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Volumn 89, Issue 2, 2015, Pages 1094-1104

The influenza virus neuraminidase protein transmembrane and head domains have coevolved

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS SIALIDASE; NA PROTEIN, INFLUENZA A VIRUS; SIALIDASE; VIRAL PROTEIN;

EID: 84920842323     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02005-14     Document Type: Article
Times cited : (24)

References (54)
  • 1
    • 84855465724 scopus 로고    scopus 로고
    • Transmembrane helix dimerization: beyond the search for sequence motifs
    • Li E, Wimley WC, Hristova K. 2012. Transmembrane helix dimerization: beyond the search for sequence motifs. Biochim Biophys Acta 1818: 183-193. http://dx.doi.org/10.1016/j.bbamem.2011.08.031.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 183-193
    • Li, E.1    Wimley, W.C.2    Hristova, K.3
  • 2
    • 67650069254 scopus 로고    scopus 로고
    • Interaction and conformational dynamics of membrane-spanning protein helices
    • Langosch D, Arkin IT. 2009. Interaction and conformational dynamics of membrane-spanning protein helices. Protein Sci 18:1343-1358. http://dx.doi.org/10.1002/pro.154.
    • (2009) Protein Sci , vol.18 , pp. 1343-1358
    • Langosch, D.1    Arkin, I.T.2
  • 3
    • 46049088691 scopus 로고    scopus 로고
    • Protein-protein interactions in the membrane: sequence, structural, and biological motifs
    • Moore DT, Berger BW, DeGrado WF. 2008. Protein-protein interactions in the membrane: sequence, structural, and biological motifs. Structure 16:991-1001. http://dx.doi.org/10.1016/j.str.2008.05.007.
    • (2008) Structure , vol.16 , pp. 991-1001
    • Moore, D.T.1    Berger, B.W.2    DeGrado, W.F.3
  • 4
    • 0025185098 scopus 로고
    • Mutations of immunoglobulin transmembrane and cytoplasmic domains: effects on intracellular signaling and antigen presentation
    • Shaw AC, Mitchell RN, Weaver YK, Campos-Torres J, Abbas AK, Leder P. 1990. Mutations of immunoglobulin transmembrane and cytoplasmic domains: effects on intracellular signaling and antigen presentation. Cell 63:381-392. http://dx.doi.org/10.1016/0092-8674(90)90171-A.
    • (1990) Cell , vol.63 , pp. 381-392
    • Shaw, A.C.1    Mitchell, R.N.2    Weaver, Y.K.3    Campos-Torres, J.4    Abbas, A.K.5    Leder, P.6
  • 5
    • 0037184955 scopus 로고    scopus 로고
    • The organizing principle in the formation of the T cell receptor-CD3 complex
    • Call ME, Pyrdol J, Wiedmann M, Wucherpfennig KW. 2002. The organizing principle in the formation of the T cell receptor-CD3 complex. Cell 111:967-979. http://dx.doi.org/10.1016/S0092-8674(02)01194-7.
    • (2002) Cell , vol.111 , pp. 967-979
    • Call, M.E.1    Pyrdol, J.2    Wiedmann, M.3    Wucherpfennig, K.W.4
  • 6
    • 0141632799 scopus 로고    scopus 로고
    • Dislocation of a type I membrane protein requires interactions between membrane-spanning segments within the lipid bilayer
    • Lilley BN, Tortorella D, Ploegh HL. 2003. Dislocation of a type I membrane protein requires interactions between membrane-spanning segments within the lipid bilayer. Mol Biol Cell 14:3690-3698. http://dx.doi.org/10.1091/mbc.E03-03-0192.
    • (2003) Mol Biol Cell , vol.14 , pp. 3690-3698
    • Lilley, B.N.1    Tortorella, D.2    Ploegh, H.L.3
  • 8
    • 14844346910 scopus 로고    scopus 로고
    • Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering
    • Luo BH, Carman CV, Takagi J, Springer TA. 2005. Disrupting integrin transmembrane domain heterodimerization increases ligand binding affinity, not valency or clustering. Proc Natl Acad Sci USA 102:3679-3684. http://dx.doi.org/10.1073/pnas.0409440102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3679-3684
    • Luo, B.H.1    Carman, C.V.2    Takagi, J.3    Springer, T.A.4
  • 9
    • 84881536447 scopus 로고    scopus 로고
    • Quality control of integral membrane proteins by assembly-dependent membrane integration
    • Feige MJ, Hendershot LM. 2013. Quality control of integral membrane proteins by assembly-dependent membrane integration. Mol Cell 51:297-309. http://dx.doi.org/10.1016/j.molcel.2013.07.013.
    • (2013) Mol Cell , vol.51 , pp. 297-309
    • Feige, M.J.1    Hendershot, L.M.2
  • 10
    • 83655162842 scopus 로고    scopus 로고
    • The cell biology of receptor-mediated virus entry
    • Grove J, Marsh M. 2011. The cell biology of receptor-mediated virus entry. J Cell Biol 195:1071-1082. http://dx.doi.org/10.1083/jcb.201108131.
    • (2011) J Cell Biol , vol.195 , pp. 1071-1082
    • Grove, J.1    Marsh, M.2
  • 11
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M, Helenius A. 2006. Virus entry: open sesame. Cell 124:729-740. http://dx.doi.org/10.1016/j.cell.2006.02.007.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 12
    • 0041765800 scopus 로고    scopus 로고
    • Insider information: what viruses tell us about endocytosis
    • Pelkmans L, Helenius A. 2003. Insider information: what viruses tell us about endocytosis. Curr Opin Cell Biol 15:414-422. http://dx.doi.org/10.1016/S0955-0674(03)00081-4.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 414-422
    • Pelkmans, L.1    Helenius, A.2
  • 13
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R, Kurowski B, Johnson AE, Hebert DN. 2003. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 11:79-90. http://dx.doi.org/10.1016/S1097-2765(02)00821-3.
    • (2003) Mol Cell , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 14
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
    • White JM, Delos SE, Brecher M, Schornberg K. 2008. Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit Rev Biochem Mol Biol 43:189-219. http://dx.doi.org/10.1080/10409230802058320.
    • (2008) Crit Rev Biochem Mol Biol , vol.43 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 15
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: biological machines that undergo a metamorphosis
    • Dutch RE, Jardetzky TS, Lamb RA. 2000. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci Rep 20: 597-612. http://dx.doi.org/10.1023/A:1010467106305.
    • (2000) Biosci Rep , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 16
    • 0342745990 scopus 로고
    • Neuraminidase: the specific enzyme of influenza virus and Vibrio cholerae
    • Gottschalk A. 1957. Neuraminidase: the specific enzyme of influenza virus and Vibrio cholerae. Biochim Biophys Acta 23:645-646. http://dx.doi.org/10.1016/0006-3002(57)90389-X.
    • (1957) Biochim Biophys Acta , vol.23 , pp. 645-646
    • Gottschalk, A.1
  • 17
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action
    • Palese P, Compans RW. 1976. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J Gen Virol 33:159-163. http://dx.doi.org/10.1099/0022-1317-33-1-159.
    • (1976) J Gen Virol , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 18
    • 0021416306 scopus 로고
    • NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation
    • Bos TJ, Davis AR, Nayak DP. 1984. NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation. Proc Natl Acad Sci USA 81:2327-2331. http://dx.doi.org/10.1073/pnas.81.8.2327.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 2327-2331
    • Bos, T.J.1    Davis, A.R.2    Nayak, D.P.3
  • 19
    • 0018092715 scopus 로고
    • Crystallization and peptide maps of neuraminidase 'heads' from H2N2 and H3N2 influenza virus strains
    • Laver WG. 1978. Crystallization and peptide maps of neuraminidase "heads" from H2N2 and H3N2 influenza virus strains. Virology 86:78-87. http://dx.doi.org/10.1016/0042-6822(78)90009-0.
    • (1978) Virology , vol.86 , pp. 78-87
    • Laver, W.G.1
  • 20
    • 84872074817 scopus 로고    scopus 로고
    • Assembly of subtype 1 influenza neuraminidase is driven by both the transmembrane and head domains
    • da Silva DV, Nordholm J, Madjo U, Pfeiffer A, Daniels R. 2013. Assembly of subtype 1 influenza neuraminidase is driven by both the transmembrane and head domains. J Biol Chem 288:644-653. http://dx.doi.org/10.1074/jbc.M112.424150.
    • (2013) J Biol Chem , vol.288 , pp. 644-653
    • da Silva, D.V.1    Nordholm, J.2    Madjo, U.3    Pfeiffer, A.4    Daniels, R.5
  • 21
    • 84876261470 scopus 로고    scopus 로고
    • Polar residues and their positional context dictate the transmembrane domain interactions of influenza a neuraminidases
    • Nordholm J, da Silva DV, Damjanovic J, Dou D, Daniels R. 2013. Polar residues and their positional context dictate the transmembrane domain interactions of influenza a neuraminidases. J Biol Chem 288:10652-10660. http://dx.doi.org/10.1074/jbc.M112.440230.
    • (2013) J Biol Chem , vol.288 , pp. 10652-10660
    • Nordholm, J.1    da Silva, D.V.2    Damjanovic, J.3    Dou, D.4    Daniels, R.5
  • 23
    • 0034705225 scopus 로고    scopus 로고
    • A DNA transfection system for generation of influenza A virus from eight plasmids
    • Hoffmann E, Neumann G, Kawaoka Y, Hobom G, Webster RG. 2000. A DNA transfection system for generation of influenza A virus from eight plasmids. Proc Natl Acad Sci USA 97:6108-6113. http://dx.doi.org/10.1073/pnas.100133697.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6108-6113
    • Hoffmann, E.1    Neumann, G.2    Kawaoka, Y.3    Hobom, G.4    Webster, R.G.5
  • 25
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent end points
    • Reed LJ, Muench H. 1938. A simple method of estimating fifty percent end points. Am J Epidemiol 27:493-497.
    • (1938) Am J Epidemiol , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 26
    • 39749094440 scopus 로고    scopus 로고
    • Analysis of protein folding and oxidation in the endoplasmic reticulum
    • Unit 15.6
    • Francis E, Daniels R, Hebert DN. 2002. Analysis of protein folding and oxidation in the endoplasmic reticulum. Curr Protoc Cell Biol Chapter 15:Unit 15.6.
    • (2002) Curr Protoc Cell Biol Chapter , vol.15
    • Francis, E.1    Daniels, R.2    Hebert, D.N.3
  • 27
    • 0037474296 scopus 로고    scopus 로고
    • GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane
    • Schneider D, Engelman DM. 2003. GALLEX, a measurement of heterologous association of transmembrane helices in a biological membrane. J Biol Chem 278:3105-3111. http://dx.doi.org/10.1074/jbc.M206287200.
    • (2003) J Biol Chem , vol.278 , pp. 3105-3111
    • Schneider, D.1    Engelman, D.M.2
  • 29
    • 67650892251 scopus 로고    scopus 로고
    • The persistent legacy of the 1918 influenza virus
    • Morens DM, Taubenberger JK, Fauci AS. 2009. The persistent legacy of the 1918 influenza virus. N Engl J Med 361:225-229. http://dx.doi.org/10.1056/NEJMp0904819.
    • (2009) N Engl J Med , vol.361 , pp. 225-229
    • Morens, D.M.1    Taubenberger, J.K.2    Fauci, A.S.3
  • 30
    • 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. http://dx.doi.org/10.1016/0042-6822(74)90276-1.
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 31
    • 0022470969 scopus 로고
    • Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus
    • Bos TJ, Nayak DP. 1986. Identification of defects in the neuraminidase gene of four temperature-sensitive mutants of A/WSN/33 influenza virus. Virology 154:85-96. http://dx.doi.org/10.1016/0042-6822(86)90432-0.
    • (1986) Virology , vol.154 , pp. 85-96
    • Bos, T.J.1    Nayak, D.P.2
  • 32
    • 0345426371 scopus 로고    scopus 로고
    • Mutation of neuraminidase cysteine residues yields temperature-sensitive influenza viruses
    • Basler CF, Garcia-Sastre A, Palese P. 1999. Mutation of neuraminidase cysteine residues yields temperature-sensitive influenza viruses. J Virol 73:8095-8103.
    • (1999) J Virol , vol.73 , pp. 8095-8103
    • Basler, C.F.1    Garcia-Sastre, A.2    Palese, P.3
  • 33
    • 0015420065 scopus 로고
    • Isolation and preliminary characterization of temperature-sensitive mutants of influenza virus
    • Sugiura A, Tobita K, Kilbourne ED. 1972. Isolation and preliminary characterization of temperature-sensitive mutants of influenza virus. J Virol 10:639-647.
    • (1972) J Virol , vol.10 , pp. 639-647
    • Sugiura, A.1    Tobita, K.2    Kilbourne, E.D.3
  • 34
    • 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, Kobasa D, Kawaoka Y. 2000. Balanced hemagglutinin and neuraminidase activities are critical for efficient replication of influenza A virus. J Virol 74: 6015-6020. http://dx.doi.org/10.1128/JVI.74.13.6015-6020.2000.
    • (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    Kobasa, D.6    Kawaoka, Y.7
  • 36
    • 0034050212 scopus 로고    scopus 로고
    • Intergenic HA-NA interactions in influenza A virus: postreassortment substitutions of charged amino acid in the hemagglutinin of different subtypes
    • Kaverin NV, Matrosovich MN, Gambaryan AS, Rudneva IA, Shilov AA, Varich NL, Makarova NV, Kropotkina EA, Sinitsin BV. 2000. Intergenic HA-NA interactions in influenza A virus: postreassortment substitutions of charged amino acid in the hemagglutinin of different subtypes. Virus Res 66:123-129. http://dx.doi.org/10.1016/S0168-1702(99)00131-8.
    • (2000) Virus Res , vol.66 , pp. 123-129
    • Kaverin, N.V.1    Matrosovich, M.N.2    Gambaryan, A.S.3    Rudneva, I.A.4    Shilov, A.A.5    Varich, N.L.6    Makarova, N.V.7    Kropotkina, E.A.8    Sinitsin, B.V.9
  • 38
    • 0026343370 scopus 로고
    • Amantadine selection of a mutant influenza virus containing an acidstable 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 acidstable hemagglutinin glycoprotein: evidence for virus-specific regulation of the pH of glycoprotein transport vesicles. Proc Natl Acad Sci USA 88:11525-11529. http://dx.doi.org/10.1073/pnas.88.24.11525.
    • (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
  • 39
    • 84908638735 scopus 로고    scopus 로고
    • Type II transmembrane domain hydrophobicity dictates the cotranslational dependence for inversion
    • Dou D, da Silva DV, Nordholm J, Wang H, Daniels R. 2014. Type II transmembrane domain hydrophobicity dictates the cotranslational dependence for inversion. Mol Biol Cell 25:3363-3374. http://dx.doi.org/10.1091/mbc.E14-04-0874.
    • (2014) Mol Biol Cell , vol.25 , pp. 3363-3374
    • Dou, D.1    da Silva, D.V.2    Nordholm, J.3    Wang, H.4    Daniels, R.5
  • 40
    • 84861434240 scopus 로고    scopus 로고
    • Shifting hydrogen bonds may produce flexible transmembrane helices
    • Cao Z, Bowie JU. 2012. Shifting hydrogen bonds may produce flexible transmembrane helices. Proc Natl Acad Sci USA 109:8121-8126. http://dx.doi.org/10.1073/pnas.1201298109.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 8121-8126
    • Cao, Z.1    Bowie, J.U.2
  • 42
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H, Lear JD, DeGrado WF. 2001. Polar side chains drive the association of model transmembrane peptides. Proc Natl Acad Sci USA 98:880-885. http://dx.doi.org/10.1073/pnas.98.3.880.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 880-885
    • Gratkowski, H.1    Lear, J.D.2    DeGrado, W.F.3
  • 43
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • Zhou FX, Cocco MJ, Russ WP, Brunger AT, Engelman DM. 2000. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nat Struct Biol 7:154-160. http://dx.doi.org/10.1038/72430.
    • (2000) Nat Struct Biol , vol.7 , pp. 154-160
    • Zhou, F.X.1    Cocco, M.J.2    Russ, W.P.3    Brunger, A.T.4    Engelman, D.M.5
  • 44
    • 0025819126 scopus 로고
    • Membrane protein association by potential intramembrane charge pairs
    • Cosson P, Lankford SP, Bonifacino JS, Klausner RD. 1991. Membrane protein association by potential intramembrane charge pairs. Nature 351: 414-416. http://dx.doi.org/10.1038/351414a0.
    • (1991) Nature , vol.351 , pp. 414-416
    • Cosson, P.1    Lankford, S.P.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 45
    • 28444469781 scopus 로고    scopus 로고
    • Tryptophan supports interaction of transmembrane helices
    • Ridder A, Skupjen P, Unterreitmeier S, Langosch D. 2005. Tryptophan supports interaction of transmembrane helices. J Mol Biol 354:894-902. http://dx.doi.org/10.1016/j.jmb.2005.09.084.
    • (2005) J Mol Biol , vol.354 , pp. 894-902
    • Ridder, A.1    Skupjen, P.2    Unterreitmeier, S.3    Langosch, D.4
  • 46
    • 1642396353 scopus 로고    scopus 로고
    • Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins
    • Schneider D, Engelman DM. 2004. Involvement of transmembrane domain interactions in signal transduction by alpha/beta integrins. J Biol Chem 279:9840-9846. http://dx.doi.org/10.1074/jbc.M312749200.
    • (2004) J Biol Chem , vol.279 , pp. 9840-9846
    • Schneider, D.1    Engelman, D.M.2
  • 47
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • Yang J, Ma YQ, Page RC, Misra S, Plow EF, Qin J. 2009. Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc Natl Acad Sci USA 106:17729-17734. http://dx.doi.org/10.1073/pnas.0909589106.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17729-17734
    • Yang, J.1    Ma, Y.Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 48
    • 84861686640 scopus 로고    scopus 로고
    • Increased hemagglutinin content in a reassortant 2009 pandemic H1N1 influenza virus with chimeric neuraminidase containing donor A/Puerto Rico/8/34 virus transmembrane and stalk domains
    • Jing X, Phy K, Li X, Ye Z. 2012. Increased hemagglutinin content in a reassortant 2009 pandemic H1N1 influenza virus with chimeric neuraminidase containing donor A/Puerto Rico/8/34 virus transmembrane and stalk domains. Vaccine 30:4144-4152. http://dx.doi.org/10.1016/j.vaccine.2012.04.073.
    • (2012) Vaccine , vol.30 , pp. 4144-4152
    • Jing, X.1    Phy, K.2    Li, X.3    Ye, Z.4
  • 49
    • 2342585501 scopus 로고    scopus 로고
    • Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza A virus neuraminidase in raft association and virus budding
    • Barman S, Adhikary L, Chakrabarti AK, Bernas C, Kawaoka Y, Nayak DP. 2004. Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza A virus neuraminidase in raft association and virus budding. J Virol 78:5258-5269. http://dx.doi.org/10.1128/JVI.78.10.5258-5269.2004.
    • (2004) J Virol , vol.78 , pp. 5258-5269
    • Barman, S.1    Adhikary, L.2    Chakrabarti, A.K.3    Bernas, C.4    Kawaoka, Y.5    Nayak, D.P.6
  • 50
    • 0041387555 scopus 로고    scopus 로고
    • Chimeric influenza A viruses with a functional influenza B virus neuraminidase or hemagglutinin
    • Flandorfer A, Garcia-Sastre A, Basler CF, Palese P. 2003. Chimeric influenza A viruses with a functional influenza B virus neuraminidase or hemagglutinin. J Virol 77:9116-9123. http://dx.doi.org/10.1128/JVI.77.17.9116-9123.2003.
    • (2003) J Virol , vol.77 , pp. 9116-9123
    • Flandorfer, A.1    Garcia-Sastre, A.2    Basler, C.F.3    Palese, P.4
  • 51
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman JS, Lamb RA. 2011. Influenza virus assembly and budding. Virology 411:229-236. http://dx.doi.org/10.1016/j.virol.2010.12.003.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 52
    • 0027261465 scopus 로고
    • Selection and characterization of a neuraminidaseminus mutant of influenza virus and its rescue by cloned neuraminidase genes
    • Liu C, Air GM. 1993. Selection and characterization of a neuraminidaseminus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194:403-407. http://dx.doi.org/10.1006/viro.1993.1276.
    • (1993) Virology , vol.194 , pp. 403-407
    • Liu, C.1    Air, G.M.2
  • 53
    • 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 229:155-165. http://dx.doi.org/10.1006/viro.1996.8421.
    • (1997) Virology , vol.229 , pp. 155-165
    • Yang, P.1    Bansal, A.2    Liu, C.3    Air, G.M.4
  • 54
    • 0036842048 scopus 로고    scopus 로고
    • A release-competent influenza A virus mutant lacking the coding capacity for the neuraminidase active site
    • Gubareva LV, Nedyalkova MS, Novikov DV, Murti KG, Hoffmann E, Hayden FG. 2002. A release-competent influenza A virus mutant lacking the coding capacity for the neuraminidase active site. J Gen Virol 83:2683-2692.
    • (2002) J Gen Virol , vol.83 , pp. 2683-2692
    • Gubareva, L.V.1    Nedyalkova, M.S.2    Novikov, D.V.3    Murti, K.G.4    Hoffmann, E.5    Hayden, F.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.