{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang XN"],"funding":["NIBIB NIH HHS","University of Southern California","National Institute of General Medical Sciences","National Institute of Biomedical Imaging and Bioengineering","NIGMS NIH HHS"],"pagination":["1982-1991"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8848837"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(7)"],"pubmed_abstract":["Among various protein posttranslational modifiers, poly-ADP-ribose polymerase 1 (PARP1) is a key player for regulating numerous cellular processes and events through enzymatic attachments of target proteins with ADP-ribose units donated by nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Human PARP1 is involved in the pathogenesis and progression of many diseases. PARP1 inhibitors have received approvals for cancer treatment. Despite these successes, our understanding about PARP1 remains limited, partially due to the presence of various ADP-ribosylation reactions catalyzed by other PARPs and their overlapped cellular functions. Here we report a synthetic NAD<sup>+</sup> featuring an adenosyl 3'-azido substitution. Acting as an ADP-ribose donor with high activity and specificity for hum"],"journal":["Chemical science"],"pubmed_title":["Discovery of an NAD<sup>+</sup> analogue with enhanced specificity for PARP1."],"pmcid":["PMC8848837"],"funding_grant_id":["Start-Up Fund for New Faculty","R35 GM137901","Sharon L. Cockrell Cancer Research Fund","R35GM137901","R01EB031830","R01 EB031830"],"pubmed_authors":["Lam AT","Li J","Strutzenberg TS","Cheng Q","Zhang Y","Griffin PR","Pei H","Courouble VV","Wang Y","Louie SG","Stiles BL","Zhang XN"],"additional_accession":[]},"is_claimable":false,"name":"Discovery of an NAD<sup>+</sup> analogue with enhanced specificity for PARP1.","description":"Among various protein posttranslational modifiers, poly-ADP-ribose polymerase 1 (PARP1) is a key player for regulating numerous cellular processes and events through enzymatic attachments of target proteins with ADP-ribose units donated by nicotinamide adenine dinucleotide (NAD<sup>+</sup>). Human PARP1 is involved in the pathogenesis and progression of many diseases. PARP1 inhibitors have received approvals for cancer treatment. Despite these successes, our understanding about PARP1 remains limited, partially due to the presence of various ADP-ribosylation reactions catalyzed by other PARPs and their overlapped cellular functions. Here we report a synthetic NAD<sup>+</sup> featuring an adenosyl 3'-azido substitution. Acting as an ADP-ribose donor with high activity and specificity for hum","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2025-04-22T07:48:22.78Z","creation":"2025-04-05T22:15:54.103Z"},"accession":"S-EPMC8848837","cross_references":{"pubmed":["35308855"],"doi":["10.1039/d1sc06256e"]}}