메뉴 건너뛰기




Volumn 184, Issue 1, 2010, Pages 141-154

Drosophila translational elongation factor-1γ is modified in response to DOA kinase activity and is essential for cellular viability

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; LAMMER PROTEIN KINASE; PROTEIN KINASE; SERINE; TRANSCRIPTION FACTOR; TRANSLATIONAL ELONGATION FACTOR 1 GAMMA; UNCLASSIFIED DRUG;

EID: 74249091177     PISSN: 00166731     EISSN: 00166731     Source Type: Journal    
DOI: 10.1534/genetics.109.109553     Document Type: Article
Times cited : (16)

References (62)
  • 1
    • 0036884863 scopus 로고    scopus 로고
    • The 3′ untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1gamma and HAX-1
    • AL-MAGHREBI, M., H. BRULE, M. PADKINA, C. ALLEN, W. M. HOLMES et al., 2002 The 3′ untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1gamma and HAX-1. Nucleic Acids Res. 30: 5017-5028.
    • (2002) Nucleic Acids Res , vol.30 , pp. 5017-5028
    • AL-MAGHREBI, M.1    BRULE, H.2    PADKINA, M.3    ALLEN, C.4    HOLMES, W.M.5
  • 2
    • 0003455528 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • ASHBURNER, M., 1989 Drosophila: A Laboratory H book. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Drosophila: A Laboratory H book
    • ASHBURNER, M.1
  • 3
    • 0004270170 scopus 로고
    • AUSUBEL, F. M, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman et al, Editors, Greene/Wiley Publishing, New York
    • AUSUBEL, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman et al. (Editors), 1989 Current Protocols in Molecular Biology. Greene/Wiley Publishing, New York.
    • (1989) Current Protocols in Molecular Biology
  • 4
    • 0024449630 scopus 로고
    • A purified complex from Xenopus oocytes contains a P-47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF1g and EF1B
    • BELLÉ, R., J. DERANCOURT, R. POULHE, J.-P. CAPONY, R. OZON et al., 1989 A purified complex from Xenopus oocytes contains a P-47 protein, an in vivo substrate of MPF, and a p30 protein respectively homologous to elongation factors EF1g and EF1B. FEBS Lett. 255: 101-104.
    • (1989) FEBS Lett , vol.255 , pp. 101-104
    • BELLÉ, R.1    DERANCOURT, J.2    POULHE, R.3    CAPONY, J.-P.4    OZON, R.5
  • 5
    • 0034705026 scopus 로고    scopus 로고
    • Drosophila Thor participates in host immune defense and connects a translational regulator with innate immunity
    • BERNAL, A., and D. A. Kimbrell, 2000 Drosophila Thor participates in host immune defense and connects a translational regulator with innate immunity. Proc. Natl. Acad. Sci. USA 97: 6019-6024.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6019-6024
    • BERNAL, A.1    Kimbrell, D.A.2
  • 7
    • 0021703254 scopus 로고
    • Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes
    • CARVALHO, M. G., J. F. CARVALHO and W. C. MERRICK, 1984 Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes. Arch. Biochem. Biophys. 234: 603-611.
    • (1984) Arch. Biochem. Biophys , vol.234 , pp. 603-611
    • CARVALHO, M.G.1    CARVALHO, J.F.2    MERRICK, W.C.3
  • 8
    • 0029744344 scopus 로고    scopus 로고
    • SRPK1 and Clk/STY protein kinases show distinct substrate specificities for Serine/Arginine-rich splicing factors
    • COLWILL, K., L. L. FENG, J.M. YEAKLEY, G.D.GISH, J. F. CACERES et al., 1996a SRPK1 and Clk/STY protein kinases show distinct substrate specificities for Serine/Arginine-rich splicing factors. J. Biol. Chem. 271: 24569-24575.
    • (1996) J. Biol. Chem , vol.271 , pp. 24569-24575
    • COLWILL, K.1    FENG, L.L.2    YEAKLEY, J.M.3    GISH, G.D.4    CACERES, J.F.5
  • 9
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/STY protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • COLWILL, K., T. PAWSON, B. ANDREWS, J. PRASAD, J. L.MANLEY et al., 1996b The Clk/STY protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. EMBO J. 15: 265-275.
    • (1996) EMBO J , vol.15 , pp. 265-275
    • COLWILL, K.1    PAWSON, T.2    ANDREWS, B.3    PRASAD, J.4    MANLEY, J.L.5
  • 10
    • 0026410645 scopus 로고
    • Molecular cloning of Xenopus elongation factor 1g, major M-phase promoting factor substrate
    • CORMIER, P., H. B. OSBORNE, J. MORALES, T. BASSEZ, R. POULE et al., 1991 Molecular cloning of Xenopus elongation factor 1g, major M-phase promoting factor substrate. Nucleic Acids Res. 19: 6644.
    • (1991) Nucleic Acids Res , vol.19 , pp. 6644
    • CORMIER, P.1    OSBORNE, H.B.2    MORALES, J.3    BASSEZ, T.4    POULE, R.5
  • 11
    • 0019772606 scopus 로고
    • Protein synthesis in yeast II. Purification and properties of elongation factor 1 from Saccharomyces cerevisiae
    • DASMAHAPATRA, B., L. SKOGERSON and K. CHAKRABURTTY, 1981 Protein synthesis in yeast II. Purification and properties of elongation factor 1 from Saccharomyces cerevisiae. J. Biol. Chem. 256: 10005-10011.
    • (1981) J. Biol. Chem , vol.256 , pp. 10005-10011
    • DASMAHAPATRA, B.1    SKOGERSON, L.2    CHAKRABURTTY, K.3
  • 12
    • 0025330717 scopus 로고
    • Potentiation of a polyadenylation site by a downstream protein-DNA interaction
    • DORSETT, D., 1990 Potentiation of a polyadenylation site by a downstream protein-DNA interaction. Proc. Natl. Acad. Sci. USA 87: 4373-4377.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4373-4377
    • DORSETT, D.1
  • 13
    • 0032238550 scopus 로고    scopus 로고
    • Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila
    • DU, C., M. E. MCGUFFIN, B. DAUWALDER, L. RABINOW and W. Mattox, 1998 Protein phosphorylation plays an essential role in the regulation of alternative splicing and sex determination in Drosophila. Mol. Cell 2: 741-750.
    • (1998) Mol. Cell , vol.2 , pp. 741-750
    • DU, C.1    MCGUFFIN, M.E.2    DAUWALDER, B.3    RABINOW, L.4    Mattox, W.5
  • 14
    • 0027251721 scopus 로고
    • The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit
    • DURFEE, T., K. BECHERER, P. L. CHEN, S. H. YEH, Y. YANG et al., 1993 The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7: 555-569.
    • (1993) Genes Dev , vol.7 , pp. 555-569
    • DURFEE, T.1    BECHERER, K.2    CHEN, P.L.3    YEH, S.H.4    YANG, Y.5
  • 15
    • 0036359281 scopus 로고    scopus 로고
    • Moonlighting functions of polypeptide elongation factor 1: From actin bundling to zinc finger protein R1-associated nuclear localization
    • EJIRI, S., 2002 Moonlighting functions of polypeptide elongation factor 1: from actin bundling to zinc finger protein R1-associated nuclear localization. Biosci. Biotechnol. Biochem. 66: 1-21.
    • (2002) Biosci. Biotechnol. Biochem , vol.66 , pp. 1-21
    • EJIRI, S.1
  • 16
    • 19344370696 scopus 로고    scopus 로고
    • Functional dissection of an innate immune response by a genome-wide RNAi screen
    • FOLEY, E., and P. H. O'FARRELL, 2004 Functional dissection of an innate immune response by a genome-wide RNAi screen. PLoS Biol. 2: 1091-1106.
    • (2004) PLoS Biol , vol.2 , pp. 1091-1106
    • FOLEY, E.1    O'FARRELL, P.H.2
  • 17
    • 43049159544 scopus 로고    scopus 로고
    • Elongation factor 1Bgamma (eEF1Bgamma) expression during the molting cycle and cold acclimation in the crayfish Procambarus clarkii
    • GILLEN, C.M., Y. GAO, M. M. NIEHAUS-SAUTER, M. R. WYLDE and M. G. Wheatly, 2008 Elongation factor 1Bgamma (eEF1Bgamma) expression during the molting cycle and cold acclimation in the crayfish Procambarus clarkii. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 150: 170-176.
    • (2008) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.150 , pp. 170-176
    • GILLEN, C.M.1    GAO, Y.2    NIEHAUS-SAUTER, M.M.3    WYLDE, M.R.4    Wheatly, M.G.5
  • 18
    • 0345600247 scopus 로고    scopus 로고
    • A protein interaction map of Drosophila melanogaster
    • GIOT, L., J. S. BADER, C. BROUWER, A. CHAUDHURI, B. KUANG et al., 2003 A protein interaction map of Drosophila melanogaster. Science 302: 1727-1736.
    • (2003) Science , vol.302 , pp. 1727-1736
    • GIOT, L.1    BADER, J.S.2    BROUWER, C.3    CHAUDHURI, A.4    KUANG, B.5
  • 20
    • 43249123805 scopus 로고    scopus 로고
    • A microtubule interactome: Complexes with roles in cell cycle and mitosis
    • HUGHES, J. R., A. M. MEIRELES, K. H. FISHER, A. GARCIA, P. R. ANTROBUS et al., 2008 A microtubule interactome: complexes with roles in cell cycle and mitosis. PLoS Biol. 6: 785-795.
    • (2008) PLoS Biol , vol.6 , pp. 785-795
    • HUGHES, J.R.1    MEIRELES, A.M.2    FISHER, K.H.3    GARCIA, A.4    ANTROBUS, P.R.5
  • 21
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • JAMES, P., J. HALLADAY and E. A. CRAIG, 1996 Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144: 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • JAMES, P.1    HALLADAY, J.2    CRAIG, E.A.3
  • 22
    • 0024286504 scopus 로고
    • Elongation factor 1bg from Artemia: Purification and properties of its subunits
    • JANSSEN, G. M. C., and W. MOLLER, 1988 Elongation factor 1bg from Artemia: purification and properties of its subunits. Eur. J. Biochem. 171: 119-129.
    • (1988) Eur. J. Biochem , vol.171 , pp. 119-129
    • JANSSEN, G.M.C.1    MOLLER, W.2
  • 23
    • 0345306580 scopus 로고    scopus 로고
    • The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae
    • JEPPESEN, M. G., P. ORTIZ, W. SHEPARD, T. G. KINZY, J. NYBORG et al., 2003 The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J. Biol. Chem. 278: 47190-47198.
    • (2003) J. Biol. Chem , vol.278 , pp. 47190-47198
    • JEPPESEN, M.G.1    ORTIZ, P.2    SHEPARD, W.3    KINZY, T.G.4    NYBORG, J.5
  • 24
    • 34948845678 scopus 로고    scopus 로고
    • Interaction between the keratin cytoskeleton and eEF1Bg affects protein synthesis in epithelial cells
    • KIM, S., J. KELLNER, C. H. LEE and P. A. COULOMBE, 2007 Interaction between the keratin cytoskeleton and eEF1Bg affects protein synthesis in epithelial cells. Nat. Struct. Mol. Biol. 14: 982-983.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 982-983
    • KIM, S.1    KELLNER, J.2    LEE, C.H.3    COULOMBE, P.A.4
  • 25
    • 42349090551 scopus 로고    scopus 로고
    • Alternative promoter usage generates multiple evolutionarily conserved isoforms of Drosophila DOA kinase
    • KPEBE, A., and L. RABINOW, 2008a Alternative promoter usage generates multiple evolutionarily conserved isoforms of Drosophila DOA kinase. Genesis 46: 132-143.
    • (2008) Genesis , vol.46 , pp. 132-143
    • KPEBE, A.1    RABINOW, L.2
  • 26
    • 55749094873 scopus 로고    scopus 로고
    • Dissection of DOA kinase isoform functions in Drosophila
    • KPEBE, A., and L. RABINOW, 2008b Dissection of DOA kinase isoform functions in Drosophila. Genetics 179: 1973-1987.
    • (2008) Genetics , vol.179 , pp. 1973-1987
    • KPEBE, A.1    RABINOW, L.2
  • 28
    • 0029910142 scopus 로고    scopus 로고
    • Activity and autophosphorylation of LAMMER protein kinases
    • LEE, K., C. DU, M. HORN and L. RABINOW, 1996 Activity and autophosphorylation of LAMMER protein kinases. J. Biol. Chem. 271: 27299-27303.
    • (1996) J. Biol. Chem , vol.271 , pp. 27299-27303
    • LEE, K.1    DU, C.2    HORN, M.3    RABINOW, L.4
  • 29
    • 0037452653 scopus 로고    scopus 로고
    • LEE,C. Y., E.A.CLOUGH,P. YELLON,T.M. TESLOVICH,D.A. STEPHANET al., 2003 Genome-wide analyses of steroid- and radiation-triggered programmed cell death in Drosophila. Curr. Biol. 13: 350-357.
    • LEE,C. Y., E.A.CLOUGH,P. YELLON,T.M. TESLOVICH,D.A. STEPHANET al., 2003 Genome-wide analyses of steroid- and radiation-triggered programmed cell death in Drosophila. Curr. Biol. 13: 350-357.
  • 30
    • 0026505436 scopus 로고
    • Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer
    • LEW, Y., D. V. JONES, W. M. MARS, D. EVANS, D. BYRD et al., 1992 Expression of elongation factor-1 gamma-related sequence in human pancreatic cancer. Pancreas 7: 144-152.
    • (1992) Pancreas , vol.7 , pp. 144-152
    • LEW, Y.1    JONES, D.V.2    MARS, W.M.3    EVANS, D.4    BYRD, D.5
  • 31
    • 0032435862 scopus 로고    scopus 로고
    • Alternative splicing of pre-mRNA: Developmental consequences and mechanisms of regulation
    • LOPEZ, A. J., 1998 Alternative splicing of pre-mRNA: developmental consequences and mechanisms of regulation. Annu. Rev. Genet. 32: 279-305.
    • (1998) Annu. Rev. Genet , vol.32 , pp. 279-305
    • LOPEZ, A.J.1
  • 32
    • 0032031685 scopus 로고    scopus 로고
    • Overexpression of elongation factor-1gamma protein in colorectal carcinoma
    • MATHUR, S., K. R. CLEARY, N. INAMDAR, Y. H. KIM, P. STECK et al., 1998 Overexpression of elongation factor-1gamma protein in colorectal carcinoma. Cancer 82: 816-821.
    • (1998) Cancer , vol.82 , pp. 816-821
    • MATHUR, S.1    CLEARY, K.R.2    INAMDAR, N.3    KIM, Y.H.4    STECK, P.5
  • 33
    • 0033785992 scopus 로고    scopus 로고
    • Biochemical characterization and localization of the dual specificity kinase CLK1
    • MENEGAY, H. J., M. P. MYERS, F. M. MOESLEIN and G. E. LANDRETH, 2000 Biochemical characterization and localization of the dual specificity kinase CLK1. J. Cell Sci. 113: 3241-3253.
    • (2000) J. Cell Sci , vol.113 , pp. 3241-3253
    • MENEGAY, H.J.1    MYERS, M.P.2    MOESLEIN, F.M.3    LANDRETH, G.E.4
  • 34
    • 74249104668 scopus 로고    scopus 로고
    • MERRICK, W. C, and J. NYBORG Editors, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • MERRICK, W. C., and J. NYBORG (Editors), 2000 The Protein Synthesis Elongation Cycle. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) The Protein Synthesis Elongation Cycle
  • 35
    • 0028941915 scopus 로고
    • The overexpression of elongation factor 1 gamma mRNA in gastric carcinoma
    • MIMORI, K., M. MORI, S. TANAKA, T. AKIYOSHI and K. SUGIMACHI, 1995 The overexpression of elongation factor 1 gamma mRNA in gastric carcinoma. Cancer 75: 1446-1449.
    • (1995) Cancer , vol.75 , pp. 1446-1449
    • MIMORI, K.1    MORI, M.2    TANAKA, S.3    AKIYOSHI, T.4    SUGIMACHI, K.5
  • 36
    • 0030068368 scopus 로고    scopus 로고
    • Elongation factor 1 gamma mRNA expression in oesophageal carcinoma
    • MIMORI, K., M. MORI, H. INOUE, H. UEO, K. MAFUNE et al., 1996 Elongation factor 1 gamma mRNA expression in oesophageal carcinoma. Gut 38: 66-70.
    • (1996) Gut , vol.38 , pp. 66-70
    • MIMORI, K.1    MORI, M.2    INOUE, H.3    UEO, H.4    MAFUNE, K.5
  • 37
    • 0033578839 scopus 로고    scopus 로고
    • The CLK family kinases CLK1 and CLK2 phosphoryate and activate the tyrosine phosphatase PTP-1B
    • MOESLEIN, F. M., M. P. MYERS and G. E. LANDRETH, 1999 The CLK family kinases CLK1 and CLK2 phosphoryate and activate the tyrosine phosphatase PTP-1B. J. Biol. Chem. 274: 26697-26704.
    • (1999) J. Biol. Chem , vol.274 , pp. 26697-26704
    • MOESLEIN, F.M.1    MYERS, M.P.2    LANDRETH, G.E.3
  • 38
    • 0035312555 scopus 로고    scopus 로고
    • Evidence for regulation of protein synthesis at the elongation step by CDK1/cyclin B phosphorylation
    • MONNIER, A., R. BELLE, J. MORALES, P. CORMIER, S. BOULBEN et al., 2001 Evidence for regulation of protein synthesis at the elongation step by CDK1/cyclin B phosphorylation. Nucleic Acids Res. 29: 1453-1457.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1453-1457
    • MONNIER, A.1    BELLE, R.2    MORALES, J.3    CORMIER, P.4    BOULBEN, S.5
  • 39
    • 0026722141 scopus 로고
    • Phosphorylation of Xenopus elongation factor-1g by cdc2 protein kinase: Identification of the phosphorylation site
    • MULNER-LORILLON, O., P. CORMIER, J. CAVADORE, J. MORALES, R. POULHE et al., 1992 Phosphorylation of Xenopus elongation factor-1g by cdc2 protein kinase: identification of the phosphorylation site. Exp. Cell Res. 202: 549-551.
    • (1992) Exp. Cell Res , vol.202 , pp. 549-551
    • MULNER-LORILLON, O.1    CORMIER, P.2    CAVADORE, J.3    MORALES, J.4    POULHE, R.5
  • 40
    • 0030778935 scopus 로고    scopus 로고
    • Characterization and comparison of four serine- and arginine-rich (SR) protein kinases
    • NAYLER, O., S. STAMM and A. ULLRICH, 1997 Characterization and comparison of four serine- and arginine-rich (SR) protein kinases. Biochem. J. 326: 693-700.
    • (1997) Biochem. J , vol.326 , pp. 693-700
    • NAYLER, O.1    STAMM, S.2    ULLRICH, A.3
  • 41
    • 0032545381 scopus 로고    scopus 로고
    • The cellular localization of the murine Serine/Arginine-rich protein kinase CLK2 is regulated by Serine 141 autophosphorylation
    • NAYLER, O., F. SCHNORRER, S. STAMM and A. ULLRICH, 1998 The cellular localization of the murine Serine/Arginine-rich protein kinase CLK2 is regulated by Serine 141 autophosphorylation. J. Biol. Chem. 273: 34341-34348.
    • (1998) J. Biol. Chem , vol.273 , pp. 34341-34348
    • NAYLER, O.1    SCHNORRER, F.2    STAMM, S.3    ULLRICH, A.4
  • 42
    • 0037065728 scopus 로고    scopus 로고
    • Phosphorylation by LAMMER protein kinases: Determination of a consensus site, identification of in vitro substrates and implications for substrate preferences
    • NIKOLAKAKI, E., C. DU, J. LAI, L. CANTLEY, T. GIANNAKOUROS et al., 2002 Phosphorylation by LAMMER protein kinases: determination of a consensus site, identification of in vitro substrates and implications for substrate preferences. Biochemistry 41: 2055-2066.
    • (2002) Biochemistry , vol.41 , pp. 2055-2066
    • NIKOLAKAKI, E.1    DU, C.2    LAI, J.3    CANTLEY, L.4    GIANNAKOUROS, T.5
  • 43
    • 0021760534 scopus 로고
    • Sequence, structure and codon preference of the Drosophila ribosomal protein 49 gene
    • O'CONNELL, P. O., and M. ROSBASH, 1984 Sequence, structure and codon preference of the Drosophila ribosomal protein 49 gene. Nucleic Acids Res. 12: 5495-5513.
    • (1984) Nucleic Acids Res , vol.12 , pp. 5495-5513
    • O'CONNELL, P.O.1    ROSBASH, M.2
  • 44
    • 33645221519 scopus 로고    scopus 로고
    • The translation elongation factor eEF1B plays a role in the oxidative stress response pathway
    • OLAREWAJU, O., P. A. ORTIZ, W. Q. CHOWDHURY, I. CHATTERJEE and T. G. KINZY, 2004 The translation elongation factor eEF1B plays a role in the oxidative stress response pathway. RNA Biol. 1: e12-e17.
    • (2004) RNA Biol , vol.1
    • OLAREWAJU, O.1    ORTIZ, P.A.2    CHOWDHURY, W.Q.3    CHATTERJEE, I.4    KINZY, T.G.5
  • 45
    • 0026490151 scopus 로고
    • Dephosphorylation of phosphoproteins with potato acid phosphatase
    • PAPAVASSILIOU, A. G., and D. BOHMANN, 1992 Dephosphorylation of phosphoproteins with potato acid phosphatase. Methods Mol. Cell. Biol. 3: 149-152.
    • (1992) Methods Mol. Cell. Biol , vol.3 , pp. 149-152
    • PAPAVASSILIOU, A.G.1    BOHMANN, D.2
  • 46
    • 0038656410 scopus 로고    scopus 로고
    • Regulation and substrate specificity of the SR protein kinase Clk/Sty
    • PRASAD, J., and J. L. MANLEY, 2003 Regulation and substrate specificity of the SR protein kinase Clk/Sty. Mol. Cell. Biol. 23: 4139-4149.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 4139-4149
    • PRASAD, J.1    MANLEY, J.L.2
  • 47
    • 0027296571 scopus 로고
    • Mutations at the Darkener of apricot locus modulate transcript levels of copia and copia-induced mutations in Drosophila melanogaster
    • RABINOW, L., S. L. CHIANG and J. A. BIRCHLER, 1993 Mutations at the Darkener of apricot locus modulate transcript levels of copia and copia-induced mutations in Drosophila melanogaster. Genetics 134: 1175-1185.
    • (1993) Genetics , vol.134 , pp. 1175-1185
    • RABINOW, L.1    CHIANG, S.L.2    BIRCHLER, J.A.3
  • 49
    • 45549104911 scopus 로고    scopus 로고
    • Drosophila immunity: Methods for monitoring the activity of Toll and Imd signaling pathways
    • ROMEO, Y., and B. LEMAITRE, 2008 Drosophila immunity: methods for monitoring the activity of Toll and Imd signaling pathways. Methods Mol. Biol. 415: 379-394.
    • (2008) Methods Mol. Biol , vol.415 , pp. 379-394
    • ROMEO, Y.1    LEMAITRE, B.2
  • 50
    • 0033998566 scopus 로고    scopus 로고
    • The ethyleneinducible PK12 kinase mediates the phosphorylation of SR splicing factors
    • SAVALDI-GOLDSTEIN, S., G. SESSA and R. FLUHR, 2000 The ethyleneinducible PK12 kinase mediates the phosphorylation of SR splicing factors. Plant J. 21: 91-96.
    • (2000) Plant J , vol.21 , pp. 91-96
    • SAVALDI-GOLDSTEIN, S.1    SESSA, G.2    FLUHR, R.3
  • 51
    • 0030331213 scopus 로고    scopus 로고
    • 1996 PK12, a plant dual-specificity protein kinase of the LAMMER family, is regulated by the hormone ethylene
    • SESSA, G., V. RAZ, S. SAVALDI and R. FLUHR, 1996 PK12, a plant dual-specificity protein kinase of the LAMMER family, is regulated by the hormone ethylene. Plant Cell 8: 2223-2234.
    • Plant Cell , vol.8 , pp. 2223-2234
    • SESSA, G.1    RAZ, V.2    SAVALDI, S.3    FLUHR, R.4
  • 53
    • 0017811266 scopus 로고
    • Purification and properties of an elongation factor functionally analogous to bacterial elongation factor Ts from embryos of Artemia salina
    • SLOBIN, L. I., and W. MOLLER, 1978 Purification and properties of an elongation factor functionally analogous to bacterial elongation factor Ts from embryos of Artemia salina. Eur. J. Biochem. 84: 69-77.
    • (1978) Eur. J. Biochem , vol.84 , pp. 69-77
    • SLOBIN, L.I.1    MOLLER, W.2
  • 54
    • 14844329503 scopus 로고    scopus 로고
    • A Drosophila protein-interaction map centered on cellcycle regulators
    • STANYON, C. A., G. LIU, B. A. MANGIOLA, N. PATEL, L. GIOT et al., 2004 A Drosophila protein-interaction map centered on cellcycle regulators. Genome Biol. 5: R96.
    • (2004) Genome Biol , vol.5
    • STANYON, C.A.1    LIU, G.2    MANGIOLA, B.A.3    PATEL, N.4    GIOT, L.5
  • 55
    • 0027463298 scopus 로고
    • Interactions among vertebrate helix-loop-helix proteins in yeast using the two-hybrid system
    • STAUDINGER, J., M. PERRY, S. J. ELLEDGE and E. N. OLSON, 1993 Interactions among vertebrate helix-loop-helix proteins in yeast using the two-hybrid system. J. Biol. Chem. 268: 4608-4611.
    • (1993) J. Biol. Chem , vol.268 , pp. 4608-4611
    • STAUDINGER, J.1    PERRY, M.2    ELLEDGE, S.J.3    OLSON, E.N.4
  • 57
    • 0024319520 scopus 로고
    • A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals translational control of the segmentation gene hunchback
    • TAUTZ, D., and C. PFEIFLE, 1989 A non-radioactive in situ hybridization method for the localization of specific RNAs in Drosophila embryos reveals translational control of the segmentation gene hunchback. Chromosoma 98: 81-85.
    • (1989) Chromosoma , vol.98 , pp. 81-85
    • TAUTZ, D.1    PFEIFLE, C.2
  • 58
    • 2942668310 scopus 로고    scopus 로고
    • Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during Xenopus oocyte maturation
    • TOKUMOTO, T., A. KONDO, J. MIWA, R. HORIGUCHI, M. TOKUMOTO et al., 2003 Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during Xenopus oocyte maturation. BMC Biochem. 4: 6.
    • (2003) BMC Biochem , vol.4 , pp. 6
    • TOKUMOTO, T.1    KONDO, A.2    MIWA, J.3    HORIGUCHI, R.4    TOKUMOTO, M.5
  • 59
    • 0027267041 scopus 로고
    • Analysis of genetic mosaics in developing and adult Drosophila tissues
    • XU, T., and G. M. RUBIN, 1993 Analysis of genetic mosaics in developing and adult Drosophila tissues. Development 117: 1223-1237.
    • (1993) Development , vol.117 , pp. 1223-1237
    • XU, T.1    RUBIN, G.M.2
  • 60
    • 0035072833 scopus 로고    scopus 로고
    • A motif-based scanning approach for genome-wide prediction of signaling pathways
    • YAFFE, M. B., G. G. LEPARC, J.LAI, T.OBATA, S.VOLINIAet al., 2001 A motif-based scanning approach for genome-wide prediction of signaling pathways. Nat. Biotech. 19: 348-353.
    • (2001) Nat. Biotech , vol.19 , pp. 348-353
    • YAFFE, M.B.1    LEPARC, G.G.2    LAI, J.3    OBATA, T.4    VOLINIA, S.5
  • 61
    • 0028303751 scopus 로고    scopus 로고
    • YUN,B.,R.FARKAS,K.LEEANDL.RABINOW, 1994 The Doa locus encodes amember of a new protein kinase family, and is essential for eye and embryonic development in Drosophila melanogaster. Genes Dev. 8: 1160-1173.
    • YUN,B.,R.FARKAS,K.LEEANDL.RABINOW, 1994 The Doa locus encodes amember of a new protein kinase family, and is essential for eye and embryonic development in Drosophila melanogaster. Genes Dev. 8: 1160-1173.
  • 62
    • 0033786972 scopus 로고    scopus 로고
    • The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germ-line cells, and is expressed as both nuclear and cytoplasmic isoforms throughout development
    • YUN, B., K. LEE, R. FARKAS, C. HITTE and L. RABINOW, 2000 The LAMMER protein kinase encoded by the Doa locus of Drosophila is required in both somatic and germ-line cells, and is expressed as both nuclear and cytoplasmic isoforms throughout development. Genetics 156: 749-761.
    • (2000) Genetics , vol.156 , pp. 749-761
    • YUN, B.1    LEE, K.2    FARKAS, R.3    HITTE, C.4    RABINOW, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.