{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T01:43:50Z","timestamp":1793065430814,"version":"4.5.0"},"reference-count":35,"publisher":"Oxford University Press (OUP)","issue":"D1","license":[{"start":{"date-parts":[[2020,11,2]],"date-time":"2020-11-02T00:00:00Z","timestamp":1604275200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000048","name":"American Cancer Society","doi-asserted-by":"publisher","award":["129539-RSG-16\u2013062-01-RMC"],"award-info":[{"award-number":["129539-RSG-16\u2013062-01-RMC"]}],"id":[{"id":"10.13039\/100000048","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01-GM104135"],"award-info":[{"award-number":["R01-GM104135"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000054","name":"National Cancer Institute","doi-asserted-by":"publisher","award":["T32CA009110"],"award-info":[{"award-number":["T32CA009110"]}],"id":[{"id":"10.13039\/100000054","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,1,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>ADP-ribosylation is a protein modification responsible for biological processes such as DNA repair, RNA regulation, cell cycle and biomolecular condensate formation. Dysregulation of ADP-ribosylation is implicated in cancer, neurodegeneration and viral infection. We developed ADPriboDB (adpribodb.leunglab.org) to facilitate studies in uncovering insights into the mechanisms and biological significance of ADP-ribosylation. ADPriboDB 2.0 serves as a one-stop repository comprising 48\u00a0346 entries and 9097 ADP-ribosylated proteins, of which 6708 were newly identified since the original database release. In this updated version, we provide information regarding the sites of ADP-ribosylation in 32\u00a0946 entries. The wealth of information allows us to interrogate existing databases or newly available data. For example, we found that ADP-ribosylated substrates are significantly associated with the recently identified human protein interaction networks associated with SARS-CoV-2, which encodes a conserved protein domain called macrodomain that binds and removes ADP-ribosylation. In addition, we create a new interactive tool to visualize the local context of ADP-ribosylation, such as structural and functional features as well as other post-translational modifications (e.g. phosphorylation, methylation and ubiquitination). This information provides opportunities to explore the biology of ADP-ribosylation and generate new hypotheses for experimental testing.<\/jats:p>","DOI":"10.1093\/nar\/gkaa941","type":"journal-article","created":{"date-parts":[[2020,10,31]],"date-time":"2020-10-31T08:11:43Z","timestamp":1604131903000},"page":"D261-D265","source":"Crossref","is-referenced-by-count":52,"title":["ADPriboDB 2.0: an updated database of ADP-ribosylated proteins"],"prefix":"10.1093","volume":"49","author":[{"given":"Vinay","family":"Ayyappan","sequence":"first","affiliation":[{"name":"Department of Biomedical Engineering, The G.W.C. Whiting School of Engineering, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricky","family":"Wat","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Calvin","family":"Barber","sequence":"additional","affiliation":[{"name":"Department of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina A","family":"Vivelo","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kathryn","family":"Gauch","sequence":"additional","affiliation":[{"name":"Department of Biology, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pat","family":"Visanpattanasin","sequence":"additional","affiliation":[{"name":"Department of Biology, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garth","family":"Cook","sequence":"additional","affiliation":[{"name":"Department of Biology, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, MD 21218, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christos","family":"Sazeides","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5569-4036","authenticated-orcid":false,"given":"Anthony K L","family":"Leung","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA"},{"name":"Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA"},{"name":"Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,11,2]]},"reference":[{"key":"2021010313133853600_B1","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1101\/gad.291518.116","article-title":"PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes","volume":"31","author":"Gupte","year":"2017","journal-title":"Genes Dev."},{"key":"2021010313133853600_B2","doi-asserted-by":"crossref","first-page":"2932","DOI":"10.1111\/febs.14078","article-title":"ADP-ribosylation: new facets of an ancient modification","volume":"284","author":"Palazzo","year":"2017","journal-title":"FEBS J."},{"key":"2021010313133853600_B3","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1038\/nrm3293","article-title":"Sirtuins as regulators of metabolism and healthspan","volume":"13","author":"Houtkooper","year":"2012","journal-title":"Nat. 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