{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,12]],"date-time":"2025-10-12T03:05:48Z","timestamp":1760238348770,"version":"build-2065373602"},"reference-count":187,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2020,8,1]],"date-time":"2020-08-01T00:00:00Z","timestamp":1596240000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Vetenskapsr\u00e5det","doi-asserted-by":"publisher","award":["2015-02358"],"award-info":[{"award-number":["2015-02358"]}],"id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002794","name":"Cancerfonden","doi-asserted-by":"publisher","award":["2019-"],"award-info":[{"award-number":["2019-"]}],"id":[{"id":"10.13039\/501100002794","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Posttranslational modifications of cellular proteins by covalent conjugation of ubiquitin and ubiquitin-like polypeptides regulate numerous cellular processes that are captured by viruses to promote infection, replication, and spreading. The importance of these protein modifications for the viral life cycle is underscored by the discovery that many viruses encode deconjugases that reverse their functions. The structural and functional characterization of these viral enzymes and the identification of their viral and cellular substrates is providing valuable insights into the biology of viral infections and the host\u2019s antiviral defense. Given the growing body of evidence demonstrating their key contribution to pathogenesis, the viral deconjugases are now recognized as attractive targets for the design of novel antiviral therapeutics.<\/jats:p>","DOI":"10.3390\/biom10081137","type":"journal-article","created":{"date-parts":[[2020,8,3]],"date-time":"2020-08-03T06:16:47Z","timestamp":1596435407000},"page":"1137","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Viral Ubiquitin and Ubiquitin-Like Deconjugases\u2014Swiss Army Knives for Infection"],"prefix":"10.3390","volume":"10","author":[{"given":"Maria Grazia","family":"Masucci","sequence":"first","affiliation":[{"name":"Department of Cell and Molecular Biology, Karolinska Institutet, S-17177 Stockholm, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2020,8,1]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1152\/physrev.00027.2001","article-title":"The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction","volume":"82","author":"Glickman","year":"2002","journal-title":"Physiol. Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1038\/nature07958","article-title":"Origin and function of ubiquitin-like proteins","volume":"458","author":"Hochstrasser","year":"2009","journal-title":"Nature"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1146\/annurev-biochem-093010-153308","article-title":"Ubiquitin-like proteins","volume":"81","author":"Ploegh","year":"2012","journal-title":"Annu. Rev. Biochem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1146\/annurev.cellbio.22.010605.093503","article-title":"Modification of proteins by ubiquitin and ubiquitin-like proteins","volume":"22","author":"Kerscher","year":"2006","journal-title":"Annu. Rev. Cell. Dev. Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3989","DOI":"10.1074\/jbc.M510787200","article-title":"The interferon-inducible ubiquitin-protein isopeptide ligase (E3) EFP also functions as an ISG15 E3 ligase","volume":"281","author":"Zou","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.cell.2004.06.016","article-title":"Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity","volume":"118","author":"Xirodimas","year":"2004","journal-title":"Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"9102","DOI":"10.1074\/jbc.M112.438234","article-title":"UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131","volume":"288","author":"Oh","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_9","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_10","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_11","doi-asserted-by":"crossref","first-page":"5433","DOI":"10.1091\/mbc.e05-08-0731","article-title":"TRAF7 sequesters c-Myb to the cytoplasm by stimulating its sumoylation","volume":"16","author":"Morita","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1042\/BST0370937","article-title":"The emerging complexity of protein ubiquitination","volume":"37","author":"Komander","year":"2009","journal-title":"Biochem. Soc. Trans."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1042\/BJ20061138","article-title":"Ubiquitin-binding domains","volume":"399","author":"Hurley","year":"2006","journal-title":"Biochem. J."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/ncb3358","article-title":"The increasing complexity of the ubiquitin code","volume":"18","author":"Yau","year":"2016","journal-title":"Nat. Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.molcel.2018.07.027","article-title":"SUMO-Mediated Regulation of Nuclear Functions and Signaling Processes","volume":"71","author":"Zhao","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_16","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_17","doi-asserted-by":"crossref","first-page":"177","DOI":"10.2174\/1389203043379783","article-title":"Cullin-based ubiquitin ligase and its control by NEDD8-conjugating system","volume":"5","author":"Chiba","year":"2004","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1073\/pnas.1019043108","article-title":"Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress","volume":"108","author":"Petroski","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1038\/nature07643","article-title":"Ubiquitin-related modifier Urm1 acts as a sulphur carrier in thiolation of eukaryotic transfer RNA","volume":"458","author":"Leidel","year":"2009","journal-title":"Nature"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1016\/j.tcb.2019.09.005","article-title":"The UFMylation System in Proteostasis and Beyond","volume":"29","author":"Gerakis","year":"2019","journal-title":"Trends Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1073\/pnas.1816202116","article-title":"Ribosomal protein RPL26 is the principal target of UFMylation","volume":"116","author":"Walczak","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Mah, M.M., Roverato, N., and Groettrup, M. (2020). Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10. Biomolecules, 10.","DOI":"10.3390\/biom10060951"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/j.it.2016.11.001","article-title":"ISG15: In Sickness and in Health","volume":"38","author":"Hermann","year":"2017","journal-title":"Trends Immunol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1089\/jir.2010.0110","article-title":"Interferon-stimulated gene 15 and the protein ISGylation system","volume":"31","author":"Zhang","year":"2011","journal-title":"J. Interferon. Cytokine Res."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1186\/gb-2011-12-7-226","article-title":"Atg8: An autophagy-related ubiquitin-like protein family","volume":"12","author":"Shpilka","year":"2011","journal-title":"Genome Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"550","DOI":"10.1038\/nrm2731","article-title":"Breaking the chains: Structure and function of the deubiquitinases","volume":"10","author":"Komander","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1242\/jcs.090985","article-title":"Cellular functions of the DUBs","volume":"125","author":"Clague","year":"2012","journal-title":"J. Cell. Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1550","DOI":"10.1016\/j.chembiol.2011.10.017","article-title":"The differential modulation of USP activity by internal regulatory domains, interactors and eight ubiquitin chain types","volume":"18","author":"Faesen","year":"2011","journal-title":"Chem. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/j.cell.2013.05.046","article-title":"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis","volume":"154","author":"Mevissen","year":"2013","journal-title":"Cell"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Catic, A., Fiebiger, E., Korbel, G.A., Blom, D., Galardy, P.J., and Ploegh, H.L. (2007). Screen for ISG15-crossreactive deubiquitinases. PLoS ONE, 2.","DOI":"10.1371\/journal.pone.0000679"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"28892","DOI":"10.1074\/jbc.M302890200","article-title":"Identification and characterization of DEN1, a deneddylase of the ULP family","volume":"278","author":"Nagamalleswari","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"161","DOI":"10.3389\/fmicb.2011.00161","article-title":"Viral takeover of the host ubiquitin system","volume":"2","author":"Gustin","year":"2011","journal-title":"Front Microbiol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/978-3-319-50044-7_21","article-title":"Viral Interplay with the Host Sumoylation System","volume":"963","author":"Wilson","year":"2017","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"3584","DOI":"10.3390\/v6093584","article-title":"The role of ubiquitin and ubiquitin-like modification systems in papillomavirus biology","volume":"6","author":"Wilson","year":"2014","journal-title":"Viruses"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1111\/boc.201100096","article-title":"Emerging roles for ubiquitin in adenovirus cell entry","volume":"104","author":"Marvin","year":"2012","journal-title":"Biol. Cell"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"386","DOI":"10.3390\/cells3020386","article-title":"The ubiquitin-conjugating system: Multiple roles in viral replication and infection","volume":"3","author":"Calistri","year":"2014","journal-title":"Cells"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/S0065-2776(06)92006-9","article-title":"Antigen presentation and the ubiquitin-proteasome system in host-pathogen interactions","volume":"92","author":"Loureiro","year":"2006","journal-title":"Adv. Immunol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/cr.2016.40","article-title":"Ubiquitin signaling in immune responses","volume":"26","author":"Hu","year":"2016","journal-title":"Cell Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.virol.2015.02.033","article-title":"Ubiquitination in the antiviral immune response","volume":"479\u2013480","author":"Davis","year":"2015","journal-title":"Virology"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1146\/annurev-immunol-032713-120156","article-title":"Innate immune sensing and signaling of cytosolic nucleic acids","volume":"32","author":"Wu","year":"2014","journal-title":"Annu. Rev. Immunol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/BJ20090272","article-title":"Pathogen recognition in the innate immune response","volume":"420","author":"Kumar","year":"2009","journal-title":"Biochem. J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/j.tim.2017.01.001","article-title":"Transcriptional Regulation of Antiviral Interferon-Stimulated Genes","volume":"25","author":"Wang","year":"2017","journal-title":"Trends Microbiol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1002\/embr.201338025","article-title":"Ubiquitin in the immune system","volume":"15","author":"Zinngrebe","year":"2014","journal-title":"EMBO Rep."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1146\/annurev.immunol.22.012703.104813","article-title":"Ubiquitin ligases and the immune response","volume":"22","author":"Liu","year":"2004","journal-title":"Annu. Rev. Immunol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1093\/jmcb\/mju005","article-title":"TRIM4 modulates type I interferon induction and cellular antiviral response by targeting RIG-I for K63-linked ubiquitination","volume":"6","author":"Yan","year":"2014","journal-title":"J. Mol. Cell Biol."},{"key":"ref_46","doi-asserted-by":"crossref","unstructured":"Oshiumi, H., Miyashita, M., Matsumoto, M., and Seya, T. (2013). A distinct role of Riplet-mediated K63-Linked polyubiquitination of the RIG-I repressor domain in human antiviral innate immune responses. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003533"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1038\/nature05732","article-title":"TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity","volume":"446","author":"Gack","year":"2007","journal-title":"Nature"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"7500","DOI":"10.1073\/pnas.0611551104","article-title":"Negative regulation of the RIG-I signaling by the ubiquitin ligase RNF125","volume":"104","author":"Arimoto","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"13293","DOI":"10.1073\/pnas.1905873116","article-title":"The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells","volume":"116","author":"Kelsall","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"3538","DOI":"10.1128\/MCB.02098-07","article-title":"Lys63-linked polyubiquitination of IRAK-1 is required for interleukin-1 receptor- and toll-like receptor-mediated NF-kappaB activation","volume":"28","author":"Conze","year":"2008","journal-title":"Mol. Cell Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1943","DOI":"10.4049\/jimmunol.1800750","article-title":"UBL4A Augments Innate Immunity by Promoting the K63-Linked Ubiquitination of TRAF6","volume":"203","author":"Peng","year":"2019","journal-title":"J. Immunol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"e1800","DOI":"10.1038\/cddis.2015.158","article-title":"Cellular IAP proteins and LUBAC differentially regulate necrosome-associated RIP1 ubiquitination","volume":"6","author":"Goncharov","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Zhu, Q., Yu, T., Gan, S., Wang, Y., Pei, Y., Zhao, Q., Pei, S., Hao, S., Yuan, J., and Xu, J. (2020). TRIM24 facilitates antiviral immunity through mediating K63-linked TRAF3 ubiquitination. J. Exp. Med., 217.","DOI":"10.1084\/jem.20192083"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1038\/ni.3641","article-title":"The ubiquitin E3 ligase TRIM31 promotes aggregation and activation of the signaling adaptor MAVS through Lys63-linked polyubiquitination","volume":"18","author":"Liu","year":"2017","journal-title":"Nat. Immunol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.chom.2012.06.009","article-title":"Linear ubiquitination of NEMO negatively regulates the interferon antiviral response through disruption of the MAVS-TRAF3 complex","volume":"12","author":"Belgnaoui","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Ni, G., Konno, H., and Barber, G.N. (2017). Ubiquitination of STING at lysine 224 controls IRF3 activation. Sci. Immunol., 2.","DOI":"10.1126\/sciimmunol.aah7119"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1111\/j.1600-065X.2012.01108.x","article-title":"Ubiquitination in signaling to and activation of IKK","volume":"246","author":"Chen","year":"2012","journal-title":"Immunol. Rev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"3214","DOI":"10.1038\/sj.onc.1210413","article-title":"Ubiquitin-mediated activation of TAK1 and IKK","volume":"26","author":"Adhikari","year":"2007","journal-title":"Oncogene"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1038\/25159","article-title":"Identification of the receptor component of the IkappaBalpha-ubiquitin ligase","volume":"396","author":"Yaron","year":"1998","journal-title":"Nature"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"351","DOI":"10.15252\/embj.201796781","article-title":"LRRC25 inhibits type I IFN signaling by targeting ISG15-associated RIG-I for autophagic degradation","volume":"37","author":"Du","year":"2018","journal-title":"EMBO J."},{"key":"ref_61","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_62","doi-asserted-by":"crossref","first-page":"23377","DOI":"10.1038\/srep23377","article-title":"Ubiquitin-like modifier FAT10 attenuates RIG-I mediated antiviral signaling by segregating activated RIG-I from its signaling platform","volume":"6","author":"Nguyen","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.bbrc.2016.11.084","article-title":"MyD88 NEDDylation negatively regulates MyD88-dependent NF-kappaB signaling through antagonizing its ubiquitination","volume":"482","author":"Yan","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_64","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_65","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/nri3581","article-title":"Regulation of type I interferon responses","volume":"14","author":"Ivashkiv","year":"2014","journal-title":"Nat. Rev. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"496","DOI":"10.1016\/j.bbrc.2005.08.132","article-title":"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells","volume":"336","author":"Giannakopoulos","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Freitas, B.T., Scholte, F.E.M., Bergeron, E., and Pegan, S.D. (2020). How ISG15 combats viral infection. Virus Res.","DOI":"10.1016\/j.virusres.2020.198036"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1038\/s41579-018-0020-5","article-title":"ISG15 in antiviral immunity and beyond","volume":"16","author":"Perng","year":"2018","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.molcel.2010.05.002","article-title":"The ISG15 conjugation system broadly targets newly synthesized proteins: Implications for the antiviral function of ISG15","volume":"38","author":"Durfee","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"12754","DOI":"10.1038\/ncomms12754","article-title":"Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins","volume":"7","author":"Zhao","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"4311","DOI":"10.4049\/jimmunol.1000098","article-title":"Inhibition of hepatitis C virus replication by IFN-mediated ISGylation of HCV-NS5A","volume":"185","author":"Kim","year":"2010","journal-title":"J. Immunol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.chom.2013.10.011","article-title":"Type I interferon imposes a TSG101\/ISG15 checkpoint at the Golgi for glycoprotein trafficking during influenza virus infection","volume":"14","author":"Sanyal","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3974","DOI":"10.1073\/pnas.0710629105","article-title":"ISG15 inhibits Ebola VP40 VLP budding in an L-domain-dependent manner by blocking Nedd4 ligase activity","volume":"105","author":"Okumura","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"47052","DOI":"10.18632\/oncotarget.9720","article-title":"Transcriptomic analysis of KSHV-infected primary oral fibroblasts: The role of interferon-induced genes in the latency of oncogenic virus","volume":"7","author":"Dai","year":"2016","journal-title":"Oncotarget"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"11572","DOI":"10.1128\/JVI.01482-15","article-title":"Kaposi\u2019s Sarcoma-Associated Herpesvirus Viral Interferon Regulatory Factor 1 Interacts with a Member of the Interferon-Stimulated Gene 15 Pathway","volume":"89","author":"Jacobs","year":"2015","journal-title":"J. Virol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"4100","DOI":"10.4049\/jimmunol.157.9.4100","article-title":"In vitro and in vivo secretion of human ISG15, an IFN-induced immunomodulatory cytokine","volume":"157","author":"Ramanujam","year":"1996","journal-title":"J. Immunol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1073\/pnas.93.1.211","article-title":"Immunoregulatory properties of ISG15, an interferon-induced cytokine","volume":"93","author":"Knight","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/j.bbrc.2003.08.038","article-title":"Identification of a ubiquitin family protein as a novel neutrophil chemotactic factor","volume":"309","author":"Owhashi","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"1107","DOI":"10.1016\/j.bbrc.2016.11.166","article-title":"Influenza a virus NS1 protein induced A20 contributes to viral replication by suppressing interferon-induced antiviral response","volume":"482","author":"Feng","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Karim, R., Tummers, B., Meyers, C., Biryukov, J.L., Alam, S., Backendorf, C., Jha, V., Offringa, R., van Ommen, G.J., and Melief, C.J. (2013). Human papillomavirus (HPV) upregulates the cellular deubiquitinase UCHL1 to suppress the keratinocyte\u2019s innate immune response. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003384"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1080\/1040841X.2017.1368999","article-title":"Viral deubiquitinases: Role in evasion of anti-viral innate immunity","volume":"44","author":"Kumari","year":"2018","journal-title":"Crit. Rev. Microbiol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"3441","DOI":"10.1016\/j.jmb.2017.06.010","article-title":"Structure and Function of Viral Deubiquitinating Enzymes","volume":"429","author":"Knaap","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.2217\/fmb-2016-0091","article-title":"Manipulation of viral infection by deubiquitinating enzymes: New players in host-virus interactions","volume":"11","author":"Gu","year":"2016","journal-title":"Future Microbiol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"10477","DOI":"10.1128\/JVI.01113-08","article-title":"Epstein-barr virus encodes three bona fide ubiquitin-specific proteases","volume":"82","author":"Sompallae","year":"2008","journal-title":"J. Virol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1038\/ncb2035","article-title":"A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases","volume":"12","author":"Gastaldello","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"6323","DOI":"10.1128\/JVI.76.12.6323-6331.2002","article-title":"Deubiquitinating function of adenovirus proteinase","volume":"76","author":"Balakirev","year":"2002","journal-title":"J. Virol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/0076-6879(94)44043-3","article-title":"Adenovirus endopeptidases","volume":"244","author":"Weber","year":"1994","journal-title":"Methods Enzymol."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Ye, R., Su, C., Xu, H., and Zheng, C. (2017). Herpes Simplex Virus 1 Ubiquitin-Specific Protease UL36 Abrogates NF-kappaB Activation in DNA Sensing Signal Pathway. J. Virol., 91.","DOI":"10.1128\/JVI.02417-16"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"11851","DOI":"10.1128\/JVI.01211-13","article-title":"Herpes simplex virus 1 ubiquitin-specific protease UL36 inhibits beta interferon production by deubiquitinating TRAF3","volume":"87","author":"Wang","year":"2013","journal-title":"J. Virol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.molcel.2005.07.003","article-title":"A deubiquitinating enzyme encoded by HSV-1 belongs to a family of cysteine proteases that is conserved across the family Herpesviridae","volume":"19","author":"Kattenhorn","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"8738","DOI":"10.1128\/JVI.00798-11","article-title":"Autocatalytic activity of the ubiquitin-specific protease domain of herpes simplex virus 1 VP1-2","volume":"85","author":"Bolstad","year":"2011","journal-title":"J. Virol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"8472","DOI":"10.1074\/jbc.M117.778076","article-title":"The herpes simplex virus 1 UL36USP deubiquitinase suppresses DNA repair in host cells via deubiquitination of proliferating cell nuclear antigen","volume":"292","author":"Dong","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"12046","DOI":"10.1128\/JVI.00411-09","article-title":"Cleavage specificity of the UL48 deubiquitinating protease activity of human cytomegalovirus and the growth of an active-site mutant virus in cultured cells","volume":"83","author":"Kim","year":"2009","journal-title":"J. Virol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3229","DOI":"10.1128\/JVI.02766-15","article-title":"Involvement of the N-Terminal Deubiquitinating Protease Domain of Human Cytomegalovirus UL48 Tegument Protein in Autoubiquitination, Virion Stability, and Virus Entry","volume":"90","author":"Kim","year":"2016","journal-title":"J. Virol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"6003","DOI":"10.1128\/JVI.00401-06","article-title":"High-molecular-weight protein (pUL48) of human cytomegalovirus is a competent deubiquitinating protease: Mutant viruses altered in its active-site cysteine or histidine are viable","volume":"80","author":"Wang","year":"2006","journal-title":"J. Virol."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Kwon, K.M., Oh, S.E., Kim, Y.E., Han, T.H., and Ahn, J.H. (2017). Cooperative inhibition of RIP1-mediated NF-kappaB signaling by cytomegalovirus-encoded deubiquitinase and inactive homolog of cellular ribonucleotide reductase large subunit. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006423"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"8097","DOI":"10.1128\/JVI.00588-12","article-title":"Epstein-Barr virus BPLF1 deubiquitinates PCNA and attenuates polymerase eta recruitment to DNA damage sites","volume":"86","author":"Whitehurst","year":"2012","journal-title":"J. Virol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"van Gent, M., Braem, S.G., de Jong, A., Delagic, N., Peeters, J.G., Boer, I.G., Moynagh, P.N., Kremmer, E., Wiertz, E.J., and Ovaa, H. (2014). Epstein-Barr virus large tegument protein BPLF1 contributes to innate immune evasion through interference with toll-like receptor signaling. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1003960"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"4345","DOI":"10.1128\/JVI.02195-08","article-title":"The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity","volume":"83","author":"Whitehurst","year":"2009","journal-title":"J. Virol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"6411","DOI":"10.1128\/JVI.00536-14","article-title":"The Rad6\/18 ubiquitin complex interacts with the Epstein-Barr virus deubiquitinating enzyme, BPLF1, and contributes to virus infectivity","volume":"88","author":"Kumar","year":"2014","journal-title":"J. Virol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"10224","DOI":"10.1128\/JVI.00589-09","article-title":"Kaposi\u2019s sarcoma-associated herpesvirus encodes a viral deubiquitinase","volume":"83","author":"Gonzalez","year":"2009","journal-title":"J. Virol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"10899","DOI":"10.1128\/JVI.00690-11","article-title":"Inhibition of RIG-I-mediated signaling by Kaposi\u2019s sarcoma-associated herpesvirus-encoded deubiquitinase ORF64","volume":"85","author":"Inn","year":"2011","journal-title":"J. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"16119","DOI":"10.1073\/pnas.0805240105","article-title":"A noncovalent class of papain-like protease\/deubiquitinase inhibitors blocks SARS virus replication","volume":"105","author":"Ratia","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.molcel.2016.04.016","article-title":"Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease","volume":"62","author":"Bekes","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1007\/s13238-014-0026-3","article-title":"SARS coronavirus papain-like protease inhibits the type I interferon signaling pathway through interaction with the STING-TRAF3-TBK1 complex","volume":"5","author":"Chen","year":"2014","journal-title":"Protein Cell"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.virol.2013.11.040","article-title":"MERS-CoV papain-like protease has deISGylating and deubiquitinating activities","volume":"450\u2013451","author":"Mielech","year":"2014","journal-title":"Virology"},{"key":"ref_107","doi-asserted-by":"crossref","unstructured":"Klemm, T., Ebert, G., Calleja, D., Allisons, C., Rihardson, L., Brenardini, J., Lu, B., Kuchel, N., Grohmann, C., and Shibata, Y. (2020). Mechanisms of inhibition of SARS-CoV-2 PLpro. bioRxiv.","DOI":"10.1101\/2020.06.18.160614"},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Shin, D., Mukherjee, R., Grew, D., Bojkova, D., Beek, K., Bhattacharya, A., Schulz, L., Widera, M., Mehdipour, A., and Tascher, G. (2020). Inhibition of papain-like protease PLpro blocks SARS-CoV-2 spread and promotes anti-viral immunity. Res. Square.","DOI":"10.21203\/rs.3.rs-27134\/v1"},{"key":"ref_109","doi-asserted-by":"crossref","unstructured":"Rut, W., Lv, Z., Zmudzinski, M., Patchett, S., Nayak, D., Snipas, S.J., El Oualid, F., Huang, T.T., Bekes, M., and Drag, M. (2020). Activity profiling and structures of inhibitor-bound SARS-CoV-2-PLpro protease provides a framework for anti-COVID-19 drug design. bioRxiv.","DOI":"10.1101\/2020.04.29.068890"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"15199","DOI":"10.1128\/JVI.79.24.15199-15208.2005","article-title":"The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme","volume":"79","author":"Lindner","year":"2005","journal-title":"J. Virol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"4550","DOI":"10.1128\/JVI.79.7.4550-4551.2005","article-title":"Deubiquitination, a new function of the severe acute respiratory syndrome coronavirus papain-like protease?","volume":"79","author":"Sulea","year":"2005","journal-title":"J. Virol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"5717","DOI":"10.1073\/pnas.0510851103","article-title":"Severe acute respiratory syndrome coronavirus papain-like protease: Structure of a viral deubiquitinating enzyme","volume":"103","author":"Ratia","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/j.chom.2007.09.014","article-title":"Ovarian tumor domain-containing viral proteases evade ubiquitin- and ISG15-dependent innate immune responses","volume":"2","author":"Giannakopoulos","year":"2007","journal-title":"Cell Host Microbe"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1016\/j.molcel.2007.01.033","article-title":"Structure of a herpesvirus-encoded cysteine protease reveals a unique class of deubiquitinating enzymes","volume":"25","author":"Schlieker","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.antiviral.2017.11.001","article-title":"Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein","volume":"149","author":"Lei","year":"2018","journal-title":"Antiviral Res."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.antiviral.2014.12.015","article-title":"The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds","volume":"115","author":"Mesecar","year":"2015","journal-title":"Antiviral Res."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"3682","DOI":"10.1128\/JVI.06432-11","article-title":"The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus","volume":"86","author":"Schipke","year":"2012","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1111\/cmi.12075","article-title":"Cytosolic herpes simplex virus capsids not only require binding inner tegument protein pUL36 but also pUL37 for active transport prior to secondary envelopment","volume":"15","author":"Sandbaumhuter","year":"2013","journal-title":"Cell Microbiol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"8847","DOI":"10.1128\/JVI.79.14.8847-8860.2005","article-title":"Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress","volume":"79","author":"Turcotte","year":"2005","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"11608","DOI":"10.1128\/JVI.74.24.11608-11618.2000","article-title":"A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells","volume":"74","author":"Desai","year":"2000","journal-title":"J. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"e01574-15","DOI":"10.1128\/mBio.01574-15","article-title":"Knockout of Epstein-Barr virus BPLF1 retards B-cell transformation and lymphoma formation in humanized mice","volume":"6","author":"Whitehurst","year":"2015","journal-title":"mBio"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1660","DOI":"10.1128\/JVI.01139-08","article-title":"Herpes simplex virus replication: Roles of viral proteins and nucleoporins in capsid-nucleus attachment","volume":"83","author":"Copeland","year":"2009","journal-title":"J. Virol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"3311","DOI":"10.1128\/JVI.01919-07","article-title":"Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleus","volume":"82","author":"Jovasevic","year":"2008","journal-title":"J. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1556\/AMicr.50.2003.1.9","article-title":"Adenain, the adenovirus endoprotease (a review)","volume":"50","author":"Weber","year":"2003","journal-title":"Acta Microbiol. Immunol. Hung."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1766","DOI":"10.1002\/j.1460-2075.1996.tb00525.x","article-title":"The role of the adenovirus protease on virus entry into cells","volume":"15","author":"Greber","year":"1996","journal-title":"EMBO J."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"32511","DOI":"10.1074\/jbc.271.51.32511","article-title":"Cleavage efficiency by adenovirus protease is site-dependent","volume":"271","author":"Diouri","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1099\/vir.0.19424-0","article-title":"Mechanisms and enzymes involved in SARS coronavirus genome expression","volume":"84","author":"Thiel","year":"2003","journal-title":"J. Gen. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"15189","DOI":"10.1128\/JVI.79.24.15189-15198.2005","article-title":"The papain-like protease of severe acute respiratory syndrome coronavirus has deubiquitinating activity","volume":"79","author":"Barretto","year":"2005","journal-title":"J. Virol."},{"key":"ref_129","doi-asserted-by":"crossref","unstructured":"Ratia, K., Kilianski, A., Baez-Santos, Y.M., Baker, S.C., and Mesecar, A. (2014). Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004113"},{"key":"ref_130","first-page":"453","article-title":"Picornaviridae: The viruses and their replication","volume":"1","author":"Knipe","year":"2013","journal-title":"Fields Virology"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"190","DOI":"10.3181\/00379727-121-30734","article-title":"A new virus isolated from the human respiratory tract","volume":"121","author":"Hamre","year":"1966","journal-title":"Proc. Soc. Exp. Biol. Med."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1056\/NEJMoa030747","article-title":"Identification of a novel coronavirus in patients with severe acute respiratory syndrome","volume":"348","author":"Drosten","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1953","DOI":"10.1056\/NEJMoa030781","article-title":"A novel coronavirus associated with severe acute respiratory syndrome","volume":"348","author":"Ksiazek","year":"2003","journal-title":"N. Engl. J. Med."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1056\/NEJMoa1211721","article-title":"Isolation of a novel coronavirus from a man with pneumonia in Saudi Arabia","volume":"367","author":"Zaki","year":"2012","journal-title":"N. Engl. J. Med."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1056\/NEJMoa2001017","article-title":"A Novel Coronavirus from Patients with Pneumonia in China, 2019","volume":"382","author":"Zhu","year":"2020","journal-title":"N. Engl. J. Med."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1001\/jama.2017.21907","article-title":"Acute Respiratory Distress Syndrome: Advances in Diagnosis and Treatment","volume":"319","author":"Fan","year":"2018","journal-title":"JAMA"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"155143","DOI":"10.1016\/j.cyto.2020.155143","article-title":"Altered cytokine levels and immune responses in patients with SARS-CoV-2 infection and related conditions","volume":"133","author":"Noroozi","year":"2020","journal-title":"Cytokine"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"13800","DOI":"10.1128\/JVI.79.21.13800-13805.2005","article-title":"Severe acute respiratory syndrome coronavirus fails to activate cytokine-mediated innate immune responses in cultured human monocyte-derived dendritic cells","volume":"79","author":"Ziegler","year":"2005","journal-title":"J. Virol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3625","DOI":"10.1172\/JCI126363","article-title":"IFN-I response timing relative to virus replication determines MERS coronavirus infection outcomes","volume":"129","author":"Channappanavar","year":"2019","journal-title":"J. Clin. Investig."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1016\/j.cell.2020.04.026","article-title":"Imbalanced Host Response to SARS-CoV-2 Drives Development of COVID-19","volume":"181","author":"Liu","year":"2020","journal-title":"Cell"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.chom.2016.01.007","article-title":"Dysregulated Type I Interferon and Inflammatory Monocyte-Macrophage Responses Cause Lethal Pneumonia in SARS-CoV-Infected Mice","volume":"19","author":"Channappanavar","year":"2016","journal-title":"Cell Host Microbe"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.antiviral.2014.06.011","article-title":"Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features","volume":"109","author":"Lei","year":"2014","journal-title":"Antiviral Res."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"6689","DOI":"10.1128\/JVI.02220-08","article-title":"Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling","volume":"83","author":"Frieman","year":"2009","journal-title":"J. Virol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.abb.2007.07.006","article-title":"Selectivity in ISG15 and ubiquitin recognition by the SARS coronavirus papain-like protease","volume":"466","author":"Lindner","year":"2007","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"32208","DOI":"10.1074\/jbc.M704870200","article-title":"Regulation of IRF-3-dependent innate immunity by the papain-like protease domain of the severe acute respiratory syndrome coronavirus","volume":"282","author":"Devaraj","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"34667","DOI":"10.1074\/jbc.M114.609644","article-title":"Crystal structure of the Middle East respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression","volume":"289","author":"Knaap","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.virusres.2007.03.015","article-title":"SARS coronavirus and innate immunity","volume":"133","author":"Frieman","year":"2008","journal-title":"Virus Res."},{"key":"ref_148","first-page":"E3119","article-title":"Mouse-adapted MERS coronavirus causes lethal lung disease in human DPP4 knockin mice","volume":"114","author":"Li","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1099\/vir.0.059014-0","article-title":"Proteolytic processing, deubiquitinase and interferon antagonist activities of Middle East respiratory syndrome coronavirus papain-like protease","volume":"95","author":"Yang","year":"2014","journal-title":"J. Gen. Virol."},{"key":"ref_150","doi-asserted-by":"crossref","unstructured":"Knaap, R., Fernandez-Delgado, R., Dalebout, T., Oreskova, N., Bredenbeek, P., Nenjuanes, L., Sola, I., Snijder, E., and Kikkert, M. (2019). The deubiquitinating activity of Middle East respiratory syndrome coronavirus papain-like protease delays the innate immune response and enhances virulence in a mouse model. bioRxiv.","DOI":"10.1101\/751578"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1474","DOI":"10.1128\/JVI.01650-07","article-title":"Negative feedback regulation of RIG-I-mediated antiviral signaling by interferon-induced ISG15 conjugation","volume":"82","author":"Kim","year":"2008","journal-title":"J. Virol."},{"key":"ref_152","doi-asserted-by":"crossref","unstructured":"Sooryanarain, H., Rogers, A.J., Cao, D., Haac, M.E.R., Karpe, Y.A., and Meng, X.J. (2017). ISG15 Modulates Type I Interferon Signaling and the Antiviral Response during Hepatitis E Virus Replication. J. Virol., 91.","DOI":"10.1128\/JVI.00621-17"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"6338","DOI":"10.1128\/MCB.25.15.6338-6345.2005","article-title":"ISG15, an interferon-stimulated ubiquitin-like protein, is not essential for STAT1 signaling and responses against vesicular stomatitis and lymphocytic choriomeningitis virus","volume":"25","author":"Osiak","year":"2005","journal-title":"Mol. Cell Biol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1093\/infdis\/163.2.293","article-title":"Genome analysis of adenovirus type 31 strains from immunocompromised and immunocompetent patients","volume":"163","author":"Johansson","year":"1991","journal-title":"J. Infect. Dis."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"4536","DOI":"10.3390\/v6114536","article-title":"Structure, function and dynamics in adenovirus maturation","volume":"6","author":"Mangel","year":"2014","journal-title":"Viruses"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"3361","DOI":"10.1172\/JCI136225","article-title":"Herpesvirus latency","volume":"130","author":"Cohen","year":"2020","journal-title":"J. Clin. Investig."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1146\/annurev.med.59.061606.095540","article-title":"Herpes simplex: Insights on pathogenesis and possible vaccines","volume":"59","author":"Koelle","year":"2008","journal-title":"Annu. Rev. Med."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"728","DOI":"10.1128\/CMR.00052-13","article-title":"Pathogenesis and current approaches to control of varicella-zoster virus infections","volume":"26","author":"Gershon","year":"2013","journal-title":"Clin. Microbiol Rev."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1002\/path.4437","article-title":"The pathogenesis of human cytomegalovirus","volume":"235","author":"Griffiths","year":"2015","journal-title":"J. Pathol."},{"key":"ref_160","first-page":"149","article-title":"Pathogenesis of human herpesvirus 6 (HHV-6)","volume":"1","author":"Yamanishi","year":"1992","journal-title":"Infect. Agents Dis."},{"key":"ref_161","doi-asserted-by":"crossref","unstructured":"Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., and Yamanishi, K. (2007). EBV-induced oncogenesis. Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis, Cambridge University Press.","DOI":"10.1017\/CBO9780511545313"},{"key":"ref_162","doi-asserted-by":"crossref","unstructured":"Arvin, A., Campadelli-Fiume, G., Mocarski, E., Moore, P.S., Roizman, B., Whitley, R., and Yamanishi, K. (2007). KSHV-induced oncogenesis. Human Herpesviruses: Biology, Therapy, and Immunoprophylaxis, Cambridge University Press.","DOI":"10.1017\/CBO9780511545313"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"1182","DOI":"10.3390\/v4081182","article-title":"Herpesvirus exploitation of host immune inhibitory pathways","volume":"4","author":"Stack","year":"2012","journal-title":"Viruses"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/S1074-5521(02)00248-X","article-title":"Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family","volume":"9","author":"Borodovsky","year":"2002","journal-title":"Chem. Biol."},{"key":"ref_165","doi-asserted-by":"crossref","unstructured":"Gastaldello, S., Chen, X., Callegari, S., and Masucci, M.G. (2013). Caspase-1 promotes Epstein-Barr virus replication by targeting the large tegument protein deneddylase to the nucleus of productively infected cells. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003664"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"6009","DOI":"10.1128\/JVI.00280-08","article-title":"Mutagenesis of the active-site cysteine in the ubiquitin-specific protease contained in large tegument protein pUL36 of pseudorabies virus impairs viral replication in vitro and neuroinvasion in vivo","volume":"82","author":"Bottcher","year":"2008","journal-title":"J. Virol."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"20025","DOI":"10.1073\/pnas.0706295104","article-title":"A herpesvirus ubiquitin-specific protease is critical for efficient T cell lymphoma formation","volume":"104","author":"Jarosinski","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.4049\/jimmunol.1402495","article-title":"Evasion of innate cytosolic DNA sensing by a gammaherpesvirus facilitates establishment of latent infection","volume":"194","author":"Sun","year":"2015","journal-title":"J. Immunol."},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Gupta, S., Yla-Anttila, P., Callegari, S., Tsai, M.H., Delecluse, H.J., and Masucci, M.G. (2018). Herpesvirus deconjugases inhibit the IFN response by promoting TRIM25 autoubiquitination and functional inactivation of the RIG-I signalosome. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1006852"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1093\/jmcb\/mjs012","article-title":"Herpes virus deneddylases interrupt the cullin-RING ligase neddylation cycle by inhibiting the binding of CAND1","volume":"4","author":"Gastaldello","year":"2012","journal-title":"J. Mol. Cell Biol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/nature07884","article-title":"An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer","volume":"458","author":"Soucy","year":"2009","journal-title":"Nature"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"8156","DOI":"10.1074\/jbc.M411405200","article-title":"Epstein-Barr virus lytic replication elicits ATM checkpoint signal transduction while providing an S-phase-like cellular environment","volume":"280","author":"Kudoh","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1146\/annurev-virology-092917-043534","article-title":"Virus DNA Replication and the Host DNA Damage Response","volume":"5","author":"Weitzman","year":"2018","journal-title":"Annu. Rev. Virol."},{"key":"ref_174","doi-asserted-by":"crossref","unstructured":"Dyson, O.F., Pagano, J.S., and Whitehurst, C.B. (2017). The Translesion Polymerase Pol eta Is Required for Efficient Epstein-Barr Virus Infectivity and Is Regulated by the Viral Deubiquitinating Enzyme BPLF1. J. Virol., 91.","DOI":"10.1128\/JVI.00600-17"},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"4060","DOI":"10.1128\/JVI.02020-12","article-title":"Epstein-Barr virus deubiquitinase downregulates TRAF6-mediated NF-kappaB signaling during productive replication","volume":"87","author":"Saito","year":"2013","journal-title":"J. Virol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"e3078","DOI":"10.1038\/cddis.2017.461","article-title":"Essential role of HCMV deubiquitinase in promoting oncogenesis by targeting anti-viral innate immune signaling pathways","volume":"8","author":"Kumari","year":"2017","journal-title":"Cell Death Dis."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Bodda, C., Reinert, L.S., Fruhwurth, S., Richardo, T., Sun, C., Zhang, B.C., Kalamvoki, M., Pohlmann, A., Mogensen, T.H., and Bergstrom, P. (2020). HSV1 VP1-2 deubiquitinates STING to block type I interferon expression and promote brain infection. J. Exp. Med., 217.","DOI":"10.1084\/jem.20191422"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.tcb.2008.10.003","article-title":"The 14-3-3 proteins: Integrators of diverse signaling cues that impact cell fate and cancer development","volume":"19","author":"Morrison","year":"2009","journal-title":"Trends Cell Biol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1146\/annurev.pharmtox.40.1.617","article-title":"14-3-3 proteins: Structure, function, and regulation","volume":"40","author":"Fu","year":"2000","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.chom.2012.04.006","article-title":"The mitochondrial targeting chaperone 14-3-3epsilon regulates a RIG-I translocon that mediates membrane association and innate antiviral immunity","volume":"11","author":"Liu","year":"2012","journal-title":"Cell Host Microbe"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"16743","DOI":"10.1073\/pnas.0804947105","article-title":"Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction","volume":"105","author":"Gack","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Gupta, S., Yla-Anttila, P., Sandalova, T., Sun, R., Achour, A., and Masucci, M.G. (2019). 14-3-3 scaffold proteins mediate the inactivation of trim25 and inhibition of the type I interferon response by herpesvirus deconjugases. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1008146"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"437","DOI":"10.3389\/fimmu.2020.00437","article-title":"Interaction With 14-3-3 Correlates With Inactivation of the RIG-I Signalosome by Herpesvirus Ubiquitin Deconjugases","volume":"11","author":"Gupta","year":"2020","journal-title":"Front. Immunol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"12511","DOI":"10.1128\/JVI.01294-14","article-title":"Catalytic function and substrate specificity of the papain-like protease domain of nsp3 from the Middle East respiratory syndrome coronavirus","volume":"88","author":"Mielech","year":"2014","journal-title":"J. Virol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1021\/jm401712t","article-title":"X-ray structural and biological evaluation of a series of potent and highly selective inhibitors of human coronavirus papain-like proteases","volume":"57","author":"Barraza","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.bmcl.2014.12.057","article-title":"Structure-based design and optimization of potent inhibitors of the adenoviral protease","volume":"25","author":"Grosche","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"104649","DOI":"10.1016\/j.antiviral.2019.104649","article-title":"Small molecule screening identifies inhibitors of the Epstein-Barr virus deubiquitinating enzyme, BPLF1","volume":"173","author":"Atkins","year":"2020","journal-title":"Antiviral Res."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/8\/1137\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:53:40Z","timestamp":1760176420000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/10\/8\/1137"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8,1]]},"references-count":187,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2020,8]]}},"alternative-id":["biom10081137"],"URL":"https:\/\/doi.org\/10.3390\/biom10081137","relation":{},"ISSN":["2218-273X"],"issn-type":[{"type":"electronic","value":"2218-273X"}],"subject":[],"published":{"date-parts":[[2020,8,1]]}}}