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Michal Harel

Researcher at Tel Aviv University

Publications -  152
Citations -  17795

Michal Harel is an academic researcher from Tel Aviv University. The author has contributed to research in topics: Acetylcholinesterase & Visual cortex. The author has an hindex of 49, co-authored 144 publications receiving 16460 citations. Previous affiliations of Michal Harel include Weizmann Institute of Science.

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Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein

TL;DR: Modeling of acetylcholine binding to the enzyme suggests that the quaternary ammonium ion is bound not to a negatively charged "anionic" site, but rather to some of the 14 aromatic residues that line the gorge.
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The α/β hydrolase fold

TL;DR: The alpha/beta hydrolase fold as mentioned in this paper is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function, including the serine protease catalytic triad.
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Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.

TL;DR: The structural and chemical data show the important role of aromatic groups as binding sites for quaternary ligands in Torpedo acetylcholinesterase, and provide complementary evidence assigning Trp-84 and Phe-330 to the "anionic" subsite of the active site andtrp-279 to the 'peripheral' anionic site.
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Relationship between intrinsic connections and functional architecture revealed by optical imaging and in vivo targeted biocytin injections in primate striate cortex

TL;DR: High-resolution functional maps of the cortical architecture were obtained by in vivo optical imaging and it was discovered that binocular domains formed a separate set of connections in area V1; binocular regions were selectively connected among themselves but were not connected to strictly monocular regions, suggesting that they constitute a distinct columnar system.
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Structure and Evolution of the Serum Paraoxonase Family of Detoxifying and Anti-Atherosclerotic Enzymes

TL;DR: The first crystal structure of a PON family member, a variant of PON1 obtained by directed evolution, is described, a six-bladed β-propeller with a unique active site lid that is also involved in HDL binding.