The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00079762" target="_blank" >RIV/00216224:14740/14:00079762 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/14:00435412
Result on the web
<a href="http://pubs.rsc.org/en/content/articlepdf/2014/ra/c4ra08278h" target="_blank" >http://pubs.rsc.org/en/content/articlepdf/2014/ra/c4ra08278h</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/c4ra08278h" target="_blank" >10.1039/c4ra08278h</a>
Alternative languages
Result language
angličtina
Original language name
The activation of N-glycosidic bond cleavage performed by base-excision repair enzyme hOGG1; theoretical study of the role of Lys 249 residue in activation of G, OxoG and FapyG
Original language description
The activation of N-glycosidic bond cleavage performed by the lysine 249 (Lys 249) residue of base-excision repair enzyme hOGG1 was calculated for 2'-deoxyguanosine (G), 8-oxo-2'-deoxyguanosine (OxoG) and N6-(2'-beta-D-deoxyribofuranosyl)-2,6-diamino-4-hydroxy-5-formamidopyrimidine (FapyG). The interaction sites of Lys 249 included the C1', N3, and N9 atoms of the nucleosides. The N9-pathway, specifically the attack of lone-pair electrons of glycosidic nitrogen N9 of a nucleoside on the proton of the Nepsilon-ammonium group of Lys 249, resulted in effective activation of the C1'-N9 bond that was highly specific with respect to normal (G) and damaged (OxoG, FapyG) nucleosides.
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
CE - Biochemistry
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)
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
RSC Advances
ISSN
2046-2069
e-ISSN
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Volume of the periodical
4
Issue of the periodical within the volume
83
Country of publishing house
GB - UNITED KINGDOM
Number of pages
9
Pages from-to
44043-44051
UT code for WoS article
000344527300030
EID of the result in the Scopus database
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