{Reference Type}: Journal Article
{Title}: PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools.
{Author}: Dasovich M;Leung AKL;
{Journal}: Mol Cell
{Volume}: 83
{Issue}: 10
{Year}: 2023 05 18
{Factor}: 19.328
{DOI}: 10.1016/j.molcel.2023.04.009
{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 achieved using genetically encoded reporters, and next-generation detection reagents have improved the precision of immunoassays for specific forms of ADP-ribosylation. Further development and refinement of these tools will continue to advance our understanding of the functions and mechanisms of ADP-ribosylation in health and disease.