메뉴 건너뛰기




Volumn 80, Issue 3, 2006, Pages 1280-1289

Palmitoylations on murine coronavirus spike proteins are essential for virion assembly and infectivity

Author keywords

[No Author keywords available]

Indexed keywords

2 BROMOPALMITIC ACID; ACYLTRANSFERASE; ACYLTRANSFERASE INHIBITOR; CYSTEINE; MEMBRANE PROTEIN; PALMITOYL ACYLTRANSFERASE; PHENYLALANINE; SERINE; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN; VIRUS SPIKE PROTEIN;

EID: 31144479683     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.3.1280-1289.2006     Document Type: Article
Times cited : (67)

References (56)
  • 1
    • 0032561327 scopus 로고    scopus 로고
    • Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues
    • Arni, S., S. A. Keilbaugh, A. G. Ostermeyer, and D. A. Brown. 1998. Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. J. Biol. Chem. 273:28478-28485.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28478-28485
    • Arni, S.1    Keilbaugh, S.A.2    Ostermeyer, A.G.3    Brown, D.A.4
  • 2
    • 0029592197 scopus 로고
    • Mutational analysis of the murine coronavirus spike protein: Effect on cell-to-cell fusion
    • Bos, E. C. W., L. Heijnen, W. Luytjes, and W. J. M. Spaan. 1995. Mutational analysis of the murine coronavirus spike protein: effect on cell-to-cell fusion, Virology 214:453-463.
    • (1995) Virology , vol.214 , pp. 453-463
    • Bos, E.C.W.1    Heijnen, L.2    Luytjes, W.3    Spaan, W.J.M.4
  • 3
    • 15144362170 scopus 로고    scopus 로고
    • Spike protein assembly into the coronavirion: Exploring the limits of its sequence requirements
    • Bosch, B. J., C. A. de Haan, S. L. Smits, and P. J. Rottier. 2005. Spike protein assembly into the coronavirion: exploring the limits of its sequence requirements. Virology 334:306-318.
    • (2005) Virology , vol.334 , pp. 306-318
    • Bosch, B.J.1    De Haan, C.A.2    Smits, S.L.3    Rottier, P.J.4
  • 4
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: Structural and functional characterization of the fusion core complex
    • Bosch, B. J., R. van der Zee, C. A. de Haan, and P. J. Rottier. 2003. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol. 77:8801-8811.
    • (2003) J. Virol. , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    Van Der Zee, R.2    De Haan, C.A.3    Rottier, P.J.4
  • 5
    • 0036195482 scopus 로고    scopus 로고
    • Structure and function of membrane rafts
    • Brown, D. 2002. Structure and function of membrane rafts. Int. J. Med. Microbiol. 291:433-437.
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 433-437
    • Brown, D.1
  • 6
    • 0002437897 scopus 로고
    • The coronavirus surface glycoprotein
    • S. G. Siddell, ed. Plenum Press, New York, N.Y.
    • Cavanagh, D. 1995. The coronavirus surface glycoprotein, p. 73-115. In S. G. Siddell, ed., The Coronaviridae. Plenum Press, New York, N.Y.
    • (1995) The Coronaviridae , pp. 73-115
    • Cavanagh, D.1
  • 7
    • 0034732109 scopus 로고    scopus 로고
    • Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein
    • Chang, K. W., Y. Sheng, and J. L. Gombold. 2000. Coronavirus-induced membrane fusion requires the cysteine-rich domain in the spike protein. Virology 269:212-224.
    • (2000) Virology , vol.269 , pp. 212-224
    • Chang, K.W.1    Sheng, Y.2    Gombold, J.L.3
  • 8
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., S. L. Pelletier, Y. I. Henis, and J. M. White. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 9
    • 0018343938 scopus 로고
    • Comparison of the morphology of three coronaviruses
    • Davies, H. A., and M. R. Macnaughton. 1979. Comparison of the morphology of three coronaviruses. Arch. Virol. 59:25-33.
    • (1979) Arch. Virol. , vol.59 , pp. 25-33
    • Davies, H.A.1    Macnaughton, M.R.2
  • 10
    • 2442680275 scopus 로고    scopus 로고
    • Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion
    • de Haan, C. A., K. Stadler, G. J. Godeke, B. J. Bosch, and P. J. Rottier. 2004. Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion. J. Virol. 78:6048-6054.
    • (2004) J. Virol. , vol.78 , pp. 6048-6054
    • De Haan, C.A.1    Stadler, K.2    Godeke, G.J.3    Bosch, B.J.4    Rottier, P.J.5
  • 11
    • 0032874344 scopus 로고    scopus 로고
    • Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein
    • de Haan, C. A. M., M. Smeets, F. Vernooij, H. Vennema, and P. J. M. Rottier. 1999. Mapping of the coronavirus membrane protein domains involved in interaction with the spike protein. J. Virol. 73:7441-7452.
    • (1999) J. Virol. , vol.73 , pp. 7441-7452
    • De Haan, C.A.M.1    Smeets, M.2    Vernooij, F.3    Vennema, H.4    Rottier, P.J.M.5
  • 12
    • 0029927840 scopus 로고    scopus 로고
    • G-protein palmitoyltransferase activity is enriched in plasma membranes
    • Dunphy, J. T., W. K. Greentree, C. L. Manahan, and M. E. Linder. 1996. G-protein palmitoyltransferase activity is enriched in plasma membranes. J. Biol. Chem. 271:7154-7159.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7154-7159
    • Dunphy, J.T.1    Greentree, W.K.2    Manahan, C.L.3    Linder, M.E.4
  • 13
    • 0023373687 scopus 로고
    • Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes
    • Fuerst, T. R., P. L. Earl, and B. Moss. 1987. Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes. Mol. Cell. Biol. 7:2538-2544.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2538-2544
    • Fuerst, T.R.1    Earl, P.L.2    Moss, B.3
  • 14
    • 0030896673 scopus 로고    scopus 로고
    • A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor
    • Gallagher, T. M. 1997. A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor. J. Virol. 71:3129-3137.
    • (1997) J. Virol. , vol.71 , pp. 3129-3137
    • Gallagher, T.M.1
  • 15
    • 0026720075 scopus 로고
    • Tight control of gene expression in mammalian cells by tetracycline-responsive promoters
    • Gossen, M., and H. Bujard. 1992. Tight control of gene expression in mammalian cells by tetracycline-responsive promoters. Proc. Natl. Acad. Sci. USA 89:5547-5551.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5547-5551
    • Gossen, M.1    Bujard, H.2
  • 16
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., P. Scheiffele, P. Verkade, and K. Simons. 1998. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141:929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 17
    • 1642540252 scopus 로고    scopus 로고
    • Virology: A class act
    • Jardetzky, T. S., and R. A. Lamb. 2004. Virology: a class act. Nature 427:307-308.
    • (2004) Nature , vol.427 , pp. 307-308
    • Jardetzky, T.S.1    Lamb, R.A.2
  • 18
    • 0030026752 scopus 로고    scopus 로고
    • Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity
    • Jin, H., K. Subbarao, S. Bagai, G. P. Leser, B. R. Murphy, and R. A. Lamb. 1996. Palmitylation of the influenza virus hemagglutinin (H3) is not essential for virus assembly or infectivity. J. Virol. 70:1406-1414.
    • (1996) J. Virol. , vol.70 , pp. 1406-1414
    • Jin, H.1    Subbarao, K.2    Bagai, S.3    Leser, G.P.4    Murphy, B.R.5    Lamb, R.A.6
  • 19
    • 0028069572 scopus 로고
    • Characterization of the budding compartment of mouse hepatitis virus: Evidence that transport from the RER to the Golgi complex requires only one vesicular transport step
    • Krijnske-Locker, J., M. Ericsson, P. J. Rottier, and G. Griffiths. 1994. Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport step. J. Cell Biol. 124:55-70.
    • (1994) J. Cell Biol. , vol.124 , pp. 55-70
    • Krijnske-Locker, J.1    Ericsson, M.2    Rottier, P.J.3    Griffiths, G.4
  • 20
    • 0035129841 scopus 로고    scopus 로고
    • Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion
    • Krueger, D. K., S. M. Kelly, D. N. Lewicki, R. Ruffolo, and T. M. Gallagher. 2001. Variations in disparate regions of the murine coronavirus spike protein impact the initiation of membrane fusion. J. Virol. 75:2792-2802.
    • (2001) J. Virol. , vol.75 , pp. 2792-2802
    • Krueger, D.K.1    Kelly, S.M.2    Lewicki, D.N.3    Ruffolo, R.4    Gallagher, T.M.5
  • 21
    • 0033982337 scopus 로고    scopus 로고
    • Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: Crossing the host cell species barrier
    • Kuo, L., G. J. Godeke, M. J. Raamsman, P. S. Masters, and P. J. Rottier. 2000. Retargeting of coronavirus by substitution of the spike glycoprotein ectodomain: crossing the host cell species barrier. J. Virol. 74:1396-1406.
    • (2000) J. Virol. , vol.74 , pp. 1396-1406
    • Kuo, L.1    Godeke, G.J.2    Raamsman, M.J.3    Masters, P.S.4    Rottier, P.J.5
  • 22
    • 0021338482 scopus 로고
    • Defective interfering particles of mouse hepatitis virus
    • Makino, S., F. Taguchi, and K. Fujiwara. 1984. Defective interfering particles of mouse hepatitis virus. Virology 133:9-17.
    • (1984) Virology , vol.133 , pp. 9-17
    • Makino, S.1    Taguchi, F.2    Fujiwara, K.3
  • 23
    • 5644298752 scopus 로고    scopus 로고
    • Coronavirus reverse genetics by targeted RNA recombination
    • Masters, P. S., and P. J. Rottier. 2005. Coronavirus reverse genetics by targeted RNA recombination. Curr. Top. Microbiol. Immunol. 287:133-159.
    • (2005) Curr. Top. Microbiol. Immunol. , vol.287 , pp. 133-159
    • Masters, P.S.1    Rottier, P.J.2
  • 24
    • 0032865424 scopus 로고    scopus 로고
    • Palmitoylation of GAP-43 by the ER-Golgi intermediate compartment and Golgi apparatus
    • McLaughlin, R. E., and J. B. Denny. 1999. Palmitoylation of GAP-43 by the ER-Golgi intermediate compartment and Golgi apparatus. Biochim. Biophys. Acta 1451:82-92.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 82-92
    • McLaughlin, R.E.1    Denny, J.B.2
  • 25
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts: Many raft proteins are acylated, while few are prenylated
    • Melkonian, K. A., A. G. Ostermeyer, J. Z. Chen, M. G. Roth, and D. A. Brown. 1999. Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts: many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274:3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 26
    • 0141856400 scopus 로고    scopus 로고
    • Enhanced virulence mediated by the murine coronavirus, mouse hepatitis virus strain JHM, is associated with a glycine at residue 310 of the spike glycoprotein
    • Ontiveros, E., T. S. Kim, T. M. Gallagher, and S. Perlman. 2003. Enhanced virulence mediated by the murine coronavirus, mouse hepatitis virus strain JHM, is associated with a glycine at residue 310 of the spike glycoprotein. J. Virol. 77:10260-10269.
    • (2003) J. Virol. , vol.77 , pp. 10260-10269
    • Ontiveros, E.1    Kim, T.S.2    Gallagher, T.M.3    Perlman, S.4
  • 27
    • 0035950592 scopus 로고    scopus 로고
    • Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS
    • Ontiveros, E., L. Kuo, P. S. Masters, and S. Perlman. 2001. Inactivation of expression of gene 4 of mouse hepatitis virus strain JHM does not affect virulence in the murine CNS. Virology 289:230-238.
    • (2001) Virology , vol.289 , pp. 230-238
    • Ontiveros, E.1    Kuo, L.2    Masters, P.S.3    Perlman, S.4
  • 29
    • 0031750728 scopus 로고    scopus 로고
    • Pathogenesis of coronavirus-induced infections
    • Perlman, S. 1998. Pathogenesis of coronavirus-induced infections. Adv. Exp. Med. Biol. 440:503-513.
    • (1998) Adv. Exp. Med. Biol. , vol.440 , pp. 503-513
    • Perlman, S.1
  • 30
    • 0344500898 scopus 로고    scopus 로고
    • Pathogenesis of chimeric MHV4/MHVA59 recombinant viruses: The murine coronavirus spike protein is a major determinant of neurovirulence
    • Phillips, J. J., M. M. Chua, E. Lavi, and S. R. Weiss. 1999. Pathogenesis of chimeric MHV4/MHVA59 recombinant viruses: the murine coronavirus spike protein is a major determinant of neurovirulence. J. Virol. 73:7752-7760.
    • (1999) J. Virol. , vol.73 , pp. 7752-7760
    • Phillips, J.J.1    Chua, M.M.2    Lavi, E.3    Weiss, S.R.4
  • 31
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle, A., P. Keller, E. L. Florin, K. Simons, and J. K. Horber. 2000. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148:997-1008.
    • (2000) J. Cell Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 32
    • 0031949315 scopus 로고    scopus 로고
    • Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections
    • Rao, P. V., and T. M. Gallagher. 1998. Intracellular complexes of viral spike and cellular receptor accumulate during cytopathic murine coronavirus infections. J. Virol. 72:3278-3288.
    • (1998) J. Virol. , vol.72 , pp. 3278-3288
    • Rao, P.V.1    Gallagher, T.M.2
  • 33
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • Resh, M. D. 2004. Membrane targeting of lipid modified signal transduction proteins. Subcell. Biochem. 37:217-232.
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 35
    • 0034610368 scopus 로고    scopus 로고
    • Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity
    • Rousso, I., M. B. Mixon, B. K. Chen, and P. S. Kim. 2000. Palmitoylation of the HIV-1 envelope glycoprotein is critical for viral infectivity. Proc. Natl. Acad. Sci. USA 97:13523-13525.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13523-13525
    • Rousso, I.1    Mixon, M.B.2    Chen, B.K.3    Kim, P.S.4
  • 36
    • 0023506740 scopus 로고
    • Characterization of a small plaque mutant of the A59 strain of mouse hepatitis virus defective in cell fusion
    • Sawicki, S. G. 1987. Characterization of a small plaque mutant of the A59 strain of mouse hepatitis virus defective in cell fusion. Adv. Exp. Med. Biol. 218:169-174.
    • (1987) Adv. Exp. Med. Biol. , vol.218 , pp. 169-174
    • Sawicki, S.G.1
  • 37
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 38
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc
    • Simmons, G., J. D. Reeves, A. J. Rennekamp, S. M. Amberg, A. J. Piefer, and P. Bates. 2004. Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc. Natl. Acad. Sci. USA 101:4240-4245.
    • (2004) Natl. Acad. Sci. USA , vol.101 , pp. 4240-4245
    • Simmons, G.1    Reeves, J.D.2    Rennekamp, A.J.3    Amberg, S.M.4    Piefer, A.J.5    Bates, P.6
  • 39
    • 0035370116 scopus 로고    scopus 로고
    • Deacylation of the transmembrane domains of Sindbis virus envelope glycoproteins E1 and E2 does not affect low-pH-induced viral membrane fusion activity
    • Smit, J. M., R. Bittman, and J. Wilschut. 2001. Deacylation of the transmembrane domains of Sindbis virus envelope glycoproteins E1 and E2 does not affect low-pH-induced viral membrane fusion activity. FEBS Lett. 498:57-61.
    • (2001) FEBS Lett. , vol.498 , pp. 57-61
    • Smit, J.M.1    Bittman, R.2    Wilschut, J.3
  • 40
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J. E., and M. E. Linder. 2004. Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 73:559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 41
    • 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., C. S. Ricard, and K. V. Holmes. 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
  • 42
    • 0015410395 scopus 로고
    • Enhanced growth of a murine coronavirus in transformed mouse cells
    • Sturman, L. S., and K. K. Takemoto. 1972. Enhanced growth of a murine coronavirus in transformed mouse cells. Infect. Immun. 6:501-507.
    • (1972) Infect. Immun. , vol.6 , pp. 501-507
    • Sturman, L.S.1    Takemoto, K.K.2
  • 43
    • 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
  • 44
    • 1542347897 scopus 로고    scopus 로고
    • Requirements for CEACAMs and cholesterol during murine coronavirus cell entry
    • Thorp, E. B., and T. M. Gallagher. 2004. Requirements for CEACAMs and cholesterol during murine coronavirus cell entry. J. Virol. 78:2682-2692.
    • (2004) J. Virol. , vol.78 , pp. 2682-2692
    • Thorp, E.B.1    Gallagher, T.M.2
  • 45
    • 0021322863 scopus 로고
    • Replication of coronavirus MHV-A59 in sac- cells: Determination of the first site of budding of progeny virions
    • Tooze, J., S. Tooze, and G. Warren. 1984. Replication of coronavirus MHV-A59 in sac- cells: determination of the first site of budding of progeny virions. Eur. J. Cell Biol. 33:281-293.
    • (1984) Eur. J. Cell Biol. , vol.33 , pp. 281-293
    • Tooze, J.1    Tooze, S.2    Warren, G.3
  • 47
    • 0036750823 scopus 로고    scopus 로고
    • A fluorescence-based high performance liquid chromatographic method for the characterization of palmitoyl acyl transferase activity
    • Varner, A. S., M. L. De Vos, S. P. Creaser, B. R. Peterson, and C. D. Smith. 2002. A fluorescence-based high performance liquid chromatographic method for the characterization of palmitoyl acyl transferase activity. Anal. Biochem. 308:160-167.
    • (2002) Anal. Biochem. , vol.308 , pp. 160-167
    • Varner, A.S.1    De Vos, M.L.2    Creaser, S.P.3    Peterson, B.R.4    Smith, C.D.5
  • 48
    • 0037431058 scopus 로고    scopus 로고
    • Biochemical characterization of the vacuolar palmitoyl acyltransferase
    • Veil, M., L. E. Dietrich, and C. Ungermann. 2003. Biochemical characterization of the vacuolar palmitoyl acyltransferase. FEBS Lett. 540:101-105.
    • (2003) FEBS Lett. , vol.540 , pp. 101-105
    • Veil, M.1    Dietrich, L.E.2    Ungermann, C.3
  • 49
    • 0029933250 scopus 로고    scopus 로고
    • Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes
    • Vennema, H., G. J. Godeke, J. W. Rossen, W. F. Voorhout, M. C. Horzinek, D. J. Opstelten, and P. J. Rottier. 1996. Nucleocapsid-independent assembly of coronavirus-like particles by co-expression of viral envelope protein genes. EMBO J. 15:2020-2028.
    • (1996) EMBO J. , vol.15 , pp. 2020-2028
    • Vennema, H.1    Godeke, G.J.2    Rossen, J.W.3    Voorhout, W.F.4    Horzinek, M.C.5    Opstelten, D.J.6    Rottier, P.J.7
  • 50
    • 18144395402 scopus 로고    scopus 로고
    • Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity
    • Wagner, R., A. Herwig, N. Azzouz, and H. D. Klenk. 2005. Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity. J. Virol. 79:6449-6458.
    • (2005) J. Virol. , vol.79 , pp. 6449-6458
    • Wagner, R.1    Herwig, A.2    Azzouz, N.3    Klenk, H.D.4
  • 51
    • 0034614557 scopus 로고    scopus 로고
    • Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids
    • Webb, V., L. Hermida-Matsumoto, and M. D. Resh. 2000. Inhibition of protein palmitoylation, raft localization, and T cell signaling by 2-bromopalmitate and polyunsaturated fatty acids. J. Biol. Chem. 275:261-270.
    • (2000) J. Biol. Chem. , vol.275 , pp. 261-270
    • Webb, V.1    Hermida-Matsumoto, L.2    Resh, M.D.3
  • 52
    • 0015623225 scopus 로고
    • Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus)
    • Weiner, L. P. 1973. Pathogenesis of demyelination induced by a mouse hepatitis virus (JHM virus). Arch. Neurol. 28:298-303.
    • (1973) Arch. Neurol. , vol.28 , pp. 298-303
    • Weiner, L.P.1
  • 53
    • 0026326156 scopus 로고
    • Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
    • Whitt, M. A., and J. K. Rose. 1991. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 185:875-878.
    • (1991) Virology , vol.185 , pp. 875-878
    • Whitt, M.A.1    Rose, J.K.2
  • 54
    • 4444301745 scopus 로고    scopus 로고
    • Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: Distinct roles for charge-rich and cysteine-rich regions of the endodomain
    • Ye, R., C. Montalto-Morrison, and P. S. Masters. 2004. Genetic analysis of determinants for spike glycoprotein assembly into murine coronavirus virions: distinct roles for charge-rich and cysteine-rich regions of the endodomain. J. Virol. 78:9904-9917.
    • (2004) J. Virol. , vol.78 , pp. 9904-9917
    • Ye, R.1    Montalto-Morrison, C.2    Masters, P.S.3
  • 55
    • 0037689221 scopus 로고    scopus 로고
    • Palmitoylation of the Autographa califormica multicapsid nucleopolyhedrovirus envelope glycoprotein GP64: Mapping, functional studies, and lipid rafts
    • Zhang, S. X., V. Han, and G. W. Blissard. 2003. Palmitoylation of the Autographa califormica multicapsid nucleopolyhedrovirus envelope glycoprotein GP64: mapping, functional studies, and lipid rafts. J. Virol. 77:6265-6273.
    • (2003) J. Virol. , vol.77 , pp. 6265-6273
    • Zhang, S.X.1    Han, V.2    Blissard, G.W.3
  • 56
    • 0028018138 scopus 로고
    • Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation
    • Zurcher, T., G. Luo, and P. Palese. 1994. Mutations at palmitylation sites of the influenza virus hemagglutinin affect virus formation. J. Virol. 68:5748-5754.
    • (1994) J. Virol. , vol.68 , pp. 5748-5754
    • Zurcher, T.1    Luo, G.2    Palese, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.