Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: A new class of antimalarial therapeutics
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F09%3A00329059" target="_blank" >RIV/61388963:_____/09:00329059 - 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
Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: A new class of antimalarial therapeutics
Original language description
Plasmodium falciparum (Pf) relies on the purine salvage enzyme, hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT), for the synthesis of the mononucleotides. Acyclic nucleoside phosphonates (ANPs) are structural analogs of the mononucleotide product of the reaction and contain a purine base linked by different combinations of atoms to a phosphonate group. Ki values for 19 ANPs were determined for PfHGXPRT and human HGPRT. IC50 values for Pf grown in cell culture and the structures of humanHGPRT in complex with three ANPs have been determined. These results provide a basis for the design of more potent and selective inhibitors as anti-malarial drugs with novel mode of action.
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
CC - Organic chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2009
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Medicinal Chemistry
ISSN
0022-2623
e-ISSN
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Volume of the periodical
52
Issue of the periodical within the volume
14
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
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UT code for WoS article
000268139900034
EID of the result in the Scopus database
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