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Volumn 214, Issue 2, 1995, Pages 453-463

Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0029592197     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1995.0056     Document Type: Article
Times cited : (81)

References (49)
  • 1
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • Barr, P. J. (1991). Mammalian subtilisins: The long-sought dibasic processing endoproteases. Cell 66, 1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 2
    • 0024322074 scopus 로고
    • Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasma-tic reticulum
    • Bonatti, S., Migliaccio, G., and Simons, K. (1989). Palmitylation of viral membrane glycoproteins takes place after exit from the endoplasma-tic reticulum. J. Biol. Chem. 264, 12590-12595.
    • (1989) J. Biol. Chem , vol.264 , pp. 12590-12595
    • Bonatti, S.1    Migliaccio, G.2    Simons, K.3
  • 3
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • Boyd, D., and Beckwith, J. (1990). The role of charged amino acids in the localization of secreted and membrane proteins. Cell 62, 1031-1033.
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyd, D.1    Beckwith, J.2
  • 4
    • 0021021580 scopus 로고
    • Coronavirus IBV: Structural characterization of IBV glycoproteins
    • Cavanagh, D. (1983). Coronavirus IBV: Structural characterization of IBV glycoproteins. J. Gen. Virol. 64, 2577-2583.
    • (1983) J. Gen. Virol , vol.64 , pp. 2577-2583
    • Cavanagh, D.1
  • 5
    • 0024828496 scopus 로고
    • Mutation of host cell determinants which discriminate between lytic and persistent mouse hepatitis virus infection results in a fusion-resistant phenotype
    • Daya, M., Wong, F., Cervin, M., Evans, G., Vennema, H., Spaan, W., and Anderson, R. (1989). Mutation of host cell determinants which discriminate between lytic and persistent mouse hepatitis virus infection results in a fusion-resistant phenotype. J. Gen. Virol. 70, 3335-3346.
    • (1989) J. Gen. Virol , vol.70 , pp. 3335-3346
    • Daya, M.1    Wong, F.2    Cervin, M.3    Evans, G.4    Vennema, H.5    Spaan, W.6    Anderson, R.7
  • 7
    • 0025103827 scopus 로고
    • Assembly of coronavirus spike protein into trimers and its role in epitope expression
    • Delmas, B., and Laude, H. (1990). Assembly of coronavirus spike protein into trimers and its role in epitope expression. J. Virol. 64, 5367-5375.
    • (1990) J. Virol , vol.64 , pp. 5367-5375
    • Delmas, B.1    Laude, H.2
  • 8
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms, R. W., Lamb, R. A., Rose, J. K., and Helenius, A. (1993). Folding and assembly of viral membrane proteins. Virology 193, 545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 9
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
    • Dubay, J. W., Roberts, S. J., Hahn, B. H., and Hunter, E. (1992). Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity. J. Virol. 66, 6616-6625.
    • (1992) J. Virol , vol.66 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 10
    • 0021080239 scopus 로고
    • Antigenic relationships of murine coronaviruses: Analysis using monoclonal antibodies to JHM (MHV-4) virus
    • Fleming, J. O., Stohlman, S. A., Harmon, R. C., Lai, M. M., Frelinger, J. A., and Weiner, L. P. (1983). Antigenic relationships of murine coronaviruses: analysis using monoclonal antibodies to JHM (MHV-4) virus. Virology 131, 296-307.
    • (1983) Virology , vol.131 , pp. 296-307
    • Fleming, J.O.1    Stohlman, S.A.2    Harmon, R.C.3    Lai, M.M.4    Frelinger, J.A.5    Weiner, L.P.6
  • 11
    • 0022399775 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion
    • Frana, M. F., Behnke, J. N., Sturman, L. S., and Holmes, K. V. (1985). Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Host-dependent differences in proteolytic cleavage and cell fusion. J. Virol. 56, 912-920.
    • (1985) J. Virol , vol.56 , pp. 912-920
    • Frana, M.F.1    Behnke, J.N.2    Sturman, L.S.3    Holmes, K.V.4
  • 12
    • 0026088715 scopus 로고
    • Alteration of the pH dependence of coronavirus-induced cell fusion: Effect of mutations in the spike glycoprotein
    • Gallagher, T. M., Escarmis, C., and Buchmeier, M. J. (1991). Alteration of the pH dependence of coronavirus-induced cell fusion: effect of mutations in the spike glycoprotein. J. Virol. 65, 1916-1928.
    • (1991) J. Virol , vol.65 , pp. 1916-1928
    • Gallagher, T.M.1    Escarmis, C.2    Buchmeier, M.J.3
  • 13
    • 0023202341 scopus 로고
    • Characterization of the structural proteins of the murine coronavirus strain A59 using monoclonal antibodies
    • Gilmore, W., Fleming, J. O., Stohlman, S. A., and Weiner, L. P. (1987). Characterization of the structural proteins of the murine coronavirus strain A59 using monoclonal antibodies. Proc. Natl. Acad. Sci. USA 185, 177-186.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.185 , pp. 177-186
    • Gilmore, W.1    Fleming, J.O.2    Stohlman, S.A.3    Weiner, L.P.4
  • 14
    • 0027313117 scopus 로고
    • Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal
    • Gombold, J. L., Hingley, S. T., and Weiss, S. R. (1993). Fusion-defective mutants of mouse hepatitis virus A59 contain a mutation in the spike protein cleavage signal. J. Virol. 67, 4504-4512.
    • (1993) J. Virol , vol.67 , pp. 4504-4512
    • Gombold, J.L.1    Hingley, S.T.2    Weiss, S.R.3
  • 15
    • 0028133455 scopus 로고
    • Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody
    • Grosse, B., and Siddell, S. G. (1994). Single amino acid changes in the S2 subunit of the MHV surface glycoprotein confer resistance to neutralization by S1 subunit-specific monoclonal antibody. Virology 202, 814-824.
    • (1994) Virology , vol.202 , pp. 814-824
    • Grosse, B.1    Siddell, S.G.2
  • 16
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond, C., Braakman, I., and Helenius, A. (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 17
    • 0023736676 scopus 로고
    • Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalian cells
    • Kawaoka, Y., and Webster, R. G. (1988). Sequence requirements for cleavage activation of influenza virus hemagglutinin expressed in mammalian cells. Proc. Natl. Acad. Sci. USA 85, 324-328.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 324-328
    • Kawaoka, Y.1    Webster, R.G.2
  • 18
    • 0023613953 scopus 로고
    • Rapid and efficient site-directed mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D., and Zakour, R. (1987). Rapid and efficient site-directed mutagenesis without phenotypic selection. Methods En-zymol. 154, 367-382.
    • (1987) Methods En-Zymol , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0022467016 scopus 로고
    • Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids
    • Lambrecht, B., and Schmidt, M. F. G. (1986). Membrane fusion induced by influenza virus hemagglutinin requires protein bound fatty acids. FEBS Lett. 202, 127-132.
    • (1986) FEBS Lett , vol.202 , pp. 127-132
    • Lambrecht, B.1    Schmidt, M.F.G.2
  • 21
    • 0023476246 scopus 로고
    • Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site
    • Luytjes, W., Sturman, L. S., Bredenbeek, P. J., Charite, J., van der Zeijst, A. M., Horzinek, M. C., and Spaan, W. J. M. (1987). Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site. Virology 161, 479-487.
    • (1987) Virology , vol.161 , pp. 479-487
    • Luytjes, W.1    Sturman, L.S.2    Bredenbeek, P.J.3    Charite, J.4    Van Der Zeijst, A.M.5    Horzinek, M.C.6    Spaan, W.J.M.7
  • 22
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • Marquardt, T., and Helenius, A. (1992). Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell. Biol. 117, 505-513.
    • (1992) J. Cell. Biol , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 23
    • 0020516226 scopus 로고
    • Fusion resistance and decreased infectability as major host cell determinants of coronavirus persistence
    • Mizzen, L., Cheley, S., Rao, M., Wolf, R., and Anderson, R. (1983). Fusion resistance and decreased infectability as major host cell determinants of coronavirus persistence. Virology 128, 407-417.
    • (1983) Virology , vol.128 , pp. 407-417
    • Mizzen, L.1    Cheley, S.2    Rao, M.3    Wolf, R.4    Anderson, R.5
  • 24
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., Bresnahan, P. A., Leppla, S. H., Klimpel, K. R., and Thomas, G. (1992). Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 26796, 16396-16402.
    • (1992) J. Biol. Chem , vol.2679 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 25
    • 0026725456 scopus 로고
    • Cytoplasmic domain truncation enhances fusion activity by the exterior glycoprotein complex of human immunodeficiency virus type 2 in selected cell types
    • Mulligan, M. J., Yamshchikov, G. V., Ritter, G. D., Gao, F., Jin, M. J., Nail, D., Spies, C. P., Hahn, B. H., and Compans, R. W. (1992). Cytoplasmic domain truncation enhances fusion activity by the exterior glycoprotein complex of human immunodeficiency virus type 2 in selected cell types. J. Virol. 66, 3971-3975.
    • (1992) J. Virol , vol.66 , pp. 3971-3975
    • Mulligan, M.J.1    Yamshchikov, G.V.2    Ritter, G.D.3    Gao, F.4    Jin, M.J.5    Nail, D.6    Spies, C.P.7    Hahn, B.H.8    Compans, R.W.9
  • 26
    • 0025053668 scopus 로고
    • Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion
    • Naeve, C. W., and Williams, D. (1990). Fatty acids on the A/Japan/305/57 influenza virus hemagglutinin have a role in membrane fusion. EMBO J. 9, 3857-3866.
    • (1990) EMBO J , vol.9 , pp. 3857-3866
    • Naeve, C.W.1    Williams, D.2
  • 27
    • 0019833716 scopus 로고
    • Coronavirus glycoprotein E1, a new type of viral glycoprotein
    • Niemann, H., and Klenk, H.-D. (1981). Coronavirus glycoprotein E1, a new type of viral glycoprotein. J. Mol. Biol. 153, 993-1010.
    • (1981) J. Mol. Biol , vol.153 , pp. 993-1010
    • Niemann, H.1    Klenk, H.-D.2
  • 28
    • 0028012576 scopus 로고
    • Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity
    • Owens, R. J., Burke, C., and Rose, J. K. (1994). Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity. J. Virol. 68, 570-574.
    • (1994) J. Virol , vol.68 , pp. 570-574
    • Owens, R.J.1    Burke, C.2    Rose, J.K.3
  • 29
    • 0024512971 scopus 로고
    • Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide
    • Paterson, R. G., Shaughnessy, M. A., and Lamb, R. A. (1989). Analysis of the relationship between cleavability of a paramyxovirus fusion protein and length of the connecting peptide. J. Virol. 63, 1293-1301.
    • (1989) J. Virol , vol.63 , pp. 1293-1301
    • Paterson, R.G.1    Shaughnessy, M.A.2    Lamb, R.A.3
  • 30
    • 0028180109 scopus 로고
    • Uncoupled expression of moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry
    • Ragheb, J. A., and Anderson, W. F. (1994). Uncoupled expression of moloney murine leukemia virus envelope polypeptides SU and TM: A functional analysis of the role of TM domains in viral entry. J. Virol. 68, 3207-3219.
    • (1994) J. Virol , vol.68 , pp. 3207-3219
    • Ragheb, J.A.1    Anderson, W.F.2
  • 31
    • 0027244528 scopus 로고
    • Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring
    • Rasile, L., Ghosh, K., Raviprakash, K., and Ghosh, H. P. (1993). Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring. J. Virol. 67, 4856-4866.
    • (1993) J. Virol , vol.67 , pp. 4856-4866
    • Rasile, L.1    Ghosh, K.2    Raviprakash, K.3    Ghosh, H.P.4
  • 32
    • 0021890935 scopus 로고
    • Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite highperformance liquid chromatography
    • Ricard, C. S., and Sturman, L. S. (1985). Isolation of the subunits of the coronavirus envelope glycoprotein E2 by hydroxyapatite highperformance liquid chromatography. J. Chromatogr. 326, 191-197.
    • (1985) J. Chromatogr , vol.326 , pp. 191-197
    • Ricard, C.S.1    Sturman, L.S.2
  • 33
    • 0023188263 scopus 로고
    • The covalent modification of eukaryotic proteins with lipid
    • Sefton, B. M., and Buss, J. E. (1987). The covalent modification of eukaryotic proteins with lipid. J. Cell Biol. 104, 1449-1453.
    • (1987) J. Cell Biol , vol.104 , pp. 1449-1453
    • Sefton, B.M.1    Buss, J.E.2
  • 34
    • 0020077726 scopus 로고
    • Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses
    • Schmidt, M. F. G. (1982). Acylation of viral spike glycoproteins: A feature of enveloped RNA viruses. Virology 116, 327-338.
    • (1982) Virology , vol.116 , pp. 327-338
    • Schmidt, M.F.G.1
  • 35
    • 0024226792 scopus 로고
    • Coronaviruses: Structure and genome expression
    • Spaan, W., Cavanagh, D., and Horzinek, M. C. (1988). Coronaviruses: Structure and genome expression. J. Gen. Virol. 69, 2939-2952.
    • (1988) J. Gen. Virol , vol.69 , pp. 2939-2952
    • Spaan, W.1    Cavanagh, D.2    Horzinek, M.C.3
  • 36
    • 0027408895 scopus 로고
    • Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity
    • Stauber, R., Pfleiderera, M., and Siddell, S. (1993). Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity. J. Gen. Virol. 74, 183-191.
    • (1993) J. Gen. Virol , vol.74 , pp. 183-191
    • Stauber, R.1    Pfleiderera, M.2    Siddell, S.3
  • 37
    • 0025882934 scopus 로고
    • Deacylation of the Hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • Steinhauer, D. A., Wharton, S. A., Wiley, D. C., and Skehel, J. J. (1991). Deacylation of the Hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties. Virology 184, 445-448.
    • (1991) Virology , vol.184 , pp. 445-448
    • Steinhauer, D.A.1    Wharton, S.A.2    Wiley, D.C.3    Skehel, J.J.4
  • 38
    • 0011246270 scopus 로고
    • The novel glycoproteins of coronaviruses
    • Sturman, L. S., and Holmes, K. V. (1985). The novel glycoproteins of coronaviruses. Trends Biochem. Sci. 10, 17-20.
    • (1985) Trends Biochem. Sci , vol.10 , pp. 17-20
    • Sturman, L.S.1    Holmes, K.V.2
  • 39
    • 0022397327 scopus 로고
    • Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: Activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments
    • Sturman, L. S., Ricard, C. S., and Holmes, K. V. (1985). Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusing activity of virions by trypsin and separation of two different 90K cleavage fragments. J. Virol. 56, 904-911.
    • (1985) J. Virol , vol.56 , pp. 904-911
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 40
    • 0025354474 scopus 로고
    • Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion
    • Sturman, L. S., Ricard, C. S., and Holmes, K. V. (1990). Conformational change of the coronavirus peplomer glycoprotein at pH 8.0 and 37°C correlates with virus aggregation and virus-induced cell fusion. J. Virol. 64, 3042-3050.
    • (1990) J. Virol , vol.64 , pp. 3042-3050
    • Sturman, L.S.1    Ricard, C.S.2    Holmes, K.V.3
  • 41
    • 0027536888 scopus 로고
    • Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2
    • Taguchi, F. (1993). Fusion formation by the uncleaved spike protein of murine coronavirus JHMV variant cl-2. J. Virol. 67, 1195-1202.
    • (1993) J. Virol , vol.67 , pp. 1195-1202
    • Taguchi, F.1
  • 42
    • 0023193669 scopus 로고
    • Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells: Brief report
    • van Berlo, M. F., van den Brink, W. J., Horzinek, M. C., and van der Zeijst, B. A. M. (1987). Fatty acid acylation of viral proteins in murine hepatitis virus-infected cells: Brief report. Arch. Virol. 95, 123-128.
    • (1987) Arch. Virol , vol.95 , pp. 123-128
    • Van Berlo, M.F.1    Van Den Brink, W.J.2    Horzinek, M.C.3    Van Der Zeijst, B.A.M.4
  • 43
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • Veit, M., Kretzschmar, E., Kuroda, K., Garten, W., Schmidt, M. F. G., Klenk, H.-D., and Rott, R. (1991). Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin. J. Virol. 65, 2491-2500.
    • (1991) J. Virol , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmidt, M.F.G.5    Klenk, H.-D.6    Rott, R.7
  • 44
    • 0025169833 scopus 로고
    • Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly
    • Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M. C., and Spaan, W. J. M. (1990). Intracellular transport of recombinant coronavirus spike proteins: Implications for virus assembly. J. Virol. 64, 339-346.
    • (1990) J. Virol , vol.64 , pp. 339-346
    • Vennema, H.1    Heijnen, L.2    Zijderveld, A.3    Horzinek, M.C.4    Spaan, W.J.M.5
  • 45
    • 0025790535 scopus 로고
    • Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system with encephalomyocarditis virus 5' untranslated region sequences
    • Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M. C., and Spaan, W. J. M. (1991). Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system with encephalomyocarditis virus 5' untranslated region sequences. Gene 108, 201-210.
    • (1991) Gene , vol.108 , pp. 201-210
    • Vennema, H.1    Rijnbrand, R.2    Heijnen, L.3    Horzinek, M.C.4    Spaan, W.J.M.5
  • 46
    • 0026748702 scopus 로고
    • Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R
    • Vey, M., Orlich, M., Adler, S., Klenk, H.-D., Rott, R., and Garten, W. (1992). Hemagglutinin activation of pathogenic avian influenza viruses of serotype H7 requires the protease recognition motif R-X-K/R-R. Virology 188, 408-413.
    • (1992) Virology , vol.188 , pp. 408-413
    • Vey, M.1    Orlich, M.2    Adler, S.3    Klenk, H.-D.4    Rott, R.5    Garten, W.6
  • 48
    • 0025375789 scopus 로고
    • Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify 2 subunits and detect a conformational change in the subunit released under mild alkaline conditions
    • Weismiller, D. G., Sturman, L. S., Buchmeier, M. J., Fleming, J. O., and Holmes, K. V. (1990). Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify 2 subunits and detect a conformational change in the subunit released under mild alkaline conditions. J. Virol. 64, 3051-3055.
    • (1990) J. Virol , vol.64 , pp. 3051-3055
    • Weismiller, D.G.1    Sturman, L.S.2    Buchmeier, M.J.3    Fleming, J.O.4    Holmes, K.V.5
  • 49
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. M. (1990). Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52, 675-679.
    • (1990) Annu. Rev. Physiol , vol.52 , pp. 675-679
    • White, J.M.1


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