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Chemico-Biological Interactions|July 29, 2008
Acetylcholinesterase: mechanisms of covalent inhibition of H447I mutant determined by computational analysesY H Cheng, X L Cheng, Z Radić, et al.
Enantiomer|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.
Biochimica Et Biophysica Acta|March 20, 1999
Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral siteM Sentjurc, S Pecar, J Stojan, 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.
The Journal of Biological Chemistry|April 15, 1994
Site of fasciculin interaction with acetylcholinesteraseZ Radić, R Duran, D C Vellom, et al.
Biochimica Et Biophysica Acta|August 14, 1999
Amino acid residues involved in the interaction of acetylcholinesterase and butyrylcholinesterase with the carbamates Ro 02-0683 and bambuterol, and with terbutalineZ Kovarik, Z Radić, B Grgas, et al.
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