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Chemico-Biological Interactions|July 27, 1999
The influence of peripheral site ligands on the reaction of symmetric and chiral organophosphates with wildtype and mutant acetylcholinesterasesZ Radić, P TaylorJournal of Applied Toxicology : JAT|March 29, 2002
Peripheral site ligands accelerate inhibition of acetylcholinesterase by neutral organophosphatesZ Radić, P TaylorThe Journal of Biological Chemistry|October 19, 2000
Interaction kinetics of reversible inhibitors and substrates with acetylcholinesterase and its fasciculin 2 complexZ Radić, P TaylorMolecular Pharmacology|January 1, 1991
Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivativesZ Radić, E Reiner, P TaylorEnantiomer|January 1, 1997
Determining ligand orientation and transphosphonylation mechanisms on acetylcholinesterase by Rp, Sp enantiomer selectivity and site-specific mutagenesisP Taylor, N A Hosea, I Tsigelny, et al.Biochemistry|November 16, 1993
Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitorsZ Radić, N A Pickering, D C Vellom, et al.The Journal of Biological Chemistry|September 1, 1995
Allosteric control of acetylcholinesterase catalysis by fasciculinZ Radić, D M Quinn, D C Vellom, et al.Protein Science : a Publication of the Protein Society|April 1, 1995
Theoretical analysis of the structure of the peptide fasciculin and its docking to acetylcholinesteraseH K van den Born, Z Radić, P Marchot, et al.The Journal of Biological Chemistry|September 12, 1997
Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculinZ Radić, P D Kirchhoff, D M Quinn, et al.Biochemistry|October 13, 1992
Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutantsZ Radić, G Gibney, S Kawamoto, et al.Pageof 225