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Person Details: Dr. Palmer W. Taylor

Superfund Research Program

Dr. Palmer W. Taylor

University of California-San Diego
Skaggs School of Pharmacy and Pharmaceutical Sciences
9500 Gilman Dr., MC 0657
La Jolla, California 92093-0657
Phone: 858-534-1366
Fax: 858-534-8248





  • Bourne Y, Sulzenbacher G, Radic Z, Araoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgo J, Taylor PW, Marchot P. 2015. Marine macrocyclic imines, pinnatoxins A and G: structural determinants and functional properties to distinguish neuronal α7 from muscle α1(2)βγδ nAChRs. Structure 23(6):1106-1115. doi:10.1016/j.str.2015.04.009 PMID:26004441 PMCID:PMC4461042


  • De Jaco A, Comoletti D, Dubin N, Camp S, Taylor PW. 2012. Processing of cholinesterase-like alpha/beta-hydrolase fold proteins: alterations associated with congenital disorders. Protein Pept Lett 19:173-179. PMID:21933121 PMCID:PMC4755491
  • De Jaco A, Dubi N, Camp S, Taylor PW. 2012. Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins. FEBS J 279(23):4293-4305. doi:10.1111/febs.12019 PMID:23035660
  • Falivelli G, De Jaco A, Favaloro FL, Kim H, Wilson J, Dubi N, Ellisman MH, Abrahams BS, Taylor PW, Comoletti D. 2012. Inherited genetic variants in autism-related CNTNAP2 show perturbed trafficking and ATF6 activation. Hum Mol Genet 21:4761-4773. doi:10.1093/hmg/dds320 PMID:22872700 PMCID:PMC3471401


  • Bernard V, Girard E, Hrabovska A, Camp S, Taylor PW, Plaud B, Krejci E. 2011. Distinct localization of collagen Q and PRiMA forms of acetylcholinesterase at the neuromuscular junction. Mol Cell Neurosci 46(1):272-281. doi:10.1016/j.mcn.2010.09.010 PMID:20883790 PMCID:PMC4755503
  • Miller MT, Mileni M, Comoletti D, Stevens RC, Harel M, Taylor PW. 2011. The crystal structure of the alpha-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function. Structure 19(6):767-778. doi:10.1016/j.str.2011.03.011 PMID:21620717 PMCID:PMC3279696
  • Valle AM, Radic Z, Rana BK, Mahboubi V, Wessel J, Shih P, Rao F, O'Connor DT, Taylor PW. 2011. Naturally occurring variations in the human cholinesterase genes: heritability and association with cardiovascular and metabolic traits. J Pharmacol Exp Ther 338(1):125-133. doi:10.1124/jpet.111.180091 PMID:21493754 PMCID:PMC3126649


  • Bourne Y, Radic Z, Araoz R, Talley TT, Benoit E, Servent D, Taylor PW, Molgo J, Marchot P. 2010. Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism. Proc Natl Acad Sci U S A 107(13):6076-6081. doi:10.1073/pnas.0912372107 PMID:20224036 PMCID:PMC2851920
  • Comoletti D, Miller MT, Jeffries CM, Wilson J, Demeler B, Taylor PW, Trewhella J, Nakagawa T. 2010. The macromolecular architecture of extracellular domain of alpha NRXN1: Domain organization, flexibility, and insights into trans-synaptic disposition. Structure 18(8):1044-1053. doi:10.1016/j.str.2010.06.005 PMID:20696403 PMCID:PMC2948785
  • De Jaco A, Lin MZ, Dubi N, Comoletti D, Miller MT, Camp S, Ellisman MH, Butko MT, Tsien RY, Taylor PW. 2010. Neuroligin trafficking deficiencies arising from mutations in the alpha/beta-hydrolase fold protein family. J Biol Chem 285:28674-28682. doi:10.1074/jbc.M110.139519 PMID:20615874 PMCID:PMC2937894
  • Leone P, Comoletti D, Ferracci G, Conrod S, Garcia S, Taylor PW, Bourne P, Bourne Y, Marchot P. 2010. Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions. EMBO J 29:2461-2471. doi:10.1038/emboj.2010.123 PMID:20543817 PMCID:PMC2910273
  • Wang X, Lee J, Di Jeso B, Treglia A, Comoletti D, Dubi N, Taylor PW, Arvan P. 2010. Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer. J Biol Chem 285(23):17564-17573. doi:10.1074/jbc.M110.111641 PMID:20353937 PMCID:PMC2878521


  • Taylor PW, Boudinot E, Bernard V, Camp S, Champagnat J, Krejci E, Foutz AS. 2009. Influence of differential expression of acetylcholinesterase in brain and muscle on respiration. Respir Physiol Neurobiol 165(1):40-48. doi:10.1016/j.resp.2008.10.003 PMID:18977317 PMCID:PMC2706911
  • Taylor PW, Dobbertin A, Hrabovska A, Dembele K, Camp S, Krejci E, Bernard V. 2009. Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit. J Neurosci 29(14):4519-4530. doi:10.1523/JNEUROSCI.3863-08.2009 PMID:19357277 PMCID:PMC2695489




  • Comoletti D, Flynn RE, Boucard AA, Demeler B, Schirf V, Shi J, Jennings LL, Newlin HR, Sudhof TC, Taylor PW. 2006. Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Biochemistry 45(42):12816-12827. PMID:17042500
  • De Jaco A, Comoletti D, Kovarik Z, Gaietta G, Radic Z, Lockridge O, Ellisman MH, Taylor PW. 2006. A mutation linked with autism reveals a common mechanism of endoplasmic retic a, B-beta-hydrolase fold protein family. J Biol Chem 281(14):9667-9676. PMID:16434405
  • Shi J, Koeppe JR, Komives EA, Taylor PW. 2006. Ligand-induced conformational changes in the acetylcholine-binding protein analyzed by hydrogen-deuterium exchange mass spectrometry. J Biol Chem 281(17):12170-12177. doi:10.1074/jbc.M600154200 PMID:16484218


  • Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor PW, Johnson DA. 2004. Nanosecond dynamics of acetylcholinesterase near the active center gorge. J Biol Chem 279(25):26612-26618. PMID:15078872
  • Comoletti D, De Jaco A, Jennings LL, Flynn RE, Gaietta G, Tsigelny I, Ellisman MH, Taylor PW. 2004. The Arg451Cys-neuroligin-3 mutation associated with autism reveals a defect in protein processing. J Neurosci 24(20):4889-4893. PMID:15152050
  • Hoffman RC, Jennings LL, Tsigelny I, Comoletti D, Flynn RE, Sudhof TC, Taylor PW. 2004. Structural characterization of recombinant soluble rat neuroligin 1: Mapping of secondary structure and glycosylation by mass spectrometry. Biochemistry 43(6):1496-1506. PMID:14769026
  • Jennings LL, Komives EA, Taylor PW. 2004. Organophosphate modifications of mouse acetylcholinesterase: detection of exposure by MALDI-TOF mass spectrometry. In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects, N.C. VII International Meeting on Cholinesterases, Pucon, Chile. pp.265-268.
  • Shi J, Radic Z, Johnson DA, Taylor PW. 2004. Analysis of acetylcholinesterase structure and dynamics by steady state and time-resolve fluorescence. In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects, N.C. VII International Meeting on Cholinesterases, Pucon, Chile. pp.225-227.
  • Taylor PW, Shi J, Radic Z, Boyd AE, Johnson DA. 2004. Spectroscopic approaches to the study of acetylcholinesterase structure and function. In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects, N.C. VII International Meeting on Cholinesterases, Pucon, Chile. pp.177-180.
  • Zhang L, Marquez M, de la Torre B, Taylor PW. 2004. Knockout mice with deletions of alternatively spliced exons of acetylcholinesterase. In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects, N.C. VII International Meeting on Cholinesterases, Pucon, Chile. pp.43-47.


  • George KM, Schule T, Sandoval LE, Jennings LL, Taylor PW, Thompson CM. 2003. Differentiation between acetylcholinesterase and the organophosphate-inhibited form using antibodies and the correlation of antibody recognition with reactivation mechanism and rate. J Biol Chem 278(46):45512-45518. PMID:12933813
  • Jennings LL, Malecki M, Komives EA, Taylor PW. 2003. Direct analysis of the kinetic profiles of organophosphate-acetylcholinesterase adducts by MALDI-TOF mass spectrometry. Biochemistry 42(37):11083-11091. PMID:12974645
  • Shi J, Tai K, McCammon JA, Taylor PW, Johnson DA. 2003. Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop. J Biol Chem 278(33):30905-30911. PMID:12759360


  • Shi J, Radic Z, Taylor PW. 2002. Inhibitors of different structure induce distinguishing conformations in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase. J Biol Chem 277(45):43301-43308. doi:10.1074/jbc.M204391200 PMID:12196517
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