메뉴 건너뛰기




Volumn 12, Issue 3, 1999, Pages 175-196

A fatal relationship - Influenza virus interactions with the host cell

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; CYTOKINE; GENE PRODUCT; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HEMAGGLUTININ; MEMBRANE PROTEIN; MESSENGER RNA; PHOSPHOPEPTIDE; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; RNA POLYMERASE; SIALIC ACID DERIVATIVE; SIALIDASE INHIBITOR; VIRUS PROTEIN; VIRUS RNA;

EID: 0032828271     PISSN: 08828245     EISSN: None     Source Type: Journal    
DOI: 10.1089/vim.1999.12.175     Document Type: Review
Times cited : (59)

References (188)
  • 1
    • 0032485487 scopus 로고    scopus 로고
    • Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs
    • Albert, M.L., B. Sauter, and N. Bhardwaj. 1998. Dendritic cells acquire antigen from apoptotic cells and induce class I-restricted CTLs. Nature. 392:86-89.
    • (1998) Nature , vol.392 , pp. 86-89
    • Albert, M.L.1    Sauter, B.2    Bhardwaj, N.3
  • 2
    • 0020323968 scopus 로고
    • Phosphorylation of the nucleoprotein of an avian influenza virus
    • Almond, J.W., and V. Felsenreich. 1982. Phosphorylation of the nucleoprotein of an avian influenza virus. J. Gen. Virol. 60:295-305.
    • (1982) J. Gen. Virol. , vol.60 , pp. 295-305
    • Almond, J.W.1    Felsenreich, V.2
  • 3
    • 0029934078 scopus 로고    scopus 로고
    • Serine 3 is critical for phosphorylation at the N-terminal end of the nucleoprotein of influenza virus A/Victoria/3/75
    • Arrese, M., and A. Portela. 1996. Serine 3 is critical for phosphorylation at the N-terminal end of the nucleoprotein of influenza virus A/Victoria/3/75. J. Virol. 70:3385-3391.
    • (1996) J. Virol. , vol.70 , pp. 3385-3391
    • Arrese, M.1    Portela, A.2
  • 4
    • 0030966390 scopus 로고    scopus 로고
    • Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells
    • Avalos, R.T., Z. Yu, and D.P. Nayak. 1997. Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells. J. Virol. 71:2947-2958.
    • (1997) J. Virol. , vol.71 , pp. 2947-2958
    • Avalos, R.T.1    Yu, Z.2    Nayak, D.P.3
  • 5
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • Baeuerle, P.A., and T. Henkel. 1994. Function and activation of NF-kappa B in the immune system. Annu. Rev. Immunol. 12:141-179.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 6
    • 0027423667 scopus 로고
    • Effect of granulocyte/macrophage colony-stimulating factor on human monocytes infected with influenza A virus. Enhancement of virus replication, cytokine release, and cytotoxicity
    • Bender, A., U. Amann, R. Jager, M. Nain, and D. Gemsa. 1993. Effect of granulocyte/macrophage colony-stimulating factor on human monocytes infected with influenza A virus. Enhancement of virus replication, cytokine release, and cytotoxicity. J. Immunol. 151:5416-5427.
    • (1993) J. Immunol. , vol.151 , pp. 5416-5427
    • Bender, A.1    Amann, U.2    Jager, R.3    Nain, M.4    Gemsa, D.5
  • 7
    • 0027299256 scopus 로고
    • The potentiating effect of LPS on tumor necrosis factor-alpha production by influenza A virus-infected macrophages
    • Bender, A., H. Sprenger, J.H. Gong, A. Henke, G. Bolte, H.P. Spengler, M. Nain, and D. Gemsa. 1993. The potentiating effect of LPS on tumor necrosis factor-alpha production by influenza A virus-infected macrophages. Immunobiology. 187:357-371.
    • (1993) Immunobiology , vol.187 , pp. 357-371
    • Bender, A.1    Sprenger, H.2    Gong, J.H.3    Henke, A.4    Bolte, G.5    Spengler, H.P.6    Nain, M.7    Gemsa, D.8
  • 8
    • 0021955901 scopus 로고
    • Protein fatty acyltransferase is located in the rough endoplasmic reticulum
    • Berger, M., and M.F. Schmidt. 1985. Protein fatty acyltransferase is located in the rough endoplasmic reticulum. FEBS. Lett. 187:289-294.
    • (1985) FEBS. Lett. , vol.187 , pp. 289-294
    • Berger, M.1    Schmidt, M.F.2
  • 9
    • 0032191176 scopus 로고    scopus 로고
    • Role of early cytokines, including alpha and beta interferons (IFN-alpha/beta), in innate and adaptive immune responses to viral infections
    • Biron, C.A. 1998. Role of early cytokines, including alpha and beta interferons (IFN-alpha/beta), in innate and adaptive immune responses to viral infections. Semin. Immunol. 10:383-390.
    • (1998) Semin. Immunol. , vol.10 , pp. 383-390
    • Biron, C.A.1
  • 10
    • 0020480480 scopus 로고
    • Identification of the cap binding protein of influenza virus
    • Blaas, D., E. Patzelt, and E. Kuechler. 1982. Identification of the cap binding protein of influenza virus. Nucleic. Acids. Res. 10:4803-4812.
    • (1982) Nucleic. Acids. Res. , vol.10 , pp. 4803-4812
    • Blaas, D.1    Patzelt, E.2    Kuechler, E.3
  • 11
    • 0027978629 scopus 로고
    • Cell tropism of influenza virus mediated by hemagglutinin activation at the stage of virus entry
    • Boycott, R., H.D. Klenk, and M. Ohuchi. 1994. Cell tropism of influenza virus mediated by hemagglutinin activation at the stage of virus entry. Virology. 203:313-319.
    • (1994) Virology , vol.203 , pp. 313-319
    • Boycott, R.1    Klenk, H.D.2    Ohuchi, M.3
  • 12
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman, I., H. Hoover-Litty, K.R. Wagner, and A. Helenius. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell. Biol. 114:401-411.
    • (1991) J. Cell. Biol. , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 13
    • 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
  • 14
    • 0025336860 scopus 로고
    • Trimer formation determines the rate of influenza virus haemagglutinin transport in the early stages of secretion in Xenopus oocytes
    • Ceriotti, A., and A. Colman. 1990. Trimer formation determines the rate of influenza virus haemagglutinin transport in the early stages of secretion in Xenopus oocytes. J. Cell. Biol. 111:409-420.
    • (1990) J. Cell. Biol. , vol.111 , pp. 409-420
    • Ceriotti, A.1    Colman, A.2
  • 15
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen, W., J. Helenius, I. Braakman, and A. Helenius. 1995. Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl. Acad. Sci. USA 92:6229-6233.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 16
    • 0029048936 scopus 로고
    • Differential activation of the influenza virus polymerase via template RNA binding
    • Cianci, C., L. Tiley, and M. Krystal. 1995. Differential activation of the influenza virus polymerase via template RNA binding. J. Virol 69:3995-3999.
    • (1995) J. Virol , vol.69 , pp. 3995-3999
    • Cianci, C.1    Tiley, L.2    Krystal, M.3
  • 17
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracellular transport
    • Copeland, C.S., R.W. Doms, E.M. Bolzau, R.G. Webster, and A. Helenius. 1986. Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell. Biol. 103:1179-1191.
    • (1986) J. Cell. Biol. , vol.103 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 18
    • 0028923921 scopus 로고
    • Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs
    • de la Luna, S., P. Fortes, A. Beloso, and J. Ortin. 1995. Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs. J. Virol. 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
  • 19
    • 0030992545 scopus 로고    scopus 로고
    • A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis
    • Der, S.D., Y.L. Yang, C. Weissmann, and B.R. Williams. 1997. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc. Natl. Acad. Sci. USA 94:3279-3283.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3279-3283
    • Der, S.D.1    Yang, Y.L.2    Weissmann, C.3    Williams, B.R.4
  • 20
    • 0032981158 scopus 로고    scopus 로고
    • Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments
    • Digard, P., D. Elton, K. Bishop, E. Medcalf, A. Weeds, and B. Pope. 1999. Modulation of nuclear localization of the influenza virus nucleoprotein through interaction with actin filaments. J. Virol. 73:2222-2231.
    • (1999) J. Virol. , vol.73 , pp. 2222-2231
    • Digard, P.1    Elton, D.2    Bishop, K.3    Medcalf, E.4    Weeds, A.5    Pope, B.6
  • 21
    • 0027180032 scopus 로고
    • Modulation of CD4+ T-cell recognition of influenza hemagglutinin by carbohydrate side chains located outside a T-cell determinant
    • Drummer, H.E., D.C. Jackson, and L.E. Brown. 1993. Modulation of CD4+ T-cell recognition of influenza hemagglutinin by carbohydrate side chains located outside a T-cell determinant. Virology. 192:282-289.
    • (1993) Virology , vol.192 , pp. 282-289
    • Drummer, H.E.1    Jackson, D.C.2    Brown, L.E.3
  • 22
    • 0027272101 scopus 로고
    • An influenza virus temperature-sensitive mutant defective in the nuclear-cytoplasmic transport of the negative-sense viral RNAs
    • Enami, K., Y. Qiao, R. Fukuda, and M. Enami. 1993. An influenza virus temperature-sensitive mutant defective in the nuclear-cytoplasmic transport of the negative-sense viral RNAs. Virology. 194:822-827.
    • (1993) Virology , vol.194 , pp. 822-827
    • Enami, K.1    Qiao, Y.2    Fukuda, R.3    Enami, M.4
  • 23
    • 0028055149 scopus 로고
    • Influenza virus NS1 protein stimulates translation of the M1 protein
    • Enami, K., T.A. Sato, S. Nakada, and M. Enami. 1994. Influenza virus NS1 protein stimulates translation of the M1 protein. J. Virol. 68:1432-1437.
    • (1994) J. Virol. , vol.68 , pp. 1432-1437
    • Enami, K.1    Sato, T.A.2    Nakada, S.3    Enami, M.4
  • 24
    • 0028265818 scopus 로고
    • Programmed cell death (apoptosis) in human monocytes infected by influenza A virus
    • Fesq, H., M. Bacher, M. Nain, and D. Gemsa. 1994. Programmed cell death (apoptosis) in human monocytes infected by influenza A virus. Immunobiology. 190:175-182.
    • (1994) Immunobiology , vol.190 , pp. 175-182
    • Fesq, H.1    Bacher, M.2    Nain, M.3    Gemsa, D.4
  • 25
    • 0032169620 scopus 로고    scopus 로고
    • Acylation of the influenza hemagglutinin modulates fusion activity
    • Fischer, C., B. Schroth-Diez, A. Herrmann, W. Garten, and H.D. Klenk. 1998. Acylation of the influenza hemagglutinin modulates fusion activity. Virology. 248:284-294.
    • (1998) Virology , vol.248 , pp. 284-294
    • Fischer, C.1    Schroth-Diez, B.2    Herrmann, A.3    Garten, W.4    Klenk, H.D.5
  • 26
    • 0029853503 scopus 로고    scopus 로고
    • Promoter elements in the influenza vRNA terminal structure
    • Flick, R., G. Neumann, E. Hoffmann, E. Neumeier, and G. Hobom. 1996. Promoter elements in the influenza vRNA terminal structure. RNA. 2:1046-1057.
    • (1996) RNA , vol.2 , pp. 1046-1057
    • Flick, R.1    Neumann, G.2    Hoffmann, E.3    Neumeier, E.4    Hobom, G.5
  • 27
    • 0029020773 scopus 로고
    • Characterization of the RNA-fork model of virion RNA in the initiation of transcription in influenza A virus
    • Fodor, E., D.C. Pritlove, and G.G. Brownlee. 1995. Characterization of the RNA-fork model of virion RNA in the initiation of transcription in influenza A virus. J. Virol. 69:4012-4019.
    • (1995) J. Virol. , vol.69 , pp. 4012-4019
    • Fodor, E.1    Pritlove, D.C.2    Brownlee, G.G.3
  • 28
    • 0028008470 scopus 로고
    • Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport
    • Fortes, P., A. Beloso, and J. Ortin. 1994. Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport. EMBO. J. 13:704-712.
    • (1994) EMBO. J. , vol.13 , pp. 704-712
    • Fortes, P.1    Beloso, A.2    Ortin, J.3
  • 29
    • 2642648639 scopus 로고    scopus 로고
    • Regulation of interferon-induced protein kinase PKR: Modulation of p58ipk inhibitory function by a novel protein. p52ripk
    • Gale, M., Jr., C.M. Blakely, D.A. Hopkins, M.W. Melville, M. Wambach, P.R. Romano, and M.G. Katze. 1998. Regulation of interferon-induced protein kinase PKR: Modulation of p58ipk inhibitory function by a novel protein. p52ripk. Mol. Cell. Biol. 18:859-871.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 859-871
    • Gale Jr., M.1    Blakely, C.M.2    Hopkins, D.A.3    Melville, M.W.4    Wambach, M.5    Romano, P.R.6    Katze, M.G.7
  • 30
    • 0024242218 scopus 로고
    • Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport, and activity of the molecule
    • Gallagher, P., J. Henneberry, I. Wilson, J. Sambrook, and M.J. Gething. 1988. Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport, and activity of the molecule. J. Cell. Biol. 107:2059-2073.
    • (1988) J. Cell. Biol. , vol.107 , pp. 2059-2073
    • Gallagher, P.1    Henneberry, J.2    Wilson, I.3    Sambrook, J.4    Gething, M.J.5
  • 31
    • 0032145579 scopus 로고    scopus 로고
    • Effects of host-dependent glycosylation of hemagglutinin on receptor-binding properties on H1N1 human influenza A virus grown in MDCK cells and in embryonated eggs
    • Gambaryan, A.S., V.P. Marinina, A.B. Tuzikov, N.V. Bovin, I.A. Rudneva, B.V. Sinitsyn, A.A. Shilov, and M.N. Matrosovich. 1998. Effects of host-dependent glycosylation of hemagglutinin on receptor-binding properties on H1N1 human influenza A virus grown in MDCK cells and in embryonated eggs. Virology. 247:170-177.
    • (1998) Virology , vol.247 , pp. 170-177
    • Gambaryan, A.S.1    Marinina, V.P.2    Tuzikov, A.B.3    Bovin, N.V.4    Rudneva, I.A.5    Sinitsyn, B.V.6    Shilov, A.A.7    Matrosovich, M.N.8
  • 34
    • 0027518202 scopus 로고
    • Translational control by influenza virus. Selective translation is mediated by sequences within the viral mRNA 5′-untranslated region
    • Garfinkel, M.S., and M.G. Katze. 1993. Translational control by influenza virus. Selective translation is mediated by sequences within the viral mRNA 5′-untranslated region. J. Biol. Chem. 268:22223-22226.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22223-22226
    • Garfinkel, M.S.1    Katze, M.G.2
  • 35
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M.J., K. McCammon, and J. Sambrook. 1986. Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell. 46:939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 36
    • 0025922586 scopus 로고
    • The TPR snap helix: A novel protein repeat motif from mitosis to transcription
    • Goebl, M., and M. Yanagida. 1991. The TPR snap helix: A novel protein repeat motif from mitosis to transcription. Trends. Biochem. Sci. 16:173-177.
    • (1991) Trends. Biochem. Sci. , vol.16 , pp. 173-177
    • Goebl, M.1    Yanagida, M.2
  • 37
    • 0025721953 scopus 로고
    • Influenza A virus infection of macrophages. Enhanced tumor necrosis factor-alpha (TNF-alpha) gene expression and lipopolysaccharide-triggered TNF-alpha release
    • Gong, J.H., H. Sprenger, F. Hinder, A. Bender, A. Schmidt, S. Horch, M. Nain, and D. Gemsa. 1991. Influenza A virus infection of macrophages. Enhanced tumor necrosis factor-alpha (TNF-alpha) gene expression and lipopolysaccharide-triggered TNF-alpha release. J. Immunol. 147:3507-3513.
    • (1991) J. Immunol. , vol.147 , pp. 3507-3513
    • Gong, J.H.1    Sprenger, H.2    Hinder, F.3    Bender, A.4    Schmidt, A.5    Horch, S.6    Nain, M.7    Gemsa, D.8
  • 38
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • Goto, H., and Y. Kawaoka. 1998. A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. USA 95:10224-10228.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 39
    • 0025151601 scopus 로고
    • An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo
    • Gotoh, B., T. Ogasawara, T. Toyoda, N.M. Inocencio, M. Hamaguchi, and Y. Nagai. 1990. An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo. EMBO. J. 9:4189-4195.
    • (1990) EMBO. J. , vol.9 , pp. 4189-4195
    • Gotoh, B.1    Ogasawara, T.2    Toyoda, T.3    Inocencio, N.M.4    Hamaguchi, M.5    Nagai, Y.6
  • 41
    • 0021288412 scopus 로고
    • The membrane (M1) protein of influenza virus occurs in two forms and is a phosphoprotein
    • Gregoriades, A., T. Christie, and K. Markarian. 1984. The membrane (M1) protein of influenza virus occurs in two forms and is a phosphoprotein. J. Virol. 49:229-235.
    • (1984) J. Virol. , vol.49 , pp. 229-235
    • Gregoriades, A.1    Christie, T.2    Markarian, K.3
  • 42
    • 0025308076 scopus 로고
    • The phosphorylation of the integral membrane (M1) protein of influenza virus
    • Gregoriades, A., G.G. Guzman, and E. Paoletti. 1990. The phosphorylation of the integral membrane (M1) protein of influenza virus. Virus. Res. 16:27-41.
    • (1990) Virus. Res. , vol.16 , pp. 27-41
    • Gregoriades, A.1    Guzman, G.G.2    Paoletti, E.3
  • 43
    • 0028123774 scopus 로고
    • Recombinant influenza virus polymerase: Requirement of both 5′ and 3′ viral ends for endonuclease activity
    • Hagen, M., T.D. Chung, J.A. Butcher, and M. Krystal. 1994. Recombinant influenza virus polymerase: requirement of both 5′ and 3′ viral ends for endonuclease activity. J. Virol. 68:1509-1515.
    • (1994) J. Virol. , vol.68 , pp. 1509-1515
    • Hagen, M.1    Chung, T.D.2    Butcher, J.A.3    Krystal, M.4
  • 44
    • 0032036611 scopus 로고    scopus 로고
    • Mx proteins: Mediators of innate resistance to RNA viruses
    • Haller, O., M. Frese, and G. Kochs. 1998. Mx proteins: Mediators of innate resistance to RNA viruses. Rev. Sci. Tech. 17:220-230.
    • (1998) Rev. Sci. Tech. , vol.17 , pp. 220-230
    • Haller, O.1    Frese, M.2    Kochs, G.3
  • 45
    • 0024759095 scopus 로고
    • Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition
    • Hankins, R.W., K. Hagata, D.J. Bucher, S. Popple, and A. Ishihama. 1989. Monoclonal antibody analysis of influenza virus matrix protein epitopes involved in transcription inhibition. Virus Genes 3:111-126.
    • (1989) Virus Genes , vol.3 , pp. 111-126
    • Hankins, R.W.1    Hagata, K.2    Bucher, D.J.3    Popple, S.4    Ishihama, A.5
  • 46
    • 0027102716 scopus 로고
    • Binding of influenza A virus NS1 protein to dsRNA in vitro
    • Hatada, E., and R. Fukuda. 1992. Binding of influenza A virus NS1 protein to dsRNA in vitro. J. Gen. Virol. 73:3325-3327.
    • (1992) J. Gen. Virol. , vol.73 , pp. 3325-3327
    • Hatada, E.1    Fukuda, R.2
  • 47
    • 0032980412 scopus 로고    scopus 로고
    • Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells
    • Hatada, E., S. Saito, and R. Fukuda. 1999. Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells. J. Virol. 73:2425-2433.
    • (1999) J. Virol. , vol.73 , pp. 2425-2433
    • Hatada, E.1    Saito, S.2    Fukuda, R.3
  • 48
    • 0030813216 scopus 로고    scopus 로고
    • Biosynthesis, intracellular transport and enzymatic activity of an avian influenza A virus neuraminidase: Role of unpaired cysteines and individual oligosaccharides
    • Hausmann, J., E. Kretzschmar, W. Garten, and H.D. Klenk. 1997. Biosynthesis, intracellular transport and enzymatic activity of an avian influenza A virus neuraminidase: Role of unpaired cysteines and individual oligosaccharides. J. Gen. Virol. 78:3233-3265.
    • (1997) J. Gen. Virol. , vol.78 , pp. 3233-3265
    • Hausmann, J.1    Kretzschmar, E.2    Garten, W.3    Klenk, H.D.4
  • 49
    • 0029065437 scopus 로고
    • N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity
    • Hausmann, J., E. Kretzschmar, W. Garten, and H.D. Klenk. 1995. N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J. Gen. Virol. 76:1719-1728.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1719-1728
    • Hausmann, J.1    Kretzschmar, E.2    Garten, W.3    Klenk, H.D.4
  • 50
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D.N., B. Foellmer, and A. Helenius. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 51
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • Hebert, D.N., J.X. Zhang, W. Chen, B. Foellmer, and A. Helenius. 1997. The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell. Biol. 139:613-623.
    • (1997) J. Cell. Biol. , vol.139 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 52
    • 0028278094 scopus 로고
    • Apoptosis: A mechanism of cell killing by influenza A and B viruses
    • Hinshaw, V.S., C.W. Olsen, N. Dybdahl-Sissoko, and D. Evans. 1994. Apoptosis: A mechanism of cell killing by influenza A and B viruses. J. Virol. 68:3667-3673.
    • (1994) J. Virol. , vol.68 , pp. 3667-3673
    • Hinshaw, V.S.1    Olsen, C.W.2    Dybdahl-Sissoko, N.3    Evans, D.4
  • 53
    • 0026632942 scopus 로고
    • Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein
    • Hogue, B.G., and D.P. Nayak. 1992. Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein. Virology. 188:510-517.
    • (1992) Virology , vol.188 , pp. 510-517
    • Hogue, B.G.1    Nayak, D.P.2
  • 54
    • 0028895957 scopus 로고
    • Analysis of the posttranslational modifications of the influenza virus M2 protein
    • Holsinger, L.J., M.A. Shaughnessy, A. Micko, L.H. Pinto, and R.A. Lamb. 1995. Analysis of the posttranslational modifications of the influenza virus M2 protein. J. Virol. 69:1219-1225.
    • (1995) J. Virol. , vol.69 , pp. 1219-1225
    • Holsinger, L.J.1    Shaughnessy, M.A.2    Micko, A.3    Pinto, L.H.4    Lamb, R.A.5
  • 55
    • 0028095251 scopus 로고
    • Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses
    • Horimoto, T., K. Nakayama, S.P. Smeekens, and Y. Kawaoka. 1994. Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses. J. Virol. 68:6074-6078.
    • (1994) J. Virol. , vol.68 , pp. 6074-6078
    • Horimoto, T.1    Nakayama, K.2    Smeekens, S.P.3    Kawaoka, Y.4
  • 56
    • 0026762397 scopus 로고
    • Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins
    • Horisberger, M.A. 1992. Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins. J. Virol. 66:4705-4709.
    • (1992) J. Virol. , vol.66 , pp. 4705-4709
    • Horisberger, M.A.1
  • 57
    • 0026729086 scopus 로고
    • Overexpression of the influenza virus polymerase can titrate out inhibition by the murine MxI protein
    • Huang, T., J. Pavlovic, P. Staeheli, and M. Krystal. 1992. Overexpression of the influenza virus polymerase can titrate out inhibition by the murine MxI protein. J. Virol. 66:4154-4160.
    • (1992) J. Virol. , vol.66 , pp. 4154-4160
    • Huang, T.1    Pavlovic, J.2    Staeheli, P.3    Krystal, M.4
  • 58
    • 0024990401 scopus 로고
    • Determination of influenza virus proteins required for genome replication
    • Huang, T.S., P. Palese, and M. Krystal. 1990. Determination of influenza virus proteins required for genome replication. J. Virol. 64:5669-5673.
    • (1990) J. Virol. , vol.64 , pp. 5669-5673
    • Huang, T.S.1    Palese, P.2    Krystal, M.3
  • 59
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S.M., D.G. Bole, H. Hoover-Litty, A. Helenius, and C.S. Copeland. 1989. Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell. Biol. 108:2117-2126.
    • (1989) J. Cell. Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 60
    • 0028883140 scopus 로고
    • Leukocyte migration and adhesion
    • Imhof, B.A., and D. Dunon. 1995. Leukocyte migration and adhesion. Adv. Immunol. 58:345-416.
    • (1995) Adv. Immunol. , vol.58 , pp. 345-416
    • Imhof, B.A.1    Dunon, D.2
  • 61
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly for infectivity
    • Jin, H., G.P. Leser, and R.A. Lamb. 1994. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly for infectivity. EMBO. J. 13:5504-5515.
    • (1994) EMBO. J. , vol.13 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 62
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin, H., G.P. Leser, J. Zhang, and R.A. Lamb. 1997. Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO. J. 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
  • 63
    • 0030026752 scopus 로고    scopus 로고
    • Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
    • Jin, H., K. Subbarao, S. Bagai, G.P. Leser, B.R. Murphy, and R.A. Lamb. 1996. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70:1406-1414.
    • (1996) J. Virol. , vol.70 , pp. 1406-1414
    • Jin, H.1    Subbarao, K.2    Bagai, S.3    Leser, G.P.4    Murphy, B.R.5    Lamb, R.A.6
  • 64
    • 0017410674 scopus 로고
    • Role for nucleocapsid protein phosphorylation in the transcription of influenza virus genome
    • Kamata, T., and Y. Watanabe. 1977. Role for nucleocapsid protein phosphorylation in the transcription of influenza virus genome. Nature. 267:460-462.
    • (1977) Nature , vol.267 , pp. 460-462
    • Kamata, T.1    Watanabe, Y.2
  • 65
    • 0021678670 scopus 로고
    • Metabolism and expression of RNA polymerase II transcripts in influenza virus-infected cells
    • Katze, M.G., and R.M. Krug. 1984. Metabolism and expression of RNA polymerase II transcripts in influenza virus-infected cells. Mol. Cell. Biol. 4:2198-3206.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2198-3206
    • Katze, M.G.1    Krug, R.M.2
  • 66
    • 0021741381 scopus 로고
    • Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin?
    • Kawaoka, Y., C.W. Naeve, and R.G. Webster. 1984. Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin? Virology. 139:303-316.
    • (1984) Virology , vol.139 , pp. 303-316
    • Kawaoka, Y.1    Naeve, C.W.2    Webster, R.G.3
  • 67
    • 0030913309 scopus 로고    scopus 로고
    • A comparison of mammalian and yeast pre-mRNA 3′-end processing
    • Keller, W., and L. Minvielle-Sebastian 1997. A comparison of mammalian and yeast pre-mRNA 3′-end processing. Curr. Opin. Cell. Biol. 9:329-336.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 329-336
    • Keller, W.1    Minvielle-Sebastian, L.2
  • 68
    • 0027173736 scopus 로고
    • Pulmonary surfactant is a potential endogenous inhibitor of proteolytic activation of Sendai virus and influenza A virus
    • Kido, H., K. Sakai, Y. Kishino, and M. Tashiro. 1993. Pulmonary surfactant is a potential endogenous inhibitor of proteolytic activation of Sendai virus and influenza A virus. FEBS. Lett. 322:115-119.
    • (1993) FEBS. Lett. , vol.322 , pp. 115-119
    • Kido, H.1    Sakai, K.2    Kishino, Y.3    Tashiro, M.4
  • 69
    • 0026689352 scopus 로고
    • Isolation and characterization of a novel trypsin-like protease found in rat bronchiolar epithelial Clara cells. A possible activator of the viral fusion glycoprotein
    • Kido, H., Y. Yokogoshi, K. Sakai, M. Tashiro, Y. Kishino, A. Fukutomi, and N. Katunuma. 1992. Isolation and characterization of a novel trypsin-like protease found in rat bronchiolar epithelial Clara cells. A possible activator of the viral fusion glycoprotein. J. Biol. Chem. 267:13573-13579.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13573-13579
    • Kido, H.1    Yokogoshi, Y.2    Sakai, K.3    Tashiro, M.4    Kishino, Y.5    Fukutomi, A.6    Katunuma, N.7
  • 70
    • 0021924118 scopus 로고
    • Phosphopeptide fingerprints of nucleoproteins of various influenza A virus strains grown in different host cells
    • Kistner, O., H. Muller, H. Becht, and C. Scholtissek. 1985. Phosphopeptide fingerprints of nucleoproteins of various influenza A virus strains grown in different host cells. J. Gen. Virol. 66:465-472.
    • (1985) J. Gen. Virol. , vol.66 , pp. 465-472
    • Kistner, O.1    Muller, H.2    Becht, H.3    Scholtissek, C.4
  • 71
    • 0024445913 scopus 로고
    • Differential phosphorylation of the nucleoprotein of influenza A viruses
    • Kistner, O., K. Muller, and C. Scholtissek. 1989. Differential phosphorylation of the nucleoprotein of influenza A viruses. J. Gen. Virol. 70:2421-2431.
    • (1989) J. Gen. Virol. , vol.70 , pp. 2421-2431
    • Kistner, O.1    Muller, K.2    Scholtissek, C.3
  • 72
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk, H.D., and W. Garten. 1994. Host cell proteases controlling virus pathogenicity. Trends. Microbiol. 2:39-43.
    • (1994) Trends. Microbiol. , vol.2 , pp. 39-43
    • Klenk, H.D.1    Garten, W.2
  • 73
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk, H.D., R. Rott, M. Orlich, and J. Blodorn. 1975. Activation of influenza A viruses by trypsin treatment. Virology. 68:426-137.
    • (1975) Virology , vol.68 , pp. 426-1137
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 74
    • 0031887717 scopus 로고    scopus 로고
    • Role of oxidants in influenza virus-induced gene expression
    • Knobil, K., A.M. Choi, G.W. Weigand, and D.B. Jacoby. 1998. Role of oxidants in influenza virus-induced gene expression. Am. J. Physiol. 274:L134-L142.
    • (1998) Am. J. Physiol. , vol.274
    • Knobil, K.1    Choi, A.M.2    Weigand, G.W.3    Jacoby, D.B.4
  • 75
    • 0030796172 scopus 로고    scopus 로고
    • Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks
    • Kobasa, D., M.E. Rodgers, K. Wells, and Y. Kawaoka. 1997. Neuraminidase hemadsorption activity, conserved in avian influenza A viruses, does not influence viral replication in ducks. J. Virol. 71:6706-6713.
    • (1997) J. Virol. , vol.71 , pp. 6706-6713
    • Kobasa, D.1    Rodgers, M.E.2    Wells, K.3    Kawaoka, Y.4
  • 76
    • 0033548268 scopus 로고    scopus 로고
    • GTP-bound human MxA protein interacts with the nucleocapsids of thogoto virus (Orthomyxoviridae)
    • Kochs, G., and O. Haller. 1999. GTP-bound human MxA protein interacts with the nucleocapsids of thogoto virus (Orthomyxoviridae). J. Biol. Chem. 274:4370-4376.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4370-4376
    • Kochs, G.1    Haller, O.2
  • 77
    • 0033514947 scopus 로고    scopus 로고
    • Interferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids
    • Kochs, G., and O. Haller. 1999. Interferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids. Proc. Natl. Acad. Sci. USA 96:2082-2086.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2082-2086
    • Kochs, G.1    Haller, O.2
  • 78
  • 79
    • 0018703697 scopus 로고
    • Are the 5′ ends of influenza viral mRNAs synthesized in vivo donated by host mRNAs?
    • Krug, R.M., B.A. Broni, and M. Bouloy. 1979. Are the 5′ ends of influenza viral mRNAs synthesized in vivo donated by host mRNAs? Cell. 18:329-334.
    • (1979) Cell , vol.18 , pp. 329-334
    • Krug, R.M.1    Broni, B.A.2    Bouloy, M.3
  • 80
    • 0022374451 scopus 로고
    • Inhibition of influenza viral mRNA synthesis in cells expressing the interferon-induced Mx gene product
    • Krug, R.M., M. Shaw, B. Broni, G. Shapiro, and O. Haller. 1985. Inhibition of influenza viral mRNA synthesis in cells expressing the interferon-induced Mx gene product. J. Virol. 56:201-206.
    • (1985) J. Virol. , vol.56 , pp. 201-206
    • Krug, R.M.1    Shaw, M.2    Broni, B.3    Shapiro, G.4    Haller, O.5
  • 81
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To TPR or not to TPR?
    • Lamb, J.R., S. Tugendreich, and P. Hieter. 1995. Tetratrico peptide repeat interactions: to TPR or not to TPR? Trends. Biochem. Sci. 20:257-259.
    • (1995) Trends. Biochem. Sci. , vol.20 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 82
    • 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., P.W. Choppin, R.M. Chanock, and C.J. Lai. 1980. Mapping of the two overlapping genes for polypeptides NS1 and NS2 on RNA segment 8 of influenza virus genome. Proc. Natl. Acad. Sci. USA 77:1857-1861.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1857-1861
    • Lamb, R.A.1    Choppin, P.W.2    Chanock, R.M.3    Lai, C.J.4
  • 83
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • B.N.e.a. Fields (ed.), Lippincott-Raven Publishers, Philadelphia
    • Lamb, R.A., and R.M. Krug. 1996. Orthomyxoviridae: The viruses and their replication, p. 1353-1395. In B.N.e.a. Fields (ed.), Fields Virology, Third edition ed. Lippincott-Raven Publishers, Philadelphia.
    • (1996) Fields Virology, Third Edition Ed. , pp. 1353-1395
    • Lamb, R.A.1    Krug, R.M.2
  • 84
    • 0019859896 scopus 로고
    • Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: Colinear and interrupted mRNAs code for overlapping proteins
    • Lamb, R.A., C.J. Lai, and P.W. Choppin. 1981. Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins. Proc. Natl. Acad. Sci. U S A. 78:4170-4174.
    • (1981) Proc. Natl. Acad. Sci. U S A , vol.78 , pp. 4170-4174
    • Lamb, R.A.1    Lai, C.J.2    Choppin, P.W.3
  • 85
    • 0022467016 scopus 로고
    • Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids
    • Lambrecht, B., and M.F. Schmidt. 1986. Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids. FEBS. Lett. 202:127-132.
    • (1986) FEBS. Lett. , vol.202 , pp. 127-132
    • Lambrecht, B.1    Schmidt, M.F.2
  • 86
    • 0016590407 scopus 로고
    • Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide
    • Lazarowitz, S.G., and P.W. Choppin. 1975. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology. 68:440-454.
    • (1975) Virology , vol.68 , pp. 440-454
    • Lazarowitz, S.G.1    Choppin, P.W.2
  • 87
    • 0015862870 scopus 로고
    • Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: Host cell activation of serum plasminogen
    • Lazarowitz, S.G., A.R. Goldberg, and P.W. Choppin. 1973. Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: host cell activation of serum plasminogen. Virology 56:172-180.
    • (1973) Virology , vol.56 , pp. 172-180
    • Lazarowitz, S.G.1    Goldberg, A.R.2    Choppin, P.W.3
  • 88
    • 0028290902 scopus 로고
    • The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis
    • Lee, S.B., and M. Esteban. 1994. The interferon-induced double-stranded RNA-activated protein kinase induces apoptosis. Virology. 199:491-496.
    • (1994) Virology , vol.199 , pp. 491-496
    • Lee, S.B.1    Esteban, M.2
  • 89
    • 0027949937 scopus 로고
    • The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins
    • Lee, T.G., N. Tang, S. Thompson, J. Miller, and M.G. Katze. 1994. The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins. Mol. Cell. Biol. 14:2331-2342.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2331-2342
    • Lee, T.G.1    Tang, N.2    Thompson, S.3    Miller, J.4    Katze, M.G.5
  • 90
    • 0026628369 scopus 로고
    • Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase
    • Lee, T.G., J. Tomita, A.G. Hovanessian, and M.G. Katze. 1992. Characterization and regulation of the 58,000-dalton cellular inhibitor of the interferon-induced, dsRNA-activated protein kinase. J. Biol. Chem. 267: 14238-14243.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14238-14243
    • Lee, T.G.1    Tomita, J.2    Hovanessian, A.G.3    Katze, M.G.4
  • 91
    • 0024973850 scopus 로고
    • Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm
    • Legrain, P., and M. Rosbash. 1989. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell. 57:573-583.
    • (1989) Cell , vol.57 , pp. 573-583
    • Legrain, P.1    Rosbash, M.2
  • 92
    • 0032189818 scopus 로고    scopus 로고
    • RNA-dependent activation of primer RNA production by influenza virus polymerase: Different regions of the same protein subunit constitute the two required RNA-binding sites
    • Li, M.L., B.C. Ramirez, and R.M. Krug. 1998. RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites. EMBO. J. 17:5844-5852.
    • (1998) EMBO. J. , vol.17 , pp. 5844-5852
    • Li, M.L.1    Ramirez, B.C.2    Krug, R.M.3
  • 93
    • 0027519686 scopus 로고
    • Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus
    • Li, S., J. Schulman, S. Itamura, and P. Palese. 1993. Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus. J. Virol. 67:6667-6673.
    • (1993) J. Virol. , vol.67 , pp. 6667-6673
    • Li, S.1    Schulman, J.2    Itamura, S.3    Palese, P.4
  • 94
    • 0028040760 scopus 로고
    • The influenza virus NS1 protein: A novel inhibitor of pre-mRNA splicing
    • Lu, Y., X.Y. Qian, and R.M. Krug. 1994. The influenza virus NS1 protein: a novel inhibitor of pre-mRNA splicing. Genes. Dev. 8:1817-1828.
    • (1994) Genes. Dev. , vol.8 , pp. 1817-1828
    • Lu, Y.1    Qian, X.Y.2    Krug, R.M.3
  • 95
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the e1F-2 translation initiation factor
    • Lu, Y., M. Wambach, M.G. Katze, and R.M. Krug. 1995. Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the e1F-2 translation initiation factor. Virology. 214:222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 96
    • 0026814133 scopus 로고
    • Genetic analysis of influenza virus
    • Luo, G., and P. Palese. 1992. Genetic analysis of influenza virus. Curr. Opin. Genet. Dev. 2:77-81.
    • (1992) Curr. Opin. Genet. Dev. , vol.2 , pp. 77-81
    • Luo, G.1    Palese, P.2
  • 97
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin, K., and A. Helenius. 1991. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell. 67:117-130.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 98
    • 0030848463 scopus 로고    scopus 로고
    • The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores
    • Melikyan, G.B. H. Jin, R.A. Lamb, and F.S. Cohen. 1997. The role of the cytoplasmic tail region of influenza virus hemagglutinin in formation and growth of fusion pores. Virology. 235:118-128.
    • (1997) Virology , vol.235 , pp. 118-128
    • Melikyan, G.B.1    Jin, H.2    Lamb, R.A.3    Cohen, F.S.4
  • 99
  • 100
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick, W.C. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56:291-315.
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 101
    • 0031041235 scopus 로고    scopus 로고
    • The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study
    • Mir-Shekari, S.Y., D.A. Ashford, D.J. Harvey, R.A. Dwek, and I.T. Schulze. 1997. The glycosylation of the influenza A virus hemagglutinin by mammalian cells. A site-specific study. J. Biol. Chem. 272:4027-4036.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4027-4036
    • Mir-Shekari, S.Y.1    Ashford, D.A.2    Harvey, D.J.3    Dwek, R.A.4    Schulze, I.T.5
  • 102
    • 0030440695 scopus 로고    scopus 로고
    • Identification of host factors that regulate the influenza virus RNA polymerase activity
    • Momose, F., H. Handa, and K. Nagata. 1996. Identification of host factors that regulate the influenza virus RNA polymerase activity. Biochimie. 78:1103-1108.
    • (1996) Biochimie. , vol.78 , pp. 1103-1108
    • Momose, F.1    Handa, H.2    Nagata, K.3
  • 103
    • 0026642422 scopus 로고
    • Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size
    • Munk, K., E. Pritzer, E. Kretzschmar, B. Gutte, W. Garten, and H.D. Klenk. 1992. Carbohydrate masking of an antigenic epitope of influenza virus haemagglutinin independent of oligosaccharide size. Glycobiology. 2:233-240.
    • (1992) Glycobiology , vol.2 , pp. 233-240
    • Munk, K.1    Pritzer, E.2    Kretzschmar, E.3    Gutte, B.4    Garten, W.5    Klenk, H.D.6
  • 104
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C.W., and D. Williams. 1990. Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO. J. 9:3857-3866.
    • (1990) EMBO. J. , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 105
    • 0025185465 scopus 로고
    • Tumor necrosis factor-alpha production of influenza A virus-infected macrophages and potentiating effect of lipopolysaccharides
    • Nain, M., F. Hinder, J.H. Gong, A. Schmidt, A. Bender, H. Sprenger, and D. Gemsa. 1990. Tumor necrosis factor-alpha production of influenza A virus-infected macrophages and potentiating effect of lipopolysaccharides. J. Immunol. 145:1921-1928.
    • (1990) J. Immunol. , vol.145 , pp. 1921-1928
    • Nain, M.1    Hinder, F.2    Gong, J.H.3    Schmidt, A.4    Bender, A.5    Sprenger, H.6    Gemsa, D.7
  • 106
    • 0025720687 scopus 로고
    • Interferon-inducible mouse Mx1 protein that confers resistance to influenza virus is GTPase
    • Nakayama, M., K. Nagata, A. Kato, and A. Ishihama. 1991. Interferon-inducible mouse Mx1 protein that confers resistance to influenza virus is GTPase. J. Biol. Chem. 266:21404-21408.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21404-21408
    • Nakayama, M.1    Nagata, K.2    Kato, A.3    Ishihama, A.4
  • 107
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′end formation of cellular pre-mRNAs
    • Nemeroff, M.E., S.M. Barabino, Y. Li, W. Keller, and R.M. Krug. 1998. Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′end formation of cellular pre-mRNAs. Mol. Cell. 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
  • 108
    • 0030731422 scopus 로고    scopus 로고
    • Nuclear import and export of influenza virus nucleoprotein
    • Neumann, G., M.R. Castrucci, and Y. Kawaoka. 1997. Nuclear import and export of influenza virus nucleoprotein. J Virol 71:9690-700.
    • (1997) J Virol , vol.71 , pp. 9690-9700
    • Neumann, G.1    Castrucci, M.R.2    Kawaoka, Y.3
  • 109
    • 0029130751 scopus 로고
    • Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import
    • O'Neill, R.E., R. Jaskunas, G. Blobel, P. Palese, and J. Moroianu. 1995. Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import. J Biol Chem. 270:22701-22704.
    • (1995) J Biol Chem. , vol.270 , pp. 22701-22704
    • O'Neill, R.E.1    Jaskunas, R.2    Blobel, G.3    Palese, P.4    Moroianu, J.5
  • 110
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill, R.E., J. Talon, and P. Palese. 1998. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO. J. 17:288-296.
    • (1998) EMBO. J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 111
    • 0030863130 scopus 로고    scopus 로고
    • Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety
    • Ohuchi, M., R. Ohuchi, A. Feldmann, and H.D. Klenk. 1997. Regulation of receptor binding affinity of influenza virus hemagglutinin by its carbohydrate moiety. J. Virol. 71:8377-8384.
    • (1997) J. Virol. , vol.71 , pp. 8377-8384
    • Ohuchi, M.1    Ohuchi, R.2    Feldmann, A.3    Klenk, H.D.4
  • 112
    • 0030940057 scopus 로고    scopus 로고
    • Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity
    • Ohuchi, R., M. Ohuchi, W. Garten, and H.D. Klenk. 1997. Oligosaccharides in the stem region maintain the influenza virus hemagglutinin in the metastable form required for fusion activity. J. Virol. 71:3719-3725.
    • (1997) J. Virol. , vol.71 , pp. 3719-3725
    • Ohuchi, R.1    Ohuchi, M.2    Garten, W.3    Klenk, H.D.4
  • 113
    • 0029978905 scopus 로고    scopus 로고
    • The influence of calcium and reactive oxygen species on influenza-virus induced apoptosis
    • Olsen, C.W., N. Dybdahl-Sissolo, and V.S. Hinshaw. 1996. The influence of calcium and reactive oxygen species on influenza-virus induced apoptosis. Cell. Death. Differ. 3:191-197.
    • (1996) Cell. Death. Differ. , vol.3 , pp. 191-197
    • Olsen, C.W.1    Dybdahl-Sissolo, N.2    Hinshaw, V.S.3
  • 114
    • 0029656251 scopus 로고    scopus 로고
    • Bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation
    • Olsen, C.W., J.C. Kehren, N.R. Dybdahl-Sissoko, and V.S. Hinshaw. 1996. Bcl-2 alters influenza virus yield, spread, and hemagglutinin glycosylation. J. Virol. 70:663-666.
    • (1996) J. Virol. , vol.70 , pp. 663-666
    • Olsen, C.W.1    Kehren, J.C.2    Dybdahl-Sissoko, N.R.3    Hinshaw, V.S.4
  • 115
    • 0031956578 scopus 로고    scopus 로고
    • Multiple levels of posttranscriptional regulation of influenza virus gene expression
    • Ortin, J. 1998. Multiple levels of posttranscriptional regulation of influenza virus gene expression. Semin. Virol. 8:335-342.
    • (1998) Semin. Virol. , vol.8 , pp. 335-342
    • Ortin, J.1
  • 116
    • 0031081340 scopus 로고    scopus 로고
    • The ER-overload response: Activation of NF-kappa B
    • Pahl, H.L., and P.A. Baeuerle. 1997. The ER-overload response: activation of NF-kappa B. Trends. Biochem. Sci. 22:63-67.
    • (1997) Trends. Biochem. Sci. , vol.22 , pp. 63-67
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 117
    • 0028797157 scopus 로고
    • Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B
    • Pahl, H.L., and P.A. Baeuerle. 1995. Expression of influenza virus hemagglutinin activates transcription factor NF-kappa B. J. Virol. 69:1480-1484.
    • (1995) J. Virol. , vol.69 , pp. 1480-1484
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 119
    • 0026524496 scopus 로고
    • Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle
    • Pavlovic, J., O. Haller, and P. Staeheli. 1992. Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle. J. Virol. 66:2564-2569.
    • (1992) J. Virol. , vol.66 , pp. 2564-2569
    • Pavlovic, J.1    Haller, O.2    Staeheli, P.3
  • 120
    • 0025331030 scopus 로고
    • Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein
    • Pavlovic, J., T. Zurcher, O. Haller, and P. Staeheli. 1990. Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein. J. Virol. 64:3370-3375.
    • (1990) J. Virol. , vol.64 , pp. 3370-3375
    • Pavlovic, J.1    Zurcher, T.2    Haller, O.3    Staeheli, P.4
  • 121
    • 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., and R.O. Donis. 1998. The matrix 1 protein of influenza A virus inhibits the transcriptase activity of a model influenza reporter genome in vivo. Virology. 249:52-61.
    • (1998) Virology , vol.249 , pp. 52-61
    • Perez, D.R.1    Donis, R.O.2
  • 122
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins
    • Peterson, J.R., A. Ora, P.N. Van, and A. Helenius. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Mol. Biol. Cell. 6:1173-1184.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van, P.N.3    Helenius, A.4
  • 123
    • 0019775198 scopus 로고
    • Phosphorylation of influenza virus nucleoprotein in vivo
    • Petri, T., and N.J. Dimmock. 1981. Phosphorylation of influenza virus nucleoprotein in vivo. J. Gen. Virol. 57:185-190.
    • (1981) J. Gen. Virol. , vol.57 , pp. 185-190
    • Petri, T.1    Dimmock, N.J.2
  • 124
    • 0029033820 scopus 로고
    • Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment
    • Philipp, H.C., B. Schroth, M. Veit, M. Krumbiegel, A. Herrmann, and M.F. Schmidt. 1995. Assessment of fusogenic properties of influenza virus hemagglutinin deacylated by site-directed mutagenesis and hydroxylamine treatment. Virology. 210:20-28.
    • (1995) Virology , vol.210 , pp. 20-28
    • Philipp, H.C.1    Schroth, B.2    Veit, M.3    Krumbiegel, M.4    Herrmann, A.5    Schmidt, M.F.6
  • 126
    • 0030026945 scopus 로고    scopus 로고
    • The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinse, PKR, to regulate its autophosphorylation and activity
    • Polyak, S.J., N. Tang, M. Wambach, G.N. Barber, and M.G. Katze. 1996. The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinse, PKR, to regulate its autophosphorylation and activity. J. Biol. Chem. 271:1702-1707.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1702-1707
    • Polyak, S.J.1    Tang, N.2    Wambach, M.3    Barber, G.N.4    Katze, M.G.5
  • 127
    • 0018098135 scopus 로고
    • Influenza virus proteins: Identity, synthesis, and modification analyzed by two-dimensional gel electrophoresis
    • Privalsky, M.L., and E.E. Penhoet. 1978. Influenza virus proteins: identity, synthesis, and modification analyzed by two-dimensional gel electrophoresis. Proc. Natl. Acad. Sci. USA 75:3625-3629.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3625-3629
    • Privalsky, M.L.1    Penhoet, E.E.2
  • 128
    • 0017673521 scopus 로고
    • Phosphorylated protein component present in influenza virions
    • Privalsky, M.L., and E.E. Penhoet. 1977. Phosphorylated protein component present in influenza virions. J. Virol. 24:401-405.
    • (1977) J. Virol. , vol.24 , pp. 401-405
    • Privalsky, M.L.1    Penhoet, E.E.2
  • 129
    • 0019424258 scopus 로고
    • The structure and synthesis of influenza virus phosphoproteins
    • Privalsky, M.L., and E.E. Penhoet. 1981. The structure and synthesis of influenza virus phosphoproteins. J. Biol. Chem. 256:5368-5376.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5368-5376
    • Privalsky, M.L.1    Penhoet, E.E.2
  • 130
    • 0028274131 scopus 로고
    • The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A)
    • Qiu, Y., and R.M. Krug. 1994. The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J. Virol. 68:2425-2432.
    • (1994) J. Virol. , vol.68 , pp. 2425-2432
    • Qiu, Y.1    Krug, R.M.2
  • 131
    • 0029295578 scopus 로고
    • The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 and U6-U4 snRNA interactions during splicing
    • Qiu, Y., M. Nemeroff, and R.M. Krug. 1995. The influenza virus NS1 protein binds to a specific region in human U6 snRNA and inhibits U6-U2 and U6-U4 snRNA interactions during splicing. RNA. 1:304-316.
    • (1995) RNA , vol.1 , pp. 304-316
    • Qiu, Y.1    Nemeroff, M.2    Krug, R.M.3
  • 132
    • 0032409781 scopus 로고    scopus 로고
    • Bcl-2 family proteins
    • Reed, J.C. 1998. Bcl-2 family proteins. Oncogene. 17:3225-3236.
    • (1998) Oncogene. , vol.17 , pp. 3225-3236
    • Reed, J.C.1
  • 133
    • 0026726876 scopus 로고
    • Nuclear retention of Ml protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins
    • Rey, O., and D.P. Nayak. 1992. Nuclear retention of Ml protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins. J. Virol. 66:5815-5824.
    • (1992) J. Virol. , vol.66 , pp. 5815-5824
    • Rey, O.1    Nayak, D.P.2
  • 134
    • 0025924358 scopus 로고
    • NS2 protein of influenza virus is found in purified virus and phosphorylated in infected cells
    • Richardson, J.C., and R.K. Akkina. 1991. NS2 protein of influenza virus is found in purified virus and phosphorylated in infected cells. Arch. Virol. 116:69-80.
    • (1991) Arch. Virol. , vol.116 , pp. 69-80
    • Richardson, J.C.1    Akkina, R.K.2
  • 135
    • 0021186349 scopus 로고
    • Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells
    • Rindler, M.J., I.E. Ivanov, H. Plesken, E. Rodriguez-Boulan, and D.D. Sabatini. 1984. Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells. J. Cell. Biol. 98:1304-1319.
    • (1984) J. Cell. Biol. , vol.98 , pp. 1304-1319
    • Rindler, M.J.1    Ivanov, I.E.2    Plesken, H.3    Rodriguez-Boulan, E.4    Sabatini, D.D.5
  • 136
    • 0017640508 scopus 로고
    • Identification of the defective genes in three mutant groups of influenza virus
    • Ritchey, M.B., and P. Palese. 1977. Identification of the defective genes in three mutant groups of influenza virus. J. Virol. 21:1196-1204.
    • (1977) J. Virol. , vol.21 , pp. 1196-1204
    • Ritchey, M.B.1    Palese, P.2
  • 137
    • 0022590991 scopus 로고
    • Interleukin 1 and interleukin 1 inhibitor production by human macrophages exposed to influenza virus or respiratory syncytial virus. Respiratory syncytial virus is a potent inducer of inhibitor activity
    • Roberts, N.J., Jr., A.M. Prill, and T.N. Mann. 1986. Interleukin 1 and interleukin 1 inhibitor production by human macrophages exposed to influenza virus or respiratory syncytial virus. Respiratory syncytial virus is a potent inducer of inhibitor activity. J. Exp. Med. 163:511-519.
    • (1986) J. Exp. Med. , vol.163 , pp. 511-519
    • Roberts Jr., N.J.1    Prill, A.M.2    Mann, T.N.3
  • 138
    • 0020569368 scopus 로고
    • Assembly of enveloped viruses in Madin-Darby canine kidney cells: Polarized budding from single attached cells and from clusters of cells in suspension
    • Rodriguez-Boulan, E., K.T. Paskiet, and D.D. Sabatini. 1983. Assembly of enveloped viruses in Madin-Darby canine kidney cells: polarized budding from single attached cells and from clusters of cells in suspension. J. Cell. Biol. 96:866-874.
    • (1983) J. Cell. Biol. , vol.96 , pp. 866-874
    • Rodriguez-Boulan, E.1    Paskiet, K.T.2    Sabatini, D.D.3
  • 139
    • 0021350457 scopus 로고
    • Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells
    • Rodriguez-Boulan, E., K.T. Paskiet, P.J. Salas, and E. Bard. 1984. Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells. J Cell Biol. 98:308-19.
    • (1984) J Cell Biol. , vol.98 , pp. 308-319
    • Rodriguez-Boulan, E.1    Paskiet, K.T.2    Salas, P.J.3    Bard, E.4
  • 140
    • 0031093544 scopus 로고    scopus 로고
    • Regulation of IFN-alpha/beta, MxA, 2′,5′-oligoadenylate synthetase, and HLA gene expression in influenza A-infected human lung epithelial cells
    • Ronni, T., S. Matikainen, T. Sareneva, K. Melen, J. Pirhonen, P. Keskinen, and I. Julkunen. 1997. Regulation of IFN-alpha/beta, MxA, 2′,5′-oligoadenylate synthetase, and HLA gene expression in influenza A-infected human lung epithelial cells. J. Immunol. 158:2363-2374.
    • (1997) J. Immunol. , vol.158 , pp. 2363-2374
    • Ronni, T.1    Matikainen, S.2    Sareneva, T.3    Melen, K.4    Pirhonen, J.5    Keskinen, P.6    Julkunen, I.7
  • 142
    • 0014931490 scopus 로고
    • Specific inhibition of influenza replication by alpha-amanitin
    • Rott, R., and C. Scholtissek. 1970. Specific inhibition of influenza replication by alpha-amanitin. Nature. 228:56.
    • (1970) Nature , vol.228 , pp. 56
    • Rott, R.1    Scholtissek, C.2
  • 143
    • 0031243735 scopus 로고    scopus 로고
    • Loss of glycosylation at Asn144 alters the substrate preference of the N8 influenza A virus neuraminidase
    • Saito, T., and K. Kawano. 1997. Loss of glycosylation at Asn144 alters the substrate preference of the N8 influenza A virus neuraminidase. J. Vet. Med. Sci. 59:923-926.
    • (1997) J. Vet. Med. Sci. , vol.59 , pp. 923-926
    • Saito, T.1    Kawano, K.2
  • 144
    • 0029015326 scopus 로고
    • Steps in maturation of influenza A virus neuraminidase
    • Saito, T., G. Taylor, and R.G. Webster. 1995. Steps in maturation of influenza A virus neuraminidase. J. Virol. 69:5011-5017.
    • (1995) J. Virol. , vol.69 , pp. 5011-5017
    • Saito, T.1    Taylor, G.2    Webster, R.G.3
  • 145
    • 0028211145 scopus 로고
    • Sendai virus infection changes the subcellular localization of tryptase Clara in rat bronchiolar epithelial cells
    • Sakai, K., T. Kohri, M. Tashiro, Y. Kishino, and H. Kido. 1994. Sendai virus infection changes the subcellular localization of tryptase Clara in rat bronchiolar epithelial cells. Eur. Respir. J. 7:686-692.
    • (1994) Eur. Respir. J. , vol.7 , pp. 686-692
    • Sakai, K.1    Kohri, T.2    Tashiro, M.3    Kishino, Y.4    Kido, H.5
  • 146
    • 0025739093 scopus 로고
    • Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly selective antiviral activities
    • Samuel, C.E. 1991. Antiviral actions of interferon. Interferon-regulated cellular proteins and their surprisingly selective antiviral activities. Virology. 183:1-11.
    • (1991) Virology , vol.183 , pp. 1-11
    • Samuel, C.E.1
  • 148
    • 0026706343 scopus 로고
    • Interactions between bacteria and influenza A virus in the development of influenza pneumonia
    • Scheiblauer, H., M. Reinacher, M. Tashiro, and R. Rott. 1992. Interactions between bacteria and influenza A virus in the development of influenza pneumonia. J. Infect. Dis. 166:783-791.
    • (1992) J. Infect. Dis. , vol.166 , pp. 783-791
    • Scheiblauer, H.1    Reinacher, M.2    Tashiro, M.3    Rott, R.4
  • 149
    • 0029069145 scopus 로고
    • Transcriptional responses to polypeptide ligands: The JAK-STAT pathway
    • Schindler, C., and J.E. Darnell, Jr. 1995. Transcriptional responses to polypeptide ligands: the JAK-STAT pathway. Annu. Rev. Biochem. 64:621-651.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 621-651
    • Schindler, C.1    Darnell Jr., J.E.2
  • 150
    • 0020077726 scopus 로고
    • Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses
    • Schmidt, M.F. 1982. Acylation of viral spike glycoproteins: a feature of enveloped RNA viruses. Virology. 116:327-338.
    • (1982) Virology , vol.116 , pp. 327-338
    • Schmidt, M.F.1
  • 151
    • 0025987805 scopus 로고
    • Failure to obtain drug-resistant variants of influenza virus after treatment with inhibiting doses of 3-deazaadenosine and H7
    • Scholtissek, C., and K. Muller. 1991. Failure to obtain drug-resistant variants of influenza virus after treatment with inhibiting doses of 3-deazaadenosine and H7. Arch. Virol. 119:111-118.
    • (1991) Arch. Virol. , vol.119 , pp. 111-118
    • Scholtissek, C.1    Muller, K.2
  • 152
    • 0029861191 scopus 로고    scopus 로고
    • Influenza virus neuraminidase activates latent transforming growth factor beta
    • Schultz-Cherry, S., and V.S. Hinshaw. 1996. Influenza virus neuraminidase activates latent transforming growth factor beta. J. Virol. 70:8624-8629.
    • (1996) J. Virol. , vol.70 , pp. 8624-8629
    • Schultz-Cherry, S.1    Hinshaw, V.S.2
  • 154
    • 0030740376 scopus 로고    scopus 로고
    • Effects of glycosylation on the properties and functions of influenza virus hemagglutinin
    • Schulze, I.T. 1997. Effects of glycosylation on the properties and functions of influenza virus hemagglutinin. J. Infect. Dis. 176(Suppl 1):S24-S28.
    • (1997) J. Infect. Dis. , vol.176 , Issue.1 SUPPL.
    • Schulze, I.T.1
  • 155
    • 0023155247 scopus 로고
    • Influenza virus gene expression: Control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs
    • Shapiro, G.I., T. Gurney, Jr., and R.M. Krug. 1987. Influenza virus gene expression: control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs. J. Virol. 61:764-773.
    • (1987) J. Virol. , vol.61 , pp. 764-773
    • Shapiro, G.I.1    Gurney Jr., T.2    Krug, R.M.3
  • 156
    • 0023948949 scopus 로고
    • Influenza virus RNA replication in vitro: Synthesis of viral template RNAs and virion RNAs in the absence of an added primer
    • Shapiro, G.I., and R.M. Krug. 1988. Influenza virus RNA replication in vitro: Synthesis of viral template RNAs and virion RNAs in the absence of an added primer. J. Virol. 62:2285-2290.
    • (1988) J. Virol. , vol.62 , pp. 2285-2290
    • Shapiro, G.I.1    Krug, R.M.2
  • 157
    • 0029887169 scopus 로고    scopus 로고
    • Recombinant-baculovirus-expressed PB2 subunit of the influenza A virus RNA polymerase binds cap groups as an isolated subunit
    • Shi, L., J.M. Galarza, and D.F. Summers. 1996. Recombinant-baculovirus-expressed PB2 subunit of the influenza A virus RNA polymerase binds cap groups as an isolated subunit. Virus. Res. 42:1-9.
    • (1996) Virus. Res. , vol.42 , pp. 1-9
    • Shi, L.1    Galarza, J.M.2    Summers, D.F.3
  • 158
    • 0026531034 scopus 로고
    • Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity
    • Simpson, D.A., and R.A. Lamb. 1992. Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity. J. Virol. 66:790-803.
    • (1992) J. Virol. , vol.66 , pp. 790-803
    • Simpson, D.A.1    Lamb, R.A.2
  • 159
    • 0029831336 scopus 로고    scopus 로고
    • Selective induction of monocyte and not neutrophil-attracting chemokines after influenza A virus infection
    • Sprenger, H., R.G. Meyer, A. Kaufmann, D. Bussfeld, E. Rischkowsky, and D. Gemsa. 1996. Selective induction of monocyte and not neutrophil-attracting chemokines after influenza A virus infection. J. Exp. Med. 184:1191-1196.
    • (1996) J. Exp. Med. , vol.184 , pp. 1191-1196
    • Sprenger, H.1    Meyer, R.G.2    Kaufmann, A.3    Bussfeld, D.4    Rischkowsky, E.5    Gemsa, D.6
  • 160
    • 0025138795 scopus 로고
    • Interferon-induced proteins and the antiviral state
    • Staeheli, P. 1990. Interferon-induced proteins and the antiviral state. Adv. Virus. Res. 38:147-200.
    • (1990) Adv. Virus. Res. , vol.38 , pp. 147-200
    • Staeheli, P.1
  • 161
    • 0025882934 scopus 로고
    • Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • Steinhauer, D.A., S.A. Wharton, D.C. Wiley, and J.J. Skehel. 1991. Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties. Virology. 184:445-448.
    • (1991) Virology , vol.184 , pp. 445-448
    • Steinhauer, D.A.1    Wharton, S.A.2    Wiley, D.C.3    Skehel, J.J.4
  • 162
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilism-like endoprotease
    • Stieneke-Grober, A., M. Vey, H. Angliker, E. Shaw, G. Thomas, C. Roberts, H.D. Klenk, and W. Garten. 1992. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilism-like endoprotease. EMBO. J. 11:2407-2414.
    • (1992) EMBO. J. , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.D.7    Garten, W.8
  • 163
    • 0027372154 scopus 로고
    • Function of the mouse Mx1 protein is inhibited by overexpression of the PB2 protein of influenza virus
    • Stranden, A.M., P. Staeheli, and J. Pavlovic. 1993. Function of the mouse Mx1 protein is inhibited by overexpression of the PB2 protein of influenza virus. Virology. 197:642-651.
    • (1993) Virology , vol.197 , pp. 642-651
    • Stranden, A.M.1    Staeheli, P.2    Pavlovic, J.3
  • 164
    • 0016838637 scopus 로고
    • Further isolation and characterization of temperature-sensitive mutants of influenza virus
    • Sugiura, A., M. Ueda, K. Tobita, and C. Enomoto. 1975. Further isolation and characterization of temperature-sensitive mutants of influenza virus. Virology. 65:363-373.
    • (1975) Virology , vol.65 , pp. 363-373
    • Sugiura, A.1    Ueda, M.2    Tobita, K.3    Enomoto, C.4
  • 165
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R.J., and A.J. Hay. 1991. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology. 180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 166
    • 0029063283 scopus 로고
    • Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon
    • Takizawa, T., R. Fukuda, T. Miyawaki, K. Ohashi, and Y. Nakanishi. 1995. Activation of the apoptotic Fas antigen-encoding gene upon influenza virus infection involving spontaneously produced beta-interferon. Virology. 209:288-296.
    • (1995) Virology , vol.209 , pp. 288-296
    • Takizawa, T.1    Fukuda, R.2    Miyawaki, T.3    Ohashi, K.4    Nakanishi, Y.5
  • 167
    • 0027382362 scopus 로고
    • Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells
    • Takizawa, T., S. Matsukawa, Y. Higuchi, S. Nakamura, Y. Nakanishi, and R. Fukuda. 1993. Induction of programmed cell death (apoptosis) by influenza virus infection in tissue culture cells. J. Gen. Virol. 74:2347-2355.
    • (1993) J. Gen. Virol. , vol.74 , pp. 2347-2355
    • Takizawa, T.1    Matsukawa, S.2    Higuchi, Y.3    Nakamura, S.4    Nakanishi, Y.5    Fukuda, R.6
  • 168
    • 0029842883 scopus 로고    scopus 로고
    • Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection
    • Takizawa, T., K. Ohashi, and Y. Nakanishi. 1996. Possible involvement of double-stranded RNA-activated protein kinase in cell death by influenza virus infection. J. Virol. 70:8128-8132.
    • (1996) J. Virol. , vol.70 , pp. 8128-8132
    • Takizawa, T.1    Ohashi, K.2    Nakanishi, Y.3
  • 169
    • 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., and M.G. Katze. 1998. 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. 18:757-766.
    • (1998) J. Interferon. Cytokine. Res. , vol.18 , pp. 757-766
    • Tan, S.L.1    Katze, M.G.2
  • 170
    • 0023136546 scopus 로고
    • Role of Staphylococcus protease in the development of influenza pneumonia
    • Tashiro, M., P. Ciborowski, H.D. Klenk, G. Pulverer, and R. Rott. 1987. Role of Staphylococcus protease in the development of influenza pneumonia. Nature. 325:536-537.
    • (1987) Nature , vol.325 , pp. 536-537
    • Tashiro, M.1    Ciborowski, P.2    Klenk, H.D.3    Pulverer, G.4    Rott, R.5
  • 171
    • 0023111155 scopus 로고
    • Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity
    • Tashiro, M., P. Ciborowski, M. Reinacher, G. Pulverer, H.D. Klenk, and R. Rott. 1987. Synergistic role of staphylococcal proteases in the induction of influenza virus pathogenicity. Virology. 157:421-430.
    • (1987) Virology , vol.157 , pp. 421-430
    • Tashiro, M.1    Ciborowski, P.2    Reinacher, M.3    Pulverer, G.4    Klenk, H.D.5    Rott, R.6
  • 172
    • 0026483126 scopus 로고
    • Tryptase Clara, an activating protease for Sendai virus in rat lungs, is involved in pneumopathogenicity
    • Tashiro, M., Y. Yokogoshi, K. Tobita, J.T. Seto, R. Rott, and H. Kido. 1992. Tryptase Clara, an activating protease for Sendai virus in rat lungs, is involved in pneumopathogenicity. J. Virol. 66:7211-7216.
    • (1992) J. Virol. , vol.66 , pp. 7211-7216
    • Tashiro, M.1    Yokogoshi, Y.2    Tobita, K.3    Seto, J.T.4    Rott, R.5    Kido, H.6
  • 173
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U., and A. Helenius. 1997. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell. Biol. 136:555-565.
    • (1997) J. Cell. Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 174
    • 0032488264 scopus 로고    scopus 로고
    • Phosphorylation of the M2 protein of influenza A virus is not essential for virus viability
    • Thomas, J.M., M.P. Stevens, N. Percy, and W.S. Barclay. 1998. Phosphorylation of the M2 protein of influenza A virus is not essential for virus viability. Virology. 252:54-64.
    • (1998) Virology , vol.252 , pp. 54-64
    • Thomas, J.M.1    Stevens, M.P.2    Percy, N.3    Barclay, W.S.4
  • 175
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson, C.B. 1995. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 176
    • 0003839687 scopus 로고
    • Role of two of the influenza virus core P proteins in recognizing cap 1 structures (m7GpppNm) on RNAs and in initiating viral RNA transcription
    • Ulmanen, I., B.A. Broni, and R.M. Krug. 1981. Role of two of the influenza virus core P proteins in recognizing cap 1 structures (m7GpppNm) on RNAs and in initiating viral RNA transcription. Proc. Natl. Acad. Sci. U S A. 78:7355-7359.
    • (1981) Proc. Natl. Acad. Sci. U S A , vol.78 , pp. 7355-7359
    • Ulmanen, I.1    Broni, B.A.2    Krug, R.M.3
  • 177
    • 0024458682 scopus 로고
    • Virulent avian influenza A viruses: Their effect on avian lymphocytes and macrophages in vivo and in vitro
    • Van Campen, H., B.C. Easterday, and V.S. Hinshaw. 1989. Virulent avian influenza A viruses: Their effect on avian lymphocytes and macrophages in vivo and in vitro. J. Gen. Virol. 70:2887-2895.
    • (1989) J. Gen. Virol. , vol.70 , pp. 2887-2895
    • Van Campen, H.1    Easterday, B.C.2    Hinshaw, V.S.3
  • 178
    • 0025754428 scopus 로고
    • The M2 protein of influenza A virus is acylated
    • Veit, M., H.D. Klenk, A. Kendal, and R. Rott. 1991. The M2 protein of influenza A virus is acylated. J. Gen. Virol. 72:1461-1465.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1461-1465
    • Veit, M.1    Klenk, H.D.2    Kendal, A.3    Rott, R.4
  • 179
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit, M., E. Kretzschmar, K. Kuroda, W. Garten, M.F. Schmidt, H.D. Klenk, and R. Rott. 1991. Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65:2491-2500.
    • (1991) J. Virol. , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmidt, M.F.5    Klenk, H.D.6    Rott, R.7
  • 180
    • 0028321980 scopus 로고
    • Influenza A virus late mRNAs are specifically retained in the nucleus in the presence of a methyltransferase or a protein kinase inhibitor
    • Vogel, U., M. Kunerl, and C. Scholtissek. 1994. Influenza A virus late mRNAs are specifically retained in the nucleus in the presence of a methyltransferase or a protein kinase inhibitor. Virology. 198:227-233.
    • (1994) Virology , vol.198 , pp. 227-233
    • Vogel, U.1    Kunerl, M.2    Scholtissek, C.3
  • 181
    • 0028157148 scopus 로고
    • Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus
    • Walker, J.A., S.S. Molloy, G. Thomas, T. Sakaguchi, T. Yoshida, T.M. Chambers, and Y. Kawaoka. 1994. Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus. J. Virol. 68:1213-1218.
    • (1994) J. Virol. , vol.68 , pp. 1213-1218
    • Walker, J.A.1    Molloy, S.S.2    Thomas, G.3    Sakaguchi, T.4    Yoshida, T.5    Chambers, T.M.6    Kawaoka, Y.7
  • 182
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza, a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang, P., P. Palese, and R.E. O'Neill. 1997. The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza, a virus nucleoprotein NP is a nonconventional nuclear localization signal. J Virol 71:1850-1856.
    • (1997) J Virol , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 183
    • 0032505542 scopus 로고    scopus 로고
    • A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins
    • Weber, F., G. Kochs, S. Gruber, and O. Haller. 1998. A classical bipartite nuclear localization signal on Thogoto and influenza A virus nucleoproteins. Virology 250:9-18.
    • (1998) Virology , vol.250 , pp. 9-18
    • Weber, F.1    Kochs, G.2    Gruber, S.3    Haller, O.4
  • 184
    • 0028961386 scopus 로고
    • Hyperphosphorylation of mutant influenza virus matrix protein, Ml, causes its retention in the nucleus
    • Whittaker, G., I. Kemler, and A. Helenius. 1995. Hyperphosphorylation of mutant influenza virus matrix protein, Ml, causes its retention in the nucleus. J. Virol. 69:439-445.
    • (1995) J. Virol. , vol.69 , pp. 439-445
    • Whittaker, G.1    Kemler, I.2    Helenius, A.3
  • 185
    • 0029942023 scopus 로고    scopus 로고
    • Interaction cloning of NS1-I, a human protein that binds to the non-structural NS1 proteins of influenza A and B viruses
    • Wolff, T., R.E. O'Neill, and P. Palese. 1996. Interaction cloning of NS1-I, a human protein that binds to the non-structural NS1 proteins of influenza A and B viruses. J. Virol. 70:5363-5372.
    • (1996) J. Virol. , vol.70 , pp. 5363-5372
    • Wolff, T.1    O'Neill, R.E.2    Palese, P.3
  • 186
    • 0031847217 scopus 로고    scopus 로고
    • NS1-Binding protein (NS1-BP): A novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells
    • Wolff, T., R.E. O'Neill, and P. Palese. 1998. NS1-Binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells. J. Virol. 72:7170-7180.
    • (1998) J. Virol. , vol.72 , pp. 7170-7180
    • Wolff, T.1    O'Neill, R.E.2    Palese, P.3
  • 187
    • 0023106182 scopus 로고
    • Functional and antigenic domains of the matrix (M1) protein of influenza A virus
    • Ye, Z.P., R. Pal, J.W. Fox, and R.R. Wagner. 1987. Functional and antigenic domains of the matrix (M1) protein of influenza A virus. J. Virol. 61:239-246.
    • (1987) J. Virol. , vol.61 , pp. 239-246
    • Ye, Z.P.1    Pal, R.2    Fox, J.W.3    Wagner, R.R.4
  • 188
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation
    • Zurcher, T., G. Luo, and P. Palese. 1994. Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68:5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zurcher, T.1    Luo, G.2    Palese, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.