{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gagne JP"],"funding":["Canadian Institutes of Health Research"],"pagination":["7788-805"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3439892"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["40(16)"],"pubmed_abstract":["Upon DNA damage induction, DNA-dependent poly(ADP-ribose) polymerases (PARPs) synthesize an anionic poly(ADP-ribose) (pADPr) scaffold to which several proteins bind with the subsequent formation of pADPr-associated multiprotein complexes. We have used a combination of affinity-purification methods and proteomics approaches to isolate these complexes and assess protein dynamics with respect to pADPr metabolism. As a first approach, we developed a substrate trapping strategy by which we demonstrate that a catalytically inactive Poly(ADP-ribose) glycohydrolase (PARG) mutant can act as a physiologically selective bait for the isolation of specific pADPr-binding proteins through its macrodomain-like domain. In addition to antibody-mediated affinity-purification methods, we used a pADPr macrodom"],"journal":["Nucleic acids research"],"pubmed_title":["Quantitative proteomics profiling of the poly(ADP-ribose)-related response to genotoxic stress."],"pmcid":["PMC3439892"],"funding_grant_id":["MOP-74648","MOP-14052"],"pubmed_authors":["Krietsch J","Boutin M","Ethier C","Poirier GG","Pic E","Paquet E","Isabelle M","Kelly I","Moon KM","Foster LJ","Gagne JP"],"additional_accession":[]},"is_claimable":false,"name":"Quantitative proteomics profiling of the poly(ADP-ribose)-related response to genotoxic stress.","description":"Upon DNA damage induction, DNA-dependent poly(ADP-ribose) polymerases (PARPs) synthesize an anionic poly(ADP-ribose) (pADPr) scaffold to which several proteins bind with the subsequent formation of pADPr-associated multiprotein complexes. We have used a combination of affinity-purification methods and proteomics approaches to isolate these complexes and assess protein dynamics with respect to pADPr metabolism. As a first approach, we developed a substrate trapping strategy by which we demonstrate that a catalytically inactive Poly(ADP-ribose) glycohydrolase (PARG) mutant can act as a physiologically selective bait for the isolation of specific pADPr-binding proteins through its macrodomain-like domain. In addition to antibody-mediated affinity-purification methods, we used a pADPr macrodom","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2026-04-29T13:32:56.652Z","creation":"2019-03-27T00:57:51Z"},"accession":"S-EPMC3439892","cross_references":{"pubmed":["22669911"],"doi":["10.1093/nar/gks486"]}}