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Education
2001 Ph.D., Pharmacology, Duke University, Durham, NC
1994 B.S., Chemistry, Coppin State University, Baltimore, MD
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Dr. Jones completed post-doctoral training at the Instituto Ramon y Cajal in Madrid, Spain and at the University of Cincinnati. Dr. Jones was a staff research scientist at the Genome Research Institute in Cincinnati, OH from 2004-2006. He held the position of Visiting Scholar in the neurobiology department at Pomona College from 2006-2007 and Visiting Professor of Neurobiology from 2007-2008. He began teaching in the College of Pharmacy at Western University of Health Sciences in 2008. He joined the faculty of the College of Osteopathic Medicine of the Pacific at Western University as Assistant Professor of Pharmacology in 2008.
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1. Jones, K.S., VanDongen, H.M.A, and VanDongen, A.M.J. (2002). The NMDA receptor M3 domain is a conserved transduction element coupling ligand binding to channel opening. Journal of Neuroscience 22: 2044-2053.
2. Jones, K.S., and VanDongen, A.M.J. (2008) Protons inhibit NMDA receptors by restricting translocation of the M3 domain. Submitted to Brain Research
3 Jones, K.S., Kim, S., and Penberthy W.T. (2008) Nicotinamide suppresses lipolysis in Zebrafish embryos. Submitted to European Journal of Lipid Science and Technology
4. Chen, J.C., Patel R.C., and Jones, K.S. NMDA blockade increases locomotor activity in the zebrafish, Danio rerio. Manuscript in progress
5. TM3 is a Dynamic Transduction Element Coupling Ligand Binding to Channel Gating in the NMDA Receptor. K.S. Jones, H.M.A. VanDongen and A.M.J. VanDongen. Society for Neuroscience (Poster presentation)
6. TM3 is a Dynamic Transduction Element Coupling Ligand Binding to Channel Gating in the NMDA Receptor. K.S. Jones, H.M.A. VanDongen and A.M.J. VanDongen. Society for Neuroscience (Oral presentation)
7. Mutations in the M3 segment of NMDAR selectively affect open channel block. K.S. Jones, H.M.A. VanDongen and A.M.J. VanDongen. Society for Neuroscience (Poster presentation)
8. Pharmacological characterization of NR1 subunit residues in the glycine binding pocket of the N-Methyl D-Aspartate Receptor. M.W.Wood, H.M.A VanDongen, K.S. Jones, and A.M.J. VanDongen Society for Neuroscience (Poster presentation)
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