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Zrinka Kovarik

Researcher at University of Zagreb

Publications -  101
Citations -  2431

Zrinka Kovarik is an academic researcher from University of Zagreb. The author has contributed to research in topics: Butyrylcholinesterase & Acetylcholinesterase. The author has an hindex of 26, co-authored 91 publications receiving 2060 citations.

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Structural aspects of flavonoids as inhibitors of human butyrylcholinesterase

TL;DR: Docking study showed that flavonoids bind to the BChE active site by forming multiple hydrogen bonds and pi-pi interactions, and UV-VIS absorption spectra of the flavonoid phosphate buffer solution revealed time dependant changes indicating precipitation of Flavonoids or in the case of myricetin, a change in the chemical structure resulting in a BChChE non-inhibiting specie.
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In vitro and in vivo evaluation of pyridinium oximes: mode of interaction with acetylcholinesterase, effect on tabun- and soman-poisoned mice and their cytotoxicity.

TL;DR: The potency of the oximes K048 and K027 to protect mice from five-fold LD50 oftabun and their low toxicity make these compounds leading in the therapy of tabun poisoning.
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New Structural Scaffolds for Centrally Acting Oxime Reactivators of Phosphylated Cholinesterases

TL;DR: The synthesis and activity of a new series of oxime reactivators of cholinesterases (ChEs) that contain tertiary amine or imidazole protonatable functional groups are described, revealing that distinct reactivator ionization states are involved in the reactivation of ChE conjugates and in conferring nucleophilic reactivity of the oxime group.
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Limitation of the Ellman method: cholinesterase activity measurement in the presence of oximes.

TL;DR: In this article, the authors measured the oximolysis between oximes (K027 and HI-6) and ATCh in the presence of DTNB at different pH values, taking into account the final concentration of a product that is thiocholine.
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Refinement of Structural Leads for Centrally Acting Oxime Reactivators of Phosphylated Cholinesterases

TL;DR: The enhanced intrinsic reactivity against the OP-AChE target combined with favorable pharmacokinetic properties resulted in great improvement of antidotal properties of RS194B compared with RS41A and the standard peripherally active oxime, 2-pyridinealdoxime methiodide.