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Zoran Radić

Researcher at University of Montana

Publications -  130
Citations -  7875

Zoran Radić is an academic researcher from University of Montana. The author has contributed to research in topics: Acetylcholinesterase & Butyrylcholinesterase. The author has an hindex of 40, co-authored 127 publications receiving 7423 citations. Previous affiliations of Zoran Radić include University of Zagreb & University at Buffalo.

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Click Chemistry In Situ: Acetylcholinesterase as a Reaction Vessel for the Selective Assembly of a Femtomolar Inhibitor from an Array of Building Blocks

TL;DR: The generation of carbonic anhydrase inhibitors by using the SN2 reaction of a thiol with an -chloroketone in the presence of the enzyme target is described herein.
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The Cholinesterases: From Genes to Proteins

TL;DR: These recent events have added a new perspective to cholinesterase research wherein all facets of gene expression become amenable to study and structure-function relation­ ships within this family of enzymes can be approached at an atomic level.
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Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site

TL;DR: These structures of AChE provide templates for designing compounds directed to the enzyme surface that modulate specific surface interactions controlling catalytic activity and non‐catalytic heterologous protein associations.
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Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors.

TL;DR: By examining inhibitor interactions with single and multiple site-specific mutants of mouse acetylcholinesterase, three distinct domains are identified that are responsible for conferring selectivity for acetyl- and butyrylcholiersterase inhibitors.
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In situ click chemistry: enzyme inhibitors made to their own specifications.

TL;DR: Three new inhibitors were discovered, derived from tacrine and phenylphenanthridinium azides and acetylenes, in the reactions with Electrophorus electricus and mouse AChE, which include the newly formed triazole nexus as a significant pharmacophore.