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M Leitner

Researcher at Israel Institute for Biological Research

Publications -  33
Citations -  1700

M Leitner is an academic researcher from Israel Institute for Biological Research. The author has contributed to research in topics: Spotted fever & Acetylcholinesterase. The author has an hindex of 17, co-authored 33 publications receiving 1651 citations.

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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.

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.
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Substrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic center.

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.

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.
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Attenuated Nontoxinogenic and Nonencapsulated Recombinant Bacillus anthracis Spore Vaccines Protect against Anthrax

TL;DR: Results suggest that some B. anthracisspore-associated antigen(s) may contribute in a significant manner to protective immunity and appear to be more efficacious than the vegetative cell vaccine.
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The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant.

TL;DR: The mutation did not seem to affect the efficiencies of either synthesis or secretion of recombinant HuAChE polypeptides, as was demonstrated in cell lines derived from human embryonic kidney as well as from a human neuroblastoma.