{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T18:17:19Z","timestamp":1790878639874,"version":"4.1.0"},"reference-count":292,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2017,8,8]],"date-time":"2017-08-08T00:00:00Z","timestamp":1502150400000},"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>Cells have multiple means to induce apoptosis in response to viral infection. Poxviruses must prevent activation of cellular apoptosis to ensure successful replication. These viruses devote a substantial portion of their genome to immune evasion. Many of these immune evasion products expressed during infection antagonize cellular apoptotic pathways. Poxvirus products target multiple points in both the extrinsic and intrinsic apoptotic pathways, thereby mitigating apoptosis during infection. Interestingly, recent evidence indicates that poxviruses also hijack cellular means of eliminating apoptotic bodies as a means to spread cell to cell through a process called apoptotic mimicry. Poxviruses are the causative agent of many human and veterinary diseases. Further, there is substantial interest in developing these viruses as vectors for a variety of uses including vaccine delivery and as oncolytic viruses to treat certain human cancers. Therefore, an understanding of the molecular mechanisms through which poxviruses regulate the cellular apoptotic pathways remains a top research priority. In this review, we consider anti-apoptotic strategies of poxviruses focusing on three relevant poxvirus genera: Orthopoxvirus, Molluscipoxvirus, and Leporipoxvirus. All three genera express multiple products to inhibit both extrinsic and intrinsic apoptotic pathways with many of these products required for virulence.<\/jats:p>","DOI":"10.3390\/v9080215","type":"journal-article","created":{"date-parts":[[2017,8,8]],"date-time":"2017-08-08T10:28:08Z","timestamp":1502188088000},"page":"215","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":75,"title":["Poxviruses Utilize Multiple Strategies to Inhibit Apoptosis"],"prefix":"10.3390","volume":"9","author":[{"given":"Daniel","family":"Nichols","sequence":"first","affiliation":[{"name":"Department of Biological Sciences, Seton Hall University, South Orange, NJ 07039, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William","family":"De Martini","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Seton Hall University, South Orange, NJ 07039, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jessica","family":"Cottrell","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences, Seton Hall University, South Orange, NJ 07039, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,8,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/S1097-2765(00)80438-4","article-title":"A conserved checkpoint pathway mediates DNA damage-induced apoptosis and cell cycle arrest in C. elegans","volume":"5","author":"Gartner","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"32608","DOI":"10.1074\/jbc.273.49.32608","article-title":"Inhibition of human caspases by peptide-based and macromolecular inhibitors","volume":"273","author":"Peterson","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"742","DOI":"10.1016\/j.cell.2011.10.033","article-title":"Programmed cell death in animal development and disease","volume":"147","author":"Fuchs","year":"2011","journal-title":"Cell"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1312","DOI":"10.1126\/science.281.5381.1312","article-title":"Caspases: Enemies within","volume":"281","author":"Thornberry","year":"1998","journal-title":"Science"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1422","DOI":"10.1038\/cdd.2017.36","article-title":"Caspase-dependent non-apoptotic processes in development","volume":"28","author":"Nakajima","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"8471","DOI":"10.1007\/s13277-016-5035-9","article-title":"Major apoptotic mechanisms and genes involved in apoptosis","volume":"37","author":"Kiraz","year":"2016","journal-title":"Tumour Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/S0092-8674(03)00521-X","article-title":"Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes","volume":"114","author":"Micheau","year":"2003","journal-title":"Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1305","DOI":"10.1126\/science.281.5381.1305","article-title":"Death receptors: Signaling and modulation","volume":"281","author":"Ashkenazi","year":"1998","journal-title":"Science"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0968-0004(01)01995-8","article-title":"The molecular architecture of the TNF superfamily","volume":"27","author":"Bodmer","year":"2002","journal-title":"Trends Biochem. Sci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/S0952-7915(99)80045-4","article-title":"Apoptosis signaling in lymphocytes","volume":"11","author":"Scaffidi","year":"1999","journal-title":"Curr. Opin. Immunol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.imlet.2017.03.015","article-title":"Vaccinia virus evasion of regulated cell death","volume":"186","author":"Veyer","year":"2017","journal-title":"Immunol. Lett."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1038\/40657","article-title":"Inhibition of death receptor signals by cellular FLIP","volume":"388","author":"Irmler","year":"1997","journal-title":"Nature"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"4026","DOI":"10.1128\/MCB.23.11.4026-4033.2003","article-title":"Role of SODD in regulation of tumor necrosis factor responses","volume":"23","author":"Takada","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1016\/j.molcel.2008.05.014","article-title":"cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination","volume":"30","author":"Bertrand","year":"2008","journal-title":"Mol. Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1007\/s10495-007-0746-4","article-title":"Embedded together: The life and death consequences of interaction of the Bcl-2 family with membranes","volume":"12","author":"Leber","year":"2007","journal-title":"Apoptosis"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/j.molcel.2009.10.011","article-title":"Emerging role for members of the Bcl-2 family in mitochondrial morphogenesis","volume":"36","author":"Autret","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.molcel.2010.01.025","article-title":"The Bcl-2 family reunion","volume":"37","author":"Chipuk","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"a008722","DOI":"10.1101\/cshperspect.a008722","article-title":"Multiple functions of BCL-2 family proteins","volume":"5","author":"Hardwick","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1016\/j.molcel.2005.02.003","article-title":"BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly","volume":"17","author":"Kuwana","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0092-8674(02)01036-X","article-title":"Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane","volume":"111","author":"Kuwana","year":"2002","journal-title":"Cell"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1038\/nature05111","article-title":"Role of Bax and Bak in mitochondrial morphogenesis","volume":"443","author":"Karbowski","year":"2006","journal-title":"Nature"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"3043","DOI":"10.4161\/cc.6.24.5115","article-title":"Regulation of mitochondrial morphological dynamics during apoptosis by Bcl-2 family proteins: A key in Bak?","volume":"6","author":"Brooks","year":"2007","journal-title":"Cell Cycle"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"11649","DOI":"10.1073\/pnas.0703976104","article-title":"Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins","volume":"104","author":"Brooks","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.molcel.2006.01.034","article-title":"Role for CED-9 and Egl-1 as regulators of mitochondrial fission and fusion dynamics","volume":"21","author":"Delivani","year":"2006","journal-title":"Mol. Cell"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.molcel.2008.08.002","article-title":"Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome c release","volume":"31","author":"Sheridan","year":"2008","journal-title":"Mol. Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/S1534-5807(01)00055-7","article-title":"The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis","volume":"1","author":"Frank","year":"2001","journal-title":"Dev. Cell"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.devcel.2007.11.019","article-title":"Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax\/Bak-dependent mitochondrial outer membrane permeabilization","volume":"14","author":"Chipuk","year":"2008","journal-title":"Dev. Cell"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2402","DOI":"10.1091\/mbc.e07-12-1287","article-title":"The novel tail-anchored membrane protein Mff controls mitochondrial and peroxisomal fission in mammalian cells","volume":"19","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"2112","DOI":"10.1016\/j.cub.2005.10.041","article-title":"Bax\/Bak-dependent release of DDP\/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death","volume":"15","author":"Arnoult","year":"2005","journal-title":"Curr. Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1038\/sj.cdd.4402107","article-title":"Inhibiting Drp1-mediated mitochondrial fission selectively prevents the release of cytochrome c during apoptosis","volume":"14","author":"Estaquier","year":"2007","journal-title":"Cell Death Differ."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1038\/ncb1907","article-title":"Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice","volume":"11","author":"Ishihara","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"7397","DOI":"10.1128\/MCB.02282-05","article-title":"Inhibiting the mitochondrial fission machinery does not prevent Bax\/Bak-dependent apoptosis","volume":"26","author":"Parone","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/j.bbamcr.2006.04.005","article-title":"Mitochondrial fission and apoptosis: An ongoing trial","volume":"1763","author":"Parone","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S1534-5807(01)00116-2","article-title":"A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis","volume":"2","author":"Scorrano","year":"2002","journal-title":"Dev. Cell"},{"key":"ref_35","first-page":"1196","article-title":"Mitochondrial membrane potential at HL-60 cell apoptosis induced by cytarabine","volume":"15","author":"Sun","year":"2007","journal-title":"Zhongguo Shi Yan Xue Ye Xue Za Zhi"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"14397","DOI":"10.1073\/pnas.0907555106","article-title":"The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor","volume":"106","author":"Rong","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1126\/science.1081208","article-title":"BAX and BAK regulation of endoplasmic reticulum Ca2+: A control point for apoptosis","volume":"300","author":"Scorrano","year":"2003","journal-title":"Science"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1016\/j.bbamcr.2010.11.012","article-title":"Integrating stress signals at the endoplasmic reticulum: The BCL-2 protein family rheostat","volume":"1813","author":"Rodriguez","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1083\/jcb.200305149","article-title":"Gene expression during ER stress-induced apoptosis in neurons: Induction of the BH3-only protein Bbc3\/PUMA and activation of the mitochondrial apoptosis pathway","volume":"162","author":"Reimertz","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1074\/jbc.M409948200","article-title":"Identification of a network involved in thapsigargin-induced apoptosis using a library of small interfering RNA expression vectors","volume":"280","author":"Futami","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/0955-0674(93)90127-C","article-title":"The modification and assembly of proteins in the endoplasmic reticulum","volume":"5","author":"Gaut","year":"1993","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1172\/JCI0216886","article-title":"Orchestrating the unfolded protein response in health and disease","volume":"110","author":"Kaufman","year":"2002","journal-title":"J. Clin. Investig."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1146\/annurev.biochem.73.011303.074134","article-title":"The mammalian unfolded protein response","volume":"74","author":"Schroder","year":"2005","journal-title":"Annu. Rev. Biochem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.mrfmmm.2004.06.056","article-title":"ER stress and the unfolded protein response","volume":"569","author":"Schroder","year":"2005","journal-title":"Mutat. Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3619","DOI":"10.1093\/emboj\/17.13.3619","article-title":"Identification of novel stress-induced genes downstream of chop","volume":"17","author":"Wang","year":"1998","journal-title":"EMBO J."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1101\/gad.12.7.982","article-title":"CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum","volume":"12","author":"Zinszner","year":"1998","journal-title":"Genes Dev."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/0014-5793(96)01016-2","article-title":"Ectopic expression of CHOP (GADD153) induces apoptosis in M1 myeloblastic leukemia cells","volume":"395","author":"Matsumoto","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1038\/sj.embor.7400779","article-title":"Mediators of endoplasmic reticulum stress-induced apoptosis","volume":"7","author":"Szegezdi","year":"2006","journal-title":"EMBO Rep."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2432","DOI":"10.1073\/pnas.0438011100","article-title":"JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis","volume":"100","author":"Lei","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"50375","DOI":"10.1074\/jbc.M408493200","article-title":"Translocation of Bim to the endoplasmic reticulum (ER) mediates ER stress signaling for activation of caspase-12 during ER stress-induced apoptosis","volume":"279","author":"Morishima","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1038\/47513","article-title":"Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-\u03b2","volume":"403","author":"Nakagawa","year":"2000","journal-title":"Nature"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1064","DOI":"10.1038\/nature04656","article-title":"Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice","volume":"440","author":"Saleh","year":"2006","journal-title":"Nature"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1196\/annals.1299.032","article-title":"Caspase-12 and ER-stress-mediated apoptosis: The story so far","volume":"1010","author":"Szegezdi","year":"2003","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1073\/pnas.62.2.357","article-title":"Inhibition of tumor growth by polyinosinic-polycytidylic acid","volume":"62","author":"Levy","year":"1969","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1038\/cdd.2012.22","article-title":"dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8","volume":"19","author":"Estornes","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.molcel.2011.06.011","article-title":"cIAPs block Ripoptosome formation, a RIP1\/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms","volume":"43","author":"Feoktistova","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1111\/j.1600-065X.2008.00737.x","article-title":"Innate immunity to virus infection","volume":"227","author":"Takeuchi","year":"2009","journal-title":"Immunol. Rev."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1593\/neo.08590","article-title":"Recurrent overexpression of c-IAP2 in EBV-associated nasopharyngeal carcinomas: Critical role in resistance to Toll-like receptor 3-mediated apoptosis","volume":"10","author":"Friboulet","year":"2008","journal-title":"Neoplasia"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"6867","DOI":"10.4049\/jimmunol.179.10.6867","article-title":"Spatiotemporal mobilization of Toll\/IL-1 receptor domain-containing adaptor molecule-1 in response to dsRNA","volume":"179","author":"Funami","year":"2007","journal-title":"J. Immunol."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"4894","DOI":"10.4049\/jimmunol.176.8.4894","article-title":"TLR3 can directly trigger apoptosis in human cancer cells","volume":"176","author":"Salaun","year":"2006","journal-title":"J. Immunol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"4565","DOI":"10.1158\/1078-0432.CCR-07-0274","article-title":"Toll-like receptor 3 expressed by melanoma cells as a target for therapy?","volume":"13","author":"Salaun","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/ni1061","article-title":"RIP1 is an essential mediator of Toll-like receptor 3-induced NF-\u03baB activation","volume":"5","author":"Meylan","year":"2004","journal-title":"Nat. Immunol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.molcel.2011.06.006","article-title":"The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs","volume":"43","author":"Tenev","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.4161\/cc.7.9.5811","article-title":"PERK and PKR: Old kinases learn new tricks","volume":"7","author":"Raven","year":"2008","journal-title":"Cell Cycle"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0092-8674(77)90330-0","article-title":"Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis","volume":"11","author":"Farrell","year":"1977","journal-title":"Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.cell.2009.01.042","article-title":"Regulation of translation initiation in eukaryotes: Mechanisms and biological targets","volume":"136","author":"Sonenberg","year":"2009","journal-title":"Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2598","DOI":"10.3390\/v4112598","article-title":"dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection","volume":"4","author":"Dabo","year":"2012","journal-title":"Viruses"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S1097-2765(02)00590-7","article-title":"X-ray crystal structure and functional analysis of vaccinia virus K3L reveals molecular determinants for PKR subversion and substrate recognition","volume":"10","author":"Dar","year":"2002","journal-title":"Mol. Cell"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1146\/annurev.immunol.14.1.649","article-title":"The NF-\u03baB and I\u03baB proteins: New discoveries and insights","volume":"14","author":"Baldwin","year":"1996","journal-title":"Annu. Rev. Immunol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"4653","DOI":"10.1128\/MCB.19.7.4653","article-title":"Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the \u03b1 subunit of eukaryotic translation initiation factor 2 and NF-\u03baB","volume":"19","author":"Gil","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"6288","DOI":"10.1073\/pnas.91.14.6288","article-title":"Double-stranded RNA-dependent protein kinase activates transcription factor NF-\u03baB by phosphorylating I\u03baB","volume":"91","author":"Kumar","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"7844","DOI":"10.1074\/jbc.271.13.7844","article-title":"Role of I\u03baB\u03b1 ubiquitination in signal-induced activation of NF\u03baB in vivo","volume":"271","author":"Roff","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1016\/j.cellsig.2006.02.010","article-title":"The N-terminus of PKR is responsible for the activation of the NF-\u03baB signaling pathway by interacting with the IKK complex","volume":"18","author":"Bonnet","year":"2006","journal-title":"Cell. Signal."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"4502","DOI":"10.1128\/MCB.24.10.4502-4512.2004","article-title":"TRAF family proteins link PKR with NF-\u03baB activation","volume":"24","author":"Gil","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/S1473-3099(13)70109-9","article-title":"Molluscum contagiosum virus infection","volume":"13","author":"Chen","year":"2013","journal-title":"Lancet Infect. Dis."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"695","DOI":"10.3201\/eid2104.140351","article-title":"Outbreak of severe zoonotic vaccinia virus infection, Southeastern Brazil","volume":"21","author":"Abrahao","year":"2015","journal-title":"Emerg. Infect. Dis."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1093\/cid\/cit703","article-title":"Human monkeypox","volume":"58","author":"McCollum","year":"2014","journal-title":"Clin. Infect. Dis."},{"key":"ref_78","doi-asserted-by":"crossref","unstructured":"Sharp, D.W., and Lattime, E.C. (2016). Recombinant Poxvirus and the Tumor Microenvironment: Oncolysis, Immune Regulation and Immunization. Biomedicines, 4.","DOI":"10.3390\/biomedicines4030019"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"4252","DOI":"10.1016\/j.vaccine.2013.05.056","article-title":"Oncolytic myxoma virus: The path to clinic","volume":"31","author":"Chan","year":"2013","journal-title":"Vaccine"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1726","DOI":"10.3390\/v7041726","article-title":"The evolution of poxvirus vaccines","volume":"7","author":"Perdiguero","year":"2015","journal-title":"Viruses"},{"key":"ref_81","unstructured":"Moss, B. (2013). Fields, Lippincott Williams and Willkins."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2367","DOI":"10.1099\/vir.0.055921-0","article-title":"Vaccinia virus immune evasion: Mechanisms, virulence and immunogenicity","volume":"94","author":"Smith","year":"2013","journal-title":"J. Gen. Virol."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/bs.aivir.2014.11.004","article-title":"Immune evasion strategies of molluscum contagiosum virus","volume":"92","author":"Shisler","year":"2015","journal-title":"Adv. Virus Res."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.celrep.2013.06.028","article-title":"Vaccinia virus entry is followed by core activation and proteasome-mediated release of the immunomodulatory effector VH1 from lateral bodies","volume":"4","author":"Schmidt","year":"2013","journal-title":"Cell Rep."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"4800","DOI":"10.3390\/v7082844","article-title":"Cloak and Dagger: Alternative Immune Evasion and Modulation Strategies of Poxviruses","volume":"7","author":"Bidgood","year":"2015","journal-title":"Viruses"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/nri1184","article-title":"Signalling pathways of the TNF superfamily: A double-edged sword","volume":"3","author":"Aggarwal","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1038\/385729a0","article-title":"A metalloproteinase disintegrin that releases tumour-necrosis factor-\u03b1 from cells","volume":"385","author":"Black","year":"1997","journal-title":"Nature"},{"key":"ref_88","first-page":"928","article-title":"iRHOM2 is a critical pathogenic mediator of inflammatory arthritis","volume":"123","author":"Issuree","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/S0092-8674(01)00237-9","article-title":"The TNF and TNF receptor superfamilies: Integrating mammalian biology","volume":"104","author":"Locksley","year":"2001","journal-title":"Cell"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1038\/nri980","article-title":"Viral mimicry of cytokines, chemokines and their receptors","volume":"3","author":"Alcami","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1084\/jem.20020319","article-title":"Inhibition of type 1 cytokine-mediated inflammation by a soluble CD30 homologue encoded by ectromelia (mousepox) virus","volume":"196","author":"Saraiva","year":"2002","journal-title":"J. Exp. Med."},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Alejo, A., Saraiva, M., Ruiz-Arguello, M.B., Viejo-Borbolla, A., de Marco, M.F., Salguero, F.J., and Alcami, A. (2009). A method for the generation of ectromelia virus (ECTV) recombinants: In vivo analysis of ECTV vCD30 deletion mutants. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0005175"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.jmb.2007.06.082","article-title":"Structure of CrmE, a virus-encoded tumour necrosis factor receptor","volume":"372","author":"Graham","year":"2007","journal-title":"J. Mol. Biol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"5995","DOI":"10.1073\/pnas.0510462103","article-title":"A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus","volume":"103","author":"Alejo","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"22517","DOI":"10.1074\/jbc.M604645200","article-title":"Variation in ligand binding specificities of a novel class of poxvirus-encoded tumor necrosis factor-binding protein","volume":"281","author":"Rahman","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1006\/viro.2001.1236","article-title":"Vaccinia virus CrmE encodes a soluble and cell surface tumor necrosis factor receptor that contributes to virus virulence","volume":"292","author":"Reading","year":"2002","journal-title":"Virology"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"15973","DOI":"10.1074\/jbc.M115.650119","article-title":"Comparative Biochemical and Functional Analysis of Viral and Human Secreted Tumor Necrosis Factor (TNF) Decoy Receptors","volume":"290","author":"Pontejo","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1006\/viro.1994.1539","article-title":"Cowpox virus contains two copies of an early gene encoding a soluble secreted form of the type II TNF receptor","volume":"204","author":"Hu","year":"1994","journal-title":"Virology"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1006\/viro.1996.0462","article-title":"Cowpox virus genome encodes a second soluble homologue of cellular TNF receptors, distinct from CrmB, that binds TNF but not LT\u03b1","volume":"223","author":"Smith","year":"1996","journal-title":"Virology"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1128\/JVI.75.1.226-233.2001","article-title":"CrmE, a novel soluble tumor necrosis factor receptor encoded by poxviruses","volume":"75","author":"Saraiva","year":"2001","journal-title":"J. Virol."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1006\/viro.1994.1585","article-title":"The myxoma virus TNF-receptor homologue (T2) inhibits tumor necrosis factor-\u03b1 in a species-specific fashion","volume":"204","author":"Schreiber","year":"1994","journal-title":"Virology"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"13333","DOI":"10.1074\/jbc.271.23.13333","article-title":"Myxoma virus T2 protein, a tumor necrosis factor (TNF) receptor homolog, is secreted as a monomer and dimer that each bind rabbit TNF\u03b1, but the dimer is a more potent TNF inhibitor","volume":"271","author":"Schreiber","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1038\/icb.1996.87","article-title":"M-T2: A poxvirus TNF receptor homologue with dual activities","volume":"74","author":"Sedger","year":"1996","journal-title":"Immunol. Cell Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1023\/A:1008136431036","article-title":"Myxoma virus expresses a TNF receptor homolog with two distinct functions","volume":"21","author":"Xu","year":"2000","journal-title":"Virus Genes"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"9300","DOI":"10.1128\/JVI.02449-05","article-title":"Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death","volume":"80","author":"Sedger","year":"2006","journal-title":"J. Virol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"8951","DOI":"10.1021\/bi00449a001","article-title":"Implications of the three-dimensional structure of \u03b1 1-antitrypsin for structure and function of serpins","volume":"28","author":"Huber","year":"1989","journal-title":"Biochemistry"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1002\/bies.950150705","article-title":"The role of conformational change in serpin structure and function","volume":"15","author":"Gettins","year":"1993","journal-title":"Bioessays"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"27657","DOI":"10.1016\/S0021-9258(18)47036-6","article-title":"Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition","volume":"269","author":"Lawrence","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"10377","DOI":"10.1074\/jbc.270.18.10377","article-title":"Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A","volume":"270","author":"Quan","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"19331","DOI":"10.1016\/S0021-9258(17)32171-3","article-title":"Inhibition of interleukin-1\u03b2 converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition","volume":"269","author":"Komiyama","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1056\/NEJM198309223091203","article-title":"Mutation of antitrypsin to antithrombin. \u03b11-antitrypsin Pittsburgh (358 Met \u2192Arg), a fatal bleeding disorder","volume":"309","author":"Owen","year":"1983","journal-title":"N. Engl. J. Med."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1186\/gb-2006-7-5-216","article-title":"An overview of the serpin superfamily","volume":"7","author":"Law","year":"2006","journal-title":"Genome Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"33293","DOI":"10.1074\/jbc.R100016200","article-title":"The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature","volume":"276","author":"Silverman","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1146\/annurev.micro.62.081307.163009","article-title":"Viral subversion of apoptotic enzymes: Escape from death row","volume":"62","author":"Best","year":"2008","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0092-8674(92)90273-F","article-title":"Vaccinia and cowpox viruses encode a novel secreted interleukin-1-binding protein","volume":"71","author":"Spriggs","year":"1992","journal-title":"Cell"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1016\/j.cell.2016.11.048","article-title":"A Multiplexed single-cell CRISPR screening platform enables systematic dissection of the unfolded protein response","volume":"167","author":"Adamson","year":"2016","journal-title":"Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"1737","DOI":"10.1128\/jvi.68.3.1737-1749.1994","article-title":"Multigenic evasion of inflammation by poxviruses","volume":"68","author":"Palumbo","year":"1994","journal-title":"J. Virol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/0042-6822(89)90128-1","article-title":"Inhibition of an inflammatory response is mediated by a 38-kDa protein of cowpox virus","volume":"172","author":"Palumbo","year":"1989","journal-title":"Virology"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"6479","DOI":"10.1128\/jvi.70.9.6479-6485.1996","article-title":"Protection against apoptosis by the vaccinia virus SPI-2 (B13R) gene product","volume":"70","author":"Dobbelstein","year":"1996","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1099\/0022-1317-78-3-677","article-title":"Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1beta-converting enzyme and protects virus-infected cells from TNF- and Fas-mediated apoptosis, but does not prevent IL-1\u03b2-induced fever","volume":"78","author":"Kettle","year":"1997","journal-title":"J. Gen. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1006\/viro.1996.0128","article-title":"The mode of death of pig kidney cells infected with cowpox virus is governed by the expression of the crmA gene","volume":"217","author":"Ray","year":"1996","journal-title":"Virology"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"7797","DOI":"10.1074\/jbc.272.12.7797","article-title":"Target protease specificity of the viral serpin CrmA. Analysis of five caspases","volume":"272","author":"Zhou","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/sj.cdd.4400594","article-title":"Caspase inhibitors","volume":"6","author":"Ekert","year":"1999","journal-title":"Cell Death Differ."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/0092-8674(92)90223-Y","article-title":"Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1\u03b2 converting enzyme","volume":"69","author":"Ray","year":"1992","journal-title":"Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1099\/vir.0.068833-0","article-title":"Analysis of the anti-apoptotic activity of four vaccinia virus proteins demonstrates that B13 is the most potent inhibitor in isolation and during viral infection","volume":"95","author":"Veyer","year":"2014","journal-title":"J. Gen. Virol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1128\/jvi.63.2.600-606.1989","article-title":"Vaccinia virus encodes two proteins that are structurally related to members of the plasma serine protease inhibitor superfamily","volume":"63","author":"Kotwal","year":"1989","journal-title":"J. Virol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"2333","DOI":"10.1099\/0022-1317-70-9-2333","article-title":"Vaccinia virus encodes a family of genes with homology to serine proteinase inhibitors","volume":"70","author":"Smith","year":"1989","journal-title":"J. Gen. Virol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/S0042-6822(95)80028-X","article-title":"Vaccinia virus serpins B13R (SPI-2) and B22R (SPI-1) encode Mr 38.5 and 40K, intracellular polypeptides that do not affect virus virulence in a murine intranasal model","volume":"206","author":"Kettle","year":"1995","journal-title":"Virology"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1006\/viro.1999.9884","article-title":"Vaccinia virus serpin-1 deletion mutant exhibits a host range defect characterized by low levels of intermediate and late mRNAs","volume":"262","author":"Shisler","year":"1999","journal-title":"Virology"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"5978","DOI":"10.1128\/jvi.69.10.5978-5987.1995","article-title":"Orthopoxvirus fusion inhibitor glycoprotein SPI-3 (open reading frame K2L) contains motifs characteristic of serine proteinase inhibitors that are not required for control of cell fusion","volume":"69","author":"Turner","year":"1995","journal-title":"J. Virol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1099\/0022-1317-73-3-549","article-title":"A vaccinia serine protease inhibitor which prevents virus-induced cell fusion","volume":"73","author":"Law","year":"1992","journal-title":"J. Gen. Virol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1006\/viro.1993.1594","article-title":"The effects of serpin gene mutations on the distinctive pathobiology of cowpox and rabbitpox virus following intranasal inoculation of Balb\/c mice","volume":"197","author":"Thompson","year":"1993","journal-title":"Virology"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1006\/viro.1999.0001","article-title":"The complete DNA sequence of myxoma virus","volume":"264","author":"Cameron","year":"1999","journal-title":"Virology"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1006\/viro.1993.1385","article-title":"SERP1, a serine proteinase inhibitor encoded by myxoma virus, is a secreted glycoprotein that interferes with inflammation","volume":"195","author":"Macen","year":"1993","journal-title":"Virology"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1006\/viro.2000.0378","article-title":"The cowpox virus SPI-3 and myxoma virus SERP1 serpins are not functionally interchangeable despite their similar proteinase inhibition profiles in vitro","volume":"272","author":"Wang","year":"2000","journal-title":"Virology"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1006\/viro.2000.0377","article-title":"The cowpox virus serpin SPI-3 complexes with and inhibits urokinase-type and tissue-type plasminogen activators and plasmin","volume":"272","author":"Turner","year":"2000","journal-title":"Virology"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"5860","DOI":"10.1128\/jvi.70.9.5860-5866.1996","article-title":"Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1\u03b2-converting enzyme","volume":"70","author":"Petit","year":"1996","journal-title":"J. Virol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"7830","DOI":"10.1128\/JVI.72.10.7830-7839.1998","article-title":"Serp2, an inhibitor of the interleukin-1\u03b2-converting enzyme, is critical in the pathobiology of myxoma virus","volume":"72","author":"Gelfi","year":"1998","journal-title":"J. Virol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"6394","DOI":"10.1128\/JVI.73.8.6394-6404.1999","article-title":"Myxoma virus Serp2 is a weak inhibitor of granzyme B and interleukin-1\u03b2 converting enzyme in vitro and unlike CrmA cannot block apoptosis in cowpox virus-infected cells","volume":"73","author":"Turner","year":"1999","journal-title":"J. Virol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1099\/vir.0.79905-0","article-title":"Cowpox virus CrmA, Myxoma virus SERP2 and baculovirus P35 are not functionally interchangeable caspase inhibitors in poxvirus infections","volume":"85","author":"Nathaniel","year":"2004","journal-title":"J. Gen. Virol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1099\/0022-1317-82-6-1407","article-title":"Characterization and functional analysis of Serp3: A novel myxoma virus-encoded serpin involved in virulence","volume":"82","author":"Guerin","year":"2001","journal-title":"J. Gen. Virol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1126\/science.273.5276.813","article-title":"Genome sequence of a human tumorigenic poxvirus: Prediction of specific host response-evasion genes","volume":"273","author":"Senkevich","year":"1996","journal-title":"Science"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1006\/viro.1997.8607","article-title":"The genome of molluscum contagiosum virus: Analysis and comparison with other poxviruses","volume":"233","author":"Senkevich","year":"1997","journal-title":"Virology"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1038\/jid.2010.256","article-title":"Spontaneous regression of highly immunogenic Molluscum contagiosum virus (MCV)-induced skin lesions is associated with plasmacytoid dendritic cells and IFN-DC infiltration","volume":"131","author":"Vermi","year":"2011","journal-title":"J. Investig. Dermatol."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.virol.2005.06.036","article-title":"The MCV MC159 protein inhibits late, but not early, events of TNF-\u03b1-induced NF-\u03baB activation","volume":"340","author":"Murao","year":"2005","journal-title":"Virology"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1128\/JVI.80.2.578-586.2006","article-title":"The MC160 protein expressed by the dermatotropic poxvirus molluscum contagiosum virus prevents tumor necrosis factor \u03b1-induced NF-\u03baB activation via inhibition of I\u03ba kinase complex formation","volume":"80","author":"Nichols","year":"2006","journal-title":"J. Virol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"3162","DOI":"10.1128\/JVI.02009-08","article-title":"Poxvirus MC160 protein utilizes multiple mechanisms to inhibit NF-\u03baB activation mediated via components of the tumor necrosis factor receptor 1 signal transduction pathway","volume":"83","author":"Nichols","year":"2009","journal-title":"J. Virol."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"561","DOI":"10.2217\/fvl.13.38","article-title":"Molluscum Contagiosum Virus: Persistence Pays Off","volume":"8","author":"Randall","year":"2013","journal-title":"Future Virol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"E265","DOI":"10.1073\/pnas.1314569111","article-title":"Inhibition of interferon gene activation by death-effector domain-containing proteins from the molluscum contagiosum virus","volume":"111","author":"Randall","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.4049\/jimmunol.1100136","article-title":"The MC159 protein from the molluscum contagiosum poxvirus inhibits NF-\u03baB activation by interacting with the I\u03baB kinase complex","volume":"188","author":"Randall","year":"2012","journal-title":"J. Immunol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"51613","DOI":"10.1074\/jbc.M305633200","article-title":"A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses","volume":"278","author":"Chan","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1577","DOI":"10.1038\/sj.cdd.4401847","article-title":"The TRAF3-binding site of human molluscipox virus FLIP molecule MC159 is critical for its capacity to inhibit Fas-induced apoptosis","volume":"13","author":"Thurau","year":"2006","journal-title":"Cell Death Differ."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1073\/pnas.94.4.1172","article-title":"Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis","volume":"94","author":"Bertin","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"9621","DOI":"10.1074\/jbc.272.15.9621","article-title":"A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis","volume":"272","author":"Hu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1006\/viro.2001.0834","article-title":"Molluscum contagiosum virus inhibitors of apoptosis: The MC159 v-FLIP protein blocks Fas-induced activation of procaspases and degradation of the related MC160 protein","volume":"282","author":"Shisler","year":"2001","journal-title":"Virology"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1016\/S0092-8674(00)81265-9","article-title":"Involvement of MACH, a novel MORT1\/FADD-interacting protease, in Fas\/APO-1- and TNF receptor-induced cell death","volume":"85","author":"Boldin","year":"1996","journal-title":"Cell"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/S0092-8674(00)81266-0","article-title":"FLICE, a novel FADD-homologous ICE\/CED-3-like protease, is recruited to the CD95 (Fas\/APO-1) death-inducing signaling complex","volume":"85","author":"Muzio","year":"1996","journal-title":"Cell"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1038\/nrm2312","article-title":"Apoptosis: Controlled demolition at the cellular level","volume":"9","author":"Taylor","year":"2008","journal-title":"Nat.Rev. Mol.Cell Biol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"1378","DOI":"10.1016\/j.str.2010.08.006","article-title":"Solution NMR investigation of the CD95\/FADD homotypic death domain complex suggests lack of engagement of the CD95 C terminus","volume":"18","author":"Esposito","year":"2010","journal-title":"Structure"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"5424","DOI":"10.1021\/bi500585u","article-title":"Structural study of the RIPoptosome core reveals a helical assembly for kinase recruitment","volume":"53","author":"Jang","year":"2014","journal-title":"Biochemistry"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1038\/nsmb.1920","article-title":"The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations","volume":"17","author":"Wang","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.molcel.2016.09.009","article-title":"Cryo-EM Structure of caspase-8 tandem DED filament reveals assembly and regulation mechanisms of the death-inducing signaling complex","volume":"64","author":"Fu","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/S1097-2765(03)00051-0","article-title":"A unified model for apical caspase activation","volume":"11","author":"Boatright","year":"2003","journal-title":"Mol. Cell"},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1016\/S0952-7915(98)80223-9","article-title":"Inhibition of Fas death signals by FLIPs","volume":"10","author":"Tschopp","year":"1998","journal-title":"Curr. Opin. Immunol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1016\/j.molcel.2016.02.023","article-title":"Co-operative and hierarchical binding of c-FLIP and caspase-8: A unified model defines how c-FLIP isoforms differentially control cell fate","volume":"61","author":"Hughes","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/j.molcel.2005.10.023","article-title":"Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition","volume":"20","author":"Yang","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"2960","DOI":"10.1074\/jbc.M511074200","article-title":"Crystal structure of a viral FLIP: Insights into FLIP-mediated inhibition of death receptor signaling","volume":"281","author":"Li","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1128\/JVI.76.2.697-706.2002","article-title":"Binding of FADD and caspase-8 to molluscum contagiosum virus MC159 v-FLIP is not sufficient for its antiapoptotic function","volume":"76","author":"Garvey","year":"2002","journal-title":"J. Virol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1083\/jcb.141.5.1243","article-title":"Death-effector filaments: Novel cytoplasmic structures that recruit caspases and trigger apoptosis","volume":"141","author":"Siegel","year":"1998","journal-title":"J. Cell Biol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2895","DOI":"10.1128\/JVI.02729-15","article-title":"Functional comparison of molluscum contagiosum virus vFLIP MC159 with murine cytomegalovirus M36\/vICA and M45\/vIRA proteins","volume":"90","author":"Huttmann","year":"2015","journal-title":"J. Virol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1007\/s11262-017-1456-9","article-title":"The molluscum contagiosum virus death effector domain containing protein MC160 RxDL motifs are not required for its known viral immune evasion functions","volume":"53","author":"Beaury","year":"2017","journal-title":"Virus Genes"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"8169","DOI":"10.1073\/pnas.0812453106","article-title":"Mechanism of procaspase-8 activation by c-FLIPL","volume":"106","author":"Yu","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1042\/BJ20101738","article-title":"FLIPL induces caspase 8 activity in the absence of interdomain caspase 8 cleavage and alters substrate specificity","volume":"433","author":"Pop","year":"2011","journal-title":"Biochem. J."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"3027","DOI":"10.1099\/0022-1317-82-12-3027","article-title":"MC159L protein from the poxvirus molluscum contagiosum virus inhibits NF-\u03baB activation and apoptosis induced by PKR","volume":"82","author":"Gil","year":"2001","journal-title":"J. Gen. Virol."},{"key":"ref_175","doi-asserted-by":"crossref","unstructured":"Graham, S.C., Bahar, M.W., Cooray, S., Chen, R.A., Whalen, D.M., Abrescia, N.G., Alderton, D., Owens, R.J., Stuart, D.I., and Smith, G.L. (2008). Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-\u03baB rather than apoptosis. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.1000128"},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"5991","DOI":"10.1074\/jbc.M114.624650","article-title":"Vaccinia virus protein A49 is an unexpected member of the B-cell Lymphoma (Bcl)-2 protein family","volume":"290","author":"Neidel","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Mansur, D.S., Maluquer de Motes, C., Unterholzner, L., Sumner, R.P., Ferguson, B.J., Ren, H., Strnadova, P., Bowie, A.G., and Smith, G.L. (2013). Poxvirus targeting of E3 ligase beta-TrCP by molecular mimicry: a mechanism to inhibit NF-\u03baB activation and promote immune evasion and virulence. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003183"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"14345","DOI":"10.1073\/pnas.2235583100","article-title":"Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis","volume":"100","author":"Wasilenko","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1038\/sj.cdd.4401718","article-title":"Modified vaccinia virus Ankara protein F1L is a novel BH3-domain-binding protein and acts together with the early viral protein E3L to block virus-associated apoptosis","volume":"13","author":"Fischer","year":"2006","journal-title":"Cell Death Differ."},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1651","DOI":"10.1038\/sj.cdd.4401853","article-title":"Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis","volume":"13","author":"Postigo","year":"2006","journal-title":"Cell Death Differ."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"1564","DOI":"10.1038\/cdd.2008.83","article-title":"Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like domain-swapped dimer that binds a highly selective subset of BH3-containing death ligands","volume":"15","author":"Kvansakul","year":"2008","journal-title":"Cell Death Differ."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"8667","DOI":"10.1128\/JVI.01092-14","article-title":"Structural insight into BH3 domain binding of vaccinia virus antiapoptotic F1L","volume":"88","author":"Campbell","year":"2014","journal-title":"J. Virol."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"1208","DOI":"10.1111\/j.1462-5822.2009.01327.x","article-title":"Vaccinia-induced epidermal growth factor receptor-MEK signalling and the anti-apoptotic protein F1L synergize to suppress cell death during infection","volume":"11","author":"Postigo","year":"2009","journal-title":"Cell Microbiol."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"5569","DOI":"10.1074\/jbc.M109.078113","article-title":"Vaccinia virus protein F1L is a caspase-9 inhibitor","volume":"285","author":"Zhai","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"14600","DOI":"10.1074\/jbc.M116.726851","article-title":"The N Terminus of the vaccinia virus protein F1L is an intrinsically unstructured region that is not involved in apoptosis regulation","volume":"291","author":"Caria","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"7808","DOI":"10.1073\/pnas.1215995110","article-title":"Vaccinia virus F1L protein promotes virulence by inhibiting inflammasome activation","volume":"110","author":"Gerlic","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"e1680","DOI":"10.1038\/cddis.2015.52","article-title":"Variola virus F1L is a Bcl-2-like protein that unlike its vaccinia virus counterpart inhibits apoptosis independent of Bim","volume":"6","author":"Marshall","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1099\/0022-1317-83-8-1965","article-title":"The vaccinia virus N1L protein is an intracellular homodimer that promotes virulence","volume":"83","author":"Bartlett","year":"2002","journal-title":"J. Gen. Virol."},{"key":"ref_189","doi-asserted-by":"crossref","unstructured":"De Motes, C.M., Cooray, S., Ren, H., Almeida, G.M., McGourty, K., Bahar, M.W., Stuart, D.I., Grimes, J.M., Graham, S.C., and Smith, G.L. (2011). Inhibition of apoptosis and NF-\u03baB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002430"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"1656","DOI":"10.1099\/vir.0.82772-0","article-title":"Functional and structural studies of the vaccinia virus virulence factor N1 reveal a Bcl-2-like anti-apoptotic protein","volume":"88","author":"Cooray","year":"2007","journal-title":"J. Gen. Virol."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1110\/ps.062454707","article-title":"Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bcl-2) family protein","volume":"16","author":"Aoyagi","year":"2007","journal-title":"Protein Sci."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1128\/JVI.05817-11","article-title":"The vaccinia virus-encoded Bcl-2 homologues do not act as direct Bax inhibitors","volume":"86","author":"Postigo","year":"2012","journal-title":"J. Virol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"36570","DOI":"10.1074\/jbc.M400567200","article-title":"Poxvirus protein N1L targets the I-\u03baB kinase complex, inhibits signaling to NF-\u03baB by the tumor necrosis factor superfamily of receptors, and inhibits NF-\u03baB and IRF3 signaling by toll-like receptors","volume":"279","author":"DiPerna","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"1487","DOI":"10.1084\/jem.191.9.1487","article-title":"M11L: A novel mitochondria-localized protein of myxoma virus that blocks apoptosis of infected leukocytes","volume":"191","author":"Everett","year":"2000","journal-title":"J. Exp. Med."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/0042-6822(92)90172-L","article-title":"Myxoma virus M11L ORF encodes a protein for which cell surface localization is critical in manifestation of viral virulence","volume":"191","author":"Graham","year":"1992","journal-title":"Virology"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1084\/jem.20011247","article-title":"The myxoma poxvirus protein, M11L, prevents apoptosis by direct interaction with the mitochondrial permeability transition pore","volume":"196","author":"Everett","year":"2002","journal-title":"J. Exp. Med."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1128\/JVI.80.3.1140-1151.2006","article-title":"Myxoma virus M11L blocks apoptosis through inhibition of conformational activation of Bax at the mitochondria","volume":"80","author":"Su","year":"2006","journal-title":"J. Virol."},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"7097","DOI":"10.1128\/JVI.78.13.7097-7111.2004","article-title":"Myxoma virus M11L prevents apoptosis through constitutive interaction with Bak","volume":"78","author":"Wang","year":"2004","journal-title":"J. Virol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1110\/ps.062720107","article-title":"Structure of M11L: A myxoma virus structural homolog of the apoptosis inhibitor, Bcl-2","volume":"16","author":"Douglas","year":"2007","journal-title":"Protein Sci."},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/j.molcel.2007.02.004","article-title":"A structural viral mimic of prosurvival Bcl-2: A pivotal role for sequestering proapoptotic Bax and Bak","volume":"25","author":"Kvansakul","year":"2007","journal-title":"Mol. Cell"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"11501","DOI":"10.1128\/JVI.01115-12","article-title":"Sheeppox virus SPPV14 encodes a Bcl-2-like cell death inhibitor that counters a distinct set of mammalian proapoptotic proteins","volume":"86","author":"Okamoto","year":"2012","journal-title":"J. Virol."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1107\/S1399004715009402","article-title":"Structural basis of Deerpox virus-mediated inhibition of apoptosis","volume":"71","author":"Burton","year":"2015","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"1922","DOI":"10.1128\/JVI.01959-10","article-title":"Deerpox virus encodes an inhibitor of apoptosis that regulates Bak and Bax","volume":"85","author":"Banadyga","year":"2011","journal-title":"J. Virol."},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"Gubser, C., Bergamaschi, D., Hollinshead, M., Lu, X., van Kuppeveld, F.J., and Smith, G.L. (2007). A new inhibitor of apoptosis from vaccinia virus and eukaryotes. PLoS Pathog., 3.","DOI":"10.1371\/journal.ppat.0030017"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"15896","DOI":"10.1074\/jbc.M111.336149","article-title":"Six-transmembrane topology for Golgi anti-apoptotic protein (GAAP) and Bax inhibitor 1 (BI-1) provides model for the transmembrane Bax inhibitor-containing motif (TMBIM) family","volume":"287","author":"Carrara","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"11785","DOI":"10.1074\/jbc.M115.637306","article-title":"Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration","volume":"290","author":"Carrara","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"13057","DOI":"10.1074\/jbc.M112.414367","article-title":"Human and viral Golgi anti-apoptotic proteins (GAAPs) oligomerize via different mechanisms and monomeric GAAP inhibits apoptosis and modulates calcium","volume":"288","author":"Saraiva","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"7018","DOI":"10.1128\/JVI.75.15.7018-7029.2001","article-title":"The vaccinia virus superoxide dismutase-like protein (A45R) is a virion component that is nonessential for virus replication","volume":"75","author":"Almazan","year":"2001","journal-title":"J. Virol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1006\/viro.2002.1383","article-title":"Leporipoxvirus Cu-Zn superoxide dismutase homologs inhibit cellular superoxide dismutase, but are not essential for virus replication or virulence","volume":"296","author":"Cao","year":"2002","journal-title":"Virology"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"5799","DOI":"10.1128\/JVI.79.9.5799-5811.2005","article-title":"Tumorigenic poxviruses up-regulate intracellular superoxide to inhibit apoptosis and promote cell proliferation","volume":"79","author":"Teoh","year":"2005","journal-title":"J. Virol."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"33175","DOI":"10.1074\/jbc.M300644200","article-title":"Leporipoxvirus Cu,Zn-superoxide dismutase (SOD) homologs are catalytically inert decoy proteins that bind copper chaperone for SOD","volume":"278","author":"Teoh","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"10265","DOI":"10.1128\/JVI.78.19.10265-10275.2004","article-title":"Amsacta moorei entomopoxvirus expresses an active superoxide dismutase","volume":"78","author":"Becker","year":"2004","journal-title":"J. Virol."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.virol.2017.02.017","article-title":"The Molluscum Contagiosum Virus protein MC163 localizes to the mitochondria and dampens mitochondrial mediated apoptotic responses","volume":"505","author":"Coutu","year":"2017","journal-title":"Virology"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"10625","DOI":"10.1128\/JVI.01187-08","article-title":"Targeting the retinoblastoma protein by MC007L, gene product of the molluscum contagiosum virus: Detection of a novel virus-cell interaction by a member of the poxviruses","volume":"82","author":"Mohr","year":"2008","journal-title":"J. Virol."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1126\/science.279.5347.102","article-title":"Ultraviolet-induced cell death blocked by a selenoprotein from a human dermatotropic poxvirus","volume":"279","author":"Shisler","year":"1998","journal-title":"Science"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1073\/pnas.64.1.396","article-title":"On the biosynthesis and structure of double-stranded RNA in vaccinia virus-infected cells","volume":"64","author":"Duesberg","year":"1969","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.chom.2015.02.003","article-title":"Cellular 5\u2032-3\u2032 mRNA exonuclease Xrn1 controls double-stranded RNA accumulation and anti-viral responses","volume":"17","author":"Burgess","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1006\/viro.1996.0259","article-title":"When two strands are better than one: The mediators and modulators of the cellular responses to double-stranded RNA","volume":"219","author":"Jacobs","year":"1996","journal-title":"Virology"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"5059","DOI":"10.1128\/JVI.80.10.5059-5064.2006","article-title":"Double-stranded RNA is produced by positive-strand RNA viruses and DNA viruses but not in detectable amounts by negative-strand RNA viruses","volume":"80","author":"Weber","year":"2006","journal-title":"J. Virol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"7765","DOI":"10.1074\/jbc.M110.194704","article-title":"Viral double-stranded RNAs from vaccinia virus early or intermediate gene transcripts possess PKR activating function, resulting in NF-\u03baB activation, when the K1 protein is absent or mutated","volume":"286","author":"Willis","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"2293","DOI":"10.1099\/vir.0.18942-0","article-title":"Vaccinia virus transcription","volume":"84","author":"Broyles","year":"2003","journal-title":"J. Gen. Virol."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1038\/222940a0","article-title":"Double-stranded RNA in vaccinia virus infected cells","volume":"222","author":"Colby","year":"1969","journal-title":"Nature"},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1128\/jvi.7.1.71-76.1971","article-title":"Mechanism of synthesis of vaccinia virus double-stranded ribonucleic acid in vivo and in vitro","volume":"7","author":"Colby","year":"1971","journal-title":"J. Virol."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1128\/jvi.30.1.365-374.1979","article-title":"Intermolecular duplexes formed from polyadenylylated vaccinia virus RNA","volume":"30","author":"Boone","year":"1979","journal-title":"J. Virol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"1992","DOI":"10.1128\/jvi.71.3.1992-2003.1997","article-title":"Double-stranded RNA is a trigger for apoptosis in vaccinia virus-infected cells","volume":"71","author":"Kibler","year":"1997","journal-title":"J. Virol."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"85","DOI":"10.4161\/viru.23134","article-title":"The multiple faces of proteinkinase R in antiviral defense","volume":"4","author":"Munir","year":"2013","journal-title":"Virulence"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1126\/scisignal.2003511","article-title":"PKR-dependent inflammatory signals","volume":"5","author":"Kang","year":"2012","journal-title":"Sci. Signal."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.cell.2005.08.012","article-title":"Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-\u03baB and IRF 3","volume":"122","author":"Seth","year":"2005","journal-title":"Cell"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1038\/ni1243","article-title":"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction","volume":"6","author":"Kawai","year":"2005","journal-title":"Nat. Immunol."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nature04734","article-title":"Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses","volume":"441","author":"Kato","year":"2006","journal-title":"Nature"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1038\/ni1087","article-title":"The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses","volume":"5","author":"Yoneyama","year":"2004","journal-title":"Nat. Immunol."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1126\/science.1132505","article-title":"5\u2032-Triphosphate RNA is the ligand for RIG-I","volume":"314","author":"Hornung","year":"2006","journal-title":"Science"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1126\/science.1132998","article-title":"RIG-I-mediated antiviral responses to single-stranded RNA bearing 5\u2032-phosphates","volume":"314","author":"Pichlmair","year":"2006","journal-title":"Science"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/ni921","article-title":"IKK\u03b5 and TBK1 are essential components of the IRF3 signaling pathway","volume":"4","author":"Fitzgerald","year":"2003","journal-title":"Nat. Immunol."},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"3781","DOI":"10.1128\/JVI.74.8.3781-3792.2000","article-title":"The IRF-3 transcription factor mediates Sendai virus-induced apoptosis","volume":"74","author":"Heylbroeck","year":"2000","journal-title":"J. Virol."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Huang, Y., Liu, H., Li, S., Tang, Y., Wei, B., Yu, H., and Wang, C. (2014). MAVS-MKK7-JNK2 defines a novel apoptotic signaling pathway during viral infection. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1004020"},{"key":"ref_237","doi-asserted-by":"crossref","unstructured":"Lei, Y., Moore, C.B., Liesman, R.M., O\u2019Connor, B.P., Bergstralh, D.T., Chen, Z.J., Pickles, R.J., and Ting, J.P. (2009). MAVS-mediated apoptosis and its inhibition by viral proteins. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0005466"},{"key":"ref_238","doi-asserted-by":"crossref","unstructured":"Eitz Ferrer, P., Potthoff, S., Kirschnek, S., Gasteiger, G., Kastenmuller, W., Ludwig, H., Paschen, S.A., Villunger, A., Sutter, G., and Drexler, I. (2011). Induction of Noxa-mediated apoptosis by modified vaccinia virus Ankara depends on viral recognition by cytosolic helicases, leading to IRF-3\/IFN-\u03b2-dependent induction of pro-apoptotic Noxa. PLoS Pathog., 7.","DOI":"10.1371\/journal.ppat.1002083"},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1006\/viro.1993.1223","article-title":"The interferon-induced double-stranded RNA-activated human p68 protein kinase inhibits the replication of vaccinia virus","volume":"193","author":"Lee","year":"1993","journal-title":"Virology"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1006\/viro.1993.1292","article-title":"Identification of a conserved motif that is necessary for binding of the vaccinia virus E3L gene products to double-stranded RNA","volume":"194","author":"Chang","year":"1993","journal-title":"Virology"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1006\/viro.1998.9072","article-title":"Vaccinia virus E3L protein is an inhibitor of the interferon (IFN)-induced 2-5A synthetase enzyme","volume":"243","author":"Rivas","year":"1998","journal-title":"Virology"},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1128\/JVI.01891-07","article-title":"Loss of protein kinase PKR expression in human HeLa cells complements the vaccinia virus E3L deletion mutant phenotype by restoration of viral protein synthesis","volume":"82","author":"Zhang","year":"2008","journal-title":"J. Virol."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.virol.2011.01.034","article-title":"RNA species generated in vaccinia virus infected cells activate cell type-specific MDA5 or RIG-I dependent interferon gene transcription and PKR dependent apoptosis","volume":"413","author":"Myskiw","year":"2011","journal-title":"Virology"},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1006\/viro.1993.1424","article-title":"Nuclear localization of a double-stranded RNA-binding protein encoded by the vaccinia virus E3L gene","volume":"195","author":"Yuwen","year":"1993","journal-title":"Virology"},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"4825","DOI":"10.1073\/pnas.89.11.4825","article-title":"The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNA-dependent protein kinase","volume":"89","author":"Chang","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"6974","DOI":"10.1073\/pnas.0431131100","article-title":"A role for Z-DNA binding in vaccinia virus pathogenesis","volume":"100","author":"Kim","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"8421","DOI":"10.1073\/pnas.94.16.8421","article-title":"A Z-DNA binding domain present in the human editing enzyme, double-stranded RNA adenosine deaminase","volume":"94","author":"Herbert","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"6605","DOI":"10.1128\/jvi.69.10.6605-6608.1995","article-title":"Rescue of vaccinia virus lacking the E3L gene by mutants of E3L","volume":"69","author":"Chang","year":"1995","journal-title":"J. Virol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1006\/viro.2002.1479","article-title":"The role of the PKR-inhibitory genes, E3L and K3L, in determining vaccinia virus host range","volume":"299","author":"Langland","year":"2002","journal-title":"Virology"},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1128\/jvi.69.1.499-505.1995","article-title":"Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene","volume":"69","author":"Beattie","year":"1995","journal-title":"J. Virol."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1006\/viro.1995.1342","article-title":"Distinct patterns of IFN sensitivity observed in cells infected with vaccinia K3L- and E3L-mutant viruses","volume":"210","author":"Beattie","year":"1995","journal-title":"Virology"},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1006\/viro.1997.8881","article-title":"Complementation of vaccinia virus deleted of the E3L gene by mutants of E3L","volume":"239","author":"Shors","year":"1997","journal-title":"Virology"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1006\/viro.1994.1151","article-title":"The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis","volume":"199","author":"Lee","year":"1994","journal-title":"Virology"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"850","DOI":"10.1128\/JVI.75.2.850-856.2001","article-title":"Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model","volume":"75","author":"Brandt","year":"2001","journal-title":"J. Virol."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/j.virol.2005.01.006","article-title":"The N-terminal domain of the vaccinia virus E3L-protein is required for neurovirulence, but not induction of a protective immune response","volume":"333","author":"Brandt","year":"2005","journal-title":"Virology"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"8379","DOI":"10.1038\/sj.onc.1206036","article-title":"Anti-apoptotic and oncogenic properties of the dsRNA-binding protein of vaccinia virus, E3L","volume":"21","author":"Garcia","year":"2002","journal-title":"Oncogene"},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1096\/fj.13-248294","article-title":"The impact of PKR activation: From neurodegeneration to cancer","volume":"28","author":"Marchal","year":"2014","journal-title":"FASEB J."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"7864","DOI":"10.1128\/JVI.00869-16","article-title":"Opposing Roles of double-stranded RNA effector pathways and viral defense proteins revealed with CRISPR-Cas9 knockout cell lines and vaccinia virus mutants","volume":"90","author":"Liu","year":"2016","journal-title":"J. Virol."},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"5382","DOI":"10.1128\/JVI.03288-14","article-title":"Mutational analysis of vaccinia virus E3 protein: The biological functions do not correlate with its biochemical capacity to bind double-stranded RNA","volume":"89","author":"Dueck","year":"2015","journal-title":"J. Virol."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1006\/viro.1998.9365","article-title":"The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: Implications for PKR autoregulation","volume":"250","author":"Sharp","year":"1998","journal-title":"Virology"},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"7304","DOI":"10.1128\/MCB.18.12.7304","article-title":"Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: Role of complex formation and the E3 N-terminal domain","volume":"18","author":"Romano","year":"1998","journal-title":"Mol. Cell. Biol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"25471","DOI":"10.1074\/jbc.M109.018895","article-title":"The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon \u03b2","volume":"284","author":"Marq","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"6757","DOI":"10.1128\/JVI.02570-08","article-title":"Vaccinia virus E3 suppresses expression of diverse cytokines through inhibition of the PKR, NF-\u03baB, and IRF3 pathways","volume":"83","author":"Myskiw","year":"2009","journal-title":"J. Virol."},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"2221","DOI":"10.1099\/vir.0.021998-0","article-title":"Inhibition of the RNA polymerase III-mediated dsDNA-sensing pathway of innate immunity by vaccinia virus protein E3","volume":"91","author":"Valentine","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"12280","DOI":"10.1128\/JVI.05505-11","article-title":"Comparative analysis of poxvirus orthologues of the vaccinia virus E3 protein: Modulation of protein kinase R activity, cytokine responses, and virus pathogenicity","volume":"85","author":"Myskiw","year":"2011","journal-title":"J. Virol."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.virol.2016.07.016","article-title":"Monkeypox virus induces the synthesis of less dsRNA than vaccinia virus, and is more resistant to the anti-poxvirus drug, IBT, than vaccinia virus","volume":"497","author":"Arndt","year":"2016","journal-title":"Virology"},{"key":"ref_267","doi-asserted-by":"crossref","unstructured":"Rahman, M.M., Liu, J., Chan, W.M., Rothenburg, S., and McFadden, G. (2013). Myxoma virus protein M029 is a dual function immunomodulator that inhibits PKR and also conscripts RHA\/DHX9 to promote expanded host tropism and viral replication. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003465"},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"5895","DOI":"10.1128\/JVI.06889-11","article-title":"The amino terminus of the vaccinia virus E3 protein is necessary to inhibit the interferon response","volume":"86","author":"White","year":"2012","journal-title":"J. Virol."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1099\/vir.0.015347-0","article-title":"Viral host-range factor C7 or K1 is essential for modified vaccinia virus Ankara late gene expression in human and murine cells, irrespective of their capacity to inhibit protein kinase R-mediated phosphorylation of eukaryotic translation initiation factor 2\u03b1","volume":"91","author":"Backes","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.chom.2015.02.002","article-title":"Poxvirus decapping enzymes enhance virulence by preventing the accumulation of dsRNA and the induction of innate antiviral responses","volume":"17","author":"Liu","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"2694","DOI":"10.4049\/jimmunol.181.4.2694","article-title":"Double-stranded RNA induces an antiviral defense status in epidermal keratinocytes through TLR3-, PKR-, and MDA5\/RIG-I-mediated differential signaling","volume":"181","author":"Kalali","year":"2008","journal-title":"J. Immunol."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1038\/nrmicro3469","article-title":"Viral apoptotic mimicry","volume":"13","author":"Amara","year":"2015","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/0042-6822(85)90338-1","article-title":"Reversible inactivation and reactivation of vaccinia virus by manipulation of viral lipid composition","volume":"142","author":"Oie","year":"1985","journal-title":"Virology"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1083\/jcb.121.3.521","article-title":"Assembly of vaccinia virus: Role of the intermediate compartment between the endoplasmic reticulum and the Golgi stacks","volume":"121","author":"Sodeik","year":"1993","journal-title":"J. Cell Biol."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"2121","DOI":"10.1242\/jcs.109.8.2121","article-title":"The envelope of vaccinia virus reveals an unusual phospholipid in Golgi complex membranes","volume":"109","author":"Cluett","year":"1996","journal-title":"J. Cell Sci."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"2198","DOI":"10.1091\/mbc.e11-11-0936","article-title":"Phosphatidylserine dynamics in cellular membranes","volume":"23","author":"Kay","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1146\/annurev.biophys.093008.131234","article-title":"The distribution and function of phosphatidylserine in cellular membranes","volume":"39","author":"Leventis","year":"2010","journal-title":"Annu. Rev. Biophys."},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.chom.2009.05.021","article-title":"Membrane rupture generates single open membrane sheets during vaccinia virus assembly","volume":"6","author":"Chlanda","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"12313","DOI":"10.1128\/JVI.02137-13","article-title":"Direct formation of vaccinia virus membranes from the endoplasmic reticulum in the absence of the newly characterized L2-interacting protein A30.5","volume":"87","author":"Weisberg","year":"2013","journal-title":"J. Virol."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1126\/science.1155164","article-title":"Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells","volume":"320","author":"Mercer","year":"2008","journal-title":"Science"},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"17517","DOI":"10.1073\/pnas.0909376106","article-title":"Appraising the apoptotic mimicry model and the role of phospholipids for poxvirus entry","volume":"106","author":"Laliberte","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"3647","DOI":"10.1038\/emboj.2011.245","article-title":"Vaccinia extracellular virions enter cells by macropinocytosis and acid-activated membrane rupture","volume":"30","author":"Schmidt","year":"2011","journal-title":"EMBO J."},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.coviro.2011.11.007","article-title":"Poxvirus host cell entry","volume":"2","author":"Schmidt","year":"2012","journal-title":"Curr. Opin Virol."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"7988","DOI":"10.1128\/JVI.00894-08","article-title":"A novel cellular protein, VPEF, facilitates vaccinia virus penetration into HeLa cells through fluid phase endocytosis","volume":"82","author":"Huang","year":"2008","journal-title":"J. Virol."},{"key":"ref_285","doi-asserted-by":"crossref","unstructured":"Sandgren, K.J., Wilkinson, J., Miranda-Saksena, M., McInerney, G.M., Byth-Wilson, K., Robinson, P.J., and Cunningham, A.L. (2010). A differential role for macropinocytosis in mediating entry of the two forms of vaccinia virus into dendritic cells. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1000866"},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1016\/j.chom.2011.03.012","article-title":"The soluble serum protein Gas6 bridges virion envelope phosphatidylserine to the TAM receptor tyrosine kinase Axl to mediate viral entry","volume":"9","author":"Morizono","year":"2011","journal-title":"Cell Host Microbe"},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1016\/j.cell.2007.10.034","article-title":"TAM receptors are pleiotropic inhibitors of the innate immune response","volume":"131","author":"Rothlin","year":"2007","journal-title":"Cell"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1016\/j.chom.2013.07.005","article-title":"Enveloped viruses disable innate immune responses in dendritic cells by direct activation of TAM receptors","volume":"14","author":"Bhattacharyya","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1172\/JCI1112","article-title":"Macrophages that have ingested apoptotic cells in vitro inhibit proinflammatory cytokine production through autocrine\/paracrine mechanisms involving TGF-\u03b2, PGE2, and PAF","volume":"101","author":"Fadok","year":"1998","journal-title":"J. Clin. Investig."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"350","DOI":"10.1038\/37022","article-title":"Immunosuppressive effects of apoptotic cells","volume":"390","author":"Voll","year":"1997","journal-title":"Nature"},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"7363","DOI":"10.1128\/JVI.79.12.7363-7370.2005","article-title":"Vaccinia virus induces strong immunoregulatory cytokine production in healthy human epidermal keratinocytes: A novel strategy for immune evasion","volume":"79","author":"Liu","year":"2005","journal-title":"J. Virol."},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1186\/1743-422X-4-22","article-title":"Pathogeneses of respiratory infections with virulent and attenuated vaccinia viruses","volume":"4","author":"Hayasaka","year":"2007","journal-title":"Virol. J."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/9\/8\/215\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:41:51Z","timestamp":1760208111000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/9\/8\/215"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8,8]]},"references-count":292,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2017,8]]}},"alternative-id":["v9080215"],"URL":"https:\/\/doi.org\/10.3390\/v9080215","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,8]]}}}