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Volumn 82, Issue 12, 2008, Pages 5986-5998

Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity

Author keywords

[No Author keywords available]

Indexed keywords

HN PROTEIN; TRYPSIN; VIRUS FUSION PROTEIN;

EID: 44949087724     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00078-08     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 0027211806 scopus 로고
    • Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Seridai virus envelope with cells
    • Bagai, S., A. Puri, R. Blumenthal, and D. P. Sarkar. 1993. Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Seridai virus envelope with cells. J. Virol. 67:3312-3318.
    • (1993) J. Virol , vol.67 , pp. 3312-3318
    • Bagai, S.1    Puri, A.2    Blumenthal, R.3    Sarkar, D.P.4
  • 2
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, K. A., R. E. Dutch, R. A. Lamb, and T. S. Jardetzky. 1999. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3:309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 3
    • 8644281996 scopus 로고    scopus 로고
    • Recombinant human metapneumovirus lacking the small hydrophobic SH and/or attachment G glycoprotein: Deletion of G yields a promising vaccine candidate
    • Biacchesi, S., M. H. Skiadopoulos, L. Yang, E. W. Lamirande, K. C. Tran, B. R. Murphy, P. L. Collins, and U. J. Buchholz. 2004. Recombinant human metapneumovirus lacking the small hydrophobic SH and/or attachment G glycoprotein: deletion of G yields a promising vaccine candidate. J. Virol. 78:12877-12887.
    • (2004) J. Virol , vol.78 , pp. 12877-12887
    • Biacchesi, S.1    Skiadopoulos, M.H.2    Yang, L.3    Lamirande, E.W.4    Tran, K.C.5    Murphy, B.R.6    Collins, P.L.7    Buchholz, U.J.8
  • 4
    • 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
  • 5
    • 34548515036 scopus 로고    scopus 로고
    • Respiratory syncytial virus and metapneumovirus
    • D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus ed, 5th ed. Lippincott Williams and Wilkins, Philadelphia, PA
    • Collins, P. L., and J. E. Crowe. 2007. Respiratory syncytial virus and metapneumovirus, p. 1601-1646. In D. M. Knipe, P. M. Howley, D. E. Griffin, R. A. Lamb, M. A. Martin, B. Roizman, and S. E. Straus (ed.), Fields virology, 5th ed. Lippincott Williams and Wilkins, Philadelphia, PA.
    • (2007) Fields virology , pp. 1601-1646
    • Collins, P.L.1    Crowe, J.E.2
  • 6
    • 33750608556 scopus 로고    scopus 로고
    • Paramyxovirus fusion: Real-time measurement of parainfluenza virus 5 virus-cell fusion
    • Connolly, S. A., and R. A. Lamb. 2007. Paramyxovirus fusion: real-time measurement of parainfluenza virus 5 virus-cell fusion. Virology 355:203-212.
    • (2007) Virology , vol.355 , pp. 203-212
    • Connolly, S.A.1    Lamb, R.A.2
  • 7
    • 33845745776 scopus 로고    scopus 로고
    • Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity
    • Crim, R. L., S. A. Audet, S. A. Feldman, H. S. Mostowski, and J. A. Beeler. 2007. Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity. J. Virol. 81:261-271.
    • (2007) J. Virol , vol.81 , pp. 261-271
    • Crim, R.L.1    Audet, S.A.2    Feldman, S.A.3    Mostowski, H.S.4    Beeler, J.A.5
  • 8
    • 0033524341 scopus 로고    scopus 로고
    • Mutations in the Newcastle disease virus hemagglutinin- neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion
    • Deng, R., Z. Wang, P. J. Mahon, M. Marinello, A. Mirza, and R. M. Iorio. 1999. Mutations in the Newcastle disease virus hemagglutinin- neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion. Virology 253:43-54.
    • (1999) Virology , vol.253 , pp. 43-54
    • Deng, R.1    Wang, Z.2    Mahon, P.J.3    Marinello, M.4    Mirza, A.5    Iorio, R.M.6
  • 9
    • 0039797301 scopus 로고
    • Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system
    • Elroy-Stein, O., T. R. Fuerst, and B. Moss. 1989. Cap-independent translation of mRNA conferred by encephalomyocarditis virus 5′ sequence improves the performance of the vaccinia virus/bacteriophage T7 hybrid expression system. Proc. Natl. Acad. Sci. USA 86:6126-6130.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 6126-6130
    • Elroy-Stein, O.1    Fuerst, T.R.2    Moss, B.3
  • 10
    • 0033918951 scopus 로고    scopus 로고
    • The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulphate
    • Feldman, S. A., S. Audet, and J. A. Beeler. 2000. The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulphate. J. Virol. 74:6442-6447.
    • (2000) J. Virol , vol.74 , pp. 6442-6447
    • Feldman, S.A.1    Audet, S.2    Beeler, J.A.3
  • 11
    • 0024505373 scopus 로고
    • Marked differences in the antigenic structure of human respiratory syncytial virus F and G glycoproteins
    • García-Barreno, B., C. Palomo, C. Peñas, T. Delgado, P. Perez-Breña, and J. A. Melero. 1989. Marked differences in the antigenic structure of human respiratory syncytial virus F and G glycoproteins. J. Virol. 63:925-932.
    • (1989) J. Virol , vol.63 , pp. 925-932
    • García-Barreno, B.1    Palomo, C.2    Peñas, C.3    Delgado, T.4    Perez-Breña, P.5    Melero, J.A.6
  • 13
    • 0028904761 scopus 로고
    • Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein
    • Heminway, B. R., Y. Yang, Y. Tanaka, M. Panin, Y. T. Huang, and M. S. Galinski. 1995. Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein. Virus Res. 36:15-35.
    • (1995) Virus Res , vol.36 , pp. 15-35
    • Heminway, B.R.1    Yang, Y.2    Tanaka, Y.3    Panin, M.4    Huang, Y.T.5    Galinski, M.S.6
  • 14
    • 0033953651 scopus 로고    scopus 로고
    • An amino acid in the heptad repeat domain 1 is important for the hemagglutinin-neuraminidase-independent fusing activity of simian virus 5 fusion protein
    • Ito, M., M. Nishio, H. Komada, Y. Ito, and M. Tsurudome. 2000. An amino acid in the heptad repeat domain 1 is important for the hemagglutinin-neuraminidase-independent fusing activity of simian virus 5 fusion protein. J. Gen. Virol. 81:719-727.
    • (2000) J. Gen. Virol , vol.81 , pp. 719-727
    • Ito, M.1    Nishio, M.2    Komada, H.3    Ito, Y.4    Tsurudome, M.5
  • 15
  • 16
    • 0033617774 scopus 로고    scopus 로고
    • Cellular proteinases trigger the infectivity of the influenza A and Sendai virus
    • Kido, H., M. Murakami, K. Oba, Y. Chen, and T. Towatari. 1999. Cellular proteinases trigger the infectivity of the influenza A and Sendai virus. Mol. Cell 9:235-244.
    • (1999) Mol. Cell , vol.9 , pp. 235-244
    • Kido, H.1    Murakami, M.2    Oba, K.3    Chen, Y.4    Towatari, T.5
  • 17
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk, H.-D., and W. Garten. 1994. Host cell proteases controlling virus pathogenicity. Trends Microbiol. 2:39-43.
    • (1994) Trends Microbiol , vol.2 , pp. 39-43
    • Klenk, H.-D.1    Garten, W.2
  • 18
    • 3342986723 scopus 로고    scopus 로고
    • A novel protein expression strategy using recombinant bovine respiratory syncytial virus (BRSV): Modifications of the peptide sequence between the two furin cleavage sites of the BRSV fusion protein yield secreted proteins, but affect processing and function of the BRSV fusion protein
    • König, P., K. Giesow, K. Schuldt, U. J. Buchholz, and G. M. Keil. 2004. A novel protein expression strategy using recombinant bovine respiratory syncytial virus (BRSV): modifications of the peptide sequence between the two furin cleavage sites of the BRSV fusion protein yield secreted proteins, but affect processing and function of the BRSV fusion protein. J. Gen. Virol. 85:1815-1824.
    • (2004) J. Gen. Virol , vol.85 , pp. 1815-1824
    • König, P.1    Giesow, K.2    Schuldt, K.3    Buchholz, U.J.4    Keil, G.M.5
  • 19
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb, R. A. 1993. Paramyxovirus fusion: a hypothesis for changes. Virology 197:1-11.
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 20
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • Lamb, R. A., R. G. Paterson, and T. S. Jardetzky. 2006. Paramyxovirus membrane fusion: lessons from the F and HN atomic structures. Virology 344:30-37.
    • (2006) Virology , vol.344 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 21
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of virus invasion: Lessons from paramyxovirus F
    • Lamb, R. A., and T. S. Jardetzky. 2007. Structural basis of virus invasion: lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 17:427-436.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 22
    • 0031744323 scopus 로고    scopus 로고
    • A proline-rich motif downstream of the receptor binding domain modulates conformation and fusogenicity of murine retroviral envelopes
    • Lavillette, D., M. Maurice, C. Roche, S. J. Russell, M. Sitbon, and F.-L. Cosset. 1998. A proline-rich motif downstream of the receptor binding domain modulates conformation and fusogenicity of murine retroviral envelopes. J. Virol. 72:9955-9965.
    • (1998) J. Virol , vol.72 , pp. 9955-9965
    • Lavillette, D.1    Maurice, M.2    Roche, C.3    Russell, S.J.4    Sitbon, M.5    Cosset, F.-L.6
  • 23
    • 0031902033 scopus 로고    scopus 로고
    • Sendai virus-like particles devoid of haemagglutinin- neuraminidase protein infect cells via the human asialoglycoprotein receptor
    • Leyrer, S., M. Bitzer, U. Lauer, J. Kramer, W. J. Neubert, and R. Sedlmeier. 1998. Sendai virus-like particles devoid of haemagglutinin- neuraminidase protein infect cells via the human asialoglycoprotein receptor. J. Gen. Virol. 79:683-687.
    • (1998) J. Gen. Virol , vol.79 , pp. 683-687
    • Leyrer, S.1    Bitzer, M.2    Lauer, U.3    Kramer, J.4    Neubert, W.J.5    Sedlmeier, R.6
  • 24
    • 33644762969 scopus 로고    scopus 로고
    • Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes
    • McGuinnes, L. W., and T. G. Morrison. 2006. Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes. J. Virol. 80:2894-2903.
    • (2006) J. Virol , vol.80 , pp. 2894-2903
    • McGuinnes, L.W.1    Morrison, T.G.2
  • 25
    • 33750897417 scopus 로고    scopus 로고
    • Melero, J. A. 2007. Molecular biology of human respiratory syncytial virus, p. 1-42. In P. A. Cane (ed.), Respiratory syncytial virus. Perspectives in medical virology, 14. Elsevier, Amsterdam, The Netherlands.
    • Melero, J. A. 2007. Molecular biology of human respiratory syncytial virus, p. 1-42. In P. A. Cane (ed.), Respiratory syncytial virus. Perspectives in medical virology, vol. 14. Elsevier, Amsterdam, The Netherlands.
  • 26
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 27
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of the paramyxovirus SV5: Destabilizing and stabilizing mutants of fusion activation
    • Paterson, R. G., C. J. Russell, and R. A. Lamb. 2000. Fusion protein of the paramyxovirus SV5: destabilizing and stabilizing mutants of fusion activation. Virology 270:17-30.
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 28
    • 0036376658 scopus 로고    scopus 로고
    • Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment
    • Ruiz-Argüello, M. B., L. González-Reyes, L. J. Calder, C. Palomo, D. Martin, M. J. Saiz, B. García-Barreno, J. J. Skehel, and J. A. Melero. 2002. Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment. Virology 298:317-326.
    • (2002) Virology , vol.298 , pp. 317-326
    • Ruiz-Argüello, M.B.1    González-Reyes, L.2    Calder, L.J.3    Palomo, C.4    Martin, D.5    Saiz, M.J.6    García-Barreno, B.7    Skehel, J.J.8    Melero, J.A.9
  • 30
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell, C. J., T. S. Jardetzky, and R. A. Lamb. 2001. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20:4024-4034.
    • (2001) EMBO J , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 31
    • 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
  • 32
    • 0015990842 scopus 로고
    • Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus
    • Scheid, A., and P. W. Choppin. 1974. Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57:475-490.
    • (1974) Virology , vol.57 , pp. 475-490
    • Scheid, A.1    Choppin, P.W.2
  • 33
    • 0036889363 scopus 로고    scopus 로고
    • Mucosal immunization with live recombinant bovine respiratory syncytial virus (BRSV) and recombinant BRSV lacking the envelope glycoprotein G protects against challenge with wild-type BRSV
    • Schmidt, U., J. Beyer, U. Polster, L. J. Gershwin, and U. J. Buchholz. 2002. Mucosal immunization with live recombinant bovine respiratory syncytial virus (BRSV) and recombinant BRSV lacking the envelope glycoprotein G protects against challenge with wild-type BRSV. J. Virol. 76:12355-12359.
    • (2002) J. Virol , vol.76 , pp. 12355-12359
    • Schmidt, U.1    Beyer, J.2    Polster, U.3    Gershwin, L.J.4    Buchholz, U.J.5
  • 34
    • 33750698660 scopus 로고    scopus 로고
    • Characterization of human metapneumovirus F protein-promoted membrane fusion: Critical roles for proteolytic processing and low pH
    • Schowalter, R. M., S. E. Smith, and R. E. Dutch. 2006. Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH. J. Virol. 80:10931-10941.
    • (2006) J. Virol , vol.80 , pp. 10931-10941
    • Schowalter, R.M.1    Smith, S.E.2    Dutch, R.E.3
  • 35
    • 0033914327 scopus 로고    scopus 로고
    • Functional analysis of the individual oligosaccharide chains of Sendai virus fusion protein
    • Segawa, H., T. Yamashita, M. Kawakita, and H. Taira. 2000. Functional analysis of the individual oligosaccharide chains of Sendai virus fusion protein. J. Biochem. 128:65-72.
    • (2000) J. Biochem , vol.128 , pp. 65-72
    • Segawa, H.1    Yamashita, T.2    Kawakita, M.3    Taira, H.4
  • 36
    • 0030761711 scopus 로고    scopus 로고
    • Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells
    • Stone-Hulslander, J., and T. G. Morrison. 1997. Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cells. J. Virol. 71:6287-6295.
    • (1997) J. Virol , vol.71 , pp. 6287-6295
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 37
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi, K., and R. W. Compans. 1996. Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion. J. Virol. 70:6112-6118.
    • (1996) J. Virol , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 38
    • 0034947770 scopus 로고    scopus 로고
    • Functional analysis of recombinant respiratory syncytial virus deletion mutants lacking the small hydrophobic and/or attachment glycoprotein gene
    • Techaarpornkul, S., N. Barretto, and M. E. Peeples. 2001. Functional analysis of recombinant respiratory syncytial virus deletion mutants lacking the small hydrophobic and/or attachment glycoprotein gene. J. Virol. 75:6825-6834.
    • (2001) J. Virol , vol.75 , pp. 6825-6834
    • Techaarpornkul, S.1    Barretto, N.2    Peeples, M.E.3
  • 39
    • 0036060278 scopus 로고    scopus 로고
    • Respiratory syncytial virus with the fusion protein as its only viral glycoprotein is less dependent on cellular glycosaminoglycans for attachment than complete virus
    • Techaarpornkul, S., P. L. Collins, and M. E. Peeples. 2002. Respiratory syncytial virus with the fusion protein as its only viral glycoprotein is less dependent on cellular glycosaminoglycans for attachment than complete virus. Virology 294:296-304.
    • (2002) Virology , vol.294 , pp. 296-304
    • Techaarpornkul, S.1    Collins, P.L.2    Peeples, M.E.3
  • 40
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. 2002. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3:753-766.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 41
    • 0034853335 scopus 로고    scopus 로고
    • Hemagglutinin-neuraminidase-independent fusion activity of Simian Virus 5 fusion (F) protein: Difference in conformation between fusogenic and non-fusogenic F proteins on the cell surface
    • Tsurudome, M., M. Ito, M. Nishio, M. Kawano, H. Komada, and Y. Ito. 2001. Hemagglutinin-neuraminidase-independent fusion activity of Simian Virus 5 fusion (F) protein: difference in conformation between fusogenic and non-fusogenic F proteins on the cell surface. J. Virol. 75:8999-9009.
    • (2001) J. Virol , vol.75 , pp. 8999-9009
    • Tsurudome, M.1    Ito, M.2    Nishio, M.3    Kawano, M.4    Komada, H.5    Ito, Y.6
  • 43
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin, H. S., X. Wen, R. G. Paterson, R. A. Lamb, and T. S. Jardetzky. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 44
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao, X., M. Singh, V. N. Malashkevich, and P. S. Kim. 2000. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl. Acad. Sci. USA 97:14172-14177.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 45
    • 0035943659 scopus 로고    scopus 로고
    • Proteolytic activation of respiratory syncytial virus fusion protein
    • Zimmer, G., L. Budz, and G. Herrler. 2001. Proteolytic activation of respiratory syncytial virus fusion protein. J. Biol. Chem. 276:31642-31650.
    • (2001) J. Biol. Chem , vol.276 , pp. 31642-31650
    • Zimmer, G.1    Budz, L.2    Herrler, G.3
  • 46
    • 0035037076 scopus 로고    scopus 로고
    • N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus
    • Zimmer, G., I. Trotz, and G. Herrler. 2001. N-glycans of F protein differentially affect fusion activity of human respiratory syncytial virus. J. Virol. 75:4744-4751.
    • (2001) J. Virol , vol.75 , pp. 4744-4751
    • Zimmer, G.1    Trotz, I.2    Herrler, G.3
  • 47
    • 0036721195 scopus 로고    scopus 로고
    • 109 and presence of the intervening peptide of the respiratory syncytial virus fusion protein are dispensable for virus replication in cell culture
    • 109 and presence of the intervening peptide of the respiratory syncytial virus fusion protein are dispensable for virus replication in cell culture. J. Virol. 76:9218-9224.
    • (2002) J. Virol , vol.76 , pp. 9218-9224
    • Zimmer, G.1    Conzelmann, K.K.2    Herrler, G.3
  • 48
    • 0344443709 scopus 로고    scopus 로고
    • Virokinin, a bioactive peptide of the tachykinin family, is released from the fusion protein of bovine respiratory syncytial virus
    • Zimmer, G., M. Rohn, G. P. McGregor, M. Schemann, K. K. Conzelman, and G. Herrler. 2003. Virokinin, a bioactive peptide of the tachykinin family, is released from the fusion protein of bovine respiratory syncytial virus. J. Biol. Chem. 278:46854-46861.
    • (2003) J. Biol. Chem , vol.278 , pp. 46854-46861
    • Zimmer, G.1    Rohn, M.2    McGregor, G.P.3    Schemann, M.4    Conzelman, K.K.5    Herrler, G.6


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