{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dasovich M"],"funding":["Johns Hopkins University","NIA NIH HHS","National Institutes of Health","NIGMS NIH HHS"],"pagination":["1552-1572"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10202152"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["83(10)"],"pubmed_abstract":["PARPs catalyze ADP-ribosylation-a post-translational modification that plays crucial roles in biological processes, including DNA repair, transcription, immune regulation, and condensate formation. ADP-ribosylation can be added to a wide range of amino acids with varying lengths and chemical structures, making it a complex and diverse modification. Despite this complexity, significant progress has been made in developing chemical biology methods to analyze ADP-ribosylated molecules and their binding proteins on a proteome-wide scale. Additionally, high-throughput assays have been developed to measure the activity of enzymes that add or remove ADP-ribosylation, leading to the development of inhibitors and new avenues for therapy. Real-time monitoring of ADP-ribosylation dynamics can be achi"],"journal":["Molecular cell"],"pubmed_title":["PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools."],"pmcid":["PMC10202152"],"funding_grant_id":["T32GM080189","R01 GM104135","T32 GM080189","R01GM104135","RF1AG071326","RF1 AG071326"],"pubmed_authors":["Dasovich M","Leung AKL"],"additional_accession":[]},"is_claimable":false,"name":"PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools.","description":"PARPs catalyze ADP-ribosylation-a post-translational modification that plays crucial roles in biological processes, including DNA repair, transcription, immune regulation, and condensate formation. ADP-ribosylation can be added to a wide range of amino acids with varying lengths and chemical structures, making it a complex and diverse modification. Despite this complexity, significant progress has been made in developing chemical biology methods to analyze ADP-ribosylated molecules and their binding proteins on a proteome-wide scale. Additionally, high-throughput assays have been developed to measure the activity of enzymes that add or remove ADP-ribosylation, leading to the development of inhibitors and new avenues for therapy. Real-time monitoring of ADP-ribosylation dynamics can be achi","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 May","modification":"2026-06-02T02:20:29.73Z","creation":"2026-04-13T03:12:12.689Z"},"accession":"S-EPMC10202152","cross_references":{"pubmed":["37119811"],"doi":["10.1016/j.molcel.2023.04.009"]}}