Site-specific Phosphorylation Dynamics of the Nuclear Proteome during the DNA Damage Response

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F10%3A10213211" target="_blank" >RIV/61989592:15110/10:10213211 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1074/mcp.M900616-MCP200" target="_blank" >http://dx.doi.org/10.1074/mcp.M900616-MCP200</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/mcp.M900616-MCP200" target="_blank" >10.1074/mcp.M900616-MCP200</a>

Result language
angličtina
Original language name
Site-specific Phosphorylation Dynamics of the Nuclear Proteome during the DNA Damage Response
Original language description
To investigate the temporal regulation of the DNA damage response, we applied quantitative mass spectrometry-based proteomics to measure site-specific phosphorylation changes of nuclear proteins after ionizing radiation. We profiled 5204 phosphorylationsites at five time points following DNA damage of which 594 sites on 209 proteins were observed to be regulated more than 2-fold. Of the 594 sites, 372 are novel phosphorylation sites primarily of nuclear origin. The 594 sites could be classified to distinct temporal profiles. Sites regulated shortly after radiation were enriched in the ataxia telangiectasia mutated (ATM) kinase SQ consensus sequence motif and a novel SXXQ motif. Importantly, in addition to induced phosphorylation, we identified a considerable group of sites that undergo DNA damage-induced dephosphorylation.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Publication year
2010
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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