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Volumn 61, Issue 11, 2012, Pages 1512-1517

CK2 and the regulation of the carbohydrate metabolism

Author keywords

Glucose metabolism; Insulin signalling; Phosphorylation; Protein kinase CK2

Indexed keywords

CARBOHYDRATE; CASEIN KINASE II;

EID: 84867853948     PISSN: 00260495     EISSN: 15328600     Source Type: Journal    
DOI: 10.1016/j.metabol.2012.07.011     Document Type: Review
Times cited : (46)

References (58)
  • 1
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • G. Burnett, and E.P. Kennedy The enzymatic phosphorylation of proteins J Biol Chem 211 1954 969 980
    • (1954) J Biol Chem , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 2
    • 38549135536 scopus 로고    scopus 로고
    • Genomic overview of protein kinases
    • G. Manning Genomic overview of protein kinases WormBook 2005 1 19
    • (2005) WormBook , pp. 1-19
    • Manning, G.1
  • 3
    • 0021166322 scopus 로고
    • Interaction of polyamines and magnesium with casein kinase II
    • G.M. Hathaway, and J.A. Traugh Interaction of polyamines and magnesium with casein kinase II Arch Biochem Biophys 233 1984 133 138
    • (1984) Arch Biochem Biophys , vol.233 , pp. 133-138
    • Hathaway, G.M.1    Traugh, J.A.2
  • 4
    • 0019198966 scopus 로고
    • Inhibition of casein kinase II by heparin
    • G.M. Hathaway, T.H. Lubben, and J.A. Traugh Inhibition of casein kinase II by heparin J Biol Chem 255 1980 8038 8041
    • (1980) J Biol Chem , vol.255 , pp. 8038-8041
    • Hathaway, G.M.1    Lubben, T.H.2    Traugh, J.A.3
  • 5
    • 78649335829 scopus 로고    scopus 로고
    • Cellular regulators of protein kinase CK2
    • M. Montenarh Cellular regulators of protein kinase CK2 Cell Tissue Res 342 2010 139 146
    • (2010) Cell Tissue Res , vol.342 , pp. 139-146
    • Montenarh, M.1
  • 6
    • 0032725769 scopus 로고    scopus 로고
    • Protein kinase CK2: Evidence for a protein kinase CK2β subunit fraction, devoid of the catalytic CK2a subunit, in mouse brain and testicles
    • B. Guerra, S. Siemer, and B. Boldyreff Protein kinase CK2: evidence for a protein kinase CK2β subunit fraction, devoid of the catalytic CK2a subunit, in mouse brain and testicles FEBS Lett 462 1999 353 357
    • (1999) FEBS Lett , vol.462 , pp. 353-357
    • Guerra, B.1    Siemer, S.2    Boldyreff, B.3
  • 7
    • 0028122060 scopus 로고
    • Asymmetric expression of protein kinase CK2 in human kidney tumors
    • G. Stalter, S. Siemer, and E. Becht Asymmetric expression of protein kinase CK2 in human kidney tumors Biochem Biophys Res Commun 202 1994 141 147
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 141-147
    • Stalter, G.1    Siemer, S.2    Becht, E.3
  • 8
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK2 (casein kinase-2) and its implication in cell division and proliferation
    • L.A. Pinna, and F. Meggio Protein kinase CK2 (casein kinase-2) and its implication in cell division and proliferation Prog Cell Cycle Res 3 1997 77 97
    • (1997) Prog Cell Cycle Res , vol.3 , pp. 77-97
    • Pinna, L.A.1    Meggio, F.2
  • 9
    • 37549025849 scopus 로고    scopus 로고
    • The alpha catalytic subunit of protein kinase CK2 is required for mouse embryonic development
    • D.Y. Lou, I. Dominguez, and P. Toselli The alpha catalytic subunit of protein kinase CK2 is required for mouse embryonic development Mol Cell Biol 28 2007 131 139
    • (2007) Mol Cell Biol , vol.28 , pp. 131-139
    • Lou, D.Y.1    Dominguez, I.2    Toselli, P.3
  • 10
    • 0032879917 scopus 로고    scopus 로고
    • Globozoospermia in mice lacking the casein kinase II a' catalytic subunit
    • X. Xu, P.A. Toselli, and L.D. Russell Globozoospermia in mice lacking the casein kinase II a' catalytic subunit Nat Genet 23 1999 118 121
    • (1999) Nat Genet , vol.23 , pp. 118-121
    • Xu, X.1    Toselli, P.A.2    Russell, L.D.3
  • 11
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation
    • L.A. Pinna Casein kinase 2: an 'eminence grise' in cellular regulation Biochim Biophys Acta Mol Cell Res 1054 1990 267 284
    • (1990) Biochim Biophys Acta Mol Cell Res , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 12
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • F. Meggio, and L.A. Pinna One-thousand-and-one substrates of protein kinase CK2? FASEB J 17 2003 349 368
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 13
    • 0027722138 scopus 로고
    • Casein kinase II in signal transduction and cell regulation
    • D.W. Litchfield, and B. Lüscher Casein kinase II in signal transduction and cell regulation Mol Cell Biochem 127/128 1993 187 199
    • (1993) Mol Cell Biochem , vol.127-128 , pp. 187-199
    • Litchfield, D.W.1    Lüscher, B.2
  • 14
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • D.W. Litchfield 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
  • 15
    • 0033018831 scopus 로고    scopus 로고
    • Protein kinase CK2 and its role in cellular proliferation, development and pathology
    • B. Guerra, and O.G. Issinger Protein kinase CK2 and its role in cellular proliferation, development and pathology Electrophoresis 20 1999 391 408
    • (1999) Electrophoresis , vol.20 , pp. 391-408
    • Guerra, B.1    Issinger, O.G.2
  • 16
    • 50649124915 scopus 로고    scopus 로고
    • Protein kinase CK2- A key suppressor of apoptosis
    • K.A. Ahmad, G. Wang, and G. Unger Protein kinase CK2- A key suppressor of apoptosis Adv Enzyme Regul 48 2008 179 187
    • (2008) Adv Enzyme Regul , vol.48 , pp. 179-187
    • Ahmad, K.A.1    Wang, G.2    Unger, G.3
  • 17
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • K. Ahmed, D.A. Gerber, and C. Cochet Joining the cell survival squad: an emerging role for protein kinase CK2 Trends Cell Biol 12 2002 226 230
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 18
    • 84865146206 scopus 로고    scopus 로고
    • Protein kinase CK2 is a regulator of angiogenesis in endometriotic lesions
    • D. Feng, S. Welker, and C. Korbel Protein kinase CK2 is a regulator of angiogenesis in endometriotic lesions Angiogenesis 15 2012 243 252
    • (2012) Angiogenesis , vol.15 , pp. 243-252
    • Feng, D.1    Welker, S.2    Korbel, C.3
  • 20
    • 16844375659 scopus 로고    scopus 로고
    • The multiple personalities of the regulatory subunit of protein kinase CK2: CK2 dependent and CK2 independent roles reveal a secret identity for CK2beta
    • A.C. Bibby, and D.W. Litchfield The multiple personalities of the regulatory subunit of protein kinase CK2: CK2 dependent and CK2 independent roles reveal a secret identity for CK2beta Int J Biol Sci 1 2005 67 79
    • (2005) Int J Biol Sci , vol.1 , pp. 67-79
    • Bibby, A.C.1    Litchfield, D.W.2
  • 21
    • 34548702649 scopus 로고    scopus 로고
    • Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: Implication for alpha-synucleinopathies
    • A. Ishii, T. Nonaka, and S. Taniguchi Casein kinase 2 is the major enzyme in brain that phosphorylates Ser129 of human alpha-synuclein: implication for alpha-synucleinopathies FEBS Lett 581 2007 4711 4717
    • (2007) FEBS Lett , vol.581 , pp. 4711-4717
    • Ishii, A.1    Nonaka, T.2    Taniguchi, S.3
  • 22
    • 84859783762 scopus 로고    scopus 로고
    • Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration
    • C.P. Xavier, R.H. Rastetter, and M. Blomacher Phosphorylation of CRN2 by CK2 regulates F-actin and Arp2/3 interaction and inhibits cell migration Sci Rep 2 2012 241
    • (2012) Sci Rep , vol.2 , pp. 241
    • Xavier, C.P.1    Rastetter, R.H.2    Blomacher, M.3
  • 23
    • 0021985671 scopus 로고
    • Effect of starvation, diabetes and insulin on the casein kinase 2 from rat liver cytosol
    • C. Martos, M. Plana, and M.D. Guasch Effect of starvation, diabetes and insulin on the casein kinase 2 from rat liver cytosol Biochem J 225 1985 321 326
    • (1985) Biochem J , vol.225 , pp. 321-326
    • Martos, C.1    Plana, M.2    Guasch, M.D.3
  • 24
    • 0021206250 scopus 로고
    • Regulation of casein kinase II by 2,3-bisphosphoglycerate in erythroid cells
    • G.M. Hathaway, and J.A. Traugh Regulation of casein kinase II by 2,3-bisphosphoglycerate in erythroid cells J Biol Chem 259 1984 2850 2855
    • (1984) J Biol Chem , vol.259 , pp. 2850-2855
    • Hathaway, G.M.1    Traugh, J.A.2
  • 25
    • 0021125696 scopus 로고
    • Kinetics of activation of casein kinase II by polyamines and reversal of 2,3-bisphosphoglycerate inhibition
    • G.M. Hathaway, and J.A. Traugh Kinetics of activation of casein kinase II 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
  • 26
    • 0035970057 scopus 로고    scopus 로고
    • The universal nature of biochemistry
    • N.R. Pace The universal nature of biochemistry Proc Natl Acad Sci USA 98 2001 805 808
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 805-808
    • Pace, N.R.1
  • 27
    • 44649117374 scopus 로고    scopus 로고
    • Pancreatic duodenal homeobox factor-1 and diabetes mellitus type 2
    • F. Al-Quobaili, and M. Montenarh Pancreatic duodenal homeobox factor-1 and diabetes mellitus type 2 Int J Mol Med 21 2008 399 404
    • (2008) Int J Mol Med , vol.21 , pp. 399-404
    • Al-Quobaili, F.1    Montenarh, M.2
  • 28
    • 77954617281 scopus 로고    scopus 로고
    • CK2 phosphorylation of Pdx-1 regulates its transcription factor activity
    • R. Meng, F. Al-Quobaili, and I. Müller CK2 phosphorylation of Pdx-1 regulates its transcription factor activity Cell Mol Life Sci 67 2010 2481 2489
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2481-2489
    • Meng, R.1    Al-Quobaili, F.2    Müller, I.3
  • 29
    • 77957778165 scopus 로고    scopus 로고
    • The role of protein kinase CK2 in the regulation of the insulin production of pancreatic islets
    • R. Meng, C. Götz, and M. Montenarh The role of protein kinase CK2 in the regulation of the insulin production of pancreatic islets Biochem Biophys Res Commun 401 2010 203 206
    • (2010) Biochem Biophys Res Commun , vol.401 , pp. 203-206
    • Meng, R.1    Götz, C.2    Montenarh, M.3
  • 30
    • 2442550827 scopus 로고    scopus 로고
    • Pdx-1 enables insulin secretion by regulating synaptotagmin 1 gene expression
    • N. Nakajima-Nagata, M. Sugai, and T. Sakurai Pdx-1 enables insulin secretion by regulating synaptotagmin 1 gene expression Biochem Biophys Res Commun 318 2004 631 635
    • (2004) Biochem Biophys Res Commun , vol.318 , pp. 631-635
    • Nakajima-Nagata, N.1    Sugai, M.2    Sakurai, T.3
  • 31
    • 0027457763 scopus 로고
    • Phosphorylation of synaptotagmin i by casein kinase II
    • B. Davletov, J.M. Sontag, and Y. Hata Phosphorylation of synaptotagmin I by casein kinase II J Biol Chem 268 1993 6816 6822
    • (1993) J Biol Chem , vol.268 , pp. 6816-6822
    • Davletov, B.1    Sontag, J.M.2    Hata, Y.3
  • 32
    • 0023474684 scopus 로고
    • Activation of casein kinase II in response to insulin and to epidermal growth factor
    • J. Sommercorn, J.A. Mulligan, and F.J. Lozeman Activation of casein kinase II in response to insulin and to epidermal growth factor Proc Natl Acad Sci USA 84 1987 8834 8838
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8834-8838
    • Sommercorn, J.1    Mulligan, J.A.2    Lozeman, F.J.3
  • 33
    • 0026094184 scopus 로고
    • Evidence that insulin activates casein kinase 2 in rat epididymal fat-cells and that this may result in the increased phosphorylation of an acid-soluble 22 kDa protein
    • T.A. Diggle, C. Schmitz-Peiffer, and A.C. Borthwick Evidence that insulin activates casein kinase 2 in rat epididymal fat-cells and that this may result in the increased phosphorylation of an acid-soluble 22 kDa protein Biochem J 279 Pt 2 1991 545 551
    • (1991) Biochem J , vol.279 , Issue.PART 2 , pp. 545-551
    • Diggle, T.A.1    Schmitz-Peiffer, C.2    Borthwick, A.C.3
  • 34
    • 0024787853 scopus 로고
    • Acute effects of insulin and glucagon on hepatic casein kinase 2 in adult fed rats: Correlation of the effects on casein kinase 2 with the changes in glycogen synthase activity
    • J. Grande, M. Perez, and M. Plana Acute effects of insulin and glucagon on hepatic casein kinase 2 in adult fed rats: correlation of the effects on casein kinase 2 with the changes in glycogen synthase activity Arch Biochem Biophys 275 1989 478 485
    • (1989) Arch Biochem Biophys , vol.275 , pp. 478-485
    • Grande, J.1    Perez, M.2    Plana, M.3
  • 35
    • 0025290028 scopus 로고
    • Evidence for an epidermal growth factor-stimulated protein kinase cascade in Swiss 3 T3 cells. Activation of serine peptide kinase activity by myelin basic protein kinases in vitro
    • N.G. Ahn, and E.G. Krebs Evidence for an epidermal growth factor-stimulated protein kinase cascade in Swiss 3 T3 cells. Activation of serine peptide kinase activity by myelin basic protein kinases in vitro J Biol Chem 265 1990 11495 11501
    • (1990) J Biol Chem , vol.265 , pp. 11495-11501
    • Ahn, N.G.1    Krebs, E.G.2
  • 36
    • 64149129617 scopus 로고    scopus 로고
    • Casein kinase II contributes to the synergistic effects of BMP7 and BDNF on Smad 1/5/8 phosphorylation in septal neurons under hypoglycemic stress
    • F. Chaverneff, and J. Barrett Casein kinase II contributes to the synergistic effects of BMP7 and BDNF on Smad 1/5/8 phosphorylation in septal neurons under hypoglycemic stress J Neurochem 109 2009 733 743
    • (2009) J Neurochem , vol.109 , pp. 733-743
    • Chaverneff, F.1    Barrett, J.2
  • 38
    • 0024282458 scopus 로고
    • Phosphorylation of hepatic insulin receptor by casein kinase 2
    • J. Grande, M. Perez, and E. Itarte 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
  • 39
    • 0030250217 scopus 로고    scopus 로고
    • Phosphotyrosine specifies the phosphorylation by protein kinase CK2 of a peptide reproducing the activation loop of the insulin receptor protein tyrosine kinase
    • O. Marin, F. Meggio, and J.W. Perich Phosphotyrosine specifies the phosphorylation by protein kinase CK2 of a peptide reproducing the activation loop of the insulin receptor protein tyrosine kinase Int J Biochem Cell Biol 28 1996 999 1005
    • (1996) Int J Biochem Cell Biol , vol.28 , pp. 999-1005
    • Marin, O.1    Meggio, F.2    Perich, J.W.3
  • 40
    • 0027202202 scopus 로고
    • Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II
    • M.J. Tanasijevic, M.G. Myers Jr., and R.S. Thoma Phosphorylation of the insulin receptor substrate IRS-1 by casein kinase II J Biol Chem 268 1993 18157 18166
    • (1993) J Biol Chem , vol.268 , pp. 18157-18166
    • Tanasijevic, M.J.1    Myers Jr., M.G.2    Thoma, R.S.3
  • 41
    • 0027166231 scopus 로고
    • Structure and function of mammalian facilitative sugar transporters
    • G.I. Bell, C.F. Burant, and J. Takeda Structure and function of mammalian facilitative sugar transporters J Biol Chem 268 1993 19161 19164
    • (1993) J Biol Chem , vol.268 , pp. 19161-19164
    • Bell, G.I.1    Burant, C.F.2    Takeda, J.3
  • 42
    • 0019877283 scopus 로고
    • Characterization of a rabbit skeletal muscle protein kinase (PC0.7) able to phosphorylate glycogen synthase and phosvitin
    • A.A. DePaoli-Roach, Z. Ahmad, and P.J. Roach Characterization of a rabbit skeletal muscle protein kinase (PC0.7) able to phosphorylate glycogen synthase and phosvitin J Biol Chem 256 1981 8955 8962
    • (1981) J Biol Chem , vol.256 , pp. 8955-8962
    • Depaoli-Roach, A.A.1    Ahmad, Z.2    Roach, P.J.3
  • 43
    • 0015515529 scopus 로고
    • Separation of the glucose-6-phosphate independent and dependent forms of glycogen synthetase from yeast
    • K.P. Huang, and E. Cabib Separation of the glucose-6-phosphate independent and dependent forms of glycogen synthetase from yeast Biochem Biophys Res Commun 49 1972 1610 1616
    • (1972) Biochem Biophys Res Commun , vol.49 , pp. 1610-1616
    • Huang, K.P.1    Cabib, E.2
  • 44
    • 0034074490 scopus 로고    scopus 로고
    • Time-co-ordinated control of glycogen synthase, protein phosphatase 2A and protein kinase CK2 during culture growth in Yarrowia lipolytica in relation to glycogen metabolism
    • C. Queiroz-Claret, P. Jolivet, and T. Chardot Time-co-ordinated control of glycogen synthase, protein phosphatase 2A and protein kinase CK2 during culture growth in Yarrowia lipolytica in relation to glycogen metabolism C R Acad Sci III 323 2000 257 266
    • (2000) C R Acad Sci III , vol.323 , pp. 257-266
    • Queiroz-Claret, C.1    Jolivet, P.2    Chardot, T.3
  • 45
    • 0034647970 scopus 로고    scopus 로고
    • Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein
    • A. Haga, Y. Niinaka, and A. Raz Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein Biochim Biophys Acta 1480 2000 235 244
    • (2000) Biochim Biophys Acta , vol.1480 , pp. 235-244
    • Haga, A.1    Niinaka, Y.2    Raz, A.3
  • 46
    • 15444361931 scopus 로고    scopus 로고
    • Differential regulation of phosphoglucose isomerase/autocrine motility factor activities by protein kinase CK2 phosphorylation
    • T. Yanagawa, T. Funasaka, and S. Tsutsumi Differential regulation of phosphoglucose isomerase/autocrine motility factor activities by protein kinase CK2 phosphorylation J Biol Chem 280 2005 10419 10426
    • (2005) J Biol Chem , vol.280 , pp. 10419-10426
    • Yanagawa, T.1    Funasaka, T.2    Tsutsumi, S.3
  • 47
    • 0026733643 scopus 로고
    • Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion
    • M. Prentki, S. Vischer, and M.C. Glennon Malonyl-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion J Biol Chem 267 1992 5802 5810
    • (1992) J Biol Chem , vol.267 , pp. 5802-5810
    • Prentki, M.1    Vischer, S.2    Glennon, M.C.3
  • 48
    • 0031568804 scopus 로고    scopus 로고
    • Protein kinase CK2 down-regulates glucose-activated expression of the acetyl-CoA carboxylase gene
    • S. Zhang, and K.H. Kim Protein kinase CK2 down-regulates glucose-activated expression of the acetyl-CoA carboxylase gene Arch Biochem Biophys 338 1997 227 232
    • (1997) Arch Biochem Biophys , vol.338 , pp. 227-232
    • Zhang, S.1    Kim, K.H.2
  • 49
    • 0020538472 scopus 로고
    • Stimulation of site-specific phosphorylation of acetyl coenzyme A carboxylase by insulin and epinephrine
    • L.A. Witters, J.P. Tipper, and G.W. Bacon Stimulation of site-specific phosphorylation of acetyl coenzyme A carboxylase by insulin and epinephrine J Biol Chem 258 1983 5643 5648
    • (1983) J Biol Chem , vol.258 , pp. 5643-5648
    • Witters, L.A.1    Tipper, J.P.2    Bacon, G.W.3
  • 50
    • 13644263231 scopus 로고    scopus 로고
    • Aging reduces glycerol-3-phosphate acyltransferase activity in activated rat splenic T-lymphocytes
    • L.W. Collison, L. Kannan, and T.M. Onorato Aging reduces glycerol-3-phosphate acyltransferase activity in activated rat splenic T-lymphocytes Biochim Biophys Acta 1687 2005 164 172
    • (2005) Biochim Biophys Acta , vol.1687 , pp. 164-172
    • Collison, L.W.1    Kannan, L.2    Onorato, T.M.3
  • 51
    • 21244453926 scopus 로고    scopus 로고
    • Phosphorylation of rat liver mitochondrial glycerol-3-phosphate acyltransferase by casein kinase 2
    • T.M. Onorato, S. Chakraborty, and D. Haldar Phosphorylation of rat liver mitochondrial glycerol-3-phosphate acyltransferase by casein kinase 2 J Biol Chem 280 2005 19527 19534
    • (2005) J Biol Chem , vol.280 , pp. 19527-19534
    • Onorato, T.M.1    Chakraborty, S.2    Haldar, D.3
  • 52
    • 0023127430 scopus 로고
    • Effects of streptozotocin-diabetes and insulin administration in vivo or in vitro on the activities of five enzymes in the adipose-tissue triacylglycerol-synthesis pathway
    • E.D. Saggerson, and C.A. Carpenter Effects of streptozotocin-diabetes and insulin administration in vivo or in vitro on the activities of five enzymes in the adipose-tissue triacylglycerol-synthesis pathway Biochem J 243 1987 289 292
    • (1987) Biochem J , vol.243 , pp. 289-292
    • Saggerson, E.D.1    Carpenter, C.A.2
  • 53
    • 0030598364 scopus 로고    scopus 로고
    • Stimulation of phospholipid synthesis in HeLa cells by epidermal growth factor and insulin: Activation of choline kinase and glycerophosphate acyltransferase
    • T. Uchida Stimulation of phospholipid synthesis in HeLa cells by epidermal growth factor and insulin: activation of choline kinase and glycerophosphate acyltransferase Biochim Biophys Acta 1304 1996 89 104
    • (1996) Biochim Biophys Acta , vol.1304 , pp. 89-104
    • Uchida, T.1
  • 54
    • 27744470520 scopus 로고    scopus 로고
    • Role for casein kinase 2 in the regulation of HIF-1 activity
    • D. Mottet, S.P. Ruys, and C. Demazy Role for casein kinase 2 in the regulation of HIF-1 activity Int J Cancer 117 2005 764 774
    • (2005) Int J Cancer , vol.117 , pp. 764-774
    • Mottet, D.1    Ruys, S.P.2    Demazy, C.3
  • 55
    • 78650321320 scopus 로고    scopus 로고
    • CX-4945, an orally bioavailable selective inhibitor of protein kinase CK2, inhibits prosurvival and angiogenic signaling and exhibits antitumor efficacy
    • A. Siddiqui-Jain, D. Drygin, and N. Streiner CX-4945, an orally bioavailable selective inhibitor of protein kinase CK2, inhibits prosurvival and angiogenic signaling and exhibits antitumor efficacy Cancer Res 70 2010 10288 10298
    • (2010) Cancer Res , vol.70 , pp. 10288-10298
    • Siddiqui-Jain, A.1    Drygin, D.2    Streiner, N.3
  • 56
    • 84855253348 scopus 로고    scopus 로고
    • Pre-clinical characterization of CX-4945, a potent and selective small molecule inhibitor of CK2 for the treatment of cancer
    • F. Pierre, P.C. Chua, and S.E. O'Brien Pre-clinical characterization of CX-4945, a potent and selective small molecule inhibitor of CK2 for the treatment of cancer Mol Cell Biochem 356 2011 37 43
    • (2011) Mol Cell Biochem , vol.356 , pp. 37-43
    • Pierre, F.1    Chua, P.C.2    O'Brien, S.E.3
  • 57
    • 50649097687 scopus 로고    scopus 로고
    • CIGB-300, a novel proapoptotic peptide that impairs the CK2 phosphorylation and exhibits anticancer properties both in vitro and in vivo
    • S.E. Perea, O. Reyes, and I. Baladron CIGB-300, a novel proapoptotic peptide that impairs the CK2 phosphorylation and exhibits anticancer properties both in vitro and in vivo Mol Cell Biochem 316 2008 163 167
    • (2008) Mol Cell Biochem , vol.316 , pp. 163-167
    • Perea, S.E.1    Reyes, O.2    Baladron, I.3
  • 58
    • 84855236499 scopus 로고    scopus 로고
    • CIGB-300, a synthetic peptide-based drug that targets the CK2 phosphoaceptor domain. Translational and clinical research
    • S.E. Perea, I. Baladron, and Y. Garcia CIGB-300, a synthetic peptide-based drug that targets the CK2 phosphoaceptor domain. Translational and clinical research Mol Cell Biochem 356 2011 45 50
    • (2011) Mol Cell Biochem , vol.356 , pp. 45-50
    • Perea, S.E.1    Baladron, I.2    Garcia, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.