메뉴 건너뛰기




Volumn 307, Issue 1, 2003, Pages 31-40

The protein kinase 60S is a free catalytic CK2α′ subunit and forms an inactive complex with superoxide dismutase SOD1

Author keywords

CK2 ; P1 P2 proteins; Protein kinases; Ribosome phosphorylation; SOD1; Yeast

Indexed keywords

BENZOTRIAZOLE DERIVATIVE; CASEIN KINASE II; CREATINE KINASE MB; PROTEIN KINASE 60S; PROTEIN SUBUNIT; SUPEROXIDE DISMUTASE; UNCLASSIFIED DRUG;

EID: 0038726155     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01126-4     Document Type: Article
Times cited : (22)

References (74)
  • 2
    • 0027997895 scopus 로고
    • The growth of research on protein phosphorylation
    • Krebs E.G. The growth of research on protein phosphorylation. Trends Biochem. Sci. 19:1994;439-444.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 439-444
    • Krebs, E.G.1
  • 3
    • 0029686290 scopus 로고    scopus 로고
    • The large ribosomal subunit stalk as a regulatory element of the eucaryotic translational machinery
    • Ballesta J.P.G., Remacha M. The large ribosomal subunit stalk as a regulatory element of the eucaryotic translational machinery. Prog. Nucl. Acid Res. Mol. Biol. 55:1996;157-193.
    • (1996) Prog. Nucl. Acid Res. Mol. Biol. , vol.55 , pp. 157-193
    • Ballesta, J.P.G.1    Remacha, M.2
  • 4
    • 0025988135 scopus 로고
    • Functional aspects of ribosomal proteins
    • Möller W. Functional aspects of ribosomal proteins. Biochimie. 73:1991;1093-1100.
    • (1991) Biochimie , vol.73 , pp. 1093-1100
    • Möller, W.1
  • 5
    • 0035999791 scopus 로고    scopus 로고
    • Structure and function of the acidic ribosomal stalk proteins
    • Wahl M.C., Möller W. Structure and function of the acidic ribosomal stalk proteins. Curr. Prot. Pept. Sci. 3:2002;93-106.
    • (2002) Curr. Prot. Pept. Sci. , vol.3 , pp. 93-106
    • Wahl, M.C.1    Möller, W.2
  • 6
    • 0024448354 scopus 로고
    • Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaebacterial, eubacterial and eucaryotes
    • Shimmin L.C., Ramirez G., Matheson A.T., Dennis P.P. Sequence alignment and evolutionary comparison of the L10 equivalent and L12 equivalent ribosomal proteins from archaebacterial, eubacterial and eucaryotes. J. Mol. Evol. 29:1989;448-462.
    • (1989) J. Mol. Evol. , vol.29 , pp. 448-462
    • Shimmin, L.C.1    Ramirez, G.2    Matheson, A.T.3    Dennis, P.P.4
  • 7
    • 0025988131 scopus 로고
    • The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins
    • Wool I.G., Chan Y.L., Glück A., Suzuki K. The primary structure of rat ribosomal proteins P0, P1, and P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie. 73:1991;861-870.
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.G.1    Chan, Y.L.2    Glück, A.3    Suzuki, K.4
  • 8
    • 0023445178 scopus 로고
    • Human acidic ribosomal phosphoproteins P0, P1 and P2. Analysis of cDNA clones, in vitro synthesis and assembly
    • Rich B.E., Steitz J.A. Human acidic ribosomal phosphoproteins P0, P1 and P2. Analysis of cDNA clones, in vitro synthesis and assembly. Mol. Cell. Biol. 7:1987;4065-4074.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4065-4074
    • Rich, B.E.1    Steitz, J.A.2
  • 10
    • 0018269897 scopus 로고
    • Isolation and characterization of the acidic phosphoproteins of 60S ribosomes from Artemia salina and a rat liver
    • van Agthoven A., Kriek A., Amons R., Möller W. Isolation and characterization of the acidic phosphoproteins of 60S ribosomes from Artemia salina and a rat liver. Eur. J. Biochem. 91:1978;553-556.
    • (1978) Eur. J. Biochem. , vol.91 , pp. 553-556
    • Van Agthoven, A.1    Kriek, A.2    Amons, R.3    Möller, W.4
  • 11
    • 18344418282 scopus 로고
    • DNA and deduced amino acid sequence of Drosophila rp21C, another "A" type ribosomal protein
    • Wigboldus J.D. DNA and deduced amino acid sequence of Drosophila rp21C, another "A" type ribosomal protein. Nucleic Acids Res. 15:1987;10064.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 10064
    • Wigboldus, J.D.1
  • 12
    • 0023099147 scopus 로고
    • Structural analysis of the Drosophila rPA1 gene, a member of he eucaryotic "A" type ribosomal protein family
    • Qian S., Zhang J.-Y., Kay M.A., Jacobs-Morena M. Structural analysis of the Drosophila rPA1 gene, a member of he eucaryotic "A" type ribosomal protein family. Nucleic Acids Res. 15:1987;987-1003.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 987-1003
    • Qian, S.1    Zhang, J.-Y.2    Kay, M.A.3    Jacobs-Morena, M.4
  • 13
    • 0024296614 scopus 로고
    • CDNA and deduced amino acid sequence of acidic ribosomal protein A2 from Saccharomyces cerevisiae
    • Mitsui K., Tsurugi K. cDNA and deduced amino acid sequence of acidic ribosomal protein A2 from Saccharomyces cerevisiae. Nucleic Acids Res. 16:1988;3575.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3575
    • Mitsui, K.1    Tsurugi, K.2
  • 14
    • 0023952119 scopus 로고
    • Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae
    • Remacha M., Saenz-Roblez M.T., Vilella M.D., Ballesta J.P.G. Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae. J. Biol. Chem. 263:1988;9094-9101.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9094-9101
    • Remacha, M.1    Saenz-Roblez, M.T.2    Vilella, M.D.3    Ballesta, J.P.G.4
  • 15
    • 0025437720 scopus 로고
    • A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 protein and a single form of the L10-equivalent ribosomal protein
    • Newton C.H., Shimmin L.C., Yee J., Dennis P.P. A family of genes encode the multiple forms of the Saccharomyces cerevisiae ribosomal proteins equivalent to the Escherichia coli L12 protein and a single form of the L10-equivalent ribosomal protein. J. Bacteriol. 172:1990;579-588.
    • (1990) J. Bacteriol. , vol.172 , pp. 579-588
    • Newton, C.H.1    Shimmin, L.C.2    Yee, J.3    Dennis, P.P.4
  • 16
    • 0025321217 scopus 로고
    • A gene family for acidic ribosomal proteins in Saccharomyces pombe: Two essential and two nonessential genes
    • Belrame M., Bianchi M.E. A gene family for acidic ribosomal proteins in Saccharomyces pombe: two essential and two nonessential genes. Mol. Cell. Biol. 10:1990;2341-2348.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2341-2348
    • Belrame, M.1    Bianchi, M.E.2
  • 17
    • 0027165694 scopus 로고
    • The Trypanosoma crusi ribosomal protein P family: Classification and antigenicity
    • Levin M.J., Vazquez M., Kaplan D., Schijman A.G. The Trypanosoma crusi ribosomal protein P family: classification and antigenicity. Parasitol. Today. 9:1993;381-384.
    • (1993) Parasitol. Today , vol.9 , pp. 381-384
    • Levin, M.J.1    Vazquez, M.2    Kaplan, D.3    Schijman, A.G.4
  • 18
    • 0025988131 scopus 로고
    • The primary structure of rat ribosomal proteins P0, P1 and, P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins
    • Wool I.G., Chan Y.-L., Glück A., Suzuki K. The primary structure of rat ribosomal proteins P0, P1 and, P2 and a proposal for a uniform nomenclature for mammalian and yeast ribosomal proteins. Biochimie. 73:1991;861-870.
    • (1991) Biochimie , vol.73 , pp. 861-870
    • Wool, I.G.1    Chan, Y.-L.2    Glück, A.3    Suzuki, K.4
  • 19
    • 0032579887 scopus 로고    scopus 로고
    • The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae
    • Planta R.J., Mager W.H. The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae. Yeast. 14:1999;471-477.
    • (1999) Yeast , vol.14 , pp. 471-477
    • Planta, R.J.1    Mager, W.H.2
  • 20
    • 0019428163 scopus 로고
    • Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosome
    • Sanchez-Madrid F., Juan-Vidales F., Ballesta J.P.G. Effect of phosphorylation on the affinity of acidic proteins from Saccharomyces cerevisiae for the ribosome. Eur. J. Biochem. 114:1981;609-613.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 609-613
    • Sanchez-Madrid, F.1    Juan-Vidales, F.2    Ballesta, J.P.G.3
  • 21
    • 0017256641 scopus 로고
    • The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins
    • Zinker S., Warner J.R.J. The ribosomal proteins of Saccharomyces cerevisiae. Phosphorylated and exchangeable proteins. J. Biol. Chem. 251:1976;1799-1807.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1799-1807
    • Zinker, S.1    Warner, J.R.J.2
  • 22
    • 0002623943 scopus 로고
    • Control of ribosome biosynthesis in plant cell cultures under the shock conditions. II. Ribosomal proteins
    • Scharf K.-D., Nover L. Control of ribosome biosynthesis in plant cell cultures under the shock conditions. II. Ribosomal proteins. Biochim. Biophys. Acta. 909:1987;44-57.
    • (1987) Biochim. Biophys. Acta , vol.909 , pp. 44-57
    • Scharf, K.-D.1    Nover, L.2
  • 23
    • 0022369647 scopus 로고
    • Evidence for exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver
    • Tsurugi K., Ogata K. Evidence for exchangeability of acidic ribosomal proteins on cytoplasmic ribosomes in regenerating rat liver. J. Biochem. 98:1985;1427-1431.
    • (1985) J. Biochem. , vol.98 , pp. 1427-1431
    • Tsurugi, K.1    Ogata, K.2
  • 24
    • 0018507922 scopus 로고
    • Acidic ribosomal proteins from eucaryotic cells. Effect on ribosomal function
    • Sanchez-Madrid F., Reyes R., Conde P., Ballesta J.P.G. Acidic ribosomal proteins from eucaryotic cells. Effect on ribosomal function. Eur. J. Biochem. 98:1979;409-416.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 409-416
    • Sanchez-Madrid, F.1    Reyes, R.2    Conde, P.3    Ballesta, J.P.G.4
  • 25
    • 0030711636 scopus 로고    scopus 로고
    • Phosphorylation of the acidic ribosomal P proteins in Saccharomyces cerevisiae: A reappraisal
    • Zambrano R., Briones E., Remacha M., Ballesta J.P.G. Phosphorylation of the acidic ribosomal P proteins in Saccharomyces cerevisiae: a reappraisal. Biochemistry. 36:1997;14436-14439.
    • (1997) Biochemistry , vol.36 , pp. 14436-14439
    • Zambrano, R.1    Briones, E.2    Remacha, M.3    Ballesta, J.P.G.4
  • 26
    • 0032564302 scopus 로고    scopus 로고
    • Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation
    • Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G. Phosphorylation of ribosomal protein P0 is not essential for ribosome function but can affect translation. Biochemistry. 37:1998;16620-16626.
    • (1998) Biochemistry , vol.37 , pp. 16620-16626
    • Rodriguez-Gabriel, M.A.1    Remacha, M.2    Ballesta, J.P.G.3
  • 28
    • 0035980142 scopus 로고    scopus 로고
    • Asymmetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk
    • Guarinos E., Remacha M., Ballesta J.P.G. Asymmetric interactions between the acidic P1 and P2 proteins in the Saccharomyces cerevisiae ribosomal stalk. J. Biol. Chem. 276:2001;32474-32479.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32474-32479
    • Guarinos, E.1    Remacha, M.2    Ballesta, J.P.G.3
  • 29
    • 0028981381 scopus 로고
    • Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae
    • Remacha M., Jimenez-Diaz A., Bermejo B., Rodriguez-Gabriel M.A., Guarinos E., Ballesta J.P.G. Ribosomal acidic phosphoproteins P1 and P2 are not required for cell viability but regulate the pattern of protein expression in Saccharomyces cerevisiae. Mol. Cell. Biol. 15:1995;4754-4762.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4754-4762
    • Remacha, M.1    Jimenez-Diaz, A.2    Bermejo, B.3    Rodriguez-Gabriel, M.A.4    Guarinos, E.5    Ballesta, J.P.G.6
  • 30
    • 0035815668 scopus 로고    scopus 로고
    • Regulated heterogeneity in 12-kDa P-protein phosphorylation and composition of ribosomes in maize (Zea mays L.)
    • Szick-Miranda K., Bailey-Serres J. Regulated heterogeneity in 12-kDa P-protein phosphorylation and composition of ribosomes in maize (Zea mays L.). J. Biol. Chem. 276:2001;10921-10928.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10921-10928
    • Szick-Miranda, K.1    Bailey-Serres, J.2
  • 31
    • 0026560274 scopus 로고
    • Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins
    • Pilecki M., Grankowski N., Jacobs J., Ga̧sior E. Specific protein kinase from Saccharomyces cerevisiae cells phosphorylating 60S ribosomal proteins. Eur. J. Biochem. 206:1992;259-268.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 259-268
    • Pilecki, M.1    Grankowski, N.2    Jacobs, J.3    Ga̧sior, E.4
  • 32
    • 0029925323 scopus 로고
    • RAP kinase, a new enzyme phosphorylating the acidic P proteins from Saccharomyces cerevisiae
    • Szyszka R., Bou G., Ballesta J.P.G. RAP kinase, a new enzyme phosphorylating the acidic P proteins from Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1293:1995;213-221.
    • (1995) Biochim. Biophys. Acta , vol.1293 , pp. 213-221
    • Szyszka, R.1    Bou, G.2    Ballesta, J.P.G.3
  • 33
    • 0033257435 scopus 로고    scopus 로고
    • Structure and function of the stalk, a putative regulatory element of the yeast ribosome. Role of stalk protein phosphorylation
    • Rodriguez-Gabriel M.A., Bou G., Briones E., Zambrano R., Remacha M., Ballesta J.P.G. Structure and function of the stalk, a putative regulatory element of the yeast ribosome. Role of stalk protein phosphorylation. Folia Microbiol. 44:1999;153-163.
    • (1999) Folia Microbiol. , vol.44 , pp. 153-163
    • Rodriguez-Gabriel, M.A.1    Bou, G.2    Briones, E.3    Zambrano, R.4    Remacha, M.5    Ballesta, J.P.G.6
  • 35
    • 0017877308 scopus 로고
    • Isolation and properties of two protein kinases from yeast which phosphorylate casein and some ribosomal proteins
    • Kudlicki W., Grankowski N., Ga̧sior E. Isolation and properties of two protein kinases from yeast which phosphorylate casein and some ribosomal proteins. Eur. J. Biochem. 84:1978;493-498.
    • (1978) Eur. J. Biochem. , vol.84 , pp. 493-498
    • Kudlicki, W.1    Grankowski, N.2    Ga̧sior, E.3
  • 36
    • 0031600914 scopus 로고    scopus 로고
    • On the physiological role of casein kinase II in Saccharomyces cerevisiae
    • Glover C.V.C. On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog. Nucl. Acids Res. Mol. Biol. 59:1998;95-133.
    • (1998) Prog. Nucl. Acids Res. Mol. Biol. , vol.59 , pp. 95-133
    • Glover, C.V.C.1
  • 37
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield D.W. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 369:2003;1-15.
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 38
    • 0033257346 scopus 로고    scopus 로고
    • Protein kinases phosphorylating acidic ribosomal proteins from yeast cells
    • Szyszka R. Protein kinases phosphorylating acidic ribosomal proteins from yeast cells. Folia Microbiol. 44:1999;142-152.
    • (1999) Folia Microbiol. , vol.44 , pp. 142-152
    • Szyszka, R.1
  • 39
    • 0031299580 scopus 로고    scopus 로고
    • The phosphorylation sites of ribosomal P proteins from Saccharomyces cerevisiae cells by endogenous CK-2, PK60S and RAP protein kinases
    • Boguszewska A., Szyszka R., Grankowski N. The phosphorylation sites of ribosomal P proteins from Saccharomyces cerevisiae cells by endogenous CK-2, PK60S and RAP protein kinases. Acta Biochim. Polon. 44:1997;191-200.
    • (1997) Acta Biochim. Polon. , vol.44 , pp. 191-200
    • Boguszewska, A.1    Szyszka, R.2    Grankowski, N.3
  • 40
    • 0019326428 scopus 로고
    • Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit
    • Kudlicki W., Szyszka R., Paleń E., Ga̧sior E. Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit. Biochim. Biophys. Acta. 633:1980;376-385.
    • (1980) Biochim. Biophys. Acta , vol.633 , pp. 376-385
    • Kudlicki, W.1    Szyszka, R.2    Paleń, E.3    Ga̧sior, E.4
  • 41
    • 0028836318 scopus 로고
    • Purification and partial characterization of an acidic ribosomal protein kinase from maize
    • Sepuvelda E., Aguilar R., Sanchez de Jimenez E. Purification and partial characterization of an acidic ribosomal protein kinase from maize. Phisiol. Plant. 94:1995;715-721.
    • (1995) Phisiol. Plant , vol.94 , pp. 715-721
    • Sepuvelda, E.1    Aguilar, R.2    Sanchez de Jimenez, E.3
  • 42
    • 0035476623 scopus 로고    scopus 로고
    • Crystal structure of human protein kinase CK2: Insights into basic properties of the CK2 holoenzyme
    • Niefind K., Guerra B., Ermakowa I., Issinger O.-G. Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme. EMBO J. 20. 2001;5320-5331.
    • (2001) EMBO J. , vol.20 , pp. 5320-5331
    • Niefind, K.1    Guerra, B.2    Ermakowa, I.3    Issinger, O.-G.4
  • 43
    • 0026039891 scopus 로고
    • Casein kinase I and II - Multipotential serine protein kinases: Structure, function, and regulation
    • Tuazon P.T., Traugh J.A. Casein kinase I and II - multipotential serine protein kinases: structure, function, and regulation. Adv. Second Messenger Phosphoprotein Res. 23:1991;123-164.
    • (1991) Adv. Second Messenger Phosphoprotein Res. , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 44
    • 0028591832 scopus 로고
    • Development of inhibitors of protein kinases CKI and CKII and some related aspects, including donor and acceptor specificities and viral protein kinases
    • Shugar D. Development of inhibitors of protein kinases CKI and CKII and some related aspects, including donor and acceptor specificities and viral protein kinases. Cell. Mol. Biol. Res. 40:1994;411-419.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 411-419
    • Shugar, D.1
  • 45
    • 0038080330 scopus 로고    scopus 로고
    • Differential phosphorylation of ribosomal acidic proteins from yeast cells by two endogenous protein kinases: Casein kinase-2 and PK60S
    • Szyszka R., Boguszewska A., Shugar D., Grankowski N. Differential phosphorylation of ribosomal acidic proteins from yeast cells by two endogenous protein kinases: casein kinase-2 and PK60S. Acta Biochim. Polon. 43:1996;348-355.
    • (1996) Acta Biochim. Polon. , vol.43 , pp. 348-355
    • Szyszka, R.1    Boguszewska, A.2    Shugar, D.3    Grankowski, N.4
  • 46
    • 0030861055 scopus 로고    scopus 로고
    • Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation
    • Leroy D., Hrishe J.K., Filhol O., Chambaz E.M., Cochet C. Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation. J. Biol. Chem. 272:1997;20820-20827.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20820-20827
    • Leroy, D.1    Hrishe, J.K.2    Filhol, O.3    Chambaz, E.M.4    Cochet, C.5
  • 47
    • 0037107552 scopus 로고    scopus 로고
    • Protein kinase CK2: A challenge to canons
    • Pinna L.A. Protein kinase CK2: a challenge to canons. J. Cell Sci. 115:2002;3873-3878.
    • (2002) J. Cell Sci. , vol.115 , pp. 3873-3878
    • Pinna, L.A.1
  • 49
    • 0022433536 scopus 로고
    • A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate
    • Szyszka R., Kudlicki W., Grankowski N., Ga̧sior E. A minor species of a type I casein kinase from yeast phosphorylating threonine residues of protein substrate. Biochim. Biophys. Acta. 838:1985;171-174.
    • (1985) Biochim. Biophys. Acta , vol.838 , pp. 171-174
    • Szyszka, R.1    Kudlicki, W.2    Grankowski, N.3    Ga̧sior, E.4
  • 51
    • 0018174535 scopus 로고
    • Isolation of phosphorylated peptides and proteins on ion exchange papers
    • Glass D.B., Masaracchia R.A., Feramisco J.R., Kemp B.E. Isolation of phosphorylated peptides and proteins on ion exchange papers. Anal. Biochem. 87:1978;566-575.
    • (1978) Anal. Biochem. , vol.87 , pp. 566-575
    • Glass, D.B.1    Masaracchia, R.A.2    Feramisco, J.R.3    Kemp, B.E.4
  • 53
    • 0027073111 scopus 로고
    • Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: Signal transduction/transformation-dependent MBP kinases
    • Wang H.C., Erikson R.L. Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases. Mol. Biol. Cell. 3:1992;1329-1337.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1329-1337
    • Wang, H.C.1    Erikson, R.L.2
  • 54
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • Kameshita I., Fujisawa H. A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem. 183:1989;139-143.
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2
  • 56
    • 0033643558 scopus 로고    scopus 로고
    • Sample preparation by SDS-Page and in-gel digestions
    • P. Jollés, Jörnvall H. Basel: Birkhauser Verlag AG
    • Hellman U. Sample preparation by SDS-Page and in-gel digestions. Jollés P., Jörnvall H. Proteomics in Functional Genomics. Protein Structure Analysis. 88:2000;43-54 Birkhauser Verlag AG, Basel.
    • (2000) Proteomics in Functional Genomics. Protein Structure Analysis , vol.88 , pp. 43-54
    • Hellman, U.1
  • 57
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantifies of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantifies of protein utilising the principle of protein-dye binding. Anal. Biochem. 72:1970;248-254.
    • (1970) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 58
    • 0032415287 scopus 로고    scopus 로고
    • Promiscuous subunit interactions: A possible mechanism for the regulation of protein kinase CK2
    • Allende C.C., Allende J.E. Promiscuous subunit interactions: a possible mechanism for the regulation of protein kinase CK2. J. Cell. Biochem. Suppl. 30-31:1998;129-136.
    • (1998) J. Cell. Biochem. Suppl. , vol.30-31 , pp. 129-136
    • Allende, C.C.1    Allende, J.E.2
  • 59
    • 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. 1054:1990;267-284.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 60
    • 0023645087 scopus 로고
    • Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides
    • Kuenzel E.A., Mulligan J.A., Sommecorn J., Krebs E.G. Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides. J. Biol. Chem. 262:1987;9136-9140.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9136-9140
    • Kuenzel, E.A.1    Mulligan, J.A.2    Sommecorn, J.3    Krebs, E.G.4
  • 61
    • 0023727050 scopus 로고
    • Synthetic peptide substrates for casein kinase 2. Assessment of minimum structural requirements for phosphorylation
    • Marchiori F., Meggio F., Marin O., Borin G., Pinna L.A. Synthetic peptide substrates for casein kinase 2. Assessment of minimum structural requirements for phosphorylation. Biochim. Biophys. Acta. 971:1988;332-338.
    • (1988) Biochim. Biophys. Acta , vol.971 , pp. 332-338
    • Marchiori, F.1    Meggio, F.2    Marin, O.3    Borin, G.4    Pinna, L.A.5
  • 63
    • 0028292988 scopus 로고
    • Casein kinase 2 down-regulation and activation by polybasic peptides are mediated by acidic residues in the 55-64 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 55-64 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
  • 64
    • 0034681360 scopus 로고    scopus 로고
    • The regulatory β subunit of protein kinase CK2 mediates formation of tetrameric CK2 complexes
    • Graham K.C., Litchfield D.W. The regulatory β subunit of protein kinase CK2 mediates formation of tetrameric CK2 complexes. J. Biol. Chem. 275:2000;5003-5010.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5003-5010
    • Graham, K.C.1    Litchfield, D.W.2
  • 65
    • 0021099186 scopus 로고
    • Oligomeric structure and catalytic activity of G type casein kinase. Isolation of the two subunits and renaturation experiments
    • Cochet C., Chambaz E.M. Oligomeric structure and catalytic activity of G type casein kinase. Isolation of the two subunits and renaturation experiments. J. Biol. Chem. 258:1983;1403-1406.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1403-1406
    • Cochet, C.1    Chambaz, E.M.2
  • 66
    • 0035677676 scopus 로고    scopus 로고
    • Visualization and molecular analysis of nuclear import of protein kinase CK2 subunits in living cells
    • Martel V., Filhol O., Nueda A., Gerber D., Benitez M.J., Cochet C. Visualization and molecular analysis of nuclear import of protein kinase CK2 subunits in living cells. Mol. Cell. Biochem. 227:1998;81-90.
    • (1998) Mol. Cell. Biochem. , vol.227 , pp. 81-90
    • Martel, V.1    Filhol, O.2    Nueda, A.3    Gerber, D.4    Benitez, M.J.5    Cochet, C.6
  • 67
    • 0030861055 scopus 로고    scopus 로고
    • Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation
    • Leroy D., Heriche J.K., Filhol O., Chambaz E.M., Cochet C. Binding of polyamines to an autonomous domain of the regulatory subunit of protein kinase CK2 induces a conformational change in the holoenzyme. A proposed role for the kinase stimulation. J. Biol. Chem. 272:1997;20820-20827.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20820-20827
    • Leroy, D.1    Heriche, J.K.2    Filhol, O.3    Chambaz, E.M.4    Cochet, C.5
  • 68
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • Slekar K.H., Kosman D.J., Culotta V.C. The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J. Biol. Chem. 271:1996;28831-28836.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28831-28836
    • Slekar, K.H.1    Kosman, D.J.2    Culotta, V.C.3
  • 69
    • 0024043518 scopus 로고
    • The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: Cloning, sequencing, and biological activity
    • Bermingham-McDonogh O., Gralla E.B., Valentine J.S. The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity. Proc. Natl. Acad. Sci USA. 85:1988;4789-4793.
    • (1988) Proc. Natl. Acad. Sci USA , vol.85 , pp. 4789-4793
    • Bermingham-McDonogh, O.1    Gralla, E.B.2    Valentine, J.S.3
  • 70
    • 0032483373 scopus 로고    scopus 로고
    • The cytoplasmic Cu,Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress. Generation of free radicals during freezing and thawing
    • Park J.I., Grant C.M., Davies M.J., Dawes I.W. The cytoplasmic Cu,Zn superoxide dismutase of Saccharomyces cerevisiae is required for resistance to freeze-thaw stress. Generation of free radicals during freezing and thawing. J. Biol. Chem. 273:1998;22921-22928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22921-22928
    • Park, J.I.1    Grant, C.M.2    Davies, M.J.3    Dawes, I.W.4
  • 72
    • 0034697370 scopus 로고    scopus 로고
    • Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism
    • DeFreitas J.M., Liba A., Meneghini R., Valentine J.S., Gralla E.B. Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism. J. Biol. Chem. 275:2000;11645-11649.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11645-11649
    • DeFreitas, J.M.1    Liba, A.2    Meneghini, R.3    Valentine, J.S.4    Gralla, E.B.5
  • 73
    • 0025145585 scopus 로고
    • Protein kinases. Regulation by autoinhibitory domains
    • Soderling T.R. Protein kinases. Regulation by autoinhibitory domains. J. Biol. Chem. 265:1990;1823-1826.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1823-1826
    • Soderling, T.R.1
  • 74
    • 0034668176 scopus 로고    scopus 로고
    • Type 2A protein phosphatase, the complex regulator of numerous signaling pathways
    • Zołnierowicz S. Type 2A protein phosphatase, the complex regulator of numerous signaling pathways. Biochem. Pharmacol. 60:2000;1225-1235.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 1225-1235
    • Zołnierowicz, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.