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Overview
Faculty
Courses
Major
Opportunities &
Activities
Careers
& Alumni
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Professional and Personal Interests
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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.
| Courses
Taught |
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- 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
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Membership in Professional Societies
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- American Scientific Affiliation
- Human Anatomy and Physiology Society
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Research |
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Individual: Biochemistry and regulation of cyclic nucleotide-dependent protein kinases, cGMP-dependent protein kinase (PKG) and cAMP-dependent protein kinase (PKA).
With Students: Site-directed mutagenesis using polymerase chain reaction (PCR), gel electrophoresis, protein expression in bacteria and baculoviral systems, and biochemical analyses of PKG and PKA. These tecniques are used to gain insight into molecular mechanisms by which PKG and PKA are regulated.
| Papers
Published and/or Presented |
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- Dey, Nupur B., Jennifer L. Busch, Sharron H. Francis, Jackie D. Corbin, and Thomas M. Lincoln, 2007. Down-regulation of type 1a 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.
Faculty continued: Dr. Raymond J.
Lewis
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