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Volumn 90, Issue 1, 2016, Pages 533-544

Baculovirus inhibitor-of-apoptosis op-IAP3 blocks apoptosis by interaction with and stabilization of a host insect cellular IAP

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; INHIBITOR OF APOPTOSIS PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN 3; UNCLASSIFIED DRUG; PROTEIN BINDING;

EID: 84953897903     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02320-15     Document Type: Article
Times cited : (37)

References (65)
  • 1
    • 68149157524 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins in Drosophila: gatekeepers of death
    • Orme M, Meier P. 2009. Inhibitor of apoptosis proteins in Drosophila: gatekeepers of death. Apoptosis 14:950-960. http://dx.doi.org/10.1007/s10495-009-0358-2.
    • (2009) Apoptosis , vol.14 , pp. 950-960
    • Orme, M.1    Meier, P.2
  • 2
    • 43049091895 scopus 로고    scopus 로고
    • IAPs: what's in a name?
    • Srinivasula SM, Ashwell JD. 2008. IAPs: what's in a name? Mol Cell 30:123-135. http://dx.doi.org/10.1016/j.molcel.2008.03.008.
    • (2008) Mol Cell , vol.30 , pp. 123-135
    • Srinivasula, S.M.1    Ashwell, J.D.2
  • 3
    • 59149097669 scopus 로고    scopus 로고
    • Diverse functions within the IAP family
    • Rumble JM, Duckett CS. 2008. Diverse functions within the IAP family. J Cell Sci 121:3505-3507. http://dx.doi.org/10.1242/jcs.040303.
    • (2008) J Cell Sci , vol.121 , pp. 3505-3507
    • Rumble, J.M.1    Duckett, C.S.2
  • 4
    • 77954930632 scopus 로고    scopus 로고
    • IAPs: from caspase inhibitors to modulators of NF-B, inflammation and cancer
    • Gyrd-Hansen M, Meier P. 2010. IAPs: from caspase inhibitors to modulators of NF-B, inflammation and cancer. Nat Rev Cancer 10:561-574. http://dx.doi.org/10.1038/nrc2889.
    • (2010) Nat Rev Cancer , vol.10 , pp. 561-574
    • Gyrd-Hansen, M.1    Meier, P.2
  • 5
    • 84928206139 scopus 로고    scopus 로고
    • Viral IAPs, then and now
    • Clem RJ. 2015. Viral IAPs, then and now. Semin Cell Dev Biol 39:72-79. http://dx.doi.org/10.1016/j.semcdb.2015.01.011.
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 72-79
    • Clem, R.J.1
  • 6
    • 53849136625 scopus 로고    scopus 로고
    • Viral subversion of apoptotic enzymes: escape from death row
    • Best SM. 2008. Viral subversion of apoptotic enzymes: escape from death row. Annu Rev Microbiol 62:171-192. http://dx.doi.org/10.1146/annurev.micro.62.081307.163009.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 171-192
    • Best, S.M.1
  • 7
    • 0028274132 scopus 로고
    • An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs
    • Birnbaum MJ, Clem RJ, Miller LK. 1994. An apoptosis-inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs. J Virol 68:2521-2528.
    • (1994) J Virol , vol.68 , pp. 2521-2528
    • Birnbaum, M.J.1    Clem, R.J.2    Miller, L.K.3
  • 8
    • 77957951305 scopus 로고    scopus 로고
    • Host insect inhibitor-ofapoptosis SfIAP functionally replaces baculovirus IAP but is differentially regulated by its N-terminal leader
    • Cerio RJ, Vandergaast R, Friesen PD. 2010. Host insect inhibitor-ofapoptosis SfIAP functionally replaces baculovirus IAP but is differentially regulated by its N-terminal leader. J Virol 84:11448-11460. http://dx.doi.org/10.1128/JVI.01311-10.
    • (2010) J Virol , vol.84 , pp. 11448-11460
    • Cerio, R.J.1    Vandergaast, R.2    Friesen, P.D.3
  • 9
    • 0034652154 scopus 로고    scopus 로고
    • Evolutionary conservation of apoptosis mechanisms: lepidopteran and baculoviral inhibitor of apoptosis proteins are inhibitors of mammalian caspase-9
    • Huang Q, Deveraux QL, Maeda S, Salvesen GS, Stennicke HR, Hammock BD, Reed JC. 2000. Evolutionary conservation of apoptosis mechanisms: lepidopteran and baculoviral inhibitor of apoptosis proteins are inhibitors of mammalian caspase-9. Proc Natl Acad Sci U S A 97:1427-1432. http://dx.doi.org/10.1073/pnas.97.4.1427.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 1427-1432
    • Huang, Q.1    Deveraux, Q.L.2    Maeda, S.3    Salvesen, G.S.4    Stennicke, H.R.5    Hammock, B.D.6    Reed, J.C.7
  • 10
    • 0029583176 scopus 로고
    • Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death
    • Hay BA, Wassarman DA, Rubin GM. 1995. Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death. Cell 83:1253-1262. http://dx.doi.org/10.1016/0092-8674(95)90150-7.
    • (1995) Cell , vol.83 , pp. 1253-1262
    • Hay, B.A.1    Wassarman, D.A.2    Rubin, G.M.3
  • 11
    • 0033961282 scopus 로고    scopus 로고
    • The BIR motifs mediate dominant interference and oligomerization of inhibitor of apoptosis Op-IAP
    • Hozak RR, Manji GA, Friesen PD. 2000. The BIR motifs mediate dominant interference and oligomerization of inhibitor of apoptosis Op-IAP. Mol Cell Biol 20:1877-1885. http://dx.doi.org/10.1128/MCB.20.5.1877-1885.2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 1877-1885
    • Hozak, R.R.1    Manji, G.A.2    Friesen, P.D.3
  • 12
    • 16844381868 scopus 로고    scopus 로고
    • The baculovirus anti-apoptotic protein Op-IAP does not inhibit Drosophila caspases or apoptosis in Drosophila S2 cells and instead sensitizes S2 cells to virusinduced apoptosis
    • Wright CW, Means JC, Penabaz T, Clem RJ. 2005. The baculovirus anti-apoptotic protein Op-IAP does not inhibit Drosophila caspases or apoptosis in Drosophila S2 cells and instead sensitizes S2 cells to virusinduced apoptosis. Virology 335:61-71. http://dx.doi.org/10.1016/j.virol.2005.02.007.
    • (2005) Virology , vol.335 , pp. 61-71
    • Wright, C.W.1    Means, J.C.2    Penabaz, T.3    Clem, R.J.4
  • 13
    • 0032545303 scopus 로고    scopus 로고
    • A mutational analysis of the baculovirus inhibitor of apoptosis Op-IAP
    • Vucic D, Kaiser WJ, Miller LK. 1998. A mutational analysis of the baculovirus inhibitor of apoptosis Op-IAP. J Biol Chem 273:33915-33921. http://dx.doi.org/10.1074/jbc.273.51.33915.
    • (1998) J Biol Chem , vol.273 , pp. 33915-33921
    • Vucic, D.1    Kaiser, W.J.2    Miller, L.K.3
  • 14
    • 0032573595 scopus 로고    scopus 로고
    • The Drosophila inhibitor of apoptosis D-IAP1 suppresses cell death induced by the caspase drICE
    • Kaiser WJ, Vucic D, Miller LK. 1998. The Drosophila inhibitor of apoptosis D-IAP1 suppresses cell death induced by the caspase drICE. FEBS Lett 440:243-248. http://dx.doi.org/10.1016/S0014-5793(98)01465-3.
    • (1998) FEBS Lett , vol.440 , pp. 243-248
    • Kaiser, W.J.1    Vucic, D.2    Miller, L.K.3
  • 15
    • 12344300349 scopus 로고    scopus 로고
    • IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms
    • Tenev T, Zachariou A, Wilson R, Ditzel M, Meier P. 2005. IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms. Nat Cell Biol 7:70-77. http://dx.doi.org/10.1038/ncb1204.
    • (2005) Nat Cell Biol , vol.7 , pp. 70-77
    • Tenev, T.1    Zachariou, A.2    Wilson, R.3    Ditzel, M.4    Meier, P.5
  • 16
    • 53249133039 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins in eukaryotic evolution and development: a model of thematic conservation
    • O'Riordan MX, Bauler LD, Scott FL, Duckett CS. 2008. Inhibitor of apoptosis proteins in eukaryotic evolution and development: a model of thematic conservation. Dev Cell 15:497-508. http://dx.doi.org/10.1016/j.devcel.2008.09.012.
    • (2008) Dev Cell , vol.15 , pp. 497-508
    • O'Riordan, M.X.1    Bauler, L.D.2    Scott, F.L.3    Duckett, C.S.4
  • 17
    • 77449084943 scopus 로고    scopus 로고
    • Assembling the building blocks: structure and function of inhibitor of apoptosis proteins
    • Mace PD, Shirley S, Day CL. 2010. Assembling the building blocks: structure and function of inhibitor of apoptosis proteins. Cell Death Differ 17:46-53. http://dx.doi.org/10.1038/cdd.2009.45.
    • (2010) Cell Death Differ , vol.17 , pp. 46-53
    • Mace, P.D.1    Shirley, S.2    Day, C.L.3
  • 18
    • 33749415123 scopus 로고    scopus 로고
    • Caspase-dependent cell death in Drosophila
    • Hay BA, Guo M. 2006. Caspase-dependent cell death in Drosophila. Annu Rev Cell Dev Biol 22:623-650. http://dx.doi.org/10.1146/annurev.cellbio.21.012804.093845.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 623-650
    • Hay, B.A.1    Guo, M.2
  • 19
    • 84905014915 scopus 로고    scopus 로고
    • IAP family of cell death and signaling regulators
    • Silke J, Vucic D. 2014. IAP family of cell death and signaling regulators. Methods Enzymol 545:35-65. http://dx.doi.org/10.1016/B978-0-12-801430-1.00002-0.
    • (2014) Methods Enzymol , vol.545 , pp. 35-65
    • Silke, J.1    Vucic, D.2
  • 20
    • 10944247878 scopus 로고    scopus 로고
    • Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs). A caspase-independent mechanism for apoptotic inhibition
    • Wilkinson JC, Wilkinson AS, Scott FL, Csomos RA, Salvesen GS, Duckett CS. 2004. Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs). A caspase-independent mechanism for apoptotic inhibition. J Biol Chem 279:51082-51090.
    • (2004) J Biol Chem , vol.279 , pp. 51082-51090
    • Wilkinson, J.C.1    Wilkinson, A.S.2    Scott, F.L.3    Csomos, R.A.4    Salvesen, G.S.5    Duckett, C.S.6
  • 21
    • 34248999834 scopus 로고    scopus 로고
    • The antiapoptotic activity of insect IAPs requires activation by an evolutionarily conserved mechanism
    • Tenev T, Ditzel M, Zachariou A, Meier P. 2007. The antiapoptotic activity of insect IAPs requires activation by an evolutionarily conserved mechanism. Cell Death Differ 14:1191-1201. http://dx.doi.org/10.1038/sj.cdd.4402118.
    • (2007) Cell Death Differ , vol.14 , pp. 1191-1201
    • Tenev, T.1    Ditzel, M.2    Zachariou, A.3    Meier, P.4
  • 22
    • 0346668315 scopus 로고    scopus 로고
    • The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC
    • Muro I, Hay BA, Clem RJ. 2002. The Drosophila DIAP1 protein is required to prevent accumulation of a continuously generated, processed form of the apical caspase DRONC. J Biol Chem 277:49644-49650. http://dx.doi.org/10.1074/jbc. M203464200.
    • (2002) J Biol Chem , vol.277 , pp. 49644-49650
    • Muro, I.1    Hay, B.A.2    Clem, R.J.3
  • 23
    • 38349142832 scopus 로고    scopus 로고
    • Flock house virus induces apoptosis by depletion of Drosophila inhibitor-of-apoptosis protein DIAP1
    • Settles EW, Friesen PD. 2008. Flock house virus induces apoptosis by depletion of Drosophila inhibitor-of-apoptosis protein DIAP1. J Virol 82: 1378-1388. http://dx.doi.org/10.1128/JVI.01941-07.
    • (2008) J Virol , vol.82 , pp. 1378-1388
    • Settles, E.W.1    Friesen, P.D.2
  • 24
    • 0037128923 scopus 로고    scopus 로고
    • The role of ARK in stress-induced apoptosis in Drosophila cells
    • Zimmermann KC, Ricci JE, Droin NM, Green DR. 2002. The role of ARK in stress-induced apoptosis in Drosophila cells. J Cell Biol 156:1077-1087. http://dx.doi.org/10.1083/jcb.20112068.
    • (2002) J Cell Biol , vol.156 , pp. 1077-1087
    • Zimmermann, K.C.1    Ricci, J.E.2    Droin, N.M.3    Green, D.R.4
  • 25
    • 79951581436 scopus 로고    scopus 로고
    • Defining the core apoptosis pathway in the mosquito disease vector Aedes aegypti: the roles of iap1, ark, dronc, and effector caspases
    • Liu Q, Clem RJ. 2011. Defining the core apoptosis pathway in the mosquito disease vector Aedes aegypti: the roles of iap1, ark, dronc, and effector caspases. Apoptosis 16:105-113. http://dx.doi.org/10.1007/s10495-010-0558-9.
    • (2011) Apoptosis , vol.16 , pp. 105-113
    • Liu, Q.1    Clem, R.J.2
  • 26
    • 79961185947 scopus 로고    scopus 로고
    • Active depletion of host cell inhibitor-of-apoptosis proteins triggers apoptosis upon baculovirus DNA replication
    • Vandergaast R, Schultz KL, Cerio RJ, Friesen PD. 2011. Active depletion of host cell inhibitor-of-apoptosis proteins triggers apoptosis upon baculovirus DNA replication. J Virol 85:8348-8358. http://dx.doi.org/10.1128/JVI.00667-11.
    • (2011) J Virol , vol.85 , pp. 8348-8358
    • Vandergaast, R.1    Schultz, K.L.2    Cerio, R.J.3    Friesen, P.D.4
  • 27
    • 84925400639 scopus 로고    scopus 로고
    • Insect inhibitor-of-apoptosis (IAP) proteins are negatively regulated by signalinduced N-terminal degrons absent within viral IAP proteins
    • Vandergaast R, Mitchell JK, Byers NM, Friesen PD. 2015. Insect inhibitor-of-apoptosis (IAP) proteins are negatively regulated by signalinduced N-terminal degrons absent within viral IAP proteins. J Virol 89: 4481-4493. http://dx.doi.org/10.1128/JVI.03659-14.
    • (2015) J Virol , vol.89 , pp. 4481-4493
    • Vandergaast, R.1    Mitchell, J.K.2    Byers, N.M.3    Friesen, P.D.4
  • 28
    • 0034737292 scopus 로고    scopus 로고
    • Drosophila p53 binds a damage response element at the reaper locus
    • Brodsky MH, Nordstrom W, Tsang G, Kwan E, Rubin GM, Abrams JM. 2000. Drosophila p53 binds a damage response element at the reaper locus. Cell 101:103-113. http://dx.doi.org/10.1016/S0092-8674(00)80627-3.
    • (2000) Cell , vol.101 , pp. 103-113
    • Brodsky, M.H.1    Nordstrom, W.2    Tsang, G.3    Kwan, E.4    Rubin, G.M.5    Abrams, J.M.6
  • 29
    • 0036300083 scopus 로고    scopus 로고
    • Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1
    • Ryoo HD, Bergmann A, Gonen H, Ciechanover A, Steller H. 2002. Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1. Nat Cell Biol 4:432-438. http://dx.doi.org/10.1038/ncb795.
    • (2002) Nat Cell Biol , vol.4 , pp. 432-438
    • Ryoo, H.D.1    Bergmann, A.2    Gonen, H.3    Ciechanover, A.4    Steller, H.5
  • 30
    • 33947384611 scopus 로고    scopus 로고
    • Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways
    • Herman-Bachinsky Y, Ryoo HD, Ciechanover A, Gonen H. 2007. Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Cell Death Differ 14:861-871. http://dx.doi.org/10.1038/sj.cdd.4402079.
    • (2007) Cell Death Differ , vol.14 , pp. 861-871
    • Herman-Bachinsky, Y.1    Ryoo, H.D.2    Ciechanover, A.3    Gonen, H.4
  • 31
    • 33746570157 scopus 로고    scopus 로고
    • Drosophila IKK-related kinase regulates nonapoptotic function of caspases via degradation of IAPs
    • Kuranaga E, Kanuka H, Tonoki A, Takemoto K, Tomioka T, Kobayashi M, Hayashi S, Miura M. 2006. Drosophila IKK-related kinase regulates nonapoptotic function of caspases via degradation of IAPs. Cell 126:583-596. http://dx.doi.org/10.1016/j.cell.2006.05.048.
    • (2006) Cell , vol.126 , pp. 583-596
    • Kuranaga, E.1    Kanuka, H.2    Tonoki, A.3    Takemoto, K.4    Tomioka, T.5    Kobayashi, M.6    Hayashi, S.7    Miura, M.8
  • 32
    • 17144377113 scopus 로고    scopus 로고
    • IAPs, RINGs and ubiquitylation
    • Vaux DL, Silke J. 2005. IAPs, RINGs and ubiquitylation. Nat Rev Mol Cell Biol 6:287-297. http://dx.doi.org/10.1038/nrm1621.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 287-297
    • Vaux, D.L.1    Silke, J.2
  • 33
    • 84928203429 scopus 로고    scopus 로고
    • IAPs: modular regulators of cell signalling
    • Budhidarmo R, Day CL. 2015. IAPs: modular regulators of cell signalling. Semin Cell Dev Biol 39:80-90. http://dx.doi.org/10.1016/j.semcdb.2014.12.002.
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 80-90
    • Budhidarmo, R.1    Day, C.L.2
  • 34
    • 0031470626 scopus 로고    scopus 로고
    • Baculovirus inhibitors of apoptosis (IAPs) block activation of Sf-caspase-1
    • Seshagiri S, Miller LK. 1997. Baculovirus inhibitors of apoptosis (IAPs) block activation of Sf-caspase-1. Proc Natl Acad Sci U S A 94:13606-13611. http://dx.doi.org/10.1073/pnas.94.25.13606.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 13606-13611
    • Seshagiri, S.1    Miller, L.K.2
  • 35
    • 0030925639 scopus 로고    scopus 로고
    • Baculovirus inhibitor of apoptosis functions at or upstream of the apoptotic suppressor P35 to prevent programmed cell death
    • Manji GA, Hozak RR, LaCount DJ, Friesen PD. 1997. Baculovirus inhibitor of apoptosis functions at or upstream of the apoptotic suppressor P35 to prevent programmed cell death. J Virol 71:4509-4516.
    • (1997) J Virol , vol.71 , pp. 4509-4516
    • Manji, G.A.1    Hozak, R.R.2    LaCount, D.J.3    Friesen, P.D.4
  • 36
    • 0034717139 scopus 로고    scopus 로고
    • Caspase inhibitor P35 and inhibitor of apoptosis Op-IAP block in vivo proteolytic activation of an effector caspase at different steps
    • LaCount DJ, Hanson SF, Schneider CL, Friesen PD. 2000. Caspase inhibitor P35 and inhibitor of apoptosis Op-IAP block in vivo proteolytic activation of an effector caspase at different steps. J Biol Chem 275:15657-15664. http://dx.doi.org/10.1074/jbc. M000791200.
    • (2000) J Biol Chem , vol.275 , pp. 15657-15664
    • LaCount, D.J.1    Hanson, S.F.2    Schneider, C.L.3    Friesen, P.D.4
  • 37
    • 85047278700 scopus 로고    scopus 로고
    • Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo
    • Zoog SJ, Schiller JJ, Wetter JA, Chejanovsky N, Friesen PD. 2002. Baculovirus apoptotic suppressor P49 is a substrate inhibitor of initiator caspases resistant to P35 in vivo. EMBO J 21:5130-5140. http://dx.doi.org/10.1038/sj.emboj.7594736.
    • (2002) EMBO J , vol.21 , pp. 5130-5140
    • Zoog, S.J.1    Schiller, J.J.2    Wetter, J.A.3    Chejanovsky, N.4    Friesen, P.D.5
  • 38
    • 0030928651 scopus 로고    scopus 로고
    • Inhibition of Reaperinduced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs)
    • Vucic D, Kaiser WJ, Harvey AJ, Miller LK. 1997. Inhibition of Reaperinduced apoptosis by interaction with inhibitor of apoptosis proteins (IAPs). Proc Natl Acad Sci U S A 94:10183-10188. http://dx.doi.org/10.1073/pnas.94.19.10183.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 10183-10188
    • Vucic, D.1    Kaiser, W.J.2    Harvey, A.J.3    Miller, L.K.4
  • 39
    • 0031815071 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM
    • Vucic D, Kaiser WJ, Miller LK. 1998. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM. Mol Cell Biol 18:3300-3309. http://dx.doi.org/10.1128/MCB.18.6.3300.
    • (1998) Mol Cell Biol , vol.18 , pp. 3300-3309
    • Vucic, D.1    Kaiser, W.J.2    Miller, L.K.3
  • 40
    • 0037169556 scopus 로고    scopus 로고
    • Sequence requirements for Hid binding and apoptosis regulation in the baculovirus inhibitor of apoptosis Op-IAP. Hid binds Op-IAP in a manner similar to Smac binding of XIAP
    • Wright CW, Clem RJ. 2002. Sequence requirements for Hid binding and apoptosis regulation in the baculovirus inhibitor of apoptosis Op-IAP. Hid binds Op-IAP in a manner similar to Smac binding of XIAP. J Biol Chem 277:2454-2462.
    • (2002) J Biol Chem , vol.277 , pp. 2454-2462
    • Wright, C.W.1    Clem, R.J.2
  • 41
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
    • Vaughn JL, Goodwin RH, Tompkins GJ, McCawley P. 1977. The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae). In Vitro 13:213-217. http://dx.doi.org/10.1007/BF02615077.
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 42
    • 0015328565 scopus 로고
    • Cell lines derived from late embryonic stages of Drosophila melanogaster
    • Schneider I. 1972. Cell lines derived from late embryonic stages of Drosophila melanogaster. J Embryol Exp Morphol 27:353-365.
    • (1972) J Embryol Exp Morphol , vol.27 , pp. 353-365
    • Schneider, I.1
  • 43
    • 0026800707 scopus 로고
    • Site-specific mutagenesis of the 35-kilodalton protein gene encoded by Autographa californica nuclear polyhedrosis virus: cell line-specific effects on virus replication
    • Hershberger PA, Dickson JA, Friesen PD. 1992. Site-specific mutagenesis of the 35-kilodalton protein gene encoded by Autographa californica nuclear polyhedrosis virus: cell line-specific effects on virus replication. J Virol 66:5525-5533.
    • (1992) J Virol , vol.66 , pp. 5525-5533
    • Hershberger, P.A.1    Dickson, J.A.2    Friesen, P.D.3
  • 44
    • 34548171631 scopus 로고    scopus 로고
    • Baculovirus caspase inhibitors P49 and P35 block virus-induced apoptosis downstream of effector caspase DrICE activation in Drosophila melanogaster cells
    • Lannan E, Vandergaast R, Friesen PD. 2007. Baculovirus caspase inhibitors P49 and P35 block virus-induced apoptosis downstream of effector caspase DrICE activation in Drosophila melanogaster cells. J Virol 81: 9319-9330. http://dx.doi.org/10.1128/JVI.00247-07.
    • (2007) J Virol , vol.81 , pp. 9319-9330
    • Lannan, E.1    Vandergaast, R.2    Friesen, P.D.3
  • 45
    • 84887162177 scopus 로고    scopus 로고
    • Baculovirus F-box protein LEF-7 modifies the host DNA damage response to enhance virus multiplication
    • Mitchell JK, Byers NM, Friesen PD. 2013. Baculovirus F-box protein LEF-7 modifies the host DNA damage response to enhance virus multiplication. J Virol 87:12592-12599. http://dx.doi.org/10.1128/JVI.02501-13.
    • (2013) J Virol , vol.87 , pp. 12592-12599
    • Mitchell, J.K.1    Byers, N.M.2    Friesen, P.D.3
  • 46
    • 0028096991 scopus 로고
    • Suppression of apoptosis in insect cells stably transfected with baculovirus p35: dominant interference by N-terminal sequences p35(1-76)
    • Cartier JL, Hershberger PA, Friesen PD. 1994. Suppression of apoptosis in insect cells stably transfected with baculovirus p35: dominant interference by N-terminal sequences p35(1-76). J Virol 68:7728-7737.
    • (1994) J Virol , vol.68 , pp. 7728-7737
    • Cartier, J.L.1    Hershberger, P.A.2    Friesen, P.D.3
  • 47
    • 47749123009 scopus 로고    scopus 로고
    • Reactive-site cleavage residues confer target specificity to baculovirus P49, a dimeric member of the P35 family of caspase inhibitors
    • Guy MP, Friesen PD. 2008. Reactive-site cleavage residues confer target specificity to baculovirus P49, a dimeric member of the P35 family of caspase inhibitors. J Virol 82:7504-7514. http://dx.doi.org/10.1128/JVI.00231-08.
    • (2008) J Virol , vol.82 , pp. 7504-7514
    • Guy, M.P.1    Friesen, P.D.2
  • 49
    • 0034979112 scopus 로고    scopus 로고
    • Oligomerization mediated by a helix-loop-helix-like domain of baculovirus IE1 is required for early promoter transactivation
    • Olson VA, Wetter JA, Friesen PD. 2001. Oligomerization mediated by a helix-loop-helix-like domain of baculovirus IE1 is required for early promoter transactivation. J Virol 75:6042-6051. http://dx.doi.org/10.1128/JVI.75.13.6042-6051.2001.
    • (2001) J Virol , vol.75 , pp. 6042-6051
    • Olson, V.A.1    Wetter, J.A.2    Friesen, P.D.3
  • 50
    • 58149384479 scopus 로고    scopus 로고
    • Transactivator IE1 is required for baculovirus early replication events that trigger apoptosis in permissive and nonpermissive cells
    • Schultz KL, Wetter JA, Fiore DC, Friesen PD. 2009. Transactivator IE1 is required for baculovirus early replication events that trigger apoptosis in permissive and nonpermissive cells. J Virol 83:262-272. http://dx.doi.org/10.1128/JVI.01827-08.
    • (2009) J Virol , vol.83 , pp. 262-272
    • Schultz, K.L.1    Wetter, J.A.2    Fiore, D.C.3    Friesen, P.D.4
  • 51
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: a hub for protein information
    • UniProt Consortium. 2015. UniProt: a hub for protein information. Nucleic Acids Res 43:D204-D212. http://dx.doi.org/10.1093/nar/gku989.
    • (2015) Nucleic Acids Res , vol.43 , pp. D204-D212
  • 52
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. 2013. MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30: 2725-2729. http://dx.doi.org/10.1093/molbev/mst197.
    • (2013) Mol Biol Evol , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 53
    • 79961196239 scopus 로고    scopus 로고
    • Structural mechanisms of DIAP1 autoinhibition and DIAP1-mediated inhibition of drICE
    • Li X, Wang J, Shi Y. 2011. Structural mechanisms of DIAP1 autoinhibition and DIAP1-mediated inhibition of drICE. Nat Commun 2:408. http://dx.doi.org/10.1038/ncomms1418.
    • (2011) Nat Commun , vol.2 , pp. 408
    • Li, X.1    Wang, J.2    Shi, Y.3
  • 55
    • 0031021919 scopus 로고    scopus 로고
    • Spodoptera frugiperda caspase-1, a novel insect death protease that cleaves the nuclear immunophilin FKBP46, is the target of the baculovirus antiapoptotic protein P35
    • Ahmad M, Srinivasula SM, Wang L, Litwack G, Fernandes-Alnemri T, Alnemri ES. 1997. Spodoptera frugiperda caspase-1, a novel insect death protease that cleaves the nuclear immunophilin FKBP46, is the target of the baculovirus antiapoptotic protein P35. J Biol Chem 272:1421-1424. http://dx.doi.org/10.1074/jbc.272.3.1421.
    • (1997) J Biol Chem , vol.272 , pp. 1421-1424
    • Ahmad, M.1    Srinivasula, S.M.2    Wang, L.3    Litwack, G.4    Fernandes-Alnemri, T.5    Alnemri, E.S.6
  • 56
    • 84875331026 scopus 로고    scopus 로고
    • SfDronc, an initiator caspase involved in apoptosis in the fall armyworm Spodoptera frugiperda
    • Huang N, Civciristov S, Hawkins CJ, Clem RJ. 2013. SfDronc, an initiator caspase involved in apoptosis in the fall armyworm Spodoptera frugiperda. Insect Biochem Mol Biol 43:444-454. http://dx.doi.org/10.1016/j.ibmb.2013.02.005.
    • (2013) Insect Biochem Mol Biol , vol.43 , pp. 444-454
    • Huang, N.1    Civciristov, S.2    Hawkins, C.J.3    Clem, R.J.4
  • 57
    • 0037936841 scopus 로고    scopus 로고
    • Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis
    • Ditzel M, Wilson R, Tenev T, Zachariou A, Paul A, Deas E, Meier P. 2003. Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis. Nat Cell Biol 5:467-473. http://dx.doi.org/10.1038/ncb984.
    • (2003) Nat Cell Biol , vol.5 , pp. 467-473
    • Ditzel, M.1    Wilson, R.2    Tenev, T.3    Zachariou, A.4    Paul, A.5    Deas, E.6    Meier, P.7
  • 58
    • 84928211026 scopus 로고    scopus 로고
    • Survivin-the inconvenient IAP
    • Altieri DC. 2015. Survivin-the inconvenient IAP. Semin Cell Dev Biol 39:91-96. http://dx.doi.org/10.1016/j.semcdb.2014.12.007.
    • (2015) Semin Cell Dev Biol , vol.39 , pp. 91-96
    • Altieri, D.C.1
  • 59
    • 21444436375 scopus 로고    scopus 로고
    • Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells
    • Muro I, Means JC, Clem RJ. 2005. Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells. J Biol Chem 280:18683-18688. http://dx.doi.org/10.1074/jbc. M501206200.
    • (2005) J Biol Chem , vol.280 , pp. 18683-18688
    • Muro, I.1    Means, J.C.2    Clem, R.J.3
  • 61
    • 16244377737 scopus 로고    scopus 로고
    • Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo
    • Conze DB, Albert L, Ferrick DA, Goeddel DV, Yeh WC, Mak T, Ashwell JD. 2005. Posttranscriptional downregulation of c-IAP2 by the ubiquitin protein ligase c-IAP1 in vivo. Mol Cell Biol 25:3348-3356. http://dx.doi.org/10.1128/MCB.25.8.3348-3356.2005.
    • (2005) Mol Cell Biol , vol.25 , pp. 3348-3356
    • Conze, D.B.1    Albert, L.2    Ferrick, D.A.3    Goeddel, D.V.4    Yeh, W.C.5    Mak, T.6    Ashwell, J.D.7
  • 62
    • 51349130944 scopus 로고    scopus 로고
    • The RING domain of cIAP1 mediates the degradation of RING-bearing inhibitor of apoptosis proteins by distinct pathways
    • Cheung HH, Plenchette S, Kern CJ, Mahoney DJ, Korneluk RG. 2008. The RING domain of cIAP1 mediates the degradation of RING-bearing inhibitor of apoptosis proteins by distinct pathways. Mol Biol Cell 19: 2729-2740. http://dx.doi.org/10.1091/mbc. E08-01-0107.
    • (2008) Mol Biol Cell , vol.19 , pp. 2729-2740
    • Cheung, H.H.1    Plenchette, S.2    Kern, C.J.3    Mahoney, D.J.4    Korneluk, R.G.5
  • 63
    • 28044469866 scopus 로고    scopus 로고
    • Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance
    • Silke J, Kratina T, Chu D, Ekert PG, Day CL, Pakusch M, Huang DC, Vaux DL. 2005. Determination of cell survival by RING-mediated regulation of inhibitor of apoptosis (IAP) protein abundance. Proc Natl Acad Sci U S A 102:16182-16187. http://dx.doi.org/10.1073/pnas.0502828102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16182-16187
    • Silke, J.1    Kratina, T.2    Chu, D.3    Ekert, P.G.4    Day, C.L.5    Pakusch, M.6    Huang, D.C.7    Vaux, D.L.8
  • 64
    • 0036809813 scopus 로고    scopus 로고
    • IAP degradation: decisive blow or altruistic sacrifice?
    • Ditzel M, Meier P. 2002. IAP degradation: decisive blow or altruistic sacrifice? Trends Cell Biol 12:449-452. http://dx.doi.org/10.1016/S0962-8924(02)02366-8.
    • (2002) Trends Cell Biol , vol.12 , pp. 449-452
    • Ditzel, M.1    Meier, P.2
  • 65
    • 8444240738 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of the antiapoptotic baculovirus protein Op-IAP3
    • Green MC, Monser KP, Clem RJ. 2004. Ubiquitin protein ligase activity of the antiapoptotic baculovirus protein Op-IAP3. Virus Res 105:89-96. http://dx.doi.org/10.1016/j.virusres.2004.04.017.
    • (2004) Virus Res , vol.105 , pp. 89-96
    • Green, M.C.1    Monser, K.P.2    Clem, R.J.3


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