FACULTY

	Palmer Taylor, Ph.D. Sandra & Monroe Trout Chair of Pharmacology; Dean, School of Pharmacy and Pharmaceutical Sciences Secondary Appointments: Associate Vice Chancellor, Health Sciences 9500 Gilman Drive, Basic Science Building 3044 La Jolla, CA 92093-0636 office tel: 858-534-1366 lab tel: 858-534-4026 Fax: 858-534-8248 Email: pwtaylor@ucsd.edu Lab Website: http://pharmacology.ucsd.edu/faculty_site/taylor/Taylor.htm
CV
Research Title
Signaling Molecules in Cholinergic Neurotransmission.
Research Description
Our laboratory is interested in the structure and function of receptors, enzymes and adhesion molecules involved in neurotransmission. We have been studying functional coupling of receptors to cellular responses, specificity of ligand recognition by nicotinic acetylcholine receptors and acetylcholinesterase, and the structures of cholinesterases, neuroligins and nicotinic receptors. With Barry Sharpless’ group at The Scripps Research Institute (TSRI), we have been employed these molecules as templates for “freeze-frame, click chemistry” synthesis of selective agonists and antagonists. Another area of investigation involves the regulation of expression of the genes encoding these proteins during differentiation and synaptogenesis in neurons, skeletal muscle and hematopoietic cells.
Recent Publications
Hoffman, R.C., Jennings, L.L., Tsigelny, I., Comoletti, D., Flynn, R.E., Sudhof, T.C. and Taylor, P. Structural Characterization of Recombinant Soluble Rat Neuroligin 1: Mapping of Secondary Structure and Glycosylation by Mass Spectrometry. Biochemistry, 43:1496-1506 (2004). Kovarik, Z., Radic, Z., Berman, H.A., Simeon-Rudolf, V., Reiner, E. and Taylor, P. Mutant Cholinesterases Possessing Enhanced Capacity for Reactivation of Their Phosphonylated Conjugates. Biochemistry, 43:3222-3229 (2004). Bourne, Y., Kolb, H.C., Radic Z., Sharpless, K.B., Taylor, P. and Marchot, P. Freeze-frame Inhibitor Captures Acetylcholinesterase in a Unique Conformation. Proc. Natl. Acad. Sci., 101:1449-1454 (2004). Comoletti, D., De Jaco, A., Jennings, L.L., Flynn, R.E., Gaietta, G., Tsigelny, I., Ellisman, M.H. and Taylor, P. The Arg451Cys-Neuroligin-3 Mutation Associated with Autism Reveals a Defect in Protein Processing. J. Neurosci., 24:4889-4893 (2004). Hibbs, R.E., Talley, T.T. and Taylor, P. Acrylodan-conjugated Cysteine Side Chains Reveal Conformational State and Ligand Site Locations of the Acetylcholine-binding Protein. J. Biol. Chem., 279:28483-28491 (2004). Hansen, S.B., Talley, T.T., Radic, Z. and Taylor, P. Structural and Ligand Recognition Characteristics of an Acetylcholine-binding Protein from Aplysia californica. J. Biol. Chem., 279:24197-24202 (2004). Bouzat, C., Gumilar, F., Spitzmaul, G., Wang, H-L., Rayes, D., Hansen, S.B., Taylor, P. and Sine, S.M. Coupling of Agonist Binding to Channel Gating in an ACh-Binding Protein Linked to an Ion Channel. Nature, 430:896-900 (2004). Chubykin, A.A., Liu, X., Comoletti, D., Tsigelny, I., Taylor, P. and Südhof, T.C. Dissection of Synapse Induction by Neuroligins: Effect of a Neuroligin Mutation Associated with Autism. J. Biol. Chem., 280:22365-22374 (2005). Bourne, Y., Talley, T.T., Hansen, S.B., Taylor, P. and Marchot, P. Crystal Structure of a Cbtx¡VAChBP Complex Reveals Essential Interactions Between Snake ƒÑ-Neurotoxins and Nicotinic Receptors. The EMBO Journal, 24:1512-1522 (2005). Krasinski, A., Radic, Z., Manetsch, R., Raushel, J., Taylor, P., Sharpless, K.B. and Kolb, H.C. In Situ Selection of Lead Compounds by Click Chemistry: Target-Guided Optimization of Acetylcholinesterase Inhibitors. J. Amer. Chem. Soc., 127:6686-6692 (2005).

Page last updated: July 14, 2009

Graduate Program in Neurosciences
University of California, San Diego

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