Ph.D. Molecular Physiology and Biophysics, Vanderbilt University, 2003
B.S. Biology, Wheaton College, 1996
About Jennifer Busch
Signal transduction is the means by which chemical signals, such as hormones, are released by the body and induce a chain reaction of subsequent protein activations that eventually cause certain physiological changes. Kinases are an important class of proteins within these transduction pathways. Specifically, I study cyclic-nucleotide dependent protein kinases. Cyclic AMP-dependent protein kinases (PKA) and cyclic GMP-dependent protein kinases (PKG) are important in many physiological processes such as blood pressure control, nerve function, and gastrointestinal motility. I am interested in learning more about the molecular mechanisms by which these kinases are regulated.
My personal interests include cycling, spending time outdoors, volunteering at my church, and reading historical fiction or biographical books. I also enjoy visiting new cities and towns; Nashville, TN, is my favorite so far.
- BIOL 241 College Biology I
- BIOL 242 College Biology II
- BIOL 321 Human Physiology
- BIOL 331 Anatomy and Physiology I
- BIOL 332 Anatomy and Physiology II
- BIOL 334 Pharmacological Physiology
Membership in Professional Societies
- American Scientific Affiliation
- Human Anatomy and Physiology Society
Dr. Busch focuses on the molecular and biochemical regulation of cyclic nucleotide-dependent protein kinases, specifically cGMP-dependent protein kinases (PKG). PKG plays important roles in a variety of physiological processes included blood flow and blood pressure modulation, learning and memory, and gastrointestinal motility.
Papers Published and/or Presented
Corbin, Jackie D., Teri-Lee Foster, Emmanuel Bessay, Jennifer L. Busch, Mitsi Blount, and Sharron H. Francis, 2011. Metal Ion Stimulators of PDE5 Cause Similar Conformational Changes in the Enzyme as does cGMP or Sildenafil. Cell. Signal. 23:778-784.
Francis, Sharron H., Jennifer L. Busch, and Jackie D. Corbin, 2010. Cyclic GMP-dependent Protein Kinase I and cGMP Phosphodiesterases in Nitric Oxide and cGMP Action. Pharmacol. Rev. 62:525-563.
Busch, Jennifer L. and Robert N. Congdon, Fall, 2009. Enhancing Student Retention and Understanding of Physiological System Integration: A Disease Assignment. HAPS EDucator 1:29-32.
Dey, Nupur B., Jennifer L. Busch, Sharron H. Francis, Jackie D. Corbin, and Thomas M. Lincoln, 2009. Cyclic GMP specifically suppresses type-Ialpha cGMP-dependent protein kinase expression by ubiquitination. Cell. Signal. 21:859-866.
Dey, Nupur B., Jennifer L. Busch, Sharron H. Francis, Jackie D. Corbin, and Thomas M. Lincoln, 2007. Down-regulation of type 1α cGMP-dependent protein kinase by the ubiquitin/proteasome pathway. Abstract. Presented at The American Heart Association Annual Conference.
Richie-Jannetta, Robyn, Jennifer L. Busch, Kristin A. Higgins, Jackie D. Corbin, and Sharron H. Francis, 2006. Isolated regulatory domains of cGMP-dependent protein kinase Ialpha and Ibeta retain dimerization and native cGMP-binding properties and undergo isoform-specific conformational changes. J. Biol. Chem. 281:6977-6984.
Busch, Jennifer L., 2005. “Are Pharmaceuticals Good or Bad?” In Not Just Science—Questions Where Christian Faith and Natural Science Intersect, ed. E.D. Cook and D.F. Chappell. Grand Rapids: Zondervan. pp. 228-234.
Busch, Jennifer L., Emmanuel P. Bessay, Sharron H. Francis, and Jackie D. Corbin, 2002. A conserved serine in PKG-I contributes to autoinhibition and lower cGMP-binding affinity. J. Biol. Chem. 277:34048-34054.
Francis, Sharron H., Celeste Poteet-Smith, Jennifer L. Busch, Robyn Richie-Jannetta, and Jackie D. Corbin, 2002. Mechanisms of autoinhibition in cyclic nucleotide-dependent protein kinases. Front. in Bioscience 7:d580.
Francis, Sharron H., Der-Ming Chu, Melissa K. Thomas, Alfreda Beasley, Kennard Grimes, Jennifer L. Busch, Illarion V. Turko, Tamara L. Haik, and Jackie D. Corbin, 1998. Ligand-induced conformational changes in cyclic nucleotide phosphodiesterases and cyclic nucleotide-dependent protein kinases. Methods 14:81-92.