Claiborne Glover
Professor of Biochemistry and Molecular Biology
Ph.D. (1979) University of Rochester
Phone: 706-542-1769
Email: glover@uga.edu
See my Laboratory Home Page

Research Interests
My laboratory is attempting to define the physiological role and mechanism of regulation of Casein Kinase II (CKII), a ubiquitous and highly conserved member of the eukaryotic Ser/Thr/Tyr protein kinase family. We have used two model systems in exploring this problem, Drosophila melanogaster and Saccharomyces cerevisiae, and are currently focusing on the latter.
  • Poole, A., Poore, T., Bandhakavi, S., McCann, R.O., Hanna, D.E. and C.V.C. Glover. 2005. A global view of CK2 function and regulation. Mol. Cell Biochem. 274: 163-170.
  • Brewer, J.M., Glover, C.V., Holland, M.J. and L. Lebioda. 2003. Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H195F and N207A enolases. J. Protein Chem. 22: 353-361.
  • Bandhakavi, S., McCann, R.O., Hanna, D.E. and C.V.C. Glover. 2003. Genetic interactions among ZDS1,2, CDC37, and protein kinase CK2 in Saccharomyces cerevisiae. FEBS Lett. 554: 295-300.
  • Bandhakavi, S., McCann, R.O., Hanna, D.E. and Glover C.V.C. 2003. A positive feedback loop between protein kinase CKII and Cdc37 promotes the activity of multiple protein kinases. J. Biol. Chem. 278: 2829-2836.
  • Zhao, W., Bidwai, A.P. and C.V.C. Glover. 2002. Interaction of casein kinase II with ribosomal protein L22 of Drosophila melanogaster. Biochem. Biophys. Res. Commun. 298: 60-66.
  • Ackermann, K., Waxmann, A., Glover, C.V.C., and W. Pyerin. 2001. Genes targeted by protein kinase CK2: A genome-wide expression array analysis in yeast. Mol. Cell. Biochem. 227: 59-66.
  • Dotan, I., Ziv, E., Dafni, N., Beckman, J. S., McCann, R.O., Glover, C.V. and D. Canaani. 2001. Functional conservation between the human, nematode, and yeast CK2 cell cycle genes. Biochem. Biophys. Res. Commun. 288: 603-609.
  • Bidwai, A.P., Saxena, A., Zhao, W., McCann, R.O. and C.V.C. Glover. 2000. Multiple, closely spaced alternative 5' exons in the DmCKIIb gene of Drosophila melanogaster. Mol. Cell Biol. Res. Commun. 3: 283-291.
  • Tenney, K.A. and C.V.C. Glover. 1999. Transcriptional regulation of the S. cerevisiae ENA1 gene by casein kinase II. Mol. Cell. Biochem. 191: 161-167.
  • Bidwai, A. P., Zhao, W. and C.V.C. Glover. 1999. A gene located at 56F1-2 in Drosophila melanogaster encodes a novel b-like subunit of casein kinase II. Mol. Cell Biol. Res. Commun. 1: 21-28.
  • Brewer, J.M., Glover, C.V.C., Holland, M.J., and L. Lebioda. 1998. Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism. Biochem. Biophys. Acta 1383: 351-355.
  • Glover III, C.V.C. 1998. On the physiological role of casein kinase II in Saccharomyces cerevisiae. Prog. Nucl. Acid Res. Mol. Biol. 57: 95-133.
  • Rethinaswamy, A., Birnbaum, M.J. and C.V.C. Glover. 1998. Temperature-sensitive mutations of the CKA1 gene reveal a role for casein kinase II in maintenance of cell polarity in Saccharomyces cerevisiae. J. Biol. Chem. 273: 5869-5877.
  • “Structure and Function of an RNA Pol II CTD Phosphatase”, NIH