Faculty: Biography

Eileen J. Kennedy, Ph.D.
Assistant Professor
Pharmaceutical and Biomedical Sciences
Address: Pharmacy South Building
University of Georgia
Athens, GA 30602
Office: Room 342
Phone: (706) 542-6497
Email: ekennedy@uga.edu
Biosketch
B.S. Biochemistry University of WashingtonSeattle1998
M.S. Chemistry (Biochemistry) University of California, San DiegoLa Jolla2002
Ph.D. Chemistry (Biochemistry) University of California, San DiegoLa Jolla2005
Post-doctoral Experience
Research Associate, Chemistry and Chemical Biology, Harvard University, Cambridge, MA July 2009-June 2010
Postdoctoral Fellow, Chemistry and Chemical Biology, Harvard University, Cambridge, MA January 2006-June 2009
Honors and Awards
2013 Invited Session Chair, 6th International Peptide Symposium/23rd American Peptide Symposium Joint Conference, Waikoloa, HI
2013 Faculty Summer Research Support for Outstanding Scientists, Office of the Provost, UGA
2013 Invited Speaker, 4th International Meeting on Anchored cAMP Signaling Complexes, Denver, CO
2013 Invited Speaker, Meeting on Cyclic Nucleotide Signaling in Malaria, CNRS, Paris, France
2011 Minority Young Scientist Travel Award by ASBMB/ASPET for Experimental Biology
2009 Scholar-in-Training Award, AACR-ACS Joint Conference for Chemistry in Cancer Research
2008 Burroughs Wellcome Fund’s Career Awards at the Scientific Interface, National Finalist
2007 Scholar-in-Training Award, AACR-ACS Joint Conference for Chemistry in Cancer Research
2006-2009 American Cancer Society Postdoctoral Fellow
2003-2005 American Heart Association Predoctoral Fellow
Research Interests
The protein kinase superfamily comprises one of the largest gene families encoded in the human genome. A comprehensive understanding of kinase activity under normal and disease states is critical in order to identify targets for disease intervention. However, studying kinase signaling is inherently challenging since there are over 500 kinases in the human genome, and as a result, there is significant crosstalk among multiple kinases for phosphorylation targets. Additionally, multiple isoforms exist for many kinases, thereby making it nearly impossible to address the question using genetic knockdowns/knockouts since other genes will compensate with altered expression levels. To address this question, Dr. Kennedy's lab is developing novel chemical biology strategies to synthetically disrupt protein:protein interactions (PPIs) using chemically stabilized peptides. This methodology allows them to develop investigative tools that can be applied to elegantly and selectively manipulate protein-protein interactions that are involved in signaling pathways within a cellular environment. Their long-term goal is to develop synthetic biologics that can be used to probe cell signaling events that are mediated by kinases. By inhibiting specific protein-protein interactions within a cellular environment, cancer-related cell signaling events can be studied in a temporal manner and highlight new strategies for therapeutic intervention. They are applying this strategy to study the AGC family of kinases as well as EGFR in breast and lung cancer models.
Representative Publications
Wang, Y., Ho, T., Bertinetti, D., Neddermann, M., Franz, E., Mo, Gary C.H., Schendowich, L.P., Sukhu, A., Spelts, R.C., Zhang, J., Herberg, F.W., and Kennedy, E.J. (2014) “Isoform-selective disruption of AKAP-localized PKA using hydrocarbon stapled peptides.” ACS Chem. Biol., 9: 635-642, (PMCID 24422448).

Fortunato, M.J., Ball, C.B., Hollinger, K., Patel, N.B., Modi, J.N., Rajasekaran, V., Nonneman, D.J., Ross, J.W., Kennedy, E.J., Selsby, J.T., and Beedle, A.M. (2014) “Development of rabbit monoclonal antibodies for detection of alph-dystrogylan in normal and dystrophic tissue.” PLoS One, 9:e97567.

Kennedy, E. J., Yang, J., Pillus, L., Taylor, S. S., and Ghosh, G. (2009) “Identifying critical non-catalytic residues that modulate PKA activity.” PLoS One, 4:e4746, (PMCID 19270744).

Yang, J., Kennedy, E. J., Wu, J., Deal, M. S., Pennypacker, J., Ghosh, G., and Taylor, S. S. (2009) “Contribution of non-catalytic core residues to activity and regulation in PKA.” J. Biol. Chem., 284: 6241-6248, (PMCID 19122195).
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