| Year |
Citation |
Score |
| 2022 |
Stokes C, Camacho-Hernandez GA, Thakur GA, Wu X, Taylor P, Papke RL. Differential Activation and Desensitization States Promoted by Noncanonical 7 Nicotinic Acetylcholine Receptor Agonists. The Journal of Pharmacology and Experimental Therapeutics. 383: 157-171. PMID 36279397 DOI: 10.1124/jpet.122.001354 |
0.424 |
|
| 2022 |
Kem WR, Andrud K, Bruno G, Xing H, Soti F, Talley TT, Taylor P. Interactions of Nereistoxin and Its Analogs with Vertebrate Nicotinic Acetylcholine Receptors and Molluscan ACh Binding Proteins. Marine Drugs. 20. PMID 35049904 DOI: 10.3390/md20010049 |
0.772 |
|
| 2021 |
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z. Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects. The Journal of Biological Chemistry. 101007. PMID 34324828 DOI: 10.1016/j.jbc.2021.101007 |
0.373 |
|
| 2021 |
Taylor P, Shong YJ, Samskey N, Ho KY, Radic' Z, Fenical W, Sharpless KB, Kovarik Z, Andrea Camacho-Hernandez G. Ligand design for human acetylcholinesterase and nicotinic acetylcholine receptors, extending beyond the conventional and canonical. Journal of Neurochemistry. PMID 33638151 DOI: 10.1111/jnc.15335 |
0.352 |
|
| 2020 |
Chandna R, Kaczanowska K, Taylor P, Kini RM. Drysdalin, a snake neurotoxin with higher affinity for soluble acetylcholine binding protein from Aplysia californica than from Lymnaea stagnalis. Toxicon : Official Journal of the International Society On Toxinology. 187: 86-92. PMID 32889025 DOI: 10.1016/J.Toxicon.2020.08.030 |
0.52 |
|
| 2020 |
Hayes TR, Blecha JE, Chao CK, Huynh TL, VanBrocklin HD, Zinn KR, Taylor PW, Gerdes JM, Thompson CM. Positron emission tomography evaluation of oxime countermeasures in live rats using the tracer O-(2-[ F]fluoroethyl)-O-(p-nitrophenyl)methylphosphonate [ F]-VXS. Annals of the New York Academy of Sciences. PMID 32436233 DOI: 10.1111/Nyas.14363 |
0.469 |
|
| 2020 |
Camacho-Hernandez GA, Taylor P. Lessons from nature: Structural studies and drug design driven by a homologous surrogate from invertebrates, AChBP. Neuropharmacology. 108108. PMID 32353365 DOI: 10.1016/J.Neuropharm.2020.108108 |
0.534 |
|
| 2020 |
Gorecki L, Gerlits O, Kong X, Cheng X, Blumenthal DK, Taylor P, Ballatore C, Kovalevsky A, Radić Z. Rational design, synthesis and evaluation of uncharged, "smart" bis-oxime antidotes of organophosphate-inhibited human acetylcholinesterase. Journal of Biological Chemistry. 295: 6784-6784. DOI: 10.2210/Pdb6U3P/Pdb |
0.367 |
|
| 2020 |
Hernandez GAC, Schnarkowski F, Harel M, Ho K, Campeau A, Sankaran B, Gonzalez D, Fenical W, Taylor P. Targeting the Homomeric α7 Nicotinic Receptor and Acetylcholine Binding Protein with Lophotoxin by X‐ray Crystallography and Mass Spectrometry The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.05138 |
0.465 |
|
| 2019 |
Maček Hrvat N, Kalisiak J, Šinko G, Radić Z, Sharpless KB, Taylor P, Kovarik Z. Evaluation of high-affinity phenyltetrahydroisoquinoline aldoximes, linked through anti-triazoles, as reactivators of phosphylated cholinesterases. Toxicology Letters. PMID 31863869 DOI: 10.1016/J.Toxlet.2019.12.016 |
0.366 |
|
| 2019 |
Camacho-Hernandez GA, Stokes C, Duggan BM, Kaczanowska K, Brandao-Araiza S, Doan L, Papke RL, Taylor P. Synthesis, pharmacological characterization, and structure-activity relationships of non-canonical selective agonists for α7 nAChRs. Journal of Medicinal Chemistry. PMID 31675224 DOI: 10.1021/acs.jmedchem.9b01467 |
0.325 |
|
| 2019 |
Gerlits O, Ho KY, Cheng X, Blumenthal D, Taylor P, Kovalevsky A, Radić Z. A new crystal form of human acetylcholinesterase for exploratory room-temperature crystallography studies. Chemico-Biological Interactions. PMID 31176713 DOI: 10.1016/J.Cbi.2019.06.011 |
0.319 |
|
| 2019 |
Kovarik Z, Hrvat NM, Kalisiak J, Katalinić M, Sit RK, Zorbaz T, Radić Z, Fokin VV, Sharpless KB, Taylor P. Counteracting tabun inhibition by reactivation by pyridinium aldoximes that interact with active center gorge mutants of acetylcholinesterase. Toxicology and Applied Pharmacology. PMID 30978400 DOI: 10.1016/J.Taap.2019.04.007 |
0.328 |
|
| 2019 |
Gerlits O, Kong X, Cheng X, Wymore T, Blumenthal DK, Taylor P, Radić Z, Kovalevsky A. Productive reorientation of a bound oxime reactivator revealed in room-temperature X-ray structures of native and VX-inhibited human acetylcholinesterase. Journal of Biological Chemistry. 294: 10607-10618. DOI: 10.2210/Pdb6O66/Pdb |
0.395 |
|
| 2017 |
Hagstrom D, Zhang S, Ho A, Tsai ES, Radić Z, Jahromi A, Kaj KJ, He Y, Taylor P, Collins ES. Planarian cholinesterase: molecular and functional characterization of an evolutionarily ancient enzyme to study organophosphorus pesticide toxicity. Archives of Toxicology. PMID 29167930 DOI: 10.1007/S00204-017-2130-7 |
0.318 |
|
| 2017 |
Molgó J, Marchot P, Aráoz R, Benoit E, Iorga BI, Zakarian A, Taylor P, Bourne Y, Servent D. Cyclic imine toxins from dinoflagellates: a growing family of potent antagonists of the nicotinic acetylcholine receptors. Journal of Neurochemistry. PMID 28326551 DOI: 10.1111/Jnc.13995 |
0.511 |
|
| 2017 |
Kaczanowska K, Camacho Hernandez GA, Bendiks L, Kohs L, Cornejo Bravo JM, Harel M, Finn MG, Taylor P. Substituted 2-Aminopyrimidines Selective for α7-Nicotinic Acetylcholine Receptor Activation and Association with Acetylcholine Binding Proteins. Journal of the American Chemical Society. PMID 28221788 DOI: 10.1021/Jacs.6B10746 |
0.564 |
|
| 2016 |
Hagstrom D, Hirokawa H, Zhang L, Radic Z, Taylor P, Collins ES. Planarian cholinesterase: in vitro characterization of an evolutionarily ancient enzyme to study organophosphorus pesticide toxicity and reactivation. Archives of Toxicology. PMID 27990564 DOI: 10.1007/S00204-016-1908-3 |
0.321 |
|
| 2016 |
Kovalevsky A, Blumenthal DK, Cheng X, Taylor P, Radić Z. Limitations in current acetylcholinesterase structure-based design of oxime antidotes for organophosphate poisoning. Annals of the New York Academy of Sciences. PMID 27371941 DOI: 10.1111/Nyas.13128 |
0.335 |
|
| 2016 |
Bourne Y, Sharpless KB, Taylor P, Marchot P. Steric and dynamic parameters influencing in situ cycloadditions to form triazole inhibitors with crystalline acetylcholinesterase. Journal of the American Chemical Society. PMID 26731630 DOI: 10.1021/Jacs.5B11384 |
0.455 |
|
| 2016 |
Maček Hrvat N, Žunec S, Taylor P, Radić Z, Kovarik Z. HI-6 assisted catalytic scavenging of VX by acetylcholinesterase choline binding site mutants Chemico-Biological Interactions. DOI: 10.1016/J.Cbi.2016.04.023 |
0.363 |
|
| 2015 |
Wu M, Puddifoot CA, Taylor P, Joiner WJ. Mechanisms of Inhibition and Potentiation of α4β2 Nicotinic Acetylcholine Receptors by Members of the Ly6 Protein Family. The Journal of Biological Chemistry. PMID 26276394 DOI: 10.1074/Jbc.M115.647248 |
0.452 |
|
| 2015 |
Jaikhan P, Boonyarat C, Arunrungvichian K, Taylor P, Vajragupta O. Design and Synthesis of Nicotinic Acetylcholine Receptor Antagonists and their Effect on Cognitive Impairment. Chemical Biology & Drug Design. PMID 26235313 DOI: 10.1111/Cbdd.12627 |
0.463 |
|
| 2015 |
Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgó J, Taylor P, Marchot P. Marine Macrocyclic Imines, Pinnatoxins A and G: Structural Determinants and Functional Properties to Distinguish Neuronal α7 from Muscle α1(2)βγδ nAChRs. Structure (London, England : 1993). 23: 1106-15. PMID 26004441 DOI: 10.1016/J.Str.2015.04.009 |
0.512 |
|
| 2015 |
Arunrungvichian K, Boonyarat C, Fokin VV, Taylor P, Vajragupta O. Cognitive Improvements in a Mouse Model with Substituted 1,2,3-Triazole Agonists for Nicotinic Acetylcholine Receptors. Acs Chemical Neuroscience. PMID 25978789 DOI: 10.1021/Acschemneuro.5B00059 |
0.331 |
|
| 2015 |
Arunrungvichian K, Fokin VV, Vajragupta O, Taylor P. Selectivity Optimization of Substituted 1,2,3-Triazoles as α7 Nicotinic Acetylcholine Receptor Agonists. Acs Chemical Neuroscience. PMID 25932897 DOI: 10.1021/Acschemneuro.5B00058 |
0.461 |
|
| 2015 |
Bourne Y, Sulzenbacher G, Radic Z, Araoz R, Reynaud M, Benoit E, Zakarian A, Servent D, Molgo J, Taylor P, Marchot P. Marine Macrocyclic Imines, Pinnatoxins A and G: Structural Determinants and Functional Properties to Distinguish Neuronal alpha 7 from Muscle alpha 12 beta gamma delta nAChRs. Structure. 23: 1106-1115. DOI: 10.2210/Pdb4Xhe/Pdb |
0.318 |
|
| 2014 |
Kaczanowska K, Harel M, Radić Z, Changeux JP, Finn MG, Taylor P. Structural basis for cooperative interactions of substituted 2-aminopyrimidines with the acetylcholine binding protein. Proceedings of the National Academy of Sciences of the United States of America. 111: 10749-54. PMID 25006260 DOI: 10.1073/Pnas.1410992111 |
0.575 |
|
| 2014 |
Bourne Y, Sulzenbacher G, Radić Z, Aráoz R, Reynaud M, Benoit E, Talley T, Zakarian A, Taylor P, Servent D, Molgó J, Marchot P. 18. Diversity in the binding interactions of marine toxins to AChBP, the soluble nAChR surrogate Toxicon. 91: 171-172. DOI: 10.1016/J.Toxicon.2014.08.026 |
0.75 |
|
| 2013 |
Morris GM, Green LG, Radić Z, Taylor P, Sharpless KB, Olson AJ, Grynszpan F. Automated docking with protein flexibility in the design of femtomolar "click chemistry" inhibitors of acetylcholinesterase. Journal of Chemical Information and Modeling. 53: 898-906. PMID 23451944 DOI: 10.1021/Ci300545A |
0.394 |
|
| 2013 |
Rodríguez LP, Vilariño N, Molgó J, Aráoz R, Louzao MC, Taylor P, Talley T, Botana LM. Development of a solid-phase receptor-based assay for the detection of cyclic imines using a microsphere-flow cytometry system. Analytical Chemistry. 85: 2340-7. PMID 23343192 DOI: 10.1021/Ac3033432 |
0.752 |
|
| 2013 |
Taylor P, Jaco AD, Comoletti D, Miller M, Camp S. Cholinesterase confabs and cousins: approaching forty years. Chemico-Biological Interactions. 203: 10-13. PMID 23085121 DOI: 10.1016/J.Cbi.2012.10.004 |
0.309 |
|
| 2013 |
Radi? Z, Sit RK, Garcia E, Zhang L, Berend S, Kovarik Z, Amitai G, Fokin VV, Barry Sharpless K, Taylor P. Mechanism of interaction of novel uncharged, centrally active reactivators with OP-hAChE conjugates. Chemico-Biological Interactions. 203: 67-71. PMID 22975155 DOI: 10.1016/J.Cbi.2012.08.014 |
0.377 |
|
| 2013 |
Kovarik Z, Ma?ek N, Sit RK, Radi? Z, Fokin VV, Barry Sharpless K, Taylor P. Centrally acting oximes in reactivation of tabun-phosphoramidated AChE. Chemico-Biological Interactions. 203: 77-80. PMID 22960624 DOI: 10.1016/J.Cbi.2012.08.019 |
0.348 |
|
| 2012 |
De Jaco A, Dubi N, Camp S, Taylor P. Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins. The Febs Journal. 279: 4293-305. PMID 23035660 DOI: 10.1111/Febs.12019 |
0.306 |
|
| 2012 |
Yamauchi JG, Gomez K, Grimster N, Dufouil M, Nemecz A, Fotsing JR, Ho KY, Talley TT, Sharpless KB, Fokin VV, Taylor P. Synthesis of selective agonists for the α7 nicotinic acetylcholine receptor with in situ click-chemistry on acetylcholine-binding protein templates. Molecular Pharmacology. 82: 687-99. PMID 22784805 DOI: 10.1124/Mol.112.080291 |
0.773 |
|
| 2012 |
Grimster NP, Stump B, Fotsing JR, Weide T, Talley TT, Yamauchi JG, Nemecz Á, Kim C, Ho KY, Sharpless KB, Taylor P, Fokin VV. Generation of candidate ligands for nicotinic acetylcholine receptors via in situ click chemistry with a soluble acetylcholine binding protein template. Journal of the American Chemical Society. 134: 6732-40. PMID 22394239 DOI: 10.1021/Ja3001858 |
0.803 |
|
| 2012 |
Radi? Z, Sit RK, Kovarik Z, Berend S, Garcia E, Zhang L, Amitai G, Green C, Radi? B, Fokin VV, Sharpless KB, Taylor P. Refinement of structural leads for centrally acting oxime reactivators of phosphylated cholinesterases. The Journal of Biological Chemistry. 287: 11798-809. PMID 22343626 DOI: 10.1074/Jbc.M111.333732 |
0.328 |
|
| 2012 |
De Jaco A, Comoletti D, Dubi N, Camp S, Taylor P. Processing of cholinesterase-like α/β-hydrolase fold proteins: alterations associated with congenital disorders. Protein and Peptide Letters. 19: 173-9. PMID 21933121 DOI: 10.2174/092986612799080103 |
0.306 |
|
| 2011 |
Nemecz A, Taylor P. Creating an α7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: crystallographic and ligand selectivity analyses. The Journal of Biological Chemistry. 286: 42555-65. PMID 22009746 DOI: 10.1074/Jbc.M111.286583 |
0.535 |
|
| 2011 |
Kombo DC, Mazurov A, Tallapragada K, Hammond PS, Chewning J, Hauser TA, Vasquez-Valdivieso M, Yohannes D, Talley TT, Taylor P, Caldwell WS. Docking studies of benzylidene anabaseine interactions with α7 nicotinic acetylcholine receptor (nAChR) and acetylcholine binding proteins (AChBPs): application to the design of related α7 selective ligands. European Journal of Medicinal Chemistry. 46: 5625-35. PMID 21986237 DOI: 10.1016/J.Ejmech.2011.09.033 |
0.768 |
|
| 2011 |
Miller MT, Mileni M, Comoletti D, Stevens RC, Harel M, Taylor P. The crystal structure of the α-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function. Structure (London, England : 1993). 19: 767-78. PMID 21620717 DOI: 10.1016/J.Str.2011.03.011 |
0.334 |
|
| 2011 |
Sit RK, Radi? Z, Gerardi V, Zhang L, Garcia E, Katalini? M, Amitai G, Kovarik Z, Fokin VV, Sharpless KB, Taylor P. New structural scaffolds for centrally acting oxime reactivators of phosphylated cholinesterases. The Journal of Biological Chemistry. 286: 19422-30. PMID 21464125 DOI: 10.1074/Jbc.M111.230656 |
0.305 |
|
| 2011 |
Yamauchi JG, Nemecz Á, Nguyen QT, Muller A, Schroeder LF, Talley TT, Lindstrom J, Kleinfeld D, Taylor P. Characterizing ligand-gated ion channel receptors with genetically encoded Ca2++ sensors. Plos One. 6: e16519. PMID 21305050 DOI: 10.1371/Journal.Pone.0016519 |
0.712 |
|
| 2011 |
Bernard V, Girard E, Hrabovska A, Camp S, Taylor P, Plaud B, Krejci E. Distinct localization of collagen Q and PRiMA forms of acetylcholinesterase at the neuromuscular junction. Molecular and Cellular Neurosciences. 46: 272-81. PMID 20883790 DOI: 10.1016/J.Mcn.2010.09.010 |
0.33 |
|
| 2011 |
Talley TT, Nemecz A, Yamauchi JG, Wu J, Ho K, Sankaran B, Taylor P. Acetylcholine binding protein-nicotinic receptor chimeras for delineating structure and determinants of ligand selectivity Biochemical Pharmacology. 82: 1028-1029. DOI: 10.1016/J.Bcp.2011.07.018 |
0.789 |
|
| 2010 |
Bourne Y, Radić Z, Taylor P, Marchot P. Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state. Journal of the American Chemical Society. 132: 18292-300. PMID 21090615 DOI: 10.1021/Ja106820E |
0.399 |
|
| 2010 |
Comoletti D, Miller MT, Jeffries CM, Wilson J, Demeler B, Taylor P, Trewhella J, Nakagawa T. The macromolecular architecture of extracellular domain of alphaNRXN1: domain organization, flexibility, and insights into trans-synaptic disposition. Structure (London, England : 1993). 18: 1044-53. PMID 20696403 DOI: 10.1016/J.Str.2010.06.005 |
0.387 |
|
| 2010 |
Taylor P. Defining the determinants of nicotine selectivity. Proceedings of the National Academy of Sciences of the United States of America. 107: 13195-6. PMID 20643924 DOI: 10.1073/Pnas.1008043107 |
0.372 |
|
| 2010 |
De Jaco A, Lin MZ, Dubi N, Comoletti D, Miller MT, Camp S, Ellisman M, Butko MT, Tsien RY, Taylor P. Neuroligin trafficking deficiencies arising from mutations in the alpha/beta-hydrolase fold protein family. The Journal of Biological Chemistry. 285: 28674-82. PMID 20615874 DOI: 10.1074/Jbc.M110.139519 |
0.311 |
|
| 2010 |
Leone P, Comoletti D, Ferracci G, Conrod S, Garcia SU, Taylor P, Bourne Y, Marchot P. Structural insights into the exquisite selectivity of neurexin/neuroligin synaptic interactions. The Embo Journal. 29: 2461-71. PMID 20543817 DOI: 10.1038/Emboj.2010.123 |
0.416 |
|
| 2010 |
Taylor P. From Split to Sibenik: The tortuous pathway in the cholinesterase field Chemico-Biological Interactions. 187: 3-9. PMID 20493179 DOI: 10.1016/J.Cbi.2010.05.005 |
0.316 |
|
| 2010 |
Radi? Z, Kalisiak J, Fokin VV, Sharpless KB, Taylor P. Interaction kinetics of oximes with native, phosphylated and aged human acetylcholinesterase. Chemico-Biological Interactions. 187: 163-6. PMID 20412789 DOI: 10.1016/J.Cbi.2010.04.014 |
0.337 |
|
| 2010 |
Küçükkilinç T, Cochran R, Kalisiak J, Garcia E, Valle A, Amitai G, Radić Z, Taylor P. Investigating the structural influence of surface mutations on acetylcholinesterase inhibition by organophosphorus compounds and oxime reactivation. Chemico-Biological Interactions. 187: 238-240. PMID 20382137 DOI: 10.1016/J.Cbi.2010.03.050 |
0.336 |
|
| 2010 |
Wang X, Lee J, Di Jeso B, Treglia AS, Comoletti D, Dubi N, Taylor P, Arvan P. Cis and trans actions of the cholinesterase-like domain within the thyroglobulin dimer. The Journal of Biological Chemistry. 285: 17564-73. PMID 20353937 DOI: 10.1074/Jbc.M110.111641 |
0.355 |
|
| 2010 |
Jaco AD, Dubi N, Comoletti D, Taylor P. Folding anomalies of neuroligin3 caused by a mutation in the α/β-hydrolase fold domain Chemico-Biological Interactions. 187: 56-58. PMID 20227402 DOI: 10.1016/J.Cbi.2010.03.012 |
0.3 |
|
| 2010 |
Bourne Y, Radic Z, Aráoz R, Talley TT, Benoit E, Servent D, Taylor P, Molgó J, Marchot P. Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism. Proceedings of the National Academy of Sciences of the United States of America. 107: 6076-81. PMID 20224036 DOI: 10.1073/Pnas.0912372107 |
0.796 |
|
| 2010 |
Leone P, Comoletti D, Taylor P, Bourne Y, Marchot P. Structure-function relationships of the alpha/beta-hydrolase fold domain of neuroligin: a comparison with acetylcholinesterase. Chemico-Biological Interactions. 187: 49-55. PMID 20100470 DOI: 10.1016/J.Cbi.2010.01.030 |
0.371 |
|
| 2010 |
Nguyen QT, Schroeder LF, Mank M, Muller A, Taylor P, Griesbeck O, Kleinfeld D. An in vivo biosensor for neurotransmitter release and in situ receptor activity. Nature Neuroscience. 13: 127-32. PMID 20010818 DOI: 10.1038/Nn.2469 |
0.349 |
|
| 2010 |
Sine SM, Wang HL, Hansen S, Taylor P. On the origin of ion selectivity in the Cys-loop receptor family. Journal of Molecular Neuroscience : Mn. 40: 70-6. PMID 19728176 DOI: 10.1007/S12031-009-9260-1 |
0.732 |
|
| 2010 |
Srivastava S, Hamouda AK, Talley TT, Pandhare A, Duddempudi PK, Hsiao H, Taylor P, Cohen JB, Blanton MP. Photoaffinity Labeling the Agonist Binding Sites of Torpedo and α4β2 Nicotinic Acetylcholine Receptors and Acetylcholine Binding Proteins (AChBPs) with [3H]Cytisine Biophysical Journal. 98: 130a-131a. DOI: 10.1016/J.Bpj.2009.12.706 |
0.778 |
|
| 2009 |
de Wit J, Sylwestrak E, O'Sullivan ML, Otto S, Tiglio K, Savas JN, Yates JR, Comoletti D, Taylor P, Ghosh A. LRRTM2 interacts with Neurexin1 and regulates excitatory synapse formation. Neuron. 64: 799-806. PMID 20064388 DOI: 10.1016/J.Neuron.2009.12.019 |
0.325 |
|
| 2009 |
Luo J, Taylor P, Losen M, de Baets MH, Shelton GD, Lindstrom J. Main immunogenic region structure promotes binding of conformation-dependent myasthenia gravis autoantibodies, nicotinic acetylcholine receptor conformation maturation, and agonist sensitivity. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 29: 13898-908. PMID 19890000 DOI: 10.1523/Jneurosci.2833-09.2009 |
0.384 |
|
| 2009 |
Utsintong M, Talley TT, Taylor PW, Olson AJ, Vajragupta O. Virtual screening against alpha-cobratoxin. Journal of Biomolecular Screening. 14: 1109-18. PMID 19734437 DOI: 10.1177/1087057109344617 |
0.784 |
|
| 2009 |
Hibbs RE, Sulzenbacher G, Shi J, Talley TT, Conrod S, Kem WR, Taylor P, Marchot P, Bourne Y. Structural determinants for interaction of partial agonists with acetylcholine binding protein and neuronal alpha7 nicotinic acetylcholine receptor. The Embo Journal. 28: 3040-51. PMID 19696737 DOI: 10.1038/Emboj.2009.227 |
0.85 |
|
| 2009 |
Rana BK, Wessel J, Mahboubi V, Rao F, Haeller J, Gayen JR, Eskin E, Valle AM, Das M, Mahata SK, Taupenot L, Stridsberg M, Talley TT, Ziegler MG, Smith DW, ... Taylor P, et al. Natural variation within the neuronal nicotinic acetylcholine receptor cluster on human chromosome 15q24: influence on heritable autonomic traits in twin pairs. The Journal of Pharmacology and Experimental Therapeutics. 331: 419-28. PMID 19671882 DOI: 10.1124/Jpet.109.157271 |
0.727 |
|
| 2009 |
Tomizawa M, Talley TT, Park JF, Maltby D, Medzihradszky KF, Durkin KA, Cornejo-Bravo JM, Burlingame AL, Casida JE, Taylor P. Nicotinic agonist binding site mapped by methionine- and tyrosine-scanning coupled with azidochloropyridinyl photoaffinity labeling. Journal of Medicinal Chemistry. 52: 3735-41. PMID 19459645 DOI: 10.1021/Jm900153C |
0.788 |
|
| 2009 |
Dobbertin A, Hrabovska A, Dembele K, Camp S, Taylor P, Krejci E, Bernard V. 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 The Journal of Neuroscience. 29: 4519-4530. PMID 19357277 DOI: 10.1523/Jneurosci.3863-08.2009 |
0.331 |
|
| 2009 |
Babakhani A, Talley TT, Taylor P, McCammon JA. A virtual screening study of the acetylcholine binding protein using a relaxed-complex approach. Computational Biology and Chemistry. 33: 160-70. PMID 19186108 DOI: 10.1016/J.Compbiolchem.2008.12.002 |
0.773 |
|
| 2008 |
Hansen SB, Wang HL, Taylor P, Sine SM. An ion selectivity filter in the extracellular domain of Cys-loop receptors reveals determinants for ion conductance. The Journal of Biological Chemistry. 283: 36066-70. PMID 18940802 DOI: 10.1074/Jbc.C800194200 |
0.723 |
|
| 2008 |
Radi? Z, Manetsch R, Fournier D, Sharpless KB, Taylor P. Probing gorge dimensions of cholinesterases by freeze-frame click chemistry. Chemico-Biological Interactions. 175: 161-5. PMID 18555981 DOI: 10.1016/J.Cbi.2008.04.048 |
0.411 |
|
| 2008 |
De Jaco A, Comoletti D, King CC, Taylor P. Trafficking of cholinesterases and neuroligins mutant proteins. An association with autism Chemico-Biological Interactions. 175: 349-351. PMID 18555979 DOI: 10.1016/J.Cbi.2008.04.023 |
0.303 |
|
| 2008 |
Comoletti D, Grishaev A, Whitten AE, Taylor P, Trewhella J. Characterization of the solution structure of a neuroligin/beta-neurexin complex. Chemico-Biological Interactions. 175: 150-5. PMID 18550038 DOI: 10.1016/J.Cbi.2008.04.040 |
0.339 |
|
| 2008 |
Talley TT, Harel M, Hibbs RE, Radic Z, Tomizawa M, Casida JE, Taylor P. Atomic interactions of neonicotinoid agonists with AChBP: molecular recognition of the distinctive electronegative pharmacophore. Proceedings of the National Academy of Sciences of the United States of America. 105: 7606-11. PMID 18477694 DOI: 10.1073/Pnas.0802197105 |
0.858 |
|
| 2008 |
Wang HL, Cheng X, Taylor P, McCammon JA, Sine SM. Control of cation permeation through the nicotinic receptor channel. Plos Computational Biology. 4: e41. PMID 18282090 DOI: 10.1371/Journal.Pcbi.0040041 |
0.571 |
|
| 2008 |
Tomizawa M, Maltby D, Talley TT, Durkin KA, Medzihradszky KF, Burlingame AL, Taylor P, Casida JE. Atypical nicotinic agonist bound conformations conferring subtype selectivity. Proceedings of the National Academy of Sciences of the United States of America. 105: 1728-32. PMID 18230720 DOI: 10.1073/Pnas.0711724105 |
0.771 |
|
| 2007 |
Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron. 56: 979-91. PMID 18093521 DOI: 10.1016/J.Neuron.2007.11.013 |
0.355 |
|
| 2007 |
Taylor P, Talley TT, Radic' Z, Hansen SB, Hibbs RE, Shi J. Structure-guided drug design: conferring selectivity among neuronal nicotinic receptor and acetylcholine-binding protein subtypes. Biochemical Pharmacology. 74: 1164-71. PMID 17826748 DOI: 10.1016/J.Bcp.2007.07.038 |
0.842 |
|
| 2007 |
Tomizawa M, Maltby D, Medzihradszky KF, Zhang N, Durkin KA, Presley J, Talley TT, Taylor P, Burlingame AL, Casida JE. Defining nicotinic agonist binding surfaces through photoaffinity labeling. Biochemistry. 46: 8798-806. PMID 17614369 DOI: 10.1021/Bi700667V |
0.803 |
|
| 2007 |
Comoletti D, Grishaev A, Whitten AE, Tsigelny I, Taylor P, Trewhella J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure (London, England : 1993). 15: 693-705. PMID 17562316 DOI: 10.1016/J.Str.2007.04.010 |
0.311 |
|
| 2007 |
Tomizawa M, Talley TT, Maltby D, Durkin KA, Medzihradszky KF, Burlingame AL, Taylor P, Casida JE. Mapping the elusive neonicotinoid binding site. Proceedings of the National Academy of Sciences of the United States of America. 104: 9075-80. PMID 17485662 DOI: 10.1073/Pnas.0703309104 |
0.798 |
|
| 2007 |
Hansen SB, Taylor P. Galanthamine and non-competitive inhibitor binding to ACh-binding protein: evidence for a binding site on non-alpha-subunit interfaces of heteromeric neuronal nicotinic receptors. Journal of Molecular Biology. 369: 895-901. PMID 17481657 DOI: 10.1016/J.Jmb.2007.03.067 |
0.723 |
|
| 2007 |
Kang TS, Radi? Z, Talley TT, Jois SD, Taylor P, Kini RM. Protein folding determinants: structural features determining alternative disulfide pairing in alpha- and chi/lambda-conotoxins. Biochemistry. 46: 3338-55. PMID 17315952 DOI: 10.1021/Bi061969O |
0.736 |
|
| 2006 |
Bourne Y, Hansen SB, Sulzenbacher G, Talley TT, Huxford T, Taylor P, Marchot P. Structural comparison of three crystalline complexes of a peptidic toxin with a synaptic acetylcholine recognition protein. Journal of Molecular Neuroscience : Mn. 30: 103-4. PMID 17192648 DOI: 10.1385/Jmn:30:1:103 |
0.78 |
|
| 2006 |
Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Bourne Y, Taylor P. Structural characterization of agonist and antagonist-bound acetylcholine-binding protein from Aplysia californica. Journal of Molecular Neuroscience : Mn. 30: 101-2. PMID 17192647 DOI: 10.1385/Jmn:30:1:101 |
0.704 |
|
| 2006 |
Girard E, Bernard V, Camp S, Taylor P, Krejci E, Molgó J. Remodeling of the neuromuscular junction in mice with deleted exons 5 and 6 of acetylcholinesterase. Journal of Molecular Neuroscience : Mn. 30: 99-100. PMID 17192646 DOI: 10.1385/Jmn:30:1:99 |
0.34 |
|
| 2006 |
Hibbs RE, Johnson DA, Shi J, Taylor P. Structural dynamics of the acetylcholine binding protein: hydrodynamic and fluorescence anisotropy decay analyses. Journal of Molecular Neuroscience : Mn. 30: 73-4. PMID 17192634 DOI: 10.1385/Jmn:30:1:73 |
0.786 |
|
| 2006 |
Hibbs RE, Radic Z, Taylor P, Johnson DA. Influence of agonists and antagonists on the segmental motion of residues near the agonist binding pocket of the acetylcholine-binding protein. The Journal of Biological Chemistry. 281: 39708-18. PMID 17068341 DOI: 10.1074/Jbc.M604752200 |
0.763 |
|
| 2006 |
Comoletti D, Flynn RE, Boucard AA, Demeler B, Schirf V, Shi J, Jennings LL, Newlin HR, Südhof TC, Taylor P. Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Biochemistry. 45: 12816-27. PMID 17042500 DOI: 10.1021/Bi0614131 |
0.302 |
|
| 2006 |
Gao F, Mer G, Tonelli M, Hansen SB, Burghardt TP, Taylor P, Sine SM. Solution NMR of acetylcholine binding protein reveals agonist-mediated conformational change of the C-loop. Molecular Pharmacology. 70: 1230-5. PMID 16847142 DOI: 10.1124/Mol.106.027185 |
0.747 |
|
| 2006 |
Talley TT, Yalda S, Ho KY, Tor Y, Soti FS, Kem WR, Taylor P. Spectroscopic analysis of benzylidene anabaseine complexes with acetylcholine binding proteins as models for ligand-nicotinic receptor interactions. Biochemistry. 45: 8894-902. PMID 16846232 DOI: 10.1021/Bi060534Y |
0.784 |
|
| 2006 |
Bourne Y, Radic Z, Sulzenbacher G, Kim E, Taylor P, Marchot P. Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding. The Journal of Biological Chemistry. 281: 29256-67. PMID 16837465 DOI: 10.1074/Jbc.M603018200 |
0.426 |
|
| 2006 |
Talley TT, Olivera BM, Han KH, Christensen SB, Dowell C, Tsigelny I, Ho KY, Taylor P, McIntosh JM. Alpha-conotoxin OmIA is a potent ligand for the acetylcholine-binding protein as well as alpha3beta2 and alpha7 nicotinic acetylcholine receptors. The Journal of Biological Chemistry. 281: 24678-86. PMID 16803900 DOI: 10.1074/Jbc.M602969200 |
0.772 |
|
| 2006 |
Kovarik Z, Ciban N, Radić Z, Simeon-Rudolf V, Taylor P. Active site mutant acetylcholinesterase interactions with 2-PAM, HI-6, and DDVP. Biochemical and Biophysical Research Communications. 342: 973-978. PMID 16598855 DOI: 10.1016/J.Bbrc.2006.02.056 |
0.363 |
|
| 2006 |
Shi J, Koeppe JR, Komives EA, Taylor P. Ligand-induced conformational changes in the acetylcholine-binding protein analyzed by hydrogen-deuterium exchange mass spectrometry. The Journal of Biological Chemistry. 281: 12170-7. PMID 16484218 DOI: 10.1074/Jbc.M600154200 |
0.498 |
|
| 2006 |
Bui JM, Radic Z, Taylor P, McCammon JA. Conformational transitions in protein-protein association: binding of fasciculin-2 to acetylcholinesterase. Biophysical Journal. 90: 3280-7. PMID 16473897 DOI: 10.1529/Biophysj.105.075564 |
0.436 |
|
| 2006 |
De Jaco A, Comoletti D, Kovarik Z, Gaietta G, Radic Z, Lockridge O, Ellisman MH, Taylor P. A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family. The Journal of Biological Chemistry. 281: 9667-76. PMID 16434405 DOI: 10.1074/Jbc.M510262200 |
0.323 |
|
| 2006 |
Radić Z, Talley TT, Hansen SB, Yu W, Taylor P. Interaction of organophosphate and carbamate cholinesterase inhibitors with acetylcholine binding proteins Toxicology Letters. 164: S239. DOI: 10.1016/J.Toxlet.2006.07.157 |
0.781 |
|
| 2005 |
Pezzementi L, Shi J, Johnson DA, Radic Z, Boyd A, Taylor P. Ligand-induced conformational changes in residues flanking the active site gorge of acetylcholinesterase. Chemico-Biological Interactions. 413-414. PMID 16429560 DOI: 10.1016/J.Cbi.2005.10.082 |
0.383 |
|
| 2005 |
Kovarik Z, Radić Z, Simeon-Rudolf V, Reiner E, Taylor P. Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates. Chemico-Biological Interactions. 157: 388-390. PMID 16429526 DOI: 10.1016/J.Cbi.2005.10.069 |
0.32 |
|
| 2005 |
De Jaco A, Kovarik Z, Comoletti D, Jennings LL, Gaietta G, Ellisman MH, Taylor P. A single mutation near the C-terminus in alpha/beta hydrolase fold protein family causes a defect in protein processing. Chemico-Biological Interactions. 157: 371-2. PMID 16429495 DOI: 10.1016/J.Cbi.2005.10.057 |
0.313 |
|
| 2005 |
Hibbs RE, Johnson DA, Shi J, Hansen SB, Taylor P. Structural dynamics of the alpha-neurotoxin-acetylcholine-binding protein complex: hydrodynamic and fluorescence anisotropy decay analyses. Biochemistry. 44: 16602-11. PMID 16342951 DOI: 10.1021/Bi051735P |
0.79 |
|
| 2005 |
Radi? Z, Manetsch R, Krasi?ski A, Raushel J, Yamauchi J, Garcia C, Kolb H, Sharpless KB, Taylor P. Molecular basis of interactions of cholinesterases with tight binding inhibitors. Chemico-Biological Interactions. 157: 133-41. PMID 16289416 DOI: 10.1016/J.Cbi.2005.10.020 |
0.455 |
|
| 2005 |
Bourne Y, Radi? Z, Kolb HC, Sharpless KB, Taylor P, Marchot P. Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE. Chemico-Biological Interactions. 157: 159-65. PMID 16259971 DOI: 10.1016/J.Cbi.2005.10.018 |
0.456 |
|
| 2005 |
Boucard AA, Chubykin AA, Comoletti D, Taylor P, Südhof TC. A splice code for trans-synaptic cell adhesion mediated by binding of neuroligin 1 to alpha- and beta-neurexins. Neuron. 48: 229-36. PMID 16242404 DOI: 10.1016/J.Neuron.2005.08.026 |
0.398 |
|
| 2005 |
Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y. Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations. The Embo Journal. 24: 3635-46. PMID 16193063 DOI: 10.1038/Sj.Emboj.7600828 |
0.726 |
|
| 2005 |
Krasi?ski A, Radi? Z, Manetsch R, Raushel J, Taylor P, Sharpless KB, Kolb HC. In situ selection of lead compounds by click chemistry: target-guided optimization of acetylcholinesterase inhibitors. Journal of the American Chemical Society. 127: 6686-92. PMID 15869290 DOI: 10.1021/Ja043031T |
0.376 |
|
| 2005 |
Bourne Y, Talley TT, Hansen SB, Taylor P, Marchot P. Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors. The Embo Journal. 24: 1512-22. PMID 15791209 DOI: 10.1038/Sj.Emboj.7600620 |
0.828 |
|
| 2005 |
Henchman RH, Wang HL, Sine SM, Taylor P, McCammon JA. Ligand-induced conformational change in the alpha7 nicotinic receptor ligand binding domain. Biophysical Journal. 88: 2564-76. PMID 15665135 DOI: 10.1529/Biophysj.104.053934 |
0.697 |
|
| 2005 |
Zhang D, Suen J, Zhang Y, Song Y, Radic Z, Taylor P, Holst MJ, Bajaj C, Baker NA, McCammon JA. Tetrameric mouse acetylcholinesterase: continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods. Biophysical Journal. 88: 1659-65. PMID 15626705 DOI: 10.1529/Biophysj.104.053850 |
0.312 |
|
| 2005 |
Gao F, Bren N, Burghardt TP, Hansen S, Henchman RH, Taylor P, McCammon JA, Sine SM. Agonist-mediated conformational changes in acetylcholine-binding protein revealed by simulation and intrinsic tryptophan fluorescence. The Journal of Biological Chemistry. 280: 8443-51. PMID 15591050 DOI: 10.1074/Jbc.M412389200 |
0.767 |
|
| 2004 |
Khan IM, Wennerholm M, Singletary E, Polston K, Zhang L, Deerinck T, Yaksh TL, Taylor P. Ablation of primary afferent terminals reduces nicotinic receptor expression and the nociceptive responses to nicotinic agonists in the spinal cord. Journal of Neurocytology. 33: 543-56. PMID 15906161 DOI: 10.1007/S11068-004-0516-6 |
0.449 |
|
| 2004 |
Manetsch R, Krasi?ski A, Radi? Z, Raushel J, Taylor P, Sharpless KB, Kolb HC. In situ click chemistry: enzyme inhibitors made to their own specifications. Journal of the American Chemical Society. 126: 12809-18. PMID 15469276 DOI: 10.1021/Ja046382G |
0.309 |
|
| 2004 |
Bouzat C, Gumilar F, Spitzmaul G, Wang HL, Rayes D, Hansen SB, Taylor P, Sine SM. Coupling of agonist binding to channel gating in an ACh-binding protein linked to an ion channel. Nature. 430: 896-900. PMID 15318223 DOI: 10.1038/Nature02753 |
0.758 |
|
| 2004 |
Hibbs RE, Talley TT, Taylor P. Acrylodan-conjugated cysteine side chains reveal conformational state and ligand site locations of the acetylcholine-binding protein. The Journal of Biological Chemistry. 279: 28483-91. PMID 15117947 DOI: 10.1074/Jbc.M403713200 |
0.843 |
|
| 2004 |
Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor P, Johnson DA. Nanosecond dynamics of acetylcholinesterase near the active center gorge. The Journal of Biological Chemistry. 279: 26612-8. PMID 15078872 DOI: 10.1074/Jbc.M401482200 |
0.395 |
|
| 2004 |
Hansen SB, Talley TT, Radic Z, Taylor P. Structural and ligand recognition characteristics of an acetylcholine-binding protein from Aplysia californica. The Journal of Biological Chemistry. 279: 24197-202. PMID 15069068 DOI: 10.1074/Jbc.M402452200 |
0.813 |
|
| 2004 |
Taylor P, Hansen SB, Talley TT, Hibbs RE, Radi? Z. Contemporary paradigms for cholinergic ligand design guided by biological structure. Bioorganic & Medicinal Chemistry Letters. 14: 1875-7. PMID 15050619 DOI: 10.1016/J.Bmcl.2003.10.072 |
0.82 |
|
| 2004 |
Kovarik Z, Radić Z, Berman HA, Simeon-Rudolf V, Reiner E, Taylor P. Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates. Biochemistry. 43: 3222-3229. PMID 15023072 DOI: 10.1021/Bi036191A |
0.342 |
|
| 2004 |
Hoffman RC, Jennings LL, Tsigelny I, Comoletti D, Flynn RE, Sudhof TC, Taylor P. Structural characterization of recombinant soluble rat neuroligin 1: mapping of secondary structure and glycosylation by mass spectrometry. Biochemistry. 43: 1496-506. PMID 14769026 DOI: 10.1021/Bi035278T |
0.356 |
|
| 2004 |
Bourne Y, Kolb HC, Radi? Z, Sharpless KB, Taylor P, Marchot P. Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation. Proceedings of the National Academy of Sciences of the United States of America. 101: 1449-54. PMID 14757816 DOI: 10.1073/Pnas.0308206100 |
0.401 |
|
| 2004 |
Saxena A, Fedorko JM, Vinayaka CR, Medhekar R, Radić Z, Taylor P, Lockridge O, Doctor BP. Aromatic amino-acid residues at the active and peripheral anionic sites control the binding of E2020 (Aricept) to cholinesterases. European Journal of Biochemistry. 270: 4447-58. PMID 14622273 DOI: 10.1046/J.1432-1033.2003.03837.X |
0.419 |
|
| 2003 |
Henchman RH, Wang HL, Sine SM, Taylor P, McCammon JA. Asymmetric structural motions of the homomeric alpha7 nicotinic receptor ligand binding domain revealed by molecular dynamics simulation. Biophysical Journal. 85: 3007-18. PMID 14581202 DOI: 10.1016/S0006-3495(03)74720-1 |
0.718 |
|
| 2003 |
Khan I, Osaka H, Stanislaus S, Calvo RM, Deerinck T, Yaksh TL, Taylor P. Nicotinic acetylcholine receptor distribution in relation to spinal neurotransmission pathways. The Journal of Comparative Neurology. 467: 44-59. PMID 14574679 DOI: 10.1002/Cne.10913 |
0.395 |
|
| 2003 |
George KM, Schule T, Sandoval LE, Jennings LL, Taylor P, Thompson CM. Differentiation between acetylcholinesterase and the organophosphate-inhibited form using antibodies and the correlation of antibody recognition with reactivation mechanism and rate. The Journal of Biological Chemistry. 278: 45512-8. PMID 12933813 DOI: 10.1074/Jbc.M304781200 |
0.522 |
|
| 2003 |
Shi J, Tai K, McCammon JA, Taylor P, Johnson DA. Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop. The Journal of Biological Chemistry. 278: 30905-11. PMID 12759360 DOI: 10.1074/Jbc.M303730200 |
0.417 |
|
| 2003 |
Gao F, Bern N, Little A, Wang HL, Hansen SB, Talley TT, Taylor P, Sine SM. Curariform antagonists bind in different orientations to acetylcholine-binding protein. The Journal of Biological Chemistry. 278: 23020-6. PMID 12682067 DOI: 10.1074/Jbc.M301151200 |
0.839 |
|
| 2003 |
Kovarik Z, Radić Z, Berman HA, Simeon-Rudolf V, Reiner E, Taylor P. Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates. Biochemical Journal. 373: 33-40. PMID 12665427 DOI: 10.1042/Bj20021862 |
0.331 |
|
| 2003 |
Bourne Y, Taylor P, Radić Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. The Embo Journal. 22: 1-12. PMID 12505979 DOI: 10.1093/Emboj/Cdg005 |
0.434 |
|
| 2002 |
Khan IM, Singletary E, Alemayehu A, Stanislaus S, Printz MP, Yaksh TL, Taylor P. Nicotinic receptor gene cluster on rat chromosome 8 in nociceptive and blood pressure hyperresponsiveness. Physiological Genomics. 11: 65-72. PMID 12388796 DOI: 10.1152/Physiolgenomics.00079.2002 |
0.333 |
|
| 2002 |
Hansen SB, Radic' Z, Talley TT, Molles BE, Deerinck T, Tsigelny I, Taylor P. Tryptophan fluorescence reveals conformational changes in the acetylcholine binding protein. The Journal of Biological Chemistry. 277: 41299-302. PMID 12235129 DOI: 10.1074/Jbc.C200462200 |
0.836 |
|
| 2002 |
Shi J, Radić Z, Taylor P. Inhibitors of Different Structure Induce Distinguishing Conformations in the Omega Loop, Cys69–Cys96, of Mouse Acetylcholinesterase Journal of Biological Chemistry. 277: 43301-43308. PMID 12196517 DOI: 10.1074/Jbc.M204391200 |
0.409 |
|
| 2002 |
Molles BE, Tsigelny I, Nguyen PD, Gao SX, Sine SM, Taylor P. Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site. Biochemistry. 41: 7895-906. PMID 12069578 DOI: 10.1021/Bi025732D |
0.7 |
|
| 2002 |
Molles BE, Rezai P, Kline EF, McArdle JJ, Sine SM, Taylor P. Identification of residues at the alpha and epsilon subunit interfaces mediating species selectivity of Waglerin-1 for nicotinic acetylcholine receptors. The Journal of Biological Chemistry. 277: 5433-40. PMID 11724791 DOI: 10.1074/Jbc.M109232200 |
0.695 |
|
| 2002 |
Molles BE, Taylor P. Structure And Function Of The Waglerins, Peptide Toxins From The Venom Of Wagler'S Pit Viper, Tropidolaemus Wagleri Journal of Toxicology-Toxin Reviews. 21: 273-292. DOI: 10.1081/Txr-120014406 |
0.477 |
|
| 2001 |
Radić Z, Taylor P. Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphates. Journal of Applied Toxicology. 21. PMID 11920914 DOI: 10.1002/Jat.790 |
0.403 |
|
| 2001 |
Shi J, Boyd AE, Radic Z, Taylor P. Reversibly Bound and Covalently Attached Ligands Induce Conformational Changes in the Omega Loop, Cys69-Cys96, of Mouse Acetylcholinesterase Journal of Biological Chemistry. 276: 42196-42204. PMID 11517229 DOI: 10.1074/Jbc.M106896200 |
0.482 |
|
| 2001 |
Keller SH, Lindstrom J, Ellisman M, Taylor P. Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor alpha-Subunit. The Journal of Biological Chemistry. 276: 18384-91. PMID 11279119 DOI: 10.1074/Jbc.M100691200 |
0.385 |
|
| 2001 |
Radić Z, Taylor P. Interaction Kinetics of Reversible Inhibitors and Substrates with Acetylcholinesterase and Its Fasciculin 2 Complex Journal of Biological Chemistry. 276: 4622-4633. PMID 11036076 DOI: 10.1074/Jbc.M006855200 |
0.382 |
|
| 2000 |
Taylor P, Malany S, Molles BE, Osaka H, Tsigelny I. Subunit interface selective toxins as probes of nicotinic acetylcholine receptor structure. Pflugers Archiv : European Journal of Physiology. 440: R115-R117. PMID 28008504 DOI: 10.1007/S004240000028 |
0.518 |
|
| 2000 |
Malany S, Osaka H, Sine SM, Taylor P. Orientation of alpha-neurotoxin at the subunit interfaces of the nicotinic acetylcholine receptor. Biochemistry. 39: 15388-98. PMID 11112524 DOI: 10.1021/Bi001825O |
0.631 |
|
| 2000 |
Taylor P, Malanz S, Molles BE, Osaka H, Tsigelny I. Subunit interface selective toxins as probes of nicotinic acetylcholine receptor structure. Pflugers Archiv : European Journal of Physiology. 440: R115-7. PMID 11005635 |
0.438 |
|
| 2000 |
Saltmarsh JR, Boyd AE, Rodriguez OP, Radić Z, Taylor P, Thompson CM. Synthesis of fluorescent probes directed to the active site gorge of acetylcholinesterase. Bioorganic & Medicinal Chemistry Letters. 10: 1523-6. PMID 10915041 DOI: 10.1016/S0960-894X(00)00275-4 |
0.499 |
|
| 2000 |
Boyd AE, Marnett AB, Wong L, Taylor P. Probing the active center gorge of acetylcholinesterase by fluorophores linked to substituted cysteines. The Journal of Biological Chemistry. 275: 22401-8. PMID 10779503 DOI: 10.1074/Jbc.M000606200 |
0.406 |
|
| 2000 |
Tsigelny I, Shindyalov IN, Bourne PE, Südhof TC, Taylor P. Common EF-hand motifs in cholinesterases and neuroligins suggest a role for Ca2+ binding in cell surface associations. Protein Science : a Publication of the Protein Society. 9: 180-5. PMID 10739260 DOI: 10.1110/Ps.9.1.180 |
0.414 |
|
| 2000 |
Osaka H, Malany S, Molles BE, Sine SM, Taylor P. Pairwise electrostatic interactions between alpha-neurotoxins and gamma, delta, and epsilon subunits of the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 275: 5478-84. PMID 10681526 DOI: 10.1074/Jbc.275.8.5478 |
0.65 |
|
| 2000 |
Quinn DM, Feaster SR, Nair HK, Baker NA, Radi? Z, Taylor P. Delineation and decomposition of energies involved in quaternary ammonium binding in the active site of acetylcholinesterase Journal of the American Chemical Society. 122: 2975-2980. DOI: 10.1021/Ja9933588 |
0.355 |
|
| 1999 |
Luo C, Saxena A, Smith M, Garcia G, Radić Z, Taylor P, Doctor BP. Phosphoryl oxime inhibition of acetylcholinesterase during oxime reactivation is prevented by edrophonium. Biochemistry. 38: 9937-9947. PMID 10433700 DOI: 10.1021/Bi9905720 |
0.312 |
|
| 1999 |
Radić Z, Taylor P. The influence of peripheral site ligands on the reaction of symmetric and chiral organophosphates with wildtype and mutant acetylcholinesterases Chemico-Biological Interactions. 119: 111-117. PMID 10421444 DOI: 10.1016/S0009-2797(99)00019-8 |
0.367 |
|
| 1999 |
Taylor P, Wong L, Radić Z, Tsigelny I, Brüggemann R, Hosea NA, Berman HA. Analysis of cholinesterase inactivation and reactivation by systematic structural modification and enantiomeric selectivity Chemico-Biological Interactions. 119: 3-5. PMID 10421434 DOI: 10.1016/S0009-2797(99)00009-5 |
0.311 |
|
| 1999 |
Osaka H, Malany S, Kanter JR, Sine SM, Taylor P. Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 274: 9581-6. PMID 10092644 DOI: 10.1074/Jbc.274.14.9581 |
0.712 |
|
| 1999 |
Keller SH, Taylor P. Determinants responsible for assembly of the nicotinic acetylcholine receptor. The Journal of General Physiology. 113: 171-6. PMID 9925816 DOI: 10.1085/Jgp.113.2.171 |
0.401 |
|
| 1999 |
Bourne Y, Taylor P, Bougis PE, Marchot P. Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. The Journal of Biological Chemistry. 274: 2963-70. PMID 9915834 DOI: 10.1074/Jbc.274.5.2963 |
0.424 |
|
| 1998 |
Khan IM, Buerkle H, Taylor P, Yaksh TL. Nociceptive and antinociceptive responses to intrathecally administered nicotinic agonists. Neuropharmacology. 37: 1515-25. PMID 9886674 DOI: 10.1016/S0028-3908(98)00143-9 |
0.381 |
|
| 1998 |
Tara S, Elcock AH, Kirchhoff PD, Briggs JM, Radic Z, Taylor P, McCammon JA. Rapid binding of a cationic active site inhibitor to wild type and mutant mouse acetylcholinesterase: Brownian dynamics simulation including diffusion in the active site gorge. Biopolymers. 46: 465-74. PMID 9838872 DOI: 10.1002/(Sici)1097-0282(199812)46:7<465::Aid-Bip4>3.0.Co;2-Y |
0.393 |
|
| 1998 |
Marchot P, Bourne Y, Prowse CN, Bougis PE, Taylor P. Inhibition of mouse acetylcholinesterase by fasciculin: crystal structure of the complex and mutagenesis of fasciculin. Toxicon : Official Journal of the International Society On Toxinology. 36: 1613-22. PMID 9792178 DOI: 10.1016/S0041-0101(98)00154-8 |
0.483 |
|
| 1998 |
Taylor P, Osaka H, Molles BE, Sugiyama N, Marchot P, Ackermann EJ, Malany S, McArdle JJ, Sine SM, Tsigelny I. Toxins selective for subunit interfaces as probes of nicotinic acetylcholine receptor structure. Journal of Physiology, Paris. 92: 79-83. PMID 9782448 DOI: 10.1016/S0928-4257(98)80142-3 |
0.648 |
|
| 1998 |
Taylor P. Development of acetylcholinesterase inhibitors in the therapy of Alzheimer's disease Neurology. 51. PMID 9674760 DOI: 10.1212/Wnl.51.1_Suppl_1.S30 |
0.312 |
|
| 1998 |
Keller SH, Lindstrom J, Taylor P. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the alpha-subunit of the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 273: 17064-72. PMID 9642271 DOI: 10.1074/Jbc.273.27.17064 |
0.438 |
|
| 1998 |
Osaka H, Sugiyama N, Taylor P. Distinctions in agonist and antagonist specificity conferred by anionic residues of the nicotinic acetylcholine receptor Journal of Biological Chemistry. 273: 12758-12765. PMID 9582301 DOI: 10.1074/Jbc.273.21.12758 |
0.547 |
|
| 1998 |
Ackermann EJ, Ang ET, Kanter JR, Tsigelny I, Taylor P. Identification of pairwise interactions in the alpha-neurotoxin-nicotinic acetylcholine receptor complex through double mutant cycles. The Journal of Biological Chemistry. 273: 10958-64. PMID 9556574 DOI: 10.1074/Jbc.273.18.10958 |
0.545 |
|
| 1998 |
Sugiyama N, Marchot P, Kawanishi C, Osaka H, Molles B, Sine SM, Taylor P. Residues at the subunit interfaces of the nicotinic acetylcholine receptor that contribute to alpha-conotoxin M1 binding. Molecular Pharmacology. 53: 787-94. PMID 9547372 DOI: 10.1124/Mol.53.4.787 |
0.638 |
|
| 1998 |
Osaka H, Ackerman EJ, Kanter J, Tsigelny I, Sine SM, Taylor P. 80Binding orientation of the α-neurotoxins with the nicotinic acetylcholine receptor Journal of Physiology-Paris. 92: 476-477. DOI: 10.1016/S0928-4257(99)80092-8 |
0.674 |
|
| 1998 |
Molles B, Kline E, Sine S, McArdle J, Taylor P. 74Probing the structure of the ligand binding site on the muscle nicotinic receptor with Waglerin peptides Journal of Physiology-Paris. 92: 470-471. DOI: 10.1016/S0928-4257(99)80086-2 |
0.681 |
|
| 1998 |
Marchot P, Taylor P, Kanter J, Bougis P, Bourne Y. Tetrameric assembly and peripheral site-occluding loop of mouse acetylcholinesterase Journal of Physiology-Paris. 92: 465. DOI: 10.1016/S0928-4257(99)80081-3 |
0.311 |
|
| 1998 |
Malany S, Ackermann E, Osaka H, Taylor P. Complementary binding studies between α-neurotoxin and the nicotinic acetylcholine receptor Journal of Physiology-Paris. 92: 462-463. DOI: 10.1016/S0928-4257(99)80079-5 |
0.485 |
|
| 1998 |
Keller SH, Taylor P. Mechanisms regulating expression of nicotinic acetylcholine receptor subunits Journal of Physiology-Paris. 92: 446-447. DOI: 10.1016/S0928-4257(99)80062-X |
0.41 |
|
| 1997 |
Ackermann EJ, Taylor P. Nonidentity of the alpha-neurotoxin binding sites on the nicotinic acetylcholine receptor revealed by modification in alpha-neurotoxin and receptor structures. Biochemistry. 36: 12836-44. PMID 9335541 DOI: 10.1021/Bi971513U |
0.561 |
|
| 1997 |
Radi? Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P. Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin. The Journal of Biological Chemistry. 272: 23265-77. PMID 9287336 DOI: 10.1074/Jbc.272.37.23265 |
0.386 |
|
| 1997 |
Saxena A, Maxwell DM, Quinn DM, Radi? Z, Taylor P, Doctor BP. Mutant acetylcholinesterases as potential detoxification agents for organophosphate poisoning. Biochemical Pharmacology. 54: 269-74. PMID 9271331 DOI: 10.1016/S0006-2952(97)00180-9 |
0.32 |
|
| 1997 |
Tsigelny I, Sugiyama N, Sine SM, Taylor P. A model of the nicotinic receptor extracellular domain based on sequence identity and residue location. Biophysical Journal. 73: 52-66. PMID 9199771 DOI: 10.1016/S0006-3495(97)78047-0 |
0.716 |
|
| 1997 |
Khan IM, Yaksh TL, Taylor P. Epibatidine binding sites and activity in the spinal cord. Brain Research. 753: 269-82. PMID 9125412 DOI: 10.1016/S0006-8993(97)00031-0 |
0.423 |
|
| 1997 |
Marchot P, Prowse CN, Kanter J, Camp S, Ackermann EJ, Radić Z, Bougis PE, Taylor P. Expression and activity of mutants of fasciculin, a peptidic acetylcholinesterase inhibitor from mamba venom. The Journal of Biological Chemistry. 272: 3502-10. PMID 9013597 DOI: 10.1074/Jbc.272.6.3502 |
0.355 |
|
| 1996 |
Khan IM, Youngblood KL, Printz MP, Yaksh TL, Taylor P. Spinal nicotinic receptor expression in spontaneously hypertensive rats. Hypertension. 28: 1093-9. PMID 8952602 DOI: 10.1161/01.Hyp.28.6.1093 |
0.387 |
|
| 1996 |
Sugiyama N, Boyd AE, Taylor P. Anionic residue in the α-subunit of the nicotinic acetylcholine receptor contributing to subunit assembly and ligand binding Journal of Biological Chemistry. 271: 26575-26581. PMID 8900129 DOI: 10.1074/Jbc.271.43.26575 |
0.507 |
|
| 1996 |
Keller SH, Lindstrom J, Taylor P. Involvement of the chaperone protein calnexin and the acetylcholine receptor beta-subunit in the assembly and cell surface expression of the receptor. The Journal of Biological Chemistry. 271: 22871-7. PMID 8798466 DOI: 10.1074/Jbc.271.37.22871 |
0.31 |
|
| 1996 |
Hosea NA, Radi? Z, Tsigelny I, Berman HA, Quinn DM, Taylor P. Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates. Biochemistry. 35: 10995-1004. PMID 8718893 DOI: 10.1021/Bi9611220 |
0.322 |
|
| 1996 |
Taylor P, Radic Z, Hosea NA, Camp S, Marchot P, Berman HA. Structural bases for the specificity of cholinesterase catalysis and inhibition. Toxicology Letters. 453-8. PMID 8597093 DOI: 10.1016/0378-4274(95)03575-3 |
0.443 |
|
| 1996 |
Bourne Y, Taylor P, Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell. 83: 503-12. PMID 8521480 DOI: 10.1016/0092-8674(95)90128-0 |
0.381 |
|
| 1995 |
Ashani Y, Radi? Z, Tsigelny I, Vellom DC, Pickering NA, Quinn DM, Doctor BP, Taylor P. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by mono- and bisquaternary oximes. The Journal of Biological Chemistry. 270: 6370-80. PMID 7890775 DOI: 10.1074/Jbc.270.11.6370 |
0.368 |
|
| 1995 |
Keller SH, Kreienkamp HJ, Kawanishi C, Taylor P. Molecular determinants conferring alpha-toxin resistance in recombinant DNA-derived acetylcholine receptors. The Journal of Biological Chemistry. 270: 4165-71. PMID 7876169 DOI: 10.1074/JBC.270.8.4165 |
0.377 |
|
| 1995 |
Kreienkamp HJ, Maeda RK, Sine SM, Taylor P. Intersubunit contacts governing assembly of the mammalian nicotinic acetylcholine receptor. Neuron. 14: 635-44. PMID 7695910 DOI: 10.1016/0896-6273(95)90320-8 |
0.448 |
|
| 1995 |
Radi? Z, Quinn DM, Vellom DC, Camp S, Taylor P. Allosteric control of acetylcholinesterase catalysis by fasciculin. The Journal of Biological Chemistry. 270: 20391-9. PMID 7657613 DOI: 10.1074/Jbc.270.35.20391 |
0.405 |
|
| 1995 |
Sine SM, Kreienkamp HJ, Bren N, Maeda R, Taylor P. Molecular dissection of subunit interfaces in the acetylcholine receptor: identification of determinants of alpha-conotoxin M1 selectivity. Neuron. 15: 205-11. PMID 7619523 DOI: 10.1016/0896-6273(95)90077-2 |
0.68 |
|
| 1995 |
van den Born HK, Radić Z, Marchot P, Taylor P, Tsigelny I. Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesterase. Protein Science : a Publication of the Protein Society. 4: 703-15. PMID 7613468 DOI: 10.1002/Pro.5560040410 |
0.43 |
|
| 1995 |
Getman DK, Mutero A, Inoue K, Taylor P. Transcription factor repression and activation of the human acetylcholinesterase gene. The Journal of Biological Chemistry. 270: 23511-9. PMID 7559515 DOI: 10.1074/Jbc.270.40.23511 |
0.306 |
|
| 1995 |
Hosea NA, Berman HA, Taylor P. Specificity and Orientation of Trigonal Carboxyl Esters and Tetrahedral Alkylphosphonyl Esters in Cholinesterases Biochemistry. 34: 11528-11536. PMID 7547883 DOI: 10.1021/Bi00036A028 |
0.357 |
|
| 1994 |
Sine SM, Quiram P, Papanikolaou F, Kreienkamp HJ, Taylor P. Conserved tyrosines in the α subunit of the nicotinic acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists Journal of Biological Chemistry. 269: 8808-8816. PMID 8132615 |
0.696 |
|
| 1994 |
Khan IM, Yaksh TL, Taylor P. Ligand specificity of nicotinic acetylcholine receptors in rat spinal cord: studies with nicotine and cytisine. The Journal of Pharmacology and Experimental Therapeutics. 270: 159-66. PMID 8035312 |
0.373 |
|
| 1994 |
Khan IM, Printz MP, Yaksh TL, Taylor P. Augmented responses to intrathecal nicotinic agonists in spontaneous hypertension Hypertension. 24: 611-619. PMID 7960022 DOI: 10.1161/01.Hyp.24.5.611 |
0.315 |
|
| 1994 |
Kreienkamp HJ, Sine SM, Maeda RK, Taylor P. Glycosylation sites selectively interfere with alpha-toxin binding to the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 269: 8108-14. PMID 7907588 |
0.624 |
|
| 1994 |
Saxena A, Qian N, Kovach IM, Kozikowski AP, Pang YP, Vellom DC, Radi? Z, Quinn D, Taylor P, Doctor BP. Identification of amino acid residues involved in the binding of Huperzine A to cholinesterases. Protein Science : a Publication of the Protein Society. 3: 1770-8. PMID 7849595 DOI: 10.1002/Pro.5560031017 |
0.382 |
|
| 1994 |
Taylor P, Radić Z, Kreienkamp HJ, Maeda R, Luo Z, Fuentes ME, Vellom D, Pickering N. Expression and ligand specificity of acetylcholinesterase and the nicotinic receptor: a tale of two cholinergic sites. Biochemical Society Transactions. 22: 740-5. PMID 7821676 DOI: 10.1042/Bst0220740 |
0.506 |
|
| 1993 |
Vellom DC, Radić Z, Li Y, Pickering NA, Camp S, Taylor P. Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry. 32: 12-7. PMID 8418833 DOI: 10.1021/Bi00052A003 |
0.314 |
|
| 1993 |
Hutchinson DO, Walls TJ, Nakano S, Camp S, Taylor P, Harper CM, Groover RV, Peterson HA, Jamieson DG, Engel AG. Congential endplate acetylocholinesterase deficiency Brain. 116: 633-653. PMID 8390325 DOI: 10.1093/Brain/116.3.633 |
0.332 |
|
| 1993 |
Fuentes ME, Taylor P. Control of acetylcholinesterase gene expression during myogenesis. Neuron. 10: 679-87. PMID 8386528 DOI: 10.1016/0896-6273(93)90169-R |
0.324 |
|
| 1993 |
Radić Z, Pickering NA, Vellom DC, Camp S, Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry. 32: 12074-84. PMID 8218285 DOI: 10.1021/Bi00096A018 |
0.397 |
|
| 1993 |
Wasserman L, Doctor BP, Gentry MK, Taylor P. Epitope mapping of form-specific and nonspecific antibodies to acetylcholinesterase Journal of Neurochemistry. 61: 2124-2132. PMID 7504082 DOI: 10.1111/J.1471-4159.1993.Tb07450.X |
0.314 |
|
| 1992 |
Radić Z, Gibney G, Kawamoto S, MacPhee-Quigley K, Bongiorno C, Taylor P. Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants. Biochemistry. 31: 9760-7. PMID 1356436 DOI: 10.1021/Bi00155A032 |
0.328 |
|
| 1991 |
Taylor P, Abramson SN, Johnson DA, Valenzuela CF, Herz J. Distinctions in ligand binding sites on the nicotinic acetylcholine receptor. Annals of the New York Academy of Sciences. 625: 568-87. PMID 2058912 DOI: 10.1111/J.1749-6632.1991.Tb33893.X |
0.53 |
|
| 1991 |
Aslanian D, Grof P, Bon S, Masson P, Négrerie M, Chatel JM, Balkanski M, Taylor P, Massoulié J. A comparative Raman spectroscopic study of cholinesterases. Biochimie. 73: 1375-86. PMID 1799630 DOI: 10.1016/0300-9084(91)90167-Y |
0.305 |
|
| 1991 |
Abramson SN, Trischman JA, Tapiolas DM, Harold EE, Fenical W, Taylor P. Structure/activity and molecular modeling studies of the lophotoxin family of irreversible nicotinic receptor antagonists. Journal of Medicinal Chemistry. 34: 1798-804. PMID 1676426 DOI: 10.1021/Jm00110A007 |
0.563 |
|
| 1991 |
Abramson SN, Fenical W, Taylor P. Lophotoxins: Irreversible active‐site‐directed inhibitors of nicotinic acetylcholine receptors Drug Development Research. 24: 297-312. DOI: 10.1002/Ddr.430240402 |
0.45 |
|
| 1990 |
Friboulet A, Rieger F, Goudou D, Amitai G, Taylor P. Interaction of an organophosphate with a peripheral site on acetylcholinesterase. Biochemistry. 29: 914-920. PMID 2340283 DOI: 10.1021/Bi00456A010 |
0.385 |
|
| 1990 |
Gibney G, Camp S, Dionne M, MacPhee-Quigley K, Taylor P. Mutagenesis of essential functional residues in acetylcholinesterase Proceedings of the National Academy of Sciences of the United States of America. 87: 7546-7550. PMID 2217185 DOI: 10.1073/Pnas.87.19.7546 |
0.31 |
|
| 1990 |
Ogert RA, Gentry MK, Richardson EC, Deal CD, Abramson SN, Alving CR, Taylor P, Doctor BP. Studies on the topography of the catalytic site of acetylcholinesterase using polyclonal and monoclonal antibodies Journal of Neurochemistry. 55: 756-763. PMID 1696619 DOI: 10.1111/J.1471-4159.1990.Tb04556.X |
0.304 |
|
| 1990 |
Abramson SN, Taylor P. Identification of nicotinic receptor ACh-binding subunits. Trends in Neurosciences. 13: 92. PMID 1691875 DOI: 10.1016/0166-2236(90)90180-I |
0.518 |
|
| 1989 |
Abramson SN, Radic Z, Manker D, Faulkner DJ, Taylor P. Onchidal: a naturally occurring irreversible inhibitor of acetylcholinesterase with a novel mechanism of action. Molecular Pharmacology. 36: 349-54. PMID 2779521 |
0.362 |
|
| 1989 |
Herz JM, Johnson DA, Taylor P. Distance between the agonist and noncompetitive inhibitor sites on the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 264: 12439-48. PMID 2745453 |
0.317 |
|
| 1989 |
Abramson SN, Li Y, Culver P, Taylor P. An analog of lophotoxin reacts covalently with Tyr190 in the alpha-subunit of the nicotinic acetylcholine receptor. The Journal of Biological Chemistry. 264: 12666-72. PMID 2568359 |
0.362 |
|
| 1989 |
Abramson SN, Ellisman MH, Deerinck TJ, Maulet Y, Gentry MK, Doctor BP, Taylor P. Differences in structure and distribution of the molecular forms of acetylcholinesterase. The Journal of Cell Biology. 108: 2301-11. PMID 2472404 DOI: 10.1083/Jcb.108.6.2301 |
0.318 |
|
| 1987 |
Herz JM, Johnson DA, Taylor P. Interaction of noncompetitive inhibitors with the acetylcholine receptor. The site specificity and spectroscopic properties of ethidium binding. The Journal of Biological Chemistry. 262: 7238-47. PMID 3584114 |
0.4 |
|
| 1986 |
Edery H, Geyer MA, Taylor P, Berman HA. Target sites for anticholinesterases on the ventral surface of the medulla oblongata: hypotension elicited by organophosphorus agents. Journal of Autonomic Pharmacology. 6: 195-205. PMID 3771592 DOI: 10.1111/J.1474-8673.1986.Tb00645.X |
0.309 |
|
| 1986 |
Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor SS, Friedmann T, Taylor P. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature. 319: 407-9. PMID 3753747 DOI: 10.1038/319407A0 |
0.338 |
|
| 1986 |
Palma A, Herz JM, Wang HH, Taylor P. Association of a spin-labeled local anesthetic with the allosterically coupled noncompetitive inhibitor site on the acetylcholine receptor. Molecular Pharmacology. 30: 243-51. PMID 3018481 |
0.409 |
|
| 1985 |
Manavalan P, Taylor P, Johnson WC. Circular dichroism studies of acetylcholine sterase conformation. Comparison of the 11 S and 5.6 S species and the differences induced by inhibitory ligands Biochimica Et Biophysica Acta. 829: 365-370. PMID 4005268 DOI: 10.1016/0167-4838(85)90246-8 |
0.351 |
|
| 1983 |
Doctor BP, Camp S, Gentry MK, Taylor SS, Taylor P. Antigenic and structural differences in the catalytic subunits of the molecular forms of acetylcholinesterase. Proceedings of the National Academy of Sciences of the United States of America. 80: 5767-71. PMID 6193524 DOI: 10.1073/Pnas.80.18.5767 |
0.324 |
|
| 1983 |
Taylor P, Brown RD, Johnson DA. The Linkage between Ligand Occupation and Response of the Nicotinic Acetylcholine Receptor Current Topics in Membranes and Transport. 18: 407-444. DOI: 10.1016/S0070-2161(08)60538-9 |
0.464 |
|
| 1982 |
Taylor P, Sine SM. Ligand occupation and the functional states of the nicotinic-cholinergic receptor Trends in Pharmacological Sciences. 3: 197-200. DOI: 10.1016/0165-6147(82)91091-4 |
0.687 |
|
| 1981 |
Berman HA, Becktel W, Taylor P. Spectroscopic studies on acetylcholinesterase: influence of peripheral-site occupation on active-center conformation. Biochemistry. 20: 4803-4810. PMID 7295650 DOI: 10.1021/Bi00519A043 |
0.322 |
|
| 1979 |
Epstein DJ, Berman HA, Taylor P. Ligand-induced conformational changes in acetylcholinesterase investigated with fluorescent phosphonates Biochemistry. 18: 4749-4754. PMID 497167 DOI: 10.1021/Bi00588A040 |
0.327 |
|
| 1979 |
Bolger MB, Taylor P. Kinetics of association between bisquaternary ammonium ligands and acetylcholinesterase. Evidence for two conformational states of the enzyme from stopped-flow measurements of fluorescence. Biochemistry. 18: 3622-3629. PMID 476071 DOI: 10.1021/Bi00583A029 |
0.303 |
|
| 1975 |
Taylor P, Lappi S. Interaction of fluorescence probes with acetylcholinesterase. Site and specificity of propidium binding Biochemistry. 14: 1989-1997. PMID 1125207 DOI: 10.1021/Bi00680A029 |
0.464 |
|
| 1975 |
Flanagan SD, Taylor P, Barondes SH. Affinity partitioning of acetylcholine receptor enriched membranes and their purification. Nature. 254: 441-3. PMID 1118030 DOI: 10.1038/254441A0 |
0.443 |
|
| 1975 |
Taylor P. Drug-Biomolecule Interactions: Mechanism of Ligand Interactions with Carbonic Anhydrase Studied by Magnetic Resonance Relaxation and Rapid Reaction Methods Journal of Pharmaceutical Sciences. 64: 501-507. PMID 239192 DOI: 10.1002/Jps.2600640340 |
0.321 |
|
| 1971 |
Taylor PW, Feeney J, Burgen ASV. Investigation of the mechanism of ligand binding with cobalt(II) human carbonic anhydrase by hydrogen-1 and fluorine-19 nuclear magnetic resonance spectroscopy Biochemistry. 10: 3866-3875. PMID 5003665 DOI: 10.1021/Bi00797A011 |
0.307 |
|
| 1971 |
Taylor PW, Burgen ASV. Kinetics of carbonic anhydrase-inhibitor complex formation. a comparison of anion- and sulfonamide-binding mechanisms. Biochemistry. 10: 3859-3866. PMID 4334280 DOI: 10.1021/Bi00797A010 |
0.347 |
|
| 1966 |
Taylor PW, Chidsey CA, Richardson KC, Cooper T, Michaelson IA. Subcellular distribution of norepinephrine in the normal and surgically denervated cat heart. Biochemical Pharmacology. 15: 681-9. PMID 5963901 DOI: 10.1016/0006-2952(66)90002-5 |
0.327 |
|
| 1965 |
WURSTER DE, TAYLOR PW. DISSOLUTION RATES. Journal of Pharmaceutical Sciences. 54: 169-75. PMID 14300999 DOI: 10.1002/Jps.2600540202 |
0.528 |
|
| 1965 |
Wurster DE, Taylor PW. Dissolution kinetics of certain crystalline forms of prednisolone. Journal of Pharmaceutical Sciences. 54: 670-6. PMID 5845876 DOI: 10.1002/Jps.2600540503 |
0.563 |
|
| 1965 |
Taylor PW, Wurster DE. Dissolution Kinetics of Certain Crystalline Forms of Prednisolone II: Influence of Low Concentrations of Sodium Lauryl Sulfate Journal of Pharmaceutical Sciences. 54: 1654-1658. DOI: 10.1002/Jps.2600541120 |
0.552 |
|
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