{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T16:43:26Z","timestamp":1790613806848,"version":"4.1.0"},"reference-count":375,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2021,3,22]],"date-time":"2021-03-22T00:00:00Z","timestamp":1616371200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>The threat of a new influenza pandemic is real. With past pandemics claiming millions of lives, finding new ways to combat this virus is essential. Host cells have developed a multi-modular system to detect incoming pathogens, a phenomenon called sensing. The signaling cascade triggered by sensing subsequently induces protection for themselves and their surrounding neighbors, termed interferon (IFN) response. This response induces the upregulation of hundreds of interferon-stimulated genes (ISGs), including antiviral effectors, establishing an antiviral state. As well as the antiviral proteins induced through the IFN system, cells also possess a so-called intrinsic immunity, constituted of antiviral proteins that are constitutively expressed, creating a first barrier preceding the induction of the interferon system. All these combined antiviral effectors inhibit the virus at various stages of the viral lifecycle, using a wide array of mechanisms. Here, we provide a review of mammalian and avian influenza A restriction factors, detailing their mechanism of action and in vivo relevance, when known. Understanding their mode of action might help pave the way for the development of new influenza treatments, which are absolutely required if we want to be prepared to face a new pandemic.<\/jats:p>","DOI":"10.3390\/v13030522","type":"journal-article","created":{"date-parts":[[2021,3,22]],"date-time":"2021-03-22T12:55:07Z","timestamp":1616417707000},"page":"522","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Mammalian and Avian Host Cell Influenza A Restriction Factors"],"prefix":"10.3390","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5440-2879","authenticated-orcid":false,"given":"Joe","family":"McKellar","sequence":"first","affiliation":[{"name":"Institut de Recherche en Infectiologie de Montpellier, CNRS, Universit\u00e9 de Montpellier, CEDEX 5, 34293 Montpellier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8913-837X","authenticated-orcid":false,"given":"Antoine","family":"Rebendenne","sequence":"additional","affiliation":[{"name":"Institut de Recherche en Infectiologie de Montpellier, CNRS, Universit\u00e9 de Montpellier, CEDEX 5, 34293 Montpellier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4200-0079","authenticated-orcid":false,"given":"M\u00e9lanie","family":"Wencker","sequence":"additional","affiliation":[{"name":"Centre International de Recherche en Infectiologie, INSERM\/CNRS\/UCBL1\/ENS de Lyon, 69007 Lyon, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0512-1824","authenticated-orcid":false,"given":"Olivier","family":"Moncorg\u00e9","sequence":"additional","affiliation":[{"name":"Institut de Recherche en Infectiologie de Montpellier, CNRS, Universit\u00e9 de Montpellier, CEDEX 5, 34293 Montpellier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8571-1108","authenticated-orcid":false,"given":"Caroline","family":"Goujon","sequence":"additional","affiliation":[{"name":"Institut de Recherche en Infectiologie de Montpellier, CNRS, Universit\u00e9 de Montpellier, CEDEX 5, 34293 Montpellier, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2021,3,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Asha, K., and Kumar, B. (2019). Emerging Influenza D Virus Threat: What We Know so Far!. J. Clin. Med., 8.","DOI":"10.3390\/jcm8020192"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1128\/mr.56.1.152-179.1992","article-title":"Evolution and ecology of influenza A viruses","volume":"56","author":"Webster","year":"1992","journal-title":"Microbiol. Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2990","DOI":"10.1128\/JVI.03146-14","article-title":"Influenza Virus Reservoirs and Intermediate Hosts: Dogs, Horses, and New Possibilities for Influenza Virus Exposure of Humans","volume":"89","author":"Parrish","year":"2015","journal-title":"J. Virol."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Tong, S., Zhu, X., Li, Y., Shi, M., Zhang, J., Bourgeois, M., Yang, H., Chen, X., Recuenco, S., and Gomez, J. (2013). New World Bats Harbor Diverse Influenza A Viruses. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003657"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"a038612","DOI":"10.1101\/cshperspect.a038612","article-title":"Bat-Borne Influenza A Viruses: An Awakening","volume":"11","author":"Ciminski","year":"2021","journal-title":"Cold Spring Harb. Perspect. Med."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1038\/s41572-018-0002-y","article-title":"Influenza","volume":"4","author":"Krammer","year":"2018","journal-title":"Nat. Rev. Dis. Prim."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.3389\/fimmu.2019.01400","article-title":"Recalling the Future: Immunological Memory Toward Unpredictable Influenza Viruses","volume":"10","author":"Auladell","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1038\/nrmicro1027","article-title":"Evidence of an absence: The genetic origins of the 1918 pandemic influenza virus","volume":"2","author":"Reid","year":"2004","journal-title":"Nat. Rev. Genet."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1056\/NEJMp0904819","article-title":"The Persistent Legacy of the 1918 Influenza Virus","volume":"361","author":"Morens","year":"2009","journal-title":"N. Engl. J. Med."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1126\/science.1176225","article-title":"Antigenic and Genetic Characteristics of Swine-Origin 2009 A(H1N1) Influenza Viruses Circulating in Humans","volume":"325","author":"Garten","year":"2009","journal-title":"Science"},{"key":"ref_11","first-page":"334","article-title":"Recent human influenza A (H1N1) viruses are closely related genetically to strains isolated in 1950","volume":"274","author":"Nakajima","year":"1978","journal-title":"Nat. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1272","DOI":"10.1126\/science.1187816","article-title":"Permissive Secondary Mutations Enable the Evolution of Influenza Oseltamivir Resistance","volume":"328","author":"Bloom","year":"2010","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1001\/jama.295.8.joc60020","article-title":"Adamantane Resistance Among Influenza A Viruses Isolated Early During the 2005-2006 Influenza Season in the United States","volume":"295","author":"Bright","year":"2006","journal-title":"JAMA"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"11613","DOI":"10.1073\/pnas.1811345115","article-title":"The mechanism of resistance to favipiravir in influenza","volume":"115","author":"Goldhill","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"9633","DOI":"10.1038\/s41598-018-27890-4","article-title":"Characterization of influenza virus variants induced by treatment with the endonuclease inhibitor baloxavir marboxil","volume":"8","author":"Omoto","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_16","first-page":"426","article-title":"Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid","volume":"333","author":"Weis","year":"1988","journal-title":"Nat. Cell Biol."},{"key":"ref_17","first-page":"1","article-title":"On the Mechanism Underlying Initiation of Influenza Virus Infection","volume":"32","author":"Gottschalk","year":"1959","journal-title":"Ergeb. Mikrobiol. Immun. Exp. Ther."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1006\/viro.1997.8580","article-title":"Avian Influenza A Viruses Differ from Human Viruses by Recognition of Sialyloligosaccharides and Gangliosides and by a Higher Conservation of the HA Receptor-Binding Site","volume":"233","author":"Matrosovich","year":"1997","journal-title":"Virology"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"28403","DOI":"10.1074\/jbc.R110.129809","article-title":"Influenza Hemagglutinin and Neuraminidase Membrane Glycoproteins","volume":"285","author":"Gamblin","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/nsmb769","article-title":"Assembly of endocytic machinery around individual influenza viruses during viral entry","volume":"11","author":"Rust","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"11790","DOI":"10.1073\/pnas.0803711105","article-title":"Epsin 1 is a cargo-specific adaptor for the clathrin-mediated endocytosis of the influenza virus","volume":"105","author":"Chen","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"De Vries, E., Tscherne, D.M., Wienholts, M.J., Cobos-Jim\u00e9nez, V., Scholte, F., Garc\u00eda-Sastre, A., Rottier, P.J.M., and De Haan, C.A.M. (2011). Dissection of the Influenza A Virus Endocytic Routes Reveals Macropinocytosis as an Alternative Entry Pathway. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1001329"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/0092-8674(92)90219-3","article-title":"Unpacking the incoming influenza virus","volume":"69","author":"Helenius","year":"1992","journal-title":"Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"8997","DOI":"10.1074\/jbc.R500020200","article-title":"The M2 Proton Channels of Influenza A and B Viruses","volume":"281","author":"Pinto","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1447","DOI":"10.1016\/j.bpj.2014.02.018","article-title":"pH-Controlled Two-Step Uncoating of Influenza Virus","volume":"106","author":"Li","year":"2014","journal-title":"Biophys. J."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1146\/annurev.biochem.69.1.531","article-title":"Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin","volume":"69","author":"Skehel","year":"2000","journal-title":"Annu. Rev. Biochem."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"5172","DOI":"10.1128\/JVI.02430-10","article-title":"Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin","volume":"85","author":"Xu","year":"2011","journal-title":"J. Virol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1111\/j.1600-0854.2005.00263.x","article-title":"An Unconventional NLS is Critical for the Nuclear Import of the Influenza A Virus Nucleoprotein and Ribonucleoprotein","volume":"6","author":"Cros","year":"2005","journal-title":"Traffic"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1038\/nrmicro3367","article-title":"At the centre: Influenza A virus ribonucleoproteins","volume":"13","author":"Eisfeld","year":"2015","journal-title":"Nat. Rev. Genet."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1016\/0092-8674(81)90449-9","article-title":"A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription","volume":"23","author":"Plotch","year":"1981","journal-title":"Cell"},{"key":"ref_31","first-page":"914","article-title":"The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit","volume":"458","author":"Dias","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1038\/nrmicro.2016.87","article-title":"Influenza virus RNA polymerase: Insights into the mechanisms of viral RNA synthesis","volume":"14","author":"Velthuis","year":"2016","journal-title":"Nat. Rev. Genet."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.virusres.2017.01.013","article-title":"Structural insights into RNA synthesis by the influenza virus transcription-replication machine","volume":"234","author":"Pflug","year":"2017","journal-title":"Virus Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev-virology-092917-043339","article-title":"Host Determinants of Influenza RNA Synthesis","volume":"6","author":"Peacock","year":"2019","journal-title":"Annu. Rev. Virol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1128\/JVI.06519-11","article-title":"A Second CRM1-Dependent Nuclear Export Signal in the Influenza A Virus NS2 Protein Contributes to the Nuclear Export of Viral Ribonucleoproteins","volume":"87","author":"Huang","year":"2012","journal-title":"J. Virol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0168-1702(03)00159-X","article-title":"Trafficking of viral genomic RNA into and out of the nucleus: Influenza, Thogoto and Borna disease viruses","volume":"95","author":"Cros","year":"2003","journal-title":"Virus Res."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"20067","DOI":"10.1074\/jbc.M114.569178","article-title":"The Nuclear Export Protein of H5N1 Influenza A Viruses Recruits Matrix 1 (M1) Protein to the Viral Ribonucleoprotein to Mediate Nuclear Export","volume":"289","author":"Brunotte","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"5848","DOI":"10.1128\/JVI.00307-10","article-title":"The Rab11 Pathway Is Required for Influenza A Virus Budding and Filament Formation","volume":"84","author":"Bruce","year":"2010","journal-title":"J. Virol."},{"key":"ref_39","first-page":"1","article-title":"Influenza virus genome reaches the plasma membrane via a modified endoplasmic reticulum and Rab11-dependent vesicles","volume":"8","author":"Martin","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1146\/annurev-virology-110615-042345","article-title":"Moving On Out: Transport and Packaging of Influenza Viral RNA into Virions","volume":"3","author":"Lakdawala","year":"2016","journal-title":"Annu. Rev. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-18108-1","article-title":"Selective flexible packaging pathways of the segmented genome of influenza A virus","volume":"11","author":"Haralampiev","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Malik, G., and Zhou, Y. (2020). Innate Immune Sensing of Influenza a Virus. Viruses, 12.","DOI":"10.3390\/v12070755"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1016\/j.immuni.2019.03.025","article-title":"Shared and Distinct Functions of Type I and Type III Interferons","volume":"50","author":"Lazear","year":"2019","journal-title":"Immunity"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.3389\/fimmu.2020.01296","article-title":"Recent Advances and Contradictions in the Study of the Individual Roles of Ubiquitin Ligases That Regulate RIG-I-Like Receptor-Mediated Antiviral Innate Immune Responses","volume":"11","author":"Oshiumi","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.cell.2010.01.020","article-title":"RIG-I Detects Viral Genomic RNA during Negative-Strand RNA Virus Infection","volume":"140","author":"Rehwinkel","year":"2010","journal-title":"Cell"},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Kandasamy, M., Suryawanshi, A., Tundup, S., Perez, J.T., Schmolke, M., Manicassamy, S., and Manicassamy, B. (2016). RIG-I Signaling Is Critical for Efficient Polyfunctional T Cell Responses during Influenza Virus Infection. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005754"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"3368","DOI":"10.4049\/jimmunol.178.6.3368","article-title":"Cutting Edge: Influenza A virus activates TLR3-dependent inflammatory and RIG-I-dependent antiviral responses in human lung epithelial cells","volume":"178","author":"Pothlichet","year":"2007","journal-title":"J. Immunol."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Le Goffic, R., Balloy, V., Lagranderie, M., Alexopoulou, L., Escriou, N., Flavell, R., Chignard, M., and Si-Tahar, M. (2006). Detrimental Contribution of the Toll-Like Receptor (TLR)3 to Influenza A Virus\u2013Induced Acute Pneumonia. PLoS Pathog., 2.","DOI":"10.1371\/journal.ppat.0020053"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"12713","DOI":"10.1128\/JVI.01675-10","article-title":"MyD88 Signaling Is Indispensable for Primary Influenza A Virus Infection but Dispensable for Secondary Infection","volume":"84","author":"Seo","year":"2010","journal-title":"J. Virol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"871","DOI":"10.4049\/jimmunol.182.2.871","article-title":"Plasmacytoid Dendritic Cells Are Dispensable during Primary Influenza Virus Infection","volume":"182","author":"Wolf","year":"2009","journal-title":"J. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/ni.3212","article-title":"Guarding the frontiers: The biology of type III interferons","volume":"16","author":"Wack","year":"2015","journal-title":"Nat. Immunol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1159\/000508379","article-title":"The Role of Type I IFNs in Influenza: Antiviral Superheroes or Immunopathogenic Villains?","volume":"12","author":"Wu","year":"2020","journal-title":"J. Innate Immun."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Zhang, Q., Zeng, L.-P., Zhou, P., Irving, A.T., Li, S., Shi, Z.-L., and Wang, L.-F. (2017). IFNAR2-dependent gene expression profile induced by IFN-\u03b1 in Pteropus alecto bat cells and impact of IFNAR2 knockout on virus infection. PLoS ONE, 12.","DOI":"10.1371\/journal.pone.0182866"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2589","DOI":"10.3389\/fimmu.2018.02589","article-title":"IFNAR2 Is Required for Anti-influenza Immunity and Alters Susceptibility to Post-influenza Bacterial Superinfections","volume":"9","author":"Shepardson","year":"2018","journal-title":"Front. Immunol."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Seo, S.-U., Kwon, H.-J., Ko, H.-J., Byun, Y.-H., Seong, B.L., Uematsu, S., Akira, S., and Kweon, M.-N. (2011). Type I Interferon Signaling Regulates Ly6Chi Monocytes and Neutrophils during Acute Viral Pneumonia in Mice. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1001304"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1128\/JVI.01718-06","article-title":"Protective Role of Beta Interferon in Host Defense against Influenza A Virus","volume":"81","author":"Koerner","year":"2006","journal-title":"J. Virol."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"8550","DOI":"10.1128\/JVI.72.11.8550-8558.1998","article-title":"The Role of Interferon in Influenza Virus Tissue Tropism","volume":"72","author":"Durbin","year":"1998","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1089\/jir.2014.0227","article-title":"Disease-Promoting Effects of Type I Interferons in Viral, Bacterial, and Coinfections","volume":"35","author":"Davidson","year":"2015","journal-title":"J. Interf. Cytokine Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"e33354","DOI":"10.7554\/eLife.33354","article-title":"IFN-\u03bb prevents influenza virus spread from the upper airways to the lungs and limits virus transmission","volume":"7","author":"Klinkhammer","year":"2018","journal-title":"eLife"},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Mordstein, M., Kochs, G., Dumoutier, L., Renauld, J.-C., Paludan, S.R., Klucher, K., and Staeheli, P. (2008). Interferon-\u03bb Contributes to Innate Immunity of Mice against Influenza A Virus but Not against Hepatotropic Viruses. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000151"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/s41577-019-0182-z","article-title":"Interferon-\u03bb orchestrates innate and adaptive mucosal immune responses","volume":"19","author":"Ye","year":"2019","journal-title":"Nat. Rev. Immunol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/j.immuni.2017.04.025","article-title":"Interferon-\u03bb Mediates Non-redundant Front-Line Antiviral Protection against Influenza Virus Infection without Compromising Host Fitness","volume":"46","author":"Galani","year":"2017","journal-title":"Immunity"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"854","DOI":"10.1111\/irv.12094","article-title":"Low-dose oral interferon alpha as prophylaxis against viral respiratory illness: A double-blind, parallel controlled trial during an influenza pandemic year","volume":"7","author":"Bennett","year":"2013","journal-title":"Influenza Other Respir. Viruses"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1084\/jem.20181621","article-title":"Severe influenza pneumonitis in children with inherited TLR3 deficiency","volume":"216","author":"Lim","year":"2019","journal-title":"J. Exp. Med."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1126\/science.aaa1578","article-title":"Life-threatening influenza and impaired interferon amplification in human IRF7 deficiency","volume":"348","author":"Ciancanelli","year":"2015","journal-title":"Science"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"2567","DOI":"10.1084\/jem.20180628","article-title":"Life-threatening influenza pneumonitis in a child with inherited IRF9 deficiency","volume":"215","author":"Hernandez","year":"2018","journal-title":"J. Exp. Med."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1038\/s41590-019-0408-z","article-title":"Interferon-\u03bb modulates dendritic cells to facilitate T cell immunity during infection with influenza A virus","volume":"20","author":"Hemann","year":"2019","journal-title":"Nat. Immunol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/s41590-019-0345-x","article-title":"Interferon-\u03bb enhances adaptive mucosal immunity by boosting release of thymic stromal lymphopoietin","volume":"20","author":"Ye","year":"2019","journal-title":"Nat. Immunol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.immuni.2010.06.016","article-title":"Type I Interferons Regulate Cytolytic Activity of Memory CD8+ T Cells in the Lung Airways during Respiratory Virus Challenge","volume":"33","author":"Kohlmeier","year":"2010","journal-title":"Immunity"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"4220","DOI":"10.4049\/jimmunol.164.8.4220","article-title":"Type I IFN Modulates Innate and Specific Antiviral Immunity","volume":"164","author":"Durbin","year":"2000","journal-title":"J. Immunol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"5397","DOI":"10.4049\/jimmunol.1003712","article-title":"Characterization of Chicken Mda5 Activity: Regulation of IFN-\u03b2 in the Absence of RIG-I Functionality","volume":"186","author":"Karpala","year":"2011","journal-title":"J. Immunol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"5913","DOI":"10.1073\/pnas.1001755107","article-title":"Association of RIG-I with innate immunity of ducks to influenza","volume":"107","author":"Barber","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1128\/JVI.00742-11","article-title":"Chicken Cells Sense Influenza A Virus Infection through MDA5 and CARDIF Signaling Involving LGP2","volume":"86","author":"Liniger","year":"2011","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1159\/000351583","article-title":"Chicken MDA5 Senses Short Double-Stranded RNA with Implications for Antiviral Response against Avian Influenza Viruses in Chicken","volume":"6","author":"Hayashi","year":"2013","journal-title":"J. Innate Immun."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1016\/j.molcel.2016.04.021","article-title":"Structural Analysis of dsRNA Binding to Anti-viral Pattern Recognition Receptors LGP2 and MDA5","volume":"62","author":"Uchikawa","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1111\/j.1365-2567.2005.02125.x","article-title":"Identification and characterization of a functional, alternatively spliced Toll-like receptor 7 (TLR7) and genomic disruption of TLR8 in chickens","volume":"114","author":"Philbin","year":"2005","journal-title":"Immunology"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1081\/ABIO-120037900","article-title":"The Interferon-\u03b1 Genes from Three Chicken Lines and Its Effects on H9N2 Influenza Viruses","volume":"15","author":"Xia","year":"2004","journal-title":"Anim. Biotechnol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"7730","DOI":"10.1128\/JVI.00063-11","article-title":"Highly Pathogenic Avian Influenza Viruses Do Not Inhibit Interferon Synthesis in Infected Chickens but Can Override the Interferon-Induced Antiviral State","volume":"85","author":"Penski","year":"2011","journal-title":"J. Virol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"2835","DOI":"10.1128\/JVI.02764-13","article-title":"Antiviral Activity of Lambda Interferon in Chickens","volume":"88","author":"Reuter","year":"2013","journal-title":"J. Virol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"2359","DOI":"10.1099\/vir.0.2008\/004606-0","article-title":"The multifunctional NS1 protein of influenza A viruses","volume":"89","author":"Hale","year":"2008","journal-title":"J. Gen. Virol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/S0021-9258(17)49923-6","article-title":"The influenza NS1 protein modulates RIG-I activation via a strain-specific direct interaction with the second CARD of RIG-I","volume":"295","author":"Jureka","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1128\/JVI.01265-06","article-title":"Inhibition of Retinoic Acid-Inducible Gene I-Mediated Induction of Beta Interferon by the NS1 Protein of Influenza A Virus","volume":"81","author":"Mibayashi","year":"2006","journal-title":"J. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1165\/rcmb.2006-0283RC","article-title":"NS1 Protein of Influenza A Virus Inhibits the Function of Intracytoplasmic Pathogen Sensor, RIG-I","volume":"36","author":"Guo","year":"2007","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.chom.2009.04.006","article-title":"Influenza A Virus NS1 Targets the Ubiquitin Ligase TRIM25 to Evade Recognition by the Host Viral RNA Sensor RIG-I","volume":"5","author":"Gack","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Rajsbaum, R., Albrecht, R.A., Wang, M.K., Maharaj, N.P., Versteeg, G.A., Nistal-Vill\u00e1n, E., Garc\u00eda-Sastre, A., and Gack, M.U. (2012). Species-Specific Inhibition of RIG-I Ubiquitination and IFN Induction by the Influenza A Virus NS1 Protein. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1003059"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-018-04214-8","article-title":"Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition","volume":"9","author":"Koliopoulos","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1111\/j.1462-5822.2008.01116.x","article-title":"The proapoptotic influenza A virus protein PB1-F2 regulates viral polymerase activity by interaction with the PB1 protein","volume":"10","author":"Mazur","year":"2008","journal-title":"Cell. Microbiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1038\/nm1201-1306","article-title":"A novel influenza A virus mitochondrial protein that induces cell death","volume":"7","author":"Chen","year":"2001","journal-title":"Nat. Med."},{"key":"ref_89","doi-asserted-by":"crossref","unstructured":"Leymarie, O., Jouvion, G., Herv\u00e9, P.-L., Chevalier, C., Lorin, V., Lecardonnel, J., Da Costa, B., Delmas, B., Escriou, N., and Le Goffic, R. (2013). Kinetic Characterization of PB1-F2-Mediated Immunopathology during Highly Pathogenic Avian H5N1 Influenza Virus Infection. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0057894"},{"key":"ref_90","doi-asserted-by":"crossref","unstructured":"Varga, Z.T., Ramos, I., Hai, R., Schmolke, M., Garc\u00eda-Sastre, A., Fernandez-Sesma, A., and Palese, P. (2011). The Influenza Virus Protein PB1-F2 Inhibits the Induction of Type I Interferon at the Level of the MAVS Adaptor Protein. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002067"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"8359","DOI":"10.1128\/JVI.01122-12","article-title":"Influenza Virus Protein PB1-F2 Inhibits the Induction of Type I Interferon by Binding to MAVS and Decreasing Mitochondrial Membrane Potential","volume":"86","author":"Varga","year":"2012","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"120109","DOI":"10.1098\/rsob.120109","article-title":"Ribosomal frameshifting used in influenza A virus expression occurs within the sequence UCC_UUU_CGU and is in the +1 direction","volume":"2","author":"Firth","year":"2012","journal-title":"Open Biol."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1126\/science.1222213","article-title":"An Overlapping Protein-Coding Region in Influenza A Virus Segment 3 Modulates the Host Response","volume":"337","author":"Jagger","year":"2012","journal-title":"Science"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Khaperskyy, D.A., Schmaling, S., Larkins-Ford, J., McCormick, C., and Gaglia, M.M. (2016). Selective Degradation of Host RNA Polymerase II Transcripts by Influenza A Virus PA-X Host Shutoff Protein. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005427"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"7131","DOI":"10.1128\/JVI.00954-16","article-title":"Critical Role of the PA-X C-Terminal Domain of Influenza A Virus in Its Subcellular Localization and Shutoff Activity","volume":"90","author":"Hayashi","year":"2016","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"6528","DOI":"10.1128\/JVI.00386-15","article-title":"Timing Is Everything: Coordinated Control of Host Shutoff by Influenza A Virus NS1 and PA-X Proteins","volume":"89","author":"Khaperskyy","year":"2015","journal-title":"J. Virol."},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Levene, R.E., and Gaglia, M.M. (2018). Host Shutoff in Influenza A Virus: Many Means to an End. Viruses, 10.","DOI":"10.3390\/v10090475"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1146\/annurev-virology-031413-085537","article-title":"IFITM-Family Proteins: The Cell\u2019s First Line of Antiviral Defense","volume":"1","author":"Bailey","year":"2014","journal-title":"Annu. Rev. Virol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12977-017-0377-y","article-title":"More than meets the I: The diverse antiviral and cellular functions of interferon-induced transmembrane proteins","volume":"14","author":"Shi","year":"2017","journal-title":"Retrovirology"},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Zhang, Z., Liu, J., Li, M., Yang, H., and Zhang, C. (2012). Evolutionary Dynamics of the Interferon-Induced Transmembrane Gene Family in Vertebrates. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0049265"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1089\/jir.2010.0112","article-title":"The Small Interferon-Induced Transmembrane Genes and Proteins","volume":"31","author":"Siegrist","year":"2011","journal-title":"J. Interf. Cytokine Res."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/j.cell.2009.12.017","article-title":"The IFITM Proteins Mediate Cellular Resistance to Influenza A H1N1 Virus, West Nile Virus, and Dengue Virus","volume":"139","author":"Brass","year":"2009","journal-title":"Cell"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"3228","DOI":"10.3389\/fmicb.2018.03228","article-title":"IFITM Genes, Variants, and Their Roles in the Control and Pathogenesis of Viral Infections","volume":"9","author":"Zhao","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"19631","DOI":"10.1074\/jbc.M112.362095","article-title":"S-Palmitoylation and Ubiquitination Differentially Regulate Interferon-induced Transmembrane Protein 3 (IFITM3)-mediated Resistance to Influenza Virus","volume":"287","author":"Yount","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"32184","DOI":"10.1074\/jbc.M113.514356","article-title":"Interferon-induced Transmembrane Protein 3 Is a Type II Transmembrane Protein","volume":"288","author":"Bailey","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_106","doi-asserted-by":"crossref","unstructured":"Weston, S., Czieso, S., White, I.J., Smith, S.E., Kellam, P., and Marsh, M. (2014). A Membrane Topology Model for Human Interferon Inducible Transmembrane Protein 1. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0104341"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"24029","DOI":"10.1038\/srep24029","article-title":"Combined approaches of EPR and NMR illustrate only one transmembrane helix in the human IFITM3","volume":"6","author":"Ling","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.2217\/fmb.14.65","article-title":"Regulation of the trafficking and antiviral activity of IFITM3 by post-translational modifications","volume":"9","author":"Chesarino","year":"2014","journal-title":"Future Microbiol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"4937","DOI":"10.1016\/j.jmb.2013.09.024","article-title":"IFITMs Restrict the Replication of Multiple Pathogenic Viruses","volume":"425","author":"Perreira","year":"2013","journal-title":"J. Mol. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"14423","DOI":"10.1021\/jacs.6b08733","article-title":"Site-Specific Bioorthogonal Labeling for Fluorescence Imaging of Intracellular Proteins in Living Cells","volume":"138","author":"Peng","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/s41589-018-0213-2","article-title":"IFITM3 directly engages and shuttles incoming virus particles to lysosomes","volume":"15","author":"Spence","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1016\/j.chom.2014.11.001","article-title":"IFITM Proteins Incorporated into HIV-1 Virions Impair Viral Fusion and Spread","volume":"16","author":"Compton","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12977-014-0103-y","article-title":"IFITM proteins are incorporated onto HIV-1 virion particles and negatively imprint their infectivity","volume":"11","author":"Tartour","year":"2014","journal-title":"Retrovirology"},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Feeley, E.M., Sims, J.S., John, S.P., Chin, C.R., Pertel, T., Chen, L.-M., Gaiha, G.D., Ryan, B.J., Donis, R.O., and Elledge, S.J. (2011). IFITM3 Inhibits Influenza A Virus Infection by Preventing Cytosolic Entry. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002337"},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Li, K., Markosyan, R.M., Zheng, Y.-M., Golfetto, O., Bungart, B., Li, M., Ding, S., Chen, L., Liang, C., and Lee, J.C. (2013). IFITM Proteins Restrict Viral Membrane Hemifusion. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003124"},{"key":"ref_116","doi-asserted-by":"crossref","unstructured":"Desai, T.M., Marin, M., Chin, C.R., Savidis, G., Brass, A.L., and Melikyan, G.B. (2014). IFITM3 Restricts Influenza A Virus Entry by Blocking the Formation of Fusion Pores following Virus-Endosome Hemifusion. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004048"},{"key":"ref_117","doi-asserted-by":"crossref","unstructured":"Suddala, K.C., Lee, C.C., Meraner, P., Marin, M., Markosyan, R.M., Desai, T.M., Cohen, F.S., Brass, A.L., and Melikyan, G.B. (2019). Interferon-induced transmembrane protein 3 blocks fusion of sensitive but not resistant viruses by partitioning into virus-carrying endosomes. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1007532"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"7837","DOI":"10.1128\/JVI.00481-13","article-title":"The CD225 Domain of IFITM3 Is Required for both IFITM Protein Association and Inhibition of Influenza A Virus and Dengue Virus Replication","volume":"87","author":"John","year":"2013","journal-title":"J. Virol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1111\/cmi.12262","article-title":"Identification of an endocytic signal essential for the antiviral action of IFITM3","volume":"16","author":"Jia","year":"2014","journal-title":"Cell. Microbiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"3683","DOI":"10.3390\/v6093683","article-title":"IFITM Proteins Inhibit Entry Driven by the MERS-Coronavirus Spike Protein: Evidence for Cholesterol-Independent Mechanisms","volume":"6","author":"Wrensch","year":"2014","journal-title":"Viruses"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1038\/nchembio.405","article-title":"Palmitoylome profiling reveals S-palmitoylation\u2013dependent antiviral activity of IFITM3","volume":"6","author":"Yount","year":"2010","journal-title":"Nat. Chem. Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"11986","DOI":"10.1074\/jbc.M114.557694","article-title":"Phosphorylation of the Antiviral Protein Interferon-inducible Transmembrane Protein 3 (IFITM3) Dually Regulates Its Endocytosis and Ubiquitination","volume":"289","author":"Chesarino","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"13697","DOI":"10.1128\/JVI.01828-12","article-title":"The N-Terminal Region of IFITM3 Modulates Its Antiviral Activity by Regulating IFITM3 Cellular Localization","volume":"86","author":"Jia","year":"2012","journal-title":"J. Virol."},{"key":"ref_124","first-page":"519","article-title":"IFITM3 restricts the morbidity and mortality associated with influenza","volume":"484","author":"Everitt","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"Bailey, C.C., Huang, I.-C., Kam, C., and Farzan, M. (2012). Ifitm3 Limits the Severity of Acute Influenza in Mice. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002909"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"18607","DOI":"10.1073\/pnas.1900784116","article-title":"IFITM3 protects the heart during influenza virus infection","volume":"116","author":"Kenney","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Infusini, G., Smith, J.M., Yuan, H., Pizzolla, A., Ng, W.C., Londrigan, S.L., Haque, A., Reading, P.C., Villadangos, J.A., and Wakim, L.M. (2015). Respiratory DC Use IFITM3 to Avoid Direct Viral Infection and Safeguard Virus-Specific CD8+ T Cell Priming. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0143539"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/ni.2525","article-title":"Enhanced survival of lung tissue-resident memory CD8+ T cells during infection with influenza virus due to selective expression of IFITM3","volume":"14","author":"Wakim","year":"2013","journal-title":"Nat. Immunol."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.bj.2019.01.004","article-title":"IFITM3: How genetics influence influenza infection demographically","volume":"42","author":"Wellington","year":"2019","journal-title":"Biomed. J."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.1038\/ncomms2433","article-title":"Interferon-induced transmembrane protein-3 genetic variant rs12252-C is associated with severe influenza in Chinese individuals","volume":"4","author":"Zhang","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1186\/s12985-017-0884-4","article-title":"Association of IFITM3 rs12252 polymorphisms, BMI, diabetes, and hypercholesterolemia with mild flu in an Iranian population","volume":"14","author":"Mehrbod","year":"2017","journal-title":"Virol. J."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"294","DOI":"10.3389\/fcimb.2017.00294","article-title":"IFITM3 Rs12252-C Variant Increases Potential Risk for Severe Influenza Virus Infection in Chinese Population","volume":"7","author":"Pan","year":"2017","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1073\/pnas.1321748111","article-title":"Early hypercytokinemia is associated with interferon-induced transmembrane protein-3 dysfunction and predictive of fatal H7N9 infection","volume":"111","author":"Wang","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Yang, X., Tan, B., Zhou, X., Xue, J., Zhang, X., Wang, P., Shao, C., Li, Y., Li, C., and Xia, H. (2015). Interferon-Inducible Transmembrane Protein 3 Genetic Variant rs12252 and Influenza Susceptibility and Severity: A Meta-Analysis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0124985"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"2975","DOI":"10.1017\/S0950268815000278","article-title":"IFITM3 rs12252 T>C polymorphism is associated with the risk of severe influenza: A meta-analysis","volume":"143","author":"Xuan","year":"2015","journal-title":"Epidemiol. Infect."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1159\/000479087","article-title":"No Correlation of the Disease Severity of Influenza A Virus Infection with the rs12252 Polymorphism of the Interferon-Induced Transmembrane Protein 3 Gene","volume":"60","author":"Kim","year":"2017","journal-title":"Intervirology"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1007\/s00251-017-1026-2","article-title":"Population genetics of IFITM3 in Portugal and Central Africa reveals a potential modifier of influenza severity","volume":"70","author":"David","year":"2018","journal-title":"Immunogenetics"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"352","DOI":"10.3389\/fcimb.2020.00352","article-title":"Investigation of Human IFITM3 Polymorphisms rs34481144A and rs12252C and Risk for Influenza A(H1N1)pdm09 Severity in a Brazilian Cohort","volume":"10","author":"Martins","year":"2020","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Williams, D.E.J., Wu, W.-L., Grotefend, C.R., Radic, V., Chung, C., Chung, Y.-H., Farzan, M., and Huang, I.-C. (2014). IFITM3 Polymorphism rs12252-C Restricts Influenza A Viruses. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0110096"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1093\/infdis\/jix242","article-title":"Evaluation of IFITM3 rs12252 Association With Severe Pediatric Influenza Infection","volume":"216","author":"Randolph","year":"2017","journal-title":"J. Infect. Dis."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1093\/infdis\/jix512","article-title":"Lack of Truncated IFITM3 Transcripts in Cells Homozygous for the rs12252-C Variant That is Associated With Severe Influenza Infection","volume":"217","author":"Wang","year":"2018","journal-title":"J. Infect. Dis."},{"key":"ref_142","doi-asserted-by":"crossref","unstructured":"Smith, J., Smith, N., Yu, L., Paton, I.R., Gutowska, M.W., Forrest, H.L., Danner, A.F., Seiler, J.P., Digard, P., and Webster, R.G. (2015). A comparative analysis of host responses to avian influenza infection in ducks and chickens highlights a role for the interferon-induced transmembrane proteins in viral resistance. BMC Genom., 16.","DOI":"10.1186\/s12864-015-1778-8"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1128\/JVI.02516-14","article-title":"Swine Interferon-Inducible Transmembrane Proteins Potently Inhibit Influenza A Virus Replication","volume":"89","author":"Lanz","year":"2014","journal-title":"J. Virol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"991","DOI":"10.1099\/vir.0.000058","article-title":"Bat and pig IFN-induced transmembrane protein 3 restrict cell entry by influenza virus and lyssaviruses","volume":"96","author":"Benfield","year":"2015","journal-title":"J. Gen. Virol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"e201900542","DOI":"10.26508\/lsa.201900542","article-title":"Bat IFITM3 restriction depends on S-palmitoylation and a polymorphic site within the CD225 domain","volume":"3","author":"Benfield","year":"2020","journal-title":"Life Sci. Alliance"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"12957","DOI":"10.1128\/JVI.01443-13","article-title":"Chicken Interferon-Inducible Transmembrane Protein 3 Restricts Influenza Viruses and LyssavirusesIn Vitro","volume":"87","author":"Smith","year":"2013","journal-title":"J. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1128\/JVI.01593-15","article-title":"Duck Interferon-Inducible Transmembrane Protein 3 Mediates Restriction of Influenza Viruses","volume":"90","author":"Blyth","year":"2015","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1007\/s00335-017-9706-7","article-title":"TLDc proteins: New players in the oxidative stress response and neurological disease","volume":"28","author":"Finelli","year":"2017","journal-title":"Mamm. Genome"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"2751","DOI":"10.1074\/jbc.M115.685222","article-title":"The Evolutionarily Conserved Tre2\/Bub2\/Cdc16 (TBC), Lysin Motif (LysM), Domain Catalytic (TLDc) Domain Is Neuroprotective against Oxidative Stress","volume":"291","author":"Finelli","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"3358","DOI":"10.1128\/MCB.22.10.3358-3372.2002","article-title":"ERAP140, a Conserved Tissue-Specific Nuclear Receptor Coactivator","volume":"22","author":"Shao","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1089\/jir.2014.0115","article-title":"Induction of a Unique Isoform of theNCOA7Oxidation Resistance Gene by Interferon \u03b2-1b","volume":"35","author":"Yu","year":"2015","journal-title":"J. Interf. Cytokine Res."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1369","DOI":"10.1038\/s41564-018-0273-9","article-title":"The interferon-inducible isoform of NCOA7 inhibits endosome-mediated viral entry","volume":"3","author":"Doyle","year":"2018","journal-title":"Nat. Microbiol."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"14827","DOI":"10.1038\/srep14827","article-title":"Mapping the H+ (V)-ATPase interactome: Identification of proteins involved in trafficking, folding, assembly and phosphorylation","volume":"5","author":"Merkulova","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Castroflorio, E., Hoed, J.D., Svistunova, D., Finelli, M.J., Cebrian-Serrano, A., Corrochano, S., Bassett, A.R., Davies, B., and Oliver, P.L. (2020). The Ncoa7 locus regulates V-ATPase formation and function, neurodevelopment and behaviour. Cell. Mol. Life Sci., 1\u201322.","DOI":"10.1007\/s00018-020-03721-6"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1084\/jem.20161270","article-title":"ZMPSTE24 defends against influenza and other pathogenic viruses","volume":"214","author":"Fu","year":"2017","journal-title":"J. Exp. Med."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"13876","DOI":"10.1038\/ncomms13876","article-title":"Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction","volume":"8","author":"Wang","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Zhao, J., Chen, J., Li, M., Chen, M., and Sun, C. (2020). Multifaceted Functions of CH25H and 25HC to Modulate the Lipid Metabolism, Immune Responses, and Broadly Antiviral Activities. Viruses, 12.","DOI":"10.3390\/v12070727"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.immuni.2012.11.004","article-title":"The Transcription Factor STAT-1 Couples Macrophage Synthesis of 25-Hydroxycholesterol to the Interferon Antiviral Response","volume":"38","author":"Blanc","year":"2013","journal-title":"Immunity"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"10666","DOI":"10.1073\/pnas.1404271111","article-title":"25-Hydroxycholesterol acts as an amplifier of inflammatory signaling","volume":"111","author":"Gold","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"1503","DOI":"10.1016\/j.celrep.2017.07.060","article-title":"A CRISPR Activation Screen Identifies a Pan-avian Influenza Virus Inhibitory Host Factor","volume":"20","author":"Heaton","year":"2017","journal-title":"Cell Rep."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"L86","DOI":"10.1152\/ajplung.2001.281.1.L86","article-title":"Involvement of the MAP kinase ERK2 in MUC1 mucin signaling","volume":"281","author":"Meerzaman","year":"2001","journal-title":"Am. J. Physiol. Cell. Mol. Physiol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1189\/jlb.0604333","article-title":"MUC1 (CD227) interacts with lck tyrosine kinase in Jurkat lymphoma cells and normal T cells","volume":"77","author":"Mukherjee","year":"2004","journal-title":"J. Leukoc. Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"29386","DOI":"10.1074\/jbc.C400010200","article-title":"MUC1 Initiates a Calcium Signal after Ligation by Intercellular Adhesion Molecule-1","volume":"279","author":"Rahn","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1016\/j.bbrc.2004.06.167","article-title":"MUC1 tyrosine phosphorylation activates the extracellular signal-regulated kinase","volume":"321","author":"Wang","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"L809","DOI":"10.1152\/ajplung.00385.2003","article-title":"Pseudomonas aeruginosastimulates phosphorylation of the airway epithelial membrane glycoprotein Muc1 and activates MAP kinase","volume":"287","author":"Lillehoj","year":"2004","journal-title":"Am. J. Physiol. Cell. Mol. Physiol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"D1040","DOI":"10.1093\/nar\/gks1215","article-title":"INTERFEROME v2.0: An updated database of annotated interferon-regulated genes","volume":"41","author":"Rusinova","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1136\/gutjnl-2014-307175","article-title":"The MUC1 mucin protects againstHelicobacter pyloripathogenesis in mice by regulation of the NLRP3 inflammasome","volume":"65","author":"Ng","year":"2016","journal-title":"Gut"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1038\/mi.2017.16","article-title":"The cell surface mucin MUC1 limits the severity of influenza A virus infection","volume":"10","author":"McAuley","year":"2017","journal-title":"Mucosal Immunol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"R411","DOI":"10.1016\/j.cub.2017.12.013","article-title":"The dynamin superfamily","volume":"28","author":"Ramachandran","year":"2018","journal-title":"Curr. Biol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.tim.2014.12.003","article-title":"Mx GTPases: Dynamin-like antiviral machines of innate immunity","volume":"23","author":"Haller","year":"2015","journal-title":"Trends Microbiol."},{"key":"ref_171","first-page":"559","article-title":"Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection","volume":"502","author":"Goujon","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_172","first-page":"563","article-title":"MX2 is an interferon-induced inhibitor of HIV-1 infection","volume":"502","author":"Kane","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1016\/j.chom.2013.08.015","article-title":"The Interferon-Inducible MxB Protein Inhibits HIV-1 Infection","volume":"14","author":"Liu","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"e01056-18","DOI":"10.1128\/JVI.01056-18","article-title":"Human MxB Protein Is a Pan-herpesvirus Restriction Factor","volume":"92","author":"Schilling","year":"2018","journal-title":"J. Virol."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-018-04379-2","article-title":"MxB is an interferon-induced restriction factor of human herpesviruses","volume":"9","author":"Crameri","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Yi, D.-R., An, N., Liu, Z.-L., Xu, F.-W., Raniga, K., Li, Q.-J., Zhou, R., Wang, J., Zhang, Y.-X., and Zhou, J.-M. (2018). Human MxB Inhibits the Replication of Hepatitis C Virus. J. Virol., 93.","DOI":"10.1128\/JVI.01285-18"},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.jhep.2019.12.009","article-title":"Interferon-inducible MX2 is a host restriction factor of hepatitis B virus replication","volume":"72","author":"Wang","year":"2020","journal-title":"J. Hepatol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1146\/annurev-virology-092917-043525","article-title":"The Discovery of the Antiviral Resistance GeneMx: A Story of Great Ideas, Great Failures, and Some Success","volume":"5","author":"Haller","year":"2018","journal-title":"Annu. Rev. Virol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"1709","DOI":"10.1128\/jvi.66.3.1709-1716.1992","article-title":"Resistance to influenza virus infection of Mx transgenic mice expressing Mx protein under the control of two constitutive promoters","volume":"66","author":"Kolb","year":"1992","journal-title":"J. Virol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1084\/jem.20161033","article-title":"In vivo evasion of MxA by avian influenza viruses requires human signature in the viral nucleoprotein","volume":"214","author":"Deeg","year":"2017","journal-title":"J. Exp. Med."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"7776","DOI":"10.1128\/JVI.00546-06","article-title":"Induction of MxA Gene Expression by Influenza A Virus Requires Type I or Type III Interferon Signaling","volume":"81","author":"Holzinger","year":"2007","journal-title":"J. Virol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"6726","DOI":"10.1128\/jvi.67.11.6726-6732.1993","article-title":"A functional GTP-binding motif is necessary for antiviral activity of Mx proteins","volume":"67","author":"Pitossi","year":"1993","journal-title":"J. Virol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"2591","DOI":"10.1128\/jvi.71.4.2591-2599.1997","article-title":"Dominant-negative mutants of human MxA protein: Domains in the carboxy-terminal moiety are important for oligomerization and antiviral activity","volume":"71","author":"Ponten","year":"1997","journal-title":"J. Virol."},{"key":"ref_184","first-page":"502","article-title":"Structural basis of oligomerization in the stalk region of dynamin-like MxA","volume":"465","author":"Gao","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"28419","DOI":"10.1074\/jbc.R110.145839","article-title":"Dynamin-like MxA GTPase: Structural Insights into Oligomerization and Implications for Antiviral Activity","volume":"285","author":"Haller","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.chom.2012.09.005","article-title":"Evolution-Guided Identification of Antiviral Specificity Determinants in the Broadly Acting Interferon-Induced Innate Immunity Factor MxA","volume":"12","author":"Mitchell","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"6020","DOI":"10.1074\/jbc.M113.543892","article-title":"Structural Requirements for the Antiviral Activity of the Human MxA Protein against Thogoto and Influenza A Virus","volume":"289","author":"Patzina","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"9017","DOI":"10.1128\/JVI.01269-14","article-title":"Transfer of the Amino-Terminal Nuclear Envelope Targeting Domain of Human MX2 Converts MX1 into an HIV-1 Resistance Factor","volume":"88","author":"Goujon","year":"2014","journal-title":"J. Virol."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"4676","DOI":"10.1128\/JVI.00169-15","article-title":"A Triple-Arginine Motif in the Amino-Terminal Domain and Oligomerization Are Required for HIV-1 Inhibition by Human MX2","volume":"89","author":"Goujon","year":"2015","journal-title":"J. Virol."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1128\/JVI.02247-15","article-title":"Oligomerization Requirements for MX2-Mediated Suppression of HIV-1 Infection","volume":"90","author":"Dicks","year":"2015","journal-title":"J. Virol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"8133","DOI":"10.1128\/JVI.00712-11","article-title":"The Viral Nucleoprotein Determines Mx Sensitivity of Influenza A Viruses","volume":"85","author":"Zimmermann","year":"2011","journal-title":"J. Virol."},{"key":"ref_192","doi-asserted-by":"crossref","unstructured":"M\u00e4nz, B., Dornfeld, D., G\u00f6tz, H., Zell, R., Zimmermann, P., Haller, O., Kochs, G., and Schwemmle, M. (2013). Pandemic Influenza A Viruses Escape from Restriction by Human MxA through Adaptive Mutations in the Nucleoprotein. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003279"},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1128\/JVI.02406-14","article-title":"The Nucleoprotein of Newly Emerged H7N9 Influenza A Virus Harbors a Unique Motif Conferring Resistance to Antiviral Human MxA","volume":"89","author":"Riegger","year":"2014","journal-title":"J. Virol."},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Ashenberg, O., Padmakumar, J., Doud, M.B., and Bloom, J.D. (2017). Deep mutational scanning identifies sites in influenza nucleoprotein that affect viral inhibition by MxA. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006288"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"3624","DOI":"10.1128\/JVI.01753-07","article-title":"Influenza A Virus Strains Differ in Sensitivity to the Antiviral Action of Mx-GTPase","volume":"82","author":"Dittmann","year":"2008","journal-title":"J. Virol."},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"13445","DOI":"10.1128\/JVI.01682-12","article-title":"Interferon-Inducible Protein Mx1 Inhibits Influenza Virus by Interfering with Functional Viral Ribonucleoprotein Complex Assembly","volume":"86","author":"Verhelst","year":"2012","journal-title":"J. Virol."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1006\/viro.1993.1639","article-title":"Function of the Mouse Mx1 Protein Is Inhibited by Overexpression of the PB2 Protein of Influenza Virus","volume":"197","author":"Staeheli","year":"1993","journal-title":"Virology"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1016\/j.immuni.2011.07.012","article-title":"Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function","volume":"35","author":"Gao","year":"2011","journal-title":"Immunity"},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"13053","DOI":"10.1128\/JVI.02220-13","article-title":"The Human Interferon-Induced MxA Protein Inhibits Early Stages of Influenza A Virus Infection by Retaining the Incoming Viral Genome in the Cytoplasm","volume":"87","author":"Xiao","year":"2013","journal-title":"J. Virol."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"23138","DOI":"10.1038\/srep23138","article-title":"Influenza A viruses escape from MxA restriction at the expense of efficient nuclear vRNP import","volume":"6","author":"Magar","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"2564","DOI":"10.1128\/jvi.66.4.2564-2569.1992","article-title":"Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle","volume":"66","author":"Pavlovic","year":"1992","journal-title":"J. Virol."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"8533","DOI":"10.1007\/s11033-012-1708-7","article-title":"Detection of new biallelic polymorphisms in the human MxA gene","volume":"39","author":"Duc","year":"2012","journal-title":"Mol. Biol. Rep."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"3056","DOI":"10.1074\/jbc.M117.812784","article-title":"Effects of allelic variations in the human myxovirus resistance protein A on its antiviral activity","volume":"293","author":"Graf","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_204","first-page":"639","article-title":"Structure and polymorphism of the human gene for the interferon-induced p78 protein (MX1): Evidence of association with alopecia areata in the Down syndrome region","volume":"106","author":"McDonagh","year":"2000","journal-title":"Qual. Life Res."},{"key":"ref_205","first-page":"695","article-title":"Mx genes: Host determinants controlling influenza virus infection and trans-species transmission","volume":"139","author":"Haller","year":"2019","journal-title":"Qual. Life Res."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"3370","DOI":"10.1128\/jvi.64.7.3370-3375.1990","article-title":"Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein","volume":"64","author":"Pavlovic","year":"1990","journal-title":"J. Virol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"10879","DOI":"10.1128\/JVI.01744-15","article-title":"Functional Comparison of Mx1 from Two Different Mouse Species Reveals the Involvement of Loop L4 in the Antiviral Activity against Influenza A Viruses","volume":"89","author":"Verhelst","year":"2015","journal-title":"J. Virol."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"4506","DOI":"10.1128\/jvi.69.7.4506-4510.1995","article-title":"Enhanced virus resistance of transgenic mice expressing the human MxA protein","volume":"69","author":"Pavlovic","year":"1995","journal-title":"J. Virol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"eaau4643","DOI":"10.1126\/sciimmunol.aau4643","article-title":"Influenza restriction factor MxA functions as inflammasome sensor in the respiratory epithelium","volume":"4","author":"Lee","year":"2019","journal-title":"Sci. Immunol."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1051\/vetres\/2010001","article-title":"Interferon-inducedSus scrofaMx1 blocks endocytic traffic of incoming influenza A virus particles","volume":"41","author":"Palm","year":"2010","journal-title":"Vet. Res."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"6263","DOI":"10.1128\/jvi.64.12.6263-6269.1990","article-title":"Activity of rat Mx proteins against a rhabdovirus","volume":"64","author":"Meier","year":"1990","journal-title":"J. Virol."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"e00361-17","DOI":"10.1128\/JVI.00361-17","article-title":"Evolution and Antiviral Specificities of Interferon-Induced Mx Proteins of Bats against Ebola, Influenza, and Other RNA Viruses","volume":"91","author":"Fuchs","year":"2017","journal-title":"J. Virol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"7533","DOI":"10.1128\/JVI.00185-08","article-title":"Asparagine 631 Variants of the Chicken Mx Protein Do Not Inhibit Influenza Virus Replication in Primary Chicken Embryo Fibroblasts or In Vitro Surrogate Assays","volume":"82","author":"Benfield","year":"2008","journal-title":"J. Virol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1089\/jir.1995.15.47","article-title":"The Interferon-Induced Mx Protein of Chickens Lacks Antiviral Activity","volume":"15","author":"Bernasconi","year":"1995","journal-title":"J. Interf. Cytokine Res."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"8307","DOI":"10.1128\/JVI.00535-11","article-title":"Mx Is Dispensable for Interferon-Mediated Resistance of Chicken Cells against Influenza A Virus","volume":"85","author":"Schusser","year":"2011","journal-title":"J. Virol."},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1089\/vim.2009.0053","article-title":"Induction of Mx and PKR Failed to Protect Chickens from H5N1 Infection","volume":"22","author":"Daviet","year":"2009","journal-title":"Viral Immunol."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1006\/viro.1993.1350","article-title":"No Enhanced Influenza Virus Resistance of Murine and Avian Cells Expressing Cloned Duck Mx Protein","volume":"195","author":"Bazzigher","year":"1993","journal-title":"Virology"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1084\/jem.20182031","article-title":"Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease","volume":"216","author":"Tretina","year":"2019","journal-title":"J. Exp. Med."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"e12791","DOI":"10.1111\/cmi.12791","article-title":"Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: Roles in intracellular lysis of pathogens","volume":"19","author":"Ngo","year":"2017","journal-title":"Cell. Microbiol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1096\/fj.11-189886","article-title":"A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication","volume":"26","author":"Nordmann","year":"2011","journal-title":"FASEB J."},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Zhu, Z., Shi, Z., Yan, W., Wei, J., Shao, N., Deng, X., Wang, S., Li, B., Tong, G., and Ma, Z. (2013). Nonstructural Protein 1 of Influenza A Virus Interacts with Human Guanylate-Binding Protein 1 to Antagonize Antiviral Activity. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0055920"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1159\/000460294","article-title":"Inducible GBP5 Mediates the Antiviral Response via Interferon-Related Pathways during Influenza A Virus Infection","volume":"9","author":"Feng","year":"2017","journal-title":"J. Innate Immun."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1016\/j.celrep.2019.04.063","article-title":"Guanylate-Binding Proteins 2 and 5 Exert Broad Antiviral Activity by Inhibiting Furin-Mediated Processing of Viral Envelope Proteins","volume":"27","author":"Braun","year":"2019","journal-title":"Cell Rep."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"30422","DOI":"10.18632\/oncotarget.16503","article-title":"The innate immunity of guinea pigs against highly pathogenic avian influenza virus infection","volume":"8","author":"Zhang","year":"2017","journal-title":"Oncotarget"},{"key":"ref_225","doi-asserted-by":"crossref","unstructured":"Feng, M., Zhang, Q., Wu, W., Chen, L., Gu, S., Ye, Y., Zhong, Y., Huang, Q., and Liu, S. (2021). Inducible Guanylate-Binding Protein 7 Facilitates Influenza A Virus Replication by Suppressing Innate Immunity via NF-\u03baB and JAK-STAT Signaling Pathways. J. Virol., 95.","DOI":"10.1128\/JVI.02038-20"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"1416","DOI":"10.1002\/hep.1840360618","article-title":"Genetic polymorphisms in interferon pathway and response to interferon treatment in hepatitis B patients: A pilot study","volume":"36","author":"King","year":"2002","journal-title":"Hepatology"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.tibs.2017.01.002","article-title":"TRIM Family Proteins: Roles in Autophagy, Immunity, and Carcinogenesis","volume":"42","author":"Hatakeyama","year":"2017","journal-title":"Trends Biochem. Sci."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"4523","DOI":"10.1128\/JVI.02548-12","article-title":"TRIM22 Inhibits Influenza A Virus Infection by Targeting the Viral Nucleoprotein for Degradation","volume":"87","author":"Oteiza","year":"2013","journal-title":"J. Virol."},{"key":"ref_229","doi-asserted-by":"crossref","unstructured":"Carthagena, L., Bergamaschi, A., Luna, J.M., David, A., Uchil, P.D., Margottin-Goguet, F., Mothes, W., Hazan, U., Transy, C., and Pancino, G. (2009). Human TRIM Gene Expression in Response to Interferons. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0004894"},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"e00110-18","DOI":"10.1128\/mSphere.00110-18","article-title":"Mutations Conferring Increased Sensitivity to Tripartite Motif 22 Restriction Accumulated Progressively in the Nucleoprotein of Seasonal Influenza A (H1N1) Viruses between 1918 and 2009","volume":"3","author":"Pagani","year":"2018","journal-title":"mSphere"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"344","DOI":"10.3389\/fmicb.2019.00344","article-title":"Inhibition of Influenza A Virus Replication by TRIM14 via Its Multifaceted Protein\u2013Protein Interaction With NP","volume":"10","author":"Wu","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1128\/JVI.00905-18","article-title":"TRIM41-Mediated Ubiquitination of Nucleoprotein Limits Influenza A Virus Infection","volume":"92","author":"Patil","year":"2018","journal-title":"J. Virol."},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Fu, B., Wang, L., Ding, H., Schwamborn, J.C., Li, S., and Dorf, M.E. (2015). TRIM32 Senses and Restricts Influenza A Virus by Ubiquitination of PB1 Polymerase. PLoS Pathog., 11.","DOI":"10.1371\/journal.ppat.1004960"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"1353","DOI":"10.1093\/hmg\/ddp036","article-title":"Deficiency of the E3 ubiquitin ligase TRIM32 in mice leads to a myopathy with a neurogenic component","volume":"18","author":"Kudryashova","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_235","doi-asserted-by":"crossref","unstructured":"Nicklas, S., Otto, A., Wu, X., Miller, P., Stelzer, S., Wen, Y., Kuang, S., Wrogemann, K., Patel, K., and Ding, H. (2012). TRIM32 Regulates Skeletal Muscle Stem Cell Differentiation and Is Necessary for Normal Adult Muscle Regeneration. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0030445"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1007\/s13238-020-00734-6","article-title":"TRIM35 mediates protection against influenza infection by activating TRAF3 and degrading viral PB2","volume":"11","author":"Sun","year":"2020","journal-title":"Protein Cell"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"e1588","DOI":"10.1002\/wrna.1588","article-title":"TRIM25 and its emerging RNA-binding roles in antiviral defense","volume":"11","author":"Choudhury","year":"2020","journal-title":"Wiley Interdiscip. Rev. RNA"},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.chom.2017.10.003","article-title":"Nuclear TRIM25 Specifically Targets Influenza Virus Ribonucleoproteins to Block the Onset of RNA Chain Elongation","volume":"22","author":"Meyerson","year":"2017","journal-title":"Cell Host Microbe"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"4369","DOI":"10.1128\/JVI.03172-15","article-title":"The C-Terminal Tail of TRIM56 Dictates Antiviral Restriction of Influenza A and B Viruses by Impeding Viral RNA Synthesis","volume":"90","author":"Liu","year":"2016","journal-title":"J. Virol."},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-018-02936-3","article-title":"TRIM56-mediated monoubiquitination of cGAS for cytosolic DNA sensing","volume":"9","author":"Seo","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1016\/j.bbamcr.2018.09.012","article-title":"From APOBEC to ZAP: Diverse mechanisms used by cellular restriction factors to inhibit virus infections","volume":"1866","author":"Chemudupati","year":"2019","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"ref_242","doi-asserted-by":"crossref","unstructured":"Li, M.M.H., Aguilar, E.G., Michailidis, E., Pabon, J., Park, P., Wu, X., De Jong, Y.P., Schneider, W.M., Molina, H., and Rice, C.M. (2019). Characterization of Novel Splice Variants of Zinc Finger Antiviral Protein (ZAP). J. Virol., 93.","DOI":"10.1128\/JVI.00715-19"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"24303","DOI":"10.1073\/pnas.1913232116","article-title":"Structure of the zinc-finger antiviral protein in complex with RNA reveals a mechanism for selective targeting of CG-rich viral sequences","volume":"116","author":"Meagher","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_244","first-page":"124","article-title":"CG dinucleotide suppression enables antiviral defence targeting non-self RNA","volume":"550","author":"Takata","year":"2017","journal-title":"Nat. Cell Biol."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"14048","DOI":"10.1073\/pnas.1509745112","article-title":"Battle between influenza A virus and a newly identified antiviral activity of the PARP-containing ZAPL protein","volume":"112","author":"Liu","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_246","doi-asserted-by":"crossref","unstructured":"Tang, Q., Wang, X., and Gao, G. (2016). The Short Form of the Zinc Finger Antiviral Protein Inhibits Influenza A Virus Protein Expression and Is Antagonized by the Virus-Encoded NS1. J. Virol., 91.","DOI":"10.1128\/JVI.01909-16"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"12379","DOI":"10.1073\/pnas.1310604110","article-title":"Zinc-finger antiviral protein mediates retinoic acid inducible gene I-like receptor-independent antiviral response to murine leukemia virus","volume":"110","author":"Lee","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"10247","DOI":"10.1128\/JVI.01487-16","article-title":"Sindbis Virus Can Exploit a Host Antiviral Protein To Evade Immune Surveillance","volume":"90","author":"Wang","year":"2016","journal-title":"J. Virol."},{"key":"ref_249","doi-asserted-by":"crossref","unstructured":"Kerns, J.A., Emerman, M., and Malik, H.S. (2008). Positive Selection and Increased Antiviral Activity Associated with the PARP-Containing Isoform of Human Zinc-Finger Antiviral Protein. PLoS Genet., 4.","DOI":"10.1371\/journal.pgen.0040021"},{"key":"ref_250","doi-asserted-by":"crossref","unstructured":"Gon\u00e7alves-Carneiro, D., Takata, M.A., Ong, H., Shilton, A., and Bieniasz, P.D. (2020). Origin and evolution of the Zinc Finger Antiviral Protein. Microbiology.","DOI":"10.1101\/2020.12.04.412510"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/j.dci.2014.05.011","article-title":"Characterisation of chicken ZAP","volume":"46","author":"Goossens","year":"2014","journal-title":"Dev. Comp. Immunol."},{"key":"ref_252","first-page":"7371","article-title":"Zinc finger protein ZFP36L1 inhibits influenza A virus through translational repression by targeting HA, M and NS RNA transcripts","volume":"48","author":"Lin","year":"2020","journal-title":"Nucleic Acids Res."},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1038\/s41467-018-08035-7","article-title":"RNA-binding protein ZFP36L1 regulates osteoarthritis by modulating members of the heat shock protein 70 family","volume":"10","author":"Son","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1038\/nri3344","article-title":"The broad-spectrum antiviral functions of IFIT and IFITM proteins","volume":"13","author":"Diamond","year":"2012","journal-title":"Nat. Rev. Immunol."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1006\/viro.1999.0135","article-title":"Induction of the Human Protein P56 by Interferon, Double-Stranded RNA, or Virus Infection","volume":"267","author":"Guo","year":"2000","journal-title":"Virology"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"624","DOI":"10.1038\/ni.2048","article-title":"IFIT1 is an antiviral protein that recognizes 5\u2032-triphosphate RNA","volume":"12","author":"Pichlmair","year":"2011","journal-title":"Nat. Immunol."},{"key":"ref_257","doi-asserted-by":"crossref","unstructured":"Habjan, M., Hubel, P., Lacerda, L., Benda, C., Holze, C., Eberl, C.H., Mann, A., Kindler, E., Gil-Cruz, C., and Ziebuhr, J. (2013). Sequestration by IFIT1 Impairs Translation of 2\u2032O-unmethylated Capped RNA. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003663"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"9997","DOI":"10.1128\/JVI.00883-13","article-title":"Ifit1 Inhibits Japanese Encephalitis Virus Replication through Binding to 5\u2032 Capped 2\u2032-O Unmethylated RNA","volume":"87","author":"Kimura","year":"2013","journal-title":"J. Virol."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1038\/emboj.2008.241","article-title":"Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1","volume":"27","author":"Terenzi","year":"2008","journal-title":"EMBO J."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1099\/jgv.0.001149","article-title":"Better together: The role of IFIT protein\u2013protein interactions in the antiviral response","volume":"99","author":"Mears","year":"2018","journal-title":"J. Gen. Virol."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"9465","DOI":"10.1128\/JVI.00996-15","article-title":"Human and Murine IFIT1 Proteins Do Not Restrict Infection of Negative-Sense RNA Viruses of the Orthomyxoviridae, Bunyaviridae, and Filoviridae Families","volume":"89","author":"Pinto","year":"2015","journal-title":"J. Virol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"1490","DOI":"10.1038\/s41564-020-0778-x","article-title":"Influenza virus repurposes the antiviral protein IFIT2 to promote translation of viral mRNAs","volume":"5","author":"Tran","year":"2020","journal-title":"Nat. Microbiol."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.dci.2018.02.007","article-title":"Broad-spectrum antiviral functions of duck interferon-induced protein with tetratricopeptide repeats (AvIFIT)","volume":"84","author":"Rong","year":"2018","journal-title":"Dev. Comp. Immunol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-24905-y","article-title":"Chicken Interferon-induced Protein with Tetratricopeptide Repeats 5 Antagonizes Replication of RNA Viruses","volume":"8","author":"Santhakumar","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"Rohaim, M.A., Santhakumar, D., El Naggar, R.F., Iqbal, M., Hussein, H.A., and Munir, M. (2018). Chickens Expressing IFIT5 Ameliorate Clinical Outcome and Pathology of Highly Pathogenic Avian Influenza and Velogenic Newcastle Disease Viruses. Front. Immunol., 9.","DOI":"10.3389\/fimmu.2018.02025"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"18601","DOI":"10.1016\/S0021-9258(17)44794-6","article-title":"Differential expression and distinct structure of 69- and 100-kDa forms of 2-5A synthetase in human cells treated with interferon","volume":"265","author":"Svab","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1089\/jir.2014.0007","article-title":"Viral Phosphodiesterases That Antagonize Double-Stranded RNA Signaling to RNase L by Degrading 2-5A","volume":"34","author":"Silverman","year":"2014","journal-title":"J. Interf. Cytokine Res."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"2108","DOI":"10.1261\/rna.2244210","article-title":"RNase L releases a small RNA from HCV RNA that refolds into a potent PAMP","volume":"16","author":"Malathi","year":"2010","journal-title":"RNA"},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1038\/nature06042","article-title":"Small self-RNA generated by RNase L amplifies antiviral innate immunity","volume":"448","author":"Malathi","year":"2007","journal-title":"Nature"},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1016\/j.immuni.2014.05.007","article-title":"Antiviral Activity of Human OASL Protein Is Mediated by Enhancing Signaling of the RIG-I RNA Sensor","volume":"40","author":"Zhu","year":"2014","journal-title":"Immunity"},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.coviro.2015.07.002","article-title":"Inhibition of the OAS\/RNase L pathway by viruses","volume":"15","author":"Drappier","year":"2015","journal-title":"Curr. Opin. Virol."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"7100","DOI":"10.1073\/pnas.0602184103","article-title":"The primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2\u2032-5\u2032 oligo (A) synthetase\/RNase L pathway","volume":"103","author":"Min","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1073\/pnas.1519657113","article-title":"Activation of RNase L is dependent on OAS3 expression during infection with diverse human viruses","volume":"113","author":"Li","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"6355","DOI":"10.1093\/emboj\/16.21.6355","article-title":"Interferon action and apoptosis are defective in mice devoid of 2\u2032,5\u2032-oligoadenylate-dependent RNase L.","volume":"16","author":"Zhou","year":"1997","journal-title":"EMBO J."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/0092-8674(90)90374-N","article-title":"Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon","volume":"62","author":"Meurs","year":"1990","journal-title":"Cell"},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/j.cell.2005.06.044","article-title":"Higher-Order Substrate Recognition of eIF2\u03b1 by the RNA-Dependent Protein Kinase PKR","volume":"122","author":"Dar","year":"2005","journal-title":"Cell"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"523","DOI":"10.3390\/v1030523","article-title":"Activation of the Antiviral Kinase PKR and Viral Countermeasures","volume":"1","author":"Dauber","year":"2009","journal-title":"Viruses"},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1128\/JVI.02151-06","article-title":"The Cellular Protein P58IPK Regulates Influenza Virus mRNA Translation and Replication through a PKR-Mediated Mechanism","volume":"81","author":"Goodman","year":"2006","journal-title":"J. Virol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1006\/viro.1995.9937","article-title":"Binding of the Influenza Virus NS1 Protein to Double-Stranded RNA Inhibits the Activation of the Protein Kinase That Phosphorylates the eIF-2 Translation Initiation Factor","volume":"214","author":"Lu","year":"1995","journal-title":"Virology"},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"6203","DOI":"10.1128\/JVI.74.13.6203-6206.2000","article-title":"Influenza Virus NS1 Protein Counteracts PKR-Mediated Inhibition of Replication","volume":"74","author":"Bergmann","year":"2000","journal-title":"J. Virol."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"2425","DOI":"10.1128\/JVI.73.3.2425-2433.1999","article-title":"Mutant Influenza Viruses with a Defective NS1 Protein Cannot Block the Activation of PKR in Infected Cells","volume":"73","author":"Hatada","year":"1999","journal-title":"J. Virol."},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"e00198-17","DOI":"10.1128\/JVI.00198-17","article-title":"Influenza A Virus Virulence Depends on Two Amino Acids in the N-Terminal Domain of Its NS1 Protein To Facilitate Inhibition of the RNA-Dependent Protein Kinase PKR","volume":"91","author":"Schierhorn","year":"2017","journal-title":"J. Virol."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S1074-7613(00)00014-5","article-title":"Essential Role for the dsRNA-Dependent Protein Kinase PKR in Innate Immunity to Viral Infection","volume":"13","author":"Balachandran","year":"2000","journal-title":"Immunity"},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.vetmic.2018.11.018","article-title":"Duck innate immune responses to high and low pathogenicity H5 avian influenza viruses","volume":"228","author":"Aldridge","year":"2019","journal-title":"Vet. Microbiol."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"20691","DOI":"10.1016\/S0021-9258(17)32048-3","article-title":"Cloning and expression of cyclosporin A- and FK506-sensitive nuclear factor of activated T-cells: NF45 and NF90","volume":"269","author":"Kao","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"32300","DOI":"10.1074\/jbc.M104207200","article-title":"Characterization of Two Evolutionarily Conserved, Alternatively Spliced Nuclear Phosphoproteins, NFAR-1 and -2, That Function in mRNA Processing and Interact with the Double-stranded RNA-dependent Protein Kinase, PKR","volume":"276","author":"Saunders","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.biochi.2014.10.022","article-title":"NF90 isoforms, a new family of cellular proteins involved in viral replication?","volume":"108","author":"Haenni","year":"2015","journal-title":"Biochimie"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"2797","DOI":"10.1002\/1873-3468.12311","article-title":"NF90 is a novel influenza A virus NS1-interacting protein that antagonizes the inhibitory role of NS1 on PKR phosphorylation","volume":"590","author":"Li","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"3753","DOI":"10.4049\/jimmunol.1302813","article-title":"NF90 Exerts Antiviral Activity through Regulation of PKR Phosphorylation and Stress Granules in Infected Cells","volume":"192","author":"Wen","year":"2014","journal-title":"J. Immunol."},{"key":"ref_290","doi-asserted-by":"crossref","unstructured":"Bortz, E., Westera, L., Maamary, J., Steel, J., Albrecht, R.A., Manicassamy, B., Chase, G., Mart\u00ednez-Sobrido, L., Schwemmle, M., and Garc\u00eda-Sastre, A. (2011). Host- and Strain-Specific Regulation of Influenza Virus Polymerase Activity by Interacting Cellular Proteins. mBio, 2.","DOI":"10.1128\/mBio.00151-11"},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"7850","DOI":"10.1128\/JVI.00735-09","article-title":"Nuclear Factor 90 Negatively Regulates Influenza Virus Replication by Interacting with Viral Nucleoprotein","volume":"83","author":"Wang","year":"2009","journal-title":"J. Virol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1084\/jem.20052078","article-title":"NF90 regulates inducible IL-2 gene expression in T cells","volume":"204","author":"Shi","year":"2007","journal-title":"J. Exp. Med."},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1038\/nrd1853","article-title":"Viral and cellular RNA helicases as antiviral targets","volume":"4","author":"Kwong","year":"2005","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"775","DOI":"10.4161\/rna.7.6.14249","article-title":"RNA helicases","volume":"7","author":"Ranji","year":"2010","journal-title":"RNA Biol."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.molcel.2014.03.017","article-title":"MOV10 Is a 5\u2032 to 3\u2032 RNA Helicase Contributing to UPF1 mRNA Target Degradation by Translocation along 3\u2032 UTRs","volume":"54","author":"Gregersen","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1016\/j.celrep.2014.10.054","article-title":"MOV10 and FMRP Regulate AGO2 Association with MicroRNA Recognition Elements","volume":"9","author":"Kenny","year":"2014","journal-title":"Cell Rep."},{"key":"ref_297","doi-asserted-by":"crossref","unstructured":"Goodier, J.L., Cheung, L.E., and Kazazian, H.H. (2012). MOV10 RNA Helicase Is a Potent Inhibitor of Retrotransposition in Cells. PLoS Genet., 8.","DOI":"10.1371\/journal.pgen.1002941"},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1186\/1742-4690-9-112","article-title":"Host restriction factors in retroviral infection: Promises in virus-host interaction","volume":"9","author":"Zheng","year":"2012","journal-title":"Retrovirology"},{"key":"ref_299","first-page":"481","article-title":"A diverse range of gene products are effectors of the type I interferon antiviral response","volume":"472","author":"Schoggins","year":"2011","journal-title":"Nat. Cell Biol."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"3877","DOI":"10.4049\/jimmunol.1501359","article-title":"MOV10 Provides Antiviral Activity against RNA Viruses by Enhancing RIG-I-MAVS-Independent IFN Induction","volume":"196","author":"Cuevas","year":"2016","journal-title":"J. Immunol."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"3966","DOI":"10.1128\/JVI.03137-15","article-title":"Host Protein Moloney Leukemia Virus 10 (MOV10) Acts as a Restriction Factor of Influenza A Virus by Inhibiting the Nuclear Import of the Viral Nucleoprotein","volume":"90","author":"Zhang","year":"2016","journal-title":"J. Virol."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1042\/BCJ20180754","article-title":"MOV10 sequesters the RNP of influenza A virus in the cytoplasm and is antagonized by viral NS1 protein","volume":"476","author":"Li","year":"2019","journal-title":"Biochem. J."},{"key":"ref_303","doi-asserted-by":"crossref","unstructured":"Skariah, G., Seimetz, J., Norsworthy, M., Lannom, M.C., Kenny, P.J., Elrakhawy, M., Forsthoefel, C., Drnevich, J., Kalsotra, A., and Ceman, S. (2017). Mov10 suppresses retroelements and regulates neuronal development and function in the developing brain. BMC Biol., 15.","DOI":"10.1186\/s12915-017-0387-1"},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/nrm3154","article-title":"From unwinding to clamping\u2014The DEAD box RNA helicase family","volume":"12","author":"Linder","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"1370","DOI":"10.1101\/gad.300624.117","article-title":"SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic R loops and safeguard genome stability","volume":"31","author":"Song","year":"2017","journal-title":"Genes Dev."},{"key":"ref_306","doi-asserted-by":"crossref","unstructured":"Taschuk, F., and Cherry, S. (2020). DEAD-Box Helicases: Sensors, Regulators, and Effectors for Antiviral Defense. Viruses, 12.","DOI":"10.3390\/v12020181"},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1016\/j.chom.2014.03.002","article-title":"Cellular DDX21 RNA Helicase Inhibits Influenza A Virus Replication but Is Counteracted by the Viral NS1 Protein","volume":"15","author":"Chen","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1038\/nrg2485","article-title":"The many roles of histone deacetylases in development and physiology: Implications for disease and therapy","volume":"10","author":"Haberland","year":"2009","journal-title":"Nat. Rev. Genet."},{"key":"ref_309","doi-asserted-by":"crossref","unstructured":"Yamauchi, Y., Boukari, H., Banerjee, I., Sbalzarini, I.F., Horvath, P., and Helenius, A. (2011). Histone Deacetylase 8 Is Required for Centrosome Cohesion and Influenza A Virus Entry. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002316"},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"4614","DOI":"10.1128\/JVI.00126-16","article-title":"Influenza A Virus Dysregulates Host Histone Deacetylase 1 That Inhibits Viral Infection in Lung Epithelial Cells","volume":"90","author":"Nagesh","year":"2016","journal-title":"J. Virol."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.3389\/fmicb.2017.01315","article-title":"Histone Deacetylase 2 Is a Component of Influenza A Virus-Induced Host Antiviral Response","volume":"8","author":"Nagesh","year":"2017","journal-title":"Front. Microbiol."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1257037","article-title":"Influenza A virus uses the aggresome processing machinery for host cell entry","volume":"346","author":"Banerjee","year":"2014","journal-title":"Science"},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"11229","DOI":"10.1128\/JVI.00727-14","article-title":"Histone Deacetylase 6 Inhibits Influenza A Virus Release by Downregulating the Trafficking of Viral Components to the Plasma Membrane via Its Substrate, Acetylated Microtubules","volume":"88","author":"Husain","year":"2014","journal-title":"J. Virol."},{"key":"ref_314","doi-asserted-by":"crossref","unstructured":"Zanin, M., DeBeauchamp, J., Vangala, G., Webby, R.J., and Husain, M. (2020). Histone Deacetylase 6 Knockout Mice Exhibit Higher Susceptibility to Influenza A Virus Infection. Viruses, 12.","DOI":"10.3390\/v12070728"},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"20207","DOI":"10.1074\/jbc.RA119.010650","article-title":"Influenza A virus-induced host caspase and viral PA-X antagonize the antiviral host factor, histone deacetylase 4","volume":"294","author":"Galvin","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_316","doi-asserted-by":"crossref","unstructured":"Koyuncu, E., Budayeva, H.G., Miteva, Y.V., Ricci, D.P., Silhavy, T.J., Shenk, T., and Cristea, I.M. (2014). Sirtuins Are Evolutionarily Conserved Viral Restriction Factors. mBio, 5.","DOI":"10.1128\/mBio.02249-14"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"e12989","DOI":"10.1111\/cmi.12989","article-title":"The Class IV human deacetylase, HDAC11, exhibits anti-influenza A virus properties via its involvement in host innate antiviral response","volume":"21","author":"Nutsford","year":"2019","journal-title":"Cell Microbiol."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1002\/bies.201400058","article-title":"Cracking the ANP32 whips: Important functions, unequal requirement, and hints at disease implications","volume":"36","author":"Reilly","year":"2014","journal-title":"BioEssays"},{"key":"ref_319","first-page":"101","article-title":"Species difference in ANP32A underlies influenza A virus polymerase host restriction","volume":"529","author":"Long","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_320","first-page":"638","article-title":"Host ANP32A mediates the assembly of the influenza virus replicase","volume":"587","author":"Carrique","year":"2020","journal-title":"Nat. Cell Biol."},{"key":"ref_321","first-page":"617","article-title":"A single gene determines the host range of influenza virus","volume":"270","author":"Almond","year":"1977","journal-title":"Nat. Cell Biol."},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"1761","DOI":"10.1128\/jvi.67.4.1761-1764.1993","article-title":"A single amino acid in the PB2 gene of influenza A virus is a determinant of host range","volume":"67","author":"Subbarao","year":"1993","journal-title":"J. Virol."},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1128\/JVI.01633-12","article-title":"Investigation of Influenza Virus Polymerase Activity in Pig Cells","volume":"87","author":"Long","year":"2013","journal-title":"J. Virol."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"13015","DOI":"10.1128\/JVI.01714-09","article-title":"Ostrich Involvement in the Selection of H5N1 Influenza Virus Possessing Mammalian-Type Amino Acids in the PB2 Protein","volume":"83","author":"Shinya","year":"2009","journal-title":"J. Virol."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/JVI.00217-19","article-title":"ANP32 Proteins Are Essential for Influenza Virus Replication in Human Cells","volume":"93","author":"Staller","year":"2019","journal-title":"J. Virol."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1093\/infdis\/jiz506","article-title":"Host-Specific Restriction of Avian Influenza Virus Caused by Differential Dynamics of ANP32 Family Members","volume":"221","author":"Park","year":"2020","journal-title":"J. Infect. Dis."},{"key":"ref_327","doi-asserted-by":"crossref","unstructured":"Reilly, P.T., Afzal, S., Wakeham, A., Haight, J., You-Ten, A., Zaugg, K., Dembowy, J., Young, A., and Mak, T.W. (2010). Generation and Characterization of the Anp32e-Deficient Mouse. PLoS ONE, 5.","DOI":"10.1371\/journal.pone.0013597"},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"450","DOI":"10.3389\/fimmu.2020.00450","article-title":"ANP32B Deficiency Protects Mice From Lethal Influenza A Virus Challenge by Dampening the Host Immune Response","volume":"11","author":"Beck","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"2581","DOI":"10.1016\/j.celrep.2018.08.012","article-title":"Differential Splicing of ANP32A in Birds Alters Its Ability to Stimulate RNA Synthesis by Restricted Influenza Polymerase","volume":"24","author":"Baker","year":"2018","journal-title":"Cell Rep."},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-11388-2","article-title":"Profiling host ANP32A splicing landscapes to predict influenza A virus polymerase adaptation","volume":"10","author":"Domingues","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"198063","DOI":"10.1016\/j.virusres.2020.198063","article-title":"SRSF10 inhibits the polymerase activity and replication of avian influenza virus by regulating the alternative splicing of chicken ANP32A","volume":"286","author":"Fang","year":"2020","journal-title":"Virus Res."},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"15623","DOI":"10.1073\/pnas.95.26.15623","article-title":"Identification of genes differentially regulated by interferon, or using oligonucleotide arrays","volume":"95","author":"Der","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"4203","DOI":"10.1016\/j.jmb.2019.03.013","article-title":"ISG15: It\u2019s Complicated","volume":"431","author":"Dzimianski","year":"2019","journal-title":"J. Mol. Biol."},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.1128\/MCB.01466-09","article-title":"Positive Regulation of Interferon Regulatory Factor 3 Activation by Herc5 via ISG15 Modification","volume":"30","author":"Shi","year":"2010","journal-title":"Mol. Cell. Biol."},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1073\/pnas.0607038104","article-title":"From the cover: IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses","volume":"104","author":"Lenschow","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1128\/JVI.02110-14","article-title":"Novel Mode of ISG15-Mediated Protection against Influenza A Virus and Sendai Virus in Mice","volume":"89","author":"Morales","year":"2014","journal-title":"J. Virol."},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1073\/pnas.0909144107","article-title":"ISG15 conjugation system targets the viral NS1 protein in influenza A virus\u2013infected cells","volume":"107","author":"Zhao","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"5777","DOI":"10.4049\/jimmunol.0903588","article-title":"Herc5 Attenuates Influenza A Virus by Catalyzing ISGylation of Viral NS1 Protein","volume":"184","author":"Tang","year":"2010","journal-title":"J. Immunol."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"7174","DOI":"10.1021\/bi010141t","article-title":"The Human Interferon- and Estrogen-RegulatedISG20\/HEM45Gene Product Degrades Single-Stranded RNA and DNA in Vitro","volume":"40","author":"Nguyen","year":"2001","journal-title":"Biochemistry"},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"35","DOI":"10.5582\/irdr.2017.01004","article-title":"Interferon-stimulated gene 20-kDa protein (ISG20) in infection and disease: Review and outlook","volume":"6","author":"Zheng","year":"2017","journal-title":"Intractable Rare Dis. Res."},{"key":"ref_341","doi-asserted-by":"crossref","unstructured":"Wu, N., Nguyen, X.-N., Wang, L., Appourchaux, R., Zhang, C., Panthu, B., Gruffat, H., Journo, C., Alais, S., and Qin, J. (2019). The interferon stimulated gene 20 protein (ISG20) is an innate defense antiviral factor that discriminates self versus non-self translation. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1008093"},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"16151","DOI":"10.1074\/jbc.M209628200","article-title":"ISG20, a New Interferon-induced RNase Specific for Single-stranded RNA, Defines an Alternative Antiviral Pathway against RNA Genomic Viruses","volume":"278","author":"Espert","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1007\/s11262-016-1366-2","article-title":"Influenza A Virus-induced expression of ISG20 inhibits viral replication by interacting with nucleoprotein","volume":"52","author":"Qu","year":"2016","journal-title":"Virus Genes"},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"e00539-18","DOI":"10.1128\/JVI.00539-18","article-title":"Lnc-ISG20 Inhibits Influenza A Virus Replication by Enhancing ISG20 Expression","volume":"92","author":"Chai","year":"2018","journal-title":"J. Virol."},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"e00209-18","DOI":"10.1128\/mSphere.00209-18","article-title":"The Interferon-Induced Exonuclease ISG20 Exerts Antiviral Activity through Upregulation of Type I Interferon Response Proteins","volume":"3","author":"Weiss","year":"2018","journal-title":"mSphere"},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1038\/ni.3156","article-title":"Intrinsic host restrictions to HIV-1 and mechanisms of viral escape","volume":"16","author":"Simon","year":"2015","journal-title":"Nat. Immunol."},{"key":"ref_347","first-page":"425","article-title":"Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu","volume":"451","author":"Neil","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"ref_348","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/j.cell.2009.08.039","article-title":"Tetherin Inhibits HIV-1 Release by Directly Tethering Virions to Cells","volume":"139","author":"Zang","year":"2009","journal-title":"Cell"},{"key":"ref_349","doi-asserted-by":"crossref","unstructured":"Winkler, M., Bertram, S., Gnir\u00df, K., Nehlmeier, I., Gawanbacht, A., Kirchhoff, F., Ehrhardt, C., Ludwig, S., Kiene, M., and Moldenhauer, A.-S. (2012). Influenza A Virus Does Not Encode a Tetherin Antagonist with Vpu-Like Activity and Induces IFN-Dependent Tetherin Expression in Infected Cells. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0043337"},{"key":"ref_350","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1099\/vir.0.038778-0","article-title":"Release of filamentous and spherical influenza A virus is not restricted by tetherin","volume":"93","author":"Bruce","year":"2012","journal-title":"J. Gen. Virol."},{"key":"ref_351","doi-asserted-by":"crossref","unstructured":"Londrigan, S.L., Tate, M.D., Job, E.R., Moffat, J.M., Wakim, L.M., Gonelli, C.A., Purcell, D.F.J., Brooks, A.G., Villadangos, J.A., and Reading, P.C. (2015). Endogenous Murine BST-2\/Tetherin Is Not a Major Restriction Factor of Influenza A Virus Infection. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0142925"},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.virol.2011.05.006","article-title":"Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin","volume":"417","author":"Watanabe","year":"2011","journal-title":"Virology"},{"key":"ref_353","doi-asserted-by":"crossref","first-page":"9178","DOI":"10.1128\/JVI.00615-15","article-title":"Tetherin Sensitivity of Influenza A Viruses Is Strain Specific: Role of Hemagglutinin and Neuraminidase","volume":"89","author":"Zmora","year":"2015","journal-title":"J. Virol."},{"key":"ref_354","doi-asserted-by":"crossref","first-page":"22015","DOI":"10.1074\/jbc.M111.319996","article-title":"Influenza Virus Partially Counteracts Restriction Imposed by Tetherin\/BST-2","volume":"287","author":"Mangeat","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1016\/j.jmb.2013.12.023","article-title":"Modulation of an Ectodomain Motif in the Influenza A Virus Neuraminidase Alters Tetherin Sensitivity and Results in Virus Attenuation In Vivo","volume":"426","author":"Hai","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref_356","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1042\/BCJ20160861","article-title":"BST-2 restricts IAV release and is countered by the viral M2 protein","volume":"474","author":"Hu","year":"2017","journal-title":"Biochem. J."},{"key":"ref_357","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.1002\/bit.26338","article-title":"Enhanced production of enveloped viruses in BST-2-deficient cell lines","volume":"114","author":"Yi","year":"2017","journal-title":"Biotechnol. Bioeng."},{"key":"ref_358","doi-asserted-by":"crossref","first-page":"2480","DOI":"10.1128\/JVI.02188-10","article-title":"Budding Capability of the Influenza Virus Neuraminidase Can Be Modulated by Tetherin","volume":"85","author":"Yondola","year":"2011","journal-title":"J. Virol."},{"key":"ref_359","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.chom.2016.06.007","article-title":"Origins and Evolution of tetherin, an Orphan Antiviral Gene","volume":"20","author":"Venkatesh","year":"2016","journal-title":"Cell Host Microbe"},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"12154","DOI":"10.1128\/JVI.02149-15","article-title":"Early Vertebrate Evolution of the Host Restriction Factor Tetherin","volume":"89","author":"Heusinger","year":"2015","journal-title":"J. Virol."},{"key":"ref_361","first-page":"01","article-title":"Antiviral Activity and Adaptive Evolution of Avian Tetherins","volume":"94","author":"Hron","year":"2020","journal-title":"J. Virol."},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"15125","DOI":"10.1073\/pnas.011593298","article-title":"Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus","volume":"98","author":"Chin","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_363","first-page":"1","article-title":"Viperin Restricts Zika Virus and Tick-Borne Encephalitis Virus Replication by Targeting NS3 for Proteasomal Degradation","volume":"92","author":"Panayiotou","year":"2018","journal-title":"J. Virol."},{"key":"ref_364","doi-asserted-by":"crossref","first-page":"30529","DOI":"10.1038\/srep30529","article-title":"Viperin inhibits rabies virus replication via reduced cholesterol and sphingomyelin and is regulated upstream by TLR4","volume":"6","author":"Tang","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1002\/jmv.25595","article-title":"Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein","volume":"92","author":"Xu","year":"2020","journal-title":"J. Med. Virol."},{"key":"ref_366","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.chom.2007.06.009","article-title":"The Interferon-Inducible Protein Viperin Inhibits Influenza Virus Release by Perturbing Lipid Rafts","volume":"2","author":"Wang","year":"2007","journal-title":"Cell Host Microbe"},{"key":"ref_367","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1099\/vir.0.040824-0","article-title":"In vivo and in vitro studies on the antiviral activities of viperin against influenza H1N1 virus infection","volume":"93","author":"Tan","year":"2012","journal-title":"J. Gen. Virol."},{"key":"ref_368","doi-asserted-by":"crossref","first-page":"e72","DOI":"10.1111\/j.1755-5922.2010.00171.x","article-title":"Review: Plasminogen Activator Inhibitor-1 (PAI-1): A Key Factor Linking Fibrinolysis and Age-Related Subclinical and Clinical Conditions","volume":"28","author":"Cesari","year":"2010","journal-title":"Cardiovasc. Ther."},{"key":"ref_369","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.cell.2015.01.040","article-title":"A Serpin Shapes the Extracellular Environment to Prevent Influenza A Virus Maturation","volume":"160","author":"Dittmann","year":"2015","journal-title":"Cell"},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.antiviral.2012.01.010","article-title":"Inhibition of Hepatitis B virus replication by Phospholipid scramblase 1 in vitro and in vivo","volume":"94","author":"Yang","year":"2012","journal-title":"Antivir. Res."},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.virol.2012.06.019","article-title":"Human phospholipid scramblase 1 interacts with and regulates transactivation of HTLV-1 Tax","volume":"432","author":"Kusano","year":"2012","journal-title":"Virology"},{"key":"ref_372","doi-asserted-by":"crossref","unstructured":"Luo, W., Zhang, J., Liang, L., Wang, G., Li, Q., Zhu, P., Zhou, Y., Li, J., Zhao, Y., and Sun, N. (2018). Phospholipid scramblase 1 interacts with influenza A virus NP, impairing its nuclear import and thereby suppressing virus replication. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006851"},{"key":"ref_373","doi-asserted-by":"crossref","first-page":"108342","DOI":"10.1016\/j.celrep.2020.108342","article-title":"Type-IInterferon-Inducible SERTAD3 Inhibits Influenza A Virus Replication by Blocking the Assembly of Viral RNA Polymerase Complex","volume":"33","author":"Sun","year":"2020","journal-title":"Cell Rep."},{"key":"ref_374","doi-asserted-by":"crossref","unstructured":"Gao, Q., Yang, C., Ren, C., Zhang, S., Gao, X., Jin, M., Chen, H., Ma, W., and Zhou, H. (2020). Eukaryotic Translation Elongation Factor 1 Delta Inhibits the Nuclear Import of the Nucleoprotein and PA-PB1 Heterodimer of Influenza A Virus. J. Virol., 95.","DOI":"10.1128\/JVI.01391-20"},{"key":"ref_375","doi-asserted-by":"crossref","first-page":"13010","DOI":"10.1128\/JVI.02651-10","article-title":"Generation and Comprehensive Analysis of an Influenza Virus Polymerase Cellular Interaction Network","volume":"85","author":"Tafforeau","year":"2011","journal-title":"J. Virol."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/3\/522\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T05:39:19Z","timestamp":1760161159000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/13\/3\/522"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,3,22]]},"references-count":375,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2021,3]]}},"alternative-id":["v13030522"],"URL":"https:\/\/doi.org\/10.3390\/v13030522","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,3,22]]}}}