{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Laspata N"],"funding":["National Center for Advancing Translational Sciences","P. Edward Evans Foundation","NCATS NIH HHS","Thomas Jefferson University","NIEHS NIH HHS","NHLBI NIH HHS","Tier I Canada Research Chair in DNA repair and Cancer Therapeutics","National Institutes of Health","Merck","UPMC Hillman Cancer Center and the Sydney Kimmel Cancer center at Thomas Jefferson University","NHLBI","National Institute of Health","NIGMS NIH HHS","Masonic Cancer Center, University of Minnesota"],"pagination":["2215-2237"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10018367"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["51(5)"],"pubmed_abstract":["PARP1 is a DNA-dependent ADP-Ribose transferase with ADP-ribosylation activity that is triggered by DNA breaks and non-B DNA structures to mediate their resolution. PARP1 was also recently identified as a component of the R-loop-associated protein-protein interaction network, suggesting a potential role for PARP1 in resolving this structure. R-loops are three-stranded nucleic acid structures that consist of a RNA-DNA hybrid and a displaced non-template DNA strand. R-loops are involved in crucial physiological processes but can also be a source of genome instability if persistently unresolved. In this study, we demonstrate that PARP1 binds R-loops in vitro and associates with R-loop formation sites in cells which activates its ADP-ribosylation activity. Conversely, PARP1 inhibition or genet"],"journal":["Nucleic acids research"],"pubmed_title":["PARP1 associates with R-loops to promote their resolution and genome stability."],"pmcid":["PMC10018367"],"funding_grant_id":["UL1 TR002494","R01HL163011","FDN-388879","UL1TR002494","R00 ES027028","R01 HL163011","KL2 TR002492","R00ES027028","CIHR PJT-173370","R01 GM123246","KL2TR002492","22-20-68-NGUY","CIHR MOP-418863"],"pubmed_authors":["Mersaoui SY","Poirier GG","Muoio D","Kaur P","Bannister MH","Wang H","Liu ZS","Curry C","Pascal JM","Laspata N","Masson JY","Fouquerel E","Nguyen HD"],"additional_accession":[]},"is_claimable":false,"name":"PARP1 associates with R-loops to promote their resolution and genome stability.","description":"PARP1 is a DNA-dependent ADP-Ribose transferase with ADP-ribosylation activity that is triggered by DNA breaks and non-B DNA structures to mediate their resolution. PARP1 was also recently identified as a component of the R-loop-associated protein-protein interaction network, suggesting a potential role for PARP1 in resolving this structure. R-loops are three-stranded nucleic acid structures that consist of a RNA-DNA hybrid and a displaced non-template DNA strand. R-loops are involved in crucial physiological processes but can also be a source of genome instability if persistently unresolved. In this study, we demonstrate that PARP1 binds R-loops in vitro and associates with R-loop formation sites in cells which activates its ADP-ribosylation activity. Conversely, PARP1 inhibition or genet","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2025-04-22T08:41:46.183Z","creation":"2025-04-05T22:41:15.312Z"},"accession":"S-EPMC10018367","cross_references":{"pubmed":["36794853"],"doi":["10.1093/nar/gkad066"]}}