast. J. Cell Biol. 127:1395-1406.
    • (1994) J. Cell Biol. , vol.127 , pp. 1395-1406
    • Peterson, J.1    Zheng, Y.2    Bender, L.3    Myers, A.4    Cerione, R.5    Bender, A.6
  • 257
    • 0034749351 scopus 로고    scopus 로고
    • Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling that act through Rom2, a guanine nucleotide exchange factor for Rho1
    • Philip, B., and D. E. Levin. 2001. Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling that act through Rom2, a guanine nucleotide exchange factor for Rho1. Mol. Cell. Biol. 21:271-280.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 271-280
    • Philip, B.1    Levin, D.E.2
  • 258
    • 0033607014 scopus 로고    scopus 로고
    • A latrophilin/CL-1-like GPS domain in polycystin-1
    • Ponting, C. P., K. Hoffman, and P. Bork. 1999. A latrophilin/CL-1-like GPS domain in polycystin-1. Curr. Biol. 9:R585-R587.
    • (1999) Curr. Biol. , vol.9
    • Ponting, C.P.1    Hoffman, K.2    Bork, P.3
  • 259
    • 0031027101 scopus 로고    scopus 로고
    • Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1 mutant of Saccharomyces cerevisiae
    • Popolo, L., D. Gilardelli, P. Bonfante, and M. Vai. 1997. Increase in chitin as an essential response to defects in assembly of cell wall polymers in the ggp1 mutant of Saccharomyces cerevisiae. J. Bacteriol. 179:463-469.
    • (1997) J. Bacteriol. , vol.179 , pp. 463-469
    • Popolo, L.1    Gilardelli, D.2    Bonfante, P.3    Vai, M.4
  • 260
    • 0027339732 scopus 로고
    • The PPZ protein phosphatases are involved in the maintenance of osmotic stability of yeast cells
    • Posas, F., A. Casamayor, and J. Arino. 1993. The PPZ protein phosphatases are involved in the maintenance of osmotic stability of yeast cells. FEBS Lett. 318:282-286.
    • (1993) FEBS Lett. , vol.318 , pp. 282-286
    • Posas, F.1    Casamayor, A.2    Arino, J.3
  • 261
    • 0032035043 scopus 로고    scopus 로고
    • Signal transduction by MAP kinase cascades in budding yeast
    • Posas, F., M. Takekawa, and H. Saito. 1998. Signal transduction by MAP kinase cascades in budding yeast. Curr. Opin. Microbiol. 1:175-182.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 175-182
    • Posas, F.1    Takekawa, M.2    Saito, H.3
  • 262
    • 0030595378 scopus 로고    scopus 로고
    • Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor
    • Posas, F., S. M. Wurgler-Murphy, T. Maeda, E. A. Witten, T. C. Thai, and H. Saito. 1996. Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor. Cell 86:865-875.
    • (1996) Cell , vol.86 , pp. 865-875
    • Posas, F.1    Wurgler-Murphy, S.M.2    Maeda, T.3    Witten, E.A.4    Thai, T.C.5    Saito, H.6
  • 264
    • 0028136467 scopus 로고
    • Conditional lethality of a yeast strain expressing human RHOA in place of RHO1
    • Qadota, H., Y. Anraku, D. Botstein, and Y. Ohya. 1994. Conditional lethality of a yeast strain expressing human RHOA in place of RHO1. Proc. Natl. Acad. Sci. USA 91:9317-9321.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9317-9321
    • Qadota, H.1    Anraku, Y.2    Botstein, D.3    Ohya, Y.4
  • 266
    • 0033916138 scopus 로고    scopus 로고
    • The Skn7 response regulator of Saccharomyces cerevisiae interacts with Hsf1 in vivo and is required for the induction of heat shock genes by oxidative stress
    • Raitt, D. C., A. L. Johnson, A. M. Erkine, K. Makino, B. Morgan, D. S. Gross, and L. H. Johnston. 2000. The Skn7 Response Regulator of Saccharomyces cerevisiae Interacts with Hsf1 In Vivo and Is Required for the Induction of Heat Shock Genes by Oxidative Stress. Mol. Biol. Cell 11: 2335-2347.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2335-2347
    • Raitt, D.C.1    Johnson, A.L.2    Erkine, A.M.3    Makino, K.4    Morgan, B.5    Gross, D.S.6    Johnston, L.H.7
  • 267
    • 0032974582 scopus 로고    scopus 로고
    • Mid2 is a putative sensor for cell integrity signaling in Saccharomyces cerevisiae
    • Rajavel, M., B. Philip, B. M. Buehrer, B. Errede, and D. E. Levin. 1999. Mid2 is a putative sensor for cell integrity signaling in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:3969-3976.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3969-3976
    • Rajavel, M.1    Philip, B.2    Buehrer, B.M.3    Errede, B.4    Levin, D.E.5
  • 268
    • 0028861675 scopus 로고
    • Identification of two cell cycle regulated genes affecting the β-1,3-glucan content of cell wall in Saccharomyces cerevisiae
    • Ram, A. F., S. S. C. Brekelmans, L. J. W. M. Oehlen, and F. M. Klis. 1995. Identification of two cell cycle regulated genes affecting the β-1,3-glucan content of cell wall in Saccharomyces cerevisiae. FEBS Lett. 358:165-170.
    • (1995) FEBS Lett. , vol.358 , pp. 165-170
    • Ram, A.F.1    Brekelmans, S.S.C.2    Oehlen, L.J.W.M.3    Klis, F.M.4
  • 269
    • 0031938052 scopus 로고    scopus 로고
    • Loss of the plasma membrane-bound protein Gas1p in Saccharomyces cerevisiae results in the release of β1,3-glucan into the medium and induces a compensation mechanism to ensure cell wall integrity
    • Ram, A. F., J. C. Kapteyn, R. C. Montijn, L. H. Caro, J. E. Douwes, W. Baginsky, P. Mazur, H. van den Ende, and F. M. Klis. 1998. Loss of the plasma membrane-bound protein Gas1p in Saccharomyces cerevisiae results in the release of β1,3-glucan into the medium and induces a compensation mechanism to ensure cell wall integrity. J. Bacteriol. 180:1418-1424.
    • (1998) J. Bacteriol. , vol.180 , pp. 1418-1424
    • Ram, A.F.1    Kapteyn, J.C.2    Montijn, R.C.3    Caro, L.H.4    Douwes, J.E.5    Baginsky, W.6    Mazur, P.7    Van Den Ende, H.8    Klis, F.M.9
  • 270
    • 0000371441 scopus 로고
    • Shapes and interactions of carbohydrate chains
    • G. O. Aspinall (ed.). Academic Press, New York, NY
    • Rees, D. A., E. R. Morris, D. Thom, and J. K. Madden. 1982. Shapes and interactions of carbohydrate chains, p. 196-290. In G. O. Aspinall (ed.), The polysaccharides, vol. 1. Academic Press, New York, NY.
    • (1982) The Polysaccharides , vol.1 , pp. 196-290
    • Rees, D.A.1    Morris, E.R.2    Thom, D.3    Madden, J.K.4
  • 271
    • 2442605728 scopus 로고    scopus 로고
    • TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae
    • Reinke, A., S. Anderson, J. M. McCaffer, J. Yates, III, S. Aronova, S. Chu, S. Fairclough, C. Iverson, K. P. Wedaman, and T. Powers. 2004. TOR complex 1 includes a novel component, Tco89p (YPL180w), and cooperates with Ssd1p to maintain cellular integrity in Saccharomyces cerevisiae. J. Biol. Chem. 279:14752-14762.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14752-14762
    • Reinke, A.1    Anderson, S.2    McCaffer, J.M.3    Yates III, J.4    Aronova, S.5    Chu, S.6    Fairclough, S.7    Iverson, C.8    Wedaman, K.P.9    Powers, T.10
  • 272
    • 0038153182 scopus 로고    scopus 로고
    • Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure
    • Reiser, V., D. C. Raitt, and H. Saito. 2003. Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. J. Cell Biol. 161:1035-1040.
    • (2003) J. Cell Biol. , vol.161 , pp. 1035-1040
    • Reiser, V.1    Raitt, D.C.2    Saito, H.3
  • 273
    • 0035793383 scopus 로고    scopus 로고
    • Bakers' yeast, a model for fungal biofilm formation
    • Reynolds, T. B., and G. R. Fink. 2001. Bakers' yeast, a model for fungal biofilm formation. Science 291:878-881.
    • (2001) Science , vol.291 , pp. 878-881
    • Reynolds, T.B.1    Fink, G.R.2
  • 274
    • 3042812985 scopus 로고    scopus 로고
    • Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth
    • Richman, T. J., K. A. Toenjes, S. E. Morales, K. C. Cole, B. T. Wasserman, C. M. Taylor, Jacob A. Koster, M. F. Whelihan, and D. I. Johnson. 2004. Analysis of cell-cycle specific localization of the Rdi1p RhoGDI and the structural determinants required for Cdc42p membrane localization and clustering at sites of polarized growth. Curr. Genet. 45:339-349.
    • (2004) Curr. Genet. , vol.45 , pp. 339-349
    • Richman, T.J.1    Toenjes, K.A.2    Morales, S.E.3    Cole, K.C.4    Wasserman, B.T.5    Taylor, C.M.6    Koster, J.A.7    Whelihan, M.F.8    Johnson, D.I.9
  • 275
    • 0028925711 scopus 로고
    • Rho-related proteins: Actin cytoskeleton and cell cycle
    • Ridley, A. J. 1995. Rho-related proteins: actin cytoskeleton and cell cycle. Curr. Opin. Genet. Dev. 5:24-30.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 24-30
    • Ridley, A.J.1
  • 277
    • 0032911043 scopus 로고    scopus 로고
    • The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization
    • Robinson, L. C., C. Bradley, J. D. Bryan, A. Jerome, Y. Kweon, and H. R. Panek. 1999. The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization. Mol. Biol. Cell 10:1077-1092.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1077-1092
    • Robinson, L.C.1    Bradley, C.2    Bryan, J.D.3    Jerome, A.4    Kweon, Y.5    Panek, H.R.6
  • 278
    • 0027168362 scopus 로고
    • Casein kinase I-like protein kinases encoded by YCK1 and YCK2 are required for yeast morphogenesis
    • Robinson, L. C., M. M. Menold, S. Garrett, and M. R. Culbertson. 1993. Casein kinase I-like protein kinases encoded by YCK1 and YCK2 are required for yeast morphogenesis. Mol. Cell. Biol. 13:2870-2881.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2870-2881
    • Robinson, L.C.1    Menold, M.M.2    Garrett, S.3    Culbertson, M.R.4
  • 279
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson, N. G., L. Guo, J. Imai, A. Tohe, Y. Matsui, and F. Tamanoi. 1999. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19:3580-3587.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3580-3587
    • Robinson, N.G.1    Guo, L.2    Imai, J.3    Tohe, A.4    Matsui, Y.5    Tamanoi, F.6
  • 280
    • 0036734541 scopus 로고    scopus 로고
    • Pkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2 and define protein kinase modules required for maintenance of cell wall integrity
    • Roelants, F. M., P. D. Torrance, N. Bezman, and J. Thorner. 2002. Pkh1 and Pkh2 differentially phosphorylate and activate Ypk1 and Ykr2 and define protein kinase modules required for maintenance of cell wall integrity. Mol. Biol. Cell 13:3005-3028.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3005-3028
    • Roelants, F.M.1    Torrance, P.D.2    Bezman, N.3    Thorner, J.4
  • 281
    • 0027939330 scopus 로고
    • Characterization of the yeast (1→6)-beta-glucan biosynthetic components, Kre6p and Skn1p, and genetic interactions between the PKC1 pathway and extracellular matrix assembly
    • Roemer, T., G. Paravicini, M. A. Payton, and H. Bussey. 1994. Characterization of the yeast (1→6)-beta-glucan biosynthetic components, Kre6p and Skn1p, and genetic interactions between the PKC1 pathway and extracellular matrix assembly. J. Cell Biol. 127:567-579.
    • (1994) J. Cell Biol. , vol.127 , pp. 567-579
    • Roemer, T.1    Paravicini, G.2    Payton, M.A.3    Bussey, H.4
  • 282
    • 0036889144 scopus 로고    scopus 로고
    • HTL1 encodes a novel factor that interacts with the RSC chromatin remodeling complex in Saccharomyces cerevisiae
    • Romeo, M. J., M. L. Angus-Hill, A. K. Sobering, Y. Kamada, B. R. Cairns, and D. E. Levin. 2002. HTL1 encodes a novel factor that interacts with the RSC chromatin remodeling complex in Saccharomyces cerevisiae. Mol. Cell. Biol. 22:8165-8174.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8165-8174
    • Romeo, M.J.1    Angus-Hill, M.L.2    Sobering, A.K.3    Kamada, Y.4    Cairns, B.R.5    Levin, D.E.6
  • 283
    • 0035812886 scopus 로고    scopus 로고
    • Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae
    • Roumanie, O., C. Weinachter, I. Larrieu, M. Crouzet, F., and Doignon. 2001. Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from Saccharomyces cerevisiae. FEBS Lett. 506:149-156.
    • (2001) FEBS Lett. , vol.506 , pp. 149-156
    • Roumanie, O.1    Weinachter, C.2    Larrieu, I.3    Crouzet, M.4    Doignon5
  • 284
    • 0033779701 scopus 로고    scopus 로고
    • Caldneurin: Form and function
    • Rusnak, F., and P. Mertz. 2000. Caldneurin: form and function. Physiol. Rev. 80:1483-1521.
    • (2000) Physiol. Rev. , vol.80 , pp. 1483-1521
    • Rusnak, F.1    Mertz, P.2
  • 285
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot, I., S. K. Klee, and D. Pellman. 2002a. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4:42-50.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 288
    • 0027076554 scopus 로고
    • Protein prenylation: Genes, enzymes, targets, and functions
    • Schafer, R. W., and J. Rine. 1992. Protein prenylation: genes, enzymes, targets, and functions. Annu. Rev. Genet. 26:209-237.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 209-237
    • Schafer, R.W.1    Rine, J.2
  • 289
    • 0000713597 scopus 로고
    • Localized deposition of chitin on the yeast cell surface in response to mating pheromone
    • Schekman, R., and V. Brawley. 1979. Localized deposition of chitin on the yeast cell surface in response to mating pheromone. Proc. Natl. Acad. Sci. USA 76:645-649.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 645-649
    • Schekman, R.1    Brawley, V.2
  • 290
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • Schmelzle, T., and M. N. Hall. 2000. TOR, a central controller of cell growth. Cell 103:253-262.
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 291
    • 0036174159 scopus 로고    scopus 로고
    • Yeast protein kinases and the RHO1 exchange factor TUS1 are novel components of the cell integrity pathway in yeast
    • Schmelzle, T., S. B. Helliwell, and M. N. Hall. 2002. Yeast protein kinases and the RHO1 exchange factor TUS1 are novel components of the cell integrity pathway in yeast. Mol. Cell. Biol. 22:1329-1339.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1329-1339
    • Schmelzle, T.1    Helliwell, S.B.2    Hall, M.N.3
  • 292
    • 0030906569 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1and RHO2 via the exchange factor ROM2
    • Schmidt, A., M. Bickle, T. Beck, and M. N. Hall. 1997. The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1and RHO2 via the exchange factor ROM2. Cell 88:531-542.
    • (1997) Cell , vol.88 , pp. 531-542
    • Schmidt, A.1    Bickle, M.2    Beck, T.3    Hall, M.N.4
  • 293
    • 0030479340 scopus 로고    scopus 로고
    • TOR2 is required for organization of the actin cytoskeleton in yeast
    • Schmidt, A., J. Kunz, and M. N. Hall. 1996. TOR2 is required for organization of the actin cytoskeleton in yeast. Proc. Natl. Acad. Sci. USA 93: 13780-13785.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13780-13785
    • Schmidt, A.1    Kunz, J.2    Hall, M.N.3
  • 294
    • 0036049408 scopus 로고    scopus 로고
    • The RHO1-GAPs SAC7, BEM2, and BAG7 control distinct RHO1 functions in Saccharomyces cerevisiae
    • Schmidt, A., T. Schmelzle, and M. Hall. 2002. The RHO1-GAPs SAC7, BEM2, and BAG7 control distinct RHO1 functions in Saccharomyces cerevisiae. Mol. Microbiol. 45:1433-1441.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1433-1441
    • Schmidt, A.1    Schmelzle, T.2    Hall, M.3
  • 295
    • 0036675575 scopus 로고    scopus 로고
    • Rho5p downregulates the yeast cell integrity pathway
    • Schmitz, H. P., S. Huppert, A. Lorberg, and J. J. Heinisch. 2002. Rho5p downregulates the yeast cell integrity pathway. J. Cell Sci. 115:3139-3148.
    • (2002) J. Cell Sci. , vol.115 , pp. 3139-3148
    • Schmitz, H.P.1    Huppert, S.2    Lorberg, A.3    Heinisch, J.J.4
  • 296
    • 0035800598 scopus 로고    scopus 로고
    • Domain shuffling as a tool for investigation of protein function: Substitution of the cysteine-rich region of Raf kinase and PKC eta for that of yeast Pkc1p
    • Schmitz, H. P., J. Jockel, C. Block, and J. J. Heinisch. 2001. Domain shuffling as a tool for investigation of protein function: substitution of the cysteine-rich region of Raf kinase and PKC eta for that of yeast Pkc1p. J. Mol. Biol. 311:1-7.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1-7
    • Schmitz, H.P.1    Jockel, J.2    Block, C.3    Heinisch, J.J.4
  • 297
    • 0036091239 scopus 로고    scopus 로고
    • Regulation of yeast protein kinase C activity by interaction with the small GTPase Rho1p through its amino-terminal HR1 domain
    • Schmitz, H. P., A. Lorberg, and J. J. Heinisch. 2002. Regulation of yeast protein kinase C activity by interaction with the small GTPase Rho1p through its amino-terminal HR1 domain. Mol. Microbiol. 44:829-840.
    • (2002) Mol. Microbiol. , vol.44 , pp. 829-840
    • Schmitz, H.P.1    Lorberg, A.2    Heinisch, J.J.3
  • 298
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • Schoenwaelder, S. M., and K. Burridge. 1999. Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. Cell Biol. 11:274-286.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 299
    • 0030668145 scopus 로고    scopus 로고
    • BIM1 encodes a microtubule-binding protein in yeast
    • Schwartz, K., K. Richards, and D. Botstein. 1997. BIM1 encodes a microtubule-binding protein in yeast. Mol. Biol. Cell 8:2677-2691.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2677-2691
    • Schwartz, K.1    Richards, K.2    Botstein, D.3
  • 301
    • 0033953950 scopus 로고    scopus 로고
    • β-1,6-glucan synthesis in Saccharomyces cerevisiae
    • Shahinian, S., and H. Bussey. 2000. β-1,6-Glucan synthesis in Saccharomyces cerevisiae. Mol. Microbiol. 35:477-489.
    • (2000) Mol. Microbiol. , vol.35 , pp. 477-489
    • Shahinian, S.1    Bussey, H.2
  • 302
    • 0029666292 scopus 로고    scopus 로고
    • Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C
    • Shao, X., B. A. Davletov, R. B. Sutton, T. C. Sudhof, and J. Rizo. 1996. Bipartite Ca2+-binding motif in C2 domains of synaptotagmin and protein kinase C. Science 273:248-251.
    • (1996) Science , vol.273 , pp. 248-251
    • Shao, X.1    Davletov, B.A.2    Sutton, R.B.3    Sudhof, T.C.4    Rizo, J.5
  • 304
    • 0031835436 scopus 로고    scopus 로고
    • Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis
    • Sheu, Y. J., B. Santos, N. Fortin, C. Costigan, and M. Snyder. 1998. Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis. Mol. Cell. Biol. 18:4053-4069.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4053-4069
    • Sheu, Y.J.1    Santos, B.2    Fortin, N.3    Costigan, C.4    Snyder, M.5
  • 306
    • 0028174396 scopus 로고
    • The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase
    • Shimizu, J., K. Yoda, and M. Yamasaki. 1994. The hypo-osmolarity- sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase. Mol. Gen. Genet. 242:641-648.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 641-648
    • Shimizu, J.1    Yoda, K.2    Yamasaki, M.3
  • 307
    • 0032538796 scopus 로고    scopus 로고
    • Control of Swe1p degradation by the morphogenesis checkpoint
    • Sia, R. A. L., E. S. G. Bardes, and D. J. Lew. 1998. Control of Swe1p degradation by the morphogenesis checkpoint. EMBO J. 17:6678-6688.
    • (1998) EMBO J. , vol.17 , pp. 6678-6688
    • Sia, R.A.L.1    Bardes, E.S.G.2    Lew, D.J.3
  • 308
    • 0027500140 scopus 로고
    • 1/S-specific transcription in Saccharomyces cerevisiae
    • 1/S-specific transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1069-1077.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1069-1077
    • Sidorova, J.M.1    Breeden, L.L.2
  • 309
    • 0028820406 scopus 로고
    • Cell cycle-regulated phosphorylation of Swi6 controls its nuclear localization
    • Sidorova, J. M., G. E. Mikesell, and L. L. Breeden. 1995. Cell cycle-regulated phosphorylation of Swi6 controls its nuclear localization. Mol. Biol. Cell 6:1641-1658.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1641-1658
    • Sidorova, J.M.1    Mikesell, G.E.2    Breeden, L.L.3
  • 310
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer, M. A., and S. Lindquist. 1998. Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1:639-648.
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 311
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: The yin and yang of trehalose
    • Singer, M. A., and S. Lindquist. 1998. Thermotolerance in Saccharomyces cerevisiae: the yin and yang of trehalose. Trends Biotechnol. 16:460-468.
    • (1998) Trends Biotechnol. , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2
  • 312
    • 0034669693 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion
    • Singh, K. K. 2000. The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion. Free Radic. Biol. Med. 29:1043-1050.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 1043-1050
    • Singh, K.K.1
  • 314
    • 0024539080 scopus 로고
    • The SPA2 protein of yeast localizes to sites of cell growth
    • Snyder, M. 1989. The SPA2 protein of yeast localizes to sites of cell growth. J. Cell Biol. 108:1419-1429.
    • (1989) J. Cell Biol. , vol.108 , pp. 1419-1429
    • Snyder, M.1
  • 315
    • 0036463448 scopus 로고    scopus 로고
    • Yeast Rpi1 is a putative transcriptional regulator that contributes to preparation for stationary phase
    • Sobering, A. K., U. S. Jung, K. S. Lee, and D. E. Levin. 2002. Yeast Rpi1 is a putative transcriptional regulator that contributes to preparation for stationary phase. Eukaryot. Cell 1:56-65.
    • (2002) Eukaryot. Cell , vol.1 , pp. 56-65
    • Sobering, A.K.1    Jung, U.S.2    Lee, K.S.3    Levin, D.E.4
  • 316
    • 2542423740 scopus 로고    scopus 로고
    • Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER
    • Sobering, A. K., R. Watanabe, M. J. Romeo, B. C. Yan, C. A. Specht, P. Orlean, H. Riezman, and D. E. Levin. 2004. Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER. Cell 117:637-648.
    • (2004) Cell , vol.117 , pp. 637-648
    • Sobering, A.K.1    Watanabe, R.2    Romeo, M.J.3    Yan, B.C.4    Specht, C.A.5    Orlean, P.6    Riezman, H.7    Levin, D.E.8
  • 317
    • 0028886777 scopus 로고
    • Characterization of domains in the yeast MAP kinase Slt2 (Mpk1) required for functional activity and in vivo interaction with protein kinases Mkk1 and Mkk2
    • Soler, M., A. Plovins, H. Martin, M. Molina, and C. Nombela. 1995. Characterization of domains in the yeast MAP kinase Slt2 (Mpk1) required for functional activity and in vivo interaction with protein kinases Mkk1 and Mkk2. Mol. Microbiol. 17:833-842.
    • (1995) Mol. Microbiol. , vol.17 , pp. 833-842
    • Soler, M.1    Plovins, A.2    Martin, H.3    Molina, M.4    Nombela, C.5
  • 319
    • 0035839533 scopus 로고    scopus 로고
    • Phosphorylation of the yeast phopsholipid synthesis regulatory protein Opi1p by protein kinase C
    • Sreenivas, A., M. J. Villa-Garcia, S. A. Henry, and G. M. Carman. 2001. Phosphorylation of the yeast phopsholipid synthesis regulatory protein Opi1p by protein kinase C. J. Biol. Chem. 276:29915-29923.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29915-29923
    • Sreenivas, A.1    Villa-Garcia, M.J.2    Henry, S.A.3    Carman, G.M.4
  • 320
    • 0031438164 scopus 로고    scopus 로고
    • Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast
    • Stathopoulos, A. M., and M. S. Cyert. 1997. Calcineurin acts through the CRZ1/TCN1-encoded transcription factor to regulate gene expression in yeast. Genes Dev. 11:3432-3444.
    • (1997) Genes Dev. , vol.11 , pp. 3432-3444
    • Stathopoulos, A.M.1    Cyert, M.S.2
  • 321
    • 0033118396 scopus 로고    scopus 로고
    • Yeast calcineurin regulates nuclear localization of the Crz1p transcription factor through dephosphorylation
    • Stathopoulos-Gerontides, A., J. J. Guo, and M. S. Cyert. 1999. Yeast calcineurin regulates nuclear localization of the Crz1p transcription factor through dephosphorylation. Genes Dev. 13:798-803.
    • (1999) Genes Dev. , vol.13 , pp. 798-803
    • Stathopoulos-Gerontides, A.1    Guo, J.J.2    Cyert, M.S.3
  • 322
    • 0034639234 scopus 로고    scopus 로고
    • Mutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formation
    • Stirling, D. A., and M. J. Stark. 2000. Mutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formation. Biochim. Biophys. Acta 1499:85-100.
    • (2000) Biochim. Biophys. Acta , vol.1499 , pp. 85-100
    • Stirling, D.A.1    Stark, M.J.2
  • 324
    • 0343130542 scopus 로고    scopus 로고
    • Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a downstream kinase in the sphingolipid-mediated signaling pathway of yeast
    • Sun, Y., R. Taniguchi, D. Tanoue, T. Yamaji, H. Takematsu, K. Mori, T. Fujita, T. Kawasaki, and Y. Kozutsumi. 2000. Sli2 (Ypk1), a homologue of mammalian protein kinase SGK, is a downstream kinase in the sphingolipid- mediated signaling pathway of yeast. Mol. Cell. Biol. 20:4411-1419.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4411-11419
    • Sun, Y.1    Taniguchi, R.2    Tanoue, D.3    Yamaji, T.4    Takematsu, H.5    Mori, K.6    Fujita, T.7    Kawasaki, T.8    Kozutsumi, Y.9
  • 326
    • 0029785953 scopus 로고    scopus 로고
    • Non-equivalent roles for the first and second zinc fingers of protein kinase C delta. Effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells
    • Szallasi, Z., K. Bogi, S. Gohari, T. Biro, P. Acs, and P. M. Blumberg. 1996. Non-equivalent roles for the first and second zinc fingers of protein kinase C delta. Effect of their mutation on phorbol ester-induced translocation in NIH 3T3 cells. J. Biol. Chem. 271:18299-18301.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18299-18301
    • Szallasi, Z.1    Bogi, K.2    Gohari, S.3    Biro, T.4    Acs, P.5    Blumberg, P.M.6
  • 327
    • 0033646892 scopus 로고    scopus 로고
    • Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-attached proteins in response to cell wall damage caused by disruption of FKS1 in Saccharomyces cerevisiae
    • Terashima, H., N. Yabuki, M. Arisawa, K. Hamada, and K. Kitada. 2000. Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-attached proteins in response to cell wall damage caused by disruption of FKS1 in Saccharomyces cerevisiae. Mol. Gen. Genet. 264:64-74.
    • (2000) Mol. Gen. Genet. , vol.264 , pp. 64-74
    • Terashima, H.1    Yabuki, N.2    Arisawa, M.3    Hamada, K.4    Kitada, K.5
  • 328
    • 0033063643 scopus 로고    scopus 로고
    • Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation
    • Thevelein, and S. Hohmann. 1999. Fps1p controls the accumulation and release of the compatible solute glycerol in yeast osmoregulation. Mol. Microbiol. 31:1087-1104.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1087-1104
    • Thevelein1    Hohmann, S.2
  • 330
    • 0027208062 scopus 로고
    • Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock
    • Toh-e, A., S. Yasunaga, H. Nisogi, K. Tanaka, T. Oguchi, and Y. Matsui. 1993. Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock. Yeast 9:481-494.
    • (1993) Yeast , vol.9 , pp. 481-494
    • Toh-e, A.1    Yasunaga, S.2    Nisogi, H.3    Tanaka, K.4    Oguchi, T.5    Matsui, Y.6
  • 331
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker, A., and A. C. Newton. 2000. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J. Biol. Chem. 275: 8271-8274.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 332
    • 0037195254 scopus 로고    scopus 로고
    • Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis
    • Tolliday, N., L. VerPlank, and R. Li. 2002. Rho1 directs formin-mediated
    • (2002) Curr. Biol. , vol.12 , pp. 1864-1870
    • Tolliday, N.1    Verplank, L.2    Li, R.3
  • 333
    • 0037044801 scopus 로고    scopus 로고
    • Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast
    • Torres, J., C. J. di Como, E. Herrero, and M. Angeles de la Torre-Ruiz. 2002. Regulation of the cell integrity pathway by rapamycin-sensitive TOR function in budding yeast. J. Biol. Chem. 277:43495-43504.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43495-43504
    • Torres, J.1    Di Como, C.J.2    Herrero, E.3    Angeles De La Torre-Ruiz, M.4
  • 335
    • 0032126535 scopus 로고    scopus 로고
    • A mutation in NPS1/STH1, an essential gene encoding a component of a novel chromatin-remodeling complex RSC, alters the chromatin structure of Saccharomyces cerevisiae centromeres
    • Tsuchiya, E., T. Hosotani, and T. Miyakawa. 1998. A mutation in NPS1/STH1, an essential gene encoding a component of a novel chromatin-remodeling complex RSC, alters the chromatin structure of Saccharomyces cerevisiae centromeres. Nucleic Acids Res. 26:3286-3292.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 3286-3292
    • Tsuchiya, E.1    Hosotani, T.2    Miyakawa, T.3
  • 337
    • 0032537023 scopus 로고    scopus 로고
    • Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1α: Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Umikawa, M., K. Tanaka, T. Kamei, K. Shimizu, H. Imamura, T. Sasaki, and Y. Takai. 1998. Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1α: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene 16:2011-2016.
    • (1998) Oncogene , vol.16 , pp. 2011-2016
    • Umikawa, M.1    Tanaka, K.2    Kamei, T.3    Shimizu, K.4    Imamura, H.5    Sasaki, T.6    Takai, Y.7
  • 338
    • 0036165569 scopus 로고    scopus 로고
    • Movement of yeast 1,3-β-glucan synthase is essential for uniform cell wall biosynthesis
    • Utsugi, T., M. Minemura, A. Hirato, M. Abe, D. Watanabe, and Y. Ohya. 2002. Movement of yeast 1,3-β-glucan synthase is essential for uniform cell wall biosynthesis. Genes Cells 7:1-9.
    • (2002) Genes Cells , vol.7 , pp. 1-9
    • Utsugi, T.1    Minemura, M.2    Hirato, A.3    Abe, M.4    Watanabe, D.5    Ohya, Y.6
  • 339
    • 0042838332 scopus 로고    scopus 로고
    • The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane
    • Valdivia, R. H., and R. Schekman. 2003. The yeasts Rho1p and Pkc1p regulate the transport of chitin synthase III (Chs3p) from internal stores to the plasma membrane. Proc. Natl. Acad. Sci. USA 100:10287-10292.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10287-10292
    • Valdivia, R.H.1    Schekman, R.2
  • 340
    • 18344403896 scopus 로고    scopus 로고
    • Specificity of cysteine-rich domains in diacylglycerol kinases and protein kinases C
    • van Blitterwijk, W. J. 1998. Specificity of cysteine-rich domains in diacylglycerol kinases and protein kinases C. Biochem. J. 331:677-680.
    • (1998) Biochem. J. , vol.331 , pp. 677-680
    • Van Blitterwijk, W.J.1
  • 341
    • 0036794109 scopus 로고    scopus 로고
    • Spa2p functions as a scaffold-like protein to recruit the Mpk1p MAP kinase module to sites of polarized growth
    • van Drogen, F., and M. Peter. 2002. Spa2p functions as a scaffold-like protein to recruit the Mpk1p MAP kinase module to sites of polarized growth. Curr. Biol. 12:1698-1703.
    • (2002) Curr. Biol. , vol.12 , pp. 1698-1703
    • Van Drogen, F.1    Peter, M.2
  • 342
    • 6444227767 scopus 로고    scopus 로고
    • Mutational analysis of the cytoplasmic domain of the Wsc1 cell wall stress sensor
    • Vay, H. A., B. Philip, and D. E. Levin. 2004. Mutational analysis of the cytoplasmic domain of the Wsc1 cell wall stress sensor. Mol. Microbiol. 150: 3281-3288.
    • (2004) Mol. Microbiol. , vol.150 , pp. 3281-3288
    • Vay, H.A.1    Philip, B.2    Levin, D.E.3
  • 343
    • 0031442669 scopus 로고    scopus 로고
    • A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae
    • Verna, J., A. Lodder, K. Lee, A. Vagts, and R. Ballester. 1997. A family of genes required for maintenance of cell wall integrity and for the stress response in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 94:13804-13809.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13804-13809
    • Verna, J.1    Lodder, A.2    Lee, K.3    Vagts, A.4    Ballester, R.5
  • 345
    • 0032534682 scopus 로고    scopus 로고
    • Inside the crawling T cell: Leukocyte function-associated antigen-1 cross-linking is associated with microtubule-directed translocation of protein kinase C isoenzymes beta(I) and delta
    • Volkov, Y., A. Long, and D. Kelleher. 1998. Inside the crawling T cell: leukocyte function-associated antigen-1 cross-linking is associated with microtubule-directed translocation of protein kinase C isoenzymes beta(I) and delta. J. Immunol. 161:6487-6495.
    • (1998) J. Immunol. , vol.161 , pp. 6487-6495
    • Volkov, Y.1    Long, A.2    Kelleher, D.3
  • 346
    • 0033258472 scopus 로고    scopus 로고
    • The yeast phosphatidylinositol-4-OH kinase Pik1 regulates secretion at the Golgi
    • 1999
    • Walch-Solimena, C., and P. Novick. 1999. The yeast phosphatidylinositol- 4-OH kinase Pik1 regulates secretion at the Golgi. Nat. Cell Biol. 1999. 1: 523-525.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 523-525
    • Walch-Solimena, C.1    Novick, P.2
  • 347
    • 0034742648 scopus 로고    scopus 로고
    • Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-β-Glucan synthesis
    • Watanabe, D., M. Abe, and Y. Ohya. 2001. Yeast Lrg1p acts as a specialized RhoGAP regulating 1,3-β-Glucan synthesis. Yeast 18:943-951.
    • (2001) Yeast , vol.18 , pp. 943-951
    • Watanabe, D.1    Abe, M.2    Ohya, Y.3
  • 348
    • 0028309762 scopus 로고
    • Saccharomyces cerevisiae PKC1 encodes a protein kinase C (PKC) homolog with a substrate specificity similar to that of mammalian PKC
    • Watanabe, M., C-Y. Chen, and D. E. Levin. 1994. Saccharomyces cerevisiae PKC1 encodes a protein kinase C (PKC) homolog with a substrate specificity similar to that of mammalian PKC. J. Biol. Chem. 269:16829-16836.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16829-16836
    • Watanabe, M.1    Chen, C.-Y.2    Levin, D.E.3
  • 349
    • 0029092609 scopus 로고
    • Yeast RLM1 encodes a serum response factor-like protein that may function downstream of the Mpk1 (Slt2) mitogen-activated protein kinase pathway
    • Watanabe, Y., K. Irie, and K. Matsumoto. 1995. Yeast RLM1 encodes a serum response factor-like protein that may function downstream of the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Mol. Cell. Biol. 15: 5740-5749.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5740-5749
    • Watanabe, Y.1    Irie, K.2    Matsumoto, K.3
  • 350
    • 0030957532 scopus 로고    scopus 로고
    • Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway
    • Watanabe, Y., G. Takaesu, M. Hagiwara, K. Irie, and K. Matsumoto. 1997. Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Mol. Cell. Biol. 17:2615-2623.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2615-2623
    • Watanabe, Y.1    Takaesu, G.2    Hagiwara, M.3    Irie, K.4    Matsumoto, K.5
  • 351
    • 0042134553 scopus 로고    scopus 로고
    • The echinocandin antifungals: An overview of the pharmacology, spectrum and clinical efficacy
    • Wiederhold, N. P., and R. E. Lewis. 2003. The echinocandin antifungals: an overview of the pharmacology, spectrum and clinical efficacy. Expert Opin. Investig. Drugs 12:1313-1333.
    • (2003) Expert Opin. Investig. Drugs , vol.12 , pp. 1313-1333
    • Wiederhold, N.P.1    Lewis, R.E.2
  • 352
    • 0031750102 scopus 로고    scopus 로고
    • Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry
    • Wigge, P. A., O. N. Jensen, S. Homes, S. Soues, M. Mann, and J. V. Kilmartin. 1998. Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. J. Cell Biol. 141:967-977.
    • (1998) J. Cell Biol. , vol.141 , pp. 967-977
    • Wigge, P.A.1    Jensen, O.N.2    Homes, S.3    Soues, S.4    Mann, M.5    Kilmartin, J.V.6
  • 353
    • 0032730623 scopus 로고    scopus 로고
    • 1-S transition in Saccharomyces cerevisiae
    • 1-S transition in Saccharomyces cerevisiae. Genetics 153:1131-1143.
    • (1999) Genetics , vol.153 , pp. 1131-1143
    • Wijnen, H.1    Futcher, B.2
  • 354
    • 2342430611 scopus 로고    scopus 로고
    • The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate
    • Wild, A. C., J. W. Yu, M. A. Lemmon, and K. J. Blumer. 2004. The p21-activated protein kinase-related kinase Cla4 is a coincidence detector of signaling by Cdc42 and phosphatidylinositol 4-phosphate. J. Biol. Chem. 279:17101-17110.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17101-17110
    • Wild, A.C.1    Yu, J.W.2    Lemmon, M.A.3    Blumer, K.J.4
  • 355
    • 0035796626 scopus 로고    scopus 로고
    • The eukaryotic response regulator Skn7p regulates calcineurin signaling through stabilization of Crz1p
    • Williams, K. E., and M. S. Cyert. 2001. The eukaryotic response regulator Skn7p regulates calcineurin signaling through stabilization of Crz1p. EMBO J. 20:3473-3483.
    • (2001) EMBO J. , vol.20 , pp. 3473-3483
    • Williams, K.E.1    Cyert, M.S.2
  • 357
    • 0030711709 scopus 로고    scopus 로고
    • Interaction between Cdc42Hs and RhoGDI is mediated through the Rho insert region
    • Wu, W. J., D. A. Leonard, R. A. Cerione, and D. Manor. 1997. Interaction between Cdc42Hs and RhoGDI is mediated through the Rho insert region. J. Biol. Chem. 272:26153-26158.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26153-26158
    • Wu, W.J.1    Leonard, D.A.2    Cerione, R.A.3    Manor, D.4
  • 358
    • 0028228614 scopus 로고
    • Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae
    • Yamochi, W., K. Tanaka, H. Nonaka, A. Maeda, T. Musha, and Y. Takai. 1994. Growth site localization of Rho1 small GTP-binding protein and its involvement in bud formation in Saccharomyces cerevisiae. J. Cell Biol. 125:1077-1093.
    • (1994) J. Cell Biol. , vol.125 , pp. 1077-1093
    • Yamochi, W.1    Tanaka, K.2    Nonaka, H.3    Maeda, A.4    Musha, T.5    Takai, Y.6
  • 359
    • 0037059011 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits: A glycosylatable photoprobe binds to the luminal domain of Ost1p
    • Yan, Q., and W. J. Lennarz. 2002. Studies on the function of oligosaccharyl transferase subunits: a glycosylatable photoprobe binds to the luminal domain of Ost1p. Proc. Natl. Acad. Sci. USA 99:15994-15999.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15994-15999
    • Yan, Q.1    Lennarz, W.J.2
  • 360
    • 17544377116 scopus 로고    scopus 로고
    • Regulation of yeast CTP synthetase activity by protein kinase C
    • Yang, W-L., M. E. C. Bruno, and G. M. Carman. 1996. Regulation of yeast CTP synthetase activity by protein kinase C. J. Biol. Chem. 271:11113-11119.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11113-11119
    • Yang, W.-L.1    Bruno, M.E.C.2    Carman, G.M.3
  • 362
    • 0026503855 scopus 로고
    • Characterization of a staurosporine-sensitive and temperature-sensitive mutant, stt1, of Saccharomyces cerevisiae-STT1 is allelic to PKC1
    • Yoshida, S., E. Ikeda, I. Uno, and H. Mitsuzawa. 1992. Characterization of a staurosporine-sensitive and temperature-sensitive mutant, stt1, of Saccharomyces cerevisiae-STT1 is allelic to PKC1. Mol. Gen. Genet. 231:337-344.
    • (1992) Mol. Gen. Genet. , vol.231 , pp. 337-344
    • Yoshida, S.1    Ikeda, E.2    Uno, I.3    Mitsuzawa, H.4
  • 363
    • 0027979837 scopus 로고
    • A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae
    • Yoshida, S., Y. Ohya, M. Goebl, A. Nakano, and Y. Anraku. 1994. A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1 protein kinase pathway of Saccharomyces cerevisiae. J. Biol. Chem. 269:1166-1172.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1166-1172
    • Yoshida, S.1    Ohya, Y.2    Goebl, M.3    Nakano, A.4    Anraku, Y.5
  • 364
    • 0028218165 scopus 로고
    • Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae
    • Yoshida, S., Y. Ohya, A. Nakano, and Y. Anraku. 1994. Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae. Mol. Gen. Genet. 242:631-640.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 631-640
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4
  • 365
    • 0028818693 scopus 로고
    • STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast
    • Yoshida, S., Y. Ohya, A. Nakano, and Y. Anraku. 1995. STT3, a novel essential gene related to the PKC1/STT1 protein kinase pathway, is involved in protein glycosylation in yeast. Gene 164:167-172.
    • (1995) Gene , vol.164 , pp. 167-172
    • Yoshida, S.1    Ohya, Y.2    Nakano, A.3    Anraku, Y.4
  • 366
    • 0037163129 scopus 로고    scopus 로고
    • Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae
    • Yoshimoto, H., K. Saltsman, A. P. Gasch, H. X. Li, N. Ogawa, D. Botstein, P. O. Brown, and M. S. Cyert. 2002. Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae. J. Biol. Chem. 277:31079-31088.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31079-31088
    • Yoshimoto, H.1    Saltsman, K.2    Gasch, A.P.3    Li, H.X.4    Ogawa, N.5    Botstein, D.6    Brown, P.O.7    Cyert, M.S.8
  • 368
    • 0030026017 scopus 로고    scopus 로고
    • The SLT2 (MPK1) MAP kinase is activated during periods of polarized cell growth in yeast
    • Zarzov, P., C. Mazzoni, and C. Mann. 1996. The SLT2 (MPK1) MAP kinase is activated during periods of polarized cell growth in yeast. EMBO J. 15:83-91.
    • (1996) EMBO J. , vol.15 , pp. 83-91
    • Zarzov, P.1    Mazzoni, C.2    Mann, C.3
  • 370
    • 2542499556 scopus 로고    scopus 로고
    • Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1
    • Zhang, X., R. L. Lester, and R. C. Dickson. 2004. Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1. J. Biol. Chem. 279:22030-22038.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22030-22038
    • Zhang, X.1    Lester, R.L.2    Dickson, R.C.3
  • 371
    • 2642616985 scopus 로고    scopus 로고
    • Temperature-induced expression of yeast FKS2 is under the dual control of protein kinase C and calcineurin
    • Zhao, C., U. S. Jung, P. Garrett-Engele, T. Roe, M. S. Cyert, and D. E. Levin. 1998. Temperature-induced expression of yeast FKS2 is under the dual control of protein kinase C and calcineurin. Mol. Cell. Biol. 18:1013-1022.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1013-1022
    • Zhao, C.1    Jung, U.S.2    Garrett-Engele, P.3    Roe, T.4    Cyert, M.S.5    Levin, D.E.6
  • 372
    • 0021122967 scopus 로고
    • Saccharomyces cerevisiae mannoproteins form an external cell wall layer that determines wall porosity
    • Zlotnik, H., M. P. Fernandez, B. Bowers, and E. Cabib. 1984. Saccharomyces cerevisiae mannoproteins form an external cell wall layer that determines wall porosity. J. Bacteriol. 181:1018-1026.
    • (1984) J. Bacteriol. , vol.181 , pp. 1018-1026
    • Zlotnik, H.1    Fernandez, M.P.2    Bowers, B.3    Cabib, E.4
  • 373
    • 0028834273 scopus 로고
    • STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo
    • Zufferey, R., R. Knauer, P. Burda, I. Stagljar, S. te Heesen, L. Lehle, and M. Aebi. 1995. STT3, a highly conserved protein required for yeast oligosaccharyl transferase activity in vivo. EMBO J. 14:4949-4960.
    • (1995) EMBO J. , vol.14 , pp. 4949-4960
    • Zufferey, R.1    Knauer, R.2    Burda, P.3    Stagljar, I.4    Te Heesen, S.5    Lehle, L.6    Aebi, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.