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Volumn 6, Issue 1, 2011, Pages 88-98

Serine-threonine protein kinases ck1, ck2 and gsk3 in normal and malignant haematopoiesis

Author keywords

Apoptosis; Haematopoiesis; Kinase inhibitors; Leukaemia; Myeloma; Protein kinases; Stem cell; Targeted therapy

Indexed keywords

BETA CATENIN; CASEIN KINASE I; CASEIN KINASE II; GLYCOGEN SYNTHASE KINASE 3; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN KINASE B; SONIC HEDGEHOG PROTEIN; TENSIN; WNT PROTEIN;

EID: 79251515755     PISSN: 15743624     EISSN: None     Source Type: Journal    
DOI: 10.2174/157436211794109370     Document Type: Article
Times cited : (3)

References (123)
  • 1
    • 64849100299 scopus 로고    scopus 로고
    • Molecular genetic pathways as therapeutic targets in acute myeloid leukemia
    • Haferlach T. Molecular genetic pathways as therapeutic targets in acute myeloid leukemia. Hematology Am Soc Hematol Educ Prog 2008; 2008: 400-11.
    • (2008) Hematology Am Soc Hematol Educ Prog , vol.2008 , pp. 400-411
    • Haferlach, T.1
  • 3
    • 40049103766 scopus 로고    scopus 로고
    • New molecular concepts and targets in acute myeloid leukemia
    • Buzzai M, Licht JD. New molecular concepts and targets in acute myeloid leukemia. Curr Opin Hematol 2008; 15: 82-7.
    • (2008) Curr Opin Hematol , vol.15 , pp. 82-87
    • Buzzai, M.1    Licht, J.D.2
  • 4
    • 61849163272 scopus 로고    scopus 로고
    • Molecular biology of bcr-abl1- positive chronic myeloid leukemia
    • Quintas-Cardama A, Cortes J. Molecular biology of bcr-abl1- positive chronic myeloid leukemia. Blood 2009; 113: 1619-30.
    • (2009) Blood , vol.113 , pp. 1619-1630
    • Quintas-Cardama, A.1    Cortes, J.2
  • 5
    • 60749136424 scopus 로고    scopus 로고
    • Targeted drugs in chronic myeloid leukemia
    • Gora-Tybor J, Robak T. Targeted drugs in chronic myeloid leukemia. Curr Med Chem 2008; 15: 3036-51.
    • (2008) Curr Med Chem , vol.15 , pp. 3036-3051
    • Gora-Tybor, J.1    Robak, T.2
  • 6
    • 56449128746 scopus 로고    scopus 로고
    • New drugs in multiple myeloma: Mechanisms of action and phase I/II clinical findings
    • Ocio EM, Mateos MV, Maiso P, Pandiella A, San-Miguel JF. New drugs in multiple myeloma: mechanisms of action and phase I/II clinical findings. Lancet Oncol 2008; 9: 1157-65.
    • (2008) Lancet Oncol , vol.9 , pp. 1157-1165
    • Ocio, E.M.1    Mateos, M.V.2    Maiso, P.3    Pandiella, A.4    San-Miguel, J.F.5
  • 7
    • 48149112664 scopus 로고    scopus 로고
    • New targets for lymphoma treatment
    • Johnson PW. New targets for lymphoma treatment. Ann Oncol 2008; 19 Suppl 4: iv56-9.
    • (2008) Ann Oncol , vol.19 , Issue.SUPPL. 4
    • Johnson, P.W.1
  • 8
    • 63749127483 scopus 로고    scopus 로고
    • Kinome signaling through regulated proteinprotein interactions in normal and cancer cells
    • Pawson T, Kofler M. Kinome signaling through regulated proteinprotein interactions in normal and cancer cells. Curr Opin Cell Biol 2009; 21: 147-53.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 147-153
    • Pawson, T.1    Kofler, M.2
  • 9
    • 61849090213 scopus 로고    scopus 로고
    • New insights into the regulation and function of serine/threonine kinases in T lymphocytes
    • Matthews SA, Cantrell DA. New insights into the regulation and function of serine/threonine kinases in T lymphocytes. Immunol Rev 2009; 228: 241-52.
    • (2009) Immunol Rev , vol.228 , pp. 241-252
    • Matthews, S.A.1    Cantrell, D.A.2
  • 10
    • 50049097137 scopus 로고    scopus 로고
    • Targeting FLT3 for the treatment of leukemia
    • Small D. Targeting FLT3 for the treatment of leukemia. Semin Hematol 2008; 45: S17-21.
    • (2008) Semin Hematol , vol.45
    • Small, D.1
  • 11
    • 33947328520 scopus 로고    scopus 로고
    • Oncogenes in myeloproliferative disorders
    • Tefferi A, Gilliland DG. Oncogenes in myeloproliferative disorders. Cell Cycle 2007; 6: 550-66.
    • (2007) Cell Cycle , vol.6 , pp. 550-566
    • Tefferi, A.1    Gilliland, D.G.2
  • 12
    • 70349330577 scopus 로고    scopus 로고
    • The regulation of protein phosphorylation
    • Johnson LN. The regulation of protein phosphorylation. Biochem Soc Trans 2009; 37: 627-41.
    • (2009) Biochem Soc Trans , vol.37 , pp. 627-641
    • Johnson, L.N.1
  • 13
    • 69449088578 scopus 로고    scopus 로고
    • MAPK signaling pathways in the regulation of hematopoiesis
    • Geest CR, Coffer PJ. MAPK signaling pathways in the regulation of hematopoiesis. J Leukoc Biol 2009; 86: 237-50.
    • (2009) J Leukoc Biol , vol.86 , pp. 237-250
    • Geest, C.R.1    Coffer, P.J.2
  • 14
    • 33744457653 scopus 로고    scopus 로고
    • Phosphoinositide 3- kinase/Akt signaling pathway and its therapeutical implications for human acute myeloid leukemia
    • Martelli AM, Nyakern M, Tabellini G, et al. Phosphoinositide 3- kinase/Akt signaling pathway and its therapeutical implications for human acute myeloid leukemia. Leukemia 2006; 20: 911-28.
    • (2006) Leukemia , vol.20 , pp. 911-928
    • Martelli, A.M.1    Nyakern, M.2    Tabellini, G.3
  • 16
    • 42449165060 scopus 로고    scopus 로고
    • Contributions of the Raf/MEK/ERK, PI3K/PTEN/Akt/mTOR and Jak/STAT pathways to leukemia
    • Steelman LS, Abrams SL, Whelan J, et al. Contributions of the Raf/MEK/ERK, PI3K/PTEN/Akt/mTOR and Jak/STAT pathways to leukemia. Leukemia 2008; 22: 686-707.
    • (2008) Leukemia , vol.22 , pp. 686-707
    • Steelman, L.S.1    Abrams, S.L.2    Whelan, J.3
  • 17
    • 0034933482 scopus 로고    scopus 로고
    • Casein kinase I: From obscurity to center stage
    • Vielhaber E, Virshup DM. Casein kinase I: from obscurity to center stage. IUBMB Life 2001; 51: 73-8.
    • (2001) IUBMB Life , vol.51 , pp. 73-78
    • Vielhaber, E.1    Virshup, D.M.2
  • 18
    • 41549142176 scopus 로고    scopus 로고
    • Setting clock speed in mammals: The CK1 epsilon tau mutation in mice accelerates circadian pacemakers by selectively destabilizing periodD proteins
    • Meng "J, Logunova L, Maywood ES, et al. Setting clock speed in mammals: the CK1 epsilon tau mutation in mice accelerates circadian pacemakers by selectively destabilizing PERIOD proteins. Neuron 2008; 58: 78-88.
    • (2008) Neuron , vol.58 , pp. 78-88
    • Meng, J.1    Logunova, L.2    Maywood, E.S.3
  • 19
    • 0037124056 scopus 로고    scopus 로고
    • Casein kinase I and casein kinase II differentially regulate axin function in Wnt and JNK pathways
    • Zhang Y, "iu WJ, Chan SC, Han J, He X, Lin SC. Casein kinase I and casein kinase II differentially regulate axin function in Wnt and JNK pathways. J Biol Chem 2002; 277: 17706-12.
    • (2002) J Biol Chem , vol.277 , pp. 17706-17712
    • Zhang, Y.1    Qui, W.J.2    Chan, S.C.3    Han, J.4    He, X.5    Lin, S.C.6
  • 20
    • 34250375258 scopus 로고    scopus 로고
    • cAMP-response element-binding protein-coactivator interactions in response to DNA damage
    • Shanware NP, Trinh AT, Williams LM, Tibbetts RS. Coregulated ataxia telangiectasia-mutated and casein kinase sites modulate cAMP-response element-binding protein-coactivator interactions in response to DNA damage. J Biol Chem 2007; 282: 6283-91.
    • (2007) J Biol Chem , vol.282 , pp. 6283-6291
    • Shanware, N.P.1    Trinh, A.T.2    Williams, L.M.3    Tibbetts, R.S.4
  • 21
    • 0030670332 scopus 로고    scopus 로고
    • P53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase-directed drugs
    • Knippschild U, Milne DM, Campbell LE, et al. p53 is phosphorylated in vitro and in vivo by the delta and epsilon isoforms of casein kinase 1 and enhances the level of casein kinase 1 delta in response to topoisomerase- directed drugs. Oncogene 1997; 15: 1727-36.
    • (1997) Oncogene , vol.15 , pp. 1727-1736
    • Knippschild, U.1    Milne, D.M.2    Campbell, L.E.3
  • 22
    • 0033429271 scopus 로고    scopus 로고
    • Protein kinase CK1 is a p53- threonine 18 kinase which requires prior phosphorylation of serine 15
    • Dumaz N, Milne DM, Meek DW. Protein kinase CK1 is a p53- threonine 18 kinase which requires prior phosphorylation of serine 15. FEBS Lett 1999; 463: 312-6.
    • (1999) FEBS Lett , vol.463 , pp. 312-316
    • Dumaz, N.1    Milne, D.M.2    Meek, D.W.3
  • 23
    • 0035871222 scopus 로고    scopus 로고
    • Phosphorylation of murine double minute clone 2 (MDM2) protein at serine-267 by protein kinase CK2 in vitro and in cultured cells
    • Hjerrild M, Milne D, Dumaz N, Hay T, Issinger OG, Meek D. Phosphorylation of murine double minute clone 2 (MDM2) protein at serine-267 by protein kinase CK2 in vitro and in cultured cells. Biochem J 2001; 355: 347-56.
    • (2001) Biochem J , vol.355 , pp. 347-356
    • Hjerrild, M.1    Milne, D.2    Dumaz, N.3    Hay, T.4    Issinger, O.G.5    Meek, D.6
  • 24
    • 28544453010 scopus 로고    scopus 로고
    • Inhibition of casein kinase I delta alters mitotic spindle formation and induces apoptosis in trophoblast cells
    • Stoter M, Bamberger AM, Aslan B, et al. Inhibition of casein kinase I delta alters mitotic spindle formation and induces apoptosis in trophoblast cells. Oncogene 2005; 24: 7964-75.
    • (2005) Oncogene , vol.24 , pp. 7964-7975
    • Stoter, M.1    Bamberger, A.M.2    Aslan, B.3
  • 25
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield DW. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 2003; 369: 1-15.
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 26
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio F, Pinna LA. One-thousand-and-one substrates of protein kinase CK2? FASEB J 2003; 17: 349-68.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 27
    • 0037306926 scopus 로고    scopus 로고
    • Disruption of the regulatory beta subunit of protein kinase CK2 in mice leads to a cellautonomous defect and early embryonic lethality
    • Buchou T, Vernet M, Blond O, et al. Disruption of the regulatory beta subunit of protein kinase CK2 in mice leads to a cellautonomous defect and early embryonic lethality. Mol Cell Biol 2003; 23: 908-15.
    • (2003) Mol Cell Biol , vol.23 , pp. 908-915
    • Buchou, T.1    Vernet, M.2    Blond, O.3
  • 29
    • 0032879917 scopus 로고    scopus 로고
    • Globozoospermia in mice lacking the casein kinase II alpha' catalytic subunit
    • Xu X, Toselli PA, Russell LD, Seldin DC. Globozoospermia in mice lacking the casein kinase II alpha' catalytic subunit. Nat Genet 1999; 23: 118-21.
    • (1999) Nat Genet , vol.23 , pp. 118-121
    • Xu, X.1    Toselli, P.A.2    Russell, L.D.3    Seldin, D.C.4
  • 30
    • 70349320107 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2: A key player in cancer biology
    • Trembley JH, Wang G, Unger G, Slaton J, Ahmed K. Protein kinase CK2 in health and disease: CK2: a key player in cancer biology. Cell Mol Life Sci 2009; 66: 1858-67.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1858-1867
    • Trembley, J.H.1    Wang, G.2    Unger, G.3    Slaton, J.4    Ahmed, K.5
  • 31
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • Ahmed K, Gerber DA, Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol 2002; 12: 226-30.
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 33
    • 0036671304 scopus 로고    scopus 로고
    • Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC
    • Li PF, Li J, Muller EC, Otto A, Dietz R, von Harsdorf R. Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC. Mol Cell 2002; 10: 247-58.
    • (2002) Mol Cell , vol.10 , pp. 247-258
    • Li, P.F.1    Li, J.2    Muller, E.C.3    Otto, A.4    Dietz, R.5    Von Harsdorf, R.6
  • 34
    • 0034799401 scopus 로고    scopus 로고
    • Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8
    • Desagher S, Osen-Sand A, Montessuit S, et al. Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell 2001; 8: 601-11.
    • (2001) Mol Cell , vol.8 , pp. 601-611
    • Desagher, S.1    Osen-Sand, A.2    Montessuit, S.3
  • 35
    • 1942486312 scopus 로고    scopus 로고
    • CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37
    • Miyata Y, Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol Cell Biol 2004; 24: 4065-74.
    • (2004) Mol Cell Biol , vol.24 , pp. 4065-4074
    • Miyata, Y.1    Nishida, E.2
  • 36
    • 15044362465 scopus 로고    scopus 로고
    • Supervision of multiple signaling protein kinases by the CK2-Cdc37 couple, a possible novel cancer therapeutic target
    • Miyata Y, Nishida E. Supervision of multiple signaling protein kinases by the CK2-Cdc37 couple, a possible novel cancer therapeutic target. Ann N Y Acad Sci 2004; 1030: 150-7.
    • (2004) Ann N Y Acad Sci , vol.1030 , pp. 150-157
    • Miyata, Y.1    Nishida, E.2
  • 37
    • 75349084777 scopus 로고
    • Addiction to protein kinase CK2: A common denominator of diverse cancer cells?
    • Ruzzene M, Pinna LA. Addiction to protein kinase CK2: a common denominator of diverse cancer cells? Biochim Biophys Acta 1804: 499-504.
    • (1804) Biochim Biophys Acta , pp. 499-504
    • Ruzzene, M.1    Pinna, L.A.2
  • 38
    • 11144355098 scopus 로고    scopus 로고
    • The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks
    • Loizou JI, El-Khamisy SF, Zlatanou A, et al. The protein kinase CK2 facilitates repair of chromosomal DNA single-strand breaks. Cell 2004; 117: 17-28.
    • (2004) Cell , vol.117 , pp. 17-28
    • Loizou, J.I.1    El-Khamisy, S.F.2    Zlatanou, A.3
  • 39
    • 44449136965 scopus 로고    scopus 로고
    • HP1- beta mobilization promotes chromatin changes that initiate the DNA damage response
    • Ayoub N, Jeyasekharan AD, Bernal JA, Venkitaraman AR. HP1- beta mobilization promotes chromatin changes that initiate the DNA damage response. Nature 2008; 453: 682-6.
    • (2008) Nature , vol.453 , pp. 682-686
    • Ayoub, N.1    Jeyasekharan, A.D.2    Bernal, J.A.3    Venkitaraman, A.R.4
  • 40
    • 0242298578 scopus 로고    scopus 로고
    • CK2 Is a CTerminal IkappaB Kinase Responsible for NF-kappaB Activation during the UV Response
    • Kato T, Jr., Delhase M, Hoffmann A, Karin M. CK2 Is a CTerminal IkappaB Kinase Responsible for NF-kappaB Activation during the UV Response. Mol Cell 2003; 12: 829-39.
    • (2003) Mol Cell , vol.12 , pp. 829-839
    • Kato Jr., T.1    Delhase, M.2    Hoffmann, A.3    Karin, M.4
  • 41
    • 15744395819 scopus 로고    scopus 로고
    • CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity
    • Li Y, Keller DM, Scott JD, Lu H. CK2 phosphorylates SSRP1 and inhibits its DNA-binding activity. J Biol Chem 2005; 280: 11869-75.
    • (2005) J Biol Chem , vol.280 , pp. 11869-11875
    • Li, Y.1    Keller, D.M.2    Scott, J.D.3    Lu, H.4
  • 42
    • 0025286104 scopus 로고
    • Molecular cloning and expression of glycogen synthase kinase-3/factor A
    • Woodgett JR. Molecular cloning and expression of glycogen synthase kinase-3/factor A. EMBO J 1990; 9: 2431-8.
    • (1990) EMBO J , vol.9 , pp. 2431-2438
    • Woodgett, J.R.1
  • 43
    • 0035477020 scopus 로고    scopus 로고
    • GSK3 takes centre stage more than 20 years after its discovery
    • Frame S, Cohen P. GSK3 takes centre stage more than 20 years after its discovery. Biochem J 2001; 359: 1-16.
    • (2001) Biochem J , vol.359 , pp. 1-16
    • Frame, S.1    Cohen, P.2
  • 44
    • 8744271562 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 in insulin and Wnt signalling: A double-edged sword?
    • Patel S, Doble B, Woodgett JR. Glycogen synthase kinase-3 in insulin and Wnt signalling: a double-edged sword? Biochem Soc Trans 2004; 32: 803-8.
    • (2004) Biochem Soc Trans , vol.32 , pp. 803-808
    • Patel, S.1    Doble, B.2    Woodgett, J.R.3
  • 45
    • 1642494586 scopus 로고    scopus 로고
    • Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event
    • Cole A, Frame S, Cohen P. Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event. Biochem J 2004; 377: 249-55.
    • (2004) Biochem J , vol.377 , pp. 249-255
    • Cole, A.1    Frame, S.2    Cohen, P.3
  • 46
    • 0034612636 scopus 로고    scopus 로고
    • Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappa;B activation
    • Hoeflich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR. Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB; activation. Nature 2000; 406: 86-90
    • (2000) Nature , vol.406 , pp. 86-90
    • Hoeflich, K.P.1    Luo, J.2    Rubie, E.A.3    Tsao, M.S.4    Jin, O.5    Woodgett, J.R.6
  • 47
    • 34548841091 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3alpha-specific regulation of murine hepatic glycogen metabolism
    • MacAulay K, Doble BW, Patel S, Hansotia T, Sinclair EM, Drucker DJ, et al. Glycogen synthase kinase 3alpha-specific regulation of murine hepatic glycogen metabolism. Cell Metab 2007; 6: 329-37.
    • (2007) Cell Metab , vol.6 , pp. 329-337
    • MacAulay, K.1    Doble, B.W.2    Patel, S.3    Hansotia, T.4    Sinclair, E.M.5    Drucker, D.J.6
  • 48
    • 2542425324 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta suppression eliminates tumor necrosis factor-related apoptosis-inducing ligand resistance in prostate cancer
    • Liao X, Zhang L, Thrasher JB, Du J, Li B. Glycogen synthase kinase-3beta suppression eliminates tumor necrosis factor-related apoptosis-inducing ligand resistance in prostate cancer. Mol Cancer Ther 2003; 2: 1215-22.
    • (2003) Mol Cancer Ther , vol.2 , pp. 1215-1222
    • Liao, X.1    Zhang, L.2    Thrasher, J.B.3    Du, J.4    Li, B.5
  • 49
    • 2642523803 scopus 로고    scopus 로고
    • Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor
    • Song L, Zhou T, Jope RS. Lithium facilitates apoptotic signaling induced by activation of the Fas death domain-containing receptor. BMC Neurosci 2004; 5: 20.
    • (2004) BMC Neurosci , vol.5 , pp. 20
    • Song, L.1    Zhou, T.2    Jope, R.S.3
  • 50
    • 16844374033 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta participates in nuclear factor kappaB-mediated gene transcription and cell survival in pancreatic cancer cells
    • Ougolkov AV, Fernandez-Zapico ME, Savoy DN, Urrutia RA, Billadeau DD. Glycogen synthase kinase-3beta participates in nuclear factor kappaB-mediated gene transcription and cell survival in pancreatic cancer cells. Cancer Res 2005; 65: 2076-81.
    • (2005) Cancer Res , vol.65 , pp. 2076-2081
    • Ougolkov, A.V.1    Fernandez-Zapico, M.E.2    Savoy, D.N.3    Urrutia, R.A.4    Billadeau, D.D.5
  • 51
    • 27244444199 scopus 로고    scopus 로고
    • A TRAIL receptor-dependent synthetic lethal relationship between MYC activation and GSK3beta/FBW7 loss of function
    • USA
    • Rottmann S, Wang Y, Nasoff M, Deveraux QL, Quon KC. A TRAIL receptor-dependent synthetic lethal relationship between MYC activation and GSK3beta/FBW7 loss of function. Proc Natl Acad Sci USA 2005; 102: 15195-200.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 15195-15200
    • Rottmann, S.1    Wang, Y.2    Nasoff, M.3    Deveraux, Q.L.4    Quon, K.C.5
  • 52
    • 0042971809 scopus 로고    scopus 로고
    • Lithium blocks the c-Jun stress response and protects neurons via its action on glycogen synthase kinase 3
    • Hongisto V, Smeds N, Brecht S, Herdegen T, Courtney MJ, Coffey ET. Lithium blocks the c-Jun stress response and protects neurons via its action on glycogen synthase kinase 3. Mol Cell Biol 2003; 23: 6027-36.
    • (2003) Mol Cell Biol , vol.23 , pp. 6027-6036
    • Hongisto, V.1    Smeds, N.2    Brecht, S.3    Herdegen, T.4    Courtney, M.J.5    Coffey, E.T.6
  • 53
    • 7744227096 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta phosphorylates Bax and promotes its mitochondrial localization during neuronal apoptosis
    • Linseman DA, Butts BD, Precht TA, et al. Glycogen synthase kinase-3beta phosphorylates Bax and promotes its mitochondrial localization during neuronal apoptosis. J Neurosci 2004; 24: 9993-10002.
    • (2004) J Neurosci , vol.24 , pp. 9993-10002
    • Linseman, D.A.1    Butts, B.D.2    Precht, T.A.3
  • 54
    • 33644855216 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1
    • Maurer U, Charvet C, Wagman AS, Dejardin E, Green DR. Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol Cell 2006; 21: 749-60.
    • (2006) Mol Cell , vol.21 , pp. 749-760
    • Maurer, U.1    Charvet, C.2    Wagman, A.S.3    Dejardin, E.4    Green, D.R.5
  • 55
    • 23044444841 scopus 로고    scopus 로고
    • Deregulated GSK3beta activity in colorectal cancer: Its association with tumor cell survival and proliferation
    • Shakoori A, Ougolkov A, Yu ZW, et al. Deregulated GSK3beta activity in colorectal cancer: its association with tumor cell survival and proliferation. Biochem Biophys Res Commun 2005; 334: 1365-73.
    • (2005) Biochem Biophys Res Commun , vol.334 , pp. 1365-1373
    • Shakoori, A.1    Ougolkov, A.2    Yu, Z.W.3
  • 56
    • 33749015218 scopus 로고    scopus 로고
    • Aberrant nuclear accumulation of glycogen synthase kinase-3beta in human pancreatic cancer: Association with kinase activity and tumor dedifferentiation
    • Ougolkov AV, Fernandez-Zapico ME, Bilim VN, Smyrk TC, Chari ST, Billadeau DD. Aberrant nuclear accumulation of glycogen synthase kinase-3beta in human pancreatic cancer: association with kinase activity and tumor dedifferentiation. Clin Cancer Res 2006; 12: 5074-81.
    • (2006) Clin Cancer Res , vol.12 , pp. 5074-5081
    • Ougolkov, A.V.1    Fernandez-Zapico, M.E.2    Bilim, V.N.3    Smyrk, T.C.4    Chari, S.T.5    Billadeau, D.D.6
  • 57
    • 33746239119 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta positively regulates the proliferation of human ovarian cancer cells
    • Cao Q, Lu X, Feng YJ. Glycogen synthase kinase-3beta positively regulates the proliferation of human ovarian cancer cells. Cell Res 2006; 16: 671-7.
    • (2006) Cell Res , vol.16 , pp. 671-677
    • Cao, Q.1    Lu, X.2    Feng, Y.J.3
  • 58
    • 4744375264 scopus 로고    scopus 로고
    • GSK- 3beta inhibition by lithium confers resistance to chemotherapyinduced apoptosis through the repression of CD95 (Fas/APO-1) expression
    • Beurel E, Kornprobst M, Blivet-Van Eggelpoel MJ, et al. GSK- 3beta inhibition by lithium confers resistance to chemotherapyinduced apoptosis through the repression of CD95 (Fas/APO-1) expression. Exp Cell Res 2004; 300: 354-64.
    • (2004) Exp Cell Res , vol.300 , pp. 354-364
    • Beurel, E.1    Kornprobst, M.2    Blivet-Van Eggelpoel, M.J.3
  • 59
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling in development and disease
    • Clevers H. Wnt/beta-catenin signaling in development and disease. Cell 2006; 127: 469-80.
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 60
    • 25144488085 scopus 로고    scopus 로고
    • Wnt, hedgehog and snail: Sister pathways that control by GSK-3beta and beta-Trcp in the regulation of metastasis
    • Zhou BP, Hung MC. Wnt, hedgehog and snail: sister pathways that control by GSK-3beta and beta-Trcp in the regulation of metastasis. Cell Cycle 2005; 4: 772-6.
    • (2005) Cell Cycle , vol.4 , pp. 772-776
    • Zhou, B.P.1    Hung, M.C.2
  • 61
    • 28644439005 scopus 로고    scopus 로고
    • A dual-kinase mechanism for Wnt co-receptor phosphorylation and activation
    • Zeng X, Tamai K, Doble B, et al. A dual-kinase mechanism for Wnt co-receptor phosphorylation and activation. Nature 2005; 438: 873-7.
    • (2005) Nature , vol.438 , pp. 873-877
    • Zeng, X.1    Tamai, K.2    Doble, B.3
  • 62
    • 38949194936 scopus 로고    scopus 로고
    • Initiation of Wnt signaling: Control of Wnt coreceptor Lrp6 phosphorylation/activation via frizzled, dishevelled and axin functions
    • Zeng X, Huang H, Tamai K, et al. Initiation of Wnt signaling: control of Wnt coreceptor Lrp6 phosphorylation/activation via frizzled, dishevelled and axin functions. Development 2008; 135: 367-75.
    • (2008) Development , vol.135 , pp. 367-375
    • Zeng, X.1    Huang, H.2    Tamai, K.3
  • 63
    • 33947312488 scopus 로고    scopus 로고
    • Wnt-5a induces Dishevelled phosphorylation and dopaminergic differentiation via a CK1-dependent mechanism
    • Bryja V, Schulte G, Rawal N, Grahn A, Arenas E. Wnt-5a induces Dishevelled phosphorylation and dopaminergic differentiation via a CK1-dependent mechanism. J Cell Sci 2007; 120: 586-95.
    • (2007) J Cell Sci , vol.120 , pp. 586-595
    • Bryja, V.1    Schulte, G.2    Rawal, N.3    Grahn, A.4    Arenas, E.5
  • 64
    • 28644444440 scopus 로고    scopus 로고
    • Casein kinase 1 gamma couples Wnt receptor activation to cytoplasmic signal transduction
    • Davidson G, Wu W, Shen J, et al. Casein kinase 1 gamma couples Wnt receptor activation to cytoplasmic signal transduction. Nature 2005; 438: 867-72.
    • (2005) Nature , vol.438 , pp. 867-872
    • Davidson, G.1    Wu, W.2    Shen, J.3
  • 65
    • 0037162282 scopus 로고    scopus 로고
    • Casein kinase 1: A Wnt'er of disconnect
    • Polakis P. Casein kinase 1: a Wnt'er of disconnect. Curr Biol 2002; 12: R499-R501.
    • (2002) Curr Biol , vol.12
    • Polakis, P.1
  • 66
    • 0034604726 scopus 로고    scopus 로고
    • Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells
    • Song DH, Sussman DJ, Seldin DC. Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells. J Biol Chem 2000; 275: 23790-7.
    • (2000) J Biol Chem , vol.275 , pp. 23790-23797
    • Song, D.H.1    Sussman, D.J.2    Seldin, D.C.3
  • 67
    • 0038267245 scopus 로고    scopus 로고
    • CK2 phosphorylation of the armadillo repeat region of betacatenin potentiates Wnt signaling
    • Song DH, Dominguez I, Mizuno J, Kaut M, Mohr SC, Seldin DC. CK2 phosphorylation of the armadillo repeat region of betacatenin potentiates Wnt signaling. J Biol Chem 2003; 278: 24018-25.
    • (2003) J Biol Chem , vol.278 , pp. 24018-24025
    • Song, D.H.1    Dominguez, I.2    Mizuno, J.3    Kaut, M.4    Mohr, S.C.5    Seldin, D.C.6
  • 68
    • 33750946790 scopus 로고    scopus 로고
    • CK2 controls the recruitment of Wnt regulators to target genes in vivo
    • Wang S, Jones KA. CK2 controls the recruitment of Wnt regulators to target genes in vivo. Curr Biol 2006; 16: 2239-44.
    • (2006) Curr Biol , vol.16 , pp. 2239-2244
    • Wang, S.1    Jones, K.A.2
  • 69
    • 0030989287 scopus 로고    scopus 로고
    • A role for the Wnt gene family in hematopoiesis: expansion of multilineage progenitor cells
    • Austin TW, Solar GP, Ziegler FC, Liem L, Matthews W. A role for the Wnt gene family in hematopoiesis: expansion of multilineage progenitor cells. Blood 1997; 89: 3624-35.
    • (1997) Blood , vol.89 , pp. 3624-3635
    • Austin, T.W.1    Solar, G.P.2    Ziegler, F.C.3    Liem, L.4    Matthews, W.5
  • 70
    • 0037737726 scopus 로고    scopus 로고
    • Wnt proteins are lipidmodified and can act as stem cell growth factors
    • Willert K, Brown JD, Danenberg E, et al. Wnt proteins are lipidmodified and can act as stem cell growth factors. Nature 2003; 423: 448-52.
    • (2003) Nature , vol.423 , pp. 448-452
    • Willert, K.1    Brown, J.D.2    Danenberg, E.3
  • 71
    • 0032212190 scopus 로고    scopus 로고
    • Role of members of the Wnt gene family in human hematopoiesis
    • Van Den Berg DJ, Sharma AK, Bruno E, Hoffman R. Role of members of the Wnt gene family in human hematopoiesis. Blood 1998; 92: 3189-202.
    • (1998) Blood , vol.92 , pp. 3189-3202
    • Van Den Berg, D.J.1    Sharma, A.K.2    Bruno, E.3    Hoffman, R.4
  • 72
    • 20144370145 scopus 로고    scopus 로고
    • Integration of Notch and Wnt signaling in hematopoietic stem cell maintenance
    • Duncan AW, Rattis FM, DiMascio LN, et al. Integration of Notch and Wnt signaling in hematopoietic stem cell maintenance. Nat Immunol 2005; 6: 314-22.
    • (2005) Nat Immunol , vol.6 , pp. 314-322
    • Duncan, A.W.1    Rattis, F.M.2    DiMascio, L.N.3
  • 73
    • 1642499734 scopus 로고    scopus 로고
    • Beta-catenin is dispensable for hematopoiesis and lymphopoiesis
    • Cobas M, Wilson A, Ernst B, et al. Beta-catenin is dispensable for hematopoiesis and lymphopoiesis. J Exp Med 2004; 199: 221-9.
    • (2004) J Exp Med , vol.199 , pp. 221-229
    • Cobas, M.1    Wilson, A.2    Ernst, B.3
  • 74
    • 38049139201 scopus 로고    scopus 로고
    • Simultaneous loss of beta- and gamma-catenin does not perturb hematopoiesis or lymphopoiesis
    • Koch U, Wilson A, Cobas M, Kemler R, Macdonald HR, Radtke F. Simultaneous loss of beta- and gamma-catenin does not perturb hematopoiesis or lymphopoiesis. Blood 2008; 111: 160-4.
    • (2008) Blood , vol.111 , pp. 160-164
    • Koch, U.1    Wilson, A.2    Cobas, M.3    Kemler, R.4    Macdonald, H.R.5    Radtke, F.6
  • 75
    • 58049203043 scopus 로고    scopus 로고
    • Wnt-related molecules and signaling pathway equilibrium in hematopoiesis
    • Malhotra S, Kincade PW. Wnt-related molecules and signaling pathway equilibrium in hematopoiesis. Cell Stem Cell 2009; 4: 27-36.
    • (2009) Cell Stem Cell , vol.4 , pp. 27-36
    • Malhotra, S.1    Kincade, P.W.2
  • 76
    • 36649002031 scopus 로고    scopus 로고
    • Loss of beta-catenin impairs the renewal of normal and CML stem cells in vivo
    • Zhao C, Blum J, Chen A, et al. Loss of beta-catenin impairs the renewal of normal and CML stem cells in vivo. Cancer Cell 2007; 12: 528-41.
    • (2007) Cancer Cell , vol.12 , pp. 528-541
    • Zhao, C.1    Blum, J.2    Chen, A.3
  • 77
    • 57049089995 scopus 로고    scopus 로고
    • Hedgehog signaling in development and cancer
    • Jiang J, Hui CC. Hedgehog signaling in development and cancer. Dev Cell 2008; 15: 801-12.
    • (2008) Dev Cell , vol.15 , pp. 801-812
    • Jiang, J.1    Hui, C.C.2
  • 78
    • 36049033946 scopus 로고    scopus 로고
    • Hedgehog regulates smoothened activity by inducing a conformational switch
    • Zhao Y, Tong C, Jiang J. Hedgehog regulates smoothened activity by inducing a conformational switch. Nature 2007; 450: 252-8.
    • (2007) Nature , vol.450 , pp. 252-258
    • Zhao, Y.1    Tong, C.2    Jiang, J.3
  • 79
    • 0037155737 scopus 로고    scopus 로고
    • Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1
    • Price MA, Kalderon D. Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1. Cell 2002; 108: 823-35.
    • (2002) Cell , vol.108 , pp. 823-835
    • Price, M.A.1    Kalderon, D.2
  • 80
    • 32644451364 scopus 로고    scopus 로고
    • CKI, there's more than one: Casein kinase I family members in Wnt and hedgehog signaling
    • Price MA. CKI, there's more than one: casein kinase I family members in Wnt and Hedgehog signaling. Genes Dev 2006; 20: 399-410.
    • (2006) Genes Dev , vol.20 , pp. 399-410
    • Price, M.A.1
  • 81
    • 0034985595 scopus 로고    scopus 로고
    • Indian hedgehog activates hematopoiesis and vasculogenesis and can respecify prospective neurectodermal cell fate in the mouse embryo
    • Dyer MA, Farrington SM, Mohn D, Munday JR, Baron MH. Indian hedgehog activates hematopoiesis and vasculogenesis and can respecify prospective neurectodermal cell fate in the mouse embryo. Development 2001; 128: 1717-30.
    • (2001) Development , vol.128 , pp. 1717-17130
    • Dyer, M.A.1    Farrington, S.M.2    Mohn, D.3    Munday, J.R.4    Baron, M.H.5
  • 82
    • 0035257660 scopus 로고    scopus 로고
    • Sonic hedgehog induces the proliferation of primitive human hematopoietic cells via BMP regulation
    • Bhardwaj G, Murdoch B, Wu D, et al. Sonic hedgehog induces the proliferation of primitive human hematopoietic cells via BMP regulation. Nat Immunol 2001; 2: 172-80.
    • (2001) Nat Immunol , vol.2 , pp. 172-180
    • Bhardwaj, G.1    Murdoch, B.2    Wu, D.3
  • 83
    • 3843082846 scopus 로고    scopus 로고
    • Indian hedgehog gene transfer augments hematopoietic support of human stromal cells including NOD/SCID-beta2m-/- repopulating cells
    • Kobune M, Ito Y, Kawano Y, et al. Indian hedgehog gene transfer augments hematopoietic support of human stromal cells including NOD/SCID-beta2m-/- repopulating cells. Blood 2004; 104: 1002-9.
    • (2004) Blood , vol.104 , pp. 1002-1009
    • Kobune, M.1    Ito, Y.2    Kawano, Y.3
  • 84
    • 66049085125 scopus 로고    scopus 로고
    • Hedgehog signaling is dispensable for adult murine hematopoietic stem cell function and hematopoiesis
    • Hofmann I, Stover EH, Cullen DE, et al. Hedgehog signaling is dispensable for adult murine hematopoietic stem cell function and hematopoiesis. Cell Stem Cell 2009; 4: 559-67.
    • (2009) Cell Stem Cell , vol.4 , pp. 559-567
    • Hofmann, I.1    Stover, E.H.2    Cullen, D.E.3
  • 85
    • 66049102512 scopus 로고    scopus 로고
    • Hedgehog signaling is dispensable for adult hematopoietic stem cell function
    • Gao J, Graves S, Koch U, et al. Hedgehog signaling is dispensable for adult hematopoietic stem cell function. Cell Stem Cell 2009; 4: 548-58.
    • (2009) Cell Stem Cell , vol.4 , pp. 548-558
    • Gao, J.1    Graves, S.2    Koch, U.3
  • 86
    • 34247192972 scopus 로고    scopus 로고
    • Hedgehog signaling maintains a tumor stem cell compartment in multiple myeloma
    • USA
    • Peacock CD, Wang Q, Gesell GS, et al. Hedgehog signaling maintains a tumor stem cell compartment in multiple myeloma. Proc Natl Acad Sci USA 2007; 104: 4048-53.
    • (2007) Proc Natl Acad Sci , vol.104 , pp. 4048-4053
    • Peacock, C.D.1    Wang, Q.2    Gesell, G.S.3
  • 87
    • 34547683699 scopus 로고    scopus 로고
    • Essential role of stromally induced hedgehog signaling in B-cell malignancies
    • Dierks C, Grbic J, Zirlik K, et al. Essential role of stromally induced hedgehog signaling in B-cell malignancies. Nat Med 2007; 13: 944-51.
    • (2007) Nat Med , vol.13 , pp. 944-951
    • Dierks, C.1    Grbic, J.2    Zirlik, K.3
  • 88
    • 50649118068 scopus 로고    scopus 로고
    • Expansion of Bcr-Abl-positive leukemic stem cells is dependent on Hedgehog pathway activation
    • Dierks C, Beigi R, Guo GR, et al. Expansion of Bcr-Abl-positive leukemic stem cells is dependent on Hedgehog pathway activation. Cancer Cell 2008; 14: 238-49.
    • (2008) Cancer Cell , vol.14 , pp. 238-249
    • Dierks, C.1    Beigi, R.2    Guo, G.R.3
  • 89
    • 64749091867 scopus 로고    scopus 로고
    • Hedgehog signalling is essential for maintenance of cancer stem cells in myeloid leukaemia
    • Zhao C, Chen A, Jamieson CH, et al. Hedgehog signalling is essential for maintenance of cancer stem cells in myeloid leukaemia. Nature 2009.
    • (2009) Nature
    • Zhao, C.1    Chen, A.2    Jamieson, C.H.3
  • 90
    • 27444445782 scopus 로고    scopus 로고
    • Cooperative phosphorylation of the tumor suppressor phosphatase and tensin homologue (PTEN) by casein kinases and glycogen synthase kinase 3beta
    • Al-Khouri AM, Ma Y, Togo SH, Williams S, Mustelin T. Cooperative phosphorylation of the tumor suppressor phosphatase and tensin homologue (PTEN) by casein kinases and glycogen synthase kinase 3beta. J Biol Chem 2005; 280: 35195-202.
    • (2005) J Biol Chem , vol.280 , pp. 35195-35202
    • Al-Khouri, A.M.1    Ma, Y.2    Togo, S.H.3    Williams, S.4    Mustelin, T.5
  • 91
    • 32944472155 scopus 로고    scopus 로고
    • Casein kinase Iepsilon down-regulates phospho-Akt via PTEN, following genotoxic stress-induced apoptosis in hematopoietic cells
    • Okamura A, Iwata N, Tamekane A, et al. Casein kinase Iepsilon down-regulates phospho-Akt via PTEN, following genotoxic stress-induced apoptosis in hematopoietic cells. Life Sci 2006; 78: 1624-9.
    • (2006) Life Sci , vol.78 , pp. 1624-1629
    • Okamura, A.1    Iwata, N.2    Tamekane, A.3
  • 92
    • 55849138418 scopus 로고    scopus 로고
    • PTEN posttranslational inactivation and hyperactivation of the PI3K/Akt pathway sustain primary T cell leukemia viability
    • Silva A, Yunes JA, Cardoso BA, et al. PTEN posttranslational inactivation and hyperactivation of the PI3K/Akt pathway sustain primary T cell leukemia viability. J Clin Invest 2008; 118: 3762-74.
    • (2008) J Clin Invest , vol.118 , pp. 3762-3774
    • Silva, A.1    Yunes, J.A.2    Cardoso, B.A.3
  • 93
    • 20044377997 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates and upregulates Akt/PKB
    • Di Maira G, Salvi M, Arrigoni G, et al. Protein kinase CK2 phosphorylates and upregulates Akt/PKB. Cell Death Differ 2005; 12: 668-77.
    • (2005) Cell Death Differ , vol.12 , pp. 668-677
    • Di Maira, G.1    Salvi, M.2    Arrigoni, G.3
  • 94
    • 70350502303 scopus 로고    scopus 로고
    • Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells
    • Di Maira G, Brustolon F, Pinna LA, Ruzzene M. Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells. Cell Mol Life Sci 2009; 66: 3363-73.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3363-3373
    • Di Maira, G.1    Brustolon, F.2    Pinna, L.A.3    Ruzzene, M.4
  • 95
    • 33646351002 scopus 로고    scopus 로고
    • PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention
    • Zhang J, Grindley JC, Yin T, et al. PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention. Nature 2006; 441: 518-22.
    • (2006) Nature , vol.441 , pp. 518-522
    • Zhang, J.1    Grindley, J.C.2    Yin, T.3
  • 96
    • 33646376411 scopus 로고    scopus 로고
    • Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells
    • Yilmaz OH, Valdez R, Theisen BK, et al. Pten dependence distinguishes haematopoietic stem cells from leukaemia-initiating cells. Nature 2006; 441: 475-82.
    • (2006) Nature , vol.441 , pp. 475-482
    • Yilmaz, O.H.1    Valdez, R.2    Theisen, B.K.3
  • 97
    • 0041629453 scopus 로고    scopus 로고
    • Casein kinase I delta (CKIdelta) is involved in lymphocyte physiology
    • Maritzen T, Lohler J, Deppert W, Knippschild U. Casein kinase I delta (CKIdelta) is involved in lymphocyte physiology. Eur J Cell Biol 2003; 82: 369-78.
    • (2003) Eur J Cell Biol , vol.82 , pp. 369-378
    • Maritzen, T.1    Lohler, J.2    Deppert, W.3    Knippschild, U.4
  • 98
    • 11144358617 scopus 로고    scopus 로고
    • Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation
    • Okamura A, Iwata N, Nagata A, et al. Involvement of casein kinase Iepsilon in cytokine-induced granulocytic differentiation. Blood 2004; 103: 2997-3004.
    • (2004) Blood , vol.103 , pp. 2997-3004
    • Okamura, A.1    Iwata, N.2    Nagata, A.3
  • 99
    • 62049084688 scopus 로고    scopus 로고
    • Casein kinase 1alpha governs antigen-receptor-induced NF-kappaB activation and human lymphoma cell survival
    • Bidere N, Ngo VN, Lee J, et al. Casein kinase 1alpha governs antigen-receptor-induced NF-kappaB activation and human lymphoma cell survival. Nature 2009; 458(7234): 92-6.
    • (2009) Nature , vol.458 , Issue.7234 , pp. 92-96
    • Bidere, N.1    Ngo, V.N.2    Lee, J.3
  • 100
    • 0035967109 scopus 로고    scopus 로고
    • Constitutive c-Myb amino-terminal phosphorylation and DNA binding activity uncoupled during entry and passage through the cell cycle
    • Cures A, House C, Kanei-Ishii C, Kemp B, Ramsay RG. Constitutive c-Myb amino-terminal phosphorylation and DNA binding activity uncoupled during entry and passage through the cell cycle. Oncogene 2001; 20: 1784-92.
    • (2001) Oncogene , vol.20 , pp. 1784-1792
    • Cures, A.1    House, C.2    Kanei-Ishii, C.3    Kemp, B.4    Ramsay, R.G.5
  • 101
    • 0035444467 scopus 로고    scopus 로고
    • The highly conserved DNA-binding domains of A-, B- and c-Myb differ with respect to DNA-binding, phosphorylation and redox properties
    • Bergholtz S, Andersen TO, Andersson KB, Borrebaek J, Luscher B, Gabrielsen OS. The highly conserved DNA-binding domains of A-, B- and c-Myb differ with respect to DNA-binding, phosphorylation and redox properties. Nucleic Acids Res 2001; 29: 3546-56.
    • (2001) Nucleic Acids Res , vol.29 , pp. 3546-3556
    • Bergholtz, S.1    Andersen, T.O.2    Andersson, K.B.3    Borrebaek, J.4    Luscher, B.5    Gabrielsen, O.S.6
  • 102
    • 0028559037 scopus 로고
    • Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II
    • Bousset K, Oelgeschlager MH, et al. Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II. Cell Mol Biol Res 1994; 40: 501-11.
    • (1994) Cell Mol Biol Res , vol.40 , pp. 501-511
    • Bousset, K.1    Oelgeschlager, M.H.2
  • 103
    • 0035884195 scopus 로고    scopus 로고
    • Targeting of the transcription factor Max during apoptosis: phosphorylationregulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1
    • Krippner-Heidenreich A, Talanian RV, Sekul R, et al. Targeting of the transcription factor Max during apoptosis: phosphorylationregulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem J 2001; 358: 705-15.
    • (2001) Biochem J , vol.358 , pp. 705-715
    • Krippner-Heidenreich, A.1    Talanian, R.V.2    Sekul, R.3
  • 104
    • 0031803277 scopus 로고    scopus 로고
    • Both PU.1 and nuclear factor-kappa B mediate lipopolysaccharide- induced HIV-1 long terminal repeat transcription in macrophages
    • Lodie TA, Reiner M, Coniglio S, Viglianti G, Fenton MJ. Both PU.1 and nuclear factor-kappa B mediate lipopolysaccharide- induced HIV-1 long terminal repeat transcription in macrophages. J Immunol 1998; 161: 268-76.
    • (1998) J Immunol , vol.161 , pp. 268-276
    • Lodie, T.A.1    Reiner, M.2    Coniglio, S.3    Viglianti, G.4    Fenton, M.J.5
  • 105
    • 34948883495 scopus 로고    scopus 로고
    • PVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2
    • Yang H, Minamishima YA, Yan Q, et al. PVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2. Mol Cell 2007; 28: 15-27.
    • (2007) Mol Cell , vol.28 , pp. 15-27
    • Yang, H.1    Minamishima, Y.A.2    Yan, Q.3
  • 106
    • 50649090911 scopus 로고    scopus 로고
    • Inhibition of protein kinase CK2 suppresses angiogenesis and hematopoietic stem cell recruitment to retinal neovascularization sites
    • Kramerov AA, Saghizadeh M, Caballero S, et al. Inhibition of protein kinase CK2 suppresses angiogenesis and hematopoietic stem cell recruitment to retinal neovascularization sites. Mol Cell Biochem 2008; 316: 177-86.
    • (2008) Mol Cell Biochem , vol.316 , pp. 177-186
    • Kramerov, A.A.1    Saghizadeh, M.2    Caballero, S.3
  • 108
    • 0037043777 scopus 로고    scopus 로고
    • Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis
    • Channavajhala P, Seldin DC. Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene 2002; 21: 5280-8.
    • (2002) Oncogene , vol.21 , pp. 5280-5288
    • Channavajhala, P.1    Seldin, D.C.2
  • 109
    • 33748163052 scopus 로고    scopus 로고
    • Multiple myeloma cell survival relies on high activity of protein kinase CK2
    • Piazza FA, Ruzzene M, Gurrieri C, et al. Multiple myeloma cell survival relies on high activity of protein kinase CK2. Blood 2006; 108: 1698-707.
    • (2006) Blood , vol.108 , pp. 1698-1707
    • Piazza, F.A.1    Ruzzene, M.2    Gurrieri, C.3
  • 110
    • 33847361829 scopus 로고    scopus 로고
    • Protein kinase CK2alpha as an unfavorable prognostic marker and novel therapeutic target in acute myeloid leukemia
    • Kim JS, Eom JI, Cheong JW, et al. Protein kinase CK2alpha as an unfavorable prognostic marker and novel therapeutic target in acute myeloid leukemia. Clin Cancer Res 2007; 13: 1019-28.
    • (2007) Clin Cancer Res , vol.13 , pp. 1019-1028
    • Kim, J.S.1    Eom, J.I.2    Cheong, J.W.3
  • 111
    • 0344441923 scopus 로고    scopus 로고
    • Protein kinase CKIIalpha interacts with the Bcr moiety of Bcr/Abl and mediates proliferation of Bcr/Abl-expressing cells
    • Mishra S, Reichert A, Cunnick J, et al. Protein kinase CKIIalpha interacts with the Bcr moiety of Bcr/Abl and mediates proliferation of Bcr/Abl-expressing cells. Oncogene 2003; 22: 8255-62.
    • (2003) Oncogene , vol.22 , pp. 8255-8262
    • Mishra, S.1    Reichert, A.2    Cunnick, J.3
  • 112
    • 33845514847 scopus 로고    scopus 로고
    • Treatment of P190 Bcr/Abl lymphoblastic leukemia cells with inhibitors of the serine/threonine kinase CK2
    • Mishra S, Pertz V, Zhang B, et al. Treatment of P190 Bcr/Abl lymphoblastic leukemia cells with inhibitors of the serine/threonine kinase CK2. Leukemia 2007; 21: 178-80.
    • (2007) Leukemia , vol.21 , pp. 178-180
    • Mishra, S.1    Pertz, V.2    Zhang, B.3
  • 114
    • 49749110451 scopus 로고    scopus 로고
    • Protein kinase CK2 as a druggable target
    • Sarno S, Pinna LA. Protein kinase CK2 as a druggable target. Mol Biosyst 2008; 4: 889-94.
    • (2008) Mol Biosyst , vol.4 , pp. 889-894
    • Sarno, S.1    Pinna, L.A.2
  • 115
    • 30044444251 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3 is an in vivo regulator of hematopoietic stem cell repopulation
    • Trowbridge JJ, Xenocostas A, Moon RT, Bhatia M. Glycogen synthase kinase-3 is an in vivo regulator of hematopoietic stem cell repopulation. Nat Med 2006; 12: 89-98.
    • (2006) Nat Med , vol.12 , pp. 89-98
    • Trowbridge, J.J.1    Xenocostas, A.2    Moon, R.T.3    Bhatia, M.4
  • 116
    • 72849126360 scopus 로고    scopus 로고
    • Pivotal role for glycogen synthase kinase-3 in hematopoietic stem cell homeostasis in mice
    • Huang J, Zhang Y, Bersenev A, et al. Pivotal role for glycogen synthase kinase-3 in hematopoietic stem cell homeostasis in mice. J Clin Invest 2009; 119: 3519-29.
    • (2009) J Clin Invest , vol.119 , pp. 3519-3529
    • Huang, J.1    Zhang, Y.2    Bersenev, A.3
  • 117
    • 55249120170 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 in MLL leukaemia maintenance and targeted therapy
    • Wang Z, Smith KS, Murphy M, Piloto O, Somervaille TC, Cleary ML. Glycogen synthase kinase 3 in MLL leukaemia maintenance and targeted therapy. Nature 2008; 455: 1205-9.
    • (2008) Nature , vol.455 , pp. 1205-1209
    • Wang, Z.1    Smith, K.S.2    Murphy, M.3    Piloto, O.4    Somervaille, T.C.5    Cleary, M.L.6
  • 118
    • 73149097234 scopus 로고    scopus 로고
    • Innate and adaptive immune responses regulated by glycogen synthase kinase-3 (GSK3)
    • Beurel E, Michalek SM, Jope RS. Innate and adaptive immune responses regulated by glycogen synthase kinase-3 (GSK3). Trends Immunol 2010; 31(1): 24-31.
    • (2010) Trends Immunol , vol.31 , Issue.1 , pp. 24-31
    • Beurel, E.1    Michalek, S.M.2    Jope, R.S.3
  • 119
    • 77249158055 scopus 로고    scopus 로고
    • SB216763 (3-(2,4- Dichlorophenyl)-4-(1-methyl-1H-indol-3-yl)-1H-pyrrole- 2,5- dione), a Glycogen Synthase Kinase-3 inhibitor, displays therapeutic properties in a mouse model of pulmonary inflammation and fibrosis
    • Gurrieri C, Piazza F, Gnoato M, et al. SB216763 (3-(2,4- Dichlorophenyl)-4-(1-methyl-1H-indol-3-yl)-1H-pyrrole-2,5- dione), a Glycogen Synthase Kinase-3 inhibitor, displays therapeutic properties in a mouse model of pulmonary inflammation and fibrosis. J Pharmacol Exp Ther 2010; 332(3): 785-94.
    • (2010) J Pharmacol Exp Ther , vol.332 , Issue.3 , pp. 785-794
    • Gurrieri, C.1    Piazza, F.2    Gnoato, M.3
  • 120
    • 34547114509 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3 activity leads to epigenetic silencing of nuclear factor kappaB target genes and induction of apoptosis in chronic lymphocytic leukemia B cells
    • Ougolkov AV, Bone ND, Fernandez-Zapico ME, Kay NE, Billadeau DD. Inhibition of glycogen synthase kinase-3 activity leads to epigenetic silencing of nuclear factor kappaB target genes and induction of apoptosis in chronic lymphocytic leukemia B cells. Blood 2007; 110: 735-42.
    • (2007) Blood , vol.110 , pp. 735-742
    • Ougolkov, A.V.1    Bone, N.D.2    Fernandez-Zapico, M.E.3    Kay, N.E.4    Billadeau, D.D.5
  • 121
    • 33744476502 scopus 로고    scopus 로고
    • A crosstalk between the Wnt and the adhesion-dependent signaling pathways governs the chemosensitivity of acute myeloid leukemia
    • De Toni F, Racaud-Sultan C, Chicanne G, et al. A crosstalk between the Wnt and the adhesion-dependent signaling pathways governs the chemosensitivity of acute myeloid leukemia. Oncogene 2006; 25: 3113-22.
    • (2006) Oncogene , vol.25 , pp. 3113-3122
    • De Toni, F.1    Racaud-Sultan, C.2    Chicanne, G.3
  • 122
    • 16844378799 scopus 로고    scopus 로고
    • Leukaemia stem cells and the evolution of cancer-stem-cell research
    • Huntly BJ, Gilliland DG. Leukaemia stem cells and the evolution of cancer-stem-cell research. Nat Rev Cancer 2005; 5: 311-21.
    • (2005) Nat Rev Cancer , vol.5 , pp. 311-321
    • Huntly, B.J.1    Gilliland, D.G.2
  • 123
    • 58249105984 scopus 로고    scopus 로고
    • Targeting the leukemic stem cell: The Holy Grail of leukemia therapy
    • Misaghian N, Ligresti G, Steelman LS, et al. Targeting the leukemic stem cell: the Holy Grail of leukemia therapy. Leukemia 2009; 23: 25-42.
    • (2009) Leukemia , vol.23 , pp. 25-42
    • Misaghian, N.1    Ligresti, G.2    Steelman, L.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.