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The entries in ADPriboDB are curated from the scientific literature on ADP-ribosylation of proteins since 1975. Over 9,000 modified proteins were found in a total of 610 papers. The majority of entries were identified as poly(ADP-ribosyl)ated, while only a few hundred entries were identified as mono(ADP-ribosyl)ated. Furthermore, the majority of papers only identified one modified protein and the majority of proteins were only identified as modified once.
The database includes a variety of information for each entry, including any drug treatments performed to obtain the identification of the modification, cell lines and species, the ADP-ribosyltransferases responsible for synthesizing the modification (if known), as well as the site of modification (if identified). Furthermore, the PMID of the journal article, and text citing the figure, table, or supplementary data are included for each entry, enriching every search by allowing the viewer to refer back to the literature and analyze the original data. Through ADPriboDB, we aim to provide the scientific community with a valuable tool for further analyzing ADP-ribosylation, cross talk with other post-translational modifications, and possible protein interaction networks. New in 2020 Since its creation in 2016, ADPriboDB has received over 26,455 unique visitors and over 1 million hits. This is a testament to the utility of repositories of data regarding protein modifications in general, and in particular to growing interest in ADP-ribosylation among scientists and clinicians. This growing body of users stands to benefit from the latest developments in our website, which include an expanded library of data as well as improved functionality. Over the past three years, we have more-than doubled the size of our database while adding several new features. The inclusion of information regarding the sites of ADP-ribosylation for over 48,000 database entries will facilitate new analyses, particularly those that seek to correlate sites of ADP-ribosylation to those of other protein modifications, such as phosphorylation. To this end, we have integrated data regarding other post-translational modifications including methylation, phosphorylation, and ubiquitination. Cover photo credit: Kinoshita, T., et al. Inhibitor-induced structural change of the active site of human poly(ADP-ribose) polymerase. FEBS Lett. 566: 43-46, 2004. |
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