메뉴 건너뛰기




Volumn 90, Issue 17, 2016, Pages 7740-7747

Pestivirus Npro directly interacts with interferon regulatory factor 3 monomer and dimer

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; DIMER; INTERFERON REGULATORY FACTOR 3; MONOMER; N TERMINAL PROTEASE; PROTEASOME; PROTEINASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; N(PRO) PROTEIN, SWINE FEVER VIRUS; PROTEIN BINDING; VIRAL PROTEIN;

EID: 84983546278     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00318-16     Document Type: Article
Times cited : (14)

References (48)
  • 1
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai T, Akira S. 2006. Innate immune recognition of viral infection. Nat Immunol 7:131-137. http://dx.doi.org/10.1038/ni1303.
    • (2006) Nat Immunol , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 2
    • 65549165903 scopus 로고    scopus 로고
    • Interferons and viral infections
    • Fensterl V, Sen GC. 2009. Interferons and viral infections. Biofactors 35:14-20. http://dx.doi.org/10.1002/biof.6.
    • (2009) Biofactors , vol.35 , pp. 14-20
    • Fensterl, V.1    Sen, G.C.2
  • 3
    • 33748051738 scopus 로고    scopus 로고
    • IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors
    • Honda K, Taniguchi T. 2006. IRFs: master regulators of signalling by Toll-like receptors and cytosolic pattern-recognition receptors. Nat Rev Immunol 6:644-658. http://dx.doi.org/10.1038/nri1900.
    • (2006) Nat Rev Immunol , vol.6 , pp. 644-658
    • Honda, K.1    Taniguchi, T.2
  • 4
    • 33748475531 scopus 로고    scopus 로고
    • Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors
    • Honda K, Takaoka A, Taniguchi T. 2006. Type I interferon [corrected] gene induction by the interferon regulatory factor family of transcription factors. Immunity 25:349-360. http://dx.doi.org/10.1016/j.immuni.2006.08.009.
    • (2006) Immunity , vol.25 , pp. 349-360
    • Honda, K.1    Takaoka, A.2    Taniguchi, T.3
  • 5
    • 42649114059 scopus 로고    scopus 로고
    • The IRF family transcription factors in immunity and oncogenesis
    • Tamura T, Yanai H, Savitsky D, Taniguchi T. 2008. The IRF family transcription factors in immunity and oncogenesis. Annu Rev Immunol 26:535-584. http://dx.doi.org/10.1146/annurev.immunol.26.021607.090400.
    • (2008) Annu Rev Immunol , vol.26 , pp. 535-584
    • Tamura, T.1    Yanai, H.2    Savitsky, D.3    Taniguchi, T.4
  • 6
    • 29144501207 scopus 로고    scopus 로고
    • The interferon response circuit:induction and suppression by pathogenic viruses
    • Haller O, Kochs G, Weber F. 2006. The interferon response circuit:induction and suppression by pathogenic viruses. Virology 344:119-130. http://dx.doi.org/10.1016/j.virol.2005.09.024.
    • (2006) Virology , vol.344 , pp. 119-130
    • Haller, O.1    Kochs, G.2    Weber, F.3
  • 7
    • 58049202272 scopus 로고    scopus 로고
    • Innate immunity to virus infection
    • Takeuchi O, Akira S. 2009. Innate immunity to virus infection. Immunol Rev 227:75-86. http://dx.doi.org/10.1111/j.1600-065X.2008.00737.x.
    • (2009) Immunol Rev , vol.227 , pp. 75-86
    • Takeuchi, O.1    Akira, S.2
  • 8
    • 79959634861 scopus 로고    scopus 로고
    • Pattern recognition receptors and the innate immune response to viral infection
    • Thompson MR, Kaminski JJ, Kurt-Jones EA, Fitzgerald KA. 2011. Pattern recognition receptors and the innate immune response to viral infection. Viruses 3:920-940. http://dx.doi.org/10.3390/v3060920.
    • (2011) Viruses , vol.3 , pp. 920-940
    • Thompson, M.R.1    Kaminski, J.J.2    Kurt-Jones, E.A.3    Fitzgerald, K.A.4
  • 9
    • 77949913872 scopus 로고    scopus 로고
    • Structural insights into interferon regulatory factor activation
    • Chen W, Royer WE, Jr. 2010. Structural insights into interferon regulatory factor activation. Cell Signal 22:883-887. http://dx.doi.org/10.1016/j .cellsig.2009.12.005.
    • (2010) Cell Signal , vol.22 , pp. 883-887
    • Chen, W.1    Royer, W.E.2
  • 10
    • 0032915860 scopus 로고    scopus 로고
    • Structural and functional analysis of interferon regulatory factor 3: localization of the transactivation and autoinhibitory domains
    • Lin R, Mamane Y, Hiscott J. 1999. Structural and functional analysis of interferon regulatory factor 3: localization of the transactivation and autoinhibitory domains. Mol Cell Biol 19:2465-2474. http://dx.doi.org/10.1128/MCB.19.4.2465.
    • (1999) Mol Cell Biol , vol.19 , pp. 2465-2474
    • Lin, R.1    Mamane, Y.2    Hiscott, J.3
  • 11
    • 0242574745 scopus 로고    scopus 로고
    • Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation
    • Qin BY, Liu C, Lam SS, Srinath H, Delston R, Correia JJ, Derynck R, Lin K. 2003. Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation. Nat Struct Biol 10:913-921. http://dx.doi.org/10.1038/nsb1002.
    • (2003) Nat Struct Biol , vol.10 , pp. 913-921
    • Qin, B.Y.1    Liu, C.2    Lam, S.S.3    Srinath, H.4    Delston, R.5    Correia, J.J.6    Derynck, R.7    Lin, K.8
  • 14
    • 0033842515 scopus 로고    scopus 로고
    • Selective DNA binding and association with the CREB binding protein coactivator contribute to differential activation of alpha/beta interferon genes by interferon regulatory factors 3 and 7
    • Lin R, Genin P, Mamane Y, Hiscott J. 2000. Selective DNA binding and association with the CREB binding protein coactivator contribute to differential activation of alpha/beta interferon genes by interferon regulatory factors 3 and 7. Mol Cell Biol 20:6342-6353. http://dx.doi.org/10.1128/MCB.20.17.6342-6353.2000.
    • (2000) Mol Cell Biol , vol.20 , pp. 6342-6353
    • Lin, R.1    Genin, P.2    Mamane, Y.3    Hiscott, J.4
  • 15
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • Iwasaki A, Medzhitov R. 2010. Regulation of adaptive immunity by the innate immune system. Science 327:291-295. http://dx.doi.org/10.1126/science.1183021.
    • (2010) Science , vol.327 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 16
    • 84971242086 scopus 로고    scopus 로고
    • Immune responses against classical swine fever virus: between ignorance and lunacy
    • Summerfield A, Ruggli N. 2015. Immune responses against classical swine fever virus: between ignorance and lunacy. Front Vet Sci 2:10. http://dx.doi.org/10.3389/fvets.2015.00010.
    • (2015) Front Vet Sci , vol.2 , pp. 10
    • Summerfield, A.1    Ruggli, N.2
  • 17
    • 54449090843 scopus 로고    scopus 로고
    • RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses
    • Magkouras I, Mätzener P, Rümenapf T, Peterhans E, Schweizer M. 2008. RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses. J Gen Virol 89:2501-2506. http://dx.doi.org/10.1099/vir.0.2008/003749-0.
    • (2008) J Gen Virol , vol.89 , pp. 2501-2506
    • Magkouras, I.1    Mätzener, P.2    Rümenapf, T.3    Peterhans, E.4    Schweizer, M.5
  • 18
    • 60749120273 scopus 로고    scopus 로고
    • The viral RNase E(rns) prevents IFN type-I triggering by pestiviral single-and double-stranded RNAs
    • Mätzener P, Magkouras I, Rümenapf T, Peterhans E, Schweizer M. 2009. The viral RNase E(rns) prevents IFN type-I triggering by pestiviral single-and double-stranded RNAs. Virus Res 140:15-23. http://dx.doi .org/10.1016/j.virusres.2008.10.015.
    • (2009) Virus Res , vol.140 , pp. 15-23
    • Mätzener, P.1    Magkouras, I.2    Rümenapf, T.3    Peterhans, E.4    Schweizer, M.5
  • 19
    • 0347626043 scopus 로고    scopus 로고
    • Role for bovine viral diarrhea virus Erns glycoprotein in the control of activation of beta interferon by double-stranded RNA
    • Iqbal M, Poole E, Goodbourn S, McCauley JW. 2004. Role for bovine viral diarrhea virus Erns glycoprotein in the control of activation of beta interferon by double-stranded RNA. J Virol 78:136-145. http://dx.doi.org /10.1128/JVI.78.1.136-145.2004.
    • (2004) J Virol , vol.78 , pp. 136-145
    • Iqbal, M.1    Poole, E.2    Goodbourn, S.3    McCauley, J.W.4
  • 20
    • 84901989753 scopus 로고    scopus 로고
    • Prolonged activity of the pestiviral RNase Erns as an interferon antagonist after uptake by clathrin-mediated endocytosis
    • Zürcher C, Sauter KS, Mathys V, Wyss F, Schweizer M. 2014. Prolonged activity of the pestiviral RNase Erns as an interferon antagonist after uptake by clathrin-mediated endocytosis. J Virol 88:7235-7243. http://dx .doi.org/10.1128/JVI.00672-14.
    • (2014) J Virol , vol.88 , pp. 7235-7243
    • Zürcher, C.1    Sauter, K.S.2    Mathys, V.3    Wyss, F.4    Schweizer, M.5
  • 21
    • 84879531380 scopus 로고    scopus 로고
    • Efficient sensing of infected cells in absence of virus particles by plasmacytoid dendritic cells is blocked by the viral ribonuclease E(rns.)
    • Python S, Gerber M, Suter R, Ruggli N, Summerfield A. 2013. Efficient sensing of infected cells in absence of virus particles by plasmacytoid dendritic cells is blocked by the viral ribonuclease E(rns.). PLoS Pathog 9:e1003412. http://dx.doi.org/10.1371/journal.ppat.1003412.
    • (2013) PLoS Pathog , vol.9
    • Python, S.1    Gerber, M.2    Suter, R.3    Ruggli, N.4    Summerfield, A.5
  • 22
    • 0031935816 scopus 로고    scopus 로고
    • N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis
    • Rumenapf T, Stark R, Heimann M, Thiel HJ. 1998. N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis. J Virol 72:2544-2547.
    • (1998) J Virol , vol.72 , pp. 2544-2547
    • Rumenapf, T.1    Stark, R.2    Heimann, M.3    Thiel, H.J.4
  • 23
    • 84896278871 scopus 로고    scopus 로고
    • Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease N(pro)
    • Gottipati K, Acholi S, Ruggli N, Choi KH. 2014. Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease N(pro). Virology 452-453:303-309. http://dx.doi.org/10.1016/j.virol.2014.01.026.
    • (2014) Virology , vol.452-453 , pp. 303-309
    • Gottipati, K.1    Acholi, S.2    Ruggli, N.3    Choi, K.H.4
  • 24
    • 36248953962 scopus 로고    scopus 로고
    • The Npro product of classical swine fever virus and bovine viral diarrhea virus uses a conserved mechanism to target interferon regulatory factor-3
    • Seago J, Hilton L, Reid E, Doceul V, Jeyatheesan J, Moganeradj K, McCauley J, Charleston B, Goodbourn S. 2007. The Npro product of classical swine fever virus and bovine viral diarrhea virus uses a conserved mechanism to target interferon regulatory factor-3. J Gen Virol 88:3002-3006. http://dx.doi.org/10.1099/vir.0.82934-0.
    • (2007) J Gen Virol , vol.88 , pp. 3002-3006
    • Seago, J.1    Hilton, L.2    Reid, E.3    Doceul, V.4    Jeyatheesan, J.5    Moganeradj, K.6    McCauley, J.7    Charleston, B.8    Goodbourn, S.9
  • 25
    • 34548566398 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus
    • Chen Z, Rijnbrand R, Jangra RK, Devaraj SG, Qu L, Ma Y, Lemon SM, Li K. 2007. Ubiquitination and proteasomal degradation of interferon regulatory factor-3 induced by Npro from a cytopathic bovine viral diarrhea virus. Virology 366:277-292. http://dx.doi.org/10.1016/j.virol.2007.04.023.
    • (2007) Virology , vol.366 , pp. 277-292
    • Chen, Z.1    Rijnbrand, R.2    Jangra, R.K.3    Devaraj, S.G.4    Qu, L.5    Ma, Y.6    Lemon, S.M.7    Li, K.8
  • 26
    • 33947382185 scopus 로고    scopus 로고
    • Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation
    • Bauhofer O, Summerfield A, Sakoda Y, Tratschin JD, Hofmann MA, Ruggli N. 2007. Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation. J Virol 81:3087-3096. http://dx.doi.org/10.1128/JVI.02032-06.
    • (2007) J Virol , vol.81 , pp. 3087-3096
    • Bauhofer, O.1    Summerfield, A.2    Sakoda, Y.3    Tratschin, J.D.4    Hofmann, M.A.5    Ruggli, N.6
  • 27
    • 33751232040 scopus 로고    scopus 로고
    • The NPro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation
    • Hilton L, Moganeradj K, Zhang G, Chen YH, Randall RE, McCauley JW, Goodbourn S. 2006. The NPro product of bovine viral diarrhea virus inhibits DNA binding by interferon regulatory factor 3 and targets it for proteasomal degradation. J Virol 80:11723-11732. http://dx.doi.org/10.1128/JVI.01145-06.
    • (2006) J Virol , vol.80 , pp. 11723-11732
    • Hilton, L.1    Moganeradj, K.2    Zhang, G.3    Chen, Y.H.4    Randall, R.E.5    McCauley, J.W.6    Goodbourn, S.7
  • 28
    • 79961180446 scopus 로고    scopus 로고
    • Classical swine fever virus N(pro) limits type I interferon induction in plasmacytoid dendritic cells by interacting with interferon regulatory factor 7
    • Fiebach AR, Guzylack-Piriou L, Python S, Summerfield A, Ruggli N. 2011. Classical swine fever virus N(pro) limits type I interferon induction in plasmacytoid dendritic cells by interacting with interferon regulatory factor 7. J Virol 85:8002-8011. http://dx.doi.org/10.1128/JVI.00330-11.
    • (2011) J Virol , vol.85 , pp. 8002-8011
    • Fiebach, A.R.1    Guzylack-Piriou, L.2    Python, S.3    Summerfield, A.4    Ruggli, N.5
  • 29
    • 84900555522 scopus 로고    scopus 로고
    • Npro of classical swine fever virus contributes to pathogenicity in pigs by preventing type I interferon induction at local replication sites
    • Tamura T, Nagashima N, Ruggli N, Summerfield A, Kida H, Sakoda Y. 2014. Npro of classical swine fever virus contributes to pathogenicity in pigs by preventing type I interferon induction at local replication sites. Vet Res 45:47. http://dx.doi.org/10.1186/1297-9716-45-47.
    • (2014) Vet Res , vol.45 , pp. 47
    • Tamura, T.1    Nagashima, N.2    Ruggli, N.3    Summerfield, A.4    Kida, H.5    Sakoda, Y.6
  • 31
    • 0344665684 scopus 로고    scopus 로고
    • Attenuation of classical swine fever virus by deletion of the viral N(pro) gene
    • Mayer D, Hofmann MA, Tratschin JD. 2004. Attenuation of classical swine fever virus by deletion of the viral N(pro) gene. Vaccine 22:317-328. http://dx.doi.org/10.1016/j.vaccine.2003.08.006.
    • (2004) Vaccine , vol.22 , pp. 317-328
    • Mayer, D.1    Hofmann, M.A.2    Tratschin, J.D.3
  • 33
    • 84930462097 scopus 로고    scopus 로고
    • Analysis of a pair of END+ and END- viruses derived from the same bovine viral diarrhea virus stock reveals the amino acid determinants in Npro responsible for inhibition of type I interferon production
    • Kozasa T, Abe Y, Mitsuhashi K, Tamura T, Aoki H, Ishimaru M, Nakamura S, Okamatsu M, Kida H, Sakoda Y. 2015. Analysis of a pair of END+ and END- viruses derived from the same bovine viral diarrhea virus stock reveals the amino acid determinants in Npro responsible for inhibition of type I interferon production. J Vet Med Sci 77:511-518. http://dx.doi.org/10.1292/jvms.14-0420.
    • (2015) J Vet Med Sci , vol.77 , pp. 511-518
    • Kozasa, T.1    Abe, Y.2    Mitsuhashi, K.3    Tamura, T.4    Aoki, H.5    Ishimaru, M.6    Nakamura, S.7    Okamatsu, M.8    Kida, H.9    Sakoda, Y.10
  • 34
    • 84887304158 scopus 로고    scopus 로고
    • The structure of classical swine fever virus N(pro): a novel cysteine autoprotease and zinc-binding protein involved in subversion of type I interferon induction
    • Gottipati K, Ruggli N, Gerber M, Tratschin JD, Benning M, Bellamy H, Choi KH. 2013. The structure of classical swine fever virus N(pro): a novel cysteine autoprotease and zinc-binding protein involved in subversion of type I interferon induction. PLoS Pathog 9:e1003704. http://dx.doi.org/10.1371/journal.ppat.1003704.
    • (2013) PLoS Pathog , vol.9
    • Gottipati, K.1    Ruggli, N.2    Gerber, M.3    Tratschin, J.D.4    Benning, M.5    Bellamy, H.6    Choi, K.H.7
  • 35
    • 84878844202 scopus 로고    scopus 로고
    • Crystal structures of the viral protease Npro imply distinct roles for the catalytic water in catalysis
    • Zogg T, Sponring M, Schindler S, Koll M, Schneider R, Brandstetter H, Auer B. 2013. Crystal structures of the viral protease Npro imply distinct roles for the catalytic water in catalysis. Structure 21:929-938. http://dx .doi.org/10.1016/j.str.2013.04.003.
    • (2013) Structure , vol.21 , pp. 929-938
    • Zogg, T.1    Sponring, M.2    Schindler, S.3    Koll, M.4    Schneider, R.5    Brandstetter, H.6    Auer, B.7
  • 36
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys J 78:1606-1619. http://dx.doi.org/10.1016/S0006-3495(00)76713-0.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 37
    • 0031893220 scopus 로고    scopus 로고
    • Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation
    • Lin R, Heylbroeck C, Pitha PM, Hiscott J. 1998. Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation. Mol Cell Biol 18:2986-2996. http://dx.doi.org/10.1128/MCB.18.5.2986.
    • (1998) Mol Cell Biol , vol.18 , pp. 2986-2996
    • Lin, R.1    Heylbroeck, C.2    Pitha, P.M.3    Hiscott, J.4
  • 38
    • 43049094372 scopus 로고    scopus 로고
    • Contribution of Ser386 and Ser396 to activation of interferon regulatory factor 3
    • Chen W, Srinath H, Lam SS, Schiffer CA, Royer WE, Jr, Lin K. 2008. Contribution of Ser386 and Ser396 to activation of interferon regulatory factor 3. J Mol Biol 379:251-260. http://dx.doi.org/10.1016/j.jmb.2008.03.050.
    • (2008) J Mol Biol , vol.379 , pp. 251-260
    • Chen, W.1    Srinath, H.2    Lam, S.S.3    Schiffer, C.A.4    Royer, W.E.5    Lin, K.6
  • 39
    • 1642297150 scopus 로고    scopus 로고
    • Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation
    • Mori M, Yoneyama M, Ito T, Takahashi K, Inagaki F, Fujita T. 2004. Identification of Ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation. J Biol Chem 279:9698-9702. http://dx.doi.org/10.1074/jbc.M310616200.
    • (2004) J Biol Chem , vol.279 , pp. 9698-9702
    • Mori, M.1    Yoneyama, M.2    Ito, T.3    Takahashi, K.4    Inagaki, F.5    Fujita, T.6
  • 40
    • 0038660668 scopus 로고    scopus 로고
    • Identification of the minimal phosphoacceptor site required for in vivo activation of interferon regulatory factor 3 in response to virus and double-stranded RNA
    • Servant MJ, Grandvaux N, ten Oever BR, Duguay D, Lin R, Hiscott J. 2003. Identification of the minimal phosphoacceptor site required for in vivo activation of interferon regulatory factor 3 in response to virus and double-stranded RNA. J Biol Chem 278:9441-9447. http://dx.doi.org/10.1074/jbc.M209851200.
    • (2003) J Biol Chem , vol.278 , pp. 9441-9447
    • Servant, M.J.1    Grandvaux, N.2    ten Oever, B.R.3    Duguay, D.4    Lin, R.5    Hiscott, J.6
  • 41
    • 34547930163 scopus 로고    scopus 로고
    • Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch
    • Panne D, McWhirter SM, Maniatis T, Harrison SC. 2007. Interferon regulatory factor 3 is regulated by a dual phosphorylation-dependent switch. J Biol Chem 282:22816-22822. http://dx.doi.org/10.1074/jbc .M703019200.
    • (2007) J Biol Chem , vol.282 , pp. 22816-22822
    • Panne, D.1    McWhirter, S.M.2    Maniatis, T.3    Harrison, S.C.4
  • 42
    • 34547098171 scopus 로고    scopus 로고
    • Mechanisms of activation of interferon regulator factor 3: the role of C-terminal domain phosphorylation in IRF-3 dimerization and DNA binding
    • Dragan AI, Hargreaves VV, Makeyeva EN, Privalov PL. 2007. Mechanisms of activation of interferon regulator factor 3: the role of C-terminal domain phosphorylation in IRF-3 dimerization and DNA binding. Nucleic Acids Res 35:3525-3534. http://dx.doi.org/10.1093/nar/gkm142.
    • (2007) Nucleic Acids Res , vol.35 , pp. 3525-3534
    • Dragan, A.I.1    Hargreaves, V.V.2    Makeyeva, E.N.3    Privalov, P.L.4
  • 43
    • 0034785837 scopus 로고    scopus 로고
    • A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies
    • Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E. 2001. A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies. Mol Cell 8:581-590. http://dx.doi.org/10.1016/S1097-2765(01)00333-1.
    • (2001) Mol Cell , vol.8 , pp. 581-590
    • Lin, C.H.1    Hare, B.J.2    Wagner, G.3    Harrison, S.C.4    Maniatis, T.5    Fraenkel, E.6
  • 45
    • 0033568642 scopus 로고    scopus 로고
    • Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences
    • Fujii Y, Shimizu T, Kusumoto M, Kyogoku Y, Taniguchi T, Hakoshima T. 1999. Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences. EMBO J 18:5028-5041. http://dx.doi.org/10.1093/emboj/18.18.5028.
    • (1999) EMBO J , vol.18 , pp. 5028-5041
    • Fujii, Y.1    Shimizu, T.2    Kusumoto, M.3    Kyogoku, Y.4    Taniguchi, T.5    Hakoshima, T.6
  • 47
    • 50549098808 scopus 로고    scopus 로고
    • The Npro product of classical swine fever virus interacts with IkappaBalpha, the NF-kappaB inhibitor
    • Doceul V, Charleston B, Crooke H, Reid E, Powell PP, Seago J. 2008. The Npro product of classical swine fever virus interacts with IkappaBalpha, the NF-kappaB inhibitor. J Gen Virol 89:1881-1889. http://dx.doi .org/10.1099/vir.0.83643-0.
    • (2008) J Gen Virol , vol.89 , pp. 1881-1889
    • Doceul, V.1    Charleston, B.2    Crooke, H.3    Reid, E.4    Powell, P.P.5    Seago, J.6
  • 48
    • 84905971496 scopus 로고    scopus 로고
    • Visualization of the Npro protein in living cells using biarsenically labeling tetracysteine-tagged classical swine fever virus
    • Li Y, Shen L, Li C, Huang J, Zhao B, Sun Y, Li S, Luo Y, Qiu HJ. 2014. Visualization of the Npro protein in living cells using biarsenically labeling tetracysteine-tagged classical swine fever virus. Virus Res 189:67-74. http://dx.doi.org/10.1016/j.virusres.2014.04.018.
    • (2014) Virus Res , vol.189 , pp. 67-74
    • Li, Y.1    Shen, L.2    Li, C.3    Huang, J.4    Zhao, B.5    Sun, Y.6    Li, S.7    Luo, Y.8    Qiu, H.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.