@article{f375628157c34086a26efd930a19f970,
title = "Acetylation blocks DNA damage–induced chromatin ADP-ribosylation",
abstract = "Recent studies report serine ADP-ribosylation on nucleosomes during the DNA damage response. We unveil histone H3 serine 10 as the primary acceptor residue for chromatin ADP-ribosylation and find that specific histone acetylation marks block this activity. Our results provide a molecular explanation for the well-documented phenomenon of rapid deacetylation at DNA damage sites and support the combinatorial application of PARP and HDAC inhibitors for the treatment of PARP-dependent cancers.",
author = "Glen Liszczak and Diehl, {Katharine L.} and Dann, {Geoffrey P.} and Muir, {Tom W.}",
note = "Funding Information: We thank current members of the Muir laboratory as well as C.D. Allis for discussions and comments. We also thank the Princeton University Sequencing Core Facility and C. Arrowsmith (University of Toronto) for the SIRT6 expression plasmid. This work was supported by National Institutes of Health (NIH) Grants R37 GM086868, R01 GM107047 and P01 CA196539. G.P.L. and K.L.D. were supported by NIH Research Service Awards (1F32GM110880 and 5F32CA206418, respectively). Publisher Copyright: {\textcopyright} 2018, The Author(s).",
year = "2018",
month = sep,
day = "1",
doi = "10.1038/s41589-018-0097-1",
language = "English (US)",
volume = "14",
pages = "837--840",
journal = "Nature chemical biology",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "9",
}