References
- Amanchy R, Periaswamy B, Mathivanan S (2007). Human Protein Reference Database-PhosphoMotif Finder: c-myc. Accession date: 03.05.2012,A curated compendium of phosphorylation motifs. Nat Biotechnol, 25, 285-6. https://doi.org/10.1038/nbt0307-285
- Amati B, Frank SR, Donjerkovic D, Taubert S (2001). Function of the c-Myc oncoprotein in chromatin remodeling and transcription. Biochim Biophys Acta, 1471, 135-45.
- Berberich SJ, Cole MD (1992). Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev, 6, 166-76. https://doi.org/10.1101/gad.6.2.166
- Bibby AC, Litchfield DW (2005). 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, 67-79.
- Bousset K, Henriksson M, Lüscher-Firzlaff JM, Litchfield DW, Lüscher B (1993). Identification of casein kinase II phosphorylation sites in Max: effects on DNA-binding kinetics of Max homo- and Myc/Max heterodimers. Oncogene, 8, 3211-20
- Bousset K, Oelgeschlager MH, Henriksson M, et al (1994). Regulation of transcription factors c-Myc, Max, and c-Myb by casein kinase II. Cell Mol Biol Res, 40, 501-11.
- Brownlie P, Ceska T, Lamers M, et al (1997). The crystal structure of an intact human Max-DNA complex: new insights into mechanisms of transcriptional control. Structure, 5, 509-20. https://doi.org/10.1016/S0969-2126(97)00207-4
- Channavajhala P, Seldin DC (20002). Functional interaction of protein kinase CK2 and c-Myc in lymphomagenesis. Oncogene, 21, 5280-8. https://doi.org/10.1038/sj.onc.1205640
- Dastidar EG, Dayer G, Holland ZM, et al (2012). Involvement of Plasmodium falciparum protein kinase CK2 in the chromatin assembly pathway. BMC Biol, 10, 5. https://doi.org/10.1186/1741-7007-10-5
- Daya-Makin M, Sanghera JS, Mogentale TL, et al (1994). Activation of a tumor-associated protein kinase (p40TAK) and casein kinase 2 in human squamous cell carcinomas and adenocarcinomas of the lung. Cancer Res, 54, 2262-8.
- Desagher S, Osen-Sand A, Montessuit S, et al (2001). Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell, 8, 601-11. https://doi.org/10.1016/S1097-2765(01)00335-5
- Dobrowolska G, Lozeman FJ, Li D, Krebs EG (1999). CK2, a protein kinase of the next millennium. Mol Cell Biochem, 191, 3-12. https://doi.org/10.1023/A:1006882910351
- Filhol O, Cochet C (2009). Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair. Cell Mol Life Sci, 66, 1830-9. https://doi.org/10.1007/s00018-009-9151-1
- Gapany M, Faust RA, Tawfic S, et al (1995). Association of elevated protein kinase CK2 activity with aggressive behavior of squamous cell carcinoma of the head and neck. Mol Med, 1, 659-66.
- Guerra B, Issinger OG (1999). Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis, 20, 391-408. https://doi.org/10.1002/(SICI)1522-2683(19990201)20:2<391::AID-ELPS391>3.0.CO;2-N
- Kelliher MA, Seldin DC, Leder P (1996). Tal-1 induces T cell acute lymphoblastic leukemia accelerated by casein kinase IIalpha. EMBO J, 15, 5160-6.
- Kim HR, Kim K, Lee KH, Kim SJ, Kim J (2008). Inhibition of casein kinase 2 enhances the death ligand- and natural kiler cell-induced hepatocellular carcinoma cell death. Clin Exp Immunol, 152, 336-44 https://doi.org/10.1111/j.1365-2249.2008.03622.x
- Krippner-Heidenreich A, Talanian RV, Sekul R, et al (2001). Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem J, 358, 705-15. https://doi.org/10.1042/0264-6021:3580705
- Landesman-Bollag E, Romieu-Mourez R, Song DH, et al (2001). Protein kinase CK2 in mammary gland tumorigenesis. Oncogene, 20, 3247-57. https://doi.org/10.1038/sj.onc.1204411
- Landesman-Bollag E, Song DH, Romieu-Mourez R, et al (2001). Protein kinase CK2: signaling and tumorigenesis in the mammary gland. Mol Cell Biochem, 227, 153-65. https://doi.org/10.1023/A:1013108822847
- Li PF, Li J, Muller EC, et al (2002). Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC. Mol Cell, 10, 247-58. https://doi.org/10.1016/S1097-2765(02)00600-7
- Litchfield DW, Bosc DG, Canton DA, et al (2001). Functional specialization of CK2 isoforms and characterization of isoform-specific binding partners. Mol Cell Biochem, 227, 21-9. https://doi.org/10.1023/A:1013188101465
- Litchfield DW (2003). Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J, 369, 1-15. https://doi.org/10.1042/BJ20021469
- Luscher B, Kuenzel EA, Krebs EG, Eisenman RN (1989). Myc oncoproteins are phosphorylated by casein kinase II. EMBO J, 8, 1111-9.
- Meek DW, Simon S, Kikkawa U, Eckhart W (1990). The p53 tumour suppressor protein is phosphorylated at serine 389 by casein kinase II. MBO J, 9, 3253-60.
- Meggio F, Marin O, Pinna LA (1994). Substrate specificity of protein kinase CK2. Cell Mol Biol Res, 40, 401-9.
- Munstermann U, Fritz G, Seitz G (1990). Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue. Eur J Biochem, 189, 251-7. https://doi.org/10.1111/j.1432-1033.1990.tb15484.x
- Olsten ME, Litchfield DW (2004). Order or chaos? An evaluation of the regulation of protein kinase CK2. Biochem Cell Biol, 82, 681-93. https://doi.org/10.1139/o04-116
- Penn LJ, Laufer EM, Land H (1990). C-MYC: evidence for multiple regulatory functions. Semin Cancer Biol, 1, 69-80.
- Pinna LA, Meggio F (1997). Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog Cell Cycle Res, 3, 77-97.
- Pinna LA (1990). Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim Biophys Acta, 1054, 267-84. https://doi.org/10.1016/0167-4889(90)90098-X
- Ponzielli R, Katz S, Barsyte-Lovejoy D, Penn LZ (2005). Cancer therapeutics: targeting the dark side of Myc. Eur J Cancer, 41, 2485-501. https://doi.org/10.1016/j.ejca.2005.08.017
- Pruitt KD, Tatusova T, Klimke W, Maglott DR (2009). NCBI Reference Sequences: current status, policy and new initiatives. Nucleic Acids Res, 37, 32-6. https://doi.org/10.1093/nar/gkn721
- Shi X, Potvin B, Huang T, et al (2001). A novel casein kinase 2 alpha-subunit regulates membrane protein traffic in the human hepatoma cell line HuH-7. J Biol Chem, 276, 2075-82. https://doi.org/10.1074/jbc.M008583200
- Shin S, Lee Y, Kim W, et al (2005). Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8. EMBO J, 24, 3532-42. https://doi.org/10.1038/sj.emboj.7600827
- Street AJ, Blackwood E, Luscher B, Eisenman RN (1990). Mutational analysis of the carboxy-terminal casein kinase II phosphorylation site in human c-myc. Curr Top Microbiol Immunol, 166, 251-8. https://doi.org/10.1007/978-3-642-75889-8_31
- Tawfic S, Yu S, Wang H, et al (2001). Protein kinase CK2 signal in neoplasia. Histol Histopathol, 16, 573-82.
- Trembley JH, Chen Z, Unger G, et al (2010). Emergence of protein kinase CK2 as a key target in cancer therapy. Biofactors, 36, 187-95. https://doi.org/10.1002/biof.96
- Trembley JH, Wang G, Unger G, Slaton J, Ahmed K (2009). Protein kinase CK2 in health and disease: CK2: a key player in cancer biology. Cell Mol Life Sci, 66, 1858-67. https://doi.org/10.1007/s00018-009-9154-y
- von Deimling A, Aguzzi A, Kleihues P, Land H, Wiestler OD (1990). Induction of primitive neuroectodermal tumors by oncogene complementation. Verh Dtsch Ges Pathol, 74, 432-6.
- Wallis YL, Macdonald F (1999). Demystified oncogenes. Mol Pathol, 52, 55-63. https://doi.org/10.1136/mp.52.2.55
- Wang D, Westerheide SD, Hanson JL, Baldwin AS (2000). Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II. J Biol Chem, 275, 32592-7. https://doi.org/10.1074/jbc.M001358200
- Yaylim I, Isbir T (2002). Enhanced casein kinase II (CK II) activity in human lung tumours. Anticancer Res, 22, 215-8.