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Volumn 16, Issue 1, 1996, Pages 179-191

Schizosaccharomyces pombe skp1+ encodes a protein kinase related to mammalian glycogen synthase kinase 3 and complements a cdc14 cytokinesis mutant

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; MAMMALIA; SCHIZOSACCHAROMYCES POMBE;

EID: 0029655786     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.1.179     Document Type: Article
Times cited : (42)

References (61)
  • 1
    • 0026572354 scopus 로고
    • Versatile shuttle vectors and genomic libraries for use with Schizosaccharomyces pombe
    • Barbet, N., W. J. Muriel, and A. M. Carr. 1992 Versatile shuttle vectors and genomic libraries for use with Schizosaccharomyces pombe. Gene 144:59-66.
    • (1992) Gene , vol.144 , pp. 59-66
    • Barbet, N.1    Muriel, W.J.2    Carr, A.M.3
  • 2
    • 0027979679 scopus 로고
    • Arabidopsis homologs of the shaggy and GSK-3 protein kinases: Molecular cloning and functional expression in Escherichia coli
    • Bianchi, M. W., D. Guivarc'h, M. Thomas, J. R. Woodgett, and M. Kreis. 1994 Arabidopsis homologs of The shaggy and GSK-3 protein kinases: molecular cloning and functional expression in Escherichia coli. Mol. Gen. Genet 242:337-345.
    • (1994) Mol. Gen. Genet , vol.242 , pp. 337-345
    • Bianchi, M.W.1    Guivarc'h, D.2    Thomas, M.3    Woodgett, J.R.4    Kreis, M.5
  • 3
    • 0027385529 scopus 로고
    • A Saccharomyces cerevisiae protein-serine kinase related to mammalian glycogen synthase kinase-3 and the Drosophila melanogaster gene shaggy product
    • Bianchi, M. W., S. E. Plyte, M. Kreis, and J. R. Woodgett. 1993. A Saccharomyces cerevisiae protein-serine kinase related to mammalian glycogen synthase kinase-3 and the Drosophila melanogaster gene shaggy product. Gene 134:51-56
    • (1993) Gene , vol.134 , pp. 51-56
    • Bianchi, M.W.1    Plyte, S.E.2    Kreis, M.3    Woodgett, J.R.4
  • 4
    • 0026661306 scopus 로고
    • Shaggy (zeste-white3) and the formation of supernumerary bristle precursors in the developing wing blade of Drosophila
    • Blair, S. S. 1992. shaggy (zeste-white3) and the formation of supernumerary bristle precursors in the developing wing blade of Drosophila. Dev Biol. 152: 265-278
    • (1992) Dev Biol. , vol.152 , pp. 265-278
    • Blair, S.S.1
  • 6
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of cJun at sites that negatively regulate its DNA binding activity
    • Boyle, W. B., T. Smeal, L. H. K. Defize, P. Angel, J. R. Woodgett, M. Karin, and T. Hunter. 1991. Activation of protein kinase C decreases phosphorylation of cJun at sites that negatively regulate its DNA binding activity. Cell 64:573-584.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.B.1    Smeal, T.2    Defize, L.H.K.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6    Hunter, T.7
  • 7
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates Methods Enzymol. 201:110-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 8
    • 85033824225 scopus 로고    scopus 로고
    • Personal communication
    • Carr, A. Personal communication.
    • Carr, A.1
  • 9
    • 85033823411 scopus 로고    scopus 로고
    • Personal communication
    • Chang, F., and P. Nurse. Personal communication.
    • Chang, F.1    Nurse, P.2
  • 10
    • 0020983488 scopus 로고
    • Detection and quantification of phosphotyrosine in proteins
    • Cooper, J. A., B. M. Sefton, and T. Hunter. 1983. Detection and quantification of phosphotyrosine in proteins. Methods Enzymol 99:387-402
    • (1983) Methods Enzymol , vol.99 , pp. 387-402
    • Cooper, J.A.1    Sefton, B.M.2    Hunter, T.3
  • 11
    • 0025224120 scopus 로고
    • Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity
    • Dailey, D., G. L. Schieven, M. Y. Lim, H. Marquardt, T. Gilmore, J. Thorner, and G. S. Martin. 1990 Novel yeast protein kinase (YPK1 gene product) is a 40-kilodalton phosphotyrosyl protein associated with protein-tyrosine kinase activity. Mol. Cell Biol. 10:6244-6256.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 6244-6256
    • Dailey, D.1    Schieven, G.L.2    Lim, M.Y.3    Marquardt, H.4    Gilmore, T.5    Thorner, J.6    Martin, G.S.7
  • 14
    • 0019026208 scopus 로고
    • Glycogen synthase kinase-3 from rabbit skeletal muscle
    • Embi, N., D. B. Rylatt, and P. Cohen. 1980. Glycogen synthase kinase-3 from rabbit skeletal muscle. Eur. J. Biochem 107:519-527.
    • (1980) Eur. J. Biochem , vol.107 , pp. 519-527
    • Embi, N.1    Rylatt, D.B.2    Cohen, P.3
  • 15
    • 0027207947 scopus 로고
    • The Schizosaccharomyces pombe cdc14 gene is required for septum formation and can also inhibit nuclear division
    • Fankhauser, C., and V. Simanis. 1993 The Schizosaccharomyces pombe cdc14 gene is required for septum formation and can also inhibit nuclear division. Mol. Biol Cell 4:531-539
    • (1993) Mol. Biol Cell , vol.4 , pp. 531-539
    • Fankhauser, C.1    Simanis, V.2
  • 16
    • 0025284833 scopus 로고
    • Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae
    • Fikes, J. D., D. M. Becker, F. Winston, and L. Guarente. 1990. Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae Nature (London) 346:291-294
    • (1990) Nature (London) , vol.346 , pp. 291-294
    • Fikes, J.D.1    Becker, D.M.2    Winston, F.3    Guarente, L.4
  • 17
    • 0344764944 scopus 로고
    • Cyclin-dependent kinases
    • J. R. Woodgett (ed.), IRL Press, Oxford
    • Gould, K. L. 1994 Cyclin-dependent kinases. In J. R. Woodgett (ed.), Protein kinases. IRL Press, Oxford.
    • (1994) Protein Kinases
    • Gould, K.L.1
  • 19
    • 0024959919 scopus 로고
    • - protein kinase regulates entry into mitosis
    • - protein kinase regulates entry into mitosis Nature (London) 342:39-45.
    • (1989) Nature (London) , vol.342 , pp. 39-45
    • Gould, K.L.1    Nurse, P.2
  • 20
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of Tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger, D. P., K. Hughes, J. R. Woodgett, J.-P. Brion, and B. H. Anderton. 1992. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of Tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci Lett. 147:58-62
    • (1992) Neurosci Lett. , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.-P.4    Anderton, B.H.5
  • 21
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database, identification of conserved features of primary structure and classification of family members
    • Hanks, S., and A. Quinn. 1991. Protein kinase catalytic domain sequence database, identification of conserved features of primary structure and classification of family members. Methods Enzymol 300:38-62.
    • (1991) Methods Enzymol , vol.300 , pp. 38-62
    • Hanks, S.1    Quinn, A.2
  • 22
    • 0028870305 scopus 로고
    • Glycogen synthase kinase-3 regulates cell fate in Dictyostelium
    • Harwood, A. J., S. E. Plyte, J. R. Woodgett, H. Strutt, and R. R. Kay. 1995. Glycogen synthase kinase-3 regulates cell fate in Dictyostelium. Cell 80: 139-148.
    • (1995) Cell , vol.80 , pp. 139-148
    • Harwood, A.J.1    Plyte, S.E.2    Woodgett, J.R.3    Strutt, H.4    Kay, R.R.5
  • 24
    • 0019630202 scopus 로고
    • Purification of glycogen synthase kinase 3 from rabbit skeletal muscle
    • Hemmings, B. A., D. Yellowlees, J. C. Kernohan, and P. Cohen. 1982 Purification of glycogen synthase kinase 3 from rabbit skeletal muscle Eur. J. Biochem. 119:443-451
    • (1982) Eur. J. Biochem. , vol.119 , pp. 443-451
    • Hemmings, B.A.1    Yellowlees, D.2    Kernohan, J.C.3    Cohen, P.4
  • 26
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • Hughes, K., E. Nikolakaki, S. E. Plyte, N. F. Totty, and J. R. Woodgett. 1993 Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J 12:803-808.
    • (1993) EMBO J , vol.12 , pp. 803-808
    • Hughes, K.1    Nikolakaki, E.2    Plyte, S.E.3    Totty, N.F.4    Woodgett, J.R.5
  • 27
    • 0026580539 scopus 로고
    • Baculovirus-mediated expression and characterisation of rat glycogen synthase kinase-3β, the mammalian homologue of the Drosophila melanogaster zeste-white-3 homeotic gene product
    • Hughes, K., B. J. Pulverer, P. Theocharous, and J. R. Woodgett. 1992 Baculovirus-mediated expression and characterisation of rat glycogen synthase kinase-3β, the mammalian homologue of the Drosophila melanogaster zeste-white-3 homeotic gene product. Eur. J. Biochem. 203:305-311.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 305-311
    • Hughes, K.1    Pulverer, B.J.2    Theocharous, P.3    Woodgett, J.R.4
  • 28
    • 0026488401 scopus 로고
    • Multifunctional ATP-citiate lyase kinase is a member of the glycosen synthase kinase-3 sub-family
    • Hughes, K., S. Ramakrishna, W. B. Benjamin, and J. R. Woodgett. 1992 Multifunctional ATP-citiate lyase kinase is a member of the glycosen synthase kinase-3 sub-family. Biochem. J. 228:309-314.
    • (1992) Biochem. J. , vol.228 , pp. 309-314
    • Hughes, K.1    Ramakrishna, S.2    Benjamin, W.B.3    Woodgett, J.R.4
  • 29
    • 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
  • 30
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to Immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins
    • Kamps, M. P., and B. M. Sefton. 1989. Acid and base hydrolysis of phosphoproteins bound to Immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Anal. Biochem. 176:22-27.
    • (1989) Anal. Biochem. , vol.176 , pp. 22-27
    • Kamps, M.P.1    Sefton, B.M.2
  • 31
    • 0344438664 scopus 로고
    • S6 kinases and MAP kinases sequential intermediates in insulin/mitogen-activated protein kinase cascades
    • J R. Woodgett (ed.), IRL Press, Oxford
    • Kyriakis, J. M., and J. Avruch. 1994. S6 kinases and MAP kinases sequential intermediates in insulin/mitogen-activated protein kinase cascades. In J R. Woodgett (ed.), Protein kinases IRL Press, Oxford.
    • (1994) Protein Kinases
    • Kyriakis, J.M.1    Avruch, J.2
  • 33
    • 0026566798 scopus 로고
    • Genetic interactions in the control of septation in Schizosaccharomyces pombe
    • Marks, J., C. Fankhauser, and V. Simanis. 1992. Genetic interactions in the control of septation in Schizosaccharomyces pombe. J. Cell Sci. 101:801-808
    • (1992) J. Cell Sci. , vol.101 , pp. 801-808
    • Marks, J.1    Fankhauser, C.2    Simanis, V.3
  • 34
    • 0022395329 scopus 로고
    • Localization of F-actin through the cell division cycle of Schizosaccharomyces pombe
    • Marks, J., and J. S. Hyams. 1985. Localization of F-actin through the cell division cycle of Schizosaccharomyces pombe. Eur. J. Cell Biol. 39:27-32
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 27-32
    • Marks, J.1    Hyams, J.S.2
  • 35
    • 0023895153 scopus 로고
    • Role of segment polarity genes in the definition and maintenance of cell states in the Drosophila embryo
    • Martinez-Arias, A., N. E. Baker, and P. W. Ingham. 1988. Role of segment polarity genes in the definition and maintenance of cell states in the Drosophila embryo. Development 103:157-170
    • (1988) Development , vol.103 , pp. 157-170
    • Martinez-Arias, A.1    Baker, N.E.2    Ingham, P.W.3
  • 36
    • 0027390036 scopus 로고
    • Thiamine-repressible expression vectors pREP and pRIP for fission yeast
    • Maundrell, K. 1993 Thiamine-repressible expression vectors pREP and pRIP for fission yeast Gene 123:127-130
    • (1993) Gene , vol.123 , pp. 127-130
    • Maundrell, K.1
  • 37
    • 0026025891 scopus 로고
    • Molecular and genetic analysis of fission yeast Schizosaccharomyces pombe
    • Moreno, S., A. Klar, and P. Nurse. 1991. Molecular and genetic analysis of fission yeast Schizosaccharomyces pombe. Methods Enzymol. 194:795-823
    • (1991) Methods Enzymol. , vol.194 , pp. 795-823
    • Moreno, S.1    Klar, A.2    Nurse, P.3
  • 38
    • 0025860025 scopus 로고
    • The yeast MCK1 gene encodes a protein kinase homolog that activates early meiotic gene expression
    • Neigheborn, L., and A. P. Mitchell. 1991. The yeast MCK1 gene encodes a protein kinase homolog that activates early meiotic gene expression Genes Dev. 5:533-548.
    • (1991) Genes Dev. , vol.5 , pp. 533-548
    • Neigheborn, L.1    Mitchell, A.P.2
  • 39
    • 0027512538 scopus 로고
    • Glycogen synthase kinase-3 phosphorylates Jun-family members in vitro and negatively regulates their transactivating potential in intact cells
    • Nikolakaki, E., P. Coffer, R. Hemelsoet, J. R. Woodgett, and L. H. K. Defize. 1993. Glycogen synthase kinase-3 phosphorylates Jun-family members in vitro and negatively regulates their transactivating potential in intact cells Oncogene 8:833-840.
    • (1993) Oncogene , vol.8 , pp. 833-840
    • Nikolakaki, E.1    Coffer, P.2    Hemelsoet, R.3    Woodgett, J.R.4    Defize, L.H.K.5
  • 40
    • 0017157413 scopus 로고
    • Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe
    • Nurse, P., P. Thuriaux, and K. Nasmyth. 1976. Genetic control of the cell division cycle in the fission yeast Schizosaccharomyces pombe. Mol. Gen Genet. 146:167-178
    • (1976) Mol. Gen Genet. , vol.146 , pp. 167-178
    • Nurse, P.1    Thuriaux, P.2    Nasmyth, K.3
  • 41
    • 0024455520 scopus 로고
    • Multiple functions of a Drosophila homeotic gene, zeste-white3, during segmentation and neurogenesis
    • Perrimon, N., and D. Smouse. 1989. Multiple functions of a Drosophila homeotic gene, zeste-white3, during segmentation and neurogenesis. Dev Biol. 135:287-305.
    • (1989) Dev Biol. , vol.135 , pp. 287-305
    • Perrimon, N.1    Smouse, D.2
  • 42
    • 0028935672 scopus 로고
    • Regulation of Spemann organizer by the intracellular kinase Xgsk-3
    • Pierce, S. B., and D. Kimelman. 1995 Regulation of Spemann organizer by the intracellular kinase Xgsk-3. Development 121:755.
    • (1995) Development , vol.121 , pp. 755
    • Pierce, S.B.1    Kimelman, D.2
  • 44
    • 0026526918 scopus 로고
    • High efficiency transformation of Schizosaccharomyces pombe by electioporation
    • Prentice, H. L. 1991 High efficiency transformation of Schizosaccharomyces pombe by electioporation. Nucleic Acids Res. 20:621.
    • (1991) Nucleic Acids Res. , vol.20 , pp. 621
    • Prentice, H.L.1
  • 46
    • 0027972558 scopus 로고
    • MDS1, a dosage suppressor of an mck1 mutant, encodes a putative yeast homolog of glycogen synthase kinase 3
    • Puziss, J. W., T. A. Hardy, R. B. Johnson, P. J. Roach, and P. Hieter. 1994. MDS1, a dosage suppressor of an mck1 mutant, encodes a putative yeast homolog of glycogen synthase kinase 3. Mol. Cell. Biol. 14:831-839.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 831-839
    • Puziss, J.W.1    Hardy, T.A.2    Johnson, R.B.3    Roach, P.J.4    Hieter, P.5
  • 47
    • 0025102029 scopus 로고
    • Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3-like kinase)
    • Ramakrishna, S., G. D'Angelo, and W. B. Benjamin. 1990. Sequence of sites on ATP-citrate lyase and phosphatase inhibitor 2 phosphorylated by multifunctional protein kinase (a glycogen synthase kinase 3-like kinase) Biochemistry 29:7617-7624.
    • (1990) Biochemistry , vol.29 , pp. 7617-7624
    • Ramakrishna, S.1    D'Angelo, G.2    Benjamin, W.B.3
  • 48
    • 0027418602 scopus 로고
    • Drosophila shaggy kinase and rat glycogen synthase kinase-3 have conserved activities and act downstream of Notch
    • Ruel, L., M. Bourouis, P. Heitzler, V. Pantesco, and P. Simpson. 1993. Drosophila shaggy kinase and rat glycogen synthase kinase-3 have conserved activities and act downstream of Notch. Nature (London) 362:557-560.
    • (1993) Nature (London) , vol.362 , pp. 557-560
    • Ruel, L.1    Bourouis, M.2    Heitzler, P.3    Pantesco, V.4    Simpson, P.5
  • 49
    • 0019025978 scopus 로고
    • Glycogen synthase kinase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase
    • Rylatt, D. B., A. Aitken, T. Bilham, G. D. Condon, N. Embi, and P. Cohen. 1980 Glycogen synthase kinase from rabbit skeletal muscle. Amino acid sequence at the sites phosphorylated by glycogen synthase kinase-3, and extension of the N-terminal sequence containing the site phosphorylated by phosphorylase kinase. Eur J. Biochem. 107:529-537.
    • (1980) Eur J. Biochem. , vol.107 , pp. 529-537
    • Rylatt, D.B.1    Aitken, A.2    Bilham, T.3    Condon, G.D.4    Embi, N.5    Cohen, P.6
  • 51
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa
    • Schagger, H., and G. Von Jagow. 1987. Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 52
    • 0025911366 scopus 로고
    • A suppressor of a centromere DNA mutation encodes a putative protein kinase (MCK1)
    • Shero, J. H., and P. Hieter. 1991 A suppressor of a centromere DNA mutation encodes a putative protein kinase (MCK1). Genes Dev 5:549-560.
    • (1991) Genes Dev , vol.5 , pp. 549-560
    • Shero, J.H.1    Hieter, P.2
  • 54
    • 0027070855 scopus 로고
    • Wingless signalling acts through zeste-white3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate
    • Siegfried, E., T. Chou, and N. Perrimon. 1992. wingless signalling acts through zeste-white3, the Drosophila homolog of glycogen synthase kinase-3, to regulate engrailed and establish cell fate Cell 71:1167-1179.
    • (1992) Cell , vol.71 , pp. 1167-1179
    • Siegfried, E.1    Chou, T.2    Perrimon, N.3
  • 55
    • 0025322840 scopus 로고
    • Putative protein kinase product of the Drosophila segment polarity gene, zeste-white 3
    • Siegfried, E., L. A. Perkins, T. M. Capaci, and N. Perrimon. 1990. Putative protein kinase product of the Drosophila segment polarity gene, zeste-white 3. Nature (London) 345:825-829.
    • (1990) Nature (London) , vol.345 , pp. 825-829
    • Siegfried, E.1    Perkins, L.A.2    Capaci, T.M.3    Perrimon, N.4
  • 56
    • 0027515127 scopus 로고
    • Inactivation of glycogen synthase kinase-3β by phosphorylation; new kinase connections in insulin and growth factor signalling
    • Southerland, C., I. Leighton, and P. Cohen. 1993. Inactivation of glycogen synthase kinase-3β by phosphorylation; new kinase connections in insulin and growth factor signalling Biochem J 296:15-19
    • (1993) Biochem J , vol.296 , pp. 15-19
    • Southerland, C.1    Leighton, I.2    Cohen, P.3
  • 57
    • 0027960448 scopus 로고
    • Mitogen inactivation of glycogen synthase kinase-3β in intact cells via serine 9 phosphorylation
    • Stambolic, V., and J. R. Woodgett. 1994. Mitogen inactivation of glycogen synthase kinase-3β in intact cells via serine 9 phosphorylation. Biochem. J 303:701.
    • (1994) Biochem. J , vol.303 , pp. 701
    • Stambolic, V.1    Woodgett, J.R.2
  • 58
    • 0028176021 scopus 로고
    • Glycogen synthase kinase-3β is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation
    • Wang, Q. M., C. J. Fiol, A. A. DePaoli-Roach, and P. J. Roach. 1994. Glycogen synthase kinase-3β is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation. J Biol. Chem. 269: 14566.
    • (1994) J Biol. Chem. , vol.269 , pp. 14566
    • Wang, Q.M.1    Fiol, C.J.2    DePaoli-Roach, A.A.3    Roach, P.J.4
  • 59
    • 0027430039 scopus 로고
    • Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B
    • Welsh, G. I., and C. G. Proud. 1993 Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B Biochem. J. 295:625-629.
    • (1993) Biochem. J. , vol.295 , pp. 625-629
    • Welsh, G.I.1    Proud, C.G.2
  • 60
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • Woodgett, J. R. 1990. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J 9:2431-2438
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1


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