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Volumn 80, Issue 12, 2006, Pages 5697-5707

Mutations in influenza virus M1 CCHH, the putative zinc finger motif, cause attenuation in mice and protect mice against lethal influenza virus infection

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CHICKEN; CONTROLLED STUDY; EGG; FEMALE; HUMAN; HUMAN CELL; INFLUENZA; INFLUENZA VIRUS; LETHALITY; LUNG ALVEOLUS CELL; MORBIDITY; MORTALITY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; UNINDEXED SEQUENCE; VIROGENESIS; VIRUS CELL INTERACTION; VIRUS MUTANT; VIRUS MUTATION; VIRUS REPLICATION; VIRUS VIRULENCE; WILD TYPE; ZINC FINGER MOTIF;

EID: 33744904964     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02729-05     Document Type: Article
Times cited : (14)

References (76)
  • 1
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali, A., R. T. Avalos, E. Ponimaskin, and D. P. Nayak. 2000. Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein. J. Virol. 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
  • 2
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin, F., I. Petit, W. Weissenhorn, and R. W. H. Ruigrok. 2001. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281:102-108.
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.H.4
  • 3
    • 0019513851 scopus 로고
    • Proteolytic cleavage of influenza virus hemagglutinins: Primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses
    • Bosch, F. X., W. Garten, H.-D. Klenk, and R. Rott. 1981. Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of avian influenza viruses. Virology 113:725-735.
    • (1981) Virology , vol.113 , pp. 725-735
    • Bosch, F.X.1    Garten, W.2    Klenk, H.-D.3    Rott, R.4
  • 4
    • 0035811003 scopus 로고    scopus 로고
    • Pattern of mutation in the genome of influenza a virus on adaptation to increased virulence in the mouse lung: Identification of functional themes
    • Brown, E., H. Liu, L. Kit, S. Baird, and M. Nesrallah. 2001. Pattern of mutation in the genome of influenza A virus on adaptation to increased virulence in the mouse lung: identification of functional themes. Proc. Natl. Acad. Sci. USA 98:6883-6888.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6883-6888
    • Brown, E.1    Liu, H.2    Kit, L.3    Baird, S.4    Nesrallah, M.5
  • 5
    • 23744512890 scopus 로고    scopus 로고
    • Role of apoptosis and cytokines in influenza virus morbidity
    • Brydon, E. W. A., S. J. Morris, and C. Sweet. 2005. Role of apoptosis and cytokines in influenza virus morbidity. FEMS Microbiol. Rev. 29:837-850.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 837-850
    • Brydon, E.W.A.1    Morris, S.J.2    Sweet, C.3
  • 6
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui, M., G. Whittaker, and A. Helenius. 1996. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 70:8391-8401.
    • (1996) J. Virol. , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 7
    • 0027397591 scopus 로고
    • Biologic importance of influenza virus stalk length in influenza a virus NA
    • Castrucci, M. R., and Y. Kawaoka. 1993. Biologic importance of influenza virus stalk length in influenza A virus NA. J. Virol. 67:759-764.
    • (1993) J. Virol. , vol.67 , pp. 759-764
    • Castrucci, M.R.1    Kawaoka, Y.2
  • 8
    • 0031782812 scopus 로고    scopus 로고
    • Type 1 interferons: Expression and signalization
    • Doly, J., A. Civas, S. Navarro, and G. Uze. 1997. Type 1 interferons: expression and signalization. Cell. Mol. Life Sci. 54:1109-1121.
    • (1997) Cell. Mol. Life Sci. , vol.54 , pp. 1109-1121
    • Doly, J.1    Civas, A.2    Navarro, S.3    Uze, G.4
  • 9
    • 0028082049 scopus 로고
    • A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction
    • Elster, C., E. Fourest, F. Baudin, K. Larsen, S. Cusack, and R. W. H. Ruigrok. 1994. A small percentage of influenza virus M1 protein contains zinc but zinc does not influence in vitro M1-RNA interaction. J. Gen. Virol. 75:37-42.
    • (1994) J. Gen. Virol. , vol.75 , pp. 37-42
    • Elster, C.1    Fourest, E.2    Baudin, F.3    Larsen, K.4    Cusack, S.5    Ruigrok, R.W.H.6
  • 10
    • 27744599754 scopus 로고    scopus 로고
    • The factors of virulence of influenza a virus
    • Fislová, T., and F. Kostolanský. 2005. The factors of virulence of influenza A virus. Acta Virol. 49:147-157.
    • (2005) Acta Virol. , vol.49 , pp. 147-157
    • Fislová, T.1    Kostolanský, F.2
  • 11
    • 0036432812 scopus 로고    scopus 로고
    • Mutational analysis of the Sendai virus V protein: Importance of the conserved residues for Zn binding, virus pathogenesis, and efficient RNA editing
    • Fukuhara, N., C. Huang, K. Klyotani, T. Yoshida, and T. Sakaguchi. 2002. Mutational analysis of the Sendai virus V protein: importance of the conserved residues for Zn binding, virus pathogenesis, and efficient RNA editing. Virology 299:172-181.
    • (2002) Virology , vol.299 , pp. 172-181
    • Fukuhara, N.1    Huang, C.2    Klyotani, K.3    Yoshida, T.4    Sakaguchi, T.5
  • 13
    • 0035864298 scopus 로고    scopus 로고
    • Inhibition of interferon-mediated antiviral responses by influenza a viruses and other negative-strand RNA viruses
    • García-Sastre, A. 2001. Inhibition of interferon-mediated antiviral responses by influenza A viruses and other negative-strand RNA viruses. Virology 279:375-384.
    • (2001) Virology , vol.279 , pp. 375-384
    • García-Sastre, A.1
  • 15
    • 0033795196 scopus 로고    scopus 로고
    • Interferons: Cell signalling, immune modulation, antiviral responses and virus countermeasures
    • Goodbourn, S., L. Didcock, and R. E. Randall. 2000. Interferons: cell signalling, immune modulation, antiviral responses and virus countermeasures. J. Gen. Virol. 81:2341-2364.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2341-2364
    • Goodbourn, S.1    Didcock, L.2    Randall, R.E.3
  • 16
    • 0033674543 scopus 로고    scopus 로고
    • Amino acid changes in the hemagglutinin and matrix proteins of influenza a (H2) viruses adapted to mice
    • Govorkova, E. A., A. S. Gambaryan, E. C. Claas, and Y. A. Smirnov. 2000. Amino acid changes in the hemagglutinin and matrix proteins of influenza A (H2) viruses adapted to mice. Acta Virol. 44:241-248.
    • (2000) Acta Virol. , vol.44 , pp. 241-248
    • Govorkova, E.A.1    Gambaryan, A.S.2    Claas, E.C.3    Smirnov, Y.A.4
  • 17
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza a viruses
    • Hatta, M., P. Gao, P. Halfmann, and Y. Kawaoka. 2001. Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293:1840-1842.
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 18
    • 0036645752 scopus 로고    scopus 로고
    • The continued pandemic threat posed by avian influenza viruses in Hong Kong
    • Hatta, M., and Y. Kawaoka. 2002. The continued pandemic threat posed by avian influenza viruses in Hong Kong. Trends Microbiol. 10:340-344.
    • (2002) Trends Microbiol. , vol.10 , pp. 340-344
    • Hatta, M.1    Kawaoka, Y.2
  • 19
    • 0026703488 scopus 로고
    • A kinetic study of immune mediators in the lungs of mice infected with influenza a virus
    • Hennet, T., H. J. Ziltener, J. Frei, and E. Peterhans. 1992. A kinetic study of immune mediators in the lungs of mice infected with influenza A virus. J. Immunol. 149:932-939.
    • (1992) J. Immunol. , vol.149 , pp. 932-939
    • Hennet, T.1    Ziltener, H.J.2    Frei, J.3    Peterhans, E.4
  • 21
    • 33144460942 scopus 로고    scopus 로고
    • YRKL sequence of influenza virus Ml functions as the L domain motif and interacts with VPS28 and Cdc42
    • Hui, E. K.-W., S. Barman, D. H.-P. Tang, B. France, and D. P. Nayak. 2006. YRKL sequence of influenza virus Ml functions as the L domain motif and interacts with VPS28 and Cdc42. J. Virol. 80:2291-2308.
    • (2006) J. Virol. , vol.80 , pp. 2291-2308
    • Hui, E.K.-W.1    Barman, S.2    Tang, D.H.-P.3    France, B.4    Nayak, D.P.5
  • 22
    • 0038618682 scopus 로고    scopus 로고
    • Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs
    • Hui, E. K.-W., S. Barman, T. Y. Yang, and D. P. Nayak. 2003. Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs. J. Virol. 77:7078-7092.
    • (2003) J. Virol. , vol.77 , pp. 7078-7092
    • Hui, E.K.-W.1    Barman, S.2    Yang, T.Y.3    Nayak, D.P.4
  • 23
    • 0035950932 scopus 로고    scopus 로고
    • Role of ATP in influenza virus budding
    • Hui, E. K.-W., and D. P. Nayak. 2001. Role of ATP in influenza virus budding. Virology 290:329-341.
    • (2001) Virology , vol.290 , pp. 329-341
    • Hui, E.K.-W.1    Nayak, D.P.2
  • 24
    • 0036937194 scopus 로고    scopus 로고
    • Role of G protein and protein kinase signalling in influenza virus budding in MDCK cells
    • Hui, E. K.-W., and D. P. Nayak. 2002. Role of G protein and protein kinase signalling in influenza virus budding in MDCK cells. J. Gen. Virol. 83:3055-3066.
    • (2002) J. Gen. Virol. , vol.83 , pp. 3055-3066
    • Hui, E.K.-W.1    Nayak, D.P.2
  • 25
    • 0242320341 scopus 로고    scopus 로고
    • Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza a virus M1 protein are not critical for influenza virus replication
    • Hui, E. K.-W., K. Ralston, A. K. Judd, and D. P. Nayak. 2003. Conserved cysteine and histidine residues in the putative zinc finger motif of the influenza A virus M1 protein are not critical for influenza virus replication. J. Gen. Virol. 84:3105-3113.
    • (2003) J. Gen. Virol. , vol.84 , pp. 3105-3113
    • Hui, E.K.-W.1    Ralston, K.2    Judd, A.K.3    Nayak, D.P.4
  • 26
    • 3342955791 scopus 로고    scopus 로고
    • Inhibition of influenza virus matrix (M1) protein expression and virus replication by U6 promoter-driven and lentivirus-mediated delivery of siRNA
    • Hui, E. K.-W., E. M. Yap, D. S. An, I. S. Y. Chen, and D. P. Nayak. 2004. Inhibition of influenza virus matrix (M1) protein expression and virus replication by U6 promoter-driven and lentivirus-mediated delivery of siRNA. J. Gen. Virol. 85:1877-1884.
    • (2004) J. Gen. Virol. , vol.85 , pp. 1877-1884
    • Hui, E.K.-W.1    Yap, E.M.2    An, D.S.3    Chen, I.S.Y.4    Nayak, D.P.5
  • 27
    • 0034744439 scopus 로고    scopus 로고
    • 2 zinc finger proteins
    • 2 zinc finger proteins. Cell. Mol. Life Sci. 58:625-635.
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 625-635
    • Iuchi, S.1
  • 30
    • 0023212842 scopus 로고
    • Molecular analyses of the hemagglutinin genes of H5 influenza viruses: Origin of a virulent turkey strain
    • Kawaoka, Y., A. Nestorowicz, D. J. Alexander, and R. G. Webster. 1987. Molecular analyses of the hemagglutinin genes of H5 influenza viruses: origin of a virulent turkey strain. Virology 158:218-227.
    • (1987) Virology , vol.158 , pp. 218-227
    • Kawaoka, Y.1    Nestorowicz, A.2    Alexander, D.J.3    Webster, R.G.4
  • 31
    • 0001561789 scopus 로고
    • Activation cleavage of viral spike proteins by host proteases
    • E. Wimmer (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Klenk, H.-D., and W. Garten. 1994. Activation cleavage of viral spike proteins by host proteases, p. 241-280. In E. Wimmer (ed.), Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 241-280
    • Klenk, H.-D.1    Garten, W.2
  • 33
    • 0029916060 scopus 로고    scopus 로고
    • Cascade of fever production in mice infected with influenza virus
    • Kurokawa, M., M. Imakita, C. A. Kumeda, and K. Shiraki. 1996. Cascade of fever production in mice infected with influenza virus. J. Med. Virol. 50:152-158.
    • (1996) J. Med. Virol. , vol.50 , pp. 152-158
    • Kurokawa, M.1    Imakita, M.2    Kumeda, C.A.3    Shiraki, K.4
  • 34
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), Lippincott Williams & Wilkins, Philadelphia, Pa
    • Lamb, R. A., and R. M. Krug. 2001. Orthomyxoviridae: the viruses and their replication, p. 725-769. In D. M. Knipe and P. M. Howley (ed.), Fundamental virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, Pa.
    • (2001) Fundamental Virology, 4th Ed. , pp. 725-769
    • Lamb, R.A.1    Krug, R.M.2
  • 35
    • 13744253459 scopus 로고    scopus 로고
    • Attenuating mutations of the matrix gene of influenza A/WSN/33 virus
    • Liu, T., and Z. Ye. 2005. Attenuating mutations of the matrix gene of influenza A/WSN/33 virus. J. Virol. 79:1918-1923.
    • (2005) J. Virol. , vol.79 , pp. 1918-1923
    • Liu, T.1    Ye, Z.2
  • 36
    • 0036891870 scopus 로고    scopus 로고
    • Restriction of viral replication by mutation of the influenza virus matrix protein
    • Liu, T., and Z. Ye. 2002. Restriction of viral replication by mutation of the influenza virus matrix protein. J. Virol. 76:13055-13061.
    • (2002) J. Virol. , vol.76 , pp. 13055-13061
    • Liu, T.1    Ye, Z.2
  • 37
    • 0033064858 scopus 로고    scopus 로고
    • A mouse model for the evaluation of pathogenesis and immunity to influenza a (HSN1) viruses isolated from human
    • Lu, X., T. M. Tumpey, T. Morken, S. R. Zaki, N. J. Cox, and J. M. Katz. 1999. A mouse model for the evaluation of pathogenesis and immunity to influenza A (HSN1) viruses isolated from human. J. Virol. 73:5903-5911.
    • (1999) J. Virol. , vol.73 , pp. 5903-5911
    • Lu, X.1    Tumpey, T.M.2    Morken, T.3    Zaki, S.R.4    Cox, N.J.5    Katz, J.M.6
  • 38
    • 18844448981 scopus 로고    scopus 로고
    • A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence
    • McCullers, J. A., E. Hoffmann, V. C. Huber, and A. D. Nickerson. 2005. A single amino acid change in the C-terminal domain of the matrix protein M1 of influenza B virus confers mouse adaptation and virulence. Virology 336: 318-326.
    • (2005) Virology , vol.336 , pp. 318-326
    • McCullers, J.A.1    Hoffmann, E.2    Huber, V.C.3    Nickerson, A.D.4
  • 39
    • 0037234342 scopus 로고    scopus 로고
    • Virus-cell interactions in the induction of type 1 interferon by influenza virus in mouse spleen cells
    • Miller, J. L., and E. M. Anders. 2003. Virus-cell interactions in the induction of type 1 interferon by influenza virus in mouse spleen cells. J. Gen. Virol. 84:193-202.
    • (2003) J. Gen. Virol. , vol.84 , pp. 193-202
    • Miller, J.L.1    Anders, E.M.2
  • 40
    • 0018886412 scopus 로고
    • Neurovirulence of influenza virus in mice. II. Mechanism of virulence as studied in a neuroblastoma cell line
    • Nakajima, S., and A. Sugiura. 1980. Neurovirulence of influenza virus in mice. II. Mechanism of virulence as studied in a neuroblastoma cell line. Virology 101:450-457.
    • (1980) Virology , vol.101 , pp. 450-457
    • Nakajima, S.1    Sugiura, A.2
  • 41
    • 0029914173 scopus 로고    scopus 로고
    • Antiviral activity of influenza virus M1 zinc finger peptides
    • Nasser, E. H., A. K. Judd, A. Sanchez, D. Anastasiou, and D. J. Bucher. 1996. Antiviral activity of influenza virus M1 zinc finger peptides. J. Virol. 70:8639-8644.
    • (1996) J. Virol. , vol.70 , pp. 8639-8644
    • Nasser, E.H.1    Judd, A.K.2    Sanchez, A.3    Anastasiou, D.4    Bucher, D.J.5
  • 42
    • 0012357782 scopus 로고    scopus 로고
    • Assembly and morphogenesis of influenza viruses
    • Nayak, D. P., and E. K.-W. Hui. 2002. Assembly and morphogenesis of influenza viruses. Recent Res. Dev. Virol. 4:35-54.
    • (2002) Recent Res. Dev. Virol. , vol.4 , pp. 35-54
    • Nayak, D.P.1    Hui, E.K.-W.2
  • 43
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • Nayak, D. P., E. K.-W. Hui, and S. Barman. 2004. Assembly and budding of influenza virus. Virus Res. 106:147-165.
    • (2004) Virus Res. , vol.106 , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.-W.2    Barman, S.3
  • 44
    • 0027417882 scopus 로고
    • Murine model for evaluation of protective immunity to influenza virus
    • Novak, M., Z. Moldoveanu, D. P. Schafer, J. Mestecky, and R. W. Compans. 1993. Murine model for evaluation of protective immunity to influenza virus. Vaccine 11:55-60.
    • (1993) Vaccine , vol.11 , pp. 55-60
    • Novak, M.1    Moldoveanu, Z.2    Schafer, D.P.3    Mestecky, J.4    Compans, R.W.5
  • 45
    • 0037465545 scopus 로고    scopus 로고
    • Zinc- And pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1
    • Okada, A., T. Miura, and H. Takeuchi. 2003. Zinc- and pH-dependent conformational transition in a putative interdomain linker region of the influenza virus matrix protein M1. Biochemistry 42:1978-1984.
    • (2003) Biochemistry , vol.42 , pp. 1978-1984
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 46
    • 0023759401 scopus 로고
    • The intracellular distribution of influenza virus matrix protein and nucleoprotein in infected cells and their relationship to hemagglutinin in the plasma membrane
    • Patterson, S., J. Gross, and J. S. Oxford. 1988. The intracellular distribution of influenza virus matrix protein and nucleoprotein in infected cells and their relationship to hemagglutinin in the plasma membrane. J. Gen. Virol. 69: 1859-1872.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1859-1872
    • Patterson, S.1    Gross, J.2    Oxford, J.S.3
  • 47
    • 0028827424 scopus 로고
    • Tumor necrosis factor as a mediator of inflammation in influenza a viral pneumonia
    • Peper, R. L., and H. Van Campen. 1995. Tumor necrosis factor as a mediator of inflammation in influenza A viral pneumonia. Microb. Pathog. 19:175-183.
    • (1995) Microb. Pathog. , vol.19 , pp. 175-183
    • Peper, R.L.1    Van Campen, H.2
  • 48
    • 0035090589 scopus 로고    scopus 로고
    • Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade
    • Pleschka, S., T. Wolff, C. Ehrhardt, G. Hobom, O. Planz, U. R. Rapp, and S. Ludwig. 2001. Influenza virus propagation is impaired by inhibition of the Raf/MEK/ERK signalling cascade. Nat. Cell Biol. 3:301-305.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 301-305
    • Pleschka, S.1    Wolff, T.2    Ehrhardt, C.3    Hobom, G.4    Planz, O.5    Rapp, U.R.6    Ludwig, S.7
  • 49
    • 0034702018 scopus 로고    scopus 로고
    • The influenza a virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C
    • Reinhardt, J., and T. Wolff. 2000. The influenza A virus M1 protein interacts with the cellular receptor of activated C kinase (RACK) 1 and can be phosphorylated by protein kinase C. Vet. Microbiol. 74:87-100.
    • (2000) Vet. Microbiol. , vol.74 , pp. 87-100
    • Reinhardt, J.1    Wolff, T.2
  • 50
    • 0019777842 scopus 로고
    • Electrophoretic separation of influenza virus ribonucleoproteins
    • Ress, P. J., and N. J. Dimmock. 1981. Electrophoretic separation of influenza virus ribonucleoproteins. J. Gen. Virol. 53:125-132.
    • (1981) J. Gen. Virol. , vol.53 , pp. 125-132
    • Ress, P.J.1    Dimmock, N.J.2
  • 51
    • 0019997498 scopus 로고
    • Kinetics of synthesis of influenza virus ribonucleoprotein structures
    • Ress, P. J., and N. J. Dimmock. 1982. Kinetics of synthesis of influenza virus ribonucleoprotein structures. J. Gen. Virol. 59:403-408.
    • (1982) J. Gen. Virol. , vol.59 , pp. 403-408
    • Ress, P.J.1    Dimmock, N.J.2
  • 52
    • 0028986024 scopus 로고
    • Activation of IFN-α, IFN-γ, MxA, and IFN regulatory factor 1 genes in influenza a virus-infected human peripheral blood mononuclear cells
    • Ronni, T., T. Sareneva, J. Pirhonen, and I. Julkunen. 1995. Activation of IFN-α, IFN-γ, MxA, and IFN regulatory factor 1 genes in influenza A virus-infected human peripheral blood mononuclear cells. J. Immunol. 154: 2764-2774.
    • (1995) J. Immunol. , vol.154 , pp. 2764-2774
    • Ronni, T.1    Sareneva, T.2    Pirhonen, J.3    Julkunen, I.4
  • 53
    • 0028916010 scopus 로고
    • Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein from structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles
    • Ruigrok, R. W. H., and F. Baudin. 1995. Structure of influenza virus ribonucleoprotein particles. II. Purified RNA-free influenza virus ribonucleoprotein from structures that are indistinguishable from the intact influenza virus ribonucleoprotein particles. J. Gen. Virol. 76:1009-1114.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1009-1114
    • Ruigrok, R.W.H.1    Baudin, F.2
  • 54
    • 0032526917 scopus 로고    scopus 로고
    • Influenza a virus-induced IFN-α/β and IL-18 synergistically enhance IFN-γ gene expression in human T cells
    • Sareneva, T., S. Matikainen, M. Kurimoto, and I. Julkunen. 1998. Influenza A virus-induced IFN-α/β and IL-18 synergistically enhance IFN-γ gene expression in human T cells. J. Immunol. 160:6032-6038.
    • (1998) J. Immunol. , vol.160 , pp. 6032-6038
    • Sareneva, T.1    Matikainen, S.2    Kurimoto, M.3    Julkunen, I.4
  • 55
    • 0031611142 scopus 로고    scopus 로고
    • Mechanisms involved in natural and experimental neuropathogenicity of influenza viruses: Evidence and speculation
    • Schlesinger, R. W., P. J. Husak, G. L. Bradshaw, and P. P. Panayotov. 1998. Mechanisms involved in natural and experimental neuropathogenicity of influenza viruses: evidence and speculation. Adv. Virus Res. 50:289-379.
    • (1998) Adv. Virus Res. , vol.50 , pp. 289-379
    • Schlesinger, R.W.1    Husak, P.J.2    Bradshaw, G.L.3    Panayotov, P.P.4
  • 56
    • 26944491901 scopus 로고    scopus 로고
    • Influenza virus assembly and budding at the viral budzone
    • Schmitt, A. P., and R. A. Lamb. 2005. Influenza virus assembly and budding at the viral budzone. Adv. Virus Res. 64:383-416.
    • (2005) Adv. Virus Res. , vol.64 , pp. 383-416
    • Schmitt, A.P.1    Lamb, R.A.2
  • 57
    • 0014354907 scopus 로고
    • The use of an animal model to study transmission of influenza virus infection
    • Schulman, J. L. 1968. The use of an animal model to study transmission of influenza virus infection. Am. J. Public Health Nations Health 58:2092-2096.
    • (1968) Am. J. Public Health Nations Health , vol.58 , pp. 2092-2096
    • Schulman, J.L.1
  • 58
    • 0033730244 scopus 로고    scopus 로고
    • In vitro and in vivo assay systems for study of influenza virus inhibitors
    • Sidwell, R. W., and D. F. Smee. 2001. In vitro and in vivo assay systems for study of influenza virus inhibitors. Antivir. Res. 48:1-16.
    • (2001) Antivir. Res. , vol.48 , pp. 1-16
    • Sidwell, R.W.1    Smee, D.F.2
  • 60
    • 0028107688 scopus 로고
    • The influenza virus variant A/FM/1/ 47-MA possesses single amino acid replacements in the hemagglutinin, controlling virulence, and in the matrix protein, controlling virulence as well as growth
    • Smeenk, C. A., and E. G. Brown. 1994. The influenza virus variant A/FM/1/ 47-MA possesses single amino acid replacements in the hemagglutinin, controlling virulence, and in the matrix protein, controlling virulence as well as growth. J. Virol. 68:530-534.
    • (1994) J. Virol. , vol.68 , pp. 530-534
    • Smeenk, C.A.1    Brown, E.G.2
  • 61
    • 0030271198 scopus 로고    scopus 로고
    • Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis
    • Smeenk, C. A., K. E. Wright, B. F. Burns, A. J. Thaker, and E. G. Brown. 1996. Mutations in the hemagglutinin and matrix genes of a virulent influenza virus variant, A/FM/1/47-MA, control different stages in pathogenesis. Virus Res. 44:79-95.
    • (1996) Virus Res. , vol.44 , pp. 79-95
    • Smeenk, C.A.1    Wright, K.E.2    Burns, B.F.3    Thaker, A.J.4    Brown, E.G.5
  • 62
    • 0033602713 scopus 로고    scopus 로고
    • Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    • Steinhauer, D. A. 1999. Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology 258:1-20.
    • (1999) Virology , vol.258 , pp. 1-20
    • Steinhauer, D.A.1
  • 64
    • 0026645960 scopus 로고
    • The attenuation phenotype conferred by the M gene of the influenza A/Ann Arbor/6/60 cold-adapted virus (H2N2) on the A/Korea/82 (H3N2) reassortant virus results from a gene constellation effect
    • Subbarao, E. K., M. Perkins, J. J. Treanor, and B. R. Murphy. 1992. The attenuation phenotype conferred by the M gene of the influenza A/Ann Arbor/6/60 cold-adapted virus (H2N2) on the A/Korea/82 (H3N2) reassortant virus results from a gene constellation effect. Virus Res. 25:37-50.
    • (1992) Virus Res. , vol.25 , pp. 37-50
    • Subbarao, E.K.1    Perkins, M.2    Treanor, J.J.3    Murphy, B.R.4
  • 65
    • 0018825909 scopus 로고
    • Neurovirulence of influenza virus in mice. I. Neurovirulence of recombinants between virulent and avirulent virus strains
    • Sugiura, A., and M. Ueda. 1980. Neurovirulence of influenza virus in mice. I. Neurovirulence of recombinants between virulent and avirulent virus strains. Virology. 101:440-449.
    • (1980) Virology , vol.101 , pp. 440-449
    • Sugiura, A.1    Ueda, M.2
  • 66
    • 0030221141 scopus 로고    scopus 로고
    • The role of proteolytic cleavage of viral glycoproteins in the pathogenesis of influenza virus infections
    • Tashiro, M., and R. Rott. 1996. The role of proteolytic cleavage of viral glycoproteins in the pathogenesis of influenza virus infections. Semin. Virol. 7:237-243.
    • (1996) Semin. Virol. , vol.7 , pp. 237-243
    • Tashiro, M.1    Rott, R.2
  • 69
    • 0025058192 scopus 로고
    • Production of interleukin 1 and tumor necrosis factor activities in bronchoalveolar washings following infection of mice by influenza virus
    • Vacheron, F., A. Rudent, S. Perin, C. Labarre, A. M. Quero, and M. Guenounou. 1990. Production of interleukin 1 and tumor necrosis factor activities in bronchoalveolar washings following infection of mice by influenza virus. J. Gen. Virol. 71:477-479.
    • (1990) J. Gen. Virol. , vol.71 , pp. 477-479
    • Vacheron, F.1    Rudent, A.2    Perin, S.3    Labarre, C.4    Quero, A.M.5    Guenounou, M.6
  • 70
    • 0034701857 scopus 로고    scopus 로고
    • Cytokines in the pathogenesis of influenza
    • Van Reeth, K. 2000. Cytokines in the pathogenesis of influenza. Vet. Microbid. 74:109-116.
    • (2000) Vet. Microbid. , vol.74 , pp. 109-116
    • Van Reeth, K.1
  • 71
    • 0024454843 scopus 로고
    • RNA-binding properties of influenza a virus matrix protein M1
    • Wakefield, L., and G. G. Brownlee. 1989. RNA-binding properties of influenza A virus matrix protein M1. Nucleic Acids Res. 17:8569-8580.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8569-8580
    • Wakefield, L.1    Brownlee, G.G.2
  • 72
    • 0030774559 scopus 로고    scopus 로고
    • Virulence of influenza a virus for mouse lung
    • Ward, A. 1997. Virulence of influenza A virus for mouse lung. Virus Genes 14:187-194.
    • (1997) Virus Genes , vol.14 , pp. 187-194
    • Ward, A.1
  • 73
    • 0003000152 scopus 로고    scopus 로고
    • Nonspecific host responses to viral infections
    • N. Nathanson (ed.), Lippincott-Raven Publishers, Philadelphia, Pa
    • Welsh, R. M., and G. C. Sen. 1997. Nonspecific host responses to viral infections, p. 109-141. In N. Nathanson (ed.), Viral pathogenesis. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (1997) Viral Pathogenesis , pp. 109-141
    • Welsh, R.M.1    Sen, G.C.2
  • 74
    • 0028051515 scopus 로고
    • Growth control of influenza a virus by M1 protein: Analysis of transfectant viruses carrying the chimeric M gene
    • Yasuda, J., D. J. Bucher, and A. Ishihama. 1994. Growth control of influenza A virus by M1 protein: analysis of transfectant viruses carrying the chimeric M gene. J. Virol. 68:8141-8146.
    • (1994) J. Virol. , vol.68 , pp. 8141-8146
    • Yasuda, J.1    Bucher, D.J.2    Ishihama, A.3
  • 75
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye, Z., T. Liu, D. P. Offringa, J. McInnis, and R. A. Levandowski. 1999. Association of influenza virus matrix protein with ribonucleoproteins. J. Virol. 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
  • 76
    • 0030825146 scopus 로고    scopus 로고
    • Histones as a target for influenza virus matrix protein M1
    • Zhimov, O. P., and H.-D. Klenk. 1997. Histones as a target for influenza virus matrix protein M1. Virology 235:302-310.
    • (1997) Virology , vol.235 , pp. 302-310
    • Zhimov, O.P.1    Klenk, H.-D.2


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