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Volumn 176, Issue 2, 2007, Pages 209-222

The Golgi-resident protease Kex2 acts in conjunction with Prm1 to facilitate cell fusion during yeast mating

Author keywords

[No Author keywords available]

Indexed keywords

KEX1 ENZYME; KEX2 ENZYME; MEMBRANE PROTEIN; PHEROMONE REGULATED MEMBRANE PROTEIN 1; PROTEINASE; STE13 ENZYME; UNCLASSIFIED DRUG;

EID: 33846451106     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200609182     Document Type: Article
Times cited : (31)

References (63)
  • 1
    • 0028879135 scopus 로고
    • Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection
    • Adames, N., K. Blundell, M.N. Ashby, and C. Boone. 1995. Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection. Science. 270:464-467.
    • (1995) Science , vol.270 , pp. 464-467
    • Adames, N.1    Blundell, K.2    Ashby, M.N.3    Boone, C.4
  • 2
    • 0031596206 scopus 로고    scopus 로고
    • Signalling in the yeasts: An informational cascade with links to the filamentous fungi
    • Banuett, F. 1998. Signalling in the yeasts: an informational cascade with links to the filamentous fungi. Microbiol. Mol. Biol. Rev. 62:249-274.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 249-274
    • Banuett, F.1
  • 3
    • 0025341613 scopus 로고
    • Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner
    • Basco, R.D., G. Gimenez-Gallego, and G. Larriba. 1990. Processing of yeast exoglucanase (beta-glucosidase) in a KEX2-dependent manner. FEBS Lett. 268:99-102.
    • (1990) FEBS Lett , vol.268 , pp. 99-102
    • Basco, R.D.1    Gimenez-Gallego, G.2    Larriba, G.3
  • 4
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P., T.G. Wolfsberg, C.W. Turck, D.G. Myles, P. Primakoff, and J.M. White. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature. 356:248-252.
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 5
    • 0021250375 scopus 로고
    • Sequence of the preprotoxin dsRNA gene of type I killer yeast: Multiple processing events produce a two-component toxin
    • Bostian, K.A., Q. Elliott, H. Bussey, V. Burn, A. Smith, and D.J. Tipper. 1984. Sequence of the preprotoxin dsRNA gene of type I killer yeast: multiple processing events produce a two-component toxin. Cell. 36:741-751.
    • (1984) Cell , vol.36 , pp. 741-751
    • Bostian, K.A.1    Elliott, Q.2    Bussey, H.3    Burn, V.4    Smith, A.5    Tipper, D.J.6
  • 6
    • 0032482228 scopus 로고    scopus 로고
    • Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae
    • Brizzio, V., A.E. Gammie, and M.D. Rose. 1998. Rvs161p interacts with Fus2p to promote cell fusion in Saccharomyces cerevisiae. J. Cell Biol. 141:567-584.
    • (1998) J. Cell Biol , vol.141 , pp. 567-584
    • Brizzio, V.1    Gammie, A.E.2    Rose, M.D.3
  • 7
    • 0031689604 scopus 로고    scopus 로고
    • New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating
    • Cappellaro, C., V. Mrsa, and W. Tanner. 1998. New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating. J. Bacteriol. 180:5030-5037.
    • (1998) J. Bacteriol , vol.180 , pp. 5030-5037
    • Cappellaro, C.1    Mrsa, V.2    Tanner, W.3
  • 9
    • 0034660644 scopus 로고    scopus 로고
    • Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: Evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion
    • Cho, C., H. Ge, D. Branciforte, P. Primakoff, and D.G. Myles. 2000. Analysis of mouse fertilin in wild-type and fertilin beta(-/-) sperm: evidence for C-terminal modification, alpha/beta dimerization, and lack of essential role of fertilin alpha in sperm-egg fusion. Dev. Biol. 222:289-295.
    • (2000) Dev. Biol , vol.222 , pp. 289-295
    • Cho, C.1    Ge, H.2    Branciforte, D.3    Primakoff, P.4    Myles, D.G.5
  • 12
    • 0030766556 scopus 로고    scopus 로고
    • Genetic analysis of myoblast fusion: Blown fuse is required for progression beyond the prefusion complex
    • Doberstein, S.K., R.D. Fetter, A.Y. Mehta, and C.S. Goodman. 1997. Genetic analysis of myoblast fusion: blown fuse is required for progression beyond the prefusion complex. J. Cell Biol. 136:1249-1261.
    • (1997) J. Cell Biol , vol.136 , pp. 1249-1261
    • Doberstein, S.K.1    Fetter, R.D.2    Mehta, A.Y.3    Goodman, C.S.4
  • 13
    • 0036067945 scopus 로고    scopus 로고
    • Myoblast fusion in Drosophila
    • Dworak, H.A., and H. Sink. 2002. Myoblast fusion in Drosophila. Bioessays. 24:591-601.
    • (2002) Bioessays , vol.24 , pp. 591-601
    • Dworak, H.A.1    Sink, H.2
  • 14
    • 0029826350 scopus 로고    scopus 로고
    • Role of the ABC transporter Ste6 in cell fusion during yeast conjugation
    • Elia, L., and L. Marsh. 1996. Role of the ABC transporter Ste6 in cell fusion during yeast conjugation. J. Cell Biol. 135:741-751.
    • (1996) J. Cell Biol , vol.135 , pp. 741-751
    • Elia, L.1    Marsh, L.2
  • 15
    • 0032555945 scopus 로고    scopus 로고
    • A role for a protease in morphogenic responses during yeast cell fusion
    • Elia, L., and L. Marsh. 1998. A role for a protease in morphogenic responses during yeast cell fusion. J. Cell Biol. 142:1473-1485.
    • (1998) J. Cell Biol , vol.142 , pp. 1473-1485
    • Elia, L.1    Marsh, L.2
  • 16
    • 0000611868 scopus 로고
    • Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease
    • Fuller, R.S., A. Brake, and J. Thorner. 1989. Yeast prohormone processing enzyme (KEX2 gene product) is a Ca2+-dependent serine protease. Proc. Natl. Acad. Sci. USA. 86:1434-1438.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1434-1438
    • Fuller, R.S.1    Brake, A.2    Thorner, J.3
  • 18
    • 0032534758 scopus 로고    scopus 로고
    • Springs and zippers: Coiled coils in SNARE-mediated membrane fusion
    • Harbury, P.A. 1998. Springs and zippers: coiled coils in SNARE-mediated membrane fusion. Structure. 6:1487-1491.
    • (1998) Structure , vol.6 , pp. 1487-1491
    • Harbury, P.A.1
  • 19
    • 0034735578 scopus 로고    scopus 로고
    • Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating
    • Heiman, M.G., and P. Walter. 2000. Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating. J. Cell Biol. 151:719-730.
    • (2000) J. Cell Biol , vol.151 , pp. 719-730
    • Heiman, M.G.1    Walter, P.2
  • 21
    • 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
  • 22
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson, F.M. 1995. Structural characterization of viral fusion proteins. Curr. Biol. 5:265-274.
    • (1995) Curr. Biol , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 23
    • 11144335897 scopus 로고    scopus 로고
    • Prm1 prevents contact-dependent lysis of yeast mating pairs
    • Jin, H., C. Carlile, S. Nolan, and E. Grote. 2004. Prm1 prevents contact-dependent lysis of yeast mating pairs. Eukaryot. Cell. 3:1664-1673.
    • (2004) Eukaryot. Cell , vol.3 , pp. 1664-1673
    • Jin, H.1    Carlile, C.2    Nolan, S.3    Grote, E.4
  • 24
    • 0020724122 scopus 로고
    • Yeast alpha factor is processed from a larger precursor polypeptide: The essential role of a membrane-bound dipeptidyl aminopeptidase
    • Julius, D., L. Blair, A. Brake, G. Sprague, and J. Thorner. 1983. Yeast alpha factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell. 32:839-852.
    • (1983) Cell , vol.32 , pp. 839-852
    • Julius, D.1    Blair, L.2    Brake, A.3    Sprague, G.4    Thorner, J.5
  • 25
    • 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
  • 27
    • 0033791650 scopus 로고    scopus 로고
    • Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells
    • Kim, J., and D.J. Klionsky. 2000. Autophagy, cytoplasm-to-vacuole targeting pathway, and pexophagy in yeast and mammalian cells. Annu. Rev. Biochem. 69:303-342.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 303-342
    • Kim, J.1    Klionsky, D.J.2
  • 28
    • 0028848292 scopus 로고
    • Shared functions in vivo of a glycosylphosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast
    • Komano, H., and R.S. Fuller. 1995. Shared functions in vivo of a glycosylphosphatidylinositol-linked aspartyl protease, Mkc7, and the proprotein processing protease Kex2 in yeast. Proc. Natl. Acad. Sci. USA. 92:10752-10756.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10752-10756
    • Komano, H.1    Fuller, R.S.2
  • 29
    • 0027964421 scopus 로고
    • Nuclear congression and membrane fusion: Two distinct events in the yeast karyogamy pathway
    • Kurihara, L.J., C.T. Beh, M. Latterich, R. Schekman, and M.D. Rose. 1994. Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway. J. Cell Biol. 126:911-923.
    • (1994) J. Cell Biol , vol.126 , pp. 911-923
    • Kurihara, L.J.1    Beh, C.T.2    Latterich, M.3    Schekman, R.4    Rose, M.D.5
  • 30
    • 0020365369 scopus 로고
    • Structure of a yeast pheromone gene (MF alpha): A putative alpha-factor precursor contains four tandem copies of mature alpha-factor
    • Kurjan, J., and I. Herskowitz. 1982. Structure of a yeast pheromone gene (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor. Cell. 30:933-943.
    • (1982) Cell , vol.30 , pp. 933-943
    • Kurjan, J.1    Herskowitz, I.2
  • 31
    • 0000352990 scopus 로고
    • A chromosomal gene required for killer plasmid expression, mating, and spore maturation in Saccharomyces cerevisiae
    • Leibowitz, M.J., and R.B. Wickner. 1976. A chromosomal gene required for killer plasmid expression, mating, and spore maturation in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 73:2061-2065.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2061-2065
    • Leibowitz, M.J.1    Wickner, R.B.2
  • 33
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 34
    • 0032618726 scopus 로고    scopus 로고
    • High-pressure freezing for preservation of high resolution fine structure and antigenicity for immunolabeling
    • McDonald, K. 1999. High-pressure freezing for preservation of high resolution fine structure and antigenicity for immunolabeling. Methods Mol. Biol. 117:77-97.
    • (1999) Methods Mol. Biol , vol.117 , pp. 77-97
    • McDonald, K.1
  • 35
    • 0036277570 scopus 로고    scopus 로고
    • Cryomethods for thin section electron microscopy
    • McDonald, K., and T. Müller-Reichert. 2002. Cryomethods for thin section electron microscopy. Methods Enzymol. 351:96-123.
    • (2002) Methods Enzymol , vol.351 , pp. 96-123
    • McDonald, K.1    Müller-Reichert, T.2
  • 39
    • 0030883927 scopus 로고    scopus 로고
    • Specific labelling of cell wall proteins by biotinylation. Identification of four covalently linked O-mannosylated proteins of Saccharomyces cerevisiae
    • Mrsa, V., T. Seidl, M. Gentzsch, and W. Tanner. 1997. Specific labelling of cell wall proteins by biotinylation. Identification of four covalently linked O-mannosylated proteins of Saccharomyces cerevisiae. Yeast. 13:1145-1154.
    • (1997) Yeast , vol.13 , pp. 1145-1154
    • Mrsa, V.1    Seidl, T.2    Gentzsch, M.3    Tanner, W.4
  • 40
    • 0141643295 scopus 로고    scopus 로고
    • Fig1p facilitates Ca2+ influx and cell fusion during mating of Saccharomyces cerevisiae
    • Muller, E.M., N.A. Mackin, S.E. Erdman, and K.W. Cunningham. 2003. Fig1p facilitates Ca2+ influx and cell fusion during mating of Saccharomyces cerevisiae. J. Biol. Chem. 278:38461-38469.
    • (2003) J. Biol. Chem , vol.278 , pp. 38461-38469
    • Muller, E.M.1    Mackin, N.A.2    Erdman, S.E.3    Cunningham, K.W.4
  • 41
    • 0030051440 scopus 로고    scopus 로고
    • ER membrane protein complex required for nuclear fusion
    • Ng, D.T., and P. Walter. 1996. ER membrane protein complex required for nuclear fusion. J. Cell Biol. 132:499-509.
    • (1996) J. Cell Biol , vol.132 , pp. 499-509
    • Ng, D.T.1    Walter, P.2
  • 42
    • 33745286618 scopus 로고    scopus 로고
    • FUS1 regulates the opening and expansion of fusion pores between mating yeast
    • Nolan, S., A.E. Cowan, D.E. Koppel, H. Jin, and E. Grote. 2006. FUS1 regulates the opening and expansion of fusion pores between mating yeast. Mol. Biol. Cell. 17:2439-2450.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2439-2450
    • Nolan, S.1    Cowan, A.E.2    Koppel, D.E.3    Jin, H.4    Grote, E.5
  • 43
    • 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
  • 44
    • 0036275984 scopus 로고    scopus 로고
    • A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch
    • O'Rourke, S.M., and I. Herskowitz. 2002. A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch. Mol. Cell. Biol. 22:4739-4749.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4739-4749
    • O'Rourke, S.M.1    Herskowitz, I.2
  • 45
    • 0344395603 scopus 로고    scopus 로고
    • Bypassing a kinase activity with an ATP-competitive drug
    • Papa, F.R., C. Zhang, K. Shokat, and P. Walter. 2003. Bypassing a kinase activity with an ATP-competitive drug. Science. 302:1533-1537.
    • (2003) Science , vol.302 , pp. 1533-1537
    • Papa, F.R.1    Zhang, C.2    Shokat, K.3    Walter, P.4
  • 46
    • 0030884717 scopus 로고    scopus 로고
    • Osmotic balance regulates cell fusion during mating in Saccharomyces cerevisiae
    • Philips, J., and I. Herskowitz. 1997. Osmotic balance regulates cell fusion during mating in Saccharomyces cerevisiae. J. Cell Biol. 138:961-974.
    • (1997) J. Cell Biol , vol.138 , pp. 961-974
    • Philips, J.1    Herskowitz, I.2
  • 47
    • 0032547791 scopus 로고    scopus 로고
    • Identification of Kel1p, a kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae
    • Philips, J., and I. Herskowitz. 1998. Identification of Kel1p, a kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae. J. Cell Biol. 143:375-389.
    • (1998) J. Cell Biol , vol.143 , pp. 375-389
    • Philips, J.1    Herskowitz, I.2
  • 48
    • 33748942475 scopus 로고    scopus 로고
    • The C. elegans developmental fusogen EFF-1 mediates homotypic fusion in heterologous cells and in vivo
    • Podbilewicz, B., E. Leikina, A. Sapir, C. Valansi, M. Suissa, G. Shemer, and L.V. Chernomordik. 2006. The C. elegans developmental fusogen EFF-1 mediates homotypic fusion in heterologous cells and in vivo. Dev. Cell. 11:471-481.
    • (2006) Dev. Cell , vol.11 , pp. 471-481
    • Podbilewicz, B.1    Leikina, E.2    Sapir, A.3    Valansi, C.4    Suissa, M.5    Shemer, G.6    Chernomordik, L.V.7
  • 49
    • 0032578032 scopus 로고    scopus 로고
    • The influenza virus hemagglutinin: A model protein in the study of membrane fusion
    • Ramalho-Santos, J., and M.C. de Lima. 1998. The influenza virus hemagglutinin: a model protein in the study of membrane fusion. Biochim. Biophys. Acta. 1376:147-154.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 147-154
    • Ramalho-Santos, J.1    de Lima, M.C.2
  • 51
    • 0026730895 scopus 로고    scopus 로고
    • Russo, P., N. Kalkkinen, H. Sareneva, J. Paakkola, and M. Makarow. 1992. A heat shock gene from Saccharomyces cerevisiae encoding a secretory glycoprotein. Proc. Natl. Acad. Sci. USA. 89:3671-3675. (published erratum appears in Proc. Natl. Acad. Sci. USA. 1992. 89:8857)
    • Russo, P., N. Kalkkinen, H. Sareneva, J. Paakkola, and M. Makarow. 1992. A heat shock gene from Saccharomyces cerevisiae encoding a secretory glycoprotein. Proc. Natl. Acad. Sci. USA. 89:3671-3675. (published erratum appears in Proc. Natl. Acad. Sci. USA. 1992. 89:8857)
  • 52
    • 4644367201 scopus 로고    scopus 로고
    • EFF-1 is sufficient to initiate and execute tissue-specific cell fusion in C. elegans
    • Shemer, G., M. Suissa, I. Kolotuev, K.C. Nguyen, D.H. Hall, and B. Podbilewicz. 2004. EFF-1 is sufficient to initiate and execute tissue-specific cell fusion in C. elegans. Curr. Biol. 14:1587-1591.
    • (2004) Curr. Biol , vol.14 , pp. 1587-1591
    • Shemer, G.1    Suissa, M.2    Kolotuev, I.3    Nguyen, K.C.4    Hall, D.H.5    Podbilewicz, B.6
  • 53
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics. 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 54
    • 0021112184 scopus 로고
    • Saccharomyces cerevisiae contains two discrete genes coding for the alpha-factor pheromone
    • Singh, A., E.Y. Chen, J.M. Lugovoy, C.N. Chang, R.A. Hitzeman, and P.H. Seeburg. 1983. Saccharomyces cerevisiae contains two discrete genes coding for the alpha-factor pheromone. Nucleic Acids Res. 11:4049-4063.
    • (1983) Nucleic Acids Res , vol.11 , pp. 4049-4063
    • Singh, A.1    Chen, E.Y.2    Lugovoy, J.M.3    Chang, C.N.4    Hitzeman, R.A.5    Seeburg, P.H.6
  • 55
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J.J., and D.C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 56
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R.B., D. Fasshauer, R. Jahn, and A.T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 57
    • 0037235251 scopus 로고    scopus 로고
    • Cell adhesion and fertilization: Steps in oocyte transport, sperm-zona pellucida interactions, and sperm-egg fusion
    • Talbot, P., B.D. Shur, and D.G. Myles. 2003. Cell adhesion and fertilization: steps in oocyte transport, sperm-zona pellucida interactions, and sperm-egg fusion. Biol. Reprod. 68:1-9.
    • (2003) Biol. Reprod , vol.68 , pp. 1-9
    • Talbot, P.1    Shur, B.D.2    Myles, D.G.3
  • 58
    • 0042122516 scopus 로고    scopus 로고
    • Mutations that are synthetically lethal with a gas1Δ allele cause defects in the cell wall of Saccharomyces cerevisiae
    • Tomishige, N., Y. Noda, H. Adachi, H. Shimoi, A. Takatsuki, and K. Yoda. 2003. Mutations that are synthetically lethal with a gas1Δ allele cause defects in the cell wall of Saccharomyces cerevisiae. Mol. Genet. Genomics. 269:562-573.
    • (2003) Mol. Genet. Genomics , vol.269 , pp. 562-573
    • Tomishige, N.1    Noda, Y.2    Adachi, H.3    Shimoi, H.4    Takatsuki, A.5    Yoda, K.6
  • 59
    • 0023376280 scopus 로고
    • Two genes required for cell fusion during yeast conjugation: Evidence for a pheromone-induced surface protein
    • Trueheart, J., J.D. Boeke, and G.R. Fink. 1987. Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein. Mol. Cell. Biol. 7:2316-2328.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 2316-2328
    • Trueheart, J.1    Boeke, J.D.2    Fink, G.R.3
  • 61
    • 0035177384 scopus 로고    scopus 로고
    • Yeast mating: Getting close to membrane merger
    • White, J.M., and M.D. Rose. 2001. Yeast mating: getting close to membrane merger. Curr. Biol. 11:R16-R20.
    • (2001) Curr. Biol , vol.11
    • White, J.M.1    Rose, M.D.2
  • 62
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A., J.J. Skehel, and D.C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature. 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 63
    • 0026588297 scopus 로고
    • Kex2-dependent processing of yeast K1 killer preprotoxin includes cleavage at ProArg-44
    • Zhu, Y.S., X.Y. Zhang, C.P. Cartwright, and D.J. Tipper. 1992. Kex2-dependent processing of yeast K1 killer preprotoxin includes cleavage at ProArg-44. Mol. Microbiol. 6:511-520.
    • (1992) Mol. Microbiol , vol.6 , pp. 511-520
    • Zhu, Y.S.1    Zhang, X.Y.2    Cartwright, C.P.3    Tipper, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.