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Volumn 85, Issue 13, 2011, Pages 6234-6243

NSs protein of rift valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; NSS PROTEIN; PROTEIN KINASE R; PROTEIN P62; TRANSCRIPTION FACTOR IIH; UNCLASSIFIED DRUG; VIRUS PROTEIN; PROTEIN SUBUNIT;

EID: 80052073169     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02255-10     Document Type: Article
Times cited : (106)

References (56)
  • 1
    • 49049097662 scopus 로고    scopus 로고
    • RNA polymerase I-mediated expression of viral RNA for the rescue of infectious virulent and avirulent Rift Valley fever viruses
    • Billecocq, A., et al. 2008. RNA polymerase I-mediated expression of viral RNA for the rescue of infectious virulent and avirulent Rift Valley fever viruses. Virology 378:377-384.
    • (2008) Virology , vol.378 , pp. 377-384
    • Billecocq, A.1
  • 2
    • 4444374579 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription
    • Billecocq, A., et al. 2004. NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription. J. Virol. 78: 9798-9806.
    • (2004) J. Virol. , vol.78 , pp. 9798-9806
    • Billecocq, A.1
  • 4
    • 0035152344 scopus 로고    scopus 로고
    • Genetic evidence for an interferon-antagonistic function of Rift Valley fever virus nonstructural protein NSs
    • Bouloy, M., et al. 2001. Genetic evidence for an interferon-antagonistic function of Rift Valley fever virus nonstructural protein NSs. J. Virol. 75: 1371-1377.
    • (2001) J. Virol. , vol.75 , pp. 1371-1377
    • Bouloy, M.1
  • 5
    • 0036678409 scopus 로고    scopus 로고
    • Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase
    • Brower, C. S., et al. 2002. Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase. Proc. Natl. Acad. Sci. U. S. A. 99:10353- 10358.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10353-10358
    • Brower, C.S.1
  • 6
    • 0022258169 scopus 로고
    • Mutagen-directed attenuation of Rift Valley fever virus as a method for vaccine development
    • Caplen, H., C. J. Peters, and D. H. Bishop. 1985. Mutagen-directed attenuation of Rift Valley fever virus as a method for vaccine development. J. Gen. Virol. 66:2271-2277.
    • (1985) J. Gen. Virol. , vol.66 , pp. 2271-2277
    • Caplen, H.1    Peters, C.J.2    Bishop, D.H.3
  • 7
    • 33745214419 scopus 로고    scopus 로고
    • Structure of the Tfb1/p53 complex: insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53
    • Di Lello, P., et al. 2006. Structure of the Tfb1/p53 complex: insights into the interaction between the p62/Tfb1 subunit of TFIIH and the activation domain of p53. Mol. Cell 22:731-740.
    • (2006) Mol. Cell , vol.22 , pp. 731-740
    • Di Lello, P.1
  • 8
    • 19644388865 scopus 로고    scopus 로고
    • NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites
    • Di Lello, P., et al. 2005. NMR structure of the amino-terminal domain from the Tfb1 subunit of TFIIH and characterization of its phosphoinositide and VP16 binding sites. Biochemistry 44:7678-7686.
    • (2005) Biochemistry , vol.44 , pp. 7678-7686
    • Di Lello, P.1
  • 9
    • 0028360068 scopus 로고
    • Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II
    • Drapkin, R., et al. 1994. Dual role of TFIIH in DNA excision repair and in transcription by RNA polymerase II. Nature 368:769-772.
    • (1994) Nature , vol.368 , pp. 769-772
    • Drapkin, R.1
  • 10
    • 0028077384 scopus 로고
    • The multifunctional TFIIH complex and transcriptional control
    • Drapkin, R., and D. Reinberg. 1994. The multifunctional TFIIH complex and transcriptional control. Trends Biochem. Sci. 19:504-508.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 504-508
    • Drapkin, R.1    Reinberg, D.2
  • 11
    • 33847062553 scopus 로고    scopus 로고
    • The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection
    • Gerrard, S. R., B. H. Bird, C. G. Albarin{ogonek}o, and S. T. Nichol. 2007. The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection. Virology 359:459-465.
    • (2007) Virology , vol.359 , pp. 459-465
    • Gerrard, S.R.1    Bird, B.H.2    Albarino, C.G.3    Nichol, S.T.4
  • 12
    • 3042781670 scopus 로고    scopus 로고
    • A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A
    • Giglia-Mari, G., et al. 2004. A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A. Nat. Genet. 36:714- 719.
    • (2004) Nat. Genet. , vol.36 , pp. 714-719
    • Giglia-Mari, G.1
  • 13
    • 0026053965 scopus 로고
    • Sequences and coding strategies of the S RNAs of Toscana and Rift Valley fever viruses compared to those of Punta Toro, Sicilian sandfly fever, and Uukuniemi viruses
    • Giorgi, C., et al. 1991. Sequences and coding strategies of the S RNAs of Toscana and Rift Valley fever viruses compared to those of Punta Toro, Sicilian sandfly fever, and Uukuniemi viruses. Virology 180:738-753.
    • (1991) Virology , vol.180 , pp. 738-753
    • Giorgi, C.1
  • 14
    • 66149086445 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNA-dependent protein kinase
    • Habjan, M., et al. 2009. NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNA-dependent protein kinase. J. Virol. 83:4365-4375.
    • (2009) J. Virol. , vol.83 , pp. 4365-4375
    • Habjan, M.1
  • 15
    • 0031840672 scopus 로고    scopus 로고
    • Molecular genetics of the RNA polymerase II general transcriptional machinery
    • Hampsey, M. 1998. Molecular genetics of the RNA polymerase II general transcriptional machinery. Microbiol. Mol. Biol. Rev. 62:465-503.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 465-503
    • Hampsey, M.1
  • 16
    • 73949101221 scopus 로고    scopus 로고
    • Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation
    • Harreman, M., et al. 2009. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proc. Natl. Acad. Sci. U. S. A. 106: 20705-20710.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 20705-20710
    • Harreman, M.1
  • 18
    • 0037013144 scopus 로고    scopus 로고
    • TFIIH plays an essential role in RNA polymerase I transcription
    • Iben, S., et al. 2002. TFIIH plays an essential role in RNA polymerase I transcription. Cell 109:297-306.
    • (2002) Cell , vol.109 , pp. 297-306
    • Iben, S.1
  • 19
    • 61449213995 scopus 로고    scopus 로고
    • Rift Valley fever virus NSs protein promotes posttranscriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation
    • Ikegami, T., et al. 2009. Rift Valley fever virus NSs protein promotes posttranscriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation. PLoS Pathog. 5:e1000287.
    • (2009) PLoS Pathog , vol.5
    • Ikegami, T.1
  • 20
    • 33644777662 scopus 로고    scopus 로고
    • Rescue of infectious Rift Valley fever virus entirely from cDNA, analysis of virus lacking the NSs gene, and expression of a foreign gene
    • Ikegami, T., S. Won, C. J. Peters, and S. Makino. 2006. Rescue of infectious Rift Valley fever virus entirely from cDNA, analysis of virus lacking the NSs gene, and expression of a foreign gene. J. Virol. 80:2933-2940.
    • (2006) J. Virol. , vol.80 , pp. 2933-2940
    • Ikegami, T.1    Won, S.2    Peters, C.J.3    Makino, S.4
  • 21
    • 24644488170 scopus 로고    scopus 로고
    • Rift Valley fever virus NSs mRNA is transcribed from an incoming anti-viral-sense S RNA segment
    • Ikegami, T., S. Won, C. J. Peters, and S. Makino. 2005. Rift Valley fever virus NSs mRNA is transcribed from an incoming anti-viral-sense S RNA segment. J. Virol. 79:12106-12111.
    • (2005) J. Virol. , vol.79 , pp. 12106-12111
    • Ikegami, T.1    Won, S.2    Peters, C.J.3    Makino, S.4
  • 22
    • 0041977209 scopus 로고    scopus 로고
    • Improved recovery of rabies virus from cloned cDNA using a vaccinia virus-free reverse genetics system
    • Ito, N., et al. 2003. Improved recovery of rabies virus from cloned cDNA using a vaccinia virus-free reverse genetics system. Microbiol. Immunol. 47:613-617.
    • (2003) Microbiol. Immunol. , vol.47 , pp. 613-617
    • Ito, N.1
  • 23
    • 57349121991 scopus 로고    scopus 로고
    • Exploring RNA transcription and turnover in vivo by using click chemistry
    • Jao, C. Y., and A. Salic. 2008. Exploring RNA transcription and turnover in vivo by using click chemistry. Proc. Natl. Acad. Sci. U. S. A. 105:15779- 15784.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15779-15784
    • Jao, C.Y.1    Salic, A.2
  • 24
    • 0030793104 scopus 로고    scopus 로고
    • The cdk7-cyclin HMAT1 complex associated with TFIIH is localized in coiled bodies
    • Jordan, P., C. Cunha, and M. Carmo-Fonseca. 1997. The cdk7-cyclin HMAT1 complex associated with TFIIH is localized in coiled bodies. Mol. Biol. Cell 8:1207-1217.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1207-1217
    • Jordan, P.1    Cunha, C.2    Carmo-Fonseca, M.3
  • 25
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk, V. I., F. M. Menzies, and D. C. Rubinsztein. 2010. Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett. 584:1393-1398.
    • (2010) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 26
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee, D. H., and A. L. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8:397-403.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 27
    • 1342264311 scopus 로고    scopus 로고
    • TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus
    • Le May, N., et al. 2004. TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus. Cell 116:541-550.
    • (2004) Cell , vol.116 , pp. 541-550
    • Le May, N.1
  • 28
    • 38949091131 scopus 로고    scopus 로고
    • A SAP30 complex inhibits IFN-beta expression in Rift Valley fever virus infected cells
    • Le May, N., et al. 2008. A SAP30 complex inhibits IFN-beta expression in Rift Valley fever virus infected cells. PLoS Pathog. 4:e13.
    • (2008) PLoS Pathog , vol.4
    • Le May, N.1
  • 29
    • 33748936181 scopus 로고    scopus 로고
    • Interaction of Bunyamwera orthobunyavirus NSs protein with mediator protein MED8: a mechanism for inhibiting the interferon response
    • Leonard, V. H., A. Kohl, T. J. Hart, and R. M. Elliott. 2006. Interaction of Bunyamwera orthobunyavirus NSs protein with mediator protein MED8: a mechanism for inhibiting the interferon response. J. Virol. 80:9667-9675.
    • (2006) J. Virol. , vol.80 , pp. 9667-9675
    • Leonard, V.H.1    Kohl, A.2    Hart, T.J.3    Elliott, R.M.4
  • 30
    • 15444361897 scopus 로고    scopus 로고
    • p62, a TFIIH subunit, directly interacts with thyroid hormone receptor and enhances T3-mediated transcription
    • Liu, Y., et al. 2005. p62, a TFIIH subunit, directly interacts with thyroid hormone receptor and enhances T3-mediated transcription. Mol. Endocrinol. 19:879-884.
    • (2005) Mol. Endocrinol. , vol.19 , pp. 879-884
    • Liu, Y.1
  • 31
    • 0026731557 scopus 로고
    • Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II
    • Lu, H., L. Zawel, L. Fisher, J. M. Egly, and D. Reinberg. 1992. Human general transcription factor IIH phosphorylates the C-terminal domain of RNA polymerase II. Nature 358:641-645.
    • (1992) Nature , vol.358 , pp. 641-645
    • Lu, H.1    Zawel, L.2    Fisher, L.3    Egly, J.M.4    Reinberg, D.5
  • 32
    • 0034440598 scopus 로고    scopus 로고
    • Cytopathogenesis and inhibition of host gene expression by RNA viruses
    • Lyles, D. S. 2000. Cytopathogenesis and inhibition of host gene expression by RNA viruses. Microbiol. Mol. Biol. Rev. 64:709-724.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 709-724
    • Lyles, D.S.1
  • 33
    • 0028318159 scopus 로고
    • Leptomycin B targets a regulatory cascade of Crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression
    • Nishi, K., et al. 1994. Leptomycin B targets a regulatory cascade of Crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269:6320-6324.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6320-6324
    • Nishi, K.1
  • 34
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng, E. A., et al. 2006. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107:4907-4916.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1
  • 35
    • 41949104574 scopus 로고    scopus 로고
    • Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH
    • Okuda, M., et al. 2008. Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH. EMBO J. 27:1161-1171.
    • (2008) EMBO J , vol.27 , pp. 1161-1171
    • Okuda, M.1
  • 36
    • 0029846871 scopus 로고    scopus 로고
    • The general transcription factors of RNA polymerase II
    • Orphanides, G., T. Lagrange, and D. Reinberg. 1996. The general transcription factors of RNA polymerase II. Genes Dev. 10:2657-2683.
    • (1996) Genes Dev , vol.10 , pp. 2657-2683
    • Orphanides, G.1    Lagrange, T.2    Reinberg, D.3
  • 37
    • 0030010769 scopus 로고    scopus 로고
    • Subpopulations of proteasomes in rat liver nuclei, microsomes and cytosol
    • Palmer, A., et al. 1996. Subpopulations of proteasomes in rat liver nuclei, microsomes and cytosol. Biochem. J. 316:401-407.
    • (1996) Biochem. J. , vol.316 , pp. 401-407
    • Palmer, A.1
  • 38
    • 77957852165 scopus 로고    scopus 로고
    • Rift Valley fever virus (Bunyaviridae: Phlebovirus): an update on pathogenesis, molecular epidemiology, vectors, diagnostics and prevention
    • Pepin, M., M. Bouloy, B. H. Bird, A. Kemp, and J. Paweska. 2010. Rift Valley fever virus (Bunyaviridae: Phlebovirus): an update on pathogenesis, molecular epidemiology, vectors, diagnostics and prevention. Vet. Res. 41:61.
    • (2010) Vet. Res. , vol.41 , pp. 61
    • Pepin, M.1    Bouloy, M.2    Bird, B.H.3    Kemp, A.4    Paweska, J.5
  • 39
    • 0000697156 scopus 로고
    • J. H. Steele, CRC handbook series in zoonoses, CRC Press, Boca Raton, FL
    • Peters, C. J., and J. M. Meegan. 1981. Viral zoonoses, p. 403-420. In J. H. Steele, CRC handbook series in zoonoses, vol. 1. CRC Press, Boca Raton, FL.
    • (1981) Viral zoonoses , vol.1 , pp. 403-420
    • Peters, C.J.1    Meegan, J.M.2
  • 40
    • 0035577765 scopus 로고    scopus 로고
    • Degradation of p53 by adenovirus E4orf6 and E1B55K proteins occurs via a novel mechanism involving a Cullin-containing complex
    • Querido, E., et al. 2001. Degradation of p53 by adenovirus E4orf6 and E1B55K proteins occurs via a novel mechanism involving a Cullin-containing complex. Genes Dev. 15:3104-3117.
    • (2001) Genes Dev , vol.15 , pp. 3104-3117
    • Querido, E.1
  • 42
    • 0035312713 scopus 로고    scopus 로고
    • Different dynamics in nuclear entry of subunits of the repair/transcription factor TFIIH
    • Santagati, F., E. Botta, M. Stefanini, and A. M. Pedrini. 2001. Different dynamics in nuclear entry of subunits of the repair/transcription factor TFIIH. Nucleic Acids Res. 29:1574-1581.
    • (2001) Nucleic Acids Res , vol.29 , pp. 1574-1581
    • Santagati, F.1    Botta, E.2    Stefanini, M.3    Pedrini, A.M.4
  • 43
    • 0031444684 scopus 로고    scopus 로고
    • Competent transcription initiation by RNA polymerase II in cell-free extracts from xeroderma pigmentosum groups B and D in an optimized RNA transcription assay
    • Satoh, M. S., and P. C. Hanawalt. 1997. Competent transcription initiation by RNA polymerase II in cell-free extracts from xeroderma pigmentosum groups B and D in an optimized RNA transcription assay. Biochim. Biophys. Acta 1354:241-251.
    • (1997) Biochim. Biophys. Acta , vol.1354 , pp. 241-251
    • Satoh, M.S.1    Hanawalt, P.C.2
  • 44
    • 0034268691 scopus 로고    scopus 로고
    • Molecular structure of human TFIIH
    • Schultz, P., et al. 2000. Molecular structure of human TFIIH. Cell 102:599- 607.
    • (2000) Cell , vol.102 , pp. 599-607
    • Schultz, P.1
  • 45
    • 0021364902 scopus 로고
    • Protein synthesis in Rift Valley fever virus-infected cells
    • Struthers, J. K., R. Swanepoel, and S. P. Shepherd. 1984. Protein synthesis in Rift Valley fever virus-infected cells. Virology 134:118-124.
    • (1984) Virology , vol.134 , pp. 118-124
    • Struthers, J.K.1    Swanepoel, R.2    Shepherd, S.P.3
  • 46
    • 0025218786 scopus 로고
    • Expression strategy of a phlebovirus: biogenesis of proteins from the Rift Valley fever virus M segment
    • Suzich, J. A., L. T. Kakach, and M. S. Collett. 1990. Expression strategy of a phlebovirus: biogenesis of proteins from the Rift Valley fever virus M segment. J. Virol. 64:1549-1555.
    • (1990) J. Virol. , vol.64 , pp. 1549-1555
    • Suzich, J.A.1    Kakach, L.T.2    Collett, M.S.3
  • 47
    • 29644444370 scopus 로고    scopus 로고
    • J. A. W. Coetzer, G. R. Thompson, R. D. Tustin, et al. (ed.), Infectious diseases of livestock with special reference to Southern Africa, 2nd ed. Oxford University Press, Cape Town, South Africa
    • Swanepoel, R., and J. A. W. Coetzer. 2004. Rift Valley fever, p. 1037-1070. In J. A. W. Coetzer, G. R. Thompson, R. D. Tustin, et al. (ed.), Infectious diseases of livestock with special reference to Southern Africa, 2nd ed. Oxford University Press, Cape Town, South Africa.
    • (2004) Rift Valley fever , pp. 1037-1070
    • Swanepoel, R.1    Coetzer, J.A.W.2
  • 48
    • 0033010723 scopus 로고    scopus 로고
    • Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7
    • Tirode, F., D. Busso, F. Coin, and J. M. Egly. 1999. Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7. Mol. Cell 3:87-95.
    • (1999) Mol. Cell , vol.3 , pp. 87-95
    • Tirode, F.1    Busso, D.2    Coin, F.3    Egly, J.M.4
  • 49
    • 0033982965 scopus 로고    scopus 로고
    • The S segment of Rift Valley fever phlebovirus (Bunyaviridae) carries determinants for attenuation and virulence in mice
    • Vialat, P., A. Billecocq, A. Kohl, and M. Bouloy. 2000. The S segment of Rift Valley fever phlebovirus (Bunyaviridae) carries determinants for attenuation and virulence in mice. J. Virol. 74:1538-1543.
    • (2000) J. Virol , vol.74 , pp. 1538-1543
    • Vialat, P.1    Billecocq, A.2    Kohl, A.3    Bouloy, M.4
  • 50
    • 0031079648 scopus 로고    scopus 로고
    • Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA
    • Wolff, B., J. J. Sanglier, and Y. Wang. 1997. Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem. Biol. 4:139-147.
    • (1997) Chem. Biol , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 51
    • 33746784160 scopus 로고    scopus 로고
    • NSm and 78-kilodalton proteins of Rift Valley fever virus are nonessential for viral replication in cell culture
    • Won, S., T. Ikegami, C. J. Peters, and S. Makino. 2006. NSm and 78-kilodalton proteins of Rift Valley fever virus are nonessential for viral replication in cell culture. J. Virol. 80:8274-8278.
    • (2006) J. Virol. , vol.80 , pp. 8274-8278
    • Won, S.1    Ikegami, T.2    Peters, C.J.3    Makino, S.4
  • 52
    • 0033061218 scopus 로고    scopus 로고
    • The carboxy-terminal acidic domain of Rift Valley fever virus NSs protein is essential for the formation of filamentous structures but not for the nuclear localization of the protein
    • Yadani, F. Z., A. Kohl, C. Prehaud, A. Billecocq, and M. Bouloy. 1999. The carboxy-terminal acidic domain of Rift Valley fever virus NSs protein is essential for the formation of filamentous structures but not for the nuclear localization of the protein. J. Virol. 73:5018-5025.
    • (1999) J. Virol. , vol.73 , pp. 5018-5025
    • Yadani, F.Z.1    Kohl, A.2    Prehaud, C.3    Billecocq, A.4    Bouloy, M.5
  • 53
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • Yu, X., et al. 2003. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 302:1056-1060.
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1
  • 54
    • 72849150471 scopus 로고    scopus 로고
    • Rift Valley fever virus L protein forms a biologically active oligomer
    • Zamoto-Niikura, A., K. Terasaki, T. Ikegami, C. J. Peters, and S. Makino. 2009. Rift Valley fever virus L protein forms a biologically active oligomer. J. Virol. 83:12779-12789.
    • (2009) J. Virol , vol.83 , pp. 12779-12789
    • Zamoto-Niikura, A.1    Terasaki, K.2    Ikegami, T.3    Peters, C.J.4    Makino, S.5
  • 55
    • 33745844503 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in health and disease
    • Zhao, L., and S. L. Ackerman. 2006. Endoplasmic reticulum stress in health and disease. Curr. Opin. Cell Biol. 18:444-452.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 444-452
    • Zhao, L.1    Ackerman, S.L.2
  • 56
    • 0141561892 scopus 로고    scopus 로고
    • The transcriptional complexity of the TFIIH complex
    • Zurita, M., and C. Merino. 2003. The transcriptional complexity of the TFIIH complex. Trends Genet. 19:578-584.
    • (2003) Trends Genet , vol.19 , pp. 578-584
    • Zurita, M.1    Merino, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.