메뉴 건너뛰기




Volumn 267, Issue 10, 2000, Pages 3065-3072

Ser/Thr phosphorylation of hematopoietic specific protein 1 (HS1). Implication of protein kinase CK2

Author keywords

Casein kinase 2; CK2; HS1; Phosphorylation; Tyrosine kinase

Indexed keywords

PROTEIN SERINE THREONINE KINASE;

EID: 0034038868     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2000.01333.x     Document Type: Article
Times cited : (18)

References (52)
  • 1
    • 0024374371 scopus 로고
    • Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage
    • 1. Kitamura, D., Kaneko, H., Miyagoe, Y., Ariyasu, T. & Watanabe, T. (1989) Isolation and characterization of a novel human gene expressed specifically in the cells of hematopoietic lineage. Nucleic Acid Res. 17, 9367-9379.
    • (1989) Nucleic Acid Res. , vol.17 , pp. 9367-9379
    • Kitamura, D.1    Kaneko, H.2    Miyagoe, Y.3    Ariyasu, T.4    Watanabe, T.5
  • 2
    • 0033548655 scopus 로고    scopus 로고
    • Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein tyrosine kinase
    • 2. Brunati, A.M., Donella-Deana, A., James, P., Quadroni, M., Contri, A., Marin, O. & Pinna, L.A. (1999) Molecular features underlying the sequential phosphorylation of HS1 protein and its association with c-Fgr protein tyrosine kinase. J. Biol. Chem. 274, 7557-7564.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7557-7564
    • Brunati, A.M.1    Donella-Deana, A.2    James, P.3    Quadroni, M.4    Contri, A.5    Marin, O.6    Pinna, L.A.7
  • 3
    • 0031569110 scopus 로고    scopus 로고
    • HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases
    • 3. Suzuki, Y., Demoliere, C., Kitamura, D., Takeshida, H., Deuschle, U. & Watanabe, T. (1997) HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family tyrosine kinases. J. Immunol. 158, 2736-2744.
    • (1997) J. Immunol. , vol.158 , pp. 2736-2744
    • Suzuki, Y.1    Demoliere, C.2    Kitamura, D.3    Takeshida, H.4    Deuschle, U.5    Watanabe, T.6
  • 5
    • 0027963242 scopus 로고
    • Tyrosine phosphorylation of MB-1, B-29, and HS1 proteins in human B cells following receptor crosslinking
    • 5. Hata, D., Nakamura, T., Kawakami, T., Kawakami, Y., Herren, B. & Mayumi, M. (1993) Tyrosine phosphorylation of MB-1, B-29, and HS1 proteins in human B cells following receptor crosslinking. Immunol. Lett. 40, 65-71.
    • (1993) Immunol. Lett. , vol.40 , pp. 65-71
    • Hata, D.1    Nakamura, T.2    Kawakami, T.3    Kawakami, Y.4    Herren, B.5    Mayumi, M.6
  • 6
    • 0028919667 scopus 로고
    • Hierarchical phosphorylation of a 50-kDa protein by protein tyrosine kinases TPK-IIB and c-Fgr, and its identification as HS1 hematopoietic-lineage cell-specific protein
    • 6. Brunati, A.M., Ruzzene, M., James, P., Guerra, B. & Pinna, L.A. (1995) Hierarchical phosphorylation of a 50-kDa protein by protein tyrosine kinases TPK-IIB and c-Fgr, and its identification as HS1 hematopoietic-lineage cell-specific protein. Eur. J. Biochem. 229, 164-170.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 164-170
    • Brunati, A.M.1    Ruzzene, M.2    James, P.3    Guerra, B.4    Pinna, L.A.5
  • 9
    • 0029151248 scopus 로고
    • Antigen-receptor induced clonal expansion and deletion of lymphocytes are impaired in mice lacking HS1 protein, a substrate of the antigen-receptor-coupled tyrosine kinases
    • 9. Taniuki, I., Kitamura, K., Maekawa, Y, Fukuda, T., Kishi, H. & Watanabe, T. (1995) Antigen-receptor induced clonal expansion and deletion of lymphocytes are impaired in mice lacking HS1 protein, a substrate of the antigen-receptor-coupled tyrosine kinases. EMBO J. 14, 3664-3678.
    • (1995) EMBO J. , vol.14 , pp. 3664-3678
    • Taniuki, I.1    Kitamura, K.2    Maekawa, Y.3    Fukuda, T.4    Kishi, H.5    Watanabe, T.6
  • 10
    • 0027934308 scopus 로고
    • Signaling properties of anti-immunoglobulin-resistant variants of WEHI-231 B lymphoma cells
    • 10. Benhamou, L.E., Watanabe, T., Kitamura, D., Cazenave, P.A. & Sarthou, P. (1994) Signaling properties of anti-immunoglobulin-resistant variants of WEHI-231 B lymphoma cells. Eur. J. Immunol. 24, 1993-1999.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1993-1999
    • Benhamou, L.E.1    Watanabe, T.2    Kitamura, D.3    Cazenave, P.A.4    Sarthou, P.5
  • 11
    • 0029086739 scopus 로고
    • Restoration of surface IgM-mediated apoptosis in an anti-IgM-resistant variant of WEHI-231 lymphoma cells by HS1, a protein-tyrosine kinase substrate
    • 11. Fukuda, T., Kitamura, D., Taniuchi, I., Maekawa, Y, Benhamou, L.E., Sarthou, P. & Watanabe, T. (1995) Restoration of surface IgM-mediated apoptosis in an anti-IgM-resistant variant of WEHI-231 lymphoma cells by HS1, a protein-tyrosine kinase substrate. Proc. Natl Acad. Sci. USA 92, 7302-7306.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7302-7306
    • Fukuda, T.1    Kitamura, D.2    Taniuchi, I.3    Maekawa, Y.4    Benhamou, L.E.5    Sarthou, P.6    Watanabe, T.7
  • 12
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidyl inositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation
    • 12. He, H., Watanabe, T., Zhan, X., Huang, C., Schuuring, E., Fukami, K., Takenawa, T., Kumar, C.C., Simpson, R.J. & Maruta, H. (1998) Role of phosphatidyl inositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation. Mol. Cell. Biol. 18, 3829-3837.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 13
    • 0032516522 scopus 로고    scopus 로고
    • Protein kinase CK2 ('is induced by serum as a delayed early gene and cooperates with Hs-ras in fibroblast transformation
    • 13. Orlandini, M., Semplici, F., Ferruzzi, R., Meggio, F., Pinna, L.A. & Oliviero, S. (1998) Protein kinase CK2 ('is induced by serum as a delayed early gene and cooperates with Hs-ras in fibroblast transformation. J. Biol. Chem. 273, 21292-21297.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21292-21297
    • Orlandini, M.1    Semplici, F.2    Ferruzzi, R.3    Meggio, F.4    Pinna, L.A.5    Oliviero, S.6
  • 14
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation?
    • 14. Pinna, L.A. (1990) Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim. Biophys. Acta 1054, 267-284.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 15
    • 0026039891 scopus 로고
    • Casein kinase I and II -multipotential serine protein kinases: Structure, function, and regulation
    • 15. Tuazon, P.T. & Traugh, J.A. (1991) Casein kinase I and II -multipotential serine protein kinases: structure, function, and regulation. Adv. Second Messenger Phosphoprotein Res. 23, 123-164.
    • (1991) Adv. Second Messenger Phosphoprotein Res. , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 16
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK ('casein kinase-2') and its implication in cell division and proliferation
    • 16. Pinna, L.A. & Meggio, F. (1997) Protein kinase CK ('casein kinase-2') and its implication in cell division and proliferation. Progr. Cell Cycle. Res. 3, 77-97.
    • (1997) Progr. Cell Cycle. Res. , vol.3 , pp. 77-97
    • Pinna, L.A.1    Meggio, F.2
  • 17
    • 0032415287 scopus 로고    scopus 로고
    • Promiscuous subunit interactions: A possible mechanism for the regulation of protein kinase CK2
    • 17. Allende, C.C. & Allende, J.E. (1998) Promiscuous subunit interactions: a possible mechanism for the regulation of protein kinase CK2. J. Cell. Biochem. (Suppl.) 30-31, 129-136.
    • (1998) J. Cell. Biochem. (Suppl.) , vol.30-31 , pp. 129-136
    • Allende, C.C.1    Allende, J.E.2
  • 18
    • 0033018831 scopus 로고    scopus 로고
    • Protein kinase CK2 and its role in cellular proliferation, development and pathology
    • 18. Guerra, B. & Issinger, O.-G. (1999) Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis 20, 391-408.
    • (1999) Electrophoresis , vol.20 , pp. 391-408
    • Guerra, B.1    Issinger, O.-G.2
  • 19
    • 0032755392 scopus 로고    scopus 로고
    • Hematopoietic lineage cell specific protein I associates with and down-regulates protein kinase CK2
    • 19. Ruzzene, M., Brunati, A.M., Sarno, S., Donella-Deana, A. & Pinna, L.A. (1999) Hematopoietic lineage cell specific protein I associates with and down-regulates protein kinase CK2. FEBS Lett. 461, 32-36.
    • (1999) FEBS Lett. , vol.461 , pp. 32-36
    • Ruzzene, M.1    Brunati, A.M.2    Sarno, S.3    Donella-Deana, A.4    Pinna, L.A.5
  • 20
    • 0029027428 scopus 로고
    • Phosphorylation and activation of protein kinase CK2 by p34cdc2 are independent events
    • 20. Meggio, F., Boldyreff, B., Marin, O., Issinger, O.-G. & Pinna, L.A. (1995) Phosphorylation and activation of protein kinase CK2 by p34cdc2 are independent events. Eur. J. Biochem. 230, 1025-1031.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1025-1031
    • Meggio, F.1    Boldyreff, B.2    Marin, O.3    Issinger, O.-G.4    Pinna, L.A.5
  • 21
    • 0019877822 scopus 로고
    • Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases
    • 21. Meggio, F., Donella-Deana, A. & Pinna, L.A. (1981) Endogenous phosphate acceptor proteins for rat liver cytosolic casein kinases. J. Biol. Chem. 256, 11958-11961.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11958-11961
    • Meggio, F.1    Donella-Deana, A.2    Pinna, L.A.3
  • 23
    • 0031019426 scopus 로고    scopus 로고
    • Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland
    • 23. Lasa, M., Marin, O. & Pinna, L.A. (1997) Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur. J. Biochem. 243, 719-725.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 719-725
    • Lasa, M.1    Marin, O.2    Pinna, L.A.3
  • 24
    • 0025848105 scopus 로고
    • The antioxidant butylated hydroxytoluene stimulates platelet protein kinase C and inhibits subsequent protein phosphorylation induced by thrombin
    • 24. Ruzzene, M., Donella-Deana, A., Alexandre, A., Francesconi, M. & Deana, R. (1991) The antioxidant butylated hydroxytoluene stimulates platelet protein kinase C and inhibits subsequent protein phosphorylation induced by thrombin. Biochim. Biophys. Acta 1094, 121-129.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 121-129
    • Ruzzene, M.1    Donella-Deana, A.2    Alexandre, A.3    Francesconi, M.4    Deana, R.5
  • 25
    • 0025796976 scopus 로고
    • Isolation and characterization of recombinant human casein kinase II subunits α and β from bacteria
    • 25. Grankowski, N., Boldyreff, B. & Issinger, O.-G. (1991) Isolation and characterization of recombinant human casein kinase II subunits α and β from bacteria. Eur. J. Biochem. 198, 25-30.
    • (1991) Eur. J. Biochem. , vol.198 , pp. 25-30
    • Grankowski, N.1    Boldyreff, B.2    Issinger, O.-G.3
  • 26
    • 17544377840 scopus 로고    scopus 로고
    • Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis
    • 26. Sarno, S., Vaglio, P., Meggio, F., Issinger, O.-G. & Pinna, L.A. (1996) Protein kinase CK2 mutants defective in substrate recognition. Purification and kinetic analysis. J. Biol. Chem. 271, 10595-10601.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10595-10601
    • Sarno, S.1    Vaglio, P.2    Meggio, F.3    Issinger, O.-G.4    Pinna, L.A.5
  • 27
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • 27. Boyle, W.J., Van der Geer, P. & Hunter, T. (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201, 111-149.
    • (1991) Methods Enzymol. , vol.201 , pp. 111-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 28
    • 0026780629 scopus 로고
    • Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1
    • 28. Perich, J.W., Meggio, F., Reynolds, E.C., Marin, O. & Pinna, L.A. (1992) Role of phosphorylated aminoacyl residues in generating atypical consensus sequences which are recognized by casein kinase-2 but not by casein kinase-1. Biochemistry 31, 5893-5897.
    • (1992) Biochemistry , vol.31 , pp. 5893-5897
    • Perich, J.W.1    Meggio, F.2    Reynolds, E.C.3    Marin, O.4    Pinna, L.A.5
  • 29
    • 0031023758 scopus 로고    scopus 로고
    • Upregulation of cortactin expression during the maturation of megakaryocytes
    • 29. Zhan, X., Haudenschild, C.C., Ni, Y., Smith, E. & Huang, C. (1997) Upregulation of cortactin expression during the maturation of megakaryocytes. Blood 89, 457-464.
    • (1997) Blood , vol.89 , pp. 457-464
    • Zhan, X.1    Haudenschild, C.C.2    Ni, Y.3    Smith, E.4    Huang, C.5
  • 30
    • 0025193521 scopus 로고
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J. Biol. Chem. 265, 2896-2902.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2896-2902
    • Heffetz, D.1    Bushkin, L.2    Dror, R.3    Zyck, Y.4
  • 31
    • 0025181418 scopus 로고
    • Okadaic acid: A new probe for the study of cellular regulation
    • 31. Cohen, P., Holmes, C.F.B. & Tsukitani, Y. (1990) Okadaic acid: a new probe for the study of cellular regulation. Trends Biochem. Sci. 15, 98-102.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.F.B.2    Tsukitani, Y.3
  • 32
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: Potent but non specific inhibitors of protein kinases
    • 32. Ruegg, U.T. & Burgess, G.M. (1989) Staurosporine, K-252 and UCN-01: potent but non specific inhibitors of protein kinases. Trends Pharmacol. Sci. 10, 218-220.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 218-220
    • Ruegg, U.T.1    Burgess, G.M.2
  • 34
    • 0025060131 scopus 로고
    • Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase 2 and casein kinase-1
    • 34. Meggio, F., Shugar, D. & Pinna, L.A. (1990) Ribofuranosyl-benzimidazole derivatives as inhibitors of casein kinase 2 and casein kinase-1. Eur. J. Biochem. 187, 89-94.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 89-94
    • Meggio, F.1    Shugar, D.2    Pinna, L.A.3
  • 35
    • 0028939610 scopus 로고
    • Halogenated benzimidazoles and benzotriazoles as selective inhibitors of protein kinase CK I and CK II from Saccharomyces cerevisiae and other sources
    • 35. Szyszka, R., Grankowski, N., Felczak, K. & Shugar, D. (1995) Halogenated benzimidazoles and benzotriazoles as selective inhibitors of protein kinase CK I and CK II from Saccharomyces cerevisiae and other sources. Biochem. Biophys. Res. Commun. 208, 418-424.
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 418-424
    • Szyszka, R.1    Grankowski, N.2    Felczak, K.3    Shugar, D.4
  • 37
    • 0028228224 scopus 로고
    • Identifying and characterizing casein kinase ii in human platelets
    • 37. Hoyt, C.H., Oh, C.J., Beekman, J.B., Litchfield, D.W. & Lerea, K.M. (1994) Identifying and characterizing casein kinase II in human platelets. Blood 83, 3517-3523.
    • (1994) Blood , vol.83 , pp. 3517-3523
    • Hoyt, C.H.1    Oh, C.J.2    Beekman, J.B.3    Litchfield, D.W.4    Lerea, K.M.5
  • 38
    • 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
    • 38. Meggio, F., Boldyreff, B., Issinger, O.-G. & Pinna, L.A. (1994) 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, 4336-4342.
    • (1994) Biochemistry , vol.33 , pp. 4336-4342
    • Meggio, F.1    Boldyreff, B.2    Issinger, O.-G.3    Pinna, L.A.4
  • 39
    • 0028600673 scopus 로고
    • Substrate specificity of protein kinase CK2
    • 39. Meggio, F., Marin, O. & Pinna, L.A. (1994) Substrate specificity of protein kinase CK2. Cell. Mol. Biol. Res. 40, 401-409.
    • (1994) Cell. Mol. Biol. Res. , vol.40 , pp. 401-409
    • Meggio, F.1    Marin, O.2    Pinna, L.A.3
  • 40
    • 0032079650 scopus 로고    scopus 로고
    • Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at a 2.1 Å resolution
    • 40. Niefind, K., Guerra, B., Pinna, L.A., Issinger, O.-G. & Schomburg, D. (1998) Crystal structure of the catalytic subunit of protein kinase CK2 from Zea mays at a 2.1 Å resolution. EMBO J. 17, 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
  • 41
    • 0032423888 scopus 로고    scopus 로고
    • Biochemical evidence that the N-terminal segment of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2
    • 41. Sarno, S., Marin, O., Ghisellini, P., Meggio, F. & Pinna, L.A. (1998) Biochemical evidence that the N-terminal segment of the α subunit and the β subunit play interchangeable roles in the activation of protein kinase CK2. FEBS Lett. 441, 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
  • 42
    • 0033002277 scopus 로고    scopus 로고
    • Searching interaction partners of protein kinase CK2β subunit by two-hybrid screening
    • 42. Grein, S., Raymond, K., Cochet, C., Pyerin, W., Chambaz, E.M. & Filhol, O. (1999) Searching interaction partners of protein kinase CK2β subunit by two-hybrid screening. Mol. Cell. Biochem. 191, 105-109.
    • (1999) Mol. Cell. Biochem. , vol.191 , pp. 105-109
    • Grein, S.1    Raymond, K.2    Cochet, C.3    Pyerin, W.4    Chambaz, E.M.5    Filhol, O.6
  • 43
    • 0030613551 scopus 로고    scopus 로고
    • The IkB kinase complex (IKK) contains two kinase subunits, IKKa and IKKb, necessary for IkB phosphorylation and NF-kB activation
    • 43. Zandi, E., Rothwarf, D.M., Delhase, M., Hayakawa, M. & Karin, M. (1997) The IkB kinase complex (IKK) contains two kinase subunits, IKKa and IKKb, necessary for IkB phosphorylation and NF-kB activation. Cell 91, 243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 44
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IΚB kinase that activates the transcription factor NF-ΚB
    • 44. Di Donato, J.A., Hayakawa, M., Rothwarf, D.M., Zandi, E. & Karin, M. (1997) A cytokine-responsive IΚB kinase that activates the transcription factor NF-ΚB. Nature 388, 548-554.
    • (1997) Nature , vol.388 , pp. 548-554
    • Di Donato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 45
    • 0032811045 scopus 로고    scopus 로고
    • Serine 32 and Serine 36 of IΚBα are directly phosphorylated by protein kinase CKII in vitro
    • 45. Taylor, J.A., Bren, G.D., Pennington, K.N., Trushin, S.A., Asin, S. & Paya, C.V. (1999) Serine 32 and Serine 36 of IΚBα are directly phosphorylated by protein kinase CKII in vitro. J. Mol. Biol. 290, 839-850.
    • (1999) J. Mol. Biol. , vol.290 , pp. 839-850
    • Taylor, J.A.1    Bren, G.D.2    Pennington, K.N.3    Trushin, S.A.4    Asin, S.5    Paya, C.V.6
  • 47
    • 0027521063 scopus 로고
    • Evidence for the induction of casein kinase II in bovine lymphocytes transformed by the intracellular protozoan parasite Theileria parva
    • 47. Ole-MoiYoi, O.K., Brown, W.C., Iams, K.P., Nayar, A., Tsukamoto, T. & Macklin, M.D. (1993) Evidence for the induction of casein kinase II in bovine lymphocytes transformed by the intracellular protozoan parasite Theileria parva. EMBO J. 12, 1621-1631.
    • (1993) EMBO J. , vol.12 , pp. 1621-1631
    • Ole-MoiYoi, O.K.1    Brown, W.C.2    Iams, K.P.3    Nayar, A.4    Tsukamoto, T.5    Macklin, M.D.6
  • 48
    • 0028950460 scopus 로고
    • Casein kinase II in theileriosis
    • 48. Ole-MoiYoi, O.K. (1995) Casein kinase II in theileriosis. Science 267, 834-836.
    • (1995) Science , vol.267 , pp. 834-836
    • Ole-MoiYoi, O.K.1
  • 50
    • 0020680934 scopus 로고
    • Cyclic adenosine 3′: 5′-monophosphate dependent and independent protein kinases in human leukemia cells
    • 50. Pena, J.M., Itarte, E., Domingo, A. & Cusso, R. (1983) Cyclic adenosine 3′: 5′-monophosphate dependent and independent protein kinases in human leukemia cells. Cancer Res. 43, 1172-1175.
    • (1983) Cancer Res. , vol.43 , pp. 1172-1175
    • Pena, J.M.1    Itarte, E.2    Domingo, A.3    Cusso, R.4
  • 51
    • 0022982050 scopus 로고
    • Altered protein kinase activity of lymphoid cells transformed by Abelson and Moloney leukemia viruses
    • 51. Brunati, A.M., Saggioro, D., Chieco-Bianchi, L. & Pinna, L.A. (1986) Altered protein kinase activity of lymphoid cells transformed by Abelson and Moloney leukemia viruses. FEBS Lett. 206, 59-63.
    • (1986) FEBS Lett. , vol.206 , pp. 59-63
    • Brunati, A.M.1    Saggioro, D.2    Chieco-Bianchi, L.3    Pinna, L.A.4
  • 52
    • 0013672807 scopus 로고    scopus 로고
    • Protein kinase CK2: Functional properties in cell growth and neoplasia
    • Baig, S.S., ed. IOS Press
    • 52. Chambaz, E.M. (1998) Protein kinase CK2: functional properties in cell growth and neoplasia. In Cancer Research Supplement BIOMED I (Baig, S.S., ed.). pp. 122-132. IOS Press.
    • (1998) Cancer Research Supplement BIOMED I , pp. 122-132
    • Chambaz, E.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.