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• W2021029128 abstract "Significance Recognition and repair of DNA lesions are critical for maintaining genomic stability and reducing the generation of mutations that lead to cancer development. A mechanism of chromatin alteration is described here that is essential for repair of DNA double-strand breaks. The histone chaperone, nucleolin, is recruited to sites of DNA breaks via binding to RAD50 of the MRE11-NBS1-RAD50 complex, where it removes histone proteins H2A and H2B from the nucleosome at the break site. This nucleosome disruption allows DNA repair proteins to access the DNA lesion and facilitate repair of the DNA break. Clinical implications of these findings include the identification of new targets, such as nucleolin, that could be modulated to enhance sensitivity of tumor cells to radiation therapy." @default.
• W2021029128 created "2016-06-24" @default.
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• W2021029128 date "2013-09-30" @default.
• W2021029128 modified "2023-10-16" @default.
• W2021029128 title "Nucleolin mediates nucleosome disruption critical for DNA double-strand break repair" @default.
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• W2021029128 doi "https://doi.org/10.1073/pnas.1306160110" @default.
• W2021029128 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3801049" @default.
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