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Volumn 155, Issue 1, 2011, Pages 240-248

Structure-based design of NS2 mutants for attenuated influenza A virus vaccines

Author keywords

Influenza A virus; NS2 NEP; Polymerase activity; Reverse genetics; Virulence

Indexed keywords

AMINO ACID; GLUTAMIC ACID; INFLUENZA VACCINE; NONSTRUCTURAL PROTEIN 1; NONSTRUCTURAL PROTEIN 2; VIRUS PROTEIN;

EID: 78650544136     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2010.10.014     Document Type: Article
Times cited : (18)

References (63)
  • 1
    • 0141737104 scopus 로고    scopus 로고
    • Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)
    • Akarsu H., Burmeister W.P., Petosa C., Petit I., Muller C.W., Ruigrok R.W., Baudin F. Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2). EMBO J. 2003, 22:4646-4655.
    • (2003) EMBO J. , vol.22 , pp. 4646-4655
    • Akarsu, H.1    Burmeister, W.P.2    Petosa, C.3    Petit, I.4    Muller, C.W.5    Ruigrok, R.W.6    Baudin, F.7
  • 2
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali A., Avalos R.T., Ponimaskin E., Nayak D.P. Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J. Virol. 2000, 74:8709-8719.
    • (2000) J. Virol. , vol.74 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 3
    • 0033838456 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus
    • Aragon T., de la Luna S., Novoa I., Carrasco L., Ortin J., Nieto A. Eukaryotic translation initiation factor 4GI is a cellular target for NS1 protein, a translational activator of influenza virus. Mol. Cell. Biol. 2000, 20:6259-6268.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6259-6268
    • Aragon, T.1    de la Luna, S.2    Novoa, I.3    Carrasco, L.4    Ortin, J.5    Nieto, A.6
  • 4
    • 0035864293 scopus 로고    scopus 로고
    • Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer
    • Arzt S., Baudin F., Barge A., Timmins P., Burmeister W.P., Ruigrok R.W. Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer. Virology 2001, 279:439-446.
    • (2001) Virology , vol.279 , pp. 439-446
    • Arzt, S.1    Baudin, F.2    Barge, A.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6
  • 5
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin F., Petit I., Weissenhorn W., Ruigrok R.W. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 2001, 281:102-108.
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 7
    • 33846822057 scopus 로고    scopus 로고
    • Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes
    • Boulo S., Akarsu H., Ruigrok R.W., Baudin F. Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes. Virus Res. 2007, 124:12-21.
    • (2007) Virus Res. , vol.124 , pp. 12-21
    • Boulo, S.1    Akarsu, H.2    Ruigrok, R.W.3    Baudin, F.4
  • 8
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui M., Wills E.G., Helenius A., Whittaker G.R. Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J. Virol. 2000, 74:1781-1786.
    • (2000) J. Virol. , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 9
    • 0035042067 scopus 로고    scopus 로고
    • Influenza A virus NEP (NS2 protein) downregulates RNA synthesis of model template RNAs
    • Bullido R., Gomez-Puertas P., Saiz M.J., Portela A. Influenza A virus NEP (NS2 protein) downregulates RNA synthesis of model template RNAs. J. Virol. 2001, 75:4912-4917.
    • (2001) J. Virol. , vol.75 , pp. 4912-4917
    • Bullido, R.1    Gomez-Puertas, P.2    Saiz, M.J.3    Portela, A.4
  • 10
    • 0346121589 scopus 로고    scopus 로고
    • PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes
    • Burgui I., Aragon T., Ortin J., Nieto A. PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes. J. Gen. Virol. 2003, 84:3263-3274.
    • (2003) J. Gen. Virol. , vol.84 , pp. 3263-3274
    • Burgui, I.1    Aragon, T.2    Ortin, J.3    Nieto, A.4
  • 11
    • 11144244386 scopus 로고    scopus 로고
    • Influenza A viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes
    • Burleigh L.M., Calder L.J., Skehel J.J., Steinhauer D.A. Influenza A viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes. J. Virol. 2005, 79:1262-1270.
    • (2005) J. Virol. , vol.79 , pp. 1262-1270
    • Burleigh, L.M.1    Calder, L.J.2    Skehel, J.J.3    Steinhauer, D.A.4
  • 12
    • 0033560753 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery
    • Chen Z., Li Y., Krug R.M. Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery. EMBO J. 1999, 18:2273-2283.
    • (1999) EMBO J. , vol.18 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 13
    • 0028923921 scopus 로고
    • Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs
    • de la Luna S., Fortes P., Beloso A., Ortin J. Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs. J. Virol. 1995, 69:2427-2433.
    • (1995) J. Virol. , vol.69 , pp. 2427-2433
    • de la Luna, S.1    Fortes, P.2    Beloso, A.3    Ortin, J.4
  • 14
    • 0030749976 scopus 로고    scopus 로고
    • Influenza virus M1 protein binds to RNA through its nuclear localization signal
    • Elster C., Larsen K., Gagnon J., Ruigrok R.W.H., Baudin F. Influenza virus M1 protein binds to RNA through its nuclear localization signal. J. Gen. Virol. 1997, 78:1589-1596.
    • (1997) J. Gen. Virol. , vol.78 , pp. 1589-1596
    • Elster, C.1    Larsen, K.2    Gagnon, J.3    Ruigrok, R.W.H.4    Baudin, F.5
  • 15
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J., Digard P. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J. Virol. 2001, 75:408-419.
    • (2001) J. Virol. , vol.75 , pp. 408-419
    • Elton, D.1    Simpson-Holley, M.2    Archer, K.3    Medcalf, L.4    Hallam, R.5    McCauley, J.6    Digard, P.7
  • 16
    • 0028055149 scopus 로고
    • Influenza virus NS1 protein stimulates translation of the M1 protein
    • Enami K., Sato T.A., Nakada S., Enami M. Influenza virus NS1 protein stimulates translation of the M1 protein. J. Virol. 1994, 68:1432-1437.
    • (1994) J. Virol. , vol.68 , pp. 1432-1437
    • Enami, K.1    Sato, T.A.2    Nakada, S.3    Enami, M.4
  • 17
    • 0029794377 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein
    • Enami M., Enami K. Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein. J. Virol. 1996, 70:6653-6657.
    • (1996) J. Virol. , vol.70 , pp. 6653-6657
    • Enami, M.1    Enami, K.2
  • 18
    • 0028008470 scopus 로고
    • Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport
    • Fortes P., Beloso A., Ortin J. Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport. EMBO J. 1994, 13:704-712.
    • (1994) EMBO J. , vol.13 , pp. 704-712
    • Fortes, P.1    Beloso, A.2    Ortin, J.3
  • 19
    • 0021815906 scopus 로고
    • Expression of influenza virus NS2 nonstructural protein in bacteria and localization of NS2 in infected eucaryotic cells
    • Greenspan D., Krystal M., Nakada S., Arnheiter H., Lyles D.S., Palese P. Expression of influenza virus NS2 nonstructural protein in bacteria and localization of NS2 in infected eucaryotic cells. J. Virol. 1985, 54:833-843.
    • (1985) J. Virol. , vol.54 , pp. 833-843
    • Greenspan, D.1    Krystal, M.2    Nakada, S.3    Arnheiter, H.4    Lyles, D.S.5    Palese, P.6
  • 20
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale B.G., Randall R.E., Ortín J., Jackson D. The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol. 2008, 89:2359-2376.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortín, J.3    Jackson, D.4
  • 21
    • 0032980412 scopus 로고    scopus 로고
    • Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells
    • Hatada E., Saito S., Fukuda R. Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J. Virol. 1999, 73:2425-2433.
    • (1999) J. Virol. , vol.73 , pp. 2425-2433
    • Hatada, E.1    Saito, S.2    Fukuda, R.3
  • 22
    • 0018648729 scopus 로고
    • The smallest genome RNA segment of influenza virus contains two genes that may overlap
    • Inglis S.C., Barrett T., Brown C.M., Almond J.W. The smallest genome RNA segment of influenza virus contains two genes that may overlap. Proc. Natl. Acad. Sci. U.S.A. 1979, 76:3790-3794.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 3790-3794
    • Inglis, S.C.1    Barrett, T.2    Brown, C.M.3    Almond, J.W.4
  • 23
    • 4444372435 scopus 로고    scopus 로고
    • Generation of influenza A virus NS2 (NEP) mutants with an altered nuclear export signal sequence
    • Iwatsuki-Horimoto K., Horimoto T., Fujii Y., Kawaoka Y. Generation of influenza A virus NS2 (NEP) mutants with an altered nuclear export signal sequence. J. Virol. 2004, 78:10149-10155.
    • (2004) J. Virol. , vol.78 , pp. 10149-10155
    • Iwatsuki-Horimoto, K.1    Horimoto, T.2    Fujii, Y.3    Kawaoka, Y.4
  • 25
    • 41949123710 scopus 로고    scopus 로고
    • A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity
    • Jackson D., Hossain M.J., Hickman D., Perez D.R., Lamb R.A. A new influenza virus virulence determinant: the NS1 protein four C-terminal residues modulate pathogenicity. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:4381-4386.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 4381-4386
    • Jackson, D.1    Hossain, M.J.2    Hickman, D.3    Perez, D.R.4    Lamb, R.A.5
  • 26
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin H., Leser G.P., Zhang J., Lamb R.A. Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J. 1997, 16:1236-1247.
    • (1997) EMBO J. , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 27
    • 0037162502 scopus 로고    scopus 로고
    • Human influenza viruses activate an interferon-independent transcription of cellular antiviral genes: outcome with influenza A virus is unique
    • Kim M.J., Latham A.G., Krug R.M. Human influenza viruses activate an interferon-independent transcription of cellular antiviral genes: outcome with influenza A virus is unique. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:10096-10101.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10096-10101
    • Kim, M.J.1    Latham, A.G.2    Krug, R.M.3
  • 28
    • 0030796172 scopus 로고    scopus 로고
    • Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks
    • Kobasa D., Rogeres M.E., Wells K., Kawaoka Y. Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J. Virol. 1997, 71:6706-6713.
    • (1997) J. Virol. , vol.71 , pp. 6706-6713
    • Kobasa, D.1    Rogeres, M.E.2    Wells, K.3    Kawaoka, Y.4
  • 29
    • 0037565268 scopus 로고    scopus 로고
    • Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein
    • Krug R.M., Yuan W., Noah D.L., Latham A.G. Intracellular warfare between human influenza viruses and human cells: the roles of the viral NS1 protein. Virology 2003, 309:181-189.
    • (2003) Virology , vol.309 , pp. 181-189
    • Krug, R.M.1    Yuan, W.2    Noah, D.L.3    Latham, A.G.4
  • 30
    • 0020696905 scopus 로고
    • The gene structure and replication of influenza virus
    • Lamb R.A., Choppin P.W. The gene structure and replication of influenza virus. Annu. Rev. Biochem. 1983, 52:467-506.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 467-506
    • Lamb, R.A.1    Choppin, P.W.2
  • 31
    • 0004787450 scopus 로고
    • Mapping of the two overlapping genes for polypeptides NS1 and NS2 on RNA segment 8 of influenza virus genome
    • Lamb R.A., Choppin P.W., Chanock R.M., Lai C.J. Mapping of the two overlapping genes for polypeptides NS1 and NS2 on RNA segment 8 of influenza virus genome. Proc. Natl. Acad. Sci. U.S.A. 1980, 77:1857-1861.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1857-1861
    • Lamb, R.A.1    Choppin, P.W.2    Chanock, R.M.3    Lai, C.J.4
  • 32
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor
    • Lu Y., Wambach M., Katze M.G., Krug R.M. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor. Virology 1995, 214:222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 33
    • 34249785982 scopus 로고    scopus 로고
    • Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes
    • Melen K., Kinnunen L., Fagerlund R., Ikonen N., Twu K.Y., Krug R.M., Julkunen I. Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J. Virol. 2007, 81:5995-6006.
    • (2007) J. Virol. , vol.81 , pp. 5995-6006
    • Melen, K.1    Kinnunen, L.2    Fagerlund, R.3    Ikonen, N.4    Twu, K.Y.5    Krug, R.M.6    Julkunen, I.7
  • 34
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • Nayak D.P., Hui E.K., Barman S. Assembly and budding of influenza virus. Virus Res. 2004, 106:147-165.
    • (2004) Virus Res. , vol.106 , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.2    Barman, S.3
  • 35
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30kDa subunit of CPSF and inhibits 3' end formation of cellular pre-mRNAs
    • Nemeroff M.E., Barabino S.M., Li Y., Keller W., Krug R.M. Influenza virus NS1 protein interacts with the cellular 30kDa subunit of CPSF and inhibits 3' end formation of cellular pre-mRNAs. Mol. Cell 1998, 1:991-1000.
    • (1998) Mol. Cell , vol.1 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 36
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1
    • Neumann G., Hughes M.T., Kawaoka Y. Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J. 2000, 19:6751-6758.
    • (2000) EMBO J. , vol.19 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 38
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa H., Yamamura K., Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 1991, 108:193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 39
    • 31444441789 scopus 로고    scopus 로고
    • Architecture of ribonucleoprotein complexes in influenza A virus particles
    • Noda T., Sagara H., Yen A., Takada A., Kida H., Cheng R.H., Kawaoka Y. Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 2006, 439:490-492.
    • (2006) Nature , vol.439 , pp. 490-492
    • Noda, T.1    Sagara, H.2    Yen, A.3    Takada, A.4    Kida, H.5    Cheng, R.H.6    Kawaoka, Y.7
  • 40
    • 34547584458 scopus 로고    scopus 로고
    • Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions
    • Noton S.L., Medcalf E., Fisher D., Mullin A.E., Elton D., Digard P. Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J. Gen. Virol. 2007, 88:2280-2290.
    • (2007) J. Gen. Virol. , vol.88 , pp. 2280-2290
    • Noton, S.L.1    Medcalf, E.2    Fisher, D.3    Mullin, A.E.4    Elton, D.5    Digard, P.6
  • 42
    • 0025311124 scopus 로고
    • Mutation in NS2, a nonstructural protein of influenza A virus, extragenically causes aberrant replication and expression of the PA gene and leads to generation of defective interfering particles
    • Odagiri T., Tobita K. Mutation in NS2, a nonstructural protein of influenza A virus, extragenically causes aberrant replication and expression of the PA gene and leads to generation of defective interfering particles. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:5988-5992.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5988-5992
    • Odagiri, T.1    Tobita, K.2
  • 43
    • 0028089192 scopus 로고
    • An amino acid change in the non-structural NS2 protein of an influenza A virus mutant is responsible for the generation of defective interfering (DI) particles by amplifying DI RNAs and suppressing complementary RNA synthesis
    • Odagiri T., Tominaga K., Tobita K., Ohta S. An amino acid change in the non-structural NS2 protein of an influenza A virus mutant is responsible for the generation of defective interfering (DI) particles by amplifying DI RNAs and suppressing complementary RNA synthesis. J. Gen. Virol. 1994, 75(Pt 1):43-53.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 1 , pp. 43-53
    • Odagiri, T.1    Tominaga, K.2    Tobita, K.3    Ohta, S.4
  • 44
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill R.E., Talon J., Palese P. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 1998, 17:288-296.
    • (1998) EMBO J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 45
    • 0028880783 scopus 로고
    • Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation
    • Park Y.W., Katze M.G. Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation. J. Biol. Chem. 1995, 270:28433-28439.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28433-28439
    • Park, Y.W.1    Katze, M.G.2
  • 46
    • 0000075974 scopus 로고    scopus 로고
    • Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1
    • Park Y.W., Wilusz J., Katze M.G. Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:6694-6699.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6694-6699
    • Park, Y.W.1    Wilusz, J.2    Katze, M.G.3
  • 47
    • 0032530138 scopus 로고    scopus 로고
    • The matrix 1 protein of influenza A virus inhibits the transcriptase activity of a model influenza reporter genome in vivo
    • Perez D.R., Donis R.O. The matrix 1 protein of influenza A virus inhibits the transcriptase activity of a model influenza reporter genome in vivo. Virology 1998, 249:52-61.
    • (1998) Virology , vol.249 , pp. 52-61
    • Perez, D.R.1    Donis, R.O.2
  • 49
    • 0025924358 scopus 로고
    • NS2 protein of influenza virus is found in purified virus and phosphorylated in infected cells
    • Richardson J.C., Akkina R.K. NS2 protein of influenza virus is found in purified virus and phosphorylated in infected cells. Arch. Virol. 1991, 116:69-80.
    • (1991) Arch. Virol. , vol.116 , pp. 69-80
    • Richardson, J.C.1    Akkina, R.K.2
  • 50
    • 0001927825 scopus 로고
    • Clinical influenza virus and the embryonated hen's eggs
    • Robertson J.S. Clinical influenza virus and the embryonated hen's eggs. Rev. Med. Virol. 1993, 3:97-108.
    • (1993) Rev. Med. Virol. , vol.3 , pp. 97-108
    • Robertson, J.S.1
  • 51
    • 67649227447 scopus 로고    scopus 로고
    • NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
    • Robb N.C., Smith M., Vreede F.T., Fodor E. NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J. Gen. Virol. 2009, 90:1398-1407.
    • (2009) J. Gen. Virol. , vol.90 , pp. 1398-1407
    • Robb, N.C.1    Smith, M.2    Vreede, F.T.3    Fodor, E.4
  • 52
    • 0028916010 scopus 로고
    • Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein forms structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles
    • Ruigrok R.W., Baudin F. Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein forms structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles. J. Gen. Virol. 1995, 76(Pt 4):1009-1014.
    • (1995) J. Gen. Virol. , vol.76 , Issue.PART 4 , pp. 1009-1014
    • Ruigrok, R.W.1    Baudin, F.2
  • 54
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha B., Luo M. Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nat. Struct. Biol. 1997, 4:239-244.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 55
    • 0023433327 scopus 로고
    • Synthesis and cellular location of the ten influenza polypeptides individually expressed by recombinant vaccinia viruses
    • Smith G.L., Levin J.Z., Palese P., Moss B. Synthesis and cellular location of the ten influenza polypeptides individually expressed by recombinant vaccinia viruses. Virology 1987, 160:336-345.
    • (1987) Virology , vol.160 , pp. 336-345
    • Smith, G.L.1    Levin, J.Z.2    Palese, P.3    Moss, B.4
  • 56
    • 0344015773 scopus 로고    scopus 로고
    • Multiple alignment comparison of the non-structural genes of influenza A viruses
    • Suarez D.L., Perdue M.L. Multiple alignment comparison of the non-structural genes of influenza A viruses. Virus Res. 1998, 54:59-69.
    • (1998) Virus Res. , vol.54 , pp. 59-69
    • Suarez, D.L.1    Perdue, M.L.2
  • 57
    • 0031670374 scopus 로고    scopus 로고
    • Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase
    • Tan S.L., Katze M.G. Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase. J. Interferon Cytokine Res. 1998, 18:757-766.
    • (1998) J. Interferon Cytokine Res. , vol.18 , pp. 757-766
    • Tan, S.L.1    Katze, M.G.2
  • 59
    • 0029656043 scopus 로고    scopus 로고
    • Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein
    • Watanabe K., Handa H., Mizumoto K., Nagata K. Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein. J. Virol. 1996, 70:241-247.
    • (1996) J. Virol. , vol.70 , pp. 241-247
    • Watanabe, K.1    Handa, H.2    Mizumoto, K.3    Nagata, K.4
  • 60
    • 0027236576 scopus 로고
    • Molecular assembly of influenza virus: association of the NS2 protein with virion matrix
    • Yasuda J., Nakada S., Kato A., Toyoda T., Ishihama A. Molecular assembly of influenza virus: association of the NS2 protein with virion matrix. Virology 1993, 196:249-255.
    • (1993) Virology , vol.196 , pp. 249-255
    • Yasuda, J.1    Nakada, S.2    Kato, A.3    Toyoda, T.4    Ishihama, A.5
  • 61
    • 0024319381 scopus 로고
    • Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotype antibodies and synthetic peptides
    • Ye Z., Baylor N.W., Wagner R.R. Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotype antibodies and synthetic peptides. J. Virol. 1989, 63:3586-3594.
    • (1989) J. Virol. , vol.63 , pp. 3586-3594
    • Ye, Z.1    Baylor, N.W.2    Wagner, R.R.3
  • 62
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye Z., Liu T., Offringa D.P., McInnis J., Levandowski R.A. Association of influenza virus matrix protein with ribonucleoproteins. J. Virol. 1999, 73:7467-7473.
    • (1999) J. Virol. , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5
  • 63
    • 0018877089 scopus 로고
    • Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine
    • Zvonarjev A.Y., Ghendon Y.Z. Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine. J. Virol. 1980, 33:583-586.
    • (1980) J. Virol. , vol.33 , pp. 583-586
    • Zvonarjev, A.Y.1    Ghendon, Y.Z.2


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