Preferential binding of IFI16 protein to cruciform structure and superhelical DNA

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F12%3A00379230" target="_blank" >RIV/68081707:_____/12:00379230 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.bbrc.2012.05.065" target="_blank" >http://dx.doi.org/10.1016/j.bbrc.2012.05.065</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbrc.2012.05.065" target="_blank" >10.1016/j.bbrc.2012.05.065</a>

Result language
angličtina
Original language name
Preferential binding of IFI16 protein to cruciform structure and superhelical DNA
Original language description
Interferon (IFN)-inducible HIN-200 proteins play an important role in transcriptional regulation linked to cell cycle control, inflammation, autoimmunity and differentiation. We demonstrate that IFI16 protein binds strongly to negatively superhelical plasmid DNA. We also detect a strong preference for IFI16 binding to cruciform DNA structure compared to linear DNA topology. This novel DNA-binding property of IFI16 protein to scDNA and cruciform structures may play critical roles in its tumor suppressorfunction.
Czech name
—
Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
—

Project
<a href="/en/project/GAP301%2F10%2F1211" target="_blank" >GAP301/10/1211: Transcriptional activities of wild-type and mutant p53, decision between cell proliferation, cell cycle arrest and apoptosis</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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