{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T15:54:30Z","timestamp":1790783670700,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T00:00:00Z","timestamp":1790467200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T00:00:00Z","timestamp":1790467200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/100013262","name":"State Key Laboratory of Respiratory Disease","doi-asserted-by":"publisher","award":["SKLRD\u2010Z\u2010202502"],"award-info":[{"award-number":["SKLRD\u2010Z\u2010202502"]}],"id":[{"id":"10.13039\/100013262","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["advanced.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Advanced Science"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Influenza A virus (IAV) commandeers host transcriptional machinery to replicate, but mechanisms remain elusive. CRISPR screen identifies PARP1 as a proviral factor that binds viral NS1. ATAC\u2011seq reveals IAV drives PARP1\u2011dependent chromatin remodeling at promoter\u2011proximal regions (\u2212100 to +300 bp), linking PARP1 to viral RNA synthesis. Mechanistically, NS1 engages PARP1's helical domain (HD), which alone forms large, irregular condensates with low fluidity, acting as a built\u2011in rheostat. HD deletion confers high droplet mobility, whereas NS1 binding locks PARP1 into a hyper\u2011condensed, gel\u2011like state. This phase transition traps Pol II in prolonged pause by enriching pausing factors (SPT5\n                    <jats:sup>\u2011PLD<\/jats:sup>\n                    , NELFA, NELFE) and excluding release factors (SPT5\n                    <jats:sup>\u2011PRD<\/jats:sup>\n                    , AFF4). The paused environment is hijacked for efficient cap\u2011snatching and viral RNA synthesis. This proviral activity is independent of PARP1's polymerase activity, revealing a non\u2011canonical mechanism that complements recent reports of PARP1\u2011mediated antiviral ADP\u2011ribosylation. Targeting this phase transition, we identify tectochrysin (TEC) and isoferulic acid (IFA), which restore fluidity, reverse pausing, and suppress IAV in mice and lung organoids without toxicity. Our work establishes that NS1 coopts PARP1 phase separation via the HD rheostat to prolong transcriptional pausing, introducing \u2018phase transition correction\u2019 as an antiviral paradigm.\n                  <\/jats:p>","DOI":"10.1002\/advs.77883","type":"journal-article","created":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T18:00:31Z","timestamp":1790532031000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["NS1\u2010Induced PARP1 Phase Transitions Prolongs Host Transcriptional Pausing to Promote Influenza A Virus Replication"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5903-1501","authenticated-orcid":false,"given":"Shufeng","family":"Ma","sequence":"first","affiliation":[{"name":"State Key Laboratory of Respiratory Disease National Clinical Research Center for Respiratory Disease National Center for Respiratory Medicine Guangzhou Institute of Respiratory Health The First 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