D
Dov Barak
Researcher at Israel Institute for Biological Research
Publications - 58
Citations - 3210
Dov Barak is an academic researcher from Israel Institute for Biological Research. The author has contributed to research in topics: Active center & Active site. The author has an hindex of 27, co-authored 58 publications receiving 3116 citations.
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Journal ArticleDOI
Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocket.
Arie Ordentlich,Dov Barak,C. Kronman,Yehuda Flashner,M Leitner,Yoffi Segall,Naomi Ariel,S. Cohen,Baruch Velan,Avigdor Shafferman +9 more
TL;DR: It is proposed that the conformational flexibility of aromatic residues generates a plasticity in the active center that contributes to the high efficiency of AChE and its ability to respond to external stimuli.
Journal ArticleDOI
Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II
Gitay Kryger,Michal Harel,Kurt Giles,Lilly Toker,Baruch Velan,Arie Lazar,Chanoch Kronman,Dov Barak,Naomi Ariel,Avigdor Shafferman,Israel Silman,Joel L. Sussman +11 more
TL;DR: The present findings are consistent with the notion that the main role of this network is the proper positioning of the Glu202 carboxylate relative to the catalytic triad, thus defining its functional role in the interaction of acetylcholinesterase with substrates and inhibitors.
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Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level.
Charles B. Millard,Gitay Kryger,Arie Ordentlich,Harry M. Greenblatt,M. Harel,Mia L. Raves,Yoffi Segall,Dov Barak,Avigdor Shafferman,Israel Silman,Joel L. Sussman +10 more
TL;DR: The active sites of aged sarin- and soman-TcAChE were essentially identical and provided structural models for the negatively charged, tetrahedral intermediate that occurs during deacylation with the natural substrate, acetylcholine.
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Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.
Avigdor Shafferman,Baruch Velan,Arie Ordentlich,C. Kronman,Haim Grosfeld,M Leitner,Yehuda Flashner,Sara Cohen,Dov Barak,Naomi Ariel +9 more
TL;DR: It is proposed that binding of acetylcholine, on the surface of AChE, may trigger sequence of conformational changes extending from the peripheral anionic site through W286 to D74, at the entrance of the ‘gorge’, and down to the catalytic center (through Y341 to F338 and Y337).
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Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
Avigdor Shafferman,C. Kronman,Yehuda Flashner,M Leitner,Haim Grosfeld,Arie Ordentlich,Yehoshua Gozes,Sara Cohen,Naomi Ariel,Dov Barak +9 more
TL;DR: The x-ray structure of the Torpedo acetylcholinesterase supports this assumption by revealing the participation of these residues in salt bridges between neighboring secondary structure elements.