<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Dasovich M</submitter><funding>Johns Hopkins University</funding><funding>NIA NIH HHS</funding><funding>National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><pagination>1552-1572</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10202152</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>83(10)</volume><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</pubmed_abstract><journal>Molecular cell</journal><pubmed_title>PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools.</pubmed_title><pmcid>PMC10202152</pmcid><funding_grant_id>T32GM080189</funding_grant_id><funding_grant_id>R01 GM104135</funding_grant_id><funding_grant_id>T32 GM080189</funding_grant_id><funding_grant_id>R01GM104135</funding_grant_id><funding_grant_id>RF1AG071326</funding_grant_id><funding_grant_id>RF1 AG071326</funding_grant_id><pubmed_authors>Dasovich M</pubmed_authors><pubmed_authors>Leung AKL</pubmed_authors></additional><is_claimable>false</is_claimable><name>PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools.</name><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</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 May</publication><modification>2026-06-02T02:20:29.73Z</modification><creation>2026-04-13T03:12:12.689Z</creation></dates><accession>S-EPMC10202152</accession><cross_references><pubmed>37119811</pubmed><doi>10.1016/j.molcel.2023.04.009</doi></cross_references></HashMap>