{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:38:57Z","timestamp":1792787937581,"version":"4.5.0"},"reference-count":77,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T00:00:00Z","timestamp":1792368000000},"content-version":"vor","delay-in-days":18,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100010269","name":"Wellcome Trust","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010269","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.jbc.2026.113682","type":"journal-article","created":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T15:21:10Z","timestamp":1792682470000},"page":"113682","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"title":["Identification of Novel Enzymes Regulating ADP-Ribosylation of Uracil and Thymine in Nucleic Acids"],"prefix":"10.1016","author":[{"given":"Yang","family":"Lu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0190-7777","authenticated-orcid":false,"given":"Waghela","family":"Deeksha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kang","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7096-9613","authenticated-orcid":false,"given":"Josip","family":"Ahel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yizhou","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Tang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marion","family":"Schuller","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dmitri V.","family":"Filippov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1229-7908","authenticated-orcid":false,"given":"Qiang","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreja","family":"Mikoc","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dragana","family":"Ahel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9446-3756","authenticated-orcid":false,"given":"Ivan","family":"Ahel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.113682_bib1","doi-asserted-by":"crossref","first-page":"2366","DOI":"10.1016\/j.csbj.2021.04.023","article-title":"ADP-ribosylation systems in bacteria and viruses","volume":"19","author":"Mikol\u010devi\u0107","year":"2021","journal-title":"Comput Struct Biotechnol J"},{"key":"10.1016\/j.jbc.2026.113682_bib2","doi-asserted-by":"crossref","first-page":"4475","DOI":"10.1016\/j.cell.2023.08.030","article-title":"ADP-ribosylation from molecular mechanisms to therapeutic implications","volume":"186","author":"Suskiewicz","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib3","doi-asserted-by":"crossref","first-page":"313","DOI":"10.3390\/cells10020313","article-title":"MARTs and MARylation in the Cytosol: Biological Functions, Mechanisms of Action, and Therapeutic Potential","volume":"10","author":"Challa","year":"2021","journal-title":"Cells"},{"key":"10.1016\/j.jbc.2026.113682_bib4","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1016\/j.molcel.2015.06.006","article-title":"PARPs and ADP-Ribosylation: 50 Years and Counting","volume":"58","author":"Kraus","year":"2015","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib5","doi-asserted-by":"crossref","first-page":"7399","DOI":"10.1111\/febs.16142","article-title":"ADP-ribosyltransferases, an update on function and nomenclature","volume":"289","author":"L\u00fcscher","year":"2022","journal-title":"FEBS J"},{"key":"10.1016\/j.jbc.2026.113682_bib6","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1016\/j.chembiol.2018.11.001","article-title":"ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition","volume":"25","author":"Rack","year":"2018","journal-title":"Cell Chem Biol"},{"key":"10.1016\/j.jbc.2026.113682_bib7","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1101\/gad.334631.119","article-title":"(ADP-ribosyl)hydrolases: structure, function, and biology","volume":"34","author":"Rack","year":"2020","journal-title":"Genes Dev"},{"key":"10.1016\/j.jbc.2026.113682_bib8","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.dnarep.2014.05.003","article-title":"Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life","volume":"23","author":"Perina","year":"2014","journal-title":"DNA Repair (Amst)"},{"key":"10.1016\/j.jbc.2026.113682_bib9","doi-asserted-by":"crossref","first-page":"616","DOI":"10.1038\/nature10404","article-title":"The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase","volume":"477","author":"Slade","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113682_bib10","doi-asserted-by":"crossref","first-page":"8217","DOI":"10.1093\/nar\/gkad514","article-title":"Updated protein domain annotation of the PARP protein family sheds new light on biological function","volume":"51","author":"Suskiewicz","year":"2023","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib11","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.sbi.2018.11.002","article-title":"PARP family enzymes: regulation and catalysis of the poly(ADP-ribose) posttranslational modification","volume":"53","author":"Langelier","year":"2018","journal-title":"Curr Opin Struct Biol"},{"key":"10.1016\/j.jbc.2026.113682_bib12","doi-asserted-by":"crossref","first-page":"2116","DOI":"10.1128\/JVI.03443-13","article-title":"Interferon-stimulated poly(ADP-Ribose) polymerases are potent inhibitors of cellular translation and virus replication","volume":"88","author":"Atasheva","year":"2014","journal-title":"J Virol"},{"key":"10.1016\/j.jbc.2026.113682_bib13","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1101\/gad.353495.125","article-title":"Structure, function, regulation, evolution, and therapeutic implications of PARP14","volume":"40","author":"Kar","year":"2026","journal-title":"Genes Dev"},{"key":"10.1016\/j.jbc.2026.113682_bib14","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1007\/s00018-023-04717-8","article-title":"Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication","volume":"80","author":"Krieg","year":"2023","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.jbc.2026.113682_bib15","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1038\/s41586-020-2013-6","article-title":"HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation","volume":"579","author":"Suskiewicz","year":"2020","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113682_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.dnarep.2021.103144","article-title":"ADP-ribosylation of DNA and RNA","volume":"105","author":"Groslambert","year":"2021","journal-title":"DNA Repair (Amst)"},{"key":"10.1016\/j.jbc.2026.113682_bib17","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1038\/s41586-021-03825-4","article-title":"Molecular basis for DarT ADP-ribosylation of a DNA base","volume":"596","author":"Schuller","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113682_bib18","doi-asserted-by":"crossref","first-page":"10608","DOI":"10.1073\/pnas.96.19.10608","article-title":"Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: possible involvement of ADP-ribosylation in its activity","volume":"96","author":"Watanabe","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jbc.2026.113682_bib19","doi-asserted-by":"crossref","first-page":"1109","DOI":"10.1016\/j.molcel.2016.11.014","article-title":"The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA","volume":"64","author":"Jankevicius","year":"2016","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib20","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.adi2687","article-title":"PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities","volume":"9","author":"\u0110uki\u0107","year":"2023","journal-title":"Sci Adv"},{"key":"10.1016\/j.jbc.2026.113682_bib21","doi-asserted-by":"crossref","first-page":"5658","DOI":"10.1093\/nar\/gkz305","article-title":"Reversible ADP-ribosylation of RNA","volume":"47","author":"Munnur","year":"2019","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib22","doi-asserted-by":"crossref","first-page":"4002","DOI":"10.1111\/febs.14297","article-title":"Reversible mono-ADP-ribosylation of DNA breaks","volume":"284","author":"Munnur","year":"2017","journal-title":"FEBS J"},{"key":"10.1016\/j.jbc.2026.113682_bib23","first-page":"9279","article-title":"Poly(ADP-ribose) polymerases covalently modify strand break termini in DNA fragments in vitro","volume":"44","author":"Talhaoui","year":"2016","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib24","doi-asserted-by":"crossref","first-page":"3484","DOI":"10.1016\/j.molcel.2022.08.015","article-title":"An ADP-ribosyltransferase toxin kills bacterial cells by modifying structured non-coding RNAs","volume":"82","author":"Bullen","year":"2022","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib25","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkaf069","article-title":"Discovery of reversing enzymes for RNA ADP-ribosylation reveals a possible defence module against toxic attack","volume":"53","author":"Lu","year":"2025","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib26","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkag289","article-title":"Reversible RNA ADP-ribosylation on uracil bases","volume":"54","author":"Lu","year":"2026","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib27","doi-asserted-by":"crossref","first-page":"82","DOI":"10.3390\/toxins18020082","article-title":"ADP-Ribosylation of Cytidine: A Novel Nucleic Acid Modification Reversed by NADAR Hydrolases","volume":"18","author":"Mikol\u010devi\u0107","year":"2026","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.jbc.2026.113682_bib28","doi-asserted-by":"crossref","first-page":"6138","DOI":"10.1038\/s41467-022-33731-w","article-title":"Mammalian N1-adenosine PARylation is a reversible DNA modification","volume":"13","author":"Musheev","year":"2022","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib29","doi-asserted-by":"crossref","first-page":"2303","DOI":"10.1016\/j.molcel.2023.06.013","article-title":"Molecular basis for the reversible ADP-ribosylation of guanosine bases","volume":"83","author":"Schuller","year":"2023","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib30","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1038\/s41586-024-08102-8","article-title":"Anti-viral defence by an mRNA ADP-ribosyltransferase that blocks translation","volume":"636","author":"Vassallo","year":"2024","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113682_bib31","first-page":"3468","article-title":"Control of replication and gene expression by ADP-ribosylation of DNA in Mycobacterium tuberculosis","volume":"44","author":"Butler","year":"2025","journal-title":"EMBO J"},{"key":"10.1016\/j.jbc.2026.113682_bib32","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1038\/s41564-022-01153-5","article-title":"The DarTG toxin-antitoxin system provides phage defence by ADP-ribosylating viral DNA","volume":"7","author":"LeRoux","year":"2022","journal-title":"Nat Microbiol"},{"key":"10.1016\/j.jbc.2026.113682_bib33","doi-asserted-by":"crossref","first-page":"1373","DOI":"10.1016\/j.celrep.2020.01.014","article-title":"DNA ADP-Ribosylation Stalls Replication and Is Reversed by RecF-Mediated Homologous Recombination and Nucleotide Excision Repair","volume":"30","author":"Lawar\u00e9e","year":"2020","journal-title":"Cell Rep"},{"key":"10.1016\/j.jbc.2026.113682_bib34","doi-asserted-by":"crossref","first-page":"208","DOI":"10.3390\/toxins16050208","article-title":"Specificity of DNA ADP-Ribosylation Reversal by NADARs","volume":"16","author":"Cihlova","year":"2024","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.jbc.2026.113682_bib35","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1038\/emboj.2013.51","article-title":"Deficiency of terminal ADP\u2010ribose protein glycohydrolase TARG1\/C6orf130 in neurodegenerative disease","volume":"32","author":"Sharifi","year":"2013","journal-title":"EMBO J"},{"key":"10.1016\/j.jbc.2026.113682_bib36","doi-asserted-by":"crossref","first-page":"3646","DOI":"10.1182\/blood-2014-07-588046","article-title":"PARP-14 combines with tristetraprolin in the selective posttranscriptional control of macrophage tissue factor expression","volume":"124","author":"Iqbal","year":"2014","journal-title":"Blood"},{"key":"10.1016\/j.jbc.2026.113682_bib37","doi-asserted-by":"crossref","first-page":"4337","DOI":"10.1016\/j.csbj.2022.08.002","article-title":"Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA","volume":"20","author":"Hlou\u0161ek-Kasun","year":"2022","journal-title":"Comput Struct Biotechnol J"},{"key":"10.1016\/j.jbc.2026.113682_bib38","doi-asserted-by":"crossref","first-page":"2164","DOI":"10.1038\/ncomms3164","article-title":"Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities","volume":"4","author":"Barkauskaite","year":"2013","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib39","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.28533","article-title":"Serine ADP-ribosylation reversal by the hydrolase ARH3","volume":"6","author":"Fontana","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.jbc.2026.113682_bib40","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1146\/annurev-biochem-060815-014935","article-title":"Macrodomains: Structure, Function, Evolution, and Catalytic Activities","volume":"85","author":"Rack","year":"2016","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.jbc.2026.113682_bib41","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/s42003-025-07901-7","article-title":"Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase","volume":"8","author":"Weixler","year":"2025","journal-title":"Commun Biol"},{"key":"10.1016\/j.jbc.2026.113682_bib42","doi-asserted-by":"crossref","first-page":"14470","DOI":"10.1074\/jbc.RA118.004284","article-title":"Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation","volume":"293","author":"Wang","year":"2018","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2026.113682_bib43","doi-asserted-by":"crossref","first-page":"4270","DOI":"10.1021\/jacs.5c17532","article-title":"Chemical Synthesis of Native ADP-Ribosylated Oligonucleotides Enables Analysis of DNA ADP-Ribosylation Hydrolase Specificity","volume":"148","author":"Tang","year":"2026","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.jbc.2026.113682_bib44","doi-asserted-by":"crossref","first-page":"30836","DOI":"10.1021\/jacs.6c02874","article-title":"Deciphering the Specificity of Reversible DNA-Phosphate ADP-Ribosylation via the Precise Synthesis and Enzymatic Profiling of Nucleotide-Phospho-ADP-Ribosyl Probes","volume":"148","author":"Liu","year":"2026","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.jbc.2026.113682_bib45","doi-asserted-by":"crossref","first-page":"10477","DOI":"10.1093\/nar\/gkab771","article-title":"TARG1 protects against toxic DNA ADP-ribosylation","volume":"49","author":"Tromans-Coia","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib46","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1004403","article-title":"Rapid evolution of PARP genes suggests a broad role for ADP-ribosylation in host-virus conflicts","volume":"10","author":"Daugherty","year":"2014","journal-title":"PLoS Genet"},{"key":"10.1016\/j.jbc.2026.113682_bib47","doi-asserted-by":"crossref","first-page":"11892","DOI":"10.1073\/pnas.0601708103","article-title":"Crystal structure and mechanistic determinants of SARS coronavirus nonstructural protein 15 define an endoribonuclease family","volume":"103","author":"Ricagno","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jbc.2026.113682_bib48","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1038\/nature07106","article-title":"Innate immunity induced by composition-dependent RIG-I recognition of hepatitis C virus RNA","volume":"454","author":"Saito","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.113682_bib49","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002839","article-title":"Uridine composition of the poly-U\/UC tract of HCV RNA defines non-self recognition by RIG-I","volume":"8","author":"Schnell","year":"2012","journal-title":"PLoS Pathog"},{"key":"10.1016\/j.jbc.2026.113682_bib50","doi-asserted-by":"crossref","first-page":"3200","DOI":"10.1038\/s41467-023-38793-y","article-title":"Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling","volume":"14","author":"Fontana","year":"2023","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib51","doi-asserted-by":"crossref","first-page":"4140","DOI":"10.1021\/acs.orglett.8b01742","article-title":"Synthetic \u03b1- and \u03b2-Ser-ADP-ribosylated Peptides Reveal \u03b1-Ser-ADPr as the Native Epimer","volume":"20","author":"Voorneveld","year":"2018","journal-title":"Org Lett"},{"key":"10.1016\/j.jbc.2026.113682_bib52","doi-asserted-by":"crossref","first-page":"3845","DOI":"10.1242\/jcs.193375","article-title":"The role of ADP-ribosylation in regulating DNA interstrand crosslink repair","volume":"129","author":"Gunn","year":"2016","journal-title":"J Cell Sci"},{"key":"10.1016\/j.jbc.2026.113682_bib53","doi-asserted-by":"crossref","first-page":"1911","DOI":"10.1038\/sj.emboj.7600664","article-title":"The macro domain is an ADP-ribose binding module","volume":"24","author":"Karras","year":"2005","journal-title":"EMBO J"},{"key":"10.1016\/j.jbc.2026.113682_bib54","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/j.molcel.2015.06.013","article-title":"Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens","volume":"59","author":"Rack","year":"2015","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib55","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1042\/BJ20141554","article-title":"Processing of protein ADP-ribosylation by Nudix hydrolases","volume":"468","author":"Palazzo","year":"2015","journal-title":"Biochem J"},{"key":"10.1016\/j.jbc.2026.113682_bib56","doi-asserted-by":"crossref","unstructured":"Musheev, M., Siefert, J., Bauten, W., B\u00fctepage, M., L\u00fcscher, B., Niehrs, C., Feijs-\u017daja, K. L. H., and \u017daja, R. (2026) Human PARPs modify RNA nucleobases in vitro and in cells. 10.64898\/2026.03.31.715305","DOI":"10.2139\/ssrn.6584065"},{"key":"10.1016\/j.jbc.2026.113682_bib57","doi-asserted-by":"crossref","first-page":"9567","DOI":"10.1038\/s41467-025-65315-9","article-title":"Regulation of ADP-ribosyltransferase activity by ART domain dimerization in PARP15","volume":"16","author":"Ebenwaldner","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib58","doi-asserted-by":"crossref","first-page":"4426","DOI":"10.1038\/ncomms5426","article-title":"Family-wide analysis of poly(ADP-ribose) polymerase activity","volume":"5","author":"Vyas","year":"2014","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib59","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1038\/s41597-025-04722-5","article-title":"Comprehensive dataset of interactors for the entire PARP family using TurboID proximity labeling","volume":"12","author":"Zheng","year":"2025","journal-title":"Sci Data"},{"key":"10.1016\/j.jbc.2026.113682_bib60","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1126\/science.1074276","article-title":"Inhibition of retroviral RNA production by ZAP, a CCCH-type zinc finger protein","volume":"297","author":"Gao","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.113682_bib61","first-page":"2929","article-title":"PARP14 and PARP9\/DTX3L regulate interferon-induced ADP-ribosylation","volume":"43","author":"Kar","year":"2024","journal-title":"EMBO J"},{"key":"10.1016\/j.jbc.2026.113682_bib62","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1186\/1476-4598-13-125","article-title":"DTX3L and ARTD9 inhibit IRF1 expression and mediate in cooperation with ARTD8 survival and proliferation of metastatic prostate cancer cells","volume":"13","author":"Bachmann","year":"2014","journal-title":"Mol Cancer"},{"key":"10.1016\/j.jbc.2026.113682_bib63","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1016\/j.molcel.2017.01.003","article-title":"Serine ADP-Ribosylation Depends on HPF1","volume":"65","author":"Bonfiglio","year":"2017","journal-title":"Mol Cell"},{"key":"10.1016\/j.jbc.2026.113682_bib64","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1016\/j.bbagrm.2013.02.003","article-title":"Tristetraprolin (TTP): interactions with mRNA and proteins, and current thoughts on mechanisms of action","volume":"1829","author":"Brooks","year":"2013","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jbc.2026.113682_bib65","doi-asserted-by":"crossref","first-page":"2935","DOI":"10.1073\/pnas.1808696116","article-title":"Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM","volume":"116","author":"Ripin","year":"2019","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jbc.2026.113682_bib66","doi-asserted-by":"crossref","first-page":"4738","DOI":"10.1093\/nar\/gkab202","article-title":"Molecular mechanism of RNase R substrate sensitivity for RNA ribose methylation","volume":"49","author":"Abula","year":"2021","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib67","doi-asserted-by":"crossref","unstructured":"Humolli, D., Ransome, J., Piel, D., Veening, J.-W., and Harms, A. (2025) Systematic mapping of bacteriophage gene essentiality with HIDEN-SEQ. 10.1101\/2025.11.20.689424","DOI":"10.1101\/2025.11.20.689424"},{"key":"10.1016\/j.jbc.2026.113682_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2026.117219","article-title":"The phage nucleus synergizes with an anti-defense protein to resist bacterial immunity","volume":"45","author":"Morgan","year":"2026","journal-title":"Cell Rep"},{"key":"10.1016\/j.jbc.2026.113682_bib69","doi-asserted-by":"crossref","first-page":"1598","DOI":"10.1038\/s41467-025-56887-7","article-title":"Phages carry orphan antitoxin-like enzymes to neutralize the DarTG1 toxin-antitoxin defense system","volume":"16","author":"Johannesman","year":"2025","journal-title":"Nat Commun"},{"key":"10.1016\/j.jbc.2026.113682_bib70","doi-asserted-by":"crossref","unstructured":"Musheev, M. U., Schomacher, L., Schott, J. M., Basu, A., M\u00f6ckel, M. M., Heinen, S., Frosch, L., Guo, P., Yang, G., Huang, Q., and Niehrs, C. (2025) PARP1 Writes N3-Cytidine ADP-Ribosylation in DNA. 10.64898\/2025.12.18.695099","DOI":"10.64898\/2025.12.18.695099"},{"key":"10.1016\/j.jbc.2026.113682_bib71","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/j.celrep.2015.12.045","article-title":"Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach","volume":"14","author":"Carter-O\u2019Connell","year":"2016","journal-title":"Cell Rep"},{"key":"10.1016\/j.jbc.2026.113682_bib72","doi-asserted-by":"crossref","first-page":"23175","DOI":"10.1074\/jbc.M116.721894","article-title":"Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor","volume":"291","author":"Lali\u0107","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jbc.2026.113682_bib73","doi-asserted-by":"crossref","first-page":"14000","DOI":"10.1021\/jacs.3c03771","article-title":"Chemoenzymatic and Synthetic Approaches To Investigate Aspartate- and Glutamate-ADP-Ribosylation","volume":"145","author":"Tashiro","year":"2023","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.jbc.2026.113682_bib74","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/978-1-0716-2891-1_8","article-title":"A Simple Method to Study ADP-Ribosylation Reversal: From Function to Drug Discovery","volume":"2609","author":"Rack","year":"2023","journal-title":"Methods Mol Biol"},{"key":"10.1016\/j.jbc.2026.113682_bib75","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1093\/nar\/gkm960","article-title":"The Pfam protein families database","volume":"36","author":"Finn","year":"2008","journal-title":"Nucleic Acids Res"},{"key":"10.1016\/j.jbc.2026.113682_bib76","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1093\/molbev\/msn067","article-title":"An improved general amino acid replacement matrix","volume":"25","author":"Le","year":"2008","journal-title":"Mol Biol Evol"},{"key":"10.1016\/j.jbc.2026.113682_bib77","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1093\/molbev\/msy096","article-title":"MEGA X: Molecular Evolutionary Genetics Analysis across Computing Platforms","volume":"35","author":"Kumar","year":"2018","journal-title":"Mol Biol Evol"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826025548?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826025548?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T20:09:22Z","timestamp":1792786162000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826025548"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":77,"alternative-id":["S0021925826025548"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113682","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification of Novel Enzymes Regulating ADP-Ribosylation of Uracil and Thymine in Nucleic Acids","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.113682","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"113682"}}