{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T22:54:56Z","timestamp":1790376896862,"version":"4.1.0"},"reference-count":179,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,6,1]],"date-time":"2017-06-01T00:00:00Z","timestamp":1496275200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,4,6]],"date-time":"2017-04-06T00:00:00Z","timestamp":1491436800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["BB\/M003647\/1"],"award-info":[{"award-number":["BB\/M003647\/1"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000265","name":"Medical Research Council","doi-asserted-by":"publisher","award":["MR\/M011607\/1"],"award-info":[{"award-number":["MR\/M011607\/1"]}],"id":[{"id":"10.13039\/501100000265","id-type":"DOI","asserted-by":"publisher"}]},{"name":"MRC and Wellcome Trust"}],"content-domain":{"domain":["clinicalkey.jp","clinicalkey.com","clinicalkey.es","clinicalkey.com.au","clinicalkey.fr","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Immunology Letters"],"published-print":{"date-parts":[[2017,6]]},"DOI":"10.1016\/j.imlet.2017.03.015","type":"journal-article","created":{"date-parts":[[2017,3,31]],"date-time":"2017-03-31T05:19:49Z","timestamp":1490937589000},"page":"68-80","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":69,"special_numbering":"C","title":["Vaccinia virus evasion of regulated cell death"],"prefix":"10.1016","volume":"186","author":[{"given":"David L.","family":"Veyer","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guia","family":"Carrara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"Maluquer de Motes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geoffrey L.","family":"Smith","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.imlet.2017.03.015_bib0005","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/bjc.1972.33","article-title":"Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics","volume":"26","author":"Kerr","year":"1972","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.imlet.2017.03.015_bib0010","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":"10.1016\/j.imlet.2017.03.015_bib0015","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/nri3131","article-title":"Viral infection and the evolution of caspase 8-regulated apoptotic and necrotic death pathways","volume":"12","author":"Mocarski","year":"2012","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0020","doi-asserted-by":"crossref","first-page":"1112","DOI":"10.1016\/j.cell.2009.05.037","article-title":"Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation","volume":"137","author":"Cho","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0025","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1038\/nri2215","article-title":"How dying cells alert the immune system to danger","volume":"8","author":"Kono","year":"2008","journal-title":"Nat. Rev. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0030","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1038\/nrm2970","article-title":"Molecular mechanisms of necroptosis: an ordered cellular explosion","volume":"11","author":"Vandenabeele","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0035","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1146\/annurev.immunol.021908.132715","article-title":"The inflammasomes: guardians of the body","volume":"27","author":"Martinon","year":"2009","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0040","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":"10.1016\/j.imlet.2017.03.015_bib0045","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/0092-8674(92)90274-G","article-title":"A soluble receptor for interleukin-1 beta encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection","volume":"71","author":"Alcami","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0050","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":"10.1016\/j.imlet.2017.03.015_bib0055","doi-asserted-by":"crossref","first-page":"3246","DOI":"10.4049\/jimmunol.164.6.3246","article-title":"A poxvirus protein that binds to and inactivates IL-18, and inhibits NK cell response","volume":"164","author":"Born","year":"2000","journal-title":"J. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0060","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1099\/0022-1317-81-5-1223","article-title":"Ectromelia, vaccinia and cowpox viruses encode secreted interleukin-18-binding proteins","volume":"81","author":"Smith","year":"2000","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0065","doi-asserted-by":"crossref","first-page":"9960","DOI":"10.1128\/JVI.77.18.9960-9968.2003","article-title":"Vaccinia virus interleukin-18-binding protein promotes virulence by reducing gamma interferon production and natural killer and T-cell activity","volume":"77","author":"Reading","year":"2003","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0070","doi-asserted-by":"crossref","first-page":"2833","DOI":"10.1099\/0022-1317-83-11-2833","article-title":"The vaccinia virus C12L protein inhibits mouse IL-18 and promotes virus virulence in the murine intranasal model","volume":"83","author":"Symons","year":"2002","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0075","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1099\/0022-1317-80-4-949","article-title":"Vaccinia virus strains Lister, USSR and Evans express soluble and cell-surface tumour necrosis factor receptors","volume":"80","author":"Alcami","year":"1999","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0080","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":"10.1016\/j.imlet.2017.03.015_bib0085","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":"10.1016\/j.imlet.2017.03.015_bib0090","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":"10.1016\/j.imlet.2017.03.015_bib0095","doi-asserted-by":"crossref","first-page":"1390","DOI":"10.1126\/science.1190217","article-title":"BID, BIM, and PUMA are essential for activation of the BAX- and BAK-dependent cell death program","volume":"330","author":"Ren","year":"2010","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0100","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0092-8674(04)00046-7","article-title":"Cell death: critical control points","volume":"116","author":"Danial","year":"2004","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0105","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.cell.2011.02.034","article-title":"Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol","volume":"145","author":"Edlich","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0110","doi-asserted-by":"crossref","first-page":"938","DOI":"10.1016\/j.molcel.2014.07.016","article-title":"Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers","volume":"55","author":"Brouwer","year":"2014","journal-title":"Mol. Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0115","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.cell.2012.12.031","article-title":"Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis","volume":"152","author":"Czabotar","year":"2013","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0120","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1038\/cdd.2013.169","article-title":"The apoptotic pore on mitochondria: are we breaking through or still stuck","volume":"21","author":"Borner","year":"2014","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.imlet.2017.03.015_bib0125","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":"10.1016\/j.imlet.2017.03.015_bib0130","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/j.molcel.2012.01.030","article-title":"Differences in the mechanisms of proapoptotic BH3 proteins binding to Bcl-XL and Bcl-2 quantified in live MCF-7 cells","volume":"45","author":"Aranovich","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0135","doi-asserted-by":"crossref","first-page":"e40","DOI":"10.1038\/cddis.2010.18","article-title":"A survey of the anti-apoptotic Bcl-2 subfamily expression in cancer types provides a platform to predict the efficacy of Bcl-2 antagonists in cancer therapy","volume":"1","author":"Placzek","year":"2010","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.imlet.2017.03.015_bib0140","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1016\/S0955-0674(03)00075-9","article-title":"Death from within: apoptosis and the secretory pathway","volume":"15","author":"Maag","year":"2003","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0145","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.bbamcr.2005.03.002","article-title":"Golgi structure in stress sensing and apoptosis","volume":"1744","author":"Hicks","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.imlet.2017.03.015_bib0150","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/S0955-0674(00)00219-2","article-title":"Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals","volume":"13","author":"Patil","year":"2001","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0155","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1126\/science.287.5453.664","article-title":"Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1","volume":"287","author":"Urano","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0160","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":"10.1016\/j.imlet.2017.03.015_bib0165","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S0143416002001884","article-title":"Opas M. Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum","volume":"32","author":"Michalak","year":"2002","journal-title":"Cell Calcium"},{"key":"10.1016\/j.imlet.2017.03.015_bib0170","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1146\/annurev-immunol-032414-112248","article-title":"Programmed necrosis in the cross talk of cell death and inflammation","volume":"33","author":"Chan","year":"2015","journal-title":"Annu. Rev. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0175","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":"10.1016\/j.imlet.2017.03.015_bib0180","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":"10.1016\/j.imlet.2017.03.015_bib0185","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":"10.1016\/j.imlet.2017.03.015_bib0190","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":"10.1016\/j.imlet.2017.03.015_bib0195","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":"10.1016\/j.imlet.2017.03.015_bib0200","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/S0092-8674(00)81590-1","article-title":"Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis","volume":"94","author":"Li","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0205","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0092-8674(00)81589-5","article-title":"Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors","volume":"94","author":"Luo","year":"1998","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0210","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1016\/j.cell.2009.05.021","article-title":"Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha","volume":"137","author":"He","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0215","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1126\/science.1172308","article-title":"RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis","volume":"325","author":"Zhang","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0220","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.cell.2011.11.031","article-title":"Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase","volume":"148","author":"Sun","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0225","doi-asserted-by":"crossref","first-page":"5322","DOI":"10.1073\/pnas.1200012109","article-title":"Mixed lineage kinase domain-like is a key receptor interacting protein 3 downstream component of TNF-induced necrosis","volume":"109","author":"Zhao","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0230","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nchembio.83","article-title":"Identification of RIP1 kinase as a specific cellular target of necrostatins","volume":"4","author":"Degterev","year":"2008","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0235","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1126\/science.1249361","article-title":"Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis","volume":"343","author":"Newton","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0240","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0966-842X(00)01936-3","article-title":"Pro-inflammatory programmed cell death","volume":"9","author":"Cookson","year":"2001","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0245","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/S1097-2765(02)00599-3","article-title":"The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta","volume":"10","author":"Martinon","year":"2002","journal-title":"Mol. Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0250","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1038\/nature10558","article-title":"Non-canonical inflammasome activation targets caspase-11","volume":"479","author":"Kayagaki","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0255","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1016\/j.immuni.2011.02.020","article-title":"Gain-of-function Pyrin mutations induce NLRP3 protein-independent interleukin-1beta activation and severe autoinflammation in mice","volume":"34","author":"Chae","year":"2011","journal-title":"Immunity"},{"key":"10.1016\/j.imlet.2017.03.015_bib0260","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nature13449","article-title":"Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome","volume":"513","author":"Xu","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0265","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. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0270","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1038\/nature07725","article-title":"AIM2 recognizes cytosolic dsDNA and forms a caspase-1-activating inflammasome with ASC","volume":"458","author":"Hornung","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0275","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1038\/nature13683","article-title":"Inflammatory caspases are innate immune receptors for intracellular LPS","volume":"514","author":"Shi","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0280","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1016\/j.immuni.2013.08.037","article-title":"Mechanisms of NOD-like receptor-associated inflammasome activation","volume":"39","author":"Wen","year":"2013","journal-title":"Immunity"},{"key":"10.1016\/j.imlet.2017.03.015_bib0285","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1006\/smim.2000.0297","article-title":"Immunology 102 at poxvirus U: avoiding apoptosis","volume":"13","author":"Shisler","year":"2001","journal-title":"Semin. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0290","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/j.virol.2005.09.032","article-title":"Near death experiences: poxvirus regulation of apoptotic death","volume":"344","author":"Taylor","year":"2006","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0295","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1101\/SQB.1987.052.01.060","article-title":"The serpins: evolution and adaptation in a family of protease inhibitors","volume":"52","author":"Carrell","year":"1987","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0300","doi-asserted-by":"crossref","first-page":"2995","DOI":"10.1099\/0022-1317-69-12-2995","article-title":"Non-essential genes in the vaccinia virus HindIII K fragment: a gene related to serine protease inhibitors and a gene related to the 37 K vaccinia virus major envelope antigen","volume":"69","author":"Boursnell","year":"1988","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0305","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":"10.1016\/j.imlet.2017.03.015_bib0310","doi-asserted-by":"crossref","first-page":"7698","DOI":"10.1073\/pnas.83.20.7698","article-title":"Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases","volume":"83","author":"Pickup","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0315","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":"10.1016\/j.imlet.2017.03.015_bib0320","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 beta converting enzyme","volume":"69","author":"Ray","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0325","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1038\/375078a0","article-title":"Involvement of an ICE-like protease in Fas-mediated apoptosis","volume":"375","author":"Enari","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0330","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1126\/science.8303301","article-title":"Prevention of vertebrate neuronal death by the crmA gene","volume":"263","author":"Gagliardini","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0335","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/375081a0","article-title":"Requirement of an ICE\/CED-3 protease for Fas\/APO-1-mediated apoptosis","volume":"375","author":"Los","year":"1995","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0340","doi-asserted-by":"crossref","first-page":"8318","DOI":"10.1073\/pnas.92.18.8318","article-title":"Tumor necrosis factor-induced apoptosis is mediated by a CrmA-sensitive cell death pathway","volume":"92","author":"Miura","year":"1995","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0345","doi-asserted-by":"crossref","first-page":"3255","DOI":"10.1074\/jbc.270.7.3255","article-title":"Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product","volume":"270","author":"Tewari","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0350","first-page":"524","article-title":"Analysis of a large cluster of nonessential genes deleted from a vaccinia virus terminal transposition mutant","volume":"167","author":"Kotwal","year":"1988","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0355","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 M(r) 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":"10.1016\/j.imlet.2017.03.015_bib0360","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":"10.1016\/j.imlet.2017.03.015_bib0365","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1046\/j.1365-2249.1996.927619.x","article-title":"Inhibition of CD95 (Fas\/Apo1)-mediated apoptosis by vaccinia virus WR","volume":"103","author":"Heinkelein","year":"1996","journal-title":"Clin. Exp. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0370","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-1beta-induced fever","volume":"78","author":"Kettle","year":"1997","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0375","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1099\/0022-1317-83-8-1977","article-title":"Dermal infection with vaccinia virus reveals roles for virus proteins not seen using other inoculation routes","volume":"83","author":"Tscharke","year":"2002","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0380","doi-asserted-by":"crossref","first-page":"2185","DOI":"10.1099\/0022-1317-71-9-2185","article-title":"Increased antibody responses to human papillomavirus type 16 L1 protein expressed by recombinant vaccinia virus lacking serine protease inhibitor genes","volume":"71","author":"Zhou","year":"1990","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0385","doi-asserted-by":"crossref","first-page":"11029","DOI":"10.1073\/pnas.93.20.11029","article-title":"A mechanism for the inhibition of fever by a virus","volume":"93","author":"Alcami","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0390","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0092-8674(00)81334-3","article-title":"Human ICE\/CED-3 protease nomenclature","volume":"87","author":"Alnemri","year":"1996","journal-title":"Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0395","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":"10.1016\/j.imlet.2017.03.015_bib0400","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":"Garcia-Calvo","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0405","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1038\/sj.cdd.4400598","article-title":"Caspase structure, proteolytic substrates, and function during apoptotic cell death","volume":"6","author":"Nicholson","year":"1999","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.imlet.2017.03.015_bib0410","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":"10.1016\/j.imlet.2017.03.015_bib0415","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.4049\/jimmunol.1400590","article-title":"Cutting edge: RIPK1 Kinase inactive mice are viable and protected from TNF-induced necroptosis in vivo","volume":"193","author":"Polykratis","year":"2014","journal-title":"J. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0420","doi-asserted-by":"crossref","first-page":"2074","DOI":"10.1038\/mt.2013.195","article-title":"Vaccinia virus induces programmed necrosis in ovarian cancer cells","volume":"21","author":"Whilding","year":"2013","journal-title":"Mol. Ther."},{"key":"10.1016\/j.imlet.2017.03.015_bib0425","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":"10.1016\/j.imlet.2017.03.015_bib0430","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1006\/viro.1994.1347","article-title":"The SPI-1 gene of rabbitpox virus determines host range and is required for hemorrhagic pock formation","volume":"202","author":"Ali","year":"1994","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0435","doi-asserted-by":"crossref","first-page":"7688","DOI":"10.1128\/JVI.69.12.7688-7698.1995","article-title":"A rabbitpox virus serpin gene controls host range by inhibiting apoptosis in restrictive cells","volume":"69","author":"Brooks","year":"1995","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0440","doi-asserted-by":"crossref","first-page":"9108","DOI":"10.1073\/pnas.93.17.9108","article-title":"Differential inhibition of the Fas- and granule-mediated cytolysis pathways by the orthopoxvirus cytokine response modifier A\/SPI-2 and SPI-1 protein","volume":"93","author":"Macen","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0445","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/0042-6822(90)90294-2","article-title":"The complete DNA sequence of vaccinia virus","volume":"179","author":"Goebel","year":"1990","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0450","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1099\/0022-1317-72-6-1349","article-title":"Nucleotide sequence of 42 kbp of vaccinia virus strain WR from near the right inverted terminal repeat","volume":"72","author":"Smith","year":"1991","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0455","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1038\/335176a0","article-title":"Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins","volume":"335","author":"Kotwal","year":"1988","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0460","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1038\/366748a0","article-title":"Potential virulence determinants in terminal regions of variola smallpox virus genome","volume":"366","author":"Massung","year":"1993","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0465","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/0014-5793(93)80041-R","article-title":"Genes of variola and vaccinia viruses necessary to overcome the host protective mechanisms","volume":"319","author":"Shchelkunov","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.imlet.2017.03.015_bib0470","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1126\/science.1125134","article-title":"Genome sequence diversity and clues to the evolution of variola (smallpox) virus","volume":"313","author":"Esposito","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0475","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0168-1702(93)90017-H","article-title":"Nucleotide sequence of XhoI O fragment of ectromelia virus DNA reveals significant differences from vaccinia virus","volume":"30","author":"Senkevich","year":"1993","journal-title":"Virus Res."},{"key":"10.1016\/j.imlet.2017.03.015_bib0480","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. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0485","doi-asserted-by":"crossref","first-page":"11032","DOI":"10.1128\/JVI.00734-07","article-title":"Fowlpox virus encodes a Bcl-2 homologue that protects cells from apoptotic death through interaction with the proapoptotic protein Bak","volume":"81","author":"Banadyga","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0490","doi-asserted-by":"crossref","first-page":"11437","DOI":"10.1128\/JVI.75.23.11437-11448.2001","article-title":"Vaccinia virus infection disarms the mitochondrion-mediated pathway of the apoptotic cascade by modulating the permeability transition pore","volume":"75","author":"Wasilenko","year":"2001","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0495","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1128\/JVI.79.2.1084-1098.2005","article-title":"Vaccinia virus F1L protein is a tail-anchored protein that functions at the mitochondria to inhibit apoptosis","volume":"79","author":"Stewart","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0500","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":"10.1016\/j.imlet.2017.03.015_bib0505","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":"10.1016\/j.imlet.2017.03.015_bib0510","doi-asserted-by":"crossref","first-page":"14031","DOI":"10.1128\/JVI.79.22.14031-14043.2005","article-title":"The vaccinia virus F1L protein interacts with the proapoptotic protein Bak and inhibits Bak activation","volume":"79","author":"Wasilenko","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0515","doi-asserted-by":"crossref","first-page":"39728","DOI":"10.1074\/jbc.M607465200","article-title":"The vaccinia virus protein F1L interacts with Bim and inhibits activation of the pro-apoptotic protein Bax","volume":"281","author":"Taylor","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0520","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":"10.1016\/j.imlet.2017.03.015_bib0525","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":"10.1016\/j.imlet.2017.03.015_bib0530","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":"10.1016\/j.imlet.2017.03.015_bib0535","doi-asserted-by":"crossref","first-page":"30748","DOI":"10.1074\/jbc.M111.280149","article-title":"Structural determinants of caspase-9 inhibition by the vaccinia virus protein, F1L","volume":"286","author":"Yu","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0540","doi-asserted-by":"crossref","first-page":"e1000480","DOI":"10.1371\/journal.ppat.1000480","article-title":"Innate immune sensing of modified vaccinia virus Ankara (MVA) is mediated by TLR2-TLR6, MDA-5 and the NALP3 inflammasome","volume":"5","author":"Delaloye","year":"2009","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.imlet.2017.03.015_bib0545","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/0042-6822(89)90627-2","article-title":"Mapping and insertional mutagenesis of a vaccinia virus gene encoding a 13,800-Da secreted protein","volume":"171","author":"Kotwal","year":"1989","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0550","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1196\/annals.1329.037","article-title":"Lack of N1L gene expression results in a significant decrease of vaccinia virus replication in mouse brain","volume":"1030","author":"Billings","year":"2004","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.imlet.2017.03.015_bib0555","doi-asserted-by":"crossref","first-page":"2877","DOI":"10.1099\/vir.0.2008\/004119-0","article-title":"Vaccinia virus lacking the Bcl-2-like protein N1 induces a stronger natural killer cell response to infection","volume":"89","author":"Jacobs","year":"2008","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0560","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":"10.1016\/j.imlet.2017.03.015_bib0565","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":"10.1016\/j.imlet.2017.03.015_bib0570","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":"10.1016\/j.imlet.2017.03.015_bib0575","doi-asserted-by":"crossref","first-page":"e1000128","DOI":"10.1371\/journal.ppat.1000128","article-title":"Vaccinia virus proteins A52 and B14 Share a Bcl-2-like fold but have evolved to inhibit NF-kappaB rather than apoptosis","volume":"4","author":"Graham","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.imlet.2017.03.015_bib0580","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.jmb.2008.09.048","article-title":"Poxvirus K7 protein adopts a Bcl-2 fold: biochemical mapping of its interactions with human DEAD box RNA helicase DDX3","volume":"385","author":"Kalverda","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0585","doi-asserted-by":"crossref","first-page":"906","DOI":"10.1002\/pro.2472","article-title":"Structure of vaccinia virus A46, an inhibitor of TLR4 signaling pathway, shows the conformation of VIPER motif","volume":"23","author":"Kim","year":"2014","journal-title":"Protein Sci."},{"key":"10.1016\/j.imlet.2017.03.015_bib0590","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":"10.1016\/j.imlet.2017.03.015_bib0595","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1186\/1743-422X-7-59","article-title":"A poxvirus Bcl-2-like gene family involved in regulation of host immune response: sequence similarity and evolutionary history","volume":"7","author":"Gonzalez","year":"2010","journal-title":"Virol. J."},{"key":"10.1016\/j.imlet.2017.03.015_bib0600","doi-asserted-by":"crossref","first-page":"7085","DOI":"10.1128\/JVI.00437-09","article-title":"The fowlpox virus BCL-2 homologue, FPV039, interacts with activated Bax and a discrete subset of BH3-only proteins to inhibit apoptosis","volume":"83","author":"Banadyga","year":"2009","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0605","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":"10.1016\/j.imlet.2017.03.015_bib0610","doi-asserted-by":"crossref","first-page":"e1002430","DOI":"10.1371\/journal.ppat.1002430","article-title":"Inhibition of apoptosis and NF-kB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence","volume":"7","author":"Maluquer de Motes","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.imlet.2017.03.015_bib0615","doi-asserted-by":"crossref","first-page":"36570","DOI":"10.1074\/jbc.M400567200","article-title":"Poxvirus protein N1L targets the I-kappaB kinase complex, inhibits signaling to NF-kappaB by the tumor necrosis factor superfamily of receptors, and inhibits NF-kappaB and IRF3 signaling by toll-like receptors","volume":"279","author":"DiPerna","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0620","doi-asserted-by":"crossref","first-page":"e22","DOI":"10.1371\/journal.ppat.0040022","article-title":"Inhibition of IkappaB kinase by vaccinia virus virulence factor B14","volume":"4","author":"Chen","year":"2008","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.imlet.2017.03.015_bib0625","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1111\/imm.12422","article-title":"Enhancement of CD8(+) T-cell memory by removal of a vaccinia virus nuclear factor-kappaB inhibitor","volume":"145","author":"Ren","year":"2015","journal-title":"Immunology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0630","doi-asserted-by":"crossref","first-page":"2038","DOI":"10.1099\/vir.0.065664-0","article-title":"Vaccinia virus virulence factor N1 can be ubiquitylated on multiple lysine residues","volume":"95","author":"Maluquer de Motes","year":"2014","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0635","doi-asserted-by":"crossref","first-page":"e17","DOI":"10.1371\/journal.ppat.0030017","article-title":"A new inhibitor of apoptosis from vaccinia virus and eukaryotes","volume":"3","author":"Gubser","year":"2007","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.imlet.2017.03.015_bib0640","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1099\/0022-1317-83-4-855","article-title":"The sequence of camelpox virus shows it is most closely related to variola virus, the cause of smallpox","volume":"83","author":"Gubser","year":"2002","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0645","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":"10.1016\/j.imlet.2017.03.015_bib0650","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.gene.2003.09.011","article-title":"Evolutionarily conserved cytoprotection provided by Bax Inhibitor-1 homologs from animals, plants, and yeast","volume":"323","author":"Chae","year":"2003","journal-title":"Gene"},{"key":"10.1016\/j.imlet.2017.03.015_bib0655","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S1097-2765(00)80034-9","article-title":"Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast","volume":"1","author":"Xu","year":"1998","journal-title":"Mol. Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0660","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":"10.1016\/j.imlet.2017.03.015_bib0665","doi-asserted-by":"crossref","first-page":"3638","DOI":"10.1091\/mbc.E09-05-0385","article-title":"Human Golgi antiapoptotic protein modulates intracellular calcium fluxes","volume":"20","author":"de Mattia","year":"2009","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.imlet.2017.03.015_bib0670","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1083\/jcb.201301016","article-title":"hGAAP promotes cell adhesion and migration via the stimulation of store-operated Ca2+ entry and calpain 2","volume":"202","author":"Saraiva","year":"2013","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0675","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":"10.1016\/j.imlet.2017.03.015_bib0680","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. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0685","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1128\/JVI.67.3.1688-1692.1993","article-title":"The E3L and K3L vaccinia virus gene products stimulate translation through inhibition of the double-stranded RNA-dependent protein kinase by different mechanisms","volume":"67","author":"Davies","year":"1993","journal-title":"J. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0690","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":"10.1016\/j.imlet.2017.03.015_bib0695","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1006\/viro.1996.0114","article-title":"Physical and functional characterization of the double-stranded RNA binding protein encoded by the vaccinia virus E3 gene","volume":"217","author":"Ho","year":"1996","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0700","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":"10.1016\/j.imlet.2017.03.015_bib0705","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. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0710","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":"10.1016\/j.imlet.2017.03.015_bib0715","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":"10.1016\/j.imlet.2017.03.015_bib0720","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. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0725","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":"10.1016\/j.imlet.2017.03.015_bib0730","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":"10.1016\/j.imlet.2017.03.015_bib0735","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":"10.1016\/j.imlet.2017.03.015_bib0740","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":"10.1016\/j.imlet.2017.03.015_bib0745","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":"10.1016\/j.imlet.2017.03.015_bib0750","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 alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB","volume":"19","author":"Gil","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0755","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1074\/jbc.273.4.2416","article-title":"Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase","volume":"273","author":"Srivastava","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0760","doi-asserted-by":"crossref","first-page":"3279","DOI":"10.1073\/pnas.94.7.3279","article-title":"A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis","volume":"94","author":"Der","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0765","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":"10.1016\/j.imlet.2017.03.015_bib0770","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":"10.1016\/j.imlet.2017.03.015_bib0775","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":"10.1016\/j.imlet.2017.03.015_bib0780","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 beta","volume":"284","author":"Marq","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.imlet.2017.03.015_bib0785","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":"10.1016\/j.imlet.2017.03.015_bib0790","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/nrc776","article-title":"Death and anti-death: tumour resistance to apoptosis","volume":"2","author":"Igney","year":"2002","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.imlet.2017.03.015_bib0795","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/nrc2545","article-title":"Targeted and armed oncolytic poxviruses: a novel multi-mechanistic therapeutic class for cancer","volume":"9","author":"Kirn","year":"2009","journal-title":"Nat. Rev. Cancer"},{"key":"10.1016\/j.imlet.2017.03.015_bib0800","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1007\/s12026-011-8211-4","article-title":"Immunotherapeutic potential of oncolytic vaccinia virus","volume":"50","author":"Thorne","year":"2011","journal-title":"Immunol. Res."},{"key":"10.1016\/j.imlet.2017.03.015_bib0805","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1158\/2326-6066.CIR-13-0059-T","article-title":"Combining oncolytic HSV-1 with immunogenic cell death-inducing drug mitoxantrone breaks cancer immune tolerance and improves therapeutic efficacy","volume":"1","author":"Workenhe","year":"2013","journal-title":"Cancer Immunol. Res"},{"key":"10.1016\/j.imlet.2017.03.015_bib0810","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/mt.2013.220","article-title":"Oncolytic virotherapy and immunogenic cancer cell death: sharpening the sword for improved cancer treatment strategies","volume":"22","author":"Workenhe","year":"2014","journal-title":"Mol. Ther."},{"key":"10.1016\/j.imlet.2017.03.015_bib0815","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/nature10358","article-title":"Intravenous delivery of a multi-mechanistic cancer-targeted oncolytic poxvirus in humans","volume":"477","author":"Breitbach","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0820","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1111\/j.1365-2249.2006.03177.x","article-title":"The highly attenuated vaccinia virus strain modified virus Ankara induces apoptosis in melanoma cells and allows bystander dendritic cells to generate a potent anti-tumoral immunity","volume":"146","author":"Greiner","year":"2006","journal-title":"Clin. Exp. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0825","doi-asserted-by":"crossref","first-page":"9991","DOI":"10.1158\/0008-5472.CAN-05-1630","article-title":"The enhanced tumor selectivity of an oncolytic vaccinia lacking the host range and antiapoptosis genes SPI-1 and SPI-2","volume":"65","author":"Guo","year":"2005","journal-title":"Cancer Res."},{"key":"10.1016\/j.imlet.2017.03.015_bib0830","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1086\/381976","article-title":"Looking back at smallpox","volume":"38","author":"Bray","year":"2004","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/j.imlet.2017.03.015_bib0835","series-title":"Smallpox and Its Eradication","author":"Fenner","year":"1988"},{"key":"10.1016\/j.imlet.2017.03.015_bib0840","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1586\/erv.11.79","article-title":"Vaccinia viruses: vaccines against smallpox and vectors against infectious diseases and tumors","volume":"10","author":"Walsh","year":"2011","journal-title":"Expert Rev. Vaccines"},{"key":"10.1016\/j.imlet.2017.03.015_bib0845","doi-asserted-by":"crossref","first-page":"10847","DOI":"10.1073\/pnas.89.22.10847","article-title":"Nonreplicating vaccinia vector efficiently expresses recombinant genes","volume":"89","author":"Sutter","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.imlet.2017.03.015_bib0850","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1089\/aid.1992.8.1445","article-title":"Highly attenuated poxvirus vectors","volume":"8","author":"Tartaglia","year":"1992","journal-title":"AIDS Res. Hum. Retroviruses"},{"key":"10.1016\/j.imlet.2017.03.015_bib0855","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1038\/32183","article-title":"Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs","volume":"392","author":"Albert","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0860","doi-asserted-by":"crossref","first-page":"2679","DOI":"10.4049\/jimmunol.178.5.2679","article-title":"Apoptotic cells induce tolerance by generating helpless CD8+ T cells that produce TRAIL","volume":"178","author":"Griffith","year":"2007","journal-title":"J. Immunol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0865","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1038\/nature03337","article-title":"CD4+ T-cell help controls CD8+ T-cell memory via TRAIL-mediated activation-induced cell death","volume":"434","author":"Janssen","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.imlet.2017.03.015_bib0870","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.aad0395","article-title":"RIPK1 and NF-kappaB signaling in dying cells determines cross-priming of CD8(+) T cells","volume":"350","author":"Yatim","year":"2015","journal-title":"Science"},{"key":"10.1016\/j.imlet.2017.03.015_bib0875","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1006\/viro.1998.9123","article-title":"The complete genomic sequence of the modified vaccinia Ankara strain: comparison with other orthopoxviruses","volume":"244","author":"Antoine","year":"1998","journal-title":"Virology"},{"key":"10.1016\/j.imlet.2017.03.015_bib0880","doi-asserted-by":"crossref","first-page":"2216","DOI":"10.1099\/vir.0.022343-0","article-title":"Mutations in modified virus Ankara protein 183 render it a non-functional counterpart of B14, an inhibitor of nuclear factor kappaB activation","volume":"91","author":"McCoy","year":"2010","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0885","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1099\/vir.0.80646-0","article-title":"Inactivation of the viral interleukin 1beta receptor improves CD8+ T-cell memory responses elicited upon immunization with modified vaccinia virus Ankara","volume":"86","author":"Staib","year":"2005","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.imlet.2017.03.015_bib0890","doi-asserted-by":"crossref","first-page":"e12395","DOI":"10.1371\/journal.pone.0012395","article-title":"Immunogenic profiling in mice of a HIV\/AIDS vaccine candidate (MVA-B) expressing four HIV-1 antigens and potentiation by specific gene deletions","volume":"5","author":"Garcia-Arriaza","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.imlet.2017.03.015_bib0895","doi-asserted-by":"crossref","first-page":"e48524","DOI":"10.1371\/journal.pone.0048524","article-title":"Deletion of the viral anti-apoptotic gene F1L in the HIV\/AIDS vaccine candidate MVA-C enhances immune responses against HIV-1 antigens","volume":"7","author":"Perdiguero","year":"2012","journal-title":"PLoS One"}],"container-title":["Immunology Letters"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165247817300548?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0165247817300548?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2020,10,4]],"date-time":"2020-10-04T18:29:14Z","timestamp":1601836154000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0165247817300548"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,6]]},"references-count":179,"alternative-id":["S0165247817300548"],"URL":"https:\/\/doi.org\/10.1016\/j.imlet.2017.03.015","relation":{},"ISSN":["0165-2478"],"issn-type":[{"value":"0165-2478","type":"print"}],"subject":[],"published":{"date-parts":[[2017,6]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Vaccinia virus evasion of regulated cell death","name":"articletitle","label":"Article Title"},{"value":"Immunology Letters","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.imlet.2017.03.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 The Authors. Published by Elsevier B.V. on behalf of European Federation of Immunological Societies.","name":"copyright","label":"Copyright"}]}}