{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T17:12:26Z","timestamp":1790529146086,"version":"4.1.0"},"reference-count":83,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2018,12,3]],"date-time":"2018-12-03T00:00:00Z","timestamp":1543795200000},"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>Small Ubiquitin-like MOdifier (SUMO) conjugation to proteins has essential roles in several processes including localization, stability, and function of several players implicated in intrinsic and innate immunity. In human, five paralogs of SUMO are known of which three are ubiquitously expressed (SUMO1, 2, and 3). Infection by rhabdoviruses triggers cellular responses through the activation of pattern recognition receptors, which leads to the production and secretion of interferon. This review will focus on the effects of the stable expression of the different SUMO paralogs or Ubc9 depletion on rhabdoviruses-induced interferon production and interferon signaling pathways as well as on the expression and functions of restriction factors conferring the resistance to rhabdoviruses.<\/jats:p>","DOI":"10.3390\/v10120686","type":"journal-article","created":{"date-parts":[[2018,12,4]],"date-time":"2018-12-04T03:01:37Z","timestamp":1543892497000},"page":"686","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Rhabdoviruses, Antiviral Defense, and SUMO Pathway"],"prefix":"10.3390","volume":"10","author":[{"given":"Faten","family":"El Asmi","sequence":"first","affiliation":[{"name":"INSERM UMR-S 1124, Universit\u00e9 Paris Descartes, 75006 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos Eduardo","family":"Brantis-de-Carvalho","sequence":"additional","affiliation":[{"name":"INSERM UMR-S 1124, Universit\u00e9 Paris Descartes, 75006 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danielle","family":"Blondel","sequence":"additional","affiliation":[{"name":"Institute for Integrative Biology of the Cell (I2BC), Universit\u00e9 Paris-Saclay, CEA, CNRS UMR 9198, Universit\u00e9 Paris-Sud, 91190 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mounira K.","family":"Chelbi-Alix","sequence":"additional","affiliation":[{"name":"INSERM UMR-S 1124, Universit\u00e9 Paris Descartes, 75006 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,12,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.cytogfr.2016.04.003","article-title":"The implication of SUMO in intrinsic and innate immunity","volume":"29","author":"Hannoun","year":"2016","journal-title":"Cytokine Growth Factor Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"6598","DOI":"10.1128\/JVI.00722-16","article-title":"MxA Mediates SUMO-Induced Resistance to Vesicular Stomatitis Virus","volume":"90","author":"Maarifi","year":"2016","journal-title":"J. Virol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2312","DOI":"10.4049\/jimmunol.1500035","article-title":"Small Ubiquitin-like Modifier Alters IFN Response","volume":"195","author":"Maarifi","year":"2015","journal-title":"J. Immunol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1038\/nrm2707","article-title":"An additional role for SUMO in ubiquitin-mediated proteolysis","volume":"10","author":"Geoffroy","year":"2009","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1042\/BST20130015","article-title":"Decoding the SUMO signal","volume":"41","author":"Hay","year":"2013","journal-title":"BioChem. Soc. Trans."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.jaut.2017.09.001","article-title":"SUMO proteins: Guardians of immune system","volume":"84","author":"Adorisio","year":"2017","journal-title":"J. Autoimmun."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/nrm3011","article-title":"The SUMO pathway: Emerging mechanisms that shape specificity, conjugation and recognition","volume":"11","author":"Gareau","year":"2010","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1038\/ncb1716","article-title":"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation","volume":"10","author":"Tatham","year":"2008","journal-title":"Nat. Cell. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1038\/s41598-018-19683-6","article-title":"Differential effects of SUMO1 and SUMO3 on PKR activation and stability","volume":"8","author":"Maarifi","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1074\/mcp.M700173-MCP200","article-title":"In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy","volume":"7","author":"Matic","year":"2008","journal-title":"Mol. Cell Proteomics"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.molcel.2008.10.010","article-title":"The fast-growing business of SUMO chains","volume":"32","author":"Ulrich","year":"2008","journal-title":"Mol. Cell."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1042\/BST0380046","article-title":"SUMO chains: Polymeric signals","volume":"38","author":"Vertegaal","year":"2010","journal-title":"BioChem. Soc. Trans."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"35368","DOI":"10.1074\/jbc.M104214200","article-title":"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1\/SAE2 and Ubc9","volume":"276","author":"Tatham","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev.biochem.73.011303.074118","article-title":"Protein modification by SUMO","volume":"73","author":"Johnson","year":"2004","journal-title":"Annu Rev. Biochem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/S0092-8674(01)00633-X","article-title":"The nucleoporin RanBP2 has SUMO1 E3 ligase activity","volume":"108","author":"Pichler","year":"2002","journal-title":"Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"968","DOI":"10.1038\/nsmb.3116","article-title":"Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase","volume":"22","author":"Cappadocia","year":"2015","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"5007","DOI":"10.1016\/j.febslet.2005.07.088","article-title":"Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo","volume":"579","author":"Weger","year":"2005","journal-title":"FEBS Lett."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1038\/onc.2010.462","article-title":"SUMO E3 ligase activity of TRIM proteins","volume":"30","author":"Chu","year":"2011","journal-title":"Oncogene"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.bbrc.2008.07.070","article-title":"Identification of TRIM22 as a RING finger E3 ubiquitin ligase","volume":"374","author":"Duan","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"14373","DOI":"10.1073\/pnas.0403498101","article-title":"Identification of a SUMO-binding motif that recognizes SUMO-modified proteins","volume":"101","author":"Song","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/s12964-017-0183-0","article-title":"Viral manipulation of the cellular sumoylation machinery","volume":"15","author":"Lowrey","year":"2017","journal-title":"Cell. Commun. Signal."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Wilson, V.G. (2017). Viral Interplay with the Host Sumoylation System. SUMO Regulation of Cellular Processes, Springer International Publishing.","DOI":"10.1007\/978-3-319-50044-7_21"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.celrep.2015.10.001","article-title":"Global Reprogramming of Host SUMOylation during Influenza Virus Infection","volume":"13","author":"Domingues","year":"2015","journal-title":"Cell Rep."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"25660","DOI":"10.1074\/jbc.M804479200","article-title":"Virus infection triggers SUMOylation of IRF3 and IRF7, leading to the negative regulation of type I interferon gene expression","volume":"283","author":"Kubota","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.4161\/cc.25868","article-title":"SUMOylation of p53 mediates interferon activities","volume":"12","author":"Vilas","year":"2013","journal-title":"Cell Cycle"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"e393","DOI":"10.1038\/cddis.2012.135","article-title":"Regulation of the tumor suppressor PTEN by SUMO","volume":"3","author":"Campagna","year":"2012","journal-title":"Cell Death Dis."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"26357","DOI":"10.1074\/jbc.M114.560961","article-title":"Activation of the double-stranded RNA-dependent protein kinase PKR by small ubiquitin-like modifier (SUMO)","volume":"289","author":"Campagna","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1196","DOI":"10.1074\/mcp.RA117.000447","article-title":"Promyelocytic Leukemia Protein (PML) Requirement for Interferon-induced Global Cellular SUMOylation","volume":"17","author":"Maroui","year":"2018","journal-title":"Mol. Cell. Proteomics"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"7754","DOI":"10.1038\/s41598-018-25150-z","article-title":"Quantitative SUMO proteomics reveals the modulation of several PML nuclear body associated proteins and an anti-senescence function of UBC9","volume":"8","author":"McManus","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1007\/s11033-009-9476-8","article-title":"Cloning the human SUMO1 promoter","volume":"37","author":"Deyrieux","year":"2010","journal-title":"Mol. Biol. Rep."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4187","DOI":"10.1038\/ncomms5187","article-title":"Interferon controls SUMO availability via the Lin28 and let-7 axis to impede virus replication","volume":"5","author":"Sahin","year":"2014","journal-title":"Nat. Commun."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.virusres.2016.10.010","article-title":"The family Rhabdoviridae: Mono- and bipartite negative-sense RNA viruses with diverse genome organization and common evolutionary origins","volume":"227","author":"Dietzgen","year":"2017","journal-title":"Virus Res."},{"key":"ref_33","doi-asserted-by":"crossref","unstructured":"Cureton, D.K., Massol, R.H., Saffarian, S., Kirchhausen, T.L., and Whelan, S.P.J. (2009). Vesicular Stomatitis Virus Enters Cells through Vesicles Incompletely Coated with Clathrin That Depend upon Actin for Internalization. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000394"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1128\/JVI.01864-08","article-title":"Host Cell Factors and Functions Involved in Vesicular Stomatitis Virus Entry","volume":"83","author":"Johannsdottir","year":"2009","journal-title":"J. Virol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Piccinotti, S., and Whelan, S.P.J. (2016). Rabies Internalizes into Primary Peripheral Neurons via Clathrin Coated Pits and Requires Fusion at the Cell Body. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1005753"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"117","DOI":"10.3390\/v4010117","article-title":"Molecular and Cellular Aspects of Rhabdovirus Entry","volume":"4","author":"Albertini","year":"2012","journal-title":"Viruses"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"7948","DOI":"10.1128\/JVI.00554-09","article-title":"Functional Characterization of Negri Bodies (NBs) in Rabies Virus-Infected Cells: Evidence that NBs Are Sites of Viral Transcription and Replication","volume":"83","author":"Lahaye","year":"2009","journal-title":"J. Virol."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Heinrich, B.S., Cureton, D.K., Rahmeh, A.A., and Whelan, S.P. (2010). Protein expression redirects vesicular stomatitis virus RNA synthesis to cytoplasmic inclusions. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000958"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/s41467-017-00102-9","article-title":"Negri bodies are viral factories with properties of liquid organelles","volume":"8","author":"Nikolic","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"e02290-17","DOI":"10.1128\/mBio.02290-17","article-title":"Phase Transitions Drive the Formation of Vesicular Stomatitis Virus Replication Compartments","volume":"9","author":"Heinrich","year":"2018","journal-title":"MBio"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/B978-0-12-387040-7.00001-9","article-title":"Chapter 1\u2014Rabies Virus Transcription and Replication","volume":"Volume 79","author":"Jackson","year":"2011","journal-title":"Advances in Virus Research"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.biochi.2007.05.001","article-title":"Interferon, a growing cytokine family: 50 years of interferon research","volume":"89","author":"Wietzerbin","year":"2007","journal-title":"Biochimie"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1038\/nrd2422","article-title":"Interferons at age 50: Past, current and future impact on biomedicine","volume":"6","author":"Borden","year":"2007","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1146\/annurev-immunol-032713-120231","article-title":"Interferon-stimulated genes: A complex web of host defenses","volume":"32","author":"Schneider","year":"2014","journal-title":"Annu. Rev. Immunol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1089\/jir.2011.0099","article-title":"The role of signal transducer and activator of transcription-2 in the interferon response","volume":"32","author":"Steen","year":"2012","journal-title":"J. Interferon Cytokine Res."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.cytogfr.2016.02.010","article-title":"The unique role of STAT2 in constitutive and IFN-induced transcription and antiviral responses","volume":"29","author":"Blaszczyk","year":"2016","journal-title":"Cytokine Growth Factor Rev."},{"key":"ref_47","first-page":"e27521","article-title":"STAT2 and IRF9: Beyond ISGF3","volume":"2","author":"Fink","year":"2013","journal-title":"Jakstat"},{"key":"ref_48","first-page":"e25790","article-title":"STAT2 phosphorylation and signaling","volume":"2","author":"Steen","year":"2013","journal-title":"Jakstat"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1007\/s13238-010-0030-1","article-title":"SUMOylation of RIG-I positively regulates the type I interferon signaling","volume":"1","author":"Mi","year":"2010","journal-title":"Protein Cell"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.molimm.2010.09.003","article-title":"MDA5 is SUMOylated by PIAS2beta in the upregulation of type I interferon signaling","volume":"48","author":"Fu","year":"2011","journal-title":"Mol. Immunol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3675","DOI":"10.3390\/v7072794","article-title":"Resistance to Rhabdoviridae Infection and Subversion of Antiviral Responses","volume":"7","author":"Blondel","year":"2015","journal-title":"Viruses"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"12646","DOI":"10.1128\/JVI.01328-10","article-title":"Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms","volume":"84","author":"Weidner","year":"2010","journal-title":"J. Virol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.immuni.2012.11.005","article-title":"Interferon-inducible cholesterol-25-hydroxylase broadly inhibits viral entry by production of 25-hydroxycholesterol","volume":"38","author":"Liu","year":"2013","journal-title":"Immunity"},{"key":"ref_54","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_55","doi-asserted-by":"crossref","first-page":"4498","DOI":"10.1128\/jvi.65.8.4498-4501.1991","article-title":"Inhibition of vesicular stomatitis virus mRNA synthesis by human MxA protein","volume":"65","author":"Staeheli","year":"1991","journal-title":"J. Virol."},{"key":"ref_56","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_57","doi-asserted-by":"crossref","first-page":"10719","DOI":"10.1128\/JVI.01286-10","article-title":"Resistance to rabies virus infection conferred by the PMLIV isoform","volume":"84","author":"Blondel","year":"2010","journal-title":"J. Virol."},{"key":"ref_58","doi-asserted-by":"crossref","unstructured":"El Asmi, F., Maroui, M.A., Dutrieux, J., Blondel, D., Nisole, S., and Chelbi-Alix, M.K. (2014). Implication of PMLIV in both intrinsic and innate immunity. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1003975"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1043","DOI":"10.1128\/JVI.72.2.1043-1051.1998","article-title":"Resistance to virus infection conferred by the interferon-induced promyelocytic leukemia protein","volume":"72","author":"Quignon","year":"1998","journal-title":"J. Virol."},{"key":"ref_60","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_61","doi-asserted-by":"crossref","first-page":"10303","DOI":"10.1128\/JVI.01341-14","article-title":"Interferon-induced protein Ifit2 protects mice from infection of the peripheral nervous system by vesicular stomatitis virus","volume":"88","author":"Fensterl","year":"2014","journal-title":"J. Virol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Fensterl, V., Wetzel, J.L., Ramachandran, S., Ogino, T., Stohlman, S.A., Bergmann, C.C., Diamond, M.S., Virgin, H.W., and Sen, G.C. (2012). Interferon-induced Ifit2\/ISG54 protects mice from lethal VSV neuropathogenesis. PLoS Pathog., 8.","DOI":"10.1371\/journal.ppat.1002712"},{"key":"ref_63","doi-asserted-by":"crossref","unstructured":"Davis, B.M., Fensterl, V., Lawrence, T.M., Hudacek, A.W., Sen, G.C., and Schnell, M.J. (2017). Ifit2 Is a Restriction Factor in Rabies Virus Pathogenicity. J. Virol., 91.","DOI":"10.1128\/JVI.00889-17"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"10671","DOI":"10.1128\/JVI.00818-10","article-title":"Identification of alpha interferon-induced genes associated with antiviral activity in Daudi cells and characterization of IFIT3 as a novel antiviral gene","volume":"84","author":"Schmeisser","year":"2010","journal-title":"J. Virol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1006\/viro.1999.9614","article-title":"Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus","volume":"256","author":"Anderson","year":"1999","journal-title":"Virology"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1038\/nature01850","article-title":"Integration of interferon-\u03b1\/\u03b2 signalling to p53 responses in tumour suppression and antiviral defence","volume":"424","author":"Takaoka","year":"2003","journal-title":"Nature"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1084\/jem.20080383","article-title":"Transcriptional role of p53 in interferon-mediated antiviral immunity","volume":"205","author":"Macip","year":"2008","journal-title":"J. Exp. Med."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"947","DOI":"10.3389\/fimmu.2017.00947","article-title":"MicroRNA-21: A Positive Regulator for Optimal Production of Type I and Type III Interferon by Plasmacytoid Dendritic Cells","volume":"8","author":"Liu","year":"2017","journal-title":"Front. Immunol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1158\/0008-5472.CAN-09-2377","article-title":"Oncolysis of prostate cancers induced by vesicular stomatitis virus in PTEN knockout mice","volume":"70","author":"Moussavi","year":"2010","journal-title":"Cancer Res."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"3117","DOI":"10.1074\/jbc.273.6.3117","article-title":"Covalent modification of PML by the sentrin family of ubiquitin-like proteins","volume":"273","author":"Kamitani","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_71","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_72","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1034\/j.1600-0854.2002.31003.x","article-title":"Interferon-Induced Mx Proteins: Dynamin-Like GTPases with Antiviral Activity","volume":"3","author":"Haller","year":"2002","journal-title":"Traffic"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"8202","DOI":"10.1128\/JVI.74.17.8202-8206.2000","article-title":"A Monomeric GTPase-Negative MxA Mutant with Antiviral Activity","volume":"74","author":"Janzen","year":"2000","journal-title":"J. Virol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"29893","DOI":"10.1074\/jbc.M115.681494","article-title":"Oligomerization and GTP-binding Requirements of MxA for Viral Target Recognition and Antiviral Activity against Influenza A Virus","volume":"290","author":"Nigg","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.yexcr.2014.10.020","article-title":"MxA interacts with and is modified by the SUMOylation machinery","volume":"330","author":"Maarifi","year":"2015","journal-title":"Exp. Cell. Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1128\/MMBR.00027-06","article-title":"Impact of protein kinase PKR in cell biology: From antiviral to antiproliferative action","volume":"70","author":"Garcia","year":"2006","journal-title":"MicroBiol. Mol. Biol. Rev."},{"key":"ref_77","first-page":"253","article-title":"Structure and function of the protein kinase R","volume":"316","author":"Sadler","year":"2007","journal-title":"Curr Top. MicroBiol. Immunol"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/S0968-0004(00)89025-8","article-title":"PKR: A new name and new roles","volume":"20","author":"Proud","year":"1995","journal-title":"Trends BioChem. Sci."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/j.biochi.2007.03.001","article-title":"The dsRNA protein kinase PKR: Virus and cell control","volume":"89","author":"Garcia","year":"2007","journal-title":"Biochimie"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1111\/j.1432-1033.1987.tb13360.x","article-title":"The double-stranded RNA-dependent protein kinase is also activated by heparin","volume":"167","author":"Hovanessian","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"4379","DOI":"10.1093\/emboj\/17.15.4379","article-title":"PACT, a protein activator of the interferon-induced protein kinase, PKR","volume":"17","author":"Patel","year":"1998","journal-title":"EMBO J."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2839","DOI":"10.1074\/jbc.M112.401851","article-title":"Activation of double-stranded RNA-activated protein kinase (PKR) by interferon-stimulated gene 15 (ISG15) modification down-regulates protein translation","volume":"288","author":"Okumura","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.cell.2016.06.010","article-title":"Compositional Control of Phase-Separated Cellular Bodies","volume":"166","author":"Banani","year":"2016","journal-title":"Cell"}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/12\/686\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:30:53Z","timestamp":1760196653000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/10\/12\/686"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,12,3]]},"references-count":83,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2018,12]]}},"alternative-id":["v10120686"],"URL":"https:\/\/doi.org\/10.3390\/v10120686","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,12,3]]}}}