Potency of five structurally different acetylcholinesterase reactivators to reactivate human brain cholinesterases inhibited by cyclosarin
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60162694%3AG44__%2F07%3A00001804" target="_blank" >RIV/60162694:G44__/07:00001804 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Potency of five structurally different acetylcholinesterase reactivators to reactivate human brain cholinesterases inhibited by cyclosarin
Original language description
Acetylcholinesterase (AChE; EC 3.1.1.7) reactivators are used as a part of the antidotes aimed for the treatment of organophosphorus pesticide and nerve agent intoxications. Cyclosarin is one member of the nerve agent family. In this work, we are interested in the comparison of reactivation potency of five structurally different AChE reactivators (pralidoxime, trimedoxime, methoxime, HS-6 and BI-6) to reactivate cyclosarin-inhibited cholinesterases of human brain. As resulted, bisquaternary monooxime reactivator BI-6 seems to be the most potent reactivator of cyclosarin-inhibited cholinesterases. Moreover, according to the obtained results, we can describe basic structural requirements, which are necessary for the efficacious reactivation process.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FP - Other medical fields
OECD FORD branch
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Result continuities
Project
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Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2007
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Clinical Toxicology
ISSN
1556-3650
e-ISSN
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Volume of the periodical
45
Issue of the periodical within the volume
5
Country of publishing house
GB - UNITED KINGDOM
Number of pages
4
Pages from-to
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UT code for WoS article
000247731600018
EID of the result in the Scopus database
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