{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T09:44:45Z","timestamp":1791884685503,"version":"4.3.4"},"reference-count":118,"publisher":"Oxford University Press (OUP)","issue":"19","license":[{"start":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T00:00:00Z","timestamp":1791849600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000001","name":"NSF","doi-asserted-by":"publisher","award":["#2153787"],"award-info":[{"award-number":["#2153787"]}],"id":[{"id":"10.13039\/100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"NIH","doi-asserted-by":"publisher","award":["R01 GM150642"],"award-info":[{"award-number":["R01 GM150642"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013678","name":"University of Colorado Cancer Center","doi-asserted-by":"publisher","award":["P30 CA046934"],"award-info":[{"award-number":["P30 CA046934"]}],"id":[{"id":"10.13039\/100013678","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Biomedical Research","award":["S10 OD025020"],"award-info":[{"award-number":["S10 OD025020"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,13]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>ZBP1 senses foreign nucleic acids in the unusual, left-handed Z-conformation via binding through its Z\u03b11 and Z\u03b12 domains and initiates cell death pathways that enable viral clearance. dsDNA and dsRNA can adopt Z-conformations; however, both typically require chemical modifications or protein binding to induce Z-form conversion and stabilization. ZBP1 has been previously shown to bind and convert B-DNA to the Z-conformation and was assumed to be able to convert A-RNA as well, despite the lack of experimental validation. Here, we use NMR and other biophysical and biochemical experiments to characterize the Z-DNA and Z-RNA binding properties of ZBP1\u2019s Z\u03b11 and Z\u03b12 domains. While ZBP1\u2019s Z\u03b1 domains are able to convert and stabilize unmodified dsDNA in the Z-conformation, they are incapable of flipping unmodified (CpG)n repeat dsRNA. ZBP1\u2019s Z\u03b1 domains require dsRNAs with Z-promoting chemical modifications to be able to bind and stabilize the Z-conformation. These results contrast with ADAR1\u2019s Z\u03b1 domain, which can bind and flip both dsDNA and dsRNA into the Z-conformation, potentially indicating finely tuned competition between ADAR1 and ZBP1 for pro-survival and pro-death outcomes, respectively. This work highlights the functional variability of Z\u03b1 domains and narrows down potential physiological substrates of ZBP1 in infection and disease.<\/jats:p>","DOI":"10.1093\/nar\/gkag972","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T11:42:20Z","timestamp":1790682140000},"source":"Crossref","is-referenced-by-count":0,"title":["ZBP1 specifically binds pre-formed Z-RNA, limiting its potential pool of nucleic acid ligands compared to ADAR1"],"prefix":"10.1093","volume":"54","author":[{"given":"Jeffrey B","family":"Krall","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lily G","family":"Beck","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Parker J","family":"Nichols","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]},{"name":"Department of Biochemistry, University of Utah School of Medicine , Salt Lake City, UT 84112 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robb","family":"Welty","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Quentin","family":"Vicens","sequence":"additional","affiliation":[{"name":"Department of Biology and Biochemistry, Center for Nuclear Receptors and Cell Signaling, University of Houston , Houston, TX 77204 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4835-5583","authenticated-orcid":false,"given":"Morkos A","family":"Henen","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1176-3137","authenticated-orcid":false,"given":"Beat","family":"V\u00f6geli","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United States"]},{"name":"RNA Bioscience Initiative, University of Colorado Anschutz Medical Campus , Aurora, CO 80045 ,","place":["United 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