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A. Ordentlich

Showing results (21-30 of 30) with videos related to

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Biochemistry|November 28, 1995
Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsiteD Barak, A Ordentlich, A Bromberg, et al.
The Journal of Biological Chemistry|March 4, 1994
Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common coreD Barak, C Kronman, A Ordentlich, et al.
Chemico-Biological Interactions|July 27, 1999
A preliminary comparison of structural models for catalytic intermediates of acetylcholinesteraseI Silman, C B Millard, A Ordentlich, et al.
The EMBO Journal|August 1, 1994
Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesteraseA Shafferman, A Ordentlich, D Barak, 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.
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.
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.
FEBS Letters|May 5, 1997
Direct determination of the chemical composition of acetylcholinesterase phosphonylation products utilizing electrospray-ionization mass spectrometryR Barak, A Ordentlich, D Barak, 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.
Biochemistry|June 3, 1999
Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic levelC B Millard, G Kryger, A Ordentlich, et al.
Pageof 3

Showing results (21-30 of 30) with videos related to

Sort By:
Pageof 3
You have reached the last page of results.This site can display upto 30 results.
Biochemistry|November 28, 1995
Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsiteD Barak, A Ordentlich, A Bromberg, et al.
The Journal of Biological Chemistry|March 4, 1994
Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common coreD Barak, C Kronman, A Ordentlich, et al.
Chemico-Biological Interactions|July 27, 1999
A preliminary comparison of structural models for catalytic intermediates of acetylcholinesteraseI Silman, C B Millard, A Ordentlich, et al.
The EMBO Journal|August 1, 1994
Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesteraseA Shafferman, A Ordentlich, D Barak, 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.
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.
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.
FEBS Letters|May 5, 1997
Direct determination of the chemical composition of acetylcholinesterase phosphonylation products utilizing electrospray-ionization mass spectrometryR Barak, A Ordentlich, D Barak, 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.
Biochemistry|June 3, 1999
Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic levelC B Millard, G Kryger, A Ordentlich, et al.
Pageof 3