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Volumn 60, Issue 3, 2000, Pages 211-246

Casein kinase 2 as a potentially important enzyme in the nervous system

Author keywords

[No Author keywords available]

Indexed keywords

BETA TUBULIN; CASEIN KINASE II; CELL ADHESION MOLECULE; HEAT SHOCK PROTEIN 90; ISOENZYME; MESSENGER RNA; MICROTUBULE ASSOCIATED PROTEIN 1; MYOSIN HEAVY CHAIN; NEUROMODULIN; PHOSPHATASE; PHOSPHOPROTEIN DARPP 32; PROTEIN KINASE; PROTEIN P53; SPECTRIN; SYNAPTOTAGMIN; TAU PROTEIN; TRANSCRIPTION FACTOR; VITRONECTIN;

EID: 0033991008     PISSN: 03010082     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-0082(99)00026-X     Document Type: Review
Times cited : (155)

References (372)
  • 1
    • 0032588901 scopus 로고    scopus 로고
    • Protein kinase CK2 alpha may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor
    • Ackermann K., Pyerin W. Protein kinase CK2 alpha may induce gene expression but unlikely acts directly as a DNA-binding transcription-activating factor. Mol. cell. Biochem. 191:1999;129-134.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 129-134
    • Ackermann, K.1    Pyerin, W.2
  • 2
    • 0005123113 scopus 로고
    • Phosphorylation of DNA topoisomerase 2 by casein kinase 2: Modulation of eukaryotic topoisomerase 2 activity in vitro
    • Ackerman P., Glover C.V.C., Osheroff N. Phosphorylation of DNA topoisomerase 2 by casein kinase 2: modulation of eukaryotic topoisomerase 2 activity in vitro. Proc. natl Acad. Sci. USA. 82:1985;3164-3168.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3164-3168
    • Ackerman, P.1    Glover, C.V.C.2    Osheroff, N.3
  • 3
    • 0025176634 scopus 로고
    • Stimulation of casein kinase 2 by epidermal growth factor: Relationship between the physiological activity of the kinase and the phosphorylation state of its β subunit
    • Ackerman P., Glover C.V.C., Osheroff N. Stimulation of casein kinase 2 by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its β subunit. Proc. natl Acad. Sci. USA. 87:1990;821-825.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 821-825
    • Ackerman, P.1    Glover, C.V.C.2    Osheroff, N.3
  • 5
    • 0023657062 scopus 로고
    • Regulation of casein kinase 2 by phosphorylation/dephosphorylation
    • Agostinis P., Goris J., Pinna L.A., Merlevede W. Regulation of casein kinase 2 by phosphorylation/dephosphorylation. Biochem. J. 248:1987;785-789.
    • (1987) Biochem. J. , vol.248 , pp. 785-789
    • Agostinis, P.1    Goris, J.2    Pinna, L.A.3    Merlevede, W.4
  • 6
    • 0027787884 scopus 로고
    • Cloning of cDNAs encoding the α and β subunits of rat casein kinase 2 (CK-2): Investigation of molecular regulation of CK-2 by androgens in rat ventral prostate
    • Ahmed K., Davis A., Hanten J., Lambert D., MacIvor R.S., Goueli S.A. Cloning of cDNAs encoding the α and β subunits of rat casein kinase 2 (CK-2): investigation of molecular regulation of CK-2 by androgens in rat ventral prostate. Cell. Mol. Biol. Res. 39:1993;451-462.
    • (1993) Cell. Mol. Biol. Res. , vol.39 , pp. 451-462
    • Ahmed, K.1    Davis, A.2    Hanten, J.3    Lambert, D.4    MacIvor, R.S.5    Goueli, S.A.6
  • 7
    • 0027232510 scopus 로고
    • Association of casein kinase 2 with nuclear chromatin in relation to androgenic regulation of rat prostate
    • Ahmed K., Yenice S., Davis A., Goueli S.A. Association of casein kinase 2 with nuclear chromatin in relation to androgenic regulation of rat prostate. Proc. natl Acad. Sci. USA. 90:1993;4426-4430.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4426-4430
    • Ahmed, K.1    Yenice, S.2    Davis, A.3    Goueli, S.A.4
  • 8
    • 0026074840 scopus 로고
    • The decreased level of casein kinase-2 in brain cortex of schizophrenic and Alzheimer's disease patients
    • Aksenova M.V., Burbaeva G.Sh., Kandror K.V., Kapkov D.V., Stepanov A.S. The decreased level of casein kinase-2 in brain cortex of schizophrenic and Alzheimer's disease patients. FEBS Lett. 279:1991;55-57.
    • (1991) FEBS Lett. , vol.279 , pp. 55-57
    • Aksenova, M.V.1    Burbaeva, G.sh.2    Kandror, K.V.3    Kapkov, D.V.4    Stepanov, A.S.5
  • 9
    • 0028909420 scopus 로고
    • Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation
    • Allende J.E., Allende C.C. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J. 9:1995;313-323.
    • (1995) FASEB J. , vol.9 , pp. 313-323
    • Allende, J.E.1    Allende, C.C.2
  • 10
    • 0028951351 scopus 로고
    • Differential binding of oocyte-type and somatic-type 5S rRNA to TF3A and ribosomal protein L5 in Xenopus oocytes: Specialization for storage versus mobilization
    • Allison L.A., North M.T., Neville L.A. Differential binding of oocyte-type and somatic-type 5S rRNA to TF3A and ribosomal protein L5 in Xenopus oocytes: specialization for storage versus mobilization. Dev. Biol. 168:1995;284-295.
    • (1995) Dev. Biol. , vol.168 , pp. 284-295
    • Allison, L.A.1    North, M.T.2    Neville, L.A.3
  • 11
    • 0029846841 scopus 로고    scopus 로고
    • Cloning, expression and properties of the α′ subunit of casein kinase 2 from zebrafish (Danio rerio)
    • Antonelli M., Daniotti J., Rojo D., Allende C.C., Allende J.E. Cloning, expression and properties of the α′ subunit of casein kinase 2 from zebrafish (Danio rerio). Eur. J. Biochem. 241:1996;272-279.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 272-279
    • Antonelli, M.1    Daniotti, J.2    Rojo, D.3    Allende, C.C.4    Allende, J.E.5
  • 12
    • 0030973394 scopus 로고    scopus 로고
    • Casein kinase 2-mediated phosphorylation of the C-terminus of spl decreases its DNA binding activity
    • Armstrong S.A., Barry D.A., Leggett R.W., Mueller C.R. Casein kinase 2-mediated phosphorylation of the C-terminus of spl decreases its DNA binding activity. J. Biol. Chem. 272:1997;13489-13495.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13489-13495
    • Armstrong, S.A.1    Barry, D.A.2    Leggett, R.W.3    Mueller, C.R.4
  • 13
    • 0028850007 scopus 로고
    • Phosphorylation of the human estrogen receptor by mitogen-activated protein kinase and casein kinase 2: Consequence on DNA binding
    • Arnold S.F., Obourn J.D., Jaffe H., Notides A.C. Phosphorylation of the human estrogen receptor by mitogen-activated protein kinase and casein kinase 2: consequence on DNA binding. J. Steroid Biochem. Molec. Biol. 55:1995;163-172.
    • (1995) J. Steroid Biochem. Molec. Biol. , vol.55 , pp. 163-172
    • Arnold, S.F.1    Obourn, J.D.2    Jaffe, H.3    Notides, A.C.4
  • 14
    • 0019315229 scopus 로고
    • Opposing kinetic effects of an acidic nucleolar phosphoprotein from Physarum polycephalum on homologous and heterologous transcription systems
    • Atmar V.J., Daniels G.R., Kuehn G.D., Braun R. Opposing kinetic effects of an acidic nucleolar phosphoprotein from Physarum polycephalum on homologous and heterologous transcription systems. FEBS Lett. 114:1980;205-208.
    • (1980) FEBS Lett. , vol.114 , pp. 205-208
    • Atmar, V.J.1    Daniels, G.R.2    Kuehn, G.D.3    Braun, R.4
  • 15
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dentrite
    • Baas P.W., Deitch J.S., Black M.M., Banker G.A. Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dentrite. Proc. natl Acad. Sci. USA. 85:1988;8335-8339.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8335-8339
    • Baas, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 16
    • 0028931552 scopus 로고
    • Neurotrophic factors and their receptors
    • Barbacid M. Neurotrophic factors and their receptors. Curr. Opin. cell. Biol. 7:1995;148-155.
    • (1995) Curr. Opin. Cell. Biol. , vol.7 , pp. 148-155
    • Barbacid, M.1
  • 18
    • 0026513834 scopus 로고
    • Casein kinase 2 is associated with neurofibrillary tangles but is not an intrinsic component of paired helical filaments
    • Baum L., Masliah E., Imoto S., Hansen L.A., Halliday W.C., Saitoh T. Casein kinase 2 is associated with neurofibrillary tangles but is not an intrinsic component of paired helical filaments. Brain Res. 593:1992;126-132.
    • (1992) Brain Res. , vol.593 , pp. 126-132
    • Baum, L.1    Masliah, E.2    Imoto, S.3    Hansen, L.A.4    Halliday, W.C.5    Saitoh, T.6
  • 19
    • 0022544235 scopus 로고
    • The acidic peptide-specific type 2 protein kinases from the nucleus and the cytosol of porcine liver nuclei
    • Baydoun P., Feth F., Hoppe J., Erdmann H., Wagner K.G. The acidic peptide-specific type 2 protein kinases from the nucleus and the cytosol of porcine liver nuclei. Arch. Biochem. Biophys. 245:1986;504-511.
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 504-511
    • Baydoun, P.1    Feth, F.2    Hoppe, J.3    Erdmann, H.4    Wagner, K.G.5
  • 21
    • 0033040261 scopus 로고    scopus 로고
    • Binding of polylysine to protein kinase CK2, measured by surface plasmon resonance
    • Benitez M.J., Mier G., Brione F., Moreno F.J., Jimenez J.S. Binding of polylysine to protein kinase CK2, measured by surface plasmon resonance. Mol. cell. Biochem. 191:1999;29-33.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 29-33
    • Benitez, M.J.1    Mier, G.2    Brione, F.3    Moreno, F.J.4    Jimenez, J.S.5
  • 22
    • 0027511827 scopus 로고
    • Casein kinase 2 phosphorylates the synaptic vesicle protein p65
    • Bennett M.K., Miller K.G., Scheller R.H. Casein kinase 2 phosphorylates the synaptic vesicle protein p65. J. Neurosci. 13:1993;1701-1707.
    • (1993) J. Neurosci. , vol.13 , pp. 1701-1707
    • Bennett, M.K.1    Miller, K.G.2    Scheller, R.H.3
  • 23
    • 0031027044 scopus 로고    scopus 로고
    • GAP-43: An intrinsic determinant of neuronal development and plasticity
    • Benowitz L.I., Routtenberg A. GAP-43: an intrinsic determinant of neuronal development and plasticity. Trends Neurosci. 20:1997;84-91.
    • (1997) Trends Neurosci. , vol.20 , pp. 84-91
    • Benowitz, L.I.1    Routtenberg, A.2
  • 24
    • 0026554939 scopus 로고
    • Casein kinase 2 inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers
    • Berberich S.J., Cole M.D. Casein kinase 2 inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev. 6:1992;166-176.
    • (1992) Genes Dev. , vol.6 , pp. 166-176
    • Berberich, S.J.1    Cole, M.D.2
  • 25
    • 0027292675 scopus 로고
    • Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2
    • Beretta L., Dobransky T., Sobel A. Multiple phosphorylation of stathmin. Identification of four sites phosphorylated in intact cells and in vitro by cyclic AMP-dependent protein kinase and p34cdc2. J. biol. Chem. 268:1993;20076-20084.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20076-20084
    • Beretta, L.1    Dobransky, T.2    Sobel, A.3
  • 26
    • 0028287642 scopus 로고
    • Casein kinase 2 of Saccharomyces cerevisiae contains two distinct regulatory subunits, β and β′
    • Birwai A.P., Reed J.C., Glover C.V.C. Casein kinase 2 of Saccharomyces cerevisiae contains two distinct regulatory subunits, β and β′ Arch. Biochem. Biophys. 309:1994;348-355.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 348-355
    • Birwai, A.P.1    Reed, J.C.2    Glover, C.V.C.3
  • 27
    • 0031862763 scopus 로고    scopus 로고
    • Neurotrophin-induced activation of casein kinase 2 in rat hippocampal slices
    • Blanquet P.R. Neurotrophin-induced activation of casein kinase 2 in rat hippocampal slices. Neuroscience. 86:1998;739-749.
    • (1998) Neuroscience , vol.86 , pp. 739-749
    • Blanquet, P.R.1
  • 28
    • 0030869405 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase 2 activity in hippocampus
    • 2+/calmodulin-dependent protein kinase 2 activity in hippocampus. J. biol. Chem. 272:1997;24133-24136.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24133-24136
    • Blanquet, P.R.1    Lamour, Y.2
  • 29
    • 0024289918 scopus 로고
    • Primary structure and expression of a product from cut, a locus involved in specifying sensory organ identity in drosophila
    • Blochlinger K., Bodmer R., Jack J., Jan L.Y., Jan Y.N. Primary structure and expression of a product from cut, a locus involved in specifying sensory organ identity in drosophila. Nature. 333:1988;629-635.
    • (1988) Nature , vol.333 , pp. 629-635
    • Blochlinger, K.1    Bodmer, R.2    Jack, J.3    Jan, L.Y.4    Jan, Y.N.5
  • 30
    • 0028036142 scopus 로고
    • Recombinant human casein kinase 2. A study with the complete set of subunits (α, α′, and β), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme
    • Bodenbach L., Fauss J., Robitzki A., Krehan A., Lorenz P., Lozeman F.J., Pyerin W. Recombinant human casein kinase 2. A study with the complete set of subunits (α, α′, and β), site-directed autophosphorylation mutants and a bicistronically expressed holoenzyme. Eur. J. Biochem. 220:1994;263-273.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 263-273
    • Bodenbach, L.1    Fauss, J.2    Robitzki, A.3    Krehan, A.4    Lorenz, P.5    Lozeman, F.J.6    Pyerin, W.7
  • 31
    • 0027433079 scopus 로고
    • DNA topoisomerase 2 and casein kinase 2 associate in a molecular complex that is catalytically active
    • Bojanowski K., Filhol O., Cochet C., Chambaz E.M., Larsen A.K. DNA topoisomerase 2 and casein kinase 2 associate in a molecular complex that is catalytically active. J. biol. Chem. 268:1993;22920-22926.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22920-22926
    • Bojanowski, K.1    Filhol, O.2    Cochet, C.3    Chambaz, E.M.4    Larsen, A.K.5
  • 32
    • 0031050906 scopus 로고    scopus 로고
    • A-Raf kinase is a new interacting partner of protein kinase CK2 β subunit
    • Boldyreff B., Issinger O.-G. A-Raf kinase is a new interacting partner of protein kinase CK2 β subunit. FEBS Lett. 403:1997;197-199.
    • (1997) FEBS Lett. , vol.403 , pp. 197-199
    • Boldyreff, B.1    Issinger, O.-G.2
  • 33
    • 0026026332 scopus 로고
    • The β subunit of CK2: Cloning of cDNAs from murine and porcine origin and expression of the porcine sequence as a fusion protein
    • Boldyreff B., Piontek K., Schmidt Spaniol I., Issinger O.-G. The β subunit of CK2: cloning of cDNAs from murine and porcine origin and expression of the porcine sequence as a fusion protein. Biochim. Biophys. Acta. 1088:1991;439-441.
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 439-441
    • Boldyreff, B.1    Piontek, K.2    Schmidt Spaniol, I.3    Issinger, O.-G.4
  • 34
    • 0026474670 scopus 로고
    • Casein kinase 2 structure-function relationship: Creation of a set mutants of the β subunit that variably surrogate the wildtype β subunit function
    • Boldyreff B., Meggio F., Pina L.A., Issinger O.-G. Casein kinase 2 structure-function relationship: creation of a set mutants of the β subunit that variably surrogate the wildtype β subunit function. Biochem. biophys. Res. Commun. 188:1992;228-234.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 228-234
    • Boldyreff, B.1    Meggio, F.2    Pina, L.A.3    Issinger, O.-G.4
  • 36
    • 0027133632 scopus 로고
    • Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated β-subunits
    • Boldyreff B., Meggio F., Pinna L.A., Issinger O.-G. Reconstitution of normal and hyperactivated forms of casein kinase-2 by variably mutated β-subunits. Biochemistry. 32:1993;12672-12677.
    • (1993) Biochemistry , vol.32 , pp. 12672-12677
    • Boldyreff, B.1    Meggio, F.2    Pinna, L.A.3    Issinger, O.-G.4
  • 37
    • 0027937388 scopus 로고
    • Efficient autophosphorylation and phosphorylation of the β-subunit by casein-kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site
    • Boldyreff B., Meggio F., Pina L.A., Issinger O.-G. Efficient autophosphorylation and phosphorylation of the β-subunit by casein-kinase-2 require the integrity of an acidic cluster 50 residues downstream from the phosphoacceptor site. J. biol. Chem. 269:1994;4827-4831.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4827-4831
    • Boldyreff, B.1    Meggio, F.2    Pina, L.A.3    Issinger, O.-G.4
  • 38
    • 0030028702 scopus 로고    scopus 로고
    • Structure of protein kinase CK2: Dimerization of the human β-subunit
    • Boldyreff B., Mietens U., Issinger O.-G. Structure of protein kinase CK2: dimerization of the human β-subunit. FEBS Lett. 379:1996;153-156.
    • (1996) FEBS Lett. , vol.379 , pp. 153-156
    • Boldyreff, B.1    Mietens, U.2    Issinger, O.-G.3
  • 40
  • 42
    • 0030027917 scopus 로고    scopus 로고
    • Nuclear import of protein kinases and cyclins
    • Boulikas T. Nuclear import of protein kinases and cyclins. J. cell. Biochem. 60:1996;61-82.
    • (1996) J. Cell. Biochem. , vol.60 , pp. 61-82
    • Boulikas, T.1
  • 43
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
    • Boyle W.J., Smeal T., Defize L.H.K., Angel P., Woodgett J.R., Karin M., Hunter T. Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell. 64:1991;573-584.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.K.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6    Hunter, T.7
  • 44
    • 0002398332 scopus 로고
    • Ig superfamily adhesion molecules in the vertebrate nervous system: Binding partners and signal transduction during axon growth
    • Burden-Gulley S.M., Lemmon V. Ig superfamily adhesion molecules in the vertebrate nervous system: binding partners and signal transduction during axon growth. Semin. Dev. Biol. 6:1995;79-87.
    • (1995) Semin. Dev. Biol. , vol.6 , pp. 79-87
    • Burden-Gulley, S.M.1    Lemmon, V.2
  • 45
    • 0024266671 scopus 로고
    • Dentrites of mitral cell neurons contain microtubules of opposite polarity
    • Burton P.R. Dentrites of mitral cell neurons contain microtubules of opposite polarity. Brain Res. 473:1988;107-115.
    • (1988) Brain Res. , vol.473 , pp. 107-115
    • Burton, P.R.1
  • 46
    • 0031006320 scopus 로고    scopus 로고
    • LTP, NMDA, genes and learning
    • Cain D.P. LTP, NMDA, genes and learning. Curr. Opin. Neurobiol. 7:1997;235-242.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 235-242
    • Cain, D.P.1
  • 48
    • 0027413177 scopus 로고
    • Regulation of topoisomerase 2 by phosphorylation: A role for casein kinase 2
    • Cardenas M.E.M., Gasser S.M. Regulation of topoisomerase 2 by phosphorylation: a role for casein kinase 2. J. Cell Sci. 104:1993;219-225.
    • (1993) J. Cell Sci. , vol.104 , pp. 219-225
    • Cardenas, M.E.M.1    Gasser, S.M.2
  • 50
    • 0024582988 scopus 로고
    • Serum-stimulated cell growth causes oscillations in casein kinase 2 activity
    • Carrol D., Marshak D. Serum-stimulated cell growth causes oscillations in casein kinase 2 activity. J. biol. Chem. 264:1989;7345-7348.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7345-7348
    • Carrol, D.1    Marshak, D.2
  • 51
    • 0024147615 scopus 로고
    • Regulating cell growth: Casein-kinase-2-dependent phosphorylation of nuclear oncoproteins
    • Carroll D., Santoro N., Marshak D.R. Regulating cell growth: casein-kinase-2-dependent phosphorylation of nuclear oncoproteins. Cold Spring Harbor Symp. Quant. Biol. 53:1988;91-95.
    • (1988) Cold Spring Harbor Symp. Quant. Biol. , vol.53 , pp. 91-95
    • Carroll, D.1    Santoro, N.2    Marshak, D.R.3
  • 52
    • 0023009331 scopus 로고
    • Amino acid sequence of protein B23 phosphorylation site
    • Chan P.-K., Aldrich M., Cook R.G., Bush H. Amino acid sequence of protein B23 phosphorylation site. J. biol. Chem. 261:1986;1868-1872.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1868-1872
    • Chan, P.-K.1    Aldrich, M.2    Cook, R.G.3    Bush, H.4
  • 53
    • 0032416988 scopus 로고    scopus 로고
    • Ethanol tolerance and synaptic plasticity
    • Chandler L.J., Harris R.A., Crews F.T. Ethanol tolerance and synaptic plasticity. TIPS. 19:1998;491-495.
    • (1998) TIPS , vol.19 , pp. 491-495
    • Chandler, L.J.1    Harris, R.A.2    Crews, F.T.3
  • 55
    • 0030948574 scopus 로고    scopus 로고
    • The casein kinase 2 β subunit binds to Mos and inhibits Mos activity
    • Chen M., Li D., Krebs E.G., Cooper J.A. The casein kinase 2 β subunit binds to Mos and inhibits Mos activity. Mol. cell. Biol. 17:1997;1904-1912.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1904-1912
    • Chen, M.1    Li, D.2    Krebs, E.G.3    Cooper, J.A.4
  • 56
    • 0023739122 scopus 로고
    • Isolation, sequencing and distribution of the CKA1 gene encoding the α subunit of yeast casein kinase 2
    • Chen-Wu J., Padmanabha R., Glover C. Isolation, sequencing and distribution of the CKA1 gene encoding the α subunit of yeast casein kinase 2. Mol. cell. Biol. 8:1988;4981-4990.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4981-4990
    • Chen-Wu, J.1    Padmanabha, R.2    Glover, C.3
  • 57
    • 0028965096 scopus 로고
    • Identification and characterization of protein kinase CK2 isoforms in HeLa cells
    • Chester N., Yu I.J., Marshak D.R. Identification and characterization of protein kinase CK2 isoforms in HeLa cells. J. biol. Chem. 270:1995;7501-7514.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7501-7514
    • Chester, N.1    Yu, I.J.2    Marshak, D.R.3
  • 58
    • 0026581191 scopus 로고
    • Interferon action: Nucleolar and nucleoplasmic localization of the interferon-inductible 72-kD protein that is encoded by the Ifi204 gene from the gene 200 cluster
    • Choubey D., Lengyel P. Interferon action: nucleolar and nucleoplasmic localization of the interferon-inductible 72-kD protein that is encoded by the Ifi204 gene from the gene 200 cluster. J. Cell Biol. 116:1992;1333-1341.
    • (1992) J. Cell Biol. , vol.116 , pp. 1333-1341
    • Choubey, D.1    Lengyel, P.2
  • 59
    • 0029808167 scopus 로고    scopus 로고
    • Basal phosphorylation of the PEST domain in IκBβ regulates its functional interaction with the C-rel proto-oncogene product
    • Chu Z-L., McKinsley T.A., Liu L., Qi X., Ballard D.W. Basal phosphorylation of the PEST domain in IκBβ regulates its functional interaction with the C-rel proto-oncogene product. Mol. cell. Biol. 16:1996;5974-5984.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5974-5984
    • Chu, Z.-L.1    McKinsley, T.A.2    Liu, L.3    Qi, X.4    Ballard, D.W.5
  • 60
    • 0022239633 scopus 로고
    • Phosphorylation of membrane proteins by cytosolic casein kinases in human erythrocytes. Effect of monovalent ions, 2,3-bisphosphoglycerate and spermine
    • Clari G., Moret V. Phosphorylation of membrane proteins by cytosolic casein kinases in human erythrocytes. Effect of monovalent ions, 2,3-bisphosphoglycerate and spermine. Mol. cell. Biochem. 68:1985;181-187.
    • (1985) Mol. Cell. Biochem. , vol.68 , pp. 181-187
    • Clari, G.1    Moret, V.2
  • 61
    • 0024294245 scopus 로고
    • Structure and phosphorylation of eukaryotic initiation factor 2. Casein kinase 2 and protein kinase C phosphorylate distinct but adjacent sites in the β-subunit
    • Clark S.J., Colthurst D.R., Proud C.G. Structure and phosphorylation of eukaryotic initiation factor 2. Casein kinase 2 and protein kinase C phosphorylate distinct but adjacent sites in the β-subunit. Biochim. biophys. Acta. 968:1988;211-219.
    • (1988) Biochim. Biophys. Acta , vol.968 , pp. 211-219
    • Clark, S.J.1    Colthurst, D.R.2    Proud, C.G.3
  • 62
    • 0021099186 scopus 로고
    • Oligomeric structure and catalytic activity of G type casein kinase
    • Cochet C., Chambaz E.M. Oligomeric structure and catalytic activity of G type casein kinase. J. biol. Chem. 258:1983;1403-1406.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1403-1406
    • Cochet, C.1    Chambaz, E.M.2
  • 63
    • 0018875784 scopus 로고
    • Adenosine 3′,5′-monophosphate-independent protein kinase activities in the bovine adrenal cortex cytosol
    • Cochet C., Job D., Pirollet F., Chambaz E.M. Adenosine 3′,5′-monophosphate-independent protein kinase activities in the bovine adrenal cortex cytosol. Endocrinology. 106:1980;750-757.
    • (1980) Endocrinology , vol.106 , pp. 750-757
    • Cochet, C.1    Job, D.2    Pirollet, F.3    Chambaz, E.M.4
  • 66
    • 0023869380 scopus 로고
    • Insulin action inhibits insulin-like growth factor-2 (IGF-2) receptor phosphorylation in H-35 hepatoma cells
    • Corvera S., Roach P.J., De Paoli-Roach A.A., Czech M.P. Insulin action inhibits insulin-like growth factor-2 (IGF-2) receptor phosphorylation in H-35 hepatoma cells. J. biol. Chem. 263:1988;3116-3122.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3116-3122
    • Corvera, S.1    Roach, P.J.2    De Paoli-Roach, A.A.3    Czech, M.P.4
  • 69
    • 0030272681 scopus 로고    scopus 로고
    • Evidence for the Hebbian hypothesis in experience-dependent physiological plasticity of neocortex: A critical review
    • Cruikshank S., Weinberger N.M. Evidence for the Hebbian hypothesis in experience-dependent physiological plasticity of neocortex: a critical review. Brain Res. Rev. 22:1996;191-228.
    • (1996) Brain Res. Rev. , vol.22 , pp. 191-228
    • Cruikshank, S.1    Weinberger, N.M.2
  • 70
    • 0027267423 scopus 로고
    • Insulin induces the phosphorylation of nucleolin. A possible mechanism of insulin-induced RNA efflux from nuclei
    • Csermely P., Schnaider T., Cheatham B., Olson M.O.J., Kahn C.R. Insulin induces the phosphorylation of nucleolin. A possible mechanism of insulin-induced RNA efflux from nuclei. J. biol. Chem. 268:1993;9747-9752.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9747-9752
    • Csermely, P.1    Schnaider, T.2    Cheatham, B.3    Olson, M.O.J.4    Kahn, C.R.5
  • 71
    • 0019876755 scopus 로고
    • Purification and properties of calf thymus casein kinases 1 and 2
    • Dahmus M.E. Purification and properties of calf thymus casein kinases 1 and 2. J. biol. Chem. 256:1981;3319-3325.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3319-3325
    • Dahmus, M.E.1
  • 72
    • 0019877637 scopus 로고
    • Calf thymus RNA polymerase 1 and 2 do not contain subunits structurally related to casein kinases 1 and 2
    • Dahmus M.E. Calf thymus RNA polymerase 1 and 2 do not contain subunits structurally related to casein kinases 1 and 2. J. biol. Chem. 256:1981;11239-11243.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11239-11243
    • Dahmus, M.E.1
  • 73
    • 0017329211 scopus 로고
    • Purification and characterization of Novikoff ascites tumor protein kinase
    • Dahmus M.E., Natzle J. Purification and characterization of Novikoff ascites tumor protein kinase. Biochemistry. 16:1977;1901-1908.
    • (1977) Biochemistry , vol.16 , pp. 1901-1908
    • Dahmus, M.E.1    Natzle, J.2
  • 74
    • 0027945831 scopus 로고
    • The role of neurotrophins in the developing nervous system
    • Davies A.M. The role of neurotrophins in the developing nervous system. J. Neurobiol. 25:1994;1334-1348.
    • (1994) J. Neurobiol. , vol.25 , pp. 1334-1348
    • Davies, A.M.1
  • 75
    • 0022872205 scopus 로고
    • Synapsin 1: A synaptic vesicle-associated neuronal phosphoprotein
    • DeCamilli P., Greengard P. Synapsin 1: a synaptic vesicle-associated neuronal phosphoprotein. Biochem. Pharmac. 35:1986;4349-4357.
    • (1986) Biochem. Pharmac. , vol.35 , pp. 4349-4357
    • Decamilli, P.1    Greengard, P.2
  • 76
    • 0029867316 scopus 로고    scopus 로고
    • Fragmin, a microfilament regulatory protein from Physarum polycephalum, is phosphorylated by casein kinase 2-type enzymes
    • De Corte V., Gettenans J., De Ville Y., Waelkens E., Vandenkerekhove J. Fragmin, a microfilament regulatory protein from Physarum polycephalum, is phosphorylated by casein kinase 2-type enzymes. Biochemistry. 35:1996;5472-5480.
    • (1996) Biochemistry , vol.35 , pp. 5472-5480
    • De Corte, V.1    Gettenans, J.2    De Ville, Y.3    Waelkens, E.4    Vandenkerekhove, J.5
  • 77
    • 0021162965 scopus 로고
    • Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase 2 (PC0.7)
    • De Paoli-Roach A.A. Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase 2 (PC0.7). J. biol. Chem. 259:1984;12144-12152.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12144-12152
    • De Paoli-Roach, A.A.1
  • 80
    • 0028915957 scopus 로고
    • Dopamine- And cAMP-regulated phosphoprotein DARPP-32: Phosphorylation of Ser-137 by casein kinase 1 inhibits dephosphorylation of Thr-34 by calcineurin
    • Desdouits F., Siciliano J.C., Greengard P., Girault J.-A. Dopamine- and cAMP-regulated phosphoprotein DARPP-32: phosphorylation of Ser-137 by casein kinase 1 inhibits dephosphorylation of Thr-34 by calcineurin. Proc. natl Acad. Sci. USA. 92:1995;2682-2685.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2682-2685
    • Desdouits, F.1    Siciliano, J.C.2    Greengard, P.3    Girault, J.-A.4
  • 81
    • 0023729788 scopus 로고
    • A casein kinase 2-related activity is involved in phosphorylation of microtubule-associated protein MAP-1B during neuroblastoma cell differentiation
    • Diaz-Nido J., Serrano L., Mendez E., Avila J. A casein kinase 2-related activity is involved in phosphorylation of microtubule-associated protein MAP-1B during neuroblastoma cell differentiation. J. biol. Chem. 106:1988;2057-2065.
    • (1988) J. Biol. Chem. , vol.106 , pp. 2057-2065
    • Diaz-Nido, J.1    Serrano, L.2    Mendez, E.3    Avila, J.4
  • 82
    • 0344735329 scopus 로고
    • Increase in cytoplasmic casein kinase 2-type activity accompanies neurite growth after DNA synthesis
    • Diaz-Nido J., Armes-Portela R., Avila J. Increase in cytoplasmic casein kinase 2-type activity accompanies neurite growth after DNA synthesis. J. Neurochem. 587:1992;1820-1828.
    • (1992) J. Neurochem. , vol.587 , pp. 1820-1828
    • Diaz-Nido, J.1    Armes-Portela, R.2    Avila, J.3
  • 83
    • 0028580279 scopus 로고
    • Regulation of protein kinase CK2 isoform expression during rat brain development
    • Diaz-Nido J., Mizuno K., Nawa H., Marshak D.R. Regulation of protein kinase CK2 isoform expression during rat brain development. Cell. Mol. Biol. Res. 40:1994;581-585.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 581-585
    • Diaz-Nido, J.1    Mizuno, K.2    Nawa, H.3    Marshak, D.R.4
  • 84
    • 0026414443 scopus 로고
    • Cloning and sequencing of the casein kinase 2α subunit from Zea mays
    • Dobrowolska G., Boldyreff B., Issinger O.-G. Cloning and sequencing of the casein kinase 2α subunit from Zea mays. Biochim. biophys. Acta. 1129:1991;139-140.
    • (1991) Biochim. Biophys. Acta , vol.1129 , pp. 139-140
    • Dobrowolska, G.1    Boldyreff, B.2    Issinger, O.-G.3
  • 86
    • 0023068568 scopus 로고
    • Identification of the 90 kDa substrate of rat liver type 2 casein kinase with the heat shock protein which binds steroid receptors
    • Dougherty J.J., Rabideau D., Iannotti A.M., Sullivan W.P., Toft D.O. Identification of the 90 kDa substrate of rat liver type 2 casein kinase with the heat shock protein which binds steroid receptors. Biochim. Biophys. Acta. 927:1987;74-80.
    • (1987) Biochim. Biophys. Acta , vol.927 , pp. 74-80
    • Dougherty, J.J.1    Rabideau, D.2    Iannotti, A.M.3    Sullivan, W.P.4    Toft, D.O.5
  • 87
    • 0031692606 scopus 로고    scopus 로고
    • Constitutive expression of heat shock proteins Hsp90, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development
    • D'Souza S.M., Brown I.R. Constitutive expression of heat shock proteins Hsp90, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development. Cell Stress and Chaperones. 3:1998;188-199.
    • (1998) Cell Stress and Chaperones , vol.3 , pp. 188-199
    • D'Souza, S.M.1    Brown, I.R.2
  • 88
    • 0022153791 scopus 로고
    • Topoisomerase 1 phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells
    • Durban E., Goodenough M., Mills J., Busch H. Topoisomerase 1 phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells. EMBO J. 4:1985;2921-2926.
    • (1985) EMBO J. , vol.4 , pp. 2921-2926
    • Durban, E.1    Goodenough, M.2    Mills, J.3    Busch, H.4
  • 91
    • 0025856717 scopus 로고
    • TAN-1, the human homolog of the Drosophila Notch gene, is broken by chromosomal translocation in T lymphoblastic neoplasms
    • Ellisen L.W., Bird J., West D.C., Lee Soreng A., Reynolds T.C., Smith S.D., Sklar J. TAN-1, the human homolog of the Drosophila Notch gene, is broken by chromosomal translocation in T lymphoblastic neoplasms. Cell. 66:1991;649-661.
    • (1991) Cell , vol.66 , pp. 649-661
    • Ellisen, L.W.1    Bird, J.2    West, D.C.3    Lee Soreng, A.4    Reynolds, T.C.5    Smith, S.D.6    Sklar, J.7
  • 92
    • 0021153976 scopus 로고
    • Expression of neural cell adhesion molecule L1 during development, in neurological mutants and in the peripheral nervous system
    • Faissner A., Kruse J., Nieke J., Schachner M. Expression of neural cell adhesion molecule L1 during development, in neurological mutants and in the peripheral nervous system. Dev. Brain Res. 15:1984;69-82.
    • (1984) Dev. Brain Res. , vol.15 , pp. 69-82
    • Faissner, A.1    Kruse, J.2    Nieke, J.3    Schachner, M.4
  • 93
    • 0019218267 scopus 로고
    • Selective inhibition of a cyclic nucleotide-independent protein kinase (G-type casein kinase) by naturally occurring glycosaminoglycans
    • Feige J.J., Pirollet F., Cochet C., Chambaz E.M. Selective inhibition of a cyclic nucleotide-independent protein kinase (G-type casein kinase) by naturally occurring glycosaminoglycans. FEBS Lett. 121:1980;139-142.
    • (1980) FEBS Lett. , vol.121 , pp. 139-142
    • Feige, J.J.1    Pirollet, F.2    Cochet, C.3    Chambaz, E.M.4
  • 94
    • 0029970008 scopus 로고    scopus 로고
    • Regulation of synaptic responses to high-frequency stimulation and LTP by neurotrophins in the hippocampus
    • Figurov A., Pozzo-Miller L.D., Olafson P., Wang T., Lu B. Regulation of synaptic responses to high-frequency stimulation and LTP by neurotrophins in the hippocampus. Nature. 381:1996;706-708.
    • (1996) Nature , vol.381 , pp. 706-708
    • Figurov, A.1    Pozzo-Miller, L.D.2    Olafson, P.3    Wang, T.4    Lu, B.5
  • 95
    • 0025134279 scopus 로고
    • Cytoplasmic and nuclear distribution of casein kinase 2: Characterization of the enzyme uptake by bovine adrenocortical nuclear preparation
    • Filhol O., Cochet C., Chambaz E.M. Cytoplasmic and nuclear distribution of casein kinase 2: characterization of the enzyme uptake by bovine adrenocortical nuclear preparation. Biochemistry. 29:1990;9928-9936.
    • (1990) Biochemistry , vol.29 , pp. 9928-9936
    • Filhol, O.1    Cochet, C.2    Chambaz, E.M.3
  • 96
    • 0025720653 scopus 로고
    • Casein kinase and polyamines may interact in the response of adrenocortical cells to their trophic hormone
    • Filhol O., Loue-Mackenbach P., Cochet C., Chambaz E.M. Casein kinase and polyamines may interact in the response of adrenocortical cells to their trophic hormone. Biochem. biophys. Res. Commun. 180:1991;623-630.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 623-630
    • Filhol, O.1    Loue-Mackenbach, P.2    Cochet, C.3    Chambaz, E.M.4
  • 97
    • 0026673798 scopus 로고
    • Casein kinase 2 and the tumor suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation
    • Filhol O., Baudier J., Delphin C., Loue-Mackenbach P., Chambaz E., Cochet C. Casein kinase 2 and the tumor suppressor protein p53 associate in a molecular complex that is negatively regulated upon p53 phosphorylation. J. biol. Chem. 267:1992;20577-20583.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20577-20583
    • Filhol, O.1    Baudier, J.2    Delphin, C.3    Loue-Mackenbach, P.4    Chambaz, E.5    Cochet, C.6
  • 98
    • 0028361117 scopus 로고
    • Oligomeric casein kinase 2 isoforms are expressed in bovine tissues and adrenocortical cells in culture
    • Filhol O., Cochet C., Loue-Mackenbach P., Chambaz E.M. Oligomeric casein kinase 2 isoforms are expressed in bovine tissues and adrenocortical cells in culture. Biochem. biophys. Res. Commun. 198:1994;660-665.
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 660-665
    • Filhol, O.1    Cochet, C.2    Loue-Mackenbach, P.3    Chambaz, E.M.4
  • 99
    • 0030856172 scopus 로고    scopus 로고
    • CREB: A major mediator of neuronal neurotrophin responses
    • Finkbeiner S., Tavazoie S.F., Maloratsky A., Jacobs K.M. CREB: a major mediator of neuronal neurotrophin responses. Neuron. 19:1997;1031-1047.
    • (1997) Neuron , vol.19 , pp. 1031-1047
    • Finkbeiner, S.1    Tavazoie, S.F.2    Maloratsky, A.3    Jacobs, K.M.4
  • 101
    • 0032079680 scopus 로고    scopus 로고
    • Synaptic tagging: Implications for late maintenance of hippocampal long-term potentiation
    • Frey U., Morris R.G.M. Synaptic tagging: implications for late maintenance of hippocampal long-term potentiation. Trends Neurosci. 21:1998;181-186.
    • (1998) Trends Neurosci. , vol.21 , pp. 181-186
    • Frey, U.1    Morris, R.G.M.2
  • 102
    • 0029971330 scopus 로고    scopus 로고
    • Growth-associated protein-43 (GAP-43) facilitates peptide hormone secretion in mouse anterior pituitary AtT-20 cells
    • Gamby C., Waage M.C., Alen R.G., Baizer L. Growth-associated protein-43 (GAP-43) facilitates peptide hormone secretion in mouse anterior pituitary AtT-20 cells. J. biol. Chem. 271:1996;10023-10028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10023-10028
    • Gamby, C.1    Waage, M.C.2    Alen, R.G.3    Baizer, L.4
  • 103
  • 107
    • 0033043437 scopus 로고    scopus 로고
    • A review of progress towards elucidating the role of protein kinase CK2 in polymerase 3 transcription: Regulation of the TATA binding protein
    • Ghavidel A., Hockman D.J., Schultz M.C. A review of progress towards elucidating the role of protein kinase CK2 in polymerase 3 transcription: regulation of the TATA binding protein. Mol. cell. Biochem. 199:1999;143-148.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 143-148
    • Ghavidel, A.1    Hockman, D.J.2    Schultz, M.C.3
  • 108
    • 0025973101 scopus 로고
    • Polyamines can protect against ischemia induced nerve cell death in gerbil forebrain
    • Gilad G., Gilad V.H. Polyamines can protect against ischemia induced nerve cell death in gerbil forebrain. Exp. Neurol. 111:1991;349-355.
    • (1991) Exp. Neurol. , vol.111 , pp. 349-355
    • Gilad, G.1    Gilad, V.H.2
  • 109
    • 0024827597 scopus 로고
    • Phosphorylation of DARPP-32, a dopamine- And cAMP-regulated phosphoprotein by casein kinase 2
    • Girault J., Hemmings H.C. Jr, Williams K.R., Nairn A.C., Greengard P. Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein by casein kinase 2. J. biol. Chem. 264:1989;21748-21759.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21748-21759
    • Girault, J.1    Hemmings H.C., Jr.2    Williams, K.R.3    Nairn, A.C.4    Greengard, P.5
  • 110
    • 0025119483 scopus 로고
    • Characterization in mammalian brain of a DARPP-32 serine kinase identical to casein kinase 2
    • Girault J.-A., Hemmings H.C., Zorn S.H., Gustafson E.L., Greengard P. Characterization in mammalian brain of a DARPP-32 serine kinase identical to casein kinase 2. J. Neurochem. 55:1990;1772-1783.
    • (1990) J. Neurochem. , vol.55 , pp. 1772-1783
    • Girault, J.-A.1    Hemmings, H.C.2    Zorn, S.H.3    Gustafson, E.L.4    Greengard, P.5
  • 111
    • 0024467314 scopus 로고
    • The c-erbA-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase 2
    • Glineur C., Bailly M., Glydael J. The c-erbA-encoded thyroid hormone receptor is phosphorylated in its amino terminal domain by casein kinase 2. Oncogene. 4:1989;1247-1254.
    • (1989) Oncogene , vol.4 , pp. 1247-1254
    • Glineur, C.1    Bailly, M.2    Glydael, J.3
  • 112
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M., Murray A.W., Kirschner M.W. Cyclin is degraded by the ubiquitin pathway. Nature. 349:1991;132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 113
    • 0028580277 scopus 로고
    • Structure and function of saccharomyces cerevisiae casein kinase 2
    • Glover C.V.C., Bidwai A.P., Reed J.C. Structure and function of saccharomyces cerevisiae casein kinase 2. Cell. Mol. Biol. Res. 40:1994;481-488.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 481-488
    • Glover, C.V.C.1    Bidwai, A.P.2    Reed, J.C.3
  • 114
    • 0024604091 scopus 로고
    • Further characterization of eukaryotic initiation factor 5 from rabbit reticulocytes. Immunochemical characterization and phosphorylation by casein kinase 2
    • Gosh S., Chevesich J., Maitra U. Further characterization of eukaryotic initiation factor 5 from rabbit reticulocytes. Immunochemical characterization and phosphorylation by casein kinase 2. J. biol. Chem. 264:1989;5134-5140.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5134-5140
    • Gosh, S.1    Chevesich, J.2    Maitra, U.3
  • 115
    • 0021207985 scopus 로고
    • Phosphorylation of the androgen receptor by a nuclear cAMP-independent protein kinase
    • Goueli S.A., Holtzman J.L., Hamed K. Phosphorylation of the androgen receptor by a nuclear cAMP-independent protein kinase. Biochem. Biophys. Res. Commun. 123:1984;778-784.
    • (1984) Biochem. Biophys. Res. Commun. , vol.123 , pp. 778-784
    • Goueli, S.A.1    Holtzman, J.L.2    Hamed, K.3
  • 116
    • 0022985859 scopus 로고
    • Purification of nuclear kinases from rat ventral prostate
    • Goueli S.A., Davis A.T., Ahmed K. Purification of nuclear kinases from rat ventral prostate. Int. J. Biochem. 18:1986;861-873.
    • (1986) Int. J. Biochem. , vol.18 , pp. 861-873
    • Goueli, S.A.1    Davis, A.T.2    Ahmed, K.3
  • 117
    • 0022961842 scopus 로고
    • Purification of cytosolic cAMP-independent protein kinases from rat ventral prostate
    • Goueli S.A., Ferkul K.M., Ahmed K. Purification of cytosolic cAMP-independent protein kinases from rat ventral prostate. Int. J. Biochem. 18:1986;875-884.
    • (1986) Int. J. Biochem. , vol.18 , pp. 875-884
    • Goueli, S.A.1    Ferkul, K.M.2    Ahmed, K.3
  • 119
    • 0024282458 scopus 로고
    • Phosphorylation of hepatic insulin receptor by casein kinase 2
    • Grande J., Perez M., Itarte E. Phosphorylation of hepatic insulin receptor by casein kinase 2. FEBS Lett. 232:1988;130-134.
    • (1988) FEBS Lett. , vol.232 , pp. 130-134
    • Grande, J.1    Perez, M.2    Itarte, E.3
  • 120
    • 0025796976 scopus 로고
    • Isolation and characterization of recombinant human CK2 subunits α and β from bacteria
    • Grankowski N., Boldyreff B., Issinger O.-G. Isolation and characterization of recombinant human CK2 subunits α and β from bacteria. Eur. J. Biochem. 198:1991;25-30.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 25-30
    • Grankowski, N.1    Boldyreff, B.2    Issinger, O.-G.3
  • 122
    • 0028049937 scopus 로고
    • Casein kinase 2 preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor
    • Greenwood J.A., Scott C.W., Spreen R.C., Caputo C.B., Johnson G.V.W. Casein kinase 2 preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor. J. biol. Chem. 269:1994;4373-4380.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4373-4380
    • Greenwood, J.A.1    Scott, C.W.2    Spreen, R.C.3    Caputo, C.B.4    Johnson, G.V.W.5
  • 123
    • 0033002132 scopus 로고    scopus 로고
    • BTF3 is a potential new substrate of protein kinase CK2
    • Grein S., Pyerin W. BTF3 is a potential new substrate of protein kinase CK2. Mol. cell. Biochem. 199:1999;121-128.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 121-128
    • Grein, S.1    Pyerin, W.2
  • 124
    • 0027232067 scopus 로고
    • NF-κB and Rel: Participants in a multiform transcriptional regulatory system
    • Grilli M., Chiu J., Lenardo M. NF-κB and Rel: participants in a multiform transcriptional regulatory system. Int. Rev. Cytol. 143:1993;1-62.
    • (1993) Int. Rev. Cytol. , vol.143 , pp. 1-62
    • Grilli, M.1    Chiu, J.2    Lenardo, M.3
  • 125
    • 0032213106 scopus 로고    scopus 로고
    • Casein kinase 1: Spatial organization and positioning of a multifunctional protein kinase family
    • Gross S.D., Anderson R.A. Casein kinase 1: spatial organization and positioning of a multifunctional protein kinase family. Cell. Signalling. 10:1998;699-711.
    • (1998) Cell. Signalling , vol.10 , pp. 699-711
    • Gross, S.D.1    Anderson, R.A.2
  • 126
    • 0032577454 scopus 로고    scopus 로고
    • Dynamics of protein kinase CK2 association with nucleosomes in relation to transcriptional activity
    • Guo C., Davis A.T., Ahmed K. Dynamics of protein kinase CK2 association with nucleosomes in relation to transcriptional activity. J. biol. Chem. 273:1998;13675-13680.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13675-13680
    • Guo, C.1    Davis, A.T.2    Ahmed, K.3
  • 128
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence datase: Identification of conserved features of primary structure and classification of family members
    • Hanks S.K., Quinn A.M. Protein kinase catalytic domain sequence datase: identification of conserved features of primary structure and classification of family members. Meth. Enzym. 200:1991;38-62.
    • (1991) Meth. Enzym. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 129
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks S.K., Quinn A.M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 241:1988;42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 130
    • 0018404386 scopus 로고
    • Cyclic nucleotide independent protein kinases from rabbit reticulocytes. Purification of casein kinases
    • Hathaway G.M., Traugh J.A. Cyclic nucleotide independent protein kinases from rabbit reticulocytes. Purification of casein kinases. J. biol. Chem. 254:1979;762-768.
    • (1979) J. Biol. Chem. , vol.254 , pp. 762-768
    • Hathaway, G.M.1    Traugh, J.A.2
  • 131
    • 0020437026 scopus 로고
    • Casein kinases multipotential protein kinases
    • E. Stadtman, & B. Horecker. New York: Academic Press
    • Hathaway G.M., Traugh J.A. Casein kinases multipotential protein kinases. Stadtman E., Horecker B. Current Topics in Cellular Regulation. 1982;101-127 Academic Press, New York.
    • (1982) Current Topics in Cellular Regulation , pp. 101-127
    • Hathaway, G.M.1    Traugh, J.A.2
  • 132
    • 0021125696 scopus 로고
    • Kinetics of activation of casein kinase 2 by polyamines and reversal of 2,3-bisphosphoglycerate inhibition
    • Hathaway G.M., Traugh J.A. Kinetics of activation of casein kinase 2 by polyamines and reversal of 2,3-bisphosphoglycerate inhibition. J. biol. Chem. 259:1984;7011-7015.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7011-7015
    • Hathaway, G.M.1    Traugh, J.A.2
  • 133
    • 0018371461 scopus 로고
    • Isolation of protein kinases from reticulocytes and phosphorylation of initiation factors
    • Hathaway G.M., Lundak T.S., Tahara S.M., Traugh J.A. Isolation of protein kinases from reticulocytes and phosphorylation of initiation factors. Meth. Enzym. 60:1979;495-511.
    • (1979) Meth. Enzym. , vol.60 , pp. 495-511
    • Hathaway, G.M.1    Lundak, T.S.2    Tahara, S.M.3    Traugh, J.A.4
  • 134
    • 0019888531 scopus 로고
    • Identification of the catalytic subunit of casein kinase 2 by affinity labeling with 5′-p-fluorosulfonylbenzoyl adenosine
    • Hathaway G.M., Zoller M.J., Traugh J.A. Identification of the catalytic subunit of casein kinase 2 by affinity labeling with 5′-p-fluorosulfonylbenzoyl adenosine. J. biol. Chem. 256:1981;11442-11446.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11442-11446
    • Hathaway, G.M.1    Zoller, M.J.2    Traugh, J.A.3
  • 135
    • 0030903056 scopus 로고    scopus 로고
    • Effect of ethanol on nuclear casein kinase 2 activity in brain
    • Haviryaji K.S.G., Vemuri M.C. Effect of ethanol on nuclear casein kinase 2 activity in brain. Neurochem. Res. 22:1997;699-704.
    • (1997) Neurochem. Res. , vol.22 , pp. 699-704
    • Haviryaji, K.S.G.1    Vemuri, M.C.2
  • 136
    • 0031009292 scopus 로고    scopus 로고
    • Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site
    • He Q.N., Dent E.W., Meiri K.F. Modulation of actin filament behavior by GAP-43 (neuromodulin) is dependent on the phosphorylation status of serine 41, the protein kinase C site. J. Neurosci. 17:1997;3515-3524.
    • (1997) J. Neurosci. , vol.17 , pp. 3515-3524
    • He, Q.N.1    Dent, E.W.2    Meiri, K.F.3
  • 137
    • 0026327502 scopus 로고
    • Enhanced casein kinase 2 activity in COS-1 cells upon overexpression of either its catalytic or noncatalytic subunit
    • Heller-Harrison R.A., Czech M.P. Enhanced casein kinase 2 activity in COS-1 cells upon overexpression of either its catalytic or noncatalytic subunit. J. biol. Chem. 266:1991;14435-14439.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14435-14439
    • Heller-Harrison, R.A.1    Czech, M.P.2
  • 138
    • 0024436837 scopus 로고
    • Cloning and characterization of a cDNA encoding the β subunit of human casein kinase 2
    • Heller-Harrison R.A., Meisner H., Czech M.P. Cloning and characterization of a cDNA encoding the β subunit of human casein kinase 2. Biochemistry. 28:1989;9053-9058.
    • (1989) Biochemistry , vol.28 , pp. 9053-9058
    • Heller-Harrison, R.A.1    Meisner, H.2    Czech, M.P.3
  • 139
    • 0020195709 scopus 로고
    • Phosphorylation of the type-2 regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5
    • Hemmings B.A., Aitken A., Cohen P., Rymond M., Hofmann F. Phosphorylation of the type-2 regulatory subunit of cyclic-AMP-dependent protein kinase by glycogen synthase kinase 3 and glycogen synthase kinase 5. Eur. J. Biochem. 127:1982;473-481.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 473-481
    • Hemmings, B.A.1    Aitken, A.2    Cohen, P.3    Rymond, M.4    Hofmann, F.5
  • 140
    • 0021714011 scopus 로고
    • DARPP-32, a dopamine- And cyclic AMP-regulated neuronal phosphoprotein. 2. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase inhibitor 1
    • Hemmings H.C. Jr, Nairn A.C., Greengard P. DARPP-32, a dopamine- and cyclic AMP-regulated neuronal phosphoprotein. 2. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase inhibitor 1. J. biol. Chem. 259:1984;14491-14497.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14491-14497
    • Hemmings H.C., Jr.1    Nairn, A.C.2    Greengard, P.3
  • 141
    • 0021702461 scopus 로고
    • DARPP-32, a dopamine- And adenosine 3′: 5′-monophosphate-regulated neuronal phosphoprotein. 1. Amino Acid sequence around the phosphorylated threonine
    • Hemmings H.C. Jr, Williams K.R., Konigsberg W.H., Greengard P. DARPP-32, a dopamine- and adenosine 3′: 5′-monophosphate-regulated neuronal phosphoprotein. 1. Amino Acid sequence around the phosphorylated threonine. J. biol. Chem. 259:1984;14486-14490.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14486-14490
    • Hemmings H.C., Jr.1    Williams, K.R.2    Konigsberg, W.H.3    Greengard, P.4
  • 142
  • 143
    • 0031149046 scopus 로고    scopus 로고
    • The c-Jun transcription factor-bipotential mediator of neuronal death, survival and regeneration
    • Herdegen T., Skene P., Bähr M. The c-Jun transcription factor-bipotential mediator of neuronal death, survival and regeneration. Trends Neurosci. 20:1997;227-231.
    • (1997) Trends Neurosci. , vol.20 , pp. 227-231
    • Herdegen, T.1    Skene, P.2    Bähr, M.3
  • 146
    • 0026010655 scopus 로고
    • Molecular structure and functional testing of human L1 cam: An interspecies comparison
    • Hlavin M.L., Lemmon V. Molecular structure and functional testing of human L1 cam: an interspecies comparison. Genomics. 11:1991;416-423.
    • (1991) Genomics , vol.11 , pp. 416-423
    • Hlavin, M.L.1    Lemmon, V.2
  • 147
    • 0030032605 scopus 로고    scopus 로고
    • Casein kinase 2 is required for efficient transcription by RNA polymerase 3
    • Hockman D.J., Schultz M.C. Casein kinase 2 is required for efficient transcription by RNA polymerase 3. Mol. cell. Biol. 16:1996;892-898.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 892-898
    • Hockman, D.J.1    Schultz, M.C.2
  • 148
    • 0025221349 scopus 로고
    • Expression of wild-type and mutated forms of the catalytic (α) subunit of Caenorhabditis elegans casein kinase 2 in Escherichia coli
    • Hu E., Rubin C.S. Expression of wild-type and mutated forms of the catalytic (α) subunit of Caenorhabditis elegans casein kinase 2 in Escherichia coli. J. biol. Chem. 265:1990;20609-20615.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20609-20615
    • Hu, E.1    Rubin, C.S.2
  • 149
    • 0025255597 scopus 로고
    • Casein kinase 2 from Caenorhabditis elegans. Properties and developmental regulation of the enzyme: Cloning and sequence analyses of cDNA and the gene for the catalytic subunit
    • Hu E., Rubin C.S. Casein kinase 2 from Caenorhabditis elegans. Properties and developmental regulation of the enzyme: cloning and sequence analyses of cDNA and the gene for the catalytic subunit. J. biol. Chem. 265:1990;5072-5080.
    • (1990) J. Biol. Chem. , vol.265 , pp. 5072-5080
    • Hu, E.1    Rubin, C.S.2
  • 150
    • 0026045590 scopus 로고
    • Casein kinase 2 from Caenorhabditis elegans. Cloning, characterization and developmental regulation of the gene encoding the β-subunit
    • Hu E., Rubin C.S. Casein kinase 2 from Caenorhabditis elegans. Cloning, characterization and developmental regulation of the gene encoding the β-subunit. J. biol. Chem. 266:1991;19796-19802.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19796-19802
    • Hu, E.1    Rubin, C.S.2
  • 151
    • 0027314325 scopus 로고
    • Casein kinase 2 activity in the postischemic rat brain increases in brain regions resistant to ischemia and decreases in vulnerable areas
    • Hu R.B., Wieloch T. Casein kinase 2 activity in the postischemic rat brain increases in brain regions resistant to ischemia and decreases in vulnerable areas. J. Neurochem. 60:1993;1722-1728.
    • (1993) J. Neurochem. , vol.60 , pp. 1722-1728
    • Hu, R.B.1    Wieloch, T.2
  • 152
    • 0026636883 scopus 로고
    • The regulation of transcription by phosphorylation
    • Hunter T., Karin M. The regulation of transcription by phosphorylation. Cell. 70:1992;375-387.
    • (1992) Cell , vol.70 , pp. 375-387
    • Hunter, T.1    Karin, M.2
  • 153
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes, R.O., 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 155
    • 0019322396 scopus 로고
    • Phosphorylation of HMG 17 by protein kinase N2 from rat liver cell nuclei
    • Inoue A., Tei Y., Hasuma T., Yukioka M., Morisawa S. Phosphorylation of HMG 17 by protein kinase N2 from rat liver cell nuclei. FEBS Lett. 117:1980;68-72.
    • (1980) FEBS Lett. , vol.117 , pp. 68-72
    • Inoue, A.1    Tei, Y.2    Hasuma, T.3    Yukioka, M.4    Morisawa, S.5
  • 156
    • 0027430998 scopus 로고
    • Casein kinases: Pleiotropic mediators of cellular regulation
    • Issinger O.-G. Casein kinases: pleiotropic mediators of cellular regulation. Pharmac. Ther. 59:1993;1-30.
    • (1993) Pharmac. Ther. , vol.59 , pp. 1-30
    • Issinger, O.-G.1
  • 157
    • 0031282249 scopus 로고    scopus 로고
    • Memory formation: The sequence of biochemical events in the hippocampus and its connection to activity in other brain structures
    • Izquierdo I., Medina J.H. Memory formation: the sequence of biochemical events in the hippocampus and its connection to activity in other brain structures. Neurobiol. Learning Memory. 68:1997;285-316.
    • (1997) Neurobiol. Learning Memory , vol.68 , pp. 285-316
    • Izquierdo, I.1    Medina, J.H.2
  • 158
    • 0024212265 scopus 로고
    • Site-specific phosphorylation of the purified receptor for calcium-channel blockers by cAMP- And cGMP-dependent protein kinases, protein kinase C, calmodulin-dependent protein kinase 2 and casein kinase 2
    • Jahn H., Nastainczyk W., Rohrkasten A., Schneider T., Hofmann F. Site-specific phosphorylation of the purified receptor for calcium-channel blockers by cAMP- and cGMP-dependent protein kinases, protein kinase C, calmodulin-dependent protein kinase 2 and casein kinase 2. Eur. J. Biochem. 178:1988;535-542.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 535-542
    • Jahn, H.1    Nastainczyk, W.2    Rohrkasten, A.3    Schneider, T.4    Hofmann, F.5
  • 159
    • 0027078419 scopus 로고
    • Characterization of the phosphotransferase domain of casein kinase 2 by site-directed mutagenesis and expression in Escherichia coli
    • Jakobi R., Traugh J.A. Characterization of the phosphotransferase domain of casein kinase 2 by site-directed mutagenesis and expression in Escherichia coli. J. biol. Chem. 267:1992;23894-23902.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23894-23902
    • Jakobi, R.1    Traugh, J.A.2
  • 160
    • 0024359463 scopus 로고
    • Human phosvitin/casein kinase type 2. Molecular cloning and sequencing of full-length cDNA encoding subunit β
    • Jakobi R., Voss H., Pyerin W. Human phosvitin/casein kinase type 2. Molecular cloning and sequencing of full-length cDNA encoding subunit β Eur. J. Biochem. 183:1989;227-233.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 227-233
    • Jakobi, R.1    Voss, H.2    Pyerin, W.3
  • 161
    • 0023134537 scopus 로고
    • A major phosphoprotein of cells infected with pseudorabies virus is phosphorylated by cellular casein kinase 2
    • Jakubowicz T., Leader D.P. A major phosphoprotein of cells infected with pseudorabies virus is phosphorylated by cellular casein kinase 2. J. Gen. Virol. 68:1987;1159-1163.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1159-1163
    • Jakubowicz, T.1    Leader, D.P.2
  • 162
    • 0026514556 scopus 로고
    • Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties
    • Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A., Stunnenberg H.G. Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties. EMBO J. 11:1992;1045-1054.
    • (1992) EMBO J. , vol.11 , pp. 1045-1054
    • Janknecht, R.1    Hipskind, R.A.2    Houthaeve, T.3    Nordheim, A.4    Stunnenberg, H.G.5
  • 163
    • 0029666261 scopus 로고    scopus 로고
    • Characterization of IκB kinases. IκB is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase 2 substrate
    • Janosch P., Schellerer M., Seitz T., Reim P., Eulitz M., Brielmeier M., Kolch W., Sedivy J.M., Mischak H. Characterization of IκB kinases. IκB is not phosphorylated by Raf-1 or protein kinase C isozymes, but is a casein kinase 2 substrate. J. biol. Chem. 271:1996;13868-13874.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13868-13874
    • Janosch, P.1    Schellerer, M.2    Seitz, T.3    Reim, P.4    Eulitz, M.5    Brielmeier, M.6    Kolch, W.7    Sedivy, J.M.8    Mischak, H.9
  • 164
    • 0345165570 scopus 로고
    • Phosphorylation-mediated regulation of signal-dependent nuclear protein transport: The "ccN motif"
    • Jans D.A. Phosphorylation-mediated regulation of signal-dependent nuclear protein transport: the "CcN motif" Membr. Prot. Transport. 2:1995;161-199.
    • (1995) Membr. Prot. Transport , vol.2 , pp. 161-199
    • Jans, D.A.1
  • 165
    • 0028066798 scopus 로고
    • Negative charge at the casein kinase 2 site flanking the nuclear localization signal of the SV40 large T-antigen is mechanistically important or enhanced nuclear import
    • Jans D.A., Jans P. Negative charge at the casein kinase 2 site flanking the nuclear localization signal of the SV40 large T-antigen is mechanistically important or enhanced nuclear import. Oncogene. 9:1994;2961-2968.
    • (1994) Oncogene , vol.9 , pp. 2961-2968
    • Jans, D.A.1    Jans, P.2
  • 167
    • 0027296619 scopus 로고
    • The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase 2 and nucleolin
    • Jin Y.J., Burakoff S.J. The 25-kDa FK506-binding protein is localized in the nucleus and associates with casein kinase 2 and nucleolin. Proc. natl Acad. Sci. USA. 90:1993;7769-7773.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7769-7773
    • Jin, Y.J.1    Burakoff, S.J.2
  • 168
    • 0032890037 scopus 로고    scopus 로고
    • Role of brain-derived neurotrophic factor and presynaptic proteins in passive avoidance learning in day-old domestic chicks
    • Johnston A.N.B., Clements M.P., Rose S.P.R. Role of brain-derived neurotrophic factor and presynaptic proteins in passive avoidance learning in day-old domestic chicks. Neuroscience. 88:1999;1033-1042.
    • (1999) Neuroscience , vol.88 , pp. 1033-1042
    • Johnston, A.N.B.1    Clements, M.P.2    Rose, S.P.R.3
  • 169
    • 0028866530 scopus 로고
    • Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase 2 site in its cytoplasmic tail
    • Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A., Thomas G. Intracellular trafficking of furin is modulated by the phosphorylation state of a casein kinase 2 site in its cytoplasmic tail. EMBO J. 14:1995;5869-5883.
    • (1995) EMBO J. , vol.14 , pp. 5869-5883
    • Jones, B.G.1    Thomas, L.2    Molloy, S.S.3    Thulin, C.D.4    Fry, M.D.5    Walsh, K.A.6    Thomas, G.7
  • 172
    • 0028988240 scopus 로고
    • Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus
    • Kang H.J., Schulman E.M. Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus. Science. 267:1995;1658-1662.
    • (1995) Science , vol.267 , pp. 1658-1662
    • Kang, H.J.1    Schulman, E.M.2
  • 173
    • 0025272486 scopus 로고
    • Loss of neurons in the frontal cortex in AIDS brains
    • Ketzler S., Weis S., Haug H., Budka H. Loss of neurons in the frontal cortex in AIDS brains. Acta Neuropathol. 80:1990;92-94.
    • (1990) Acta Neuropathol. , vol.80 , pp. 92-94
    • Ketzler, S.1    Weis, S.2    Haug, H.3    Budka, H.4
  • 175
    • 0001171768 scopus 로고    scopus 로고
    • Interaction of the β subunit of casein kinase 2 with the ribosomal protein L5
    • Kim J-M., Cha J-Y., Marshak D.R., Bae Y-S. Interaction of the β subunit of casein kinase 2 with the ribosomal protein L5. Biochem. biophys. Res. Commun. 226:1996;180-186.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 180-186
    • Kim, J.-M.1    Cha, J.-Y.2    Marshak, D.R.3    Bae, Y.-S.4
  • 176
    • 0029026540 scopus 로고
    • Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways
    • Kimura Y., Yahara I., Lindquist S. Role of the protein chaperone YDJ1 in establishing Hsp90-mediated signal transduction pathways. Science. 268:1995;1362-1365.
    • (1995) Science , vol.268 , pp. 1362-1365
    • Kimura, Y.1    Yahara, I.2    Lindquist, S.3
  • 177
    • 0023149125 scopus 로고
    • Phosphorylation of serine 833 in cytoplasmic domain of low density lipoprotein receptor by a high molecular weight enzyme resembling casein kinase 2
    • Kishimoto A., Brown M.S.M., Slaughter C.A., Goldstein J.L. Phosphorylation of serine 833 in cytoplasmic domain of low density lipoprotein receptor by a high molecular weight enzyme resembling casein kinase 2. J. biol. Chem. 262:1987;1344-1351.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1344-1351
    • Kishimoto, A.1    Brown, M.S.M.2    Slaughter, C.A.3    Goldstein, J.L.4
  • 178
    • 0023797153 scopus 로고
    • Insulin-like growth factor 1 and insulin rapidly increase casein kinase 2
    • Klarlund J.K., Czech M.P. Insulin-like growth factor 1 and insulin rapidly increase casein kinase 2 activity in BALB/c3T3 fibroblasts. J. biol. Chem. 263:1988;15872-15875.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15872-15875
    • Klarlund, J.K.1    Czech, M.P.2
  • 180
    • 0028072001 scopus 로고
    • Casein kinase 2 stimulates Xenopus laevis DNA topoisomerase 1 by physical association
    • Kordiyak G.J., Jakes S., Ingebritsen T.S., Benbow R.M. Casein kinase 2 stimulates Xenopus laevis DNA topoisomerase 1 by physical association. Biochemistry. 33:1994;13484-13491.
    • (1994) Biochemistry , vol.33 , pp. 13484-13491
    • Kordiyak, G.J.1    Jakes, S.2    Ingebritsen, T.S.3    Benbow, R.M.4
  • 181
  • 183
    • 0033063107 scopus 로고    scopus 로고
    • Intermolecular contact sites in protein kinase CK2
    • Krehan A., Pyerin W. Intermolecular contact sites in protein kinase CK2. Mol. cell. Biochem. 191:1999;21-28.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 21-28
    • Krehan, A.1    Pyerin, W.2
  • 184
    • 0029928784 scopus 로고    scopus 로고
    • Interaction sites between catalytic and regulatory subunits in human protein kinase CK2 holoenzymes as indicated by chemical cross-linking and immunological investigations
    • Krehan A., Lorenz P., Plana-Coll M., Pyerin W. Interaction sites between catalytic and regulatory subunits in human protein kinase CK2 holoenzymes as indicated by chemical cross-linking and immunological investigations. Biochemistry. 35:1996;4966-4975.
    • (1996) Biochemistry , vol.35 , pp. 4966-4975
    • Krehan, A.1    Lorenz, P.2    Plana-Coll, M.3    Pyerin, W.4
  • 185
    • 0026531390 scopus 로고
    • Casein kinase 2 is a predominantly nuclear enzyme
    • Krek W., Maridor G., Nigg E.A. Casein kinase 2 is a predominantly nuclear enzyme. J. cell. Biol. 116:1992;43-55.
    • (1992) J. Cell. Biol. , vol.116 , pp. 43-55
    • Krek, W.1    Maridor, G.2    Nigg, E.A.3
  • 186
    • 0030723127 scopus 로고    scopus 로고
    • Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain
    • Kuret J., Johnson G.S., Cha D., Christenson E.R., DeMaggio A.J., Hoekstra M.F. Casein kinase 1 is tightly associated with paired-helical filaments isolated from Alzheimer's disease brain. J. Neurochem. 69:1997;2506-2515.
    • (1997) J. Neurochem. , vol.69 , pp. 2506-2515
    • Kuret, J.1    Johnson, G.S.2    Cha, D.3    Christenson, E.R.4    Demaggio, A.J.5    Hoekstra, M.F.6
  • 187
  • 188
    • 0031019426 scopus 로고    scopus 로고
    • Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland
    • Lasa M., Marin O., Pinna L.A. Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur. J. Biochem. 243:1997;719-725.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 719-725
    • Lasa, M.1    Marin, O.2    Pinna, L.A.3
  • 189
    • 0032588906 scopus 로고    scopus 로고
    • CK2 alpha-protein phosphatase 2A molecular complex: Possible interaction with the MAP kinase pathway
    • Lebrin F., Bianchini L., Rabilloud T., Chambaz E.M., Goldberg Y. CK2 alpha-protein phosphatase 2A molecular complex: possible interaction with the MAP kinase pathway. Mol. cell. Biochem. 199:1999;207-212.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 207-212
    • Lebrin, F.1    Bianchini, L.2    Rabilloud, T.3    Chambaz, E.M.4    Goldberg, Y.5
  • 190
    • 0025666845 scopus 로고
    • Cyclic-AMP-responsive transcriptional activation of CREB-237 involves interdependent phosphorylated subdomains
    • Lee C.Q., Yun Y., Hoeffler J.P., Habener J.F. Cyclic-AMP-responsive transcriptional activation of CREB-237 involves interdependent phosphorylated subdomains. EMBO J. 9:1990;4455-4465.
    • (1990) EMBO J. , vol.9 , pp. 4455-4465
    • Lee, C.Q.1    Yun, Y.2    Hoeffler, J.P.3    Habener, J.F.4
  • 191
    • 0343295754 scopus 로고
    • Gene regulation in the nervous system
    • Z.W. Hall. Sunderland, MA: Sinauer Associates
    • Lemke G. Gene regulation in the nervous system. Hall Z.W. An Introduction to Molecular Neurobiology. 1992;326-327 Sinauer Associates, Sunderland, MA.
    • (1992) An Introduction to Molecular Neurobiology , pp. 326-327
    • Lemke, G.1
  • 192
    • 0343295754 scopus 로고
    • Gene regulation in the nervous system
    • Z.W. Hall. Sunderland, MA: Sinauer Associates
    • Lemke G. Gene regulation in the nervous system. Hall Z.W. An Introduction to Molecular Neurobiology. 1992;331-335 Sinauer Associates, Sunderland, MA.
    • (1992) An Introduction to Molecular Neurobiology , pp. 331-335
    • Lemke, G.1
  • 194
    • 0030000158 scopus 로고    scopus 로고
    • Selective role for trkB neurotrophin receptors in rapid modulation of hippocampal synaptic transmission
    • Levine E.S., Dreyfus C.F., Black I.B., Plummer M.R. Selective role for trkB neurotrophin receptors in rapid modulation of hippocampal synaptic transmission. Mol. Brain Res. 38:1996;300-303.
    • (1996) Mol. Brain Res. , vol.38 , pp. 300-303
    • Levine, E.S.1    Dreyfus, C.F.2    Black, I.B.3    Plummer, M.R.4
  • 195
    • 0029900546 scopus 로고    scopus 로고
    • The physical association of casein kinase 2 with nucleolin
    • Li D., Dobrowolska G., Krebs E.G. The physical association of casein kinase 2 with nucleolin. J. biol. Chem. 271:1996;15662-15668.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15662-15668
    • Li, D.1    Dobrowolska, G.2    Krebs, E.G.3
  • 196
    • 0031013280 scopus 로고    scopus 로고
    • Specific interaction between casein kinase 2 and the nucleolar protein Nopp140
    • Li D., Meier U.T., Dobrowolska G., Krebs E.G. Specific interaction between casein kinase 2 and the nucleolar protein Nopp140. J. biol. Chem. 272:1997;3773-3779.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3773-3779
    • Li, D.1    Meier, U.T.2    Dobrowolska, G.3    Krebs, E.G.4
  • 197
    • 0033039190 scopus 로고    scopus 로고
    • Identification of proteins that associate with protein kinase CK2
    • Li D., Dobrowolska G., Krebs E.G. Identification of proteins that associate with protein kinase CK2. Mol. cell. Biochem. 191:1999;223-228.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 223-228
    • Li, D.1    Dobrowolska, G.2    Krebs, E.G.3
  • 198
    • 0032555642 scopus 로고    scopus 로고
    • Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau
    • Liao H., Li Y., Brautigan D.L., Gundersen G.G. Protein phosphatase 1 is targeted to microtubules by the microtubule-associated protein Tau. J. biol. Chem. 273:1998;21901-21908.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21901-21908
    • Liao, H.1    Li, Y.2    Brautigan, D.L.3    Gundersen, G.G.4
  • 200
    • 0029670085 scopus 로고    scopus 로고
    • Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase 2 affects intrinsic protein stability
    • Lin R., Beauparlant P., Makris C., Meloche S., Hiscott J. Phosphorylation of IκBα in the C-terminal PEST domain by casein kinase 2 affects intrinsic protein stability. Mol. cell. Biol. 16:1996;1401-1409.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1401-1409
    • Lin, R.1    Beauparlant, P.2    Makris, C.3    Meloche, S.4    Hiscott, J.5
  • 201
    • 0033000436 scopus 로고    scopus 로고
    • A role for casein kinase 2 phosphorylation in the regulation of IRF-1 transcriptional activity
    • Lin R.T., Hiscott J. A role for casein kinase 2 phosphorylation in the regulation of IRF-1 transcriptional activity. Mol. cell. Biochem. 199:1999;169-180.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 169-180
    • Lin, R.T.1    Hiscott, J.2
  • 206
    • 0026589214 scopus 로고
    • Regulatory interactions and role in cell type specification of the Malpighian tubules by the cut, Krüppel, and caudal genes of Drosophila
    • Liu S., Jack J. Regulatory interactions and role in cell type specification of the Malpighian tubules by the cut, Krüppel, and caudal genes of Drosophila. Dev. Biol. 150:1992;133-143.
    • (1992) Dev. Biol. , vol.150 , pp. 133-143
    • Liu, S.1    Jack, J.2
  • 207
    • 0028878537 scopus 로고
    • Detection of a cdc2-related kinase associated with Alzheimer paired helical filaments
    • Liu W.K., Williams R.T., Hall F.L., Dickson D.W., Yen S.H. Detection of a cdc2-related kinase associated with Alzheimer paired helical filaments. Am. J. Pathol. 146:1995;228-238.
    • (1995) Am. J. Pathol. , vol.146 , pp. 228-238
    • Liu, W.K.1    Williams, R.T.2    Hall, F.L.3    Dickson, D.W.4    Yen, S.H.5
  • 208
    • 0027509617 scopus 로고
    • Cell biological studies with monoclonal and polyclonal antibodies against human casein kinase 2 subunit β demonstrate participation of the kinase in mitogenic signaling
    • Lorenz P., Pepperkok R., Ansorge W., Pyerin W. Cell biological studies with monoclonal and polyclonal antibodies against human casein kinase 2 subunit β demonstrate participation of the kinase in mitogenic signaling. J. biol. Chem. 268:1993;2733-2739.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2733-2739
    • Lorenz, P.1    Pepperkok, R.2    Ansorge, W.3    Pyerin, W.4
  • 209
    • 0025062054 scopus 로고
    • Isolation and characterization of human cDNA clones encoding the α and the α′ subunits of casein kinase 2
    • Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G. Isolation and characterization of human cDNA clones encoding the α and the α′ subunits of casein kinase 2. Biochemistry. 29:1990;8436-8447.
    • (1990) Biochemistry , vol.29 , pp. 8436-8447
    • Lozeman, F.J.1    Litchfield, D.W.2    Piening, C.3    Takio, K.4    Walsh, K.A.5    Krebs, E.G.6
  • 210
    • 0027267492 scopus 로고
    • Copurification of casein kinase 2 with 20S proteasome and phosphorylation of a 30 kDa proteasome subunit
    • Ludeman R., Lerea K.M., Etlinger J.D. Copurification of casein kinase 2 with 20S proteasome and phosphorylation of a 30 kDa proteasome subunit. J. biol. Chem. 268:1993;17413-17417.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17413-17417
    • Ludeman, R.1    Lerea, K.M.2    Etlinger, J.D.3
  • 211
    • 0028265483 scopus 로고
    • Biosynthesis and degradation of casein kinase 2 in lymphoid cell lines
    • Lüscher B., Litchfield D.W. Biosynthesis and degradation of casein kinase 2 in lymphoid cell lines. Eur. J. Biochem. 220:1994;521-526.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 521-526
    • Lüscher, B.1    Litchfield, D.W.2
  • 212
    • 0024446021 scopus 로고
    • Myc oncoproteins are phosphorylated by casein kinase 2
    • Lüscher B., Kuenzel E.A., Krebs E.G., Eisenman R.N. Myc oncoproteins are phosphorylated by casein kinase 2. EMBO J. 8:1989;1111-1119.
    • (1989) EMBO J. , vol.8 , pp. 1111-1119
    • Lüscher, B.1    Kuenzel, E.A.2    Krebs, E.G.3    Eisenman, R.N.4
  • 213
    • 0342546629 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor antisense oligonucleotide impairs memory retention and inhibits long-term potentiation in rats
    • Ma Y.L., Wang H.L., Wu H.C., Wei C.L., Lee E.H.Y. Brain-derived neurotrophic factor antisense oligonucleotide impairs memory retention and inhibits long-term potentiation in rats. Neuroscience. 82:1998;957-967.
    • (1998) Neuroscience , vol.82 , pp. 957-967
    • Ma, Y.L.1    Wang, H.L.2    Wu, H.C.3    Wei, C.L.4    Lee, E.H.Y.5
  • 214
    • 0030022860 scopus 로고    scopus 로고
    • Casein kinase 2 phosphorylates IκBα at S-283, S-289, S-293 and T-291 and is required for its degradation
    • MacElhinny J.A., Trushin S.A., Bren G.D., Chester N., Paya C.V. Casein kinase 2 phosphorylates IκBα at S-283, S-289, S-293 and T-291 and is required for its degradation. Mol. cell. Biol. 16:1996;899-906.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 899-906
    • MacElhinny, J.A.1    Trushin, S.A.2    Bren, G.D.3    Chester, N.4    Paya, C.V.5
  • 215
    • 0033059744 scopus 로고    scopus 로고
    • Protein kinase CK2-dependent regulation of p53 function: Evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable
    • MacKendrick L., Milne D., Meek D. Protein kinase CK2-dependent regulation of p53 function: evidence that the phosphorylation status of the serine 386 (CK2) site of p53 is constitutive and stable. Mol. cell. Biochem. 191:1999;187-199.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 187-199
    • MacKendrick, L.1    Milne, D.2    Meek, D.3
  • 216
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: Implications for therapy of Alzheimer and other neurodegenerative diseases
    • MacGeer P.L., MacGeer E.G. The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Res. Rev. 21:1995;195-218.
    • (1995) Brain Res. Rev. , vol.21 , pp. 195-218
    • MacGeer, P.L.1    MacGeer, E.G.2
  • 217
    • 0024419685 scopus 로고
    • Phosphorylation of the high-mobility-group-like protein P1 by casein kinase-2
    • Maelandsmo G.M., Ostvold A.C., Laland S.G. Phosphorylation of the high-mobility-group-like protein P1 by casein kinase-2. Eur. J. Biochem. 184:1989;529-534.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 529-534
    • Maelandsmo, G.M.1    Ostvold, A.C.2    Laland, S.G.3
  • 218
    • 0031004401 scopus 로고    scopus 로고
    • Protein phosphatase inhibitors induce modification of synapse structure and Tau hyperphosphorylation in cultured rat hippocampal neurons
    • Malchiodi-Albedi F., Petrucci T.C., Picconi B., Iosi F., Falchi M. Protein phosphatase inhibitors induce modification of synapse structure and Tau hyperphosphorylation in cultured rat hippocampal neurons. J. Neurosci. Res. 48:1997;425-438.
    • (1997) J. Neurosci. Res. , vol.48 , pp. 425-438
    • Malchiodi-Albedi, F.1    Petrucci, T.C.2    Picconi, B.3    Iosi, F.4    Falchi, M.5
  • 219
    • 0025313511 scopus 로고
    • Casein kinase 2 enhances the DNA binding activity of serum response factor
    • Manak J.R., De Bisschop N., Kris R.M., Prywes R. Casein kinase 2 enhances the DNA binding activity of serum response factor. Genes Dev. 4:1990;955-967.
    • (1990) Genes Dev. , vol.4 , pp. 955-967
    • Manak, J.R.1    De Bisschop, N.2    Kris, R.M.3    Prywes, R.4
  • 221
    • 0026594930 scopus 로고
    • Casein kinase 2 phosphorylation increases the rate of serum response factor-binding site exchange
    • Marais R.M., Hsuan J.J., MacGuigan C., Wynne J., Treisman R. Casein kinase 2 phosphorylation increases the rate of serum response factor-binding site exchange. EMBO J. 11:1992;97-105.
    • (1992) EMBO J. , vol.11 , pp. 97-105
    • Marais, R.M.1    Hsuan, J.J.2    MacGuigan, C.3    Wynne, J.4    Treisman, R.5
  • 222
    • 0025861471 scopus 로고
    • Casein kinase 2. cDNA sequences, developmental expression and tissue distribution of mRNAs for α, α′ and β subunits of the chicken enzyme
    • Maridor G., Park W., Krek W., Nigg E.A. Casein kinase 2. cDNA sequences, developmental expression and tissue distribution of mRNAs for α, α′ and β subunits of the chicken enzyme. J. biol. Chem. 266:1991;2362-2368.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2362-2368
    • Maridor, G.1    Park, W.2    Krek, W.3    Nigg, E.A.4
  • 223
    • 0030921077 scopus 로고    scopus 로고
    • Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 β-subunit
    • Marin O., Meggio F., Sarno S., Pinna L.A. Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 β-subunit. Biochemistry. 36:1997;7192-7198.
    • (1997) Biochemistry , vol.36 , pp. 7192-7198
    • Marin, O.1    Meggio, F.2    Sarno, S.3    Pinna, L.A.4
  • 224
    • 0025272580 scopus 로고
    • Subcellular and regional distribution of casein kinase 2 and initiation factor 2 activities during rat brain development
    • Martin M., Alcazar A., Salinas M. Subcellular and regional distribution of casein kinase 2 and initiation factor 2 activities during rat brain development. Int. J. Dev. Neurosci. 8:1990;47-54.
    • (1990) Int. J. Dev. Neurosci. , vol.8 , pp. 47-54
    • Martin, M.1    Alcazar, A.2    Salinas, M.3
  • 227
    • 0023674299 scopus 로고
    • Microtubule-associated proteins: Their potential role in determining neuronal morphology
    • Matus A. Microtubule-associated proteins: their potential role in determining neuronal morphology. A. Rev. Neurosci. 11:1988;29-44.
    • (1988) A. Rev. Neurosci. , vol.11 , pp. 29-44
    • Matus, A.1
  • 228
    • 0028943627 scopus 로고
    • Stathmin interaction with a putative kinase and coiled-coil forming protein domains
    • Maucuer A., Camonis J., Sobel A. Stathmin interaction with a putative kinase and coiled-coil forming protein domains. Proc. natl Acad. Sci. USA. 92:1995;3100-3104.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3100-3104
    • Maucuer, A.1    Camonis, J.2    Sobel, A.3
  • 229
    • 0033038527 scopus 로고    scopus 로고
    • i and the toxic actions of the HIV coat protein GP120
    • i and the toxic actions of the HIV coat protein GP120. Eur. J. Neurosci. 11:1999;1167-1178.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1167-1178
    • Medina, I.1    Ghose, S.2    Ben-Ari, Y.3
  • 230
    • 0021745794 scopus 로고
    • Subunit structure and autophosphorylation mechanism of casein kinase TS (type 2) from rat liver cytosol
    • Meggio F., Pinna L.A. Subunit structure and autophosphorylation mechanism of casein kinase TS (type 2) from rat liver cytosol. Eur. J. Biochem. 145:1984;593-599.
    • (1984) Eur. J. Biochem. , vol.145 , pp. 593-599
    • Meggio, F.1    Pinna, L.A.2
  • 231
    • 0019877822 scopus 로고
    • Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases
    • Meggio F., Donella-Deana A., Pinna L.A. Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases. J. biol. Chem. 256:1981;11958-11961.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11958-11961
    • Meggio, F.1    Donella-Deana, A.2    Pinna, L.A.3
  • 232
    • 0021110057 scopus 로고
    • Autophosphorylation of type 2 casein kinase TS at both its α- And β-subunits
    • Meggio F., Brunati A.M., Pinna L.A. Autophosphorylation of type 2 casein kinase TS at both its α- and β-subunits. FEBS Lett. 160:1983;203-208.
    • (1983) FEBS Lett. , vol.160 , pp. 203-208
    • Meggio, F.1    Brunati, A.M.2    Pinna, L.A.3
  • 234
    • 0022388395 scopus 로고
    • Casein kinase and their protein substrates in rat liver cytosol: Evidence for their participation in multimolecular system
    • Meggio F., Agostinis P., Pinna L.A. Casein kinase and their protein substrates in rat liver cytosol: evidence for their participation in multimolecular system. Biochim. Biophys. Acta. 846:1985;248-256.
    • (1985) Biochim. Biophys. Acta , vol.846 , pp. 248-256
    • Meggio, F.1    Agostinis, P.2    Pinna, L.A.3
  • 235
    • 0023650934 scopus 로고
    • 2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase
    • 2+-antagonized phosphorylation of calmodulin by casein kinase-2 and a spleen tyrosine protein kinase. FEBS Lett. 215:1987;241-246.
    • (1987) FEBS Lett. , vol.215 , pp. 241-246
    • Meggio, F.1    Brunati, A.M.2    Pinna, L.A.3
  • 237
    • 0026508869 scopus 로고
    • Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme
    • Meggio F., Boldyreff B., Marin O., Pinna L.A., Issinger O.-G. Role of the β subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme. Eur. J. Biochem. 204:1992;293-297.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 293-297
    • Meggio, F.1    Boldyreff, B.2    Marin, O.3    Pinna, L.A.4    Issinger, O.-G.5
  • 238
    • 0027237630 scopus 로고
    • cdc2 phosphorylation sites of casein kinase 2 β subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme
    • cdc2 phosphorylation sites of casein kinase 2 β subunit are not essential for reconstituting the fully-active heterotetrameric holoenzyme. Biochim. Biophys. Acta. 1164:1993;223-225.
    • (1993) Biochim. Biophys. Acta , vol.1164 , pp. 223-225
    • Meggio, F.1    Boldyreff, B.2    Issinger, O.-G.3    Pinna, L.A.4
  • 239
    • 0028292988 scopus 로고
    • Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 5-64 region of the β-subunit. A study with calmodulin as phosphorylatable substrate
    • Meggio F., Boldyreff B., Issinger O-G., Pinna L.A. Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 5-64 region of the β-subunit. A study with calmodulin as phosphorylatable substrate. Biochemistry. 33:1994;4336-4342.
    • (1994) Biochemistry , vol.33 , pp. 4336-4342
    • Meggio, F.1    Boldyreff, B.2    Issinger, O.-G.3    Pinna, L.A.4
  • 241
    • 0026773097 scopus 로고
    • Nopp140 shuttles on tracks between nucleolus and cytoplasm
    • Meier U.T., Blodel G. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell. 70:1992;127-138.
    • (1992) Cell , vol.70 , pp. 127-138
    • Meier, U.T.1    Blodel, G.2
  • 242
    • 0026177469 scopus 로고
    • Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase 2
    • Meisner H., Czech M.P. Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase 2. Curr. Opin. Cell Biol. 3:1991;474-483.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 474-483
    • Meisner, H.1    Czech, M.P.2
  • 243
    • 0024582158 scopus 로고
    • Molecular cloning of the human casein kinase 2 α subunit
    • Meisner H., Heller-Harrison R., Buxton J., Czech P. Molecular cloning of the human casein kinase 2 α subunit. Biochemistry. 28:1989;4072-4076.
    • (1989) Biochemistry , vol.28 , pp. 4072-4076
    • Meisner, H.1    Heller-Harrison, R.2    Buxton, J.3    Czech, P.4
  • 244
    • 0026669310 scopus 로고
    • The 90-kDa heat shock protein HSP90, binds and protects casein kinase 2 from self-aggregation and enhances its kinase activity
    • Miyata Y., Yahara I. The 90-kDa heat shock protein HSP90, binds and protects casein kinase 2 from self-aggregation and enhances its kinase activity. J. biol. Chem. 267:1992;7042-7047.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7042-7047
    • Miyata, Y.1    Yahara, I.2
  • 245
    • 0029063877 scopus 로고
    • Interaction between casein kinase 2 and the 90-kDa stress protein, HSP90
    • Miyata Y., Yahara I. Interaction between casein kinase 2 and the 90-kDa stress protein, HSP90. Biochemistry. 34:1995;8123-8129.
    • (1995) Biochemistry , vol.34 , pp. 8123-8129
    • Miyata, Y.1    Yahara, I.2
  • 246
    • 0031779645 scopus 로고    scopus 로고
    • Phosphorylation of stathmin modulates its function as a microtubule depolymerizing factor
    • Moreno F.J., Avila J. Phosphorylation of stathmin modulates its function as a microtubule depolymerizing factor. Mol. cell. Biochem. 183:1998;201-209.
    • (1998) Mol. Cell. Biochem. , vol.183 , pp. 201-209
    • Moreno, F.J.1    Avila, J.2
  • 247
    • 0345580628 scopus 로고    scopus 로고
    • Distribution of CK2, its substrate MAB1B and phosphatases in neuronal cells
    • Moreno F.J., DiazNido J., Jimenez J.S., Avila J. Distribution of CK2, its substrate MAB1B and phosphatases in neuronal cells. Mol. cell. Biochem. 191:1999;201-205.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 201-205
    • Moreno, F.J.1    Diaznido, J.2    Jimenez, J.S.3    Avila, J.4
  • 248
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D.O. Principles of CDK regulation. Nature. 374:1995;131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 249
    • 0025026980 scopus 로고
    • M-phase-specific cdc2 protein kinase phosphorylates the β subunit of casein kinase 2 and increases casein kinase 2 activity
    • Mulner-Lorillon O., Cormier P., Labbé J-C., Dorée M., Poulhe R., Osborne H., Bellé R. M-phase-specific cdc2 protein kinase phosphorylates the β subunit of casein kinase 2 and increases casein kinase 2 activity. Eur. J. Biochem. 93:1990;529-534.
    • (1990) Eur. J. Biochem. , vol.93 , pp. 529-534
    • Mulner-Lorillon, O.1    Cormier, P.2    Labbé, J.-C.3    Dorée, M.4    Poulhe, R.5    Osborne, H.6    Bellé, R.7
  • 250
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and functions in cell growth
    • Mumby M.C., Walter G. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol. Rev. 73:1993;673-699.
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 251
    • 0021268378 scopus 로고
    • Purification and identification of myosin heavy chain kinase from bovine brain
    • Murakami N., Matsumura S., Kumon A. Purification and identification of myosin heavy chain kinase from bovine brain. J. Biochem. (Tokyo). 95:1984;651-660.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 651-660
    • Murakami, N.1    Matsumura, S.2    Kumon, A.3
  • 254
    • 0026582389 scopus 로고
    • A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6κB-related motifs whose activities are repressed in lymphoid cells
    • Nakamaya K., Shimizu H., Mitomo K., Watanabe T., Okamoto S.-I., Yamamoto K.-I. A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6κB-related motifs whose activities are repressed in lymphoid cells. Mol. cell. Biol. 12:1992;1736-1746.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1736-1746
    • Nakamaya, K.1    Shimizu, H.2    Mitomo, K.3    Watanabe, T.4    Okamoto, S.-I.5    Yamamoto, K.-I.6
  • 256
    • 0032079650 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution
    • Niefind K., Guerra B., Pinna L.A., Issinger O.-G., Schomburg D. Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at 2.1 A resolution. EMBO J. 17:1998;2451-2462.
    • (1998) EMBO J. , vol.17 , pp. 2451-2462
    • Niefind, K.1    Guerra, B.2    Pinna, L.A.3    Issinger, O.-G.4    Schomburg, D.5
  • 257
    • 0030831116 scopus 로고    scopus 로고
    • Bidirectional regulation of DARPP-32 phosphorylation by dopamine
    • Nishi A., Snyder G.L., Greengard P. Bidirectional regulation of DARPP-32 phosphorylation by dopamine. J. Neurosci. 17:1997;8147-8155.
    • (1997) J. Neurosci. , vol.17 , pp. 8147-8155
    • Nishi, A.1    Snyder, G.L.2    Greengard, P.3
  • 258
    • 0032577641 scopus 로고    scopus 로고
    • Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase 2 in vitro
    • Ohtsuki K., Maekawa T., Harada S., Karino A., Morikawa Y., Ito M. Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase 2 in vitro. FEBS Lett. 428:1998;235-240.
    • (1998) FEBS Lett. , vol.428 , pp. 235-240
    • Ohtsuki, K.1    Maekawa, T.2    Harada, S.3    Karino, A.4    Morikawa, Y.5    Ito, M.6
  • 259
    • 0022850973 scopus 로고
    • Microtubule-associated proteins
    • Olmsted J.B. Microtubule-associated proteins. A. Rev. Cell Biol. 2:1986;421-457.
    • (1986) A. Rev. Cell Biol. , vol.2 , pp. 421-457
    • Olmsted, J.B.1
  • 262
    • 0031172065 scopus 로고    scopus 로고
    • NF-κB: A crucial transcription factor for glial and neuronal cell function
    • O'Neill L.A.J., Kaltschmidt C. NF-κB: a crucial transcription factor for glial and neuronal cell function. Trends Neurosci. 20:1997;252-258.
    • (1997) Trends Neurosci. , vol.20 , pp. 252-258
    • O'Neill, L.A.J.1    Kaltschmidt, C.2
  • 263
    • 0242722234 scopus 로고    scopus 로고
    • Is the Ras-MAPK signalling pathway necessary for long-term memory formation
    • Orban P.C., Chapman P.F., Brambilla R. Is the Ras-MAPK signalling pathway necessary for long-term memory formation. TINS. 22:1999;38-44.
    • (1999) TINS , vol.22 , pp. 38-44
    • Orban, P.C.1    Chapman, P.F.2    Brambilla, R.3
  • 264
    • 0032516522 scopus 로고    scopus 로고
    • Protein kinase CK2α′ is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation
    • Orlandini M., Semplici F., Ferruzi R., Meggio F., Pinna L.A., Oliviero S. Protein kinase CK2α′ is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation. J. biol. Chem. 273:1998;21291-21297.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21291-21297
    • Orlandini, M.1    Semplici, F.2    Ferruzi, R.3    Meggio, F.4    Pinna, L.A.5    Oliviero, S.6
  • 265
    • 0027055846 scopus 로고
    • Purification of a soluble casein kinase 2 from Dictostelium discoideum lacking the β subunit: Regulation during proliferation and differentiation
    • Ospina B., Nunez A., Fernandez-Renart M. Purification of a soluble casein kinase 2 from Dictostelium discoideum lacking the β subunit: regulation during proliferation and differentiation. Mol. cell. Biochem. 118:1992;49-60.
    • (1992) Mol. Cell. Biochem. , vol.118 , pp. 49-60
    • Ospina, B.1    Nunez, A.2    Fernandez-Renart, M.3
  • 266
    • 0027057336 scopus 로고
    • Casein kinase 2 phosphorylation of signal sequence receptor α and the associated membrane chaperone calnexin
    • Ou W-J., Thomas D.Y., Bell A.W., Bergeron J.J.M. Casein kinase 2 phosphorylation of signal sequence receptor α and the associated membrane chaperone calnexin. J. biol. Chem. 267:1992;23789-23796.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23789-23796
    • Ou, W.-J.1    Thomas, D.Y.2    Bell, A.W.3    Bergeron, J.J.M.4
  • 267
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen D.J., Noble M.E.M., Garman E.F., Papageorgiou A.C., Johnson L.N. Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Structure. 3:1995;467-482.
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.M.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 268
    • 0025281150 scopus 로고
    • Isolation, sequencing and disruption of the yeast CKA2 gene: Casein kinase 2 is essential for viability in Saccharomyces cerevisiae
    • Padmanabha R., Chen-Wu J., Hanna D.E., Glover C.V.C. Isolation, sequencing and disruption of the yeast CKA2 gene: casein kinase 2 is essential for viability in Saccharomyces cerevisiae. Mol. cell. Biol. 10:1990;4089-4099.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4089-4099
    • Padmanabha, R.1    Chen-Wu, J.2    Hanna, D.E.3    Glover, C.V.C.4
  • 269
    • 0030176079 scopus 로고    scopus 로고
    • Recombinant BDNF rescues deficits in basal synaptic transmission and hippocampal LTP in BDNF knockout mice
    • Patterson S.L., Abel T., Deuel T.A.S., Martin K.C., Rose J.C., Kandel E.R. Recombinant BDNF rescues deficits in basal synaptic transmission and hippocampal LTP in BDNF knockout mice. Neuron. 16:1996;1137-1145.
    • (1996) Neuron , vol.16 , pp. 1137-1145
    • Patterson, S.L.1    Abel, T.2    Deuel, T.A.S.3    Martin, K.C.4    Rose, J.C.5    Kandel, E.R.6
  • 270
    • 0030778825 scopus 로고    scopus 로고
    • Neurotrophins as in vitro growth cone guidance molecules for embryonic sensory neurons
    • Paves H., Saarma M. Neurotrophins as in vitro growth cone guidance molecules for embryonic sensory neurons. Cell Tissue Res. 290:1997;285-298.
    • (1997) Cell Tissue Res. , vol.290 , pp. 285-298
    • Paves, H.1    Saarma, M.2
  • 271
    • 0027253644 scopus 로고
    • System for quantitation of gene expression in single cells by computerized microimaging: Application to c-fos expression after microinjection of anti-casein kinase 2 antibody
    • Pepperkok R., Herr S., Lorenz P., Pyerin W., Ansorge W. System for quantitation of gene expression in single cells by computerized microimaging: application to c-fos expression after microinjection of anti-casein kinase 2 antibody. Exp. Cell Res. 204:1993;278-285.
    • (1993) Exp. Cell Res. , vol.204 , pp. 278-285
    • Pepperkok, R.1    Herr, S.2    Lorenz, P.3    Pyerin, W.4    Ansorge, W.5
  • 272
    • 17144432951 scopus 로고    scopus 로고
    • The expression of casein kinase 2 alpha′ and phosphatase 2A activity
    • Perez M., Avila J. The expression of casein kinase 2 alpha′ and phosphatase 2A activity. Biochim. Biophys. Acta - Mol. Cell Res. 1449:1999;150-156.
    • (1999) Biochim. Biophys. Acta - Mol. Cell Res. , vol.1449 , pp. 150-156
    • Perez, M.1    Avila, J.2
  • 273
    • 0031783079 scopus 로고    scopus 로고
    • Prenatal ethanol exposure decreases GAP-43 phosphorylation and protein kinase C activity in the hippocampus of adult rat offspring
    • PerroneBizzozero N.I., Isaacson T.V., Keidan G.M.O., Eriqat C., Savage D.D., Allen A.M. Prenatal ethanol exposure decreases GAP-43 phosphorylation and protein kinase C activity in the hippocampus of adult rat offspring. J. Neurochem. 71:1998;2104-2111.
    • (1998) J. Neurochem. , vol.71 , pp. 2104-2111
    • Perronebizzozero, N.I.1    Isaacson, T.V.2    Keidan, G.M.O.3    Eriqat, C.4    Savage, D.D.5    Allen, A.M.6
  • 275
    • 0025113220 scopus 로고
    • Casein kinase 2: An "eminence grise" in cellular regulation
    • Pinna L.A. Casein kinase 2: an "eminence grise" in cellular regulation. Biochim. Biophys. Acta. 104:1990;267-284.
    • (1990) Biochim. Biophys. Acta , vol.104 , pp. 267-284
    • Pinna, L.A.1
  • 276
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation
    • Pinna L.A., Meggio F. Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog. Cell Cycle Res. 3:1997;77-79.
    • (1997) Prog. Cell Cycle Res. , vol.3 , pp. 77-79
    • Pinna, L.A.1    Meggio, F.2
  • 277
    • 0023718841 scopus 로고
    • Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase 2
    • Pisano M., Hegazi M.A., Reimann E.M., Dokas L.A. Phosphorylation of protein B-50 (GAP-43) from adult rat brain cortex by casein kinase 2. Biochem. biophys. Res. Commun. 155:1988;1207-1212.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , pp. 1207-1212
    • Pisano, M.1    Hegazi, M.A.2    Reimann, E.M.3    Dokas, L.A.4
  • 278
    • 0028559537 scopus 로고
    • Cytosolic factors in nuclear transport: What's importin?
    • Powers M.A., Forbes D.J. Cytosolic factors in nuclear transport: what's importin? Cell. 79:1994;931-934.
    • (1994) Cell , vol.79 , pp. 931-934
    • Powers, M.A.1    Forbes, D.J.2
  • 279
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt W.B. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. biol. Chem. 268:1993;21455-21458.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 280
    • 0023832296 scopus 로고
    • The brain in AIDS: Central nervous system HIV-1 infection and AIDS dementia complex
    • Price R.W., Brew B., Sidtis J., Rosenblum M., Scheck A.C., Cleary P. The brain in AIDS: central nervous system HIV-1 infection and AIDS dementia complex. Science. 239:1988;586-592.
    • (1988) Science , vol.239 , pp. 586-592
    • Price, R.W.1    Brew, B.2    Sidtis, J.3    Rosenblum, M.4    Scheck, A.C.5    Cleary, P.6
  • 281
    • 0028189423 scopus 로고
    • Human casein kinase 2: Structures, genes, expression and requirement in cell growth stimulation
    • Pyerin W. Human casein kinase 2: structures, genes, expression and requirement in cell growth stimulation. Adv. Enzyme Regul. 34:1994;225-246.
    • (1994) Adv. Enzyme Regul. , vol.34 , pp. 225-246
    • Pyerin, W.1
  • 282
    • 0023148911 scopus 로고
    • Catalytic and molecular properties of highly purified phosvitin/casein kinase type 2 from human epithelial cells in culture (HeLa) and relation to ecto protein kinase
    • Pyerin W., Burow E., Michaely K., Kübler D., Kinzel V. Catalytic and molecular properties of highly purified phosvitin/casein kinase type 2 from human epithelial cells in culture (HeLa) and relation to ecto protein kinase. Biol. Chem. Hoppe-Seyler. 368:1987;215-227.
    • (1987) Biol. Chem. Hoppe-Seyler , vol.368 , pp. 215-227
    • Pyerin, W.1    Burow, E.2    Michaely, K.3    Kübler, D.4    Kinzel, V.5
  • 283
    • 0344303068 scopus 로고
    • Protein kinases and cell growth: Molecular biological studies on the β-subunit of human casein kinase 2
    • Pyerin W., Voss H., Pepperkok R., Jakobi R., Wirkner U., Lorenz P. Protein kinases and cell growth: molecular biological studies on the β-subunit of human casein kinase 2. Rec. Adv. cell. Mol. Biol. 4:1992;87-100.
    • (1992) Rec. Adv. Cell. Mol. Biol. , vol.4 , pp. 87-100
    • Pyerin, W.1    Voss, H.2    Pepperkok, R.3    Jakobi, R.4    Wirkner, U.5    Lorenz, P.6
  • 284
    • 0029897541 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein tethered to the CD4 extracellular domain is localized to the plasma membrane and is biologically active in the secretory pathway of mammalian cells: Implications for the mechanisms of Vpu function
    • Raja N.U., Jabbar M.A. The human immunodeficiency virus type 1 Vpu protein tethered to the CD4 extracellular domain is localized to the plasma membrane and is biologically active in the secretory pathway of mammalian cells: implications for the mechanisms of Vpu function. Virology. 220:1996;141-151.
    • (1996) Virology , vol.220 , pp. 141-151
    • Raja, N.U.1    Jabbar, M.A.2
  • 285
    • 0029077622 scopus 로고
    • Temporal differences in the phosphorylation state of pre- And postsynaptic protein kinase C substrates B-50/GAP-43 and neurogranin during long-term potentiation
    • Ramakers G.M.J., De Graan P.N.E., Urban I.J.A., Kraay D., Tang T., Pasinelli P., Oestreicher A.B., Gispen W.H. Temporal differences in the phosphorylation state of pre- and postsynaptic protein kinase C substrates B-50/GAP-43 and neurogranin during long-term potentiation. J. biol. Chem. 270:1995;13892-13898.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13892-13898
    • Ramakers, G.M.J.1    De Graan, P.N.E.2    Urban, I.J.A.3    Kraay, D.4    Tang, T.5    Pasinelli, P.6    Oestreicher, A.B.7    Gispen, W.H.8
  • 286
    • 0032563118 scopus 로고    scopus 로고
    • Regulation of casein kinase 2 by direct interaction with cell surface receptor CD5
    • Raman C., Kuo A., Deshane J., Litchfield D.W., Kimberly R. Regulation of casein kinase 2 by direct interaction with cell surface receptor CD5. J. biol. Chem. 273:1998;19183-19189.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19183-19189
    • Raman, C.1    Kuo, A.2    Deshane, J.3    Litchfield, D.W.4    Kimberly, R.5
  • 287
    • 0032488840 scopus 로고    scopus 로고
    • Casein kinase 2 stabilizes the activity of human topoisomerase 2α in a phosphorylation-independent manner
    • Redwood C., Davies S.L., Wells N.J., Fry A.M., Hickson I.D. Casein kinase 2 stabilizes the activity of human topoisomerase 2α in a phosphorylation-independent manner. J. biol. Chem. 273:1998;3635-3642.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3635-3642
    • Redwood, C.1    Davies, S.L.2    Wells, N.J.3    Fry, A.M.4    Hickson, I.D.5
  • 289
    • 0033064008 scopus 로고    scopus 로고
    • Association of protein kinase CK2 with eukaryotic translation initiation factor elF-2 and with grp94/endoplasmin
    • Riera M., Roher N., Miro F., Gil C., Trujillo R., Aguilera J., Plana M., Itarte E. Association of protein kinase CK2 with eukaryotic translation initiation factor elF-2 and with grp94/endoplasmin. Mol. cell. Biochem. 191:1999;97-104.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 97-104
    • Riera, M.1    Roher, N.2    Miro, F.3    Gil, C.4    Trujillo, R.5    Aguilera, J.6    Plana, M.7    Itarte, E.8
  • 290
    • 0026026630 scopus 로고
    • The rate of nuclear cytoplasmic protein transport is determined by casein kinase 2 site flanking the nuclear localization sequence of the SV T-antigen
    • Rihis H.P., Jans D.A., Fan H., Peters R. The rate of nuclear cytoplasmic protein transport is determined by casein kinase 2 site flanking the nuclear localization sequence of the SV T-antigen. EMBO J. 10:1991;633-639.
    • (1991) EMBO J. , vol.10 , pp. 633-639
    • Rihis, H.P.1    Jans, D.A.2    Fan, H.3    Peters, R.4
  • 292
    • 0027416727 scopus 로고
    • Human casein kinase 2. The subunit α protein activates transcription of the subunit β gene
    • Robitzki A., Bodenback L., Voss H., Pyerin W. Human casein kinase 2. The subunit α protein activates transcription of the subunit β gene. J. biol. Chem. 268:1993;5694-5702.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5694-5702
    • Robitzki, A.1    Bodenback, L.2    Voss, H.3    Pyerin, W.4
  • 293
    • 0028081892 scopus 로고
    • The Schizosaccharomyces pompe casein kinase 2 α and β subunits: Evolutionary conservation and positive role of the β subunit
    • Roussou I., Draetta G. The Schizosaccharomyces pompe casein kinase 2 α and β subunits: evolutionary conservation and positive role of the β subunit. Mol. Cell Biol. 14:1994;576-586.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 576-586
    • Roussou, I.1    Draetta, G.2
  • 294
    • 0013690440 scopus 로고    scopus 로고
    • A novel signaling system from the synapse to the nucleus
    • Routtenberg A., Meberg P.M. A novel signaling system from the synapse to the nucleus. Trend Neurosci. 21:1998;106.
    • (1998) Trend Neurosci. , vol.21 , pp. 106
    • Routtenberg, A.1    Meberg, P.M.2
  • 295
    • 0026733342 scopus 로고
    • Casein kinase 2 phosphorylated p34cdc2 kinase in G1 phase of the HeLa cell division cycle
    • Russo G., Vandenberg M., Yu I.Y., Bae Y.-S., Franza B.R., Marshak D.R. Casein kinase 2 phosphorylated p34cdc2 kinase in G1 phase of the HeLa cell division cycle. J. biol. Chem. 267:1992;20317-20325.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20317-20325
    • Russo, G.1    Vandenberg, M.2    Yu, I.Y.3    Bae, Y.-S.4    Franza, B.R.5    Marshak, D.R.6
  • 297
    • 0032423888 scopus 로고    scopus 로고
    • Biochemical evidence that the N-terminal segments of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2
    • Sarno S., Marin O., Ghisellini P., Meggio F., Pinna L.A. Biochemical evidence that the N-terminal segments of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2. FEBS Lett. 441:1998;29-33.
    • (1998) FEBS Lett. , vol.441 , pp. 29-33
    • Sarno, S.1    Marin, O.2    Ghisellini, P.3    Meggio, F.4    Pinna, L.A.5
  • 298
    • 0023423872 scopus 로고
    • Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase
    • Saxena A., Padmanabha R., Glover C.V.C. Isolation and sequencing of cDNA clones encoding alpha and beta subunits of Drosophila melanogaster casein kinase. Mol. cell. Biol. 7:1987;3409-3412.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3409-3412
    • Saxena, A.1    Padmanabha, R.2    Glover, C.V.C.3
  • 299
    • 0028965141 scopus 로고
    • Glycans and the modulation of neural-recognition molecule function
    • Schachner M., Martini R. Glycans and the modulation of neural-recognition molecule function. Trends Neurosci. 18:1995;183-191.
    • (1995) Trends Neurosci. , vol.18 , pp. 183-191
    • Schachner, M.1    Martini, R.2
  • 300
    • 0032944350 scopus 로고    scopus 로고
    • Memory consolidation for contextual and auditory fear conditioning is dependent on protein synthesis, PKA, and MAP kinase
    • Schafe G.E., Nadel N.V., Sullivan G.M., Harris A., LeDoux J.E. Memory consolidation for contextual and auditory fear conditioning is dependent on protein synthesis, PKA, and MAP kinase. Learning and Memory. 6:1999;97-110.
    • (1999) Learning and Memory , vol.6 , pp. 97-110
    • Schafe, G.E.1    Nadel, N.V.2    Sullivan, G.M.3    Harris, A.4    Ledoux, J.E.5
  • 301
    • 0023816256 scopus 로고
    • Nucleolin (C23), a physiological substrate for casein kinase 2
    • Schneider H.R., Issinger O.-G. Nucleolin (C23), a physiological substrate for casein kinase 2. Biochem. Biophys. Res. Commun. 156:1988;1390-1397.
    • (1988) Biochem. Biophys. Res. Commun. , vol.156 , pp. 1390-1397
    • Schneider, H.R.1    Issinger, O.-G.2
  • 302
    • 0343658045 scopus 로고
    • CK2, a multifunctional protein kinase and its role during proliferation
    • Schneider H.R., Issinger O.-G. CK2, a multifunctional protein kinase and its role during proliferation. Biotec. Europe. 6:1989;82-88.
    • (1989) Biotec. Europe , vol.6 , pp. 82-88
    • Schneider, H.R.1    Issinger, O.-G.2
  • 304
    • 0029015092 scopus 로고
    • Protein phosphorylation in neuronal plasticity and gene expression
    • Schulman H. Protein phosphorylation in neuronal plasticity and gene expression. Curr. Opin. Neurobiol. 5:1995;375-381.
    • (1995) Curr. Opin. Neurobiol. , vol.5 , pp. 375-381
    • Schulman, H.1
  • 305
    • 0029665597 scopus 로고    scopus 로고
    • Constitutive phosphorylation of IκBα by casein kinase 2 occurs preferentially at serine 293: Requirement for degradation of free IκBα
    • Schwarz E.M., Van Antwerp D., Verma I.M. Constitutive phosphorylation of IκBα by casein kinase 2 occurs preferentially at serine 293: requirement for degradation of free IκBα Mol. cell. Biol. 16:1996;3554-3559.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3554-3559
    • Schwarz, E.M.1    Van Antwerp, D.2    Verma, I.M.3
  • 306
    • 0032544409 scopus 로고    scopus 로고
    • Phosphorylation of vitronectin by casein kinase 2. Identification of the sites and their promotion of cell adhesion and spreading
    • Seger D., Gechtman Z., Shaltiel S. Phosphorylation of vitronectin by casein kinase 2. Identification of the sites and their promotion of cell adhesion and spreading. J. biol. Chem. 273:1998;24805-24813.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24805-24813
    • Seger, D.1    Gechtman, Z.2    Shaltiel, S.3
  • 307
    • 0028985936 scopus 로고
    • Casein kinase 2α transgene-induced murine lymphoma: Relation to Theileriosis in cattle
    • Seldin D.C., Leder P. Casein kinase 2α transgene-induced murine lymphoma: relation to Theileriosis in cattle. Science. 267:1995;894-897.
    • (1995) Science , vol.267 , pp. 894-897
    • Seldin, D.C.1    Leder, P.2
  • 308
    • 0022844710 scopus 로고
    • Localization of the high-affinity calcium-binding site on tubulin molecule
    • Serrano L., Valencia A., Caballero R., Avila J. Localization of the high-affinity calcium-binding site on tubulin molecule. J. biol. Chem. 261:1986;7076-7081.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7076-7081
    • Serrano, L.1    Valencia, A.2    Caballero, R.3    Avila, J.4
  • 309
    • 0023424860 scopus 로고
    • Tubulin phosphorylation by casein kinase 2 is similar to that found in vivo
    • Serrano L., Diaz-Nido J., Wandosell F., Avila J. Tubulin phosphorylation by casein kinase 2 is similar to that found in vivo. J. Cell Biol. 105:1987;1731-1739.
    • (1987) J. Cell Biol. , vol.105 , pp. 1731-1739
    • Serrano, L.1    Diaz-Nido, J.2    Wandosell, F.3    Avila, J.4
  • 312
    • 0027984076 scopus 로고
    • The hippocampus: A biological model for studying learning and memory
    • Shen Y., Specht S.M., De Saint Ghislain I., Li R. The hippocampus: a biological model for studying learning and memory. Prog. Neurobiol. 44:1994;485-496.
    • (1994) Prog. Neurobiol. , vol.44 , pp. 485-496
    • Shen, Y.1    Specht, S.M.2    De Saint Ghislain, I.3    Li, R.4
  • 313
    • 0030019841 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel casein kinase 2 substrate, HASPP28, from rat brain
    • Shen L., Huang K-P., Chen H-C., Huang F.L. Molecular cloning and characterization of a novel casein kinase 2 substrate, HASPP28, from rat brain. Arch. Biochem. Biophys. 327:1996;131-141.
    • (1996) Arch. Biochem. Biophys. , vol.327 , pp. 131-141
    • Shen, L.1    Huang, K.-P.2    Chen, H.-C.3    Huang, F.L.4
  • 314
    • 0025267015 scopus 로고
    • The regulation and function of c-fos and other immediate early genes in the nervous system
    • Sheng M., Greenberg M.E. The regulation and function of c-fos and other immediate early genes in the nervous system. Neuron. 4:1990;477-485.
    • (1990) Neuron , vol.4 , pp. 477-485
    • Sheng, M.1    Greenberg, M.E.2
  • 315
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signalling
    • Shepherd P., Withers D.J., Siddle K. Phosphoinositide 3-kinase: the key switch mechanism in insulin signalling. Biochem. J. 333:1998;471-490.
    • (1998) Biochem. J. , vol.333 , pp. 471-490
    • Shepherd, P.1    Withers, D.J.2    Siddle, K.3
  • 316
    • 0033056148 scopus 로고    scopus 로고
    • A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CK2
    • Sheu G.T., Traugh J.A. A structural model for elongation factor 1 (EF-1) and phosphorylation by protein kinase CK2. Mol. cell. Biochem. 199:1999;181-186.
    • (1999) Mol. Cell. Biochem. , vol.199 , pp. 181-186
    • Sheu, G.T.1    Traugh, J.A.2
  • 317
    • 0023181166 scopus 로고
    • Colocalization of MAP-1A and MAP-2 on neuronal microtubules in situ revealed with double-label immunofluorescence microscopy
    • Shiomura Y., Hirokawa N. Colocalization of MAP-1A and MAP-2 on neuronal microtubules in situ revealed with double-label immunofluorescence microscopy. J. Cell Biol. 104:1987;1575-1578.
    • (1987) J. Cell Biol. , vol.104 , pp. 1575-1578
    • Shiomura, Y.1    Hirokawa, N.2
  • 318
    • 0026046957 scopus 로고
    • A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase 2
    • Shiozaki K., Yanagida M. A functional 125-kDa core polypeptide of fission yeast DNA topoisomerase 2. Mol. cell. Biol. 11:1991;6093-6102.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6093-6102
    • Shiozaki, K.1    Yanagida, M.2
  • 319
    • 0022249124 scopus 로고
    • Glycogen synthase (casein) kinase-1: Tissue distribution and subcellular localization
    • Singh T.J., Huang K. Glycogen synthase (casein) kinase-1: tissue distribution and subcellular localization. FEBS Lett. 190:1985;84-88.
    • (1985) FEBS Lett. , vol.190 , pp. 84-88
    • Singh, T.J.1    Huang, K.2
  • 320
    • 0032514233 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor rapidly potentiates synaptic transmission through NMDA, but suppresses it through non-NMDA receptor in rat hippocampal neuron
    • Song D-K., Choe B-k., Bae J.H., Park W.K., Han I.S., Ho W-K., Earm Y.E. Brain-derived neurotrophic factor rapidly potentiates synaptic transmission through NMDA, but suppresses it through non-NMDA receptor in rat hippocampal neuron. Brain Res. 799:1998;176-179.
    • (1998) Brain Res. , vol.799 , pp. 176-179
    • Song, D.-K.1    Choe, B.-k.2    Bae, J.H.3    Park, W.K.4    Han, I.S.5    Ho, W.-K.6    Earm, Y.E.7
  • 322
    • 0030461275 scopus 로고    scopus 로고
    • Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A
    • Sontag E., Nunbhakdi-Craig V., Lee G., Bloom G.S., Mumby M.C. Regulation of the phosphorylation state and microtubule-binding activity of Tau by protein phosphatase 2A. Neuron. 17:1996;1201-1207.
    • (1996) Neuron , vol.17 , pp. 1201-1207
    • Sontag, E.1    Nunbhakdi-Craig, V.2    Lee, G.3    Bloom, G.S.4    Mumby, M.C.5
  • 323
    • 0027715235 scopus 로고
    • A majority of casein kinase 2 α subunit is tightly bound to intranuclear components but not to the β subunit
    • Stigare J., Buddelmeijer N., Pigon A., Egyhazi E. A majority of casein kinase 2 α subunit is tightly bound to intranuclear components but not to the β subunit. Mol. cell. Biochem. 129:1993;77-85.
    • (1993) Mol. Cell. Biochem. , vol.129 , pp. 77-85
    • Stigare, J.1    Buddelmeijer, N.2    Pigon, A.3    Egyhazi, E.4
  • 324
    • 0032536810 scopus 로고    scopus 로고
    • Brain protein phosphatase 2A: Developmental regulation and distinct cellular and subcellular localization by B subunits
    • Strack S., Zaucha J.A., Ebner F.F., Colbran R.J., Wadzinski B.E. Brain protein phosphatase 2A: developmental regulation and distinct cellular and subcellular localization by B subunits. J. comp. Neurol. 392:1998;515-527.
    • (1998) J. Comp. Neurol. , vol.392 , pp. 515-527
    • Strack, S.1    Zaucha, J.A.2    Ebner, F.F.3    Colbran, R.J.4    Wadzinski, B.E.5
  • 325
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 326
    • 0022391350 scopus 로고
    • Effects of androgen and polyamines on the phosphorylation of nucleolar proteins from rat ventral prostates with particular reference to 110-kDa phosphoprotein
    • Suzuki N., Matsui H., Hosoya T. Effects of androgen and polyamines on the phosphorylation of nucleolar proteins from rat ventral prostates with particular reference to 110-kDa phosphoprotein. J. biol. Chem. 260:1985;8050-8055.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8050-8055
    • Suzuki, N.1    Matsui, H.2    Hosoya, T.3
  • 327
    • 0023182945 scopus 로고
    • In vivo effects of dexamethasone and cycloheximide on the phosphorylation of 110 kDa proteins and the protein kinase activities of rat liver nucleoli
    • Suzuki N., Saitoh T., Hosoya T. In vivo effects of dexamethasone and cycloheximide on the phosphorylation of 110 kDa proteins and the protein kinase activities of rat liver nucleoli. J. biol. Chem. 262:1987;4696-4700.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4696-4700
    • Suzuki, N.1    Saitoh, T.2    Hosoya, T.3
  • 328
    • 0026655113 scopus 로고
    • Effect of dexamethasone on nucleolar casein kinase 2 activity and phosphorylation of nucleolin in lymphosarcoma P1798 cells
    • Suzuki N., Suzuki T., Uchida A., Thompson E.A., Hosoya T. Effect of dexamethasone on nucleolar casein kinase 2 activity and phosphorylation of nucleolin in lymphosarcoma P1798 cells. J. Steroid Biochem. Molec. Biol. 42:1992;305-312.
    • (1992) J. Steroid Biochem. Molec. Biol. , vol.42 , pp. 305-312
    • Suzuki, N.1    Suzuki, T.2    Uchida, A.3    Thompson, E.A.4    Hosoya, T.5
  • 330
    • 0023374853 scopus 로고
    • Amino acid sequence of the beta subunit of bovine lung casein kinase 2
    • Takio K., Kuenzel E.A., Walsh K.A., Krebs E.G. Amino acid sequence of the beta subunit of bovine lung casein kinase 2. Proc. natl Acad. Sci. USA. 84:1987;4851-4855.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4851-4855
    • Takio, K.1    Kuenzel, E.A.2    Walsh, K.A.3    Krebs, E.G.4
  • 331
    • 0028290651 scopus 로고
    • Association of casein kinase 2 with nuclear matrix. Possible role in nuclear matrix protein phosphorylation
    • Tawfic S., Ahmed K. Association of casein kinase 2 with nuclear matrix. Possible role in nuclear matrix protein phosphorylation. J. biol. Chem. 269:1994;7489-7493.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7489-7493
    • Tawfic, S.1    Ahmed, K.2
  • 332
    • 0027267678 scopus 로고
    • Androgenic regulation of the expression and phosphorylation of prostatic nucleolar protein B23
    • Tawfic S., Goueli S.A., Olson M.O.J., Ahmed K. Androgenic regulation of the expression and phosphorylation of prostatic nucleolar protein B23. Cell. Mol. Biol. Res. 39:1993;43-51.
    • (1993) Cell. Mol. Biol. Res. , vol.39 , pp. 43-51
    • Tawfic, S.1    Goueli, S.A.2    Olson, M.O.J.3    Ahmed, K.4
  • 333
    • 0029798888 scopus 로고    scopus 로고
    • Nuclear matrix as an anchor for protein kinase CK2 nuclear signalling
    • Tawfic S., Faust R.A., Gapany M., Ahmed K. Nuclear matrix as an anchor for protein kinase CK2 nuclear signalling. J. cell. Biochem. 62:1996;165-171.
    • (1996) J. Cell. Biochem. , vol.62 , pp. 165-171
    • Tawfic, S.1    Faust, R.A.2    Gapany, M.3    Ahmed, K.4
  • 335
    • 0028866230 scopus 로고
    • Neurotrophins and neuronal plasticity
    • Thoenen H. Neurotrophins and neuronal plasticity. Science. 270:1995;593-597.
    • (1995) Science , vol.270 , pp. 593-597
    • Thoenen, H.1
  • 336
    • 0028986194 scopus 로고
    • IκB-β regulates the persistent response in a biphasic activation of NF-κB
    • Thompson J.E., Phillips R.J., Erdjument-Bromage H., Tempst P., Ghosh S. IκB-β regulates the persistent response in a biphasic activation of NF-κB. Cell. 80:1995;573-582.
    • (1995) Cell , vol.80 , pp. 573-582
    • Thompson, J.E.1    Phillips, R.J.2    Erdjument-Bromage, H.3    Tempst, P.4    Ghosh, S.5
  • 337
    • 0017747503 scopus 로고
    • Purification of rat liver nuclear protein kinase N2
    • Thornburg W., Lindell T.J. Purification of rat liver nuclear protein kinase N2. J. biol. Chem. 252:1977;6660-6665.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6660-6665
    • Thornburg, W.1    Lindell, T.J.2
  • 339
    • 0027755168 scopus 로고
    • Casein kinase 2 β-subunit inhibits the activity of the catalytic α-subunit in the absence of salt
    • Tiganis T., House C.M., Kemp B.E. Casein kinase 2 β-subunit inhibits the activity of the catalytic α-subunit in the absence of salt. Biochim. Biophys. Acta. 1203:1993;282-289.
    • (1993) Biochim. Biophys. Acta , vol.1203 , pp. 282-289
    • Tiganis, T.1    House, C.M.2    Kemp, B.E.3
  • 340
    • 0021006448 scopus 로고
    • Phosphorylation of acetyl-coenzyme A carboxylase by casein kinase 1 and casein kinase 2
    • Tipper J.P., Bacon G.W., Witters L.A. Phosphorylation of acetyl-coenzyme A carboxylase by casein kinase 1 and casein kinase 2. Arch. Biochem. Biophys. 227:1983;386-396.
    • (1983) Arch. Biochem. Biophys. , vol.227 , pp. 386-396
    • Tipper, J.P.1    Bacon, G.W.2    Witters, L.A.3
  • 342
    • 0026465665 scopus 로고
    • ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes
    • Troelstra C., van Gool A., de Wit J., Vermeulen W., Bootsma D., Hoeijmakers J.H.J. ERCC6, a member of a subfamily of putative helicases, is involved in Cockayne's syndrome and preferential repair of active genes. Cell. 71:1992;939-953.
    • (1992) Cell , vol.71 , pp. 939-953
    • Troelstra, C.1    Van Gool, A.2    De Wit, J.3    Vermeulen, W.4    Bootsma, D.5    Hoeijmakers, J.H.J.6
  • 344
    • 0001320048 scopus 로고
    • Casein kinase 1 and 2-multipotential serine protein kinases: Structure, function and regulation
    • P. Greengard, Robinson G.A. New York: Raven Press
    • Tuazon P.T., Traugh J.A. Casein kinase 1 and 2-multipotential serine protein kinases: structure, function and regulation. Greengard P., Robinson G.A. Advances in Second Messenger and Phosphoprotein Research. vol. 23:1991;126-264 Raven Press, New York.
    • (1991) Advances in Second Messenger and Phosphoprotein Research , vol.23 , pp. 126-264
    • Tuazon, P.T.1    Traugh, J.A.2
  • 345
    • 0030601135 scopus 로고    scopus 로고
    • Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase 2 increases estrogen response element binding but does not alter ligand stability
    • Tzeng D.T., Klinge C.M. Phosphorylation of purified estradiol-liganded estrogen receptor by casein kinase 2 increases estrogen response element binding but does not alter ligand stability. Biochem. biophys. Res. Commun. 223:1996;554-560.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 554-560
    • Tzeng, D.T.1    Klinge, C.M.2
  • 346
    • 0027538331 scopus 로고
    • Depletion of casein kinase 2 by antisense oligonucleotide prevents neuritogenesis in neuroblastoma cells
    • Ulloa L., Diaz-Nido J., Avila J. Depletion of casein kinase 2 by antisense oligonucleotide prevents neuritogenesis in neuroblastoma cells. EMBO J. 12:1993;1633-1640.
    • (1993) EMBO J. , vol.12 , pp. 1633-1640
    • Ulloa, L.1    Diaz-Nido, J.2    Avila, J.3
  • 347
    • 0030062446 scopus 로고    scopus 로고
    • Mapping the residues of protein kinase CK2 α subunit responsible for responsiveness to polyanionic inhibitors
    • Vaglio P., Sarno S., Marin O., Meggio F., Issinger O.-G., Pinna L.A. Mapping the residues of protein kinase CK2 α subunit responsible for responsiveness to polyanionic inhibitors. FEBS Lett. 380:1996;25-28.
    • (1996) FEBS Lett. , vol.380 , pp. 25-28
    • Vaglio, P.1    Sarno, S.2    Marin, O.3    Meggio, F.4    Issinger, O.-G.5    Pinna, L.A.6
  • 348
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallée B.L., Auld D.S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry. 29:1990;5647-5659.
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallée, B.L.1    Auld, D.S.2
  • 349
    • 0026591023 scopus 로고
    • The nucleolar transcription factor mUBF is phosphoylated by casein kinase 2 in the C-terminal hyperacidic tail which is essential for transactivation
    • Voit R., Schnapp A., Kuhn A., Rosenbauer H., Hirschmann P., Stunnerberg H.G., Grummt I. The nucleolar transcription factor mUBF is phosphoylated by casein kinase 2 in the C-terminal hyperacidic tail which is essential for transactivation. EMBO J. 11:1992;2210-2218.
    • (1992) EMBO J. , vol.11 , pp. 2210-2218
    • Voit, R.1    Schnapp, A.2    Kuhn, A.3    Rosenbauer, H.4    Hirschmann, P.5    Stunnerberg, H.G.6    Grummt, I.7
  • 351
    • 0025987814 scopus 로고
    • Isolation and expression of cDNA clones encoding mammalian poly(A)polymerase
    • Wahle E., Martin G., Schitz E., Keller W. Isolation and expression of cDNA clones encoding mammalian poly(A)polymerase. EMBO J. 10:1991;4251-4257.
    • (1991) EMBO J. , vol.10 , pp. 4251-4257
    • Wahle, E.1    Martin, G.2    Schitz, E.3    Keller, W.4
  • 352
    • 0021337614 scopus 로고
    • DARPP-32, a dopamine- And adenosine 3′:5′-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. 1. Regional and cellular distribution in the rat brain
    • Walaas S.I., Greengard P. DARPP-32, a dopamine- and adenosine 3′:5′-monophosphate-regulated phosphoprotein enriched in dopamine-innervated brain regions. 1. Regional and cellular distribution in the rat brain. J. Neurosci. 4:1984;84-98.
    • (1984) J. Neurosci. , vol.4 , pp. 84-98
    • Walaas, S.I.1    Greengard, P.2
  • 353
    • 0020596656 scopus 로고
    • Identity of the in vitro phosphorylation site in high mobility group protein in Hela cells with the site phosphorylated by casein kinase 2 in vitro
    • Walton G.M., Gill G.N. Identity of the in vitro phosphorylation site in high mobility group protein in Hela cells with the site phosphorylated by casein kinase 2 in vitro. J. biol. Chem. 258:1983;4440-4446.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4440-4446
    • Walton, G.M.1    Gill, G.N.2
  • 355
    • 0029129557 scopus 로고
    • Serine/threonine protein phosphatases
    • Wera S., Hemmings B.A. Serine/threonine protein phosphatases. Biochem. J. 311:1995;17-29.
    • (1995) Biochem. J. , vol.311 , pp. 17-29
    • Wera, S.1    Hemmings, B.A.2
  • 357
    • 0033534615 scopus 로고    scopus 로고
    • Identification of kinase phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A
    • Westphal R.S., Coffee R.L., Marotta A. Jr, Pelech S.L., Wadzinski B.E. Identification of kinase phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A. J. biol. Chem. 274:1999;687-692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 687-692
    • Westphal, R.S.1    Coffee, R.L.2    Marotta A., Jr.3    Pelech, S.L.4    Wadzinski, B.E.5
  • 358
    • 0031027599 scopus 로고    scopus 로고
    • Systems of memory in the human brain
    • Willingham D.B. Systems of memory in the human brain. Neuron. 18:1997;5-8.
    • (1997) Neuron , vol.18 , pp. 5-8
    • Willingham, D.B.1
  • 359
    • 0030976507 scopus 로고    scopus 로고
    • Casein kinase 2 catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3
    • Wilson L.K., Dhillon N., Thorner J., Martin G.S. Casein kinase 2 catalyzes tyrosine phosphorylation of the yeast nucleolar immunophilin Fpr3. J. biol. Chem. 272:1997;12961-12967.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12961-12967
    • Wilson, L.K.1    Dhillon, N.2    Thorner, J.3    Martin, G.S.4
  • 360
    • 0032588904 scopus 로고    scopus 로고
    • CK2 alpha loci in the human genome: Structure and transcriptional activity
    • Wirkner U., Pyerin W. CK2 alpha loci in the human genome: structure and transcriptional activity. Mol. cell. Biochem. 191:1999;59-64.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 59-64
    • Wirkner, U.1    Pyerin, W.2
  • 361
    • 0026632846 scopus 로고
    • Human casein kinase 2 subunit α: Sequence of a processed (pseudo) gene and its localization on chromosome 11
    • Wirkner U., Voss H., Lichter P., Weitz S., Ansorge A., Pyerin W. Human casein kinase 2 subunit α: sequence of a processed (pseudo) gene and its localization on chromosome 11. Biochim. Biophys. Acta. 1131:1992;220-222.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 220-222
    • Wirkner, U.1    Voss, H.2    Lichter, P.3    Weitz, S.4    Ansorge, A.5    Pyerin, W.6
  • 362
    • 0030066569 scopus 로고    scopus 로고
    • Casein kinase 2 phosphorylates the neural cell adhesion molecule L1
    • Wong E.V., Schaefer A.W., Landreth G., Lemmon V. Casein kinase 2 phosphorylates the neural cell adhesion molecule L1. J. Neurochem. 66:1996;779-786.
    • (1996) J. Neurochem. , vol.66 , pp. 779-786
    • Wong, E.V.1    Schaefer, A.W.2    Landreth, G.3    Lemmon, V.4
  • 363
  • 364
    • 0028844508 scopus 로고
    • The cellular factor TRP-185 regulates RNA polymerase 2 binding to HIV-1 TAR RNA
    • Wu-Baer F., Lane W.S., Gaynor R.B. The cellular factor TRP-185 regulates RNA polymerase 2 binding to HIV-1 TAR RNA. EMBO J. 14:1995;5995-6009.
    • (1995) EMBO J. , vol.14 , pp. 5995-6009
    • Wu-Baer, F.1    Lane, W.S.2    Gaynor, R.B.3
  • 365
    • 0030068092 scopus 로고    scopus 로고
    • Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase 2 and TRP-185 to human immunodeficient virus 1 TAR RNA
    • Wu-Baer F., Lane W.S., Gaynor R.B. Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase 2 and TRP-185 to human immunodeficient virus 1 TAR RNA. J. biol. Chem. 271:1996;4201-4208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4201-4208
    • Wu-Baer, F.1    Lane, W.S.2    Gaynor, R.B.3
  • 366
    • 0023712739 scopus 로고
    • Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB
    • Yamamoto K.K., Gonzalez G.A., Biggs W.H., Montminy M.R. Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREB. Nature. 334:1988;494-497.
    • (1988) Nature , vol.334 , pp. 494-497
    • Yamamoto, K.K.1    Gonzalez, G.A.2    Biggs, W.H.3    Montminy, M.R.4
  • 367
    • 0026328078 scopus 로고
    • Mapping of the human casein kinase 2 catalytic subunit genes: Two loci carrying the homologous sequences for the α subunit
    • Yang-Feng T.L., Zheng K., Kopatz I., Naiman T., Canaani D. Mapping of the human casein kinase 2 catalytic subunit genes: two loci carrying the homologous sequences for the α subunit. Nucleic Acids Res. 19:1991;7125-7129.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 7125-7129
    • Yang-Feng, T.L.1    Zheng, K.2    Kopatz, I.3    Naiman, T.4    Canaani, D.5
  • 368
    • 0028337445 scopus 로고
    • Isolation of two E-box binding factors that interact with the rat tyrosine hydroxylase enhancer
    • Yoon S.O., Chikaraishi D.M. Isolation of two E-box binding factors that interact with the rat tyrosine hydroxylase enhancer. J. biol. Chem. 269:1994;18453-18462.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18453-18462
    • Yoon, S.O.1    Chikaraishi, D.M.2
  • 369
    • 0026080046 scopus 로고
    • Immunocytochemical localization of casein kinase 2 during interphase and mitosis
    • Yu I.J., Spector D.L., Bae Y.-S., Marshak D.R. Immunocytochemical localization of casein kinase 2 during interphase and mitosis. J. Cell Biol. 114:1991;1217-1232.
    • (1991) J. Cell Biol. , vol.114 , pp. 1217-1232
    • Yu, I.J.1    Spector, D.L.2    Bae, Y.-S.3    Marshak, D.R.4
  • 370
  • 371
    • 0023000520 scopus 로고
    • Casein kinase type 2 is involved in the inhibition by 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole of specific RNA polymerase 2 transcription
    • Zandomeni R., Zandomeni M.C., Shugar D., Weinmann R. Casein kinase type 2 is involved in the inhibition by 5,6-dichloro-1-β-D-ribofuranosylbenzimidazole of specific RNA polymerase 2 transcription. J. biol. Chem. 261:1986;3414-3419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 3414-3419
    • Zandomeni, R.1    Zandomeni, M.C.2    Shugar, D.3    Weinmann, R.4
  • 372
    • 0029834383 scopus 로고    scopus 로고
    • Tat-SF1: Cofactor for stimulation of transcriptional elongation by HIV-1 Tat
    • Zhou Q., Sharp P.A. Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science. 274:1996;605-610.
    • (1996) Science , vol.274 , pp. 605-610
    • Zhou, Q.1    Sharp, P.A.2


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