{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T21:07:13Z","timestamp":1791407233548,"version":"4.3.3"},"reference-count":32,"publisher":"American Society for Microbiology","issue":"14","license":[{"start":{"date-parts":[[2009,7,15]],"date-time":"2009-07-15T00:00:00Z","timestamp":1247616000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2009,7,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Diverse members of the\n            <jats:italic>Paramyxovirus<\/jats:italic>\n            family of negative-strand RNA viruses effectively suppress host innate immune responses through the actions of their V proteins. The V protein mediates interference with the interferon regulatory RNA helicase MDA5 to avoid cellular antiviral responses. Analysis of the interaction interface revealed the MDA5 helicase C domain as necessary and sufficient for association with V proteins from human parainfluenza virus type 2, parainfluenza virus type 5, measles virus, mumps virus, Hendra virus, and Nipah virus. The identified \u223c130-residue region is highly homologous between MDA5 and the related antiviral helicase LGP2, but not RIG-I. Results indicate that the paramyxovirus V proteins can also associate with LGP2. The V protein interaction was found to disrupt ATP hydrolysis mediated by both MDA5 and LGP2. These findings provide a potential mechanistic basis for V protein-mediated helicase interference and identify LGP2 as a second cellular RNA helicase targeted by paramyxovirus V proteins.\n          <\/jats:p>","DOI":"10.1128\/jvi.00153-09","type":"journal-article","created":{"date-parts":[[2009,4,30]],"date-time":"2009-04-30T00:45:28Z","timestamp":1241052328000},"page":"7252-7260","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":116,"title":["A Shared Interface Mediates Paramyxovirus Interference with Antiviral RNA Helicases MDA5 and LGP2"],"prefix":"10.1128","volume":"83","author":[{"given":"Jean-Patrick","family":"Parisien","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 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