{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T23:02:08Z","timestamp":1776294128071,"version":"3.50.1"},"reference-count":42,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2020,7,16]],"date-time":"2020-07-16T00:00:00Z","timestamp":1594857600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31722056"],"award-info":[{"award-number":["31722056"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2020,7,16]]},"abstract":"<jats:p>\n            Porcine reproductive and respiratory syndrome virus (PRRSV) is a major respiratory disease agent in pigs that causes enormous economic losses to the global swine industry. PRRSV helicase nsp10 is a multifunctional protein with translocation and unwinding activities and plays a vital role in viral RNA synthesis. Here, we report the first structure of full-length nsp10 from the arterivirus PRRSV at 3.0-\u00c5 resolution. Our results show that the 1B domain of PRRSV nsp10 adopts a novel open state and has a unique C-terminal domain structure, which plays a crucial role in nsp10 helicase activity. Furthermore, mutagenesis and structural analysis revealed conservation of the helicase catalytic domain across the order\n            <jats:italic>Nidovirales<\/jats:italic>\n            (families\n            <jats:italic>Arteriviridae<\/jats:italic>\n            and\n            <jats:italic>Coronaviridae<\/jats:italic>\n            ). Importantly, our results will provide a structural basis for further understanding the function of helicases in the order\n            <jats:italic>Nidovirales<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jvi.02158-19","type":"journal-article","created":{"date-parts":[[2020,5,25]],"date-time":"2020-05-25T13:17:41Z","timestamp":1590412661000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":18,"title":["Structural Characterization of the Helicase nsp10 Encoded by Porcine Reproductive and Respiratory Syndrome Virus"],"prefix":"10.1128","volume":"94","author":[{"given":"Yuejun","family":"Shi","sequence":"first","affiliation":[{"name":"State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China"},{"name":"Key Laboratory of Preventive Veterinary Medicine in Hubei Province, The Cooperative Innovation Center for Sustainable Pig 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