{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T12:51:31Z","timestamp":1791204691696,"version":"4.2.0"},"reference-count":86,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T00:00:00Z","timestamp":1791158400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100004012","name":"Jane ja Aatos Erkon S\u00e4\u00e4ti\u00f6","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004012","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006306","name":"Sigrid Jus\u00e9liuksen S\u00e4\u00e4ti\u00f6","doi-asserted-by":"publisher","award":["220094 and 250122"],"award-info":[{"award-number":["220094 and 250122"]}],"id":[{"id":"10.13039\/501100006306","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100020019","name":"Biocenter, University of Oulu","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100020019","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"abstract":"<jats:p>\n                    PARP proteins are enzymes catalyzing ADP\u2010ribosylation, a well\u2010conserved post\u2010translational modification. In addition to the catalytic domain present in all PARPs, these proteins have a wide variety of other domains possessing different functions. Additional domains present in human PARP15 are macrodomains, capable of binding ADP\u2010ribose. PARP15 is the least studied of the macrodomain\u2010containing human PARPs, and it is linked to different diseases from infections to cancer. We show that the full\u2010length canonical isoform 1 of PARP15 auto\u2010ADP\u2010ribosylates robustly on glutamate and aspartate residues, from which the modification can be hydrolyzed by known ADP\u2010ribosylhydrolases. We have been able to locate several modification sites in the region of tandem macrodomains. Consistent with previous findings that the catalytic domain dimerization is necessary for enzymatic activity, we confirm this in the full\u2010length context with the recombinant isoform 1 of PARP15. We show that dimerization is required for the efficient substrate NAD\n                    <jats:sup>+<\/jats:sup>\n                    binding, and we provide structural basis for this requirement with the help of a co\u2010crystal structure of the catalytic domain dimer with an unhydrolyzable substrate analog.\n                  <\/jats:p>","DOI":"10.1111\/febs.70758","type":"journal-article","created":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T11:58:58Z","timestamp":1791201538000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Dimerization of human\n                    <scp>PARP15<\/scp>\n                    is required for\n                    <scp>NAD<\/scp>\n                    <sup>+<\/sup>\n                    binding and automodification"],"prefix":"10.1111","author":[{"given":"Anna","family":"Tuovinen","sequence":"first","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Johan","family":"P\u00e4\u00e4kk\u00f6nen","sequence":"additional","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirko M.","family":"Maksimainen","sequence":"additional","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lea","family":"Hirschen","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology, Medical School of the RWTH Aachen University  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heli I.","family":"Hentil\u00e4","sequence":"additional","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie","family":"Tauscher","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology, Medical School of the RWTH Aachen University  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9622-8709","authenticated-orcid":false,"given":"Bernhard","family":"L\u00fcscher","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology, Medical School of the RWTH Aachen University  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"Vela\u2010Rodr\u00edguez","sequence":"additional","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia","family":"Korn","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology, Medical School of the RWTH Aachen University  Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7250-832X","authenticated-orcid":false,"given":"Lari","family":"Lehti\u00f6","sequence":"additional","affiliation":[{"name":"Faculty of Biochemistry and Molecular Medicine &amp; Biocenter Oulu University of Oulu  Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,10,5]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"crossref","first-page":"7399","DOI":"10.1111\/febs.16142","article-title":"ADP\u2010ribosyltransferases, an update on function and nomenclature","volume":"289","author":"L\u00fcscher B","year":"2022","journal-title":"FEBS 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