메뉴 건너뛰기




Volumn 83, Issue 8, 2009, Pages 3568-3580

Amino acid residues in the fusion peptide pocket regulate the ph of activation of the H5N1 influenza virus hemagglutinin protein

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CELL SURFACE PROTEIN; HISTIDINE; INFLUENZA VIRUS HEMAGGLUTININ; PROTEIN SUBUNIT; VIRUS FUSION PROTEIN; HEMAGGLUTININ, AVIAN INFLUENZA A VIRUS;

EID: 64049092310     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02238-08     Document Type: Article
Times cited : (89)

References (53)
  • 1
  • 2
    • 0032888955 scopus 로고    scopus 로고
    • Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter
    • Buchholz, U. J., S. Finke, and K. K. Conzelmann. 1999. Generation of bovine respiratory syncytial virus (BRSV) from cDNA: BRSV NS2 is not essential for virus replication in tissue culture, and the human RSV leader region acts as a functional BRSV genome promoter. J. Virol. 73:251-259.
    • (1999) J. Virol. , vol.73 , pp. 251-259
    • Buchholz, U.J.1    Finke, S.2    Conzelmann, K.K.3
  • 3
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 4
    • 33744983345 scopus 로고    scopus 로고
    • pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide
    • Chang, D. K., and S. F. Cheng. 2006. pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide. Biochem. J. 396:557-563.
    • (2006) Biochem. J. , vol.396 , pp. 557-563
    • Chang, D.K.1    Cheng, S.F.2
  • 5
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor, R. J., Y. Kawaoka, R. G. Webster, and J. C. Paulson. 1994. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 6
    • 0035881708 scopus 로고    scopus 로고
    • Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    • DOI 10.1093/emboj/20.16.4432
    • Cross, K. J., S. A. Wharton, J. J. Skehel, D. C. Wiley, and D. A. Steinhauer. 2001. Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics. EMBO J. 20:4432-4442. (Pubitemid 32772038)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4432-4442
    • Cross, K.J.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Steinhauer, D.A.5
  • 9
    • 0022656816 scopus 로고
    • Variant influenza virus hemagglutinin that induces fusion at elevated pH
    • Doms, R. W., M. J. Gething, J. Henneberry, J. White, and A. Helenius. 1986. Variant influenza virus hemagglutinin that induces fusion at elevated pH. J. Virol. 57:603-613. (Pubitemid 16147866)
    • (1986) Journal of Virology , vol.57 , Issue.2 , pp. 603-613
    • Doms, R.W.1    Gething, M.-J.2    Henneberry, J.3
  • 12
    • 0028074306 scopus 로고
    • Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones
    • Garten, W., S. Hallenberger, D. Ortmann, W. Schafer, M. Vey, H. Angliker, E. Shaw, and H. D. Klenk. 1994. Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones. Biochimie 76:217-225.
    • (1994) Biochimie , vol.76 , pp. 217-225
    • Garten, W.1    Hallenberger, S.2    Ortmann, D.3    Schafer, W.4    Vey, M.5    Angliker, H.6    Shaw, E.7    Klenk, H.D.8
  • 13
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething, M. J., R. W. Doms, D. York, and J. White. 1986. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 14
    • 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
  • 15
    • 30344461926 scopus 로고    scopus 로고
    • Comparison of in vitro replication features of H7N3 influenza viruses from wild ducks and turkeys: Potential implications for interspecies transmission
    • Giannecchini, S., L. Campitelli, L. Calzoletti, M. A. De Marco, A. Azzi, and I. Donatelli. 2006. Comparison of in vitro replication features of H7N3 influenza viruses from wild ducks and turkeys: potential implications for interspecies transmission. J. Gen. Virol. 87:171-175.
    • (2006) J. Gen. Virol. , vol.87 , pp. 171-175
    • Giannecchini, S.1    Campitelli, L.2    Calzoletti, L.3    De Marco, M.A.4    Azzi, A.5    Donatelli, I.6
  • 16
    • 0036500549 scopus 로고    scopus 로고
    • H5 avian and H9 swine influenza virus haemagglutinin structures: Possible origin of influenza subtypes
    • Ha, Y., D. J. Stevens, J. J. Skehel, and D. C. Wiley. 2002. H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. EMBO J. 21:865-875.
    • (2002) EMBO J. , vol.21 , pp. 865-875
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 17
    • 0038240827 scopus 로고    scopus 로고
    • X-ray structure of the hemagglutinin of a potential H3 avian progenitor of the 1968 Hong Kong pandemic influenza virus
    • Ha, Y., D. J. Stevens, J. J. Skehel, and D. C. Wiley. 2003. X-ray structure of the hemagglutinin of a potential H3 avian progenitor of the 1968 Hong Kong pandemic influenza virus. Virology 309:209-218.
    • (2003) Virology , vol.309 , pp. 209-218
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 18
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha, Y., D. J. Stevens, J. J. Skehel, and D. C. Wiley. 2001. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc. Natl. Acad. Sci. USA 98:11181-11186.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 19
  • 20
    • 0035559445 scopus 로고    scopus 로고
    • Universal primer set for the full-length amplification of all influenza a viruses
    • DOI 10.1007/s007050170002
    • Hoffmann, E., J. Stech, Y. Guan, R. G. Webster, and D. R. Perez. 2001. Universal primer set for the full-length amplification of all influenza A viruses. Arch. Virol. 146:2275-2289. (Pubitemid 34682391)
    • (2001) Archives of Virology , vol.146 , Issue.12 , pp. 2275-2289
    • Hoffmann, E.1    Stech, J.2    Guan, Y.3    Webster, R.G.4    Perez, D.R.5
  • 21
    • 34047190342 scopus 로고    scopus 로고
    • Contribution of H7 haemagglutinin to amantadine resistance and infectivity of influenza virus
    • DOI 10.1099/vir.0.82256-0
    • Ilyushina, N. A., E. A. Govorkova, C. J. Russell, E. Hoffmann, and R. G. Webster. 2007. Contribution of H7 haemagglutinin to amantadine resistance and infectivity of influenza virus. J. Gen. Virol. 88:1266-1274. (Pubitemid 46523516)
    • (2007) Journal of General Virology , vol.88 , Issue.4 , pp. 1266-1274
    • Ilyushina, N.A.1    Govorkova, E.A.2    Russell, C.J.3    Hoffmann, E.4    Webster, R.G.5
  • 24
    • 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 68:426-439.
    • (1975) Virology , vol.68 , pp. 426-439
    • Klenk, H.D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 25
    • 0033060915 scopus 로고    scopus 로고
    • Conformational intermediates and fusion activity of influenza virus hemagglutinin
    • Korte, T., K. Ludwig, F. P. Booy, R. Blumenthal, and A. Herrmann. 1999. Conformational intermediates and fusion activity of influenza virus hemagglutinin. J. Virol. 73:4567-4574. (Pubitemid 29246714)
    • (1999) Journal of Virology , vol.73 , Issue.6 , pp. 4567-4574
    • Korte, T.1    Ludwig, K.2    Booy, F.P.3    Blumenthal, R.4    Herrmann, A.5
  • 26
    • 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
  • 27
    • 0007600773 scopus 로고    scopus 로고
    • Adaptation of egg-grown and transfectant influenza viruses for growth in mammalian cells: Selection of hemagglutinin mutants with elevated pH of membrane fusion
    • Lin, Y. P., S. A. Wharton, J. Martin, J. J. Skehel, D. C. Wiley, and D. A. Steinhauer. 1997. Adaptation of egg-grown and transfectant influenza viruses for growth in mammalian cells: selection of hemagglutinin mutants with elevated pH of membrane fusion. Virology 233:402-410.
    • (1997) Virology , vol.233 , pp. 402-410
    • Lin, Y.P.1    Wharton, S.A.2    Martin, J.3    Skehel, J.J.4    Wiley, D.C.5    Steinhauer, D.A.6
  • 28
    • 33947425986 scopus 로고    scopus 로고
    • Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein
    • DOI 10.1128/JVI.02464-06
    • Luque, L. E., and C. J. Russell. 2007. Spring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein. J. Virol. 81:3130-3141. (Pubitemid 46456622)
    • (2007) Journal of Virology , vol.81 , Issue.7 , pp. 3130-3141
    • Luque, L.E.1    Russell, C.J.2
  • 29
    • 0035146799 scopus 로고    scopus 로고
    • Evolution of intermediates of influenza virus hemagglutinnin-mediated fusion revealed by kinetic measurements of pore formation
    • Markosyan, R. M., G. B. Melikyan, and F. S. Cohen. 2001. Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation. Biophys. J. 80:812-821. (Pubitemid 32128332)
    • (2001) Biophysical Journal , vol.80 , Issue.2 , pp. 812-821
    • Markosyan, R.M.1    Melikyan, G.B.2    Cohen, F.S.3
  • 30
    • 0025279843 scopus 로고
    • Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: Effects of acid pretreatment
    • Puri, A., F. P. Booy, R. W. Doms, J. M. White, and R. Blumenthal. 1990. Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatment. J. Virol. 64:3824-3832.
    • (1990) J. Virol. , vol.64 , pp. 3824-3832
    • Puri, A.1    Booy, F.P.2    Doms, R.W.3    White, J.M.4    Blumenthal, R.5
  • 31
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
    • Rogers, G. N., J. C. Paulson, R. S. Daniels, J. J. Skehel, I. A. Wilson, and D. C. Wiley. 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
  • 32
    • 0023240456 scopus 로고
    • Significance of viral glycoproteins for infectivity and pathogenicity
    • Rott, R., and H. D. Klenk. 1987. Significance of viral glycoproteins for infectivity and pathogenicity. Zentralbl. Bakteriol. Mikrobiol. Hyg. A 266:145-154.
    • (1987) Zentralbl. Bakteriol. Mikrobiol. Hyg. A , vol.266 , pp. 145-154
    • Rott, R.1    Klenk, H.D.2
  • 33
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: Activation and membrane fusion
    • Russell, C. J., K. L. Kantor, T. S. Jardetzky, and R. A. Lamb. 2003. A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion. J. Cell Biol. 163:363-374.
    • (2003) J. Cell Biol. , vol.163 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 34
    • 27544484489 scopus 로고    scopus 로고
    • The genesis of a pandemic influenza virus
    • Russell, C. J., and R. G. Webster. 2005. The genesis of a pandemic influenza virus. Cell 123:368-371.
    • (2005) Cell , vol.123 , pp. 368-371
    • Russell, C.J.1    Webster, R.G.2
  • 35
    • 3142574848 scopus 로고    scopus 로고
    • H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
    • Russell, R. J., S. J. Gamblin, L. F. Haire, D. J. Stevens, B. Xiao, Y. Ha, and J. J. Skehel. 2004. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology 325:287-296.
    • (2004) Virology , vol.325 , pp. 287-296
    • Russell, R.J.1    Gamblin, S.J.2    Haire, L.F.3    Stevens, D.J.4    Xiao, B.5    Ha, Y.6    Skehel, J.J.7
  • 37
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J. J., and D. C. Wiley. 1998. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95:871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 38
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 39
    • 0029828938 scopus 로고    scopus 로고
    • Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity
    • Steinhauer, D. A., J. Martin, Y. P. Lin, S. A. Wharton, M. B. Oldstone, J. J. Skehel, and D. C. Wiley. 1996. Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity. Proc. Natl. Acad. Sci. USA 93:12873-12878.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12873-12878
    • Steinhauer, D.A.1    Martin, J.2    Lin, Y.P.3    Wharton, S.A.4    Oldstone, M.B.5    Skehel, J.J.6    Wiley, D.C.7
  • 40
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer, D. A., S. A. Wharton, J. J. Skehel, and D. C. Wiley. 1995. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 41
    • 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, D. A., S. A. Wharton, J. J. Skehel, D. C. Wiley, and A. J. Hay. 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.
    • (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
  • 42
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens, J., O. Blixt, T. M. Tumpey, J. K. Taubenberger, J. C. Paulson, and I. A. Wilson. 2006. Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312:404-410.
    • (2006) Science , vol.312 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5    Wilson, I.A.6
  • 43
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens, J., A. L. Corper, C. F. Basler, J. K. Taubenberger, P. Palese, and I. A. Wilson. 2004. Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 303:1866-1870.
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 45
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda, M., G. P. Leser, C. J. Russell, and R. A. Lamb. 2003. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. USA 100:14610-14617.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 46
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes, S., Z. N. Li, B. J. Lee, W. A. Langley, J. J. Skehel, R. J. Russell, and D. A. Steinhauer. 2008. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1    Li, Z.N.2    Lee, B.J.3    Langley, W.A.4    Skehel, J.J.5    Russell, R.J.6    Steinhauer, D.A.7
  • 47
    • 0023666999 scopus 로고
    • Influenza virus A pathogenicity: The pivotal role of hemagglutinin
    • Webster, R. G., and R. Rott. 1987. Influenza virus A pathogenicity: the pivotal role of hemagglutinin. Cell 50:665-666.
    • (1987) Cell , vol.50 , pp. 665-666
    • Webster, R.G.1    Rott, R.2
  • 48
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • DOI 10.1038/333426a0
    • Weis, W., J. H. Brown, S. Cusack, J. C. Paulson, J. J. Skehel, and D. C. Wiley. 1988. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431. (Pubitemid 18130612)
    • (1988) Nature , vol.333 , Issue.6172 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 49
    • 0025117784 scopus 로고
    • The structure of a membrane fusion mutant of the influenza virus haemagglutinin
    • Weis, W. I., S. C. Cusack, J. H. Brown, R. S. Daniels, J. J. Skehel, and D. C. Wiley. 1990. The structure of a membrane fusion mutant of the influenza virus haemagglutinin. EMBO J. 9:17-24. (Pubitemid 20029244)
    • (1990) EMBO Journal , vol.9 , Issue.1 , pp. 17-24
    • Weis, W.I.1    Cusack, S.C.2    Brown, J.H.3    Daniels, R.S.4    Skehel, J.J.5    Wiley, D.C.6
  • 50
    • 0022657187 scopus 로고
    • Studies of influenza haemagglutinin-mediated membrane fusion
    • Wharton, S. A., J. J. Skehel, and D. C. Wiley. 1986. Studies of influenza haemagglutinin-mediated membrane fusion. Virology 149:27-35.
    • (1986) Virology , vol.149 , pp. 27-35
    • Wharton, S.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 51
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 53
    • 0021270365 scopus 로고
    • Uncoating of influenza virus in endosomes
    • Yoshimura, A., and S. Ohnishi. 1984. Uncoating of influenza virus in endosomes. J. Virol. 51:497-504. (Pubitemid 14091442)
    • (1984) Journal of Virology , vol.51 , Issue.2 , pp. 497-504
    • Yoshimura, A.1    Ohnishi, S.-I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.