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The EMBO Journal|October 1, 1992
Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic centerA Shafferman, B Velan, A Ordentlich, et al.
The Journal of Biological Chemistry|August 15, 1993
Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocketA Ordentlich, D Barak, C Kronman, et al.
Gene|November 16, 1992
Production and secretion of high levels of recombinant human acetylcholinesterase in cultured cell lines: microheterogeneity of the catalytic subunitC Kronman, B Velan, Y Gozes, et al.
The Journal of Biological Chemistry|September 5, 1992
Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide foldingA Shafferman, C Kronman, Y Flashner, et al.
Gene|January 1, 1985
Plasmid vectors designed for the analysis of transcription termination signalsA Honigman, J Mahajna, S Altuvia, et al.
Cell|July 15, 1988
The T cell receptor V alpha 3 gene segment is associated with reactivity to p-azobenzenearsonateK N Tan, B M Datlof, J A Gilmore, et al.
Cellular and Molecular Neurobiology|February 1, 1991
Recombinant human acetylcholinesterase is secreted from transiently transfected 293 cells as a soluble globular enzymeB Velan, C Kronman, H Grosfeld, et al.
Vaccine|July 26, 2005
Efficacious, nontoxigenic Bacillus anthracis spore vaccines based on strains expressing mutant variants of lethal toxin componentsI Mendelson, O Gat, R Aloni-Grinstein, et al.
Biochemistry|March 13, 1999
Exploring the active center of human acetylcholinesterase with stereomers of an organophosphorus inhibitor with two chiral centersA Ordentlich, D Barak, C Kronman, et al.
Acta Crystallographica. Section D, Biological Crystallography|October 29, 2000
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-IIG Kryger, M Harel, K Giles, et al.
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