{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T00:33:33Z","timestamp":1790728413834,"version":"4.1.0"},"reference-count":175,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2017,10,6]],"date-time":"2017-10-06T00:00:00Z","timestamp":1507248000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["APP1103871"],"award-info":[{"award-number":["APP1103871"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","award":["FT130101349"],"award-info":[{"award-number":["FT130101349"]}],"id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Members of the B cell lymphoma-2 (Bcl-2) family are pivotal arbiters of mitochondrially mediated apoptosis, a process of fundamental importance during tissue development, homeostasis, and disease. At the structural and mechanistic level, the mammalian members of the Bcl-2 family are increasingly well understood, with their interplay ultimately deciding the fate of a cell. Dysregulation of Bcl-2-mediated apoptosis underlies a plethora of diseases, and numerous viruses have acquired homologs of Bcl-2 to subvert host cell apoptosis and autophagy to prevent premature death of an infected cell. Here we review the structural biology, interactions, and mechanisms of action of virus-encoded Bcl-2 proteins, and how they impact on host-virus interactions to ultimately enable successful establishment and propagation of viral infections.<\/jats:p>","DOI":"10.3390\/v9100290","type":"journal-article","created":{"date-parts":[[2017,10,6]],"date-time":"2017-10-06T10:56:34Z","timestamp":1507287394000},"page":"290","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":114,"title":["The Bcl-2 Family in Host-Virus Interactions"],"prefix":"10.3390","volume":"9","author":[{"given":"Marc","family":"Kvansakul","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofia","family":"Caria","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Hinds","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, VIC 3086, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2017,10,6]]},"reference":[{"key":"ref_1","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":"ref_2","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/cdd.2011.96","article-title":"Molecular definitions of cell death subroutines: Recommendations of the Nomenclature Committee on Cell Death 2012","volume":"19","author":"Galluzzi","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"3667","DOI":"10.1038\/emboj.2011.307","article-title":"Deciphering the rules of programmed cell death to improve therapy of cancer and other diseases","volume":"30","author":"Strasser","year":"2011","journal-title":"EMBO J."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Hardwick, J.M., and Soane, L. (2013). Multiple functions of BCL-2 family proteins. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a008722"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1038\/nrm2308","article-title":"The BCL-2 protein family: Opposing activities that mediate cell death","volume":"9","author":"Youle","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1007\/s10495-014-1051-7","article-title":"The Bcl-2 family: Structures, interactions and targets for drug discovery","volume":"20","author":"Kvansakul","year":"2015","journal-title":"Apoptosis"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/B978-0-12-417158-9.00003-0","article-title":"The structural biology of BH3-only proteins","volume":"544","author":"Kvansakul","year":"2014","journal-title":"Methods Enzymol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"e909","DOI":"10.1038\/cddis.2013.436","article-title":"Structural biology of the Bcl-2 family and its mimicry by viral proteins","volume":"4","author":"Kvansakul","year":"2013","journal-title":"Cell Death Dis."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/nrc.2015.17","article-title":"Thirty years of BCL-2: Translating cell death discoveries into novel cancer therapies","volume":"16","author":"Delbridge","year":"2016","journal-title":"Nat. Rev. Cancer"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1042\/BJ20041142","article-title":"The protein structures that shape caspase activity, specificity, activation and inhibition","volume":"384","author":"Salvesen","year":"2004","journal-title":"Biochem. J."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1038\/nrm3735","article-title":"Self-consumption: The interplay of autophagy and apoptosis","volume":"15","author":"Marino","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.gene.2004.02.017","article-title":"Comparative genomics: The evolutionary history of the Bcl-2 family","volume":"333","author":"Lanave","year":"2004","journal-title":"Gene"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"a008649","DOI":"10.1101\/cshperspect.a008649","article-title":"Evolution of the animal apoptosis network","volume":"5","author":"Zmasek","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.tcb.2012.10.010","article-title":"Evolution of Bcl-2 homology motifs: Homology versus homoplasy","volume":"23","author":"Aouacheria","year":"2013","journal-title":"Trends Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2395","DOI":"10.1093\/molbev\/msi234","article-title":"Phylogenomics of life-or-death switches in multicellular animals: Bcl-2, BH3-Only, and BNip families of apoptotic regulators","volume":"22","author":"Aouacheria","year":"2005","journal-title":"Mol. Biol. Evol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1808","DOI":"10.3390\/ijms11041808","article-title":"Intrinsically disordered proteins in Bcl-2 regulated apoptosis","volume":"11","author":"Rautureau","year":"2010","journal-title":"Int. J. Mol. Sci."},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Shamas-Din, A., Kale, J., Leber, B., and Andrews, D.W. (2013). Mechanisms of action of Bcl-2 family proteins. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a008714"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1038\/cdd.2011.210","article-title":"BCL-2 family member BOK is widely expressed but its loss has only minimal impact in mice","volume":"19","author":"Ke","year":"2012","journal-title":"Cell Death Differ."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/S0092-8674(00)80572-3","article-title":"Solution structure of BID, an intracellular amplifier of apoptotic signaling","volume":"96","author":"Chou","year":"1999","journal-title":"Cell"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/S0092-8674(00)80573-5","article-title":"Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists","volume":"96","author":"McDonnell","year":"1999","journal-title":"Cell"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"S93","DOI":"10.1038\/onc.2009.47","article-title":"Bid: A Bax-like BH3 protein","volume":"27","author":"Billen","year":"2008","journal-title":"Oncogene"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"35840","DOI":"10.1074\/jbc.M113.503680","article-title":"Structural insights of tBid, the caspase-8-activated Bid, and its BH3 domain","volume":"288","author":"Wang","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"8704","DOI":"10.1021\/bi901171n","article-title":"Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL","volume":"48","author":"Yao","year":"2009","journal-title":"Biochemistry"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1038\/sj.cdd.4400906","article-title":"Sponge Bcl-2 homologous protein (BHP2-GC) confers distinct stress resistance to human HEK-293 cells","volume":"8","author":"Wiens","year":"2001","journal-title":"Cell Death Differ."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1139\/z05-165","article-title":"Cell death in Porifera: Molecular players in the game of apoptotic cell death in living fossils","volume":"84","author":"Wiens","year":"2006","journal-title":"Can. J. Zool."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1093\/icb\/45.4.631","article-title":"Hydra and the evolution of apoptosis","volume":"45","author":"David","year":"2005","journal-title":"Integr. Comp. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1089\/dna.2006.25.152","article-title":"Axial (apical-basal) expression of pro-apoptotic and pro-survival genes in the lake baikal demosponge Lubomirskia baicalensis","volume":"25","author":"Wiens","year":"2006","journal-title":"DNA Cell Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1038\/cr.2010.66","article-title":"The molecular cell death machinery in the simple cnidarian Hydra includes an expanded caspase family and pro- and anti-apoptotic Bcl-2 proteins","volume":"20","author":"Lasi","year":"2010","journal-title":"Cell Res."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/j.ejcb.2006.05.006","article-title":"Monomeric red fluorescent protein variants used for imaging studies in different species","volume":"85","author":"Vos","year":"2006","journal-title":"Eur. J. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.semcancer.2006.11.008","article-title":"Programmed cell death in Hydra","volume":"17","author":"Bottger","year":"2007","journal-title":"Semin. Cancer Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"155","DOI":"10.3354\/dao02882","article-title":"In situ hybridisation detects pro-apoptotic gene expression of a Bcl-2 family member in white syndrome-affected coral","volume":"117","author":"Ainsworth","year":"2015","journal-title":"Dis. Aquat. Organ."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"e2543","DOI":"10.1038\/cddis.2016.469","article-title":"Structural insight into an evolutionarily ancient programmed cell death regulator - the crystal structure of marine sponge BHP2 bound to LB-Bak-2","volume":"8","author":"Caria","year":"2017","journal-title":"Cell Death Dis."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/S1074-7613(03)00234-6","article-title":"The structure of a Bcl-xL\/Bim fragment complex: Implications for Bim function","volume":"19","author":"Liu","year":"2003","journal-title":"Immunity"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Kvansakul, M., Wei, A.H., Fletcher, J.I., Willis, S.N., Chen, L., Roberts, A.W., Huang, D.C., and Colman, P.M. (2010). Structural basis for apoptosis inhibition by Epstein-Barr virus BHRF1. PLoS Pathog., 6.","DOI":"10.1371\/journal.ppat.1001236"},{"key":"ref_35","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_36","doi-asserted-by":"crossref","unstructured":"Banjara, S., Caria, S., Dixon, L.K., Hinds, M.G., and Kvansakul, M. (2017). Structural Insight into African Swine Fever Virus A179L-Mediated Inhibition of Apoptosis. J. Virol., 91.","DOI":"10.1128\/JVI.02228-16"},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Ku, B., Woo, J.S., Liang, C., Lee, K.H., Hong, H.S., E, X., Kim, K.S., Jung, J.U., and Oh, B.H. (2008). Structural and biochemical bases for the inhibition of autophagy and apoptosis by viral BCL-2 of murine gamma-herpesvirus 68. PLoS Pathog., 4.","DOI":"10.1371\/journal.ppat.0040025"},{"key":"ref_38","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_39","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_40","doi-asserted-by":"crossref","first-page":"1478","DOI":"10.1038\/cdd.2017.82","article-title":"BCL-2 family: Integrating stress responses at the ER to control cell demise","volume":"24","author":"Pihan","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1038\/ni.2991","article-title":"Emerging functions of the unfolded protein response in immunity","volume":"15","author":"Janssens","year":"2014","journal-title":"Nat. Immunol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/S1097-2765(00)00136-2","article-title":"The combined functions of proapoptotic Bcl-2 family members Bak and Bax are essential for normal development of multiple tissues","volume":"6","author":"Lindsten","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1126\/science.287.5457.1485","article-title":"Translocation of C. elegans CED-4 to nuclear membranes during programmed cell death","volume":"287","author":"Chen","year":"2000","journal-title":"Science"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.virusres.2015.02.026","article-title":"How do viruses control mitochondria-mediated apoptosis?","volume":"209","author":"Neumann","year":"2015","journal-title":"Virus Res."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"2737","DOI":"10.1099\/0022-1317-80-10-2737","article-title":"The murine gammaherpesvirus-68 M11 protein inhibits Fas- and TNF-induced apoptosis","volume":"80","author":"Wang","year":"1999","journal-title":"J. Gen. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"6553","DOI":"10.1128\/jvi.68.10.6553-6566.1994","article-title":"Functional complementation of the adenovirus E1B 19-kilodalton protein with Bcl-2 in the inhibition of apoptosis in infected cells","volume":"68","author":"Chiou","year":"1994","journal-title":"J. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"8479","DOI":"10.1073\/pnas.90.18.8479","article-title":"Epstein-Barr virus-coded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death","volume":"90","author":"Henderson","year":"1993","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1073\/pnas.94.2.690","article-title":"A Bcl-2 homolog encoded by Kaposi sarcoma-associated virus, human herpesvirus 8, inhibits apoptosis but does not heterodimerize with Bax or Bak","volume":"94","author":"Cheng","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"3428","DOI":"10.1073\/pnas.062525799","article-title":"Solution structure of a Bcl-2 homolog from Kaposi sarcoma virus","volume":"99","author":"Huang","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.virol.2003.08.014","article-title":"Characterization of vNR-13, the first alphaherpesvirus gene of the bcl-2 family","volume":"316","author":"Aouacheria","year":"2003","journal-title":"Virology"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1006\/viro.1996.0592","article-title":"African swine fever virus gene A179L, a viral homologue of bcl-2, protects cells from programmed cell death","volume":"225","author":"Brun","year":"1996","journal-title":"Virology"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.virol.2005.05.021","article-title":"Complete genome sequence analysis of an iridovirus isolated from the orange-spotted grouper, Epinephelus coioides","volume":"339","author":"Lu","year":"2005","journal-title":"Virology"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1128\/JVI.79.4.2010-2023.2005","article-title":"Complete genome sequence of the grouper iridovirus and comparison of genomic organization with those of other iridoviruses","volume":"79","author":"Tsai","year":"2005","journal-title":"J. Virol."},{"key":"ref_54","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_55","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_56","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_57","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_58","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_59","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.virol.2014.10.023","article-title":"Ectromelia virus encodes an anti-apoptotic protein that regulates cell death","volume":"475","author":"Mehta","year":"2015","journal-title":"Virology"},{"key":"ref_60","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_61","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_62","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_63","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":"ref_64","doi-asserted-by":"crossref","first-page":"9010","DOI":"10.1074\/jbc.M116.768879","article-title":"Structural basis of apoptosis inhibition by the fowlpox virus protein FPV039","volume":"292","author":"Anasir","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1128\/JVI.78.1.353-366.2004","article-title":"The genome of canarypox virus","volume":"78","author":"Tulman","year":"2004","journal-title":"J. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"7178","DOI":"10.1128\/JVI.00404-07","article-title":"A novel Bcl-2-like inhibitor of apoptosis is encoded by the parapoxvirus ORF virus","volume":"81","author":"Westphal","year":"2007","journal-title":"J. Virol."},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"Uren, R.T., Iyer, S., and Kluck, R.M. (2017). Pore formation by dimeric Bak and Bax: An unusual pore?. Philos. Trans. R. Soc. Lond. B Biol. Sci., 372.","DOI":"10.1098\/rstb.2016.0218"},{"key":"ref_68","doi-asserted-by":"crossref","unstructured":"Altmann, M., and Hammerschmidt, W. (2005). Epstein-Barr virus provides a new paradigm: A requirement for the immediate inhibition of apoptosis. PLoS Biol., 3.","DOI":"10.1371\/journal.pbio.0030404"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"67","DOI":"10.15252\/embj.201488806","article-title":"Differential retrotranslocation of mitochondrial Bax and Bak","volume":"34","author":"Todt","year":"2015","journal-title":"EMBO J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1083\/jcb.200302084","article-title":"Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis","volume":"162","author":"Zong","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_71","first-page":"2468","article-title":"Multiple subcellular localization of Bcl-2: Detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes","volume":"54","author":"Akao","year":"1994","journal-title":"Cancer Res."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1083\/jcb.139.5.1281","article-title":"Movement of Bax from the cytosol to mitochondria during apoptosis","volume":"139","author":"Wolter","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3668","DOI":"10.1073\/pnas.94.8.3668","article-title":"Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis","volume":"94","author":"Hsu","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","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":"ref_75","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1038\/cdd.2012.131","article-title":"The C-terminal helix of Bcl-x(L) mediates Bax retrotranslocation from the mitochondria","volume":"20","author":"Todt","year":"2013","journal-title":"Cell Death Differ."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/j.molcel.2012.12.022","article-title":"Bax exists in a dynamic equilibrium between the cytosol and mitochondria to control apoptotic priming","volume":"49","author":"Schellenberg","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/S0092-8674(00)00167-7","article-title":"Structure of Bax: Coregulation of dimer formation and intracellular localization","volume":"103","author":"Suzuki","year":"2000","journal-title":"Cell"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/0092-8674(93)90509-O","article-title":"Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death","volume":"74","author":"Oltvai","year":"1993","journal-title":"Cell"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1083\/jcb.200302144","article-title":"Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity","volume":"162","author":"Crawford","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1093\/emboj\/cdg144","article-title":"The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity","volume":"22","author":"Hinds","year":"2003","journal-title":"EMBO J."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"4720","DOI":"10.1128\/jvi.66.8.4720-4731.1992","article-title":"Deletion analysis of two tandemly arranged virulence genes in myxoma virus, M11L and myxoma growth factor","volume":"66","author":"Opgenorth","year":"1992","journal-title":"J. Virol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2330","DOI":"10.1093\/emboj\/18.9.2330","article-title":"Conformation of the Bax C-terminus regulates subcellular location and cell death","volume":"18","author":"Nechushtan","year":"1999","journal-title":"EMBO J."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Tait, S.W., and Green, D.R. (2013). Mitochondrial regulation of cell death. Cold Spring Harb. Perspect. Biol., 5.","DOI":"10.1101\/cshperspect.a008706"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1038\/nrm3722","article-title":"Control of apoptosis by the BCL-2 protein family: Implications for physiology and therapy","volume":"15","author":"Czabotar","year":"2014","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"e1735","DOI":"10.1038\/cddis.2015.105","article-title":"Bid chimeras indicate that most BH3-only proteins can directly activate Bak and Bax, and show no preference for Bak versus Bax","volume":"6","author":"Hockings","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_86","first-page":"2865","article-title":"Nuclear envelope localization of an adenovirus tumor antigen maintains the integrity of cellular DNA","volume":"4","author":"White","year":"1984","journal-title":"Mol. Cell Biol."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1038\/sj.onc.1201323","article-title":"The E1B 19K protein associates with lamins in vivo and its proper localization is required for inhibition of apoptosis","volume":"15","author":"Rao","year":"1997","journal-title":"Oncogene"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"9199","DOI":"10.1128\/JVI.00637-13","article-title":"Frog virus 3 open reading frame 97R localizes to the endoplasmic reticulum and induces nuclear invaginations","volume":"87","author":"Ring","year":"2013","journal-title":"J. Virol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"305","DOI":"10.2174\/156652413804810736","article-title":"A179L, a new viral Bcl2 homolog targeting Beclin 1 autophagy related protein","volume":"13","author":"Hernaez","year":"2013","journal-title":"Curr. Mol. Med."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.tcb.2016.11.004","article-title":"Bax and Bak Pores: Are We Closing the Circle?","volume":"27","author":"Cosentino","year":"2017","journal-title":"Trends Cell Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1310","DOI":"10.1016\/j.str.2017.06.009","article-title":"Conformational Heterogeneity in the Activation Mechanism of Bax","volume":"25","author":"Barnes","year":"2017","journal-title":"Structure"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1038\/s41467-017-00086-6","article-title":"Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation","volume":"8","author":"Bleicken","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"402","DOI":"10.15252\/embj.201592789","article-title":"Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis","volume":"35","author":"Grosse","year":"2016","journal-title":"EMBO J."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"389","DOI":"10.15252\/embj.201593384","article-title":"Bax assembly into rings and arcs in apoptotic mitochondria is linked to membrane pores","volume":"35","author":"Mund","year":"2016","journal-title":"EMBO J."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1073\/pnas.1612322114","article-title":"Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes","volume":"114","author":"Sancho","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2262","DOI":"10.1016\/j.jmb.2015.02.019","article-title":"Conformation of BCL-XL upon Membrane Integration","volume":"427","author":"Yao","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1038\/381335a0","article-title":"X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death","volume":"381","author":"Muchmore","year":"1996","journal-title":"Nature"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.pep.2016.02.010","article-title":"Characterization of the membrane-inserted C-terminus of cytoprotective BCL-XL","volume":"122","author":"Yao","year":"2016","journal-title":"Protein Expr. Purif."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1038\/cdd.2015.15","article-title":"Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains","volume":"22","author":"Iyer","year":"2015","journal-title":"Cell Death Differ."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/j.molcel.2009.11.008","article-title":"Bak activation for apoptosis involves oligomerization of dimers via their \u03b16 helices","volume":"36","author":"Dewson","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1076","DOI":"10.1038\/nature07396","article-title":"BAX activation is initiated at a novel interaction site","volume":"455","author":"Gavathiotis","year":"2008","journal-title":"Nature"},{"key":"ref_102","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":"ref_103","doi-asserted-by":"crossref","first-page":"e1809","DOI":"10.1038\/cddis.2015.141","article-title":"Crystal structure of Bax bound to the BH3 peptide of Bim identifies important contacts for interaction","volume":"6","author":"Robin","year":"2015","journal-title":"Cell Death Dis."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.jmb.2005.11.032","article-title":"BCL-XL dimerization by three-dimensional domain swapping","volume":"356","author":"Manion","year":"2006","journal-title":"J. Mol. Biol."},{"key":"ref_105","first-page":"49","article-title":"Avian reovirus-triggered apoptosis enhances both virus spread and the processing of the viral nonstructural muNS protein","volume":"462\u2013463","author":"Busch","year":"2014","journal-title":"Virology"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1101\/gad.10.4.461","article-title":"The E1B 19K protein blocks apoptosis by interacting with and inhibiting the p53-inducible and death-promoting Bax protein","volume":"10","author":"Han","year":"1996","journal-title":"Genes Dev."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1038\/374731a0","article-title":"Cloning of a Bcl-2 homologue by interaction with adenovirus E1B 19K","volume":"374","author":"Farrow","year":"1995","journal-title":"Nature"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"6052","DOI":"10.1128\/MCB.18.10.6052","article-title":"E1B 19,000-molecular-weight protein interacts with and inhibits CED-4-dependent, FLICE-mediated apoptosis","volume":"18","author":"Han","year":"1998","journal-title":"Mol. Cell Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1016\/j.jmb.2003.08.007","article-title":"Solution structure of the BHRF1 protein from Epstein-Barr virus, a homolog of human Bcl-2","volume":"332","author":"Huang","year":"2003","journal-title":"J. Mol. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"580","DOI":"10.1038\/sj.cdd.4402292","article-title":"BH3 domains define selective inhibitory interactions with BHRF-1 and KSHV BCL-2","volume":"15","author":"Flanagan","year":"2008","journal-title":"Cell Death Differ."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"5663","DOI":"10.1073\/pnas.0901036106","article-title":"The Epstein-Barr virus Bcl-2 homolog, BHRF1, blocks apoptosis by binding to a limited amount of Bim","volume":"106","author":"Desbien","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Kelly, G.L., Long, H.M., Stylianou, J., Thomas, W.A., Leese, A., Bell, A.I., Bornkamm, G.W., Mautner, J., Rickinson, A.B., and Rowe, M. (2009). An Epstein-Barr virus anti-apoptotic protein constitutively expressed in transformed cells and implicated in burkitt lymphomagenesis: The Wp\/BHRF1 link. PLoS Pathog., 5.","DOI":"10.1371\/journal.ppat.1000341"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"5181","DOI":"10.1128\/JVI.73.6.5181-5185.1999","article-title":"Epstein-Barr virus encodes a novel homolog of the bcl-2 oncogene that inhibits apoptosis and associates with Bax and Bak","volume":"73","author":"Marshall","year":"1999","journal-title":"J. Virol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"2469","DOI":"10.1128\/jvi.76.5.2469-2479.2002","article-title":"Epstein-Barr virus BALF1 is a BCL-2-like antagonist of the herpesvirus antiapoptotic BCL-2 proteins","volume":"76","author":"Bellows","year":"2002","journal-title":"J. Virol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1644","DOI":"10.1016\/j.cell.2014.04.034","article-title":"A computationally designed inhibitor of an Epstein-Barr viral Bcl-2 protein induces apoptosis in infected cells","volume":"157","author":"Procko","year":"2014","journal-title":"Cell"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1521","DOI":"10.1107\/S1744309112043333","article-title":"Crystallization and preliminary X-ray characterization of Epstein-Barr virus BHRF1 in complex with a benzoylurea peptidomimetic","volume":"68","author":"Caria","year":"2012","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/nm0397-293","article-title":"Kaposi\u2019s sarcoma-associated herpesvirus encodes a functional Bcl-2 homologue","volume":"3","author":"Sarid","year":"1997","journal-title":"Nat. Med."},{"key":"ref_118","doi-asserted-by":"crossref","unstructured":"Gallo, A., Lampe, M., Gunther, T., and Brune, W. (2017). The Viral Bcl-2 Homologs of Kaposi\u2019s Sarcoma-Associated Herpesvirus and Rhesus Rhadinovirus Share an Essential Role for Viral Replication. J. Virol., 91.","DOI":"10.1128\/JVI.01875-16"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"4118","DOI":"10.1128\/jvi.71.5.4118-4122.1997","article-title":"Herpesvirus saimiri encodes a functional homolog of the human Bcl-2 oncogene","volume":"71","author":"Nava","year":"1997","journal-title":"J. Virol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"5894","DOI":"10.1128\/jvi.71.8.5894-5904.1997","article-title":"Complete sequence and genomic analysis of murine \u03b3herpesvirus 68","volume":"71","author":"Virgin","year":"1997","journal-title":"J. Virol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1007\/s007050070030","article-title":"Murine \u03b3herpesvirus M11 gene product inhibits apoptosis and is expressed during virus persistence","volume":"145","author":"Roy","year":"2000","journal-title":"Arch. Virol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"989","DOI":"10.4161\/auto.6803","article-title":"Molecular basis of the regulation of Beclin 1-dependent autophagy by the \u03b3-herpesvirus 68 Bcl-2 homolog M11","volume":"4","author":"Sinha","year":"2008","journal-title":"Autophagy"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"12536","DOI":"10.1073\/pnas.96.22.12536","article-title":"A cytomegalovirus-encoded mitochondria-localized inhibitor of apoptosis structurally unrelated to Bcl-2","volume":"96","author":"Goldmacher","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_124","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_125","doi-asserted-by":"crossref","first-page":"6232","DOI":"10.1128\/JVI.02710-07","article-title":"Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins","volume":"82","author":"Norris","year":"2008","journal-title":"J. Virol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"20901","DOI":"10.1073\/pnas.1217094110","article-title":"Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA","volume":"109","author":"Ma","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1038\/cdd.2009.147","article-title":"Cytomegaloviruses inhibit Bak- and Bax-mediated apoptosis with two separate viral proteins","volume":"17","author":"Cam","year":"2010","journal-title":"Cell Death Differ."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/cdd.2008.152","article-title":"Virally mediated inhibition of Bax in leukocytes promotes dissemination of murine cytomegalovirus","volume":"16","author":"Manzur","year":"2009","journal-title":"Cell Death Differ."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1007\/s10495-008-0245-2","article-title":"The murine cytomegalovirus cell death suppressor m38.5 binds Bax and blocks Bax-mediated mitochondrial outer membrane permeabilization","volume":"13","author":"Arnoult","year":"2008","journal-title":"Apoptosis"},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Fleming, P., Kvansakul, M., Voigt, V., Kile, B.T., Kluck, R.M., Huang, D.C., Degli-Esposti, M.A., and Andoniou, C.E. (2013). MCMV-mediated inhibition of the pro-apoptotic Bak protein is required for optimal in vivo replication. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003192"},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"3592","DOI":"10.1128\/JVI.02657-12","article-title":"Viral inhibition of BAK promotes murine cytomegalovirus dissemination to salivary glands","volume":"87","author":"Handke","year":"2013","journal-title":"J. Virol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1101\/gad.13.6.718","article-title":"Role of Nr13 in regulation of programmed cell death in the bursa of Fabricius","volume":"13","author":"Lee","year":"1999","journal-title":"Genes Dev."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"12481","DOI":"10.1074\/jbc.C000871200","article-title":"Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak","volume":"276","author":"Ke","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"5846","DOI":"10.1038\/sj.onc.1204740","article-title":"Nrh, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor of apoptosis","volume":"20","author":"Aouacheria","year":"2001","journal-title":"Oncogene"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"e443","DOI":"10.1038\/cddis.2012.178","article-title":"The restricted binding repertoire of Bcl-B leaves Bim as the universal BH3-only prosurvival Bcl-2 protein antagonist","volume":"3","author":"Rautureau","year":"2012","journal-title":"Cell Death Dis."},{"key":"ref_136","first-page":"2181","article-title":"The structure of Boo\/Diva reveals a divergent Bcl-2 protein","volume":"78","author":"Rautureau","year":"2010","journal-title":"Proteins"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"519","DOI":"10.4161\/auto.5846","article-title":"An insight into the mechanistic role of Beclin 1 and its inhibition by prosurvival Bcl-2 family proteins","volume":"4","author":"Ku","year":"2008","journal-title":"Autophagy"},{"key":"ref_138","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_139","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.molcel.2004.12.030","article-title":"Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function","volume":"17","author":"Chen","year":"2005","journal-title":"Mol. Cell"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1016\/j.str.2008.02.009","article-title":"Structural plasticity underpins promiscuous binding of the prosurvival protein A1","volume":"16","author":"Smits","year":"2008","journal-title":"Structure"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.1101\/gad.1304105","article-title":"Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins","volume":"19","author":"Willis","year":"2005","journal-title":"Genes Dev."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"18081","DOI":"10.1073\/pnas.0808691105","article-title":"Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax","volume":"105","author":"Fletcher","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_143","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_144","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":"ref_145","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_146","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":"ref_147","doi-asserted-by":"crossref","first-page":"4695","DOI":"10.1074\/jbc.M109.053769","article-title":"Vaccinia virus F1L interacts with Bak using highly divergent Bcl-2 homology domains and replaces the function of Mcl-1","volume":"285","author":"Campbell","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_148","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":"ref_149","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_150","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_151","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_152","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1007\/s10495-009-0403-1","article-title":"The orf virus inhibitor of apoptosis functions in a Bcl-2-like manner, binding and neutralizing a set of BH3-only proteins and active Bax","volume":"14","author":"Westphal","year":"2009","journal-title":"Apoptosis"},{"key":"ref_153","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":"ref_154","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.1128\/jvi.67.7.4391-4394.1993","article-title":"An African swine fever virus gene with similarity to the proto-oncogene Bcl-2 and the Epstein-Barr virus gene BHRF1","volume":"67","author":"Neilan","year":"1993","journal-title":"J. Virol."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.virol.2008.01.050","article-title":"A179L, a viral Bcl-2 homologue, targets the core Bcl-2 apoptotic machinery and its upstream BH3 activators with selective binding restrictions for Bid and Noxa","volume":"375","author":"Galindo","year":"2008","journal-title":"Virology"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1007\/s10495-007-0152-y","article-title":"Iridovirus Bcl-2 protein inhibits apoptosis in the early stage of viral infection","volume":"13","author":"Lin","year":"2008","journal-title":"Apoptosis"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.cell.2005.07.002","article-title":"Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy","volume":"122","author":"Pattingre","year":"2005","journal-title":"Cell"},{"key":"ref_158","doi-asserted-by":"crossref","unstructured":"Piya, S., White, E.J., Klein, S.R., Jiang, H., McDonnell, T.J., Gomez-Manzano, C., and Fueyo, J. (2011). The E1B19K oncoprotein complexes with Beclin 1 to regulate autophagy in adenovirus-infected cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0029467"},{"key":"ref_159","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_160","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":"ref_161","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_162","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_163","doi-asserted-by":"crossref","unstructured":"De Motes, C.M., Cooray, S., Ren, H., Almeida, G.M.F., 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_164","doi-asserted-by":"crossref","first-page":"3749","DOI":"10.1074\/jbc.M113.512756","article-title":"Characterization and structure of the vaccinia virus NF-\u03baB antagonist A46","volume":"289","author":"Fedosyuk","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_165","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":"ref_166","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_167","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":"ref_168","doi-asserted-by":"crossref","unstructured":"Fedosyuk, S., Bezerra, G.A., Radakovics, K., Smith, T.K., Sammito, M., Bobik, N., Round, A., Ten Eyck, L.F., Djinovic-Carugo, K., and Uson, I. (2016). Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins. PLoS Pathog., 12.","DOI":"10.1371\/journal.ppat.1006079"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1016\/j.str.2009.09.005","article-title":"Structural basis for targeting of human RNA helicase DDX3 by poxvirus protein K7","volume":"17","author":"Oda","year":"2009","journal-title":"Structure"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1038\/emboj.2008.143","article-title":"Viral targeting of DEAD box protein 3 reveals its role in TBK1\/IKKepsilon-mediated IRF activation","volume":"27","author":"Schroder","year":"2008","journal-title":"EMBO J."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1083\/jcb.200905153","article-title":"The role of BH3-only protein Bim extends beyond inhibiting Bcl-2-like prosurvival proteins","volume":"186","author":"Merino","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"22605","DOI":"10.1074\/jbc.M308408200","article-title":"An anti-apoptotic viral protein that recruits Bax to mitochondria","volume":"279","author":"Poncet","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1038\/cdd.2008.14","article-title":"Viral pro-survival proteins block separate stages in Bax activation but changes in mitochondrial ultrastructure still occur","volume":"15","author":"Cross","year":"2008","journal-title":"Cell Death Differ."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"1401","DOI":"10.1038\/cdd.2017.59","article-title":"Viral hijacking of host caspases: An emerging category of pathogen-host interactions","volume":"24","author":"Connolly","year":"2017","journal-title":"Cell Death Differ."},{"key":"ref_175","first-page":"2356","article-title":"Human Cytomegalovirus Promotes Survival of Infected Monocytes via a Distinct Temporal Regulation of Cellular Bcl-2 Family Proteins","volume":"90","author":"Kim","year":"2015","journal-title":"J. Virol."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/9\/10\/290\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T18:46:39Z","timestamp":1760208399000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/9\/10\/290"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10,6]]},"references-count":175,"journal-issue":{"issue":"10","published-online":{"date-parts":[[2017,10]]}},"alternative-id":["v9100290"],"URL":"https:\/\/doi.org\/10.3390\/v9100290","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,10,6]]}}}