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Volumn 36, Issue , 2002, Pages 305-332

Genetics of influenza viruses

Author keywords

Antigenicity; Mutants; Pathogenicity; Reassortment; Recombination

Indexed keywords

AMANTADINE; ANTIVIRUS AGENT; OSELTAMIVIR; RIMANTADINE; ZANAMIVIR;

EID: 0036953373     PISSN: 00664197     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.genet.36.052402.152757     Document Type: Review
Times cited : (124)

References (176)
  • 1
    • 0022257421 scopus 로고
    • Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase
    • Air GM, Els MC, Brown LE, Laver WG, Webster RG. 1985. Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase. Virology 145:237-48
    • (1985) Virology , vol.145 , pp. 237-248
    • Air, G.M.1    Els, M.C.2    Brown, L.E.3    Laver, W.G.4    Webster, R.G.5
  • 2
    • 0021253051 scopus 로고
    • Expression of defective-interfering influenza virus-specific transcripts and polypeptides in infected cells
    • Akkina RK, Chambers TM, Nayak DP. 1984. Expression of defective-interfering influenza virus-specific transcripts and polypeptides in infected cells. J. Virol. 51:395-403
    • (1984) J. Virol. , vol.51 , pp. 395-403
    • Akkina, R.K.1    Chambers, T.M.2    Nayak, D.P.3
  • 3
    • 0026060512 scopus 로고
    • Replication of avian influenza viruses in humans
    • Baere AS, Webster RG. 1991. Replication of avian influenza viruses in humans. Arch. Virol. 119:37-42
    • (1991) Arch. Virol. , vol.119 , pp. 37-42
    • Baere, A.S.1    Webster, R.G.2
  • 4
    • 0035813039 scopus 로고    scopus 로고
    • Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture
    • Baigent SJ, McCauley JW. 2001. Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture. Virus Res. 79:177-85
    • (2001) Virus Res. , vol.79 , pp. 177-185
    • Baigent, S.J.1    McCauley, J.W.2
  • 5
    • 12244293053 scopus 로고
    • Evidence for genetic interaction between non-infectious and infectious influenza A viruses
    • Baron S, Jensen KE. 1955. Evidence for genetic interaction between non-infectious and infectious influenza A viruses. J. Exp. Med. 102:677-97
    • (1955) J. Exp. Med. , vol.102 , pp. 677-697
    • Baron, S.1    Jensen, K.E.2
  • 6
    • 0018730113 scopus 로고
    • Transcription and replication of influenza virus RNA
    • Barrett T, Wolstenholme AJ, Mahy BW. 1979. Transcription and replication of influenza virus RNA. Virology 98:211-25
    • (1979) Virology , vol.98 , pp. 211-225
    • Barrett, T.1    Wolstenholme, A.J.2    Mahy, B.W.3
  • 7
    • 0012568303 scopus 로고
    • The multiplication of influenza virus. II. Multiplicity reactivation of ultraviolet irradiated virus
    • Barry RD. 1961. The multiplication of influenza virus. II. Multiplicity reactivation of ultraviolet irradiated virus. Virology 14:398-405
    • (1961) Virology , vol.14 , pp. 398-405
    • Barry, R.D.1
  • 8
    • 0017289944 scopus 로고
    • Transcriptase activity and genome composition of defective influenza virus
    • Bean WJ Jr, Simpson RW. 1976. Transcriptase activity and genome composition of defective influenza virus. J. Virol. 18:365-69
    • (1976) J. Virol. , vol.18 , pp. 365-369
    • Bean W.J., Jr.1    Simpson, R.W.2
  • 9
    • 2142778976 scopus 로고
    • Transcription antitermination during influenza viral template RNA synthesis requires the nucleocapsid protein and the absence of a 5′ capped end
    • Beaton AR, Krug RM. 1986. Transcription antitermination during influenza viral template RNA synthesis requires the nucleocapsid protein and the absence of a 5′ capped end. Proc. Natl. Acad. Sci. USA 83:6282-86
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6282-6286
    • Beaton, A.R.1    Krug, R.M.2
  • 10
    • 0033080392 scopus 로고    scopus 로고
    • Characterization of the surface proteins of influenza A (H5N1) viruses isolated from humans in 1997-1998
    • Bender C, Hall H, Huang J, Klimov A, Cox N, et al. 1999. Characterization of the surface proteins of influenza A (H5N1) viruses isolated from humans in 1997-1998. Virology 254:115-23
    • (1999) Virology , vol.254 , pp. 115-123
    • Bender, C.1    Hall, H.2    Huang, J.3    Klimov, A.4    Cox, N.5
  • 11
    • 0026464671 scopus 로고
    • Transfection-mediated recombination of influenza A virus
    • Bergmann M, Garcia-Sastre A, Palese P. 1992. Transfection-mediated recombination of influenza A virus. J. Virol. 66:7576-80
    • (1992) J. Virol. , vol.66 , pp. 7576-7580
    • Bergmann, M.1    Garcia-Sastre, A.2    Palese, P.3
  • 12
    • 0029558592 scopus 로고
    • The relative amount of an influenza A virus segment present in the viral particle is not affected by a reduction in replication of that segment
    • Bergmann M, Muster T. 1995. The relative amount of an influenza A virus segment present in the viral particle is not affected by a reduction in replication of that segment. J. Gen. Virol. 76:3211-15
    • (1995) J. Gen. Virol. , vol.76 , pp. 3211-3215
    • Bergmann, M.1    Muster, T.2
  • 13
    • 0029823231 scopus 로고    scopus 로고
    • The NB protein is an integral component of the membrane of influenza B virus
    • Betakova T, Nermut MV, Hay AJ. 1996. The NB protein is an integral component of the membrane of influenza B virus. J. Gen. Virol. 77:2689-94
    • (1996) J. Gen. Virol. , vol.77 , pp. 2689-2694
    • Betakova, T.1    Nermut, M.V.2    Hay, A.J.3
  • 14
    • 0028118520 scopus 로고
    • Mutational analysis of the conserved motifs of influenza A virus polymerase basic protein 1
    • Biswas SK, Nayak DP. 1994. Mutational analysis of the conserved motifs of influenza A virus polymerase basic protein 1. J. Virol. 68:1819-26
    • (1994) J. Virol. , vol.68 , pp. 1819-1826
    • Biswas, S.K.1    Nayak, D.P.2
  • 16
    • 0029026358 scopus 로고
    • Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
    • Bizebard T, Gigant B, Rigolet P, Rasmussen B, Diat O, et al. 1995. Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Nature 376:92-94
    • (1995) Nature , vol.376 , pp. 92-94
    • Bizebard, T.1    Gigant, B.2    Rigolet, P.3    Rasmussen, B.4    Diat, O.5
  • 17
    • 0029999258 scopus 로고    scopus 로고
    • Influenza B virus NB glycoprotein is a component of the virion
    • Brassard DL, Leser GP, Lamb RA. 1996. Influenza B virus NB glycoprotein is a component of the virion. Virology 220:350-60
    • (1996) Virology , vol.220 , pp. 350-360
    • Brassard, D.L.1    Leser, G.P.2    Lamb, R.A.3
  • 19
    • 0012519832 scopus 로고
    • Recombination of characters between two influenza virus strains
    • Burnet FM, Lind PE. 1949. Recombination of characters between two influenza virus strains. Aust. J. Sci. 12:109-10
    • (1949) Aust. J. Sci. , vol.12 , pp. 109-110
    • Burnet, F.M.1    Lind, P.E.2
  • 20
    • 0012518256 scopus 로고
    • A genetic approach to variation in influenza viruses. 3. Recombination of characters in influenza virus strains used in mixed infections
    • Burnet FM, Lind PE. 1951. A genetic approach to variation in influenza viruses. 3. Recombination of characters in influenza virus strains used in mixed infections. J. Gen. Microbiol. 5:59-66
    • (1951) J. Gen. Microbiol. , vol.5 , pp. 59-66
    • Burnet, F.M.1    Lind, P.E.2
  • 21
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton AJ, Brownlee GG, Yewdell JW, Gerhard W. 1982. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31:417-27
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 22
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, Wiley DC. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95:409-17
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 23
    • 0035658084 scopus 로고    scopus 로고
    • A novel influenza A virus mitochondrial protein that induces cell death
    • Chen W, Calvo PA, Malide D, Gibbs J, Schubert U, et al. 2001. A novel influenza A virus mitochondrial protein that induces cell death. Nat. Med. 7:1306-12
    • (2001) Nat. Med. , vol.7 , pp. 1306-1312
    • Chen, W.1    Calvo, P.A.2    Malide, D.3    Gibbs, J.4    Schubert, U.5
  • 24
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov IV, Geraghty FM, Ogden DC, Hayhurst A, Antoniou M, Hay AJ. 1996. Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J. Physiol. 494:329-36
    • (1996) J. Physiol. , vol.494 , pp. 329-336
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 25
    • 0000283734 scopus 로고
    • Studies of two kinds of virus particles which comprise influenza A2 strains. III. Morphological characteristics: Independence of morphological and functional traits
    • Choppin PW, Murphy JS, Tamm I. 1960. Studies of two kinds of virus particles which comprise influenza A2 strains. III. Morphological characteristics: independence of morphological and functional traits. J. Exp. Med. 112:945-52
    • (1960) J. Exp. Med. , vol.112 , pp. 945-952
    • Choppin, P.W.1    Murphy, J.S.2    Tamm, I.3
  • 26
    • 0000443647 scopus 로고
    • Filamentous forms associated with newly isolated influenza virus
    • Chu CM, Dawson IM, Elford WJ. 1949. Filamentous forms associated with newly isolated influenza virus. Lancet i:602-3
    • (1949) Lancet , vol.1 , pp. 602-603
    • Chu, C.M.1    Dawson, I.M.2    Elford, W.J.3
  • 27
    • 0032515638 scopus 로고    scopus 로고
    • Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus
    • Claas EC, Osterhaus AD, van Beek R, De Jong JC, Rimmelzwaan GF, et al. 1998. Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus. Lancet 351:472-77
    • (1998) Lancet , vol.351 , pp. 472-477
    • Claas, E.C.1    Osterhaus, A.D.2    Van Beek, R.3    De Jong, J.C.4    Rimmelzwaan, G.F.5
  • 28
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman PM, Varghese JN, Laver WG. 1983. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303:41-44
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 29
    • 0021910031 scopus 로고
    • Fusion mutants of the influenza virus hemagglutinin glycoprotein
    • Daniels RS, Downie JC, Hay AJ, Knossow M, Skehel JJ, et al. 1985. Fusion mutants of the influenza virus hemagglutinin glycoprotein. Cell 40:431-39
    • (1985) Cell , vol.40 , pp. 431-439
    • Daniels, R.S.1    Downie, J.C.2    Hay, A.J.3    Knossow, M.4    Skehel, J.J.5
  • 31
    • 1842345479 scopus 로고
    • Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence
    • Deshpande KL, Fried VA, Ando M, Webster RG. 1987. Glycosylation affects cleavage of an H5N2 influenza virus hemagglutinin and regulates virulence. Proc. Natl. Acad. Sci. USA 84:36-40
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 36-40
    • Deshpande, K.L.1    Fried, V.A.2    Ando, M.3    Webster, R.G.4
  • 32
    • 0001658090 scopus 로고
    • Counts of influenza virus particles
    • Donald HB, Issacs A. 1954. Counts of influenza virus particles. J. Gen. Microbiol. 10:457-64
    • (1954) J. Gen. Microbiol. , vol.10 , pp. 457-464
    • Donald, H.B.1    Issacs, A.2
  • 33
    • 0029963536 scopus 로고    scopus 로고
    • Defective RNAs inhibit the assembly of influenza virus genome segments in a segment-specific manner
    • Duhaut SD, McCauley JW. 1996. Defective RNAs inhibit the assembly of influenza virus genome segments in a segment-specific manner. Virology 216:326-37
    • (1996) Virology , vol.216 , pp. 326-337
    • Duhaut, S.D.1    McCauley, J.W.2
  • 34
    • 0033982808 scopus 로고    scopus 로고
    • Distinct pathogenesis of Hong Kong-origin H5N1 viruses in mice compared to that of other highly pathogenic H5 avian influenza viruses
    • Dybing JK, Schultz-Cherry S, Swayne DE, Suarez DL, Perdue ML. 2000. Distinct pathogenesis of Hong Kong-origin H5N1 viruses in mice compared to that of other highly pathogenic H5 avian influenza viruses. J. Virol. 74:1443-50
    • (2000) J. Virol. , vol.74 , pp. 1443-1450
    • Dybing, J.K.1    Schultz-Cherry, S.2    Swayne, D.E.3    Suarez, D.L.4    Perdue, M.L.5
  • 35
    • 0022349314 scopus 로고
    • Transcription and replication of eight RNA segments of influenza virus
    • Enami M, Fukuda R, Ishihama A. 1985. Transcription and replication of eight RNA segments of influenza virus. Virology 142:68-77
    • (1985) Virology , vol.142 , pp. 68-77
    • Enami, M.1    Fukuda, R.2    Ishihama, A.3
  • 36
    • 0025314308 scopus 로고
    • Introduction of site-specific mutations into the genome of influenza virus
    • Enami M, Luytjes W, Krystal M, Palese P. 1990. Introduction of site-specific mutations into the genome of influenza virus. Proc. Natl. Acad. Sci. USA 87:3802-5
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3802-3805
    • Enami, M.1    Luytjes, W.2    Krystal, M.3    Palese, P.4
  • 37
    • 0025951699 scopus 로고
    • An influenza virus containing nine different RNA segments
    • Enami M, Sharma G, Benham C, Palese P. 1991. An influenza virus containing nine different RNA segments. Virology 185:291-98
    • (1991) Virology , vol.185 , pp. 291-298
    • Enami, M.1    Sharma, G.2    Benham, C.3    Palese, P.4
  • 38
    • 0019815973 scopus 로고
    • Nucleotide-sequence heterogeneity and sequence rearrangements in influenza virus cDNA
    • Fields S, Winter G. 1981. Nucleotide-sequence heterogeneity and sequence rearrangements in influenza virus cDNA. Gene 15:207-14
    • (1981) Gene , vol.15 , pp. 207-214
    • Fields, S.1    Winter, G.2
  • 39
    • 0020047414 scopus 로고
    • Nucleotide sequences of influenza virus segments 1 and 3 reveal mosaic structure of a small viral RNA segment
    • Fields S, Winter G. 1982. Nucleotide sequences of influenza virus segments 1 and 3 reveal mosaic structure of a small viral RNA segment. Cell 28:303-13
    • (1982) Cell , vol.28 , pp. 303-313
    • Fields, S.1    Winter, G.2
  • 40
    • 0033053331 scopus 로고    scopus 로고
    • A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site
    • Fleury D, Barrere B, Bizebard T, Daniels RS, Skehel JJ, Knossow M. 1999. A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site. Nat. Struct. Biol. 6:530-34
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 530-534
    • Fleury, D.1    Barrere, B.2    Bizebard, T.3    Daniels, R.S.4    Skehel, J.J.5    Knossow, M.6
  • 42
    • 0033014710 scopus 로고    scopus 로고
    • Biological heterogeneity, including systemic replication in mice, of H5N1 influenza A virus isolates from humans in Hong Kong
    • Gao P, Watanabe S, Ito T, Goto H, Wells K, et al. 1999. Biological heterogeneity, including systemic replication in mice, of H5N1 influenza A virus isolates from humans in Hong Kong. J. Virol. 73:3184-89
    • (1999) J. Virol. , vol.73 , pp. 3184-3189
    • Gao, P.1    Watanabe, S.2    Ito, T.3    Goto, H.4    Wells, K.5
  • 43
    • 0035864298 scopus 로고    scopus 로고
    • Inhibition of interferon-mediated antiviral responses by influenza A viruses and other negative-strand RNA viruses
    • Garcia-Sastre A. 2001. Inhibition of interferon-mediated antiviral responses by influenza A viruses and other negative-strand RNA viruses. Virology 279:375-84
    • (2001) Virology , vol.279 , pp. 375-384
    • Garcia-Sastre, A.1
  • 44
    • 0027455154 scopus 로고
    • Genetic manipulation of negative-strand RNA virus genomes
    • Garcia-Sastre A, Palese P. 1993. Genetic manipulation of negative-strand RNA virus genomes. Annu. Rev. Microbiol. 47:765-90
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 765-790
    • Garcia-Sastre, A.1    Palese, P.2
  • 45
    • 0029014741 scopus 로고
    • The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in packaging this protein into viral envelopes
    • Garcia-Sastre A, Palese P. 1995. The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in packaging this protein into viral envelopes. Virus Res. 37:37-47
    • (1995) Virus Res. , vol.37 , pp. 37-47
    • Garcia-Sastre, A.1    Palese, P.2
  • 46
    • 0034977654 scopus 로고    scopus 로고
    • The role of the antibody response in influenza virus infection
    • Gerhard W. 2001. The role of the antibody response in influenza virus infection. Curr. Top. Microbiol. Immunol. 260:171-90
    • (2001) Curr. Top. Microbiol. Immunol. , vol.260 , pp. 171-190
    • Gerhard, W.1
  • 47
    • 0020368602 scopus 로고
    • Studies of fowl plague virus temperature-sensitive mutants with defects in transcription
    • Ghendon YZ, Markushin SG, Klimov AI, Hay AJ. 1982. Studies of fowl plague virus temperature-sensitive mutants with defects in transcription. J. Gen. Virol. 63:103-11
    • (1982) J. Gen. Virol. , vol.63 , pp. 103-111
    • Ghendon, Y.Z.1    Markushin, S.G.2    Klimov, A.I.3    Hay, A.J.4
  • 48
    • 0035822899 scopus 로고    scopus 로고
    • Recombination in the hemagglutinin gene of the 1918 "Spanish flu"
    • Gibbs MJ, Armstrong JS, Gibbs AJ. 2001. Recombination in the hemagglutinin gene of the 1918 "Spanish flu." Science 293:1842-45
    • (2001) Science , vol.293 , pp. 1842-1845
    • Gibbs, M.J.1    Armstrong, J.S.2    Gibbs, A.J.3
  • 49
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • Goto H, Kawaoka Y. 1998. A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. USA 95:10224-28
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 50
    • 0027103930 scopus 로고
    • Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses
    • Grambas S, Bennett MS, Hay AJ. 1992. Influence of amantadine resistance mutations on the pH regulatory function of the M2 protein of influenza A viruses. Virology 191:541-49
    • (1992) Virology , vol.191 , pp. 541-549
    • Grambas, S.1    Bennett, M.S.2    Hay, A.J.3
  • 51
    • 0026787707 scopus 로고
    • Maturation of influenza A virus hemagglutinin-estimates of the pH encountered during transport and its regulation by the M2 protein
    • Grambas S, Hay AJ. 1992. Maturation of influenza A virus hemagglutinin-estimates of the pH encountered during transport and its regulation by the M2 protein. Virology 190:11-18
    • (1992) Virology , vol.190 , pp. 11-18
    • Grambas, S.1    Hay, A.J.2
  • 52
    • 0030028671 scopus 로고    scopus 로고
    • Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en
    • Gubareva LV, Bethell R, Hart GJ, Murti KG, Penn CR, Webster RG. 1996. Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en. J. Virol. 70:1818-27
    • (1996) J. Virol. , vol.70 , pp. 1818-1827
    • Gubareva, L.V.1    Bethell, R.2    Hart, G.J.3    Murti, K.G.4    Penn, C.R.5    Webster, R.G.6
  • 53
    • 0034603350 scopus 로고    scopus 로고
    • Influenza virus neuraminidase inhibitors
    • Gubareva LV, Kaiser L, Hayden FG. 2000. Influenza virus neuraminidase inhibitors. Lancet 355:827-35
    • (2000) Lancet , vol.355 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 54
    • 0031766022 scopus 로고    scopus 로고
    • Characterization of influenza A/HongKong/156/97 (H5N1) virus in a mouse model and protective effect of zanamivir on H5N1 infection in mice
    • Gubareva LV, McCullers JA, Bethell RC, Webster RG. 1998. Characterization of influenza A/HongKong/156/97 (H5N1) virus in a mouse model and protective effect of zanamivir on H5N1 infection in mice. J. Infect. Dis. 178:1592-96
    • (1998) J. Infect. Dis. , vol.178 , pp. 1592-1596
    • Gubareva, L.V.1    McCullers, J.A.2    Bethell, R.C.3    Webster, R.G.4
  • 55
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta M, Gao P, Halfmann P, Kawaoka Y. 2001. Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293:1840-42
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 57
    • 0018305077 scopus 로고
    • The matrix protein gene determines amantadine-sensitivity of influenza viruses
    • Hay AJ, Kennedy NC, Skehel JJ, Appleyard G. 1979. The matrix protein gene determines amantadine-sensitivity of influenza viruses. J. Gen. Virol. 42:189-91
    • (1979) J. Gen. Virol. , vol.42 , pp. 189-191
    • Hay, A.J.1    Kennedy, N.C.2    Skehel, J.J.3    Appleyard, G.4
  • 58
    • 0020051391 scopus 로고
    • Characterization of influenza virus RNA complete transcripts
    • Hay AJ, Skehel JJ, McCauley J. 1982. Characterization of influenza virus RNA complete transcripts. Virology 116:517-22
    • (1982) Virology , vol.116 , pp. 517-522
    • Hay, A.J.1    Skehel, J.J.2    McCauley, J.3
  • 59
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay AJ, Wolstenholme AJ, Skehel JJ, Smith MH. 1985. The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 4:3021-24
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 60
    • 0012618031 scopus 로고
    • Studies on host-virus interactions in the chick embryo influenza virus system
    • Henle W, Liu OC. 1951. Studies on host-virus interactions in the chick embryo influenza virus system. J. Exp. Med. 94:305-22
    • (1951) J. Exp. Med. , vol.94 , pp. 305-322
    • Henle, W.1    Liu, O.C.2
  • 62
    • 0020546479 scopus 로고
    • Altered tissue tropism of human-avian reassortant influenza viruses
    • Hinshaw VS, Webster RG, Naeve CW, Murphy BR. 1983. Altered tissue tropism of human-avian reassortant influenza viruses. Virology 128:260-63
    • (1983) Virology , vol.128 , pp. 260-263
    • Hinshaw, V.S.1    Webster, R.G.2    Naeve, C.W.3    Murphy, B.R.4
  • 63
    • 73849176898 scopus 로고
    • Genetic recombination with Newcastle disease virus, poliovirus, and influenza
    • Hirst GK. 1962. Genetic recombination with Newcastle disease virus, poliovirus, and influenza. Cold Spring Harbor Symp. Quant. Biol. 27:303-8
    • (1962) Cold Spring Harbor Symp. Quant. Biol. , vol.27 , pp. 303-308
    • Hirst, G.K.1
  • 64
    • 12244285001 scopus 로고
    • The experimental production of combination forms of virus. V. Alterations in the virulence of neurotropic influenza virus as a result of mixed infection
    • Hirst GK, Gotlieb T. 1955. The experimental production of combination forms of virus. V. Alterations in the virulence of neurotropic influenza virus as a result of mixed infection. Virology 1:221-35
    • (1955) Virology , vol.1 , pp. 221-235
    • Hirst, G.K.1    Gotlieb, T.2
  • 66
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger LJ, Lamb RA. 1991. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183:32-43
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 67
    • 0028095251 scopus 로고
    • Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses
    • Horimoto T, Nakayama K, Smeekens SP, Kawaoka Y. 1994. Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses. J. Virol. 68:6074-78
    • (1994) J. Virol. , vol.68 , pp. 6074-6078
    • Horimoto, T.1    Nakayama, K.2    Smeekens, S.P.3    Kawaoka, Y.4
  • 68
    • 0019997624 scopus 로고
    • Identification of a catalytic activity of the large basic P polypeptide of influenza virus
    • Horisberger MA. 1982. Identification of a catalytic activity of the large basic P polypeptide of influenza virus. Virology 120:279-86
    • (1982) Virology , vol.120 , pp. 279-286
    • Horisberger, M.A.1
  • 69
    • 12244268998 scopus 로고
    • The structure and composition of myxoviruses. I. Electron microscope studies of the structure of myxovirus particles by negative staining techniques
    • Horne RW, Waterson AP, Wildy P, Farnham AP. 1960. The structure and composition of myxoviruses. I. Electron microscope studies of the structure of myxovirus particles by negative staining techniques. Virology 11:79-98
    • (1960) Virology , vol.11 , pp. 79-98
    • Horne, R.W.1    Waterson, A.P.2    Wildy, P.3    Farnham, A.P.4
  • 70
    • 0025358767 scopus 로고
    • Eukaryotic coupled translation of tandem cistrons: Identification of the influenza B virus BM2 polypeptide
    • Horvath CM, Williams MA, Lamb RA. 1990. Eukaryotic coupled translation of tandem cistrons: identification of the influenza B virus BM2 polypeptide. EMBO J. 9:2639-47
    • (1990) EMBO J. , vol.9 , pp. 2639-2647
    • Horvath, C.M.1    Williams, M.A.2    Lamb, R.A.3
  • 71
    • 0000455473 scopus 로고
    • The structure and composition of the myxoviruses II. Components released from the influenza virus particle by ether
    • Hoyle L, Horne RW, Waterson AP. 1961. The structure and composition of the myxoviruses II. Components released from the influenza virus particle by ether. Virology 13:448-59
    • (1961) Virology , vol.13 , pp. 448-459
    • Hoyle, L.1    Horne, R.W.2    Waterson, A.P.3
  • 72
    • 0035080020 scopus 로고    scopus 로고
    • Adaptation of influenza A viruses to cells expressing low levels of sialic acid leads to loss of neuraminidase activity
    • Hughes MT, McGregor M, Suzuki T, Suzuki Y, Kawaoka Y. 2001. Adaptation of influenza A viruses to cells expressing low levels of sialic acid leads to loss of neuraminidase activity. J. Virol. 75:3766-70
    • (2001) J. Virol. , vol.75 , pp. 3766-3770
    • Hughes, M.T.1    McGregor, M.2    Suzuki, T.3    Suzuki, Y.4    Kawaoka, Y.5
  • 73
    • 0031820637 scopus 로고    scopus 로고
    • Molecular basis for the generation in pigs of influenza A viruses with pandemic potential
    • Ito T, Couceiro JN, Kelm S, Baum LG, Krauss S, et al. 1998. Molecular basis for the generation in pigs of influenza A viruses with pandemic potential. J. Virol. 72:7367-73
    • (1998) J. Virol. , vol.72 , pp. 7367-7373
    • Ito, T.1    Couceiro, J.N.2    Kelm, S.3    Baum, L.G.4    Krauss, S.5
  • 74
    • 0020826340 scopus 로고
    • Does the higher order structure of the influenza virus ribonucleo-protein guide sequence rearrangements in influenza viral RNA?
    • Jennings PA, Finch JT, Winter G, Robertson JS. 1983. Does the higher order structure of the influenza virus ribonucleo-protein guide sequence rearrangements in influenza viral RNA? Cell 34:619-27
    • (1983) Cell , vol.34 , pp. 619-627
    • Jennings, P.A.1    Finch, J.T.2    Winter, G.3    Robertson, J.S.4
  • 75
    • 0014498560 scopus 로고
    • Inhibition of uncoating of fowl plague virus by ladamantanamine hydrochloride
    • Kato N, Eggers HJ. 1969. Inhibition of uncoating of fowl plague virus by ladamantanamine hydrochloride. Virology 37:632-41
    • (1969) Virology , vol.37 , pp. 632-641
    • Kato, N.1    Eggers, H.J.2
  • 77
    • 0024439330 scopus 로고
    • Avian-to-human transmission of of the PB1 gene of influenza A virus in the 1957 and 1968 pandemics
    • Kawaoka Y, Krauss S, Webster RG. 1989. Avian-to-human transmission of of the PB1 gene of influenza A virus in the 1957 and 1968 pandemics. J. Virol. 63:4603-8
    • (1989) J. Virol. , vol.63 , pp. 4603-4608
    • Kawaoka, Y.1    Krauss, S.2    Webster, R.G.3
  • 78
    • 0021741381 scopus 로고
    • Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin?
    • Kawaoka Y, Naeve CW, Webster RG. 1984. Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin? Virology 139:303-16
    • (1984) Virology , vol.139 , pp. 303-316
    • Kawaoka, Y.1    Naeve, C.W.2    Webster, R.G.3
  • 79
    • 0024396988 scopus 로고
    • Interplay between carbohydrate in the stalk and the length of the connecting peptide determines the cleavability of influenza virus hemagglutinin
    • Kawaoka Y, Webster RG. 1989. Interplay between carbohydrate in the stalk and the length of the connecting peptide determines the cleavability of influenza virus hemagglutinin. J. Virol. 63:3296-300
    • (1989) J. Virol. , vol.63 , pp. 3296-3300
    • Kawaoka, Y.1    Webster, R.G.2
  • 80
    • 0018241627 scopus 로고
    • Antigenic similarity of influenza A (H1N1) viruses from epidemics in 1977-1978 to "Scandinavian" strains isolated in epidemics of 1950-1951
    • Kendal AP NG, Skehel JJ, Dowdle WR. 1978. Antigenic similarity of influenza A (H1N1) viruses from epidemics in 1977-1978 to "Scandinavian" strains isolated in epidemics of 1950-1951. Virology 89:632-36
    • (1978) Virology , vol.89 , pp. 632-636
    • Kendal, A.P.N.G.1    Skehel, J.J.2    Dowdle, W.R.3
  • 81
    • 0024347652 scopus 로고
    • Increased viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the haemagglutinin gene of an influenza virus
    • Khatchikian D, Orlich M, Rott R. 1989. Increased viral pathogenicity after insertion of a 28S ribosomal RNA sequence into the haemagglutinin gene of an influenza virus. Nature 340:156-57
    • (1989) Nature , vol.340 , pp. 156-157
    • Khatchikian, D.1    Orlich, M.2    Rott, R.3
  • 83
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk HD, Garten W. 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
  • 84
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk HD, Rott R, Orlich M, Blodorn J. 1975. Activation of influenza A viruses by trypsin treatment. Virology 68:426-39
    • (1975) Virology , vol.68 , pp. 426-439
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 85
    • 0004250845 scopus 로고    scopus 로고
    • Philadelphia: Lippincott, Williams & Wilkins
    • Knipe DM, Howley PM, eds. 2001. Fields Virology. Philadelphia: Lippincott, Williams & Wilkins
    • (2001) Fields Virology
    • Knipe, D.M.1    Howley, P.M.2
  • 86
    • 0016824581 scopus 로고
    • Temperature-sensitive mutants of influenza WSN virus defective in virus-specific RNA synthesis
    • Krug RM, Ueda M, Palese P. 1975. Temperature-sensitive mutants of influenza WSN virus defective in virus-specific RNA synthesis. J. Virol. 16:790-96
    • (1975) J. Virol. , vol.16 , pp. 790-796
    • Krug, R.M.1    Ueda, M.2    Palese, P.3
  • 87
    • 0020696905 scopus 로고
    • The gene structure and replication of influenza virus
    • Lamb RA, Choppin PW. 1983. The gene structure and replication of influenza virus. Annu. Rev. Biochem. 52:467-506
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 467-506
    • Lamb, R.A.1    Choppin, P.W.2
  • 89
    • 0016590407 scopus 로고
    • Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide
    • Lazarowitz SG, Choppin PW. 1975. Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide. Virology 68:440-54
    • (1975) Virology , vol.68 , pp. 440-454
    • Lazarowitz, S.G.1    Choppin, P.W.2
  • 90
    • 0035901509 scopus 로고    scopus 로고
    • The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
    • Li ML, Rao P, Krug RM. 2001. The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits. EMBO J. 20:2078-86
    • (2001) EMBO J. , vol.20 , pp. 2078-2086
    • Li, M.L.1    Rao, P.2    Krug, R.M.3
  • 91
    • 0027519686 scopus 로고
    • Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus
    • Li S, Schulman J, Itamura S, Palese P. 1993. Glycosylation of neuraminidase determines the neurovirulence of influenza A/WSN/33 virus. J. Virol. 67:6667-73
    • (1993) J. Virol. , vol.67 , pp. 6667-6673
    • Li, S.1    Schulman, J.2    Itamura, S.3    Palese, P.4
  • 92
    • 12944270582 scopus 로고    scopus 로고
    • Avian-to-human transmission of H9N2 subtype influenza A viruses: Relationship between H9N2 and H5N1 human isolates
    • Lin YP, Shaw M, Gregory V, Cameron K, Lim W, et al. 2000. Avian-to-human transmission of H9N2 subtype influenza A viruses: relationship between H9N2 and H5N1 human isolates. Proc. Natl. Acad. Sci. USA 97:9654-58
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9654-9658
    • Lin, Y.P.1    Shaw, M.2    Gregory, V.3    Cameron, K.4    Lim, W.5
  • 93
    • 12244293052 scopus 로고
    • Recombination between virulent and non-virulent strains of influenza virus. 2. The behavior of virulence markers on recombination
    • Lind PE, Burnet FM. 1957. Recombination between virulent and non-virulent strains of influenza virus. 2. The behavior of virulence markers on recombination. Aust. J. Exp. Biol. Med. Sci. 35:67-78
    • (1957) Aust. J. Exp. Biol. Med. Sci. , vol.35 , pp. 67-78
    • Lind, P.E.1    Burnet, F.M.2
  • 94
    • 0027261465 scopus 로고
    • Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes
    • Liu C, Air GM. 1993. Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194:403-7
    • (1993) Virology , vol.194 , pp. 403-407
    • Liu, C.1    Air, G.M.2
  • 95
    • 0033064858 scopus 로고    scopus 로고
    • A mouse model for the evaluation of pathogenesis and immunity to influenza A (H5N1) viruses isolated from humans
    • Lu X, Tumpey TM, Morken T, Zaki SR, Cox NJ, Katz JM. 1999. A mouse model for the evaluation of pathogenesis and immunity to influenza A (H5N1) viruses isolated from humans. J. Virol. 73:5903-11
    • (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
  • 96
    • 0018196437 scopus 로고
    • Susceptibility of influenza A viruses to amantadine is influenced by the gene coding for M protein
    • Lubeck MD, Schulman JL, Palese P. 1978. Susceptibility of influenza A viruses to amantadine is influenced by the gene coding for M protein. J. Virol. 28:710-16
    • (1978) J. Virol. , vol.28 , pp. 710-716
    • Lubeck, M.D.1    Schulman, J.L.2    Palese, P.3
  • 97
    • 0029169776 scopus 로고
    • Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus
    • Ludwig S, Vogel U, Scholtissek C. 1995. Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus. Arch. Virol. 140:945-50
    • (1995) Arch. Virol. , vol.140 , pp. 945-950
    • Ludwig, S.1    Vogel, U.2    Scholtissek, C.3
  • 98
    • 0024846089 scopus 로고
    • Amplification, expression, and packaging of foreign gene by influenza virus
    • Luytjes W, Krystal M, Enami M, Pavin JD, Palese P. 1989. Amplification, expression, and packaging of foreign gene by influenza virus. Cell 59:1107-13
    • (1989) Cell , vol.59 , pp. 1107-1113
    • Luytjes, W.1    Krystal, M.2    Enami, M.3    Pavin, J.D.4    Palese, P.5
  • 99
    • 0032748256 scopus 로고    scopus 로고
    • The development of live attenuated cold-adapted influenza virus vaccine for humans
    • Maassab HF, Bryant ML. 1999. The development of live attenuated cold-adapted influenza virus vaccine for humans. Rev. Med. Virol. 9:237-44
    • (1999) Rev. Med. Virol. , vol.9 , pp. 237-244
    • Maassab, H.F.1    Bryant, M.L.2
  • 100
    • 0002579084 scopus 로고
    • Mutants of influenza virus
    • ed. DW Kingsbury, P Palese. Berlin: Springer-Verlag
    • Mahy BWJ. 1983. Mutants of influenza virus. In Genetics of Influenza Viruses, ed. DW Kingsbury, P Palese, pp. 192-254. Berlin: Springer-Verlag
    • (1983) Genetics of Influenza Viruses , pp. 192-254
    • Mahy, B.W.J.1
  • 101
    • 0032005708 scopus 로고    scopus 로고
    • Studies of the binding properties of influenza hemagglutinin receptor-site mutants
    • Martin J, Wharton SA, Lin YP, Takemoto DK, Skehel JJ, et al. 1998. Studies of the binding properties of influenza hemagglutinin receptor-site mutants. Virology 241:101-11
    • (1998) Virology , vol.241 , pp. 101-111
    • Martin, J.1    Wharton, S.A.2    Lin, Y.P.3    Takemoto, D.K.4    Skehel, J.J.5
  • 102
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleo-proteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin K, Helenius A. 1991. Nuclear transport of influenza virus ribonucleo-proteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67:117-30
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 103
    • 0015579348 scopus 로고
    • Nonlinkage of neurovirulence exclusively to viral hemagglutinin or neuraminidase in genetic recombinants of A/NWS (H0N1) influenza virus
    • Mayer V, Schulman JL, Kilbourne ED. 1973. Nonlinkage of neurovirulence exclusively to viral hemagglutinin or neuraminidase in genetic recombinants of A/NWS (H0N1) influenza virus. J. Virol. 11:272-78
    • (1973) J. Virol. , vol.11 , pp. 272-278
    • Mayer, V.1    Schulman, J.L.2    Kilbourne, E.D.3
  • 104
    • 0017105769 scopus 로고
    • The influenza virus genome consists of eight distinct RNA species
    • McGeoch D, Fellner P, Newton C. 1976. The influenza virus genome consists of eight distinct RNA species. Proc. Natl. Acad. Sci. USA 73:3045-49
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3045-3049
    • McGeoch, D.1    Fellner, P.2    Newton, C.3
  • 105
    • 0033897803 scopus 로고    scopus 로고
    • Resistance of influenza viruses to neuraminidase inhibitors - A review
    • McKimm-Breschkin JL. 2000. Resistance of influenza viruses to neuraminidase inhibitors-a review. Antiviral Res. 47:1-17
    • (2000) Antiviral Res , vol.47 , pp. 1-17
    • McKimm-Breschkin, J.L.1
  • 106
    • 0030069140 scopus 로고    scopus 로고
    • The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication
    • Mitnaul LJ, Castrucci MR, Murti KG, Kawaoka Y. 1996. The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication. J. Virol. 70:873-79
    • (1996) J. Virol. , vol.70 , pp. 873-879
    • Mitnaul, L.J.1    Castrucci, M.R.2    Murti, K.G.3    Kawaoka, Y.4
  • 107
    • 0034099655 scopus 로고    scopus 로고
    • Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus
    • Mitnaul LJ, Matrosovich MN, Castrucci MR, Tuzikov AB, Bovin NV, et al. 2000. Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus. J. Virol. 74:6015-20
    • (2000) J. Virol. , vol.74 , pp. 6015-6020
    • Mitnaul, L.J.1    Matrosovich, M.N.2    Castrucci, M.R.3    Tuzikov, A.B.4    Bovin, N.V.5
  • 109
    • 0018197440 scopus 로고
    • P1 is required for initiation of cRNA synthesis in WSN influenza virus
    • Mowshowitz SL. 1978. P1 is required for initiation of cRNA synthesis in WSN influenza virus. Virology 91:493-95
    • (1978) Virology , vol.91 , pp. 493-495
    • Mowshowitz, S.L.1
  • 110
    • 0026091023 scopus 로고
    • Involvement of the influenza A virus PB2 protein in the regulation of viral gene expression
    • Mukaigawa J, Hatada E, Fukuda R, Shimizu K. 1991. Involvement of the influenza A virus PB2 protein in the regulation of viral gene expression. J. Gen. Virol. 72:2661-70
    • (1991) J. Gen. Virol. , vol.72 , pp. 2661-2670
    • Mukaigawa, J.1    Hatada, E.2    Fukuda, R.3    Shimizu, K.4
  • 111
    • 0026003178 scopus 로고
    • An influenza A virus containing influenza B virus 5′ and 3′ noncoding regions on the neuraminidase gene is attenuated in mice
    • Muster T, Subbarao EK, Enami M, Murphy BR, Palese P. 1991. An influenza A virus containing influenza B virus 5′ and 3′ noncoding regions on the neuraminidase gene is attenuated in mice. Proc. Natl. Acad. Sci. USA 88:5177-81
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5177-5181
    • Muster, T.1    Subbarao, E.K.2    Enami, M.3    Murphy, B.R.4    Palese, P.5
  • 112
    • 0018149877 scopus 로고
    • Recent human influenza A (H1N1) viruses are closely related genetically to strains isolated in 1950
    • Nakajima K, Desselberger U, Palese P. 1978. Recent human influenza A (H1N1) viruses are closely related genetically to strains isolated in 1950. Nature 274:334-39
    • (1978) Nature , vol.274 , pp. 334-339
    • Nakajima, K.1    Desselberger, U.2    Palese, P.3
  • 113
    • 0018343066 scopus 로고
    • Origin of small RNA in von Magnus particles of influenza virus
    • Nakajima K, Ueda M, Sugiura A. 1979. Origin of small RNA in von Magnus particles of influenza virus. J. Virol. 29:1142-48
    • (1979) J. Virol. , vol.29 , pp. 1142-1148
    • Nakajima, K.1    Ueda, M.2    Sugiura, A.3
  • 114
    • 0021947461 scopus 로고
    • Defective-interfering (DI) RNAs of influenza viruses: Origin, structure, expression, and interference
    • Nayak DP, Chambers TM, Akkina RK. 1985. Defective-interfering (DI) RNAs of influenza viruses: origin, structure, expression, and interference. Curr. Top. Microbiol. Immunol. 114:103-51
    • (1985) Curr. Top. Microbiol. Immunol. , vol.114 , pp. 103-151
    • Nayak, D.P.1    Chambers, T.M.2    Akkina, R.K.3
  • 115
    • 0035450506 scopus 로고    scopus 로고
    • Reverse genetics of influenza virus
    • Neumann G, Kawaoka Y. 2001. Reverse genetics of influenza virus. Virology 287:243-50
    • (2001) Virology , vol.287 , pp. 243-250
    • Neumann, G.1    Kawaoka, Y.2
  • 117
    • 0027978143 scopus 로고
    • RNA polymerase I-mediated expression of influenza viral RNA molecules
    • Neumann G, Zobel A, Hobom G. 1994. RNA polymerase I-mediated expression of influenza viral RNA molecules. Virology 202:477-79
    • (1994) Virology , vol.202 , pp. 477-479
    • Neumann, G.1    Zobel, A.2    Hobom, G.3
  • 118
    • 0019818384 scopus 로고
    • Evidence for the involvement of influenza A (fowl plague Rostock) virus protein P2 in ApG and mRNA primed in vitro RNA synthesis
    • Nichol ST, Penn CR, Mahy BW. 1981. Evidence for the involvement of influenza A (fowl plague Rostock) virus protein P2 in ApG and mRNA primed in vitro RNA synthesis. J. Gen. Virol. 57:407-13
    • (1981) J. Gen. Virol. , vol.57 , pp. 407-413
    • Nichol, S.T.1    Penn, C.R.2    Mahy, B.W.3
  • 119
    • 0033804340 scopus 로고    scopus 로고
    • Characterization of human influenza A (H5N1) virus infection in mice: Neuro-, pneumo- and adipotropic infection
    • Nishimura H, Itamura S, Iwasaki T, Kurata T, Tashiro M. 2000. Characterization of human influenza A (H5N1) virus infection in mice: neuro-, pneumo- and adipotropic infection. J. Gen. Virol. 81:2503-10
    • (2000) J. Gen. Virol. , vol.81 , pp. 2503-2510
    • Nishimura, H.1    Itamura, S.2    Iwasaki, T.3    Kurata, T.4    Tashiro, M.5
  • 120
    • 0027478170 scopus 로고
    • Identification of critical contact residues in the NC41 epitope of a subtype N9 influenza virus neuraminidase
    • Nuss JM, Whitaker PB, Air GM. 1993. Identification of critical contact residues in the NC41 epitope of a subtype N9 influenza virus neuraminidase. Proteins 15:121-32
    • (1993) Proteins , vol.15 , pp. 121-132
    • Nuss, J.M.1    Whitaker, P.B.2    Air, G.M.3
  • 121
    • 0023244889 scopus 로고
    • Temperature-sensitive defect of influenza A/Ann Arbor/6/60 cold-adapted variant leads to a blockage of matrix polypeptide incorporation into the plasma membrane of the infected cells
    • Odagiri T, Tanaka T, Tobita K. 1987. Temperature-sensitive defect of influenza A/Ann Arbor/6/60 cold-adapted variant leads to a blockage of matrix polypeptide incorporation into the plasma membrane of the infected cells. Virus Res. 7:203-18
    • (1987) Virus Res. , vol.7 , pp. 203-218
    • Odagiri, T.1    Tanaka, T.2    Tobita, K.3
  • 122
    • 0028086229 scopus 로고
    • Non-homologous recombination between the hemagglutinin gene and the nucleoprorein gene of an influenza virus
    • Orlich M, Gottwald H, Rott R. 1994. Non-homologous recombination between the hemagglutinin gene and the nucleoprorein gene of an influenza virus. Virology 204:462-65
    • (1994) Virology , vol.204 , pp. 462-465
    • Orlich, M.1    Gottwald, H.2    Rott, R.3
  • 123
    • 0017326183 scopus 로고
    • P1 and P3 proteins of influenza virus are required for complementary RNA synthesis
    • Palese P, Ritchey MB, Schulman JL. 1977. P1 and P3 proteins of influenza virus are required for complementary RNA synthesis. J. Virol. 21:1187-95
    • (1977) J. Virol. , vol.21 , pp. 1187-1195
    • Palese, P.1    Ritchey, M.B.2    Schulman, J.L.3
  • 124
    • 0017263506 scopus 로고
    • Differences in RNA patterns of influenza A viruses
    • Palese P, Schulman JL. 1976. Differences in RNA patterns of influenza A viruses. J. Virol. 17:876-84
    • (1976) J. Virol. , vol.17 , pp. 876-884
    • Palese, P.1    Schulman, J.L.2
  • 125
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese P, Tobita K, Ueda M, Compans RW. 1974. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61:397-410
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 126
    • 0020067634 scopus 로고
    • Variation of influenza A, B, and C viruses
    • Palese P, Young JF. 1982. Variation of influenza A, B, and C viruses. Science 215:1468-74
    • (1982) Science , vol.215 , pp. 1468-1474
    • Palese, P.1    Young, J.F.2
  • 127
    • 0033761734 scopus 로고    scopus 로고
    • Identification of a membrane targeting and degradation signal in the p42 protein of influenza C virus
    • Pekosz A, Lamb RA. 2000. Identification of a membrane targeting and degradation signal in the p42 protein of influenza C virus. J. Virol. 74:10480-88
    • (2000) J. Virol. , vol.74 , pp. 10480-10488
    • Pekosz, A.1    Lamb, R.A.2
  • 128
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto LH, Holsinger LJ, Lamb RA. 1992. Influenza virus M2 protein has ion channel activity. Cell 69:517-28
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 130
    • 0018459347 scopus 로고
    • Transfer of 5′-terminal cap of globin mRNA to influenza viral complementary RNA during transcription in vitro
    • Plotch SJ, Bouloy M, Krug RM. 1979. Transfer of 5′-terminal cap of globin mRNA to influenza viral complementary RNA during transcription in vitro. Proc. Natl. Acad. Sci. USA 76:1618-22
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1618-1622
    • Plotch, S.J.1    Bouloy, M.2    Krug, R.M.3
  • 131
    • 0019394947 scopus 로고
    • A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription
    • Plotch SJ, Bouloy M, Ulmanen I, Krug RM. 1981. A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription. Cell 23:847-58
    • (1981) Cell , vol.23 , pp. 847-858
    • Plotch, S.J.1    Bouloy, M.2    Ulmanen, I.3    Krug, R.M.4
  • 132
    • 0025322445 scopus 로고
    • Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: Theoretical assignment of functional domains
    • Poch O, Blumberg BM, Bougueleret L, Tordo N. 1990. Sequence comparison of five polymerases (L proteins) of unsegmented negative-strand RNA viruses: theoretical assignment of functional domains. J. Gen. Virol. 71:1153-62
    • (1990) J. Gen. Virol. , vol.71 , pp. 1153-1162
    • Poch, O.1    Blumberg, B.M.2    Bougueleret, L.3    Tordo, N.4
  • 133
    • 0017264409 scopus 로고
    • A re-examination of influenza single-and double-stranded RNAs by gel electrophoresis
    • Pons MW. 1976. A re-examination of influenza single-and double-stranded RNAs by gel electrophoresis. Virology 69:789-92
    • (1976) Virology , vol.69 , pp. 789-792
    • Pons, M.W.1
  • 134
    • 0026726876 scopus 로고
    • Nuclear retention of M1 protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins
    • Rey O, Nayak DP. 1992. Nuclear retention of M1 protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins. J. Virol. 66:5815-24
    • (1992) J. Virol. , vol.66 , pp. 5815-5824
    • Rey, O.1    Nayak, D.P.2
  • 135
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
    • Rogers GN, Paulson JC, Daniels RS, Skehel JJ, Wilson IA, Wiley DC. 1983. Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature 304:76-78
    • (1983) Nature , vol.304 , pp. 76-78
    • Rogers, G.N.1    Paulson, J.C.2    Daniels, R.S.3    Skehel, J.J.4    Wilson, I.A.5    Wiley, D.C.6
  • 136
    • 0019154189 scopus 로고
    • On the offgin of the gene coding for an influenza A virus nucleocapsid protein
    • Rohde W, Scholtissek C. 1980. On the offgin of the gene coding for an influenza A virus nucleocapsid protein. Arch. Virol. 64:213-23
    • (1980) Arch. Virol. , vol.64 , pp. 213-223
    • Rohde, W.1    Scholtissek, C.2
  • 137
    • 0032487864 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus
    • Rosenthal PB, Zhang X, Formanowski F, Fitz W, Wong CH, et al. 1998. Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus. Nature 396:92-96
    • (1998) Nature , vol.396 , pp. 92-96
    • Rosenthal, P.B.1    Zhang, X.2    Formanowski, F.3    Fitz, W.4    Wong, C.H.5
  • 138
    • 0018721596 scopus 로고
    • Correlation of pathogenicity and gene constellation of influenza A viruses. III. Non-pathogenic recombinants derived from highly pathogenic parent strains
    • Rott R, Orlich M, Scholtissek C. 1979. Correlation of pathogenicity and gene constellation of influenza A viruses. III. Non-pathogenic recombinants derived from highly pathogenic parent strains. J. Gen. Virol. 44:471-77
    • (1979) J. Gen. Virol. , vol.44 , pp. 471-477
    • Rott, R.1    Orlich, M.2    Scholtissek, C.3
  • 139
    • 0031611142 scopus 로고    scopus 로고
    • Mechanisms involved in natural and experimental neuropathology of influenza viruses: Evidence and speculation
    • Schlesinger RW, Husak PJ, Bradshaw GL, Panayotov PP. 1998. Mechanisms involved in natural and experimental neuropathology 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
  • 140
    • 0016775571 scopus 로고
    • Isolation and characterization of temperature-sensitive mutants of fow1 plague virus
    • Scholtissek C, Bowles AL. 1975. Isolation and characterization of temperature-sensitive mutants of fow1 plague virus. Virology 67:576-87
    • (1975) Virology , vol.67 , pp. 576-587
    • Scholtissek, C.1    Bowles, A.L.2
  • 141
    • 0022377314 scopus 로고
    • The nucleoprotein as a possible major factor in determining host specificity of influenza H3N2 viruses
    • Scholtissek C, Burger H, Kistner O, Shortridge KF. 1985. The nucleoprotein as a possible major factor in determining host specificity of influenza H3N2 viruses. Virology 147:287-94
    • (1985) Virology , vol.147 , pp. 287-294
    • Scholtissek, C.1    Burger, H.2    Kistner, O.3    Shortridge, K.F.4
  • 143
    • 0017638141 scopus 로고
    • Correlation of pathogenicity and gene constellation of an influenza A virus (fowl plague). I. Exchange of a single gene
    • Scholtissek C, Rott R, Orlich M, Harms E, Rohde W. 1977. Correlation of pathogenicity and gene constellation of an influenza A virus (fowl plague). I. Exchange of a single gene. Virology 81:74-80
    • (1977) Virology , vol.81 , pp. 74-80
    • Scholtissek, C.1    Rott, R.2    Orlich, M.3    Harms, E.4    Rohde, W.5
  • 144
    • 0018216361 scopus 로고
    • Genetic relatedness between the new 1977 epidemic strains (H1N1) of influenza and human influenza strains isolated between 1947 and 1957 (H1N1)
    • Scholtissek C, von Hoyningen V, Rott R. 1978. Genetic relatedness between the new 1977 epidemic strains (H1N1) of influenza and human influenza strains isolated between 1947 and 1957 (H1N1). Virology 89:613-17
    • (1978) Virology , vol.89 , pp. 613-617
    • Scholtissek, C.1    Von Hoyningen, V.2    Rott, R.3
  • 145
    • 0018144758 scopus 로고
    • On the origin of the human influenza virus subtypes H2N2 and H3N2
    • Scholtissek C, von Hoyningen V, Rott R. 1978. On the origin of the human influenza virus subtypes H2N2 and H3N2. Virology 87:13-20
    • (1978) Virology , vol.87 , pp. 13-20
    • Scholtissek, C.1    Von Hoyningen, V.2    Rott, R.3
  • 147
    • 0029861191 scopus 로고    scopus 로고
    • Influenza virus neuraminidase activates latent transforming growth factor beta
    • Schultz-Cherry S, Hinshaw VS. 1996. Influenza virus neuraminidase activates latent transforming growth factor beta. J. Virol. 70:8624-29
    • (1996) J. Virol. , vol.70 , pp. 8624-8629
    • Schultz-Cherry, S.1    Hinshaw, V.S.2
  • 148
    • 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 GI, Krug RM. 1988. Influenza virus RNA replication in vitro: synthesis of viral template RNAs and virion RNAs in the absence of an added primer. J. Virol. 62:2285-90
    • (1988) J. Virol. , vol.62 , pp. 2285-2290
    • Shapiro, G.I.1    Krug, R.M.2
  • 149
    • 0345471424 scopus 로고    scopus 로고
    • Characterization of avian H5N1 influenza viruses from poultry in Hong Kong
    • Shortridge KF, Zhou NN, Guan Y, Gao P, Ito T, et al. 1998. Characterization of avian H5N1 influenza viruses from poultry in Hong Kong. Virology 252:331-42
    • (1998) Virology , vol.252 , pp. 331-342
    • Shortridge, K.F.1    Zhou, N.N.2    Guan, Y.3    Gao, P.4    Ito, T.5
  • 150
    • 0014288506 scopus 로고
    • Temperature-sensitive mutants of influenza A virus: Isolation of mutants and preliminary observations on genetic recombination and complementation
    • Simpson RW, Hirst GK. 1968. Temperature-sensitive mutants of influenza A virus: isolation of mutants and preliminary observations on genetic recombination and complementation. Virology 35:41-49
    • (1968) Virology , vol.35 , pp. 41-49
    • Simpson, R.W.1    Hirst, G.K.2
  • 151
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-69
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 152
    • 0001058676 scopus 로고
    • Variation in influenza virus genes: Epidemiology, pathogenic, and evolutionary consequenses
    • ed. RM Krug. New York: Plenum
    • Smith FL, Palese P. 1989. Variation in influenza virus genes: epidemiology, pathogenic, and evolutionary consequenses. In The Influenza Viruses, ed. RM Krug, pp. 319-59. New York: Plenum
    • (1989) The Influenza Viruses , pp. 319-359
    • Smith, F.L.1    Palese, P.2
  • 153
    • 0020033132 scopus 로고
    • Replication of the influenza virus genome
    • Smith GL, Hay AJ. 1982. Replication of the influenza virus genome. Virology 118:96-108
    • (1982) Virology , vol.118 , pp. 96-108
  • 154
    • 0033602713 scopus 로고    scopus 로고
    • Role of hemagglutinin cleavage for the pathogenicity of influenza virus
    • Steinhauer DA. 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
  • 155
    • 0026343370 scopus 로고
    • Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: Evidence for virus-specific regulation of the pH of glycoprotein transport vesicles
    • Steinhauer DA, Wharton SA, Skehel JJ, Wiley DC, Hay AJ. 1991. Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles. Proc. Natl. Acad. Sci. USA 88:11525-29
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11525-11529
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Hay, A.J.5
  • 156
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multi-basic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Grober A, Vey M, Angliker H, Shaw E, Thomas G, et al. 1992. Influenza virus hemagglutinin with multi-basic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11:2407-14
    • (1992) EMBO J. , vol.11 , pp. 2407-2414
    • Stieneke-Grober, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5
  • 157
    • 0031903499 scopus 로고    scopus 로고
    • Comparisons of highly virulent H5N1 influenza A viruses isolated from humans and chickens from Hong Kong
    • Suarez DL, Perdue ML, Cox N, Rowe T, Bender C, et al. 1998. Comparisons of highly virulent H5N1 influenza A viruses isolated from humans and chickens from Hong Kong. J. Virol. 72:6678-88
    • (1998) J. Virol. , vol.72 , pp. 6678-6688
    • Suarez, D.L.1    Perdue, M.L.2    Cox, N.3    Rowe, T.4    Bender, C.5
  • 158
    • 14444284599 scopus 로고    scopus 로고
    • Characterization of an avian influenza A (H5N1) virus isolated from a child with a fatal respiratory illness
    • Subbarao K, Klimov A, Katz J, Regnery H, Lim W, et al. 1998. Characterization of an avian influenza A (H5N1) virus isolated from a child with a fatal respiratory illness. Science 279:393-96
    • (1998) Science , vol.279 , pp. 393-396
    • Subbarao, K.1    Klimov, A.2    Katz, J.3    Regnery, H.4    Lim, W.5
  • 159
    • 0016838637 scopus 로고
    • Further isolation and characterization of temperature-sensitive mutants of influenza virus
    • Sugiura A, Ueda M, Tobita K, Enomoto C. 1975. Further isolation and characterization of temperature-sensitive mutants of influenza virus, Virology 65:363-73
    • (1975) Virology , vol.65 , pp. 363-373
    • Sugiura, A.1    Ueda, M.2    Tobita, K.3    Enomoto, C.4
  • 161
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue RJ, Hay AJ. 1991. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 180:617-24
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 162
    • 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, Broni BA, Krug RM. 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. USA 78:7355-59
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7355-7359
    • Ulmanen, I.1    Broni, B.A.2    Krug, R.M.3
  • 163
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein M, Wu WY, Kok GB, Pegg MS, Dyason JC, et al. 1993. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363:418-23
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, M.1    Wu, W.Y.2    Kok, G.B.3    Pegg, M.S.4    Dyason, J.C.5
  • 164
    • 0022619050 scopus 로고
    • Comparative analyses of the specificities of anti-influenza hemagglutinin antibodies in human sera
    • Wang ML, Skehel JJ, Wiley DC. 1986. Comparative analyses of the specificities of anti-influenza hemagglutinin antibodies in human sera. J. Virol. 57:124-28
    • (1986) J. Virol. , vol.57 , pp. 124-128
    • Wang, M.L.1    Skehel, J.J.2    Wiley, D.C.3
  • 165
    • 0023226739 scopus 로고
    • Antigenic structure and variation in an influenza virus N9 neuraminidase
    • Webster RG, Air GM, Metzger DW, Colman PM, Varghese JN, et al. 1987. Antigenic structure and variation in an influenza virus N9 neuraminidase. J. Virol. 61:2910-16
    • (1987) J. Virol. , vol.61 , pp. 2910-2916
    • Webster, R.G.1    Air, G.M.2    Metzger, D.W.3    Colman, P.M.4    Varghese, J.N.5
  • 167
    • 0023666999 scopus 로고
    • Influenza virus A pathogenicity: The pivotal role of hemagglutinin
    • Webster RG, Rott R. 1987. Influenza virus A pathogenicity: the pivotal role of hemagglutinin. Cell 50:665-66
    • (1987) Cell , vol.50 , pp. 665-666
    • Webster, R.G.1    Rott, R.2
  • 168
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-94
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 169
    • 0037066845 scopus 로고    scopus 로고
    • Questioning the evidence for genetic recombination in the 1918 "Spanish flu" virus
    • Worobey M, Rambaut A, Pybus OG, Robertson DL. 2002. Questioning the evidence for genetic recombination in the 1918 "Spanish flu" virus. Science 296:211
    • (2002) Science , vol.296 , pp. 211
    • Worobey, M.1    Rambaut, A.2    Pybus, O.G.3    Robertson, D.L.4
  • 172
    • 0023730218 scopus 로고
    • Evidence that the matrix protein of influenza C virus is coded for by a spliced mRNA
    • Yamashita M, Krystal M, Palese P. 1988. Evidence that the matrix protein of influenza C virus is coded for by a spliced mRNA. J. Virol. 62:3348-55
    • (1988) J. Virol. , vol.62 , pp. 3348-3355
    • Yamashita, M.1    Krystal, M.2    Palese, P.3
  • 173
    • 0031550787 scopus 로고    scopus 로고
    • Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses
    • Yang P, Bansal A, Liu C, Air GM. 1997. Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses. Virology 229:155-65
    • (1997) Virology , vol.229 , pp. 155-165
    • Yang, P.1    Bansal, A.2    Liu, C.3    Air, G.M.4
  • 174
    • 0000210314 scopus 로고
    • Evolution of human influenza A viruses in nature: Recombination contributes to genetic variation of H1N1 strains
    • Young JF, Palese P. 1979. Evolution of human influenza A viruses in nature: recombination contributes to genetic variation of H1N1 strains. Proc. Natl. Acad. Sci. USA 76:6547-51
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6547-6551
    • Young, J.F.1    Palese, P.2
  • 175
    • 0035253852 scopus 로고    scopus 로고
    • Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein
    • Yuan W, Krug RM. 2001. Influenza B virus NS1 protein inhibits conjugation of the interferon (IFN)-induced ubiquitin-like ISG15 protein. EMBO J. 20:362-71
    • (2001) EMBO J. , vol.20 , pp. 362-371
    • Yuan, W.1    Krug, R.M.2
  • 176
    • 0025266931 scopus 로고
    • Solubilization of matrix protein M1/M from virions occurs at different pH for orthomyxo- and paramyxoviruses
    • Zhirnov OP. 1990. Solubilization of matrix protein M1/M from virions occurs at different pH for orthomyxo- and paramyxoviruses. Virology 176:274-79
    • (1990) Virology , vol.176 , pp. 274-279
    • Zhirnov, O.P.1


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