[Frontiers in Bioscience 2, a26-30, September 15, 1997]

Table of Conents
 Previous Section   Next Section


Rati Verma and Kuang Yu Chen

Department of Chemistry and The Cancer Institute of New Jersey, Rutgers, The State University of New Jersey, Piscataway, New Jersey 08855-0939

Received 8/19/97 Accepted 8/25/97


1. G.M. Hathaway & G.A. Traugh: Casein kinases: Multipotential protein kinases. Curr Topics in Cellular Regul 21, 101-127 (1982)

2. H. Meisner & M.P. Czech: Phosphorylation of transcriptional factors and cell-cycle-dependent proteins by casein kinase II. Curr. Opin. Cell Biol 3, 474-483 (1991)

3. R. Ofir, J. Dwarki, D. Rashid, & I. Verma: Phosphorylation of the C-terminus of Fos protein is required for transcriptional transrepression of the c-Fos promoter. Nature 348, 80-82, (1990)

4. D. Eliyahu, A. Raz, P. Gruss, D. Givol & M. Oren: Participation of p53 cellular tumor antigen in transformation of normal embryo cells. Nature 312, 646-654 (1984)

5. F. Meggio & L. Pinna: Subunit structure and autophosphorylation mechanism of casein kinase II from rat liver cytosol. Eur J Biochem 145, 593-599 (1984)

6. D.E. Hana, A. Rethinaswamy & C.V. Glover: Casein kinase II is required for cell cycle progression during G1 amd G2/M in Saccharomyces cerevisiae. J Biol Chem 270, 25905-25914 (1995)

7. D.R. Marshak & G.L. Russo: Regulation of protein kinase CKII during the cell division cycle. Cell Mol Biol Res 40, 513-517 (1994)

8. T. Hara & H. Endo: Polyamines alter the substrate preference of nuclear protein kinase NII. Biochemistry 21, 2632-2644 (1982)

9. H. Tabor & C.W. Tabor: Polyamines. Ann Rev Biochem 53, 749-790 (1984)

10. S.S. Cohen: Introduction to Polyamines, Prentice Hall, Inc., Englewood Cliffs, NJ. 1-179 (1971)

11. A.E. Pegg: Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy. Cancer Res 48, 759-774 (1988)

12. D. M. Hougaard, L. Bolund, K. Fujiwara & L. I. Larsson: Endogenous polyamines are intimately associated with highly condensed chromatin in vivo. A fluorescence cytochemical and immunocytochemical study of spermine and spermidine during the cell cycle and in reactivated nuclei. Eur J Cell Biol, 44, 151-155 (1987)

13. K.Y. Chen & R. Verma: Spermine specifically inhibits the phosphorylation of an 11,000-dalton nuclear protein in various cultured mammalian cell lines. Biochem Biophys Res Commun 118, 710-716 (1984)

14. R. Verma & K.Y. Chen: Spermine inhibits the phosphorylation of the 11,000- and 10,000-dalton nuclear proteins catalyzed by nuclear protein kinase NI in NB-15 mouse neuroblastoma cells. J Biol Chem 261, 2890-2896 (1986)

15. M.M. Bradford:A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254 (1976)

16.M.E.Dahmus: Purification and properties of calf thymus casein kinases I and II. J Biol Chem 256, 3319-3325 (1981)

17. V. Wunderlich & M.J. Bottger: High-mobility-group proteins and cancer--an emerging link. Cancer Res Clin Oncol, 123, 133-140 (1997)

18.M.S.Chapekar, M. Bustin, & R.I. Glazer: Evidence that high mobility group protein 17 is not phosphorylated in human colon carcinoma cells. Biochim Biophys Acta

838, 351-354 (1985)

19. F. Weighard, G. Biamonti & S. Riva: The roles of heterogeneous nuclear ribonucleoproteins (hnRNP) in RNA metabolism. Bioessays 18, 747-756 (1996)

20. H. Nakayasu & R. Berezney: Nuclear matrins: identification of the major nuclear matrix. Proc Natl Acad Sci U S A 88, 10312-10316 1991

21. P Loidl & A. Eberharter: Nuclear matrix and the cell cycle. Int Rev Cytol 162B, 377-403 (1995)

22. D. He, C. Zeng & B.R. Brinkley: Nuclear matrix proteins as structural and functional components of the mitotic apparatus. Int Rev Cytol 162B, 1-74 (1995)