
Brooks, C.L., B.G. Kim, P. Aphale, B. Kleeman and G.C. Johnson: Phosphorylated Variants of Bovine Prolactin. Molecular and Cellular Endocrinology 71:117-123 (1990).
Kim, B.G. and Brooks C.L.: Isolation and Characterization of Phosphorylated Bovine Prolactin. Biochemical Journal 296: 41-47 (1993).
Brooks, C.L., Isaacs
Wicks, J.R. and Brooks, C.L. Biological Activity of Phosphorylated and Dephosphorylated Bovine Prolactin. Molecular and Cellular Endocrinology 112:223-229 (1995).
Maciejewski, P.M., Peterson, F.C., Anderson P.J., and Brooks, C.L.. Mutation of Serine 90 to Glutamic Acid Mimics Phosphorylation of Bovine Prolactin. Journal of Biological Chemistry 270:27661-27665 (1995)
Oglesbee, M., Liu, Z., Kenney, H., and Brooks, C.L. The Highly Inducible Member of the 70kDa Family of Heat Shock Proteins Increases Canine Distemper Virus Polymerase Activity. Journal General Virology 77:2125-2135 (1996).
Permyakov, E.A., Veprintsev, D.B., Deikus, G.Y., Permyakov, S.E., Kalinichenko, L.P., Grischenko, V.M., and Brooks, C.L. pH-induced Transition and Zn2+-binding Properties of Bovine Prolactin. FEBS Letters 405:273-276 (1997).
Anderson, P.J., Brooks, C.L. and Berliner, L.J. Functional Identification of Calcium Binding Residues in Bovine α-Lactalbumin. Biochemistry 36:11648-11643 (1997).
Peterson, F.C. and Brooks, C.L. Identification of a Motif Associated with the Lactogenic Actions of Human Growth Hormone. J. Biol. Chem. 272:21444-21448 (1997).
Brooks, C.L. and Saiduddin, S. Phosphorylation of Bovine Prolactin Eliminates Luteotrophic Activity in the Rat. Life Sciences 63:1281-1287 (1998).
Wicks, J.R. and Brooks, C.L. Prolactin Kinase Activity in Bovine Anterior Pituitary Subcellular Fractions. Molec. Cell. Endo. 147: 125-132 (1999).
Peterson, F.C. Anderson, P.J., Berliner, L.J. and Brooks, C.L. Efficient Expression, Folding and Characterization of Small Molecular Weight Proteins with a pT7-7-derived Phagemid. Protein Expression and Purification, 15:16-23 (1999).
Duda, K.M. and Brooks, C.L. Human Growth Hormone Site 2 Lactogenic Activity Requires a Distant Tyrosine 164. FEBS Letters, 449: 120-124 (1999).
Wicks, J.R. and Brooks, C.L. Growth Hormone Kinase Activity in Bovine Anterior Pituitary Subcellular Fractions. Endocrine 10: 77-82 (1999).
Veprintsev, D.B., Naryan, M, Permyakov, S.E., Uversky, V.N., Brooks, C.L., Cherskaya, A.M.,Permyakov, E.A. and Berliner, L.J. Fine Tuning the N-terminus of a Calcium α-lactalbumin. Binding Protein. Proteins: Structure, Function and Genetics 37: 65-72 (1999).
Peterson, F.C. and Brooks, C.L. Species Specificity of Growth Hormone. FEBS Letters 472:276-282 (2000).
Permykov, S.E., Veprintsev, D.B., Brooks, C.L., Permykov, E.A. and Berliner, L.J. α- lactalbumin:Zinc Binding in Bovine Sequence Homology May Not Be a Predictor of Subtile Functional Features. Proteins: Structure, Function and Genetics 40: 106-111 (2000).
Frangione-Beebe, M., Albrecht, B., Dakappagari, N., Rose, R.T, Brooks, C.L., Schwendeman, S.P., Lairmore, M.D. and Kaumaya, P.T.P. Enhanced Immunogenicity of a Conformational Epitope of Human T-Lymphotropic Virus Type 1 using a Novel Chimeric Peptide. Vaccine 19: 1068-1081 (2001).
Permyakov, S.E., Uversky, V.N., Veprintsev, D.B., Cherskaya, A.M., Brooks, C.L., Permyakov, E.A. and Berliner, L.J. α-Lactalbumin: Effects Mutating Aspartate in the Calcium Binding Site of on the Protein Stability and Cation Binding. Protein Engineering 14: 785-789 (2001).
Zhang, X., Glendening, C., Link, H., Parks, C.L., Brooks, C.L.,
Schenck, E.J.H., Canfield J.M. and Brooks, C.L., Functional Relationship of Serine 90 Phosphorylation and the Surrounding Putative
Duda, K.M. and Brooks, C.L., Identification of Residues Outside the Two Binding Sites that are Critical for the Lactogenic Activity of Human Growth Hormone. J. Biol. Chem. 278: 22734-22739 (2003).
Duda, K.M. and Brooks, C.L., Differential Effects of Zinc on Functionally Distinct Human Growth Hormone Mutations. Protein Engineering 16: 531-534 (2003).
Svensson, M., Fast, J., Mossberg, A.-K., Duringer, C., Gustafsson, L., Hallgren, O., Brooks, C.L., Berliner, L., Linse, S. and Svanborg, C. α-Lactalbumin Unfolding is Not Sufficient to Cause Apoptosis but is Required for the Conversion to Hamlet (human α-lactalbumin made lethal to tumor cells). Protein Science 12: 2794-2804 (2003).
Peterson, F.C. and Brooks, C.L., Mini-helix-1 is Required for Lactogenic But Not Somatotrophic Activity of Human Lactogenic Hormones. Protein Engineering, Design and Selection, 17: 417-424 (2004).
Sivaprasad, U. and
Permyakov S.E., Makhatadze G.I., Owenius R., Uversky V.N., Brooks C.L., Permykov, E.A. and Berliner, L.J., How to Improve Nature: Study of the Electrostatic Properties of the Surface of α-Lactalbumin. Protein Engineering, Design and Structure 18: 425-422 (2005).
Schenck, E.J.H. and Brooks, C.L., Effects of S85E Bovine Growth Hormone in Transgenic Mice. Experimental Biology and Medicine 231: 296-302 (2006).
Chaudhury C., Brooks C.L., Carter D.C., Robinson J.M. and
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