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Volumn 88, Issue 9, 2014, Pages 4853-4865

Ectromelia virus encodes a BTB/kelch protein, EVM150, that inhibits NF-κB signaling

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN; CULLIN 3; EVM150 PROTEIN; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; INTERLEUKIN 1BETA; SMALL INTERFERING RNA; STAT3 PROTEIN; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84897494376     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02923-13     Document Type: Article
Times cited : (23)

References (71)
  • 1
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden MS, Ghosh S. 2008. Shared principles in NF-κB signaling. Cell 132:344-362. http://dx.doi.org/10.1016/j.cell.2008.01.020.
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 2
    • 33750435582 scopus 로고    scopus 로고
    • NF-κB and the immune response
    • Hayden MS, West AP, Ghosh S. 2006. NF-κB and the immune response. Oncogene 25:6758-6780. http://dx.doi.org/10.1038/sj.onc.1209943.
    • (2006) Oncogene , vol.25 , pp. 6758-6780
    • Hayden, M.S.1    West, A.P.2    Ghosh, S.3
  • 3
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-κB transcription factors in the immune system
    • Vallabhapurapu S, Karin M. 2009. Regulation and function of NF-κB transcription factors in the immune system. Annu. Rev. Immunol. 27: 693-733. http://dx.doi.org/10.1146/annurev.immunol.021908.132641.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 6
    • 0023724778 scopus 로고
    • IκB: a specific inhibitor of the NF-κBtranscription factor
    • Baeuerle PA, Baltimore D. 1988. IκB: a specific inhibitor of the NF-κBtranscription factor. Science 242:540-546. http://dx.doi.org/10.1126/science.3140380.
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 7
    • 84856641109 scopus 로고    scopus 로고
    • NF-κB, the first quarter-century: remarkable progress and outstanding questions
    • Hayden MS, Ghosh S. 2012. NF-κB, the first quarter-century: remarkable progress and outstanding questions. Genes Dev. 26:203-234. http://dx.doi.org/10.1101/gad.183434.111.
    • (2012) Genes Dev. , vol.26 , pp. 203-234
    • Hayden, M.S.1    Ghosh, S.2
  • 8
    • 33750448661 scopus 로고    scopus 로고
    • Transcriptional regulation via the NF-κB signaling module
    • Hoffmann A, Natoli G, Ghosh G. 2006. Transcriptional regulation via the NF-κB signaling module. Oncogene 25:6706-6716. http://dx.doi.org/10.1038/sj.onc.1209933.
    • (2006) Oncogene , vol.25 , pp. 6706-6716
    • Hoffmann, A.1    Natoli, G.2    Ghosh, G.3
  • 9
    • 0028978032 scopus 로고
    • Phosphorylation of human IκB-alpha on serines 32 and 36 controls IκBαproteolysis and NF-κB activation in response to diverse stimuli
    • Traenckner EB, Pahl HL, Henkel T, Schmidt KN, Wilk S, Baeuerle PA. 1995. Phosphorylation of human IκB-alpha on serines 32 and 36 controls IκBαproteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:2876-2883.
    • (1995) EMBO J. , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 10
    • 0037689535 scopus 로고    scopus 로고
    • Poxvirus immunomodulatory strategies: current perspectives
    • Johnston JB, McFadden G. 2003. Poxvirus immunomodulatory strategies: current perspectives. J. Virol. 77:6093-6100. http://dx.doi.org/10.1128/JVI.77.11.6093-6100.2003.
    • (2003) J. Virol. , vol.77 , pp. 6093-6100
    • Johnston, J.B.1    McFadden, G.2
  • 11
    • 70349918182 scopus 로고    scopus 로고
    • NF-κB inhibitors: strategies from poxviruses
    • Mohamed MR, McFadden G. 2009. NF-κB inhibitors: strategies from poxviruses. Cell Cycle 8:3125-3132. http://dx.doi.org/10.4161/cc.8.19.9683.
    • (2009) Cell Cycle , vol.8 , pp. 3125-3132
    • Mohamed, M.R.1    McFadden, G.2
  • 15
    • 79959932581 scopus 로고    scopus 로고
    • Tumor necrosis factor inhibitors from poxviruses with an emphasis on tanapoxvirus-2L protein
    • Jeng D, Rahman MM, McFadden G, Essani K. 2011. Tumor necrosis factor inhibitors from poxviruses with an emphasis on tanapoxvirus-2L protein. Recent Patterns DNA Gene Seq. 5:97-103. http://dx.doi.org/10.2174/187221511796392033.
    • (2011) Recent Patterns DNA Gene Seq. , vol.5 , pp. 97-103
    • Jeng, D.1    Rahman, M.M.2    McFadden, G.3    Essani, K.4
  • 16
    • 33748511011 scopus 로고    scopus 로고
    • Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death
    • Sedger LM, Osvath SR, Xu XM, Li G, Chan FK, Barrett JW, McFadden G. 2006. Poxvirus tumor necrosis factor receptor (TNFR)-like T2 proteins contain a conserved preligand assembly domain that inhibits cellular TNFR1-induced cell death. J. Virol. 80:9300-9309. http://dx.doi.org/10.1128/JVI.02449-05.
    • (2006) J. Virol. , vol.80 , pp. 9300-9309
    • Sedger, L.M.1    Osvath, S.R.2    Xu, X.M.3    Li, G.4    Chan, F.K.5    Barrett, J.W.6    McFadden, G.7
  • 17
    • 0026646637 scopus 로고
    • A soluble receptor for interleukin-1β encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection
    • Alcami A, Smith GL. 1992. A soluble receptor for interleukin-1β encoded by vaccinia virus: a novel mechanism of virus modulation of the host response to infection. Cell 71:153-167. http://dx.doi.org/10.1016/0092-8674(92)90274-G.
    • (1992) Cell , vol.71 , pp. 153-167
    • Alcami, A.1    Smith, G.L.2
  • 18
    • 0034730146 scopus 로고    scopus 로고
    • A46R and A52R from vaccinia virus are antagonists of host IL-1 and Toll-like receptor signaling
    • Bowie A, Kiss-Toth E, Symons JA, Smith GL, Dower SK, O'Neill LA. 2000. A46R and A52R from vaccinia virus are antagonists of host IL-1 and Toll-like receptor signaling. Proc. Natl. Acad. Sci. U. S. A. 97:10162-10167. http://dx.doi.org/10.1073/pnas.160027697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 10162-10167
    • Bowie, A.1    Kiss-Toth, E.2    Symons, J.A.3    Smith, G.L.4    Dower, S.K.5    O'Neill, L.A.6
  • 20
    • 30344457034 scopus 로고    scopus 로고
    • The MC160 protein expressed by the dermatotropic poxvirus molluscum contagiosum virus prevents tumor necrosis factor alpha-induced NF-κB activation via inhibition of I kappa kinase complex formation
    • Nichols DB, Shisler JL. 2006. The MC160 protein expressed by the dermatotropic poxvirus molluscum contagiosum virus prevents tumor necrosis factor alpha-induced NF-κB activation via inhibition of I kappa kinase complex formation. J. Virol. 80:578-586. http://dx.doi.org/10.1128/JVI.80.2.578-586.2006.
    • (2006) J. Virol. , vol.80 , pp. 578-586
    • Nichols, D.B.1    Shisler, J.L.2
  • 21
    • 63149089887 scopus 로고    scopus 로고
    • Poxvirus MC160 protein utilizes multiple mechanisms to inhibit NF-κB activation mediated via components of the tumor necrosis factor receptor 1 signal transduction pathway
    • Nichols DB, Shisler JL. 2009. Poxvirus MC160 protein utilizes multiple mechanisms to inhibit NF-κB activation mediated via components of the tumor necrosis factor receptor 1 signal transduction pathway. J. Virol. 83:3162-3174. http://dx.doi.org/10.1128/JVI.02009-08.
    • (2009) J. Virol. , vol.83 , pp. 3162-3174
    • Nichols, D.B.1    Shisler, J.L.2
  • 22
    • 40349085775 scopus 로고    scopus 로고
    • Inhibition of IκB kinase by vaccinia virus virulence factor B14
    • Chen RA, Ryzhakov G, Cooray S, Randow F, Smith GL. 2008. Inhibition of IκB kinase by vaccinia virus virulence factor B14. PLoS Pathog. 4:e22. http://dx.doi.org/10.1371/journal.ppat.0040022.
    • (2008) PLoS Pathog. , vol.4
    • Chen, R.A.1    Ryzhakov, G.2    Cooray, S.3    Randow, F.4    Smith, G.L.5
  • 23
    • 1842614361 scopus 로고    scopus 로고
    • The vaccinia virus K1L gene product inhibits host NF-κB activation by preventing IκBα degradation
    • Shisler JL, Jin XL. 2004. The vaccinia virus K1L gene product inhibits host NF-κB activation by preventing IκBα degradation. J. Virol. 78:3553-3560. http://dx.doi.org/10.1128/JVI.78.7.3553-3560.2004.
    • (2004) J. Virol. , vol.78 , pp. 3553-3560
    • Shisler, J.L.1    Jin, X.L.2
  • 24
    • 66149101255 scopus 로고    scopus 로고
    • Poxvirus host range protein CP77 contains an F-box-like domain that is necessary to suppress NF-κB activation by tumor necrosis factor alpha but is independent of its host range function
    • Chang SJ, Hsiao JC, Sonnberg S, Chiang CT, Yang MH, Tzou DL, Mercer AA, Chang W. 2009. Poxvirus host range protein CP77 contains an F-box-like domain that is necessary to suppress NF-κB activation by tumor necrosis factor alpha but is independent of its host range function. J. Virol. 83:4140-4152. http://dx.doi.org/10.1128/JVI.01835-08.
    • (2009) J. Virol. , vol.83 , pp. 4140-4152
    • Chang, S.J.1    Hsiao, J.C.2    Sonnberg, S.3    Chiang, C.T.4    Yang, M.H.5    Tzou, D.L.6    Mercer, A.A.7    Chang, W.8
  • 26
    • 69449103056 scopus 로고    scopus 로고
    • Cowpox virus expresses a novel ankyrin repeat NF-κB inhibitor that controls inflammatory cell influx into virus-infected tissues and is critical for virus pathogenesis
    • Mohamed MR, Rahman MM, Rice A, Moyer RW, Werden SJ, McFadden G. 2009. Cowpox virus expresses a novel ankyrin repeat NF-κB inhibitor that controls inflammatory cell influx into virus-infected tissues and is critical for virus pathogenesis. J. Virol. 83:9223-9236. http://dx.doi.org/10.1128/JVI.00861-09.
    • (2009) J. Virol. , vol.83 , pp. 9223-9236
    • Mohamed, M.R.1    Rahman, M.M.2    Rice, A.3    Moyer, R.W.4    Werden, S.J.5    McFadden, G.6
  • 27
    • 4344600796 scopus 로고    scopus 로고
    • Poxvirus protein N1L targets the I-κB kinase complex, inhibits signaling to NF-κB by the tumor necrosis factor superfamily of receptors, and inhibits NF-κB and IRF3 signaling by Toll-like receptors
    • DiPerna G, Stack J, Bowie AG, Boyd A, Kotwal G, Zhang Z, Arvikar S, Latz E, Fitzgerald KA, Marshall WL. 2004. Poxvirus protein N1L targets the I-κB kinase complex, inhibits signaling to NF-κB by the tumor necrosis factor superfamily of receptors, and inhibits NF-κB and IRF3 signaling by Toll-like receptors. J. Biol. Chem. 279:36570-36578. http://dx.doi.org/10.1074/jbc.M400567200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36570-36578
    • DiPerna, G.1    Stack, J.2    Bowie, A.G.3    Boyd, A.4    Kotwal, G.5    Zhang, Z.6    Arvikar, S.7    Latz, E.8    Fitzgerald, K.A.9    Marshall, W.L.10
  • 29
    • 84855265610 scopus 로고    scopus 로고
    • Inhibition of apoptosis and NF-κB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence
    • Maluquer de Motes C, Cooray S, Ren H, Almeida GM, McGourty K, Bahar MW, Stuart DI, Grimes JM, Graham SC, Smith GL. 2011. Inhibition of apoptosis and NF-κB activation by vaccinia protein N1 occur via distinct binding surfaces and make different contributions to virulence. PLoS Pathog. 7:e1002430. http://dx.doi.org/10.1371/journal.ppat.1002430.
    • (2011) PLoS Pathog. , vol.7
    • Maluquer de Motes, C.1    Cooray, S.2    Ren, H.3    Almeida, G.M.4    McGourty, K.5    Bahar, M.W.6    Stuart, D.I.7    Grimes, J.M.8    Graham, S.C.9    Smith, G.L.10
  • 30
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signaling in the NF-κB pathway
    • Chen ZJ. 2005. Ubiquitin signaling in the NF-κB pathway. Nat. Cell Biol. 7:758-765. http://dx.doi.org/10.1038/ncb0805-758.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 31
    • 65249083913 scopus 로고    scopus 로고
    • Ubiquitin in NF-κB signaling
    • Chiu YH, Zhao M, Chen ZJ. 2009. Ubiquitin in NF-κB signaling. Chem. Rev. 109:1549-1560. http://dx.doi.org/10.1021/cr800554j.
    • (2009) Chem. Rev. , vol.109 , pp. 1549-1560
    • Chiu, Y.H.1    Zhao, M.2    Chen, Z.J.3
  • 33
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM. 2001. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. 2:169-178. http://dx.doi.org/10.1038/35056563.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 34
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski MD, Deshaies RJ. 2005. Function and regulation of cullin-RING ubiquitin ligases. Nat. Rev. Mol. Cell. Biol. 6:9-20. http://dx.doi.org/10.1038/nrm1547.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 35
    • 0242575197 scopus 로고    scopus 로고
    • Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases
    • Furukawa M, He YJ, Borchers C, Xiong Y. 2003. Targeting of protein ubiquitination by BTB-Cullin 3-Roc1 ubiquitin ligases. Nat. Cell Biol. 5:1001-1007. http://dx.doi.org/10.1038/ncb1056.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1001-1007
    • Furukawa, M.1    He, Y.J.2    Borchers, C.3    Xiong, Y.4
  • 36
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • Geyer R, Wee S, Anderson S, Yates J, Wolf DA. 2003. BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases. Mol. Cell 12:783-790. http://dx.doi.org/10.1016/S1097-2765(03)00341-1.
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 37
    • 0141493447 scopus 로고    scopus 로고
    • BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3
    • Xu L, Wei Y, Reboul J, Vaglio P, Shin TH, Vidal M, Elledge SJ, Harper JW. 2003. BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3. Nature 425:316-321. http://dx.doi.org/10.1038/nature01985.
    • (2003) Nature , vol.425 , pp. 316-321
    • Xu, L.1    Wei, Y.2    Reboul, J.3    Vaglio, P.4    Shin, T.H.5    Vidal, M.6    Elledge, S.J.7    Harper, J.W.8
  • 38
    • 79952162490 scopus 로고    scopus 로고
    • Poxvirus exploitation of the ubiquitin-proteasome system
    • Barry M, van Buuren N, Burles K, Mottet K, Wang Q, Teale A. 2010. Poxvirus exploitation of the ubiquitin-proteasome system. Viruses 2:2356-2380. http://dx.doi.org/10.3390/v2102356.
    • (2010) Viruses , vol.2 , pp. 2356-2380
    • Barry, M.1    van Buuren, N.2    Burles, K.3    Mottet, K.4    Wang, Q.5    Teale, A.6
  • 39
    • 41649100863 scopus 로고    scopus 로고
    • Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases
    • Wilton BA, Campbell S, Van Buuren N, Garneau R, Furukawa M, Xiong Y, Barry M. 2008. Ectromelia virus BTB/kelch proteins, EVM150 and EVM167, interact with cullin-3-based ubiquitin ligases. Virology 374: 82-99. http://dx.doi.org/10.1016/j.virol.2007.11.036.
    • (2008) Virology , vol.374 , pp. 82-99
    • Wilton, B.A.1    Campbell, S.2    Van Buuren, N.3    Garneau, R.4    Furukawa, M.5    Xiong, Y.6    Barry, M.7
  • 40
    • 0347627796 scopus 로고    scopus 로고
    • The genomic sequence of ectromelia virus, the causative agent of mousepox
    • Chen N, Danila MI, Feng Z, Buller RM, Wang C, Han X, Lefkowitz EJ, Upton C. 2003. The genomic sequence of ectromelia virus, the causative agent of mousepox. Virology 317:165-186. http://dx.doi.org/10.1016/S0042-6822(03)00520-8.
    • (2003) Virology , vol.317 , pp. 165-186
    • Chen, N.1    Danila, M.I.2    Feng, Z.3    Buller, R.M.4    Wang, C.5    Han, X.6    Lefkowitz, E.J.7    Upton, C.8
  • 41
    • 0036117562 scopus 로고    scopus 로고
    • Species-specific differences in organization of orthopoxvirus kelch-like proteins
    • Shchelkunov S, Totmenin A, Kolosova I. 2002. Species-specific differences in organization of orthopoxvirus kelch-like proteins. Virus Genes 24:157-162. http://dx.doi.org/10.1023/A:1014524717271.
    • (2002) Virus Genes , vol.24 , pp. 157-162
    • Shchelkunov, S.1    Totmenin, A.2    Kolosova, I.3
  • 43
    • 78650643409 scopus 로고    scopus 로고
    • A vaccinia virus deletion mutant reveals the presence of additional inhibitors of NF-κB
    • Fagan-Garcia K, Barry M. 2011. A vaccinia virus deletion mutant reveals the presence of additional inhibitors of NF-κB. J. Virol. 85:883-894. http://dx.doi.org/10.1128/JVI.01267-10.
    • (2011) J. Virol. , vol.85 , pp. 883-894
    • Fagan-Garcia, K.1    Barry, M.2
  • 44
    • 28844499047 scopus 로고    scopus 로고
    • Production of antipolyubiquitin monoclonal antibodies and their use for characterization and isolation of polyubiquitinated proteins
    • Fujimuro M, Yokosawa H. 2005. Production of antipolyubiquitin monoclonal antibodies and their use for characterization and isolation of polyubiquitinated proteins. Methods Enzymol. 399:75-86. http://dx.doi.org/10.1016/S0076-6879(05)99006-X.
    • (2005) Methods Enzymol. , vol.399 , pp. 75-86
    • Fujimuro, M.1    Yokosawa, H.2
  • 45
    • 0033781272 scopus 로고    scopus 로고
    • The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1
    • Furukawa M, Zhang Y, McCarville J, Ohta T, Xiong Y. 2000. The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1. Mol. Cell. Biol. 20:8185-8197. http://dx.doi.org/10.1128/MCB.20.21.8185-8197.2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8185-8197
    • Furukawa, M.1    Zhang, Y.2    McCarville, J.3    Ohta, T.4    Xiong, Y.5
  • 46
    • 0025961008 scopus 로고
    • The target DNA sequence for resolution of poxvirus replicative intermediates is an active late promoter
    • Stuart D, Graham K, Schreiber M, Macaulay C, McFadden G. 1991. The target DNA sequence for resolution of poxvirus replicative intermediates is an active late promoter. J. Virol. 65:61-70.
    • (1991) J. Virol. , vol.65 , pp. 61-70
    • Stuart, D.1    Graham, K.2    Schreiber, M.3    Macaulay, C.4    McFadden, G.5
  • 47
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
    • Karin M, Ben-Neriah Y. 2000. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu. Rev. Immunol. 18:621-663. http://dx.doi.org/10.1146/annurev.immunol.18.1.621.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 48
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • Fujimuro M, Sawada H, Yokosawa H. 1994. Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins. FEBS Lett. 349:173-180. http://dx.doi.org/10.1016/0014-5793(94)00647-4.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 49
    • 34447499052 scopus 로고    scopus 로고
    • Triggering the innate antiviral response through IRF-3 activation
    • Hiscott J. 2007. Triggering the innate antiviral response through IRF-3 activation. J. Biol. Chem. 282:15325-15329. http://dx.doi.org/10.1074/jbc.R700002200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15325-15329
    • Hiscott, J.1
  • 50
  • 51
    • 65449183853 scopus 로고    scopus 로고
    • Viral avoidance and exploitation of the ubiquitin system
    • Randow F, Lehner PJ. 2009. Viral avoidance and exploitation of the ubiquitin system. Nat. Cell Biol. 11:527-534. http://dx.doi.org/10.1038/ncb0509-527.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 527-534
    • Randow, F.1    Lehner, P.J.2
  • 52
    • 0042854790 scopus 로고    scopus 로고
    • The vaccinia virus kelch-like protein C2L affects calciumindependent adhesion to the extracellular matrix and inflammation in a murine intradermal model
    • Pires de Miranda M, Reading PC, Tscharke DC, Murphy BJ, Smith GL. 2003. The vaccinia virus kelch-like protein C2L affects calciumindependent adhesion to the extracellular matrix and inflammation in a murine intradermal model. J. Gen. Virol. 84:2459-2471. http://dx.doi.org/10.1099/vir.0.19292-0.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2459-2471
    • Pires de Miranda, M.1    Reading, P.C.2    Tscharke, D.C.3    Murphy, B.J.4    Smith, G.L.5
  • 53
    • 33744792283 scopus 로고    scopus 로고
    • Vaccinia virus kelch protein A55 is a 64-kDa intracellular factor that affects virus-induced cytopathic effect and the outcome of infection in a murine intradermal model
    • Beard PM, Froggatt GC, Smith GL. 2006. Vaccinia virus kelch protein A55 is a 64-kDa intracellular factor that affects virus-induced cytopathic effect and the outcome of infection in a murine intradermal model. J. Gen. Virol. 87:1521-1529. http://dx.doi.org/10.1099/vir.0.81854-0.
    • (2006) J. Gen. Virol. , vol.87 , pp. 1521-1529
    • Beard, P.M.1    Froggatt, G.C.2    Smith, G.L.3
  • 54
    • 34347334675 scopus 로고    scopus 로고
    • Vaccinia virus gene F3L encodes an intracellular protein that affects the innate immune response
    • Froggatt GC, Smith GL, Beard PM. 2007. Vaccinia virus gene F3L encodes an intracellular protein that affects the innate immune response. J. Gen. Virol. 88:1917-1921. http://dx.doi.org/10.1099/vir.0.82815-0.
    • (2007) J. Gen. Virol. , vol.88 , pp. 1917-1921
    • Froggatt, G.C.1    Smith, G.L.2    Beard, P.M.3
  • 55
    • 23844535402 scopus 로고    scopus 로고
    • Effects of deletions of kelch-like genes on cowpox virus biological properties
    • Kochneva G, Kolosova I, Maksyutova T, Ryabchikova E, Shchelkunov S. 2005. Effects of deletions of kelch-like genes on cowpox virus biological properties. Arch. Virol. 150:1857-1870. http://dx.doi.org/10.1007/s00705-005-0530-0.
    • (2005) Arch. Virol. , vol.150 , pp. 1857-1870
    • Kochneva, G.1    Kolosova, I.2    Maksyutova, T.3    Ryabchikova, E.4    Shchelkunov, S.5
  • 57
    • 10644248286 scopus 로고    scopus 로고
    • Post-translational modification of RelA( p65) NF-κB
    • Campbell KJ, Perkins ND. 2004. Post-translational modification of RelA( p65) NF-κB. Biochem. Soc. Trans. 32:1087-1089. http://dx.doi.org/10.1042/BST0321087.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 1087-1089
    • Campbell, K.J.1    Perkins, N.D.2
  • 58
    • 18144426719 scopus 로고    scopus 로고
    • NF-κB is transported into the nucleus by importin α3 and importin α4
    • Fagerlund R, Kinnunen L, Kohler M, Julkunen I, Melen K. 2005. NF-κB is transported into the nucleus by importin α3 and importin α4. J. Biol. Chem. 280:15942-15951. http://dx.doi.org/10.1074/jbc.M500814200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 15942-15951
    • Fagerlund, R.1    Kinnunen, L.2    Kohler, M.3    Julkunen, I.4    Melen, K.5
  • 59
    • 45449112571 scopus 로고    scopus 로고
    • NF-κB p52, RelB, and c-Rel are transported into the nucleus via a subset of importin alpha molecules
    • Fagerlund R, Melen K, Cao X, Julkunen I. 2008. NF-κB p52, RelB, and c-Rel are transported into the nucleus via a subset of importin alpha molecules. Cell Signal. 20:1442-1451. http://dx.doi.org/10.1016/j.cellsig.2008.03.012.
    • (2008) Cell Signal. , vol.20 , pp. 1442-1451
    • Fagerlund, R.1    Melen, K.2    Cao, X.3    Julkunen, I.4
  • 60
    • 59749104967 scopus 로고    scopus 로고
    • Hantaan virus nucleocapsid protein binds to importin alpha proteins and inhibits tumor necrosis factor alpha-induced activation of nuclear factor κB
    • Taylor SL, Frias-Staheli N, Garcia-Sastre A, Schmaljohn CS. 2009. Hantaan virus nucleocapsid protein binds to importin alpha proteins and inhibits tumor necrosis factor alpha-induced activation of nuclear factor κB. J. Virol. 83:1271-1279. http://dx.doi.org/10.1128/JVI.00986-08.
    • (2009) J. Virol. , vol.83 , pp. 1271-1279
    • Taylor, S.L.1    Frias-Staheli, N.2    Garcia-Sastre, A.3    Schmaljohn, C.S.4
  • 62
    • 0033068154 scopus 로고    scopus 로고
    • β-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro
    • β-TRCP-ubiquitin ligase complex associates specifically with phosphorylated destruction motifs in IκBα and β-catenin and stimulates IκBα ubiquitination in vitro. Genes Dev. 13:270-283. http://dx.doi.org/10.1101/gad.13.3.270.
    • (1999) Genes Dev. , vol.13 , pp. 270-283
    • Winston, J.T.1    Strack, P.2    Beer-Romero, P.3    Chu, C.Y.4    Elledge, S.J.5    Harper, J.W.6
  • 63
  • 66
    • 0028040875 scopus 로고
    • The POZ domain: a conserved proteinprotein interaction motif
    • Bardwell VJ, Treisman R. 1994. The POZ domain: a conserved proteinprotein interaction motif. Genes Dev. 8:1664-1677. http://dx.doi.org/10.1101/gad.8.14.1664.
    • (1994) Genes Dev. , vol.8 , pp. 1664-1677
    • Bardwell, V.J.1    Treisman, R.2
  • 67
    • 0033838360 scopus 로고    scopus 로고
    • In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions
    • Melnick A, Ahmad KF, Arai S, Polinger A, Ball H, Borden KL, Carlile GW, Prive GG, Licht JD. 2000. In-depth mutational analysis of the promyelocytic leukemia zinc finger BTB/POZ domain reveals motifs and residues required for biological and transcriptional functions. Mol. Cell. Biol. 20:6550-6567. http://dx.doi.org/10.1128/MCB.20.17.6550-6567.2000.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6550-6567
    • Melnick, A.1    Ahmad, K.F.2    Arai, S.3    Polinger, A.4    Ball, H.5    Borden, K.L.6    Carlile, G.W.7    Prive, G.G.8    Licht, J.D.9
  • 68
    • 1242274394 scopus 로고    scopus 로고
    • Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes
    • Kang MI, Kobayashi A, Wakabayashi N, Kim SG, Yamamoto M. 2004. Scaffolding of Keap1 to the actin cytoskeleton controls the function of Nrf2 as key regulator of cytoprotective phase 2 genes. Proc. Natl. Acad. Sci. U. S. A. 101:2046-2051. http://dx.doi.org/10.1073/pnas.0308347100.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2046-2051
    • Kang, M.I.1    Kobayashi, A.2    Wakabayashi, N.3    Kim, S.G.4    Yamamoto, M.5
  • 69
    • 33947542986 scopus 로고    scopus 로고
    • Evidence for actin cytoskeleton-dependent and-independent pathways for RelA/p65 nuclear translocation in endothelial cells
    • Fazal F, Minhajuddin M, Bijli KM, McGrath JL, Rahman A. 2007. Evidence for actin cytoskeleton-dependent and-independent pathways for RelA/p65 nuclear translocation in endothelial cells. J. Biol. Chem. 282: 3940-3950.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3940-3950
    • Fazal, F.1    Minhajuddin, M.2    Bijli, K.M.3    McGrath, J.L.4    Rahman, A.5
  • 70
    • 0034193240 scopus 로고    scopus 로고
    • The p65/RelA subunit of NF-κB interacts with actin-containing structures
    • Are AF, Galkin VE, Pospelova TV, Pinaev GP. 2000. The p65/RelA subunit of NF-κB interacts with actin-containing structures. Exp. Cell Res. 256:533-544. http://dx.doi.org/10.1006/excr.2000.4830.
    • (2000) Exp. Cell Res. , vol.256 , pp. 533-544
    • Are, A.F.1    Galkin, V.E.2    Pospelova, T.V.3    Pinaev, G.P.4
  • 71
    • 61349179565 scopus 로고    scopus 로고
    • Role of actin cytoskeleton in LPS-induced NF-κB activation and nitric oxide production in murine macrophages
    • Eswarappa SM, Pareek V, Chakravortty D. 2008. Role of actin cytoskeleton in LPS-induced NF-κB activation and nitric oxide production in murine macrophages. Innate Immun. 14:309-318. http://dx.doi.org/10.1177/1753425908096856.
    • (2008) Innate Immun. , vol.14 , pp. 309-318
    • Eswarappa, S.M.1    Pareek, V.2    Chakravortty, D.3


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