메뉴 건너뛰기




Volumn 82, Issue 6, 2008, Pages 2883-2894

Aromatic amino acids in the juxtamembrane domain of severe acute respiratory syndrome coronavirus spike glycoprotein are important for receptor-dependent virus entry and cell-cell fusion

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ANGIOTENSIN CONVERTING ENZYME 2; AROMATIC AMINO ACID; TRYPSIN; VIRUS SPIKE PROTEIN;

EID: 40149103631     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01805-07     Document Type: Article
Times cited : (35)

References (59)
  • 2
    • 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
  • 3
    • 31144434388 scopus 로고    scopus 로고
    • Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry
    • Broer, R., B. Boson, W. Spaan, F. L. Cosset, and J. Corver. 2006. Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry. J. Virol. 80:1302-1310.
    • (2006) J. Virol , vol.80 , pp. 1302-1310
    • Broer, R.1    Boson, B.2    Spaan, W.3    Cosset, F.L.4    Corver, J.5
  • 4
    • 0031585552 scopus 로고    scopus 로고
    • Host range and cytopathogenicity of the highly attenuated MVA strain of vaccinia virus: Propagation and generation of recombinant viruses in a nonhuman mammalian cell line
    • Carroll, M. W., and B. Moss. 1997. Host range and cytopathogenicity of the highly attenuated MVA strain of vaccinia virus: propagation and generation of recombinant viruses in a nonhuman mammalian cell line. Virology 238: 198-211.
    • (1997) Virology , vol.238 , pp. 198-211
    • Carroll, M.W.1    Moss, B.2
  • 5
    • 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
  • 6
    • 0030782261 scopus 로고    scopus 로고
    • Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex
    • Cluett, E. B., E. Kuismanen, and C. E. Machamer. 1997. Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex. Mol. Biol. Cell 8:2233-2240.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2233-2240
    • Cluett, E.B.1    Kuismanen, E.2    Machamer, C.E.3
  • 7
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman, P. M., and M. C. Lawrence. 2003. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell Biol. 4:309-319.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 8
    • 23844555503 scopus 로고    scopus 로고
    • The nipah virus fusion protein is cleaved within the endosomal compartment
    • Diederich, S., M. Moll, H. D. Klenk, and A. Maisner. 2005. The nipah virus fusion protein is cleaved within the endosomal compartment. J. Biol. Chem. 280:29899-29903.
    • (2005) J. Biol. Chem , vol.280 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.D.3    Maisner, A.4
  • 10
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: Biological machines that undergo a metamorphosis
    • Dutch, R. E., T. S. Jardetzky, and R. A. Lamb. 2000. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci. Rep. 20:597-612.
    • (2000) Biosci. Rep , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 12
    • 33745282653 scopus 로고    scopus 로고
    • Furin cleavage of the SARS Coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry
    • Follis, K. E., J. York, and J. H. Nunberg. 2006. Furin cleavage of the SARS Coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry. Virology 350:358-369.
    • (2006) Virology , vol.350 , pp. 358-369
    • Follis, K.E.1    York, J.2    Nunberg, J.H.3
  • 13
    • 1942456669 scopus 로고    scopus 로고
    • Dissection of seroreactivity against the tryptophan-rich motif of the feline immunodeficiency virus transmembrane glycoprotein
    • Freer, G., S. Giannecchini, A. Tissot, M. F. Bachmann, P. Rovero, P. F. Serres, and M. Bendinelli. 2004. Dissection of seroreactivity against the tryptophan-rich motif of the feline immunodeficiency virus transmembrane glycoprotein. Virology 322:360-369.
    • (2004) Virology , vol.322 , pp. 360-369
    • Freer, G.1    Giannecchini, S.2    Tissot, A.3    Bachmann, M.F.4    Rovero, P.5    Serres, P.F.6    Bendinelli, M.7
  • 15
    • 24044441008 scopus 로고    scopus 로고
    • Feline immunodeficiency virus plasma load reduction by a retroinverso octapeptide reproducing the Trp-rich motif of the transmembrane glycoprotein
    • Giannecchini, S., M. C. Alcaro, P. Isola, O. Sichi, M. Pistello, A. M. Papini, P. Rovero, and M. Bendinelli. 2005. Feline immunodeficiency virus plasma load reduction by a retroinverso octapeptide reproducing the Trp-rich motif of the transmembrane glycoprotein. Antivir. Ther. 10:671-680.
    • (2005) Antivir. Ther , vol.10 , pp. 671-680
    • Giannecchini, S.1    Alcaro, M.C.2    Isola, P.3    Sichi, O.4    Pistello, M.5    Papini, A.M.6    Rovero, P.7    Bendinelli, M.8
  • 16
    • 1542300886 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region in the transmembrane glycoprotein ectodomain of feline immunodeficiency virus is important for cell entry
    • Giannecchini, S., F. Bonci, M. Pistello, D. Matteucci, O. Sichi, P. Rovero, and M. Bendinelli. 2004. The membrane-proximal tryptophan-rich region in the transmembrane glycoprotein ectodomain of feline immunodeficiency virus is important for cell entry. Virology 320:156-166.
    • (2004) Virology , vol.320 , pp. 156-166
    • Giannecchini, S.1    Bonci, F.2    Pistello, M.3    Matteucci, D.4    Sichi, O.5    Rovero, P.6    Bendinelli, M.7
  • 17
  • 18
    • 13744249901 scopus 로고    scopus 로고
    • Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: Implications for the viral fusion mechanism
    • Guillen, J., A. J. Perez-Berna, M. R. Moreno, and J. Villalain. 2005. Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: implications for the viral fusion mechanism. J. Virol. 79:1743-1752.
    • (2005) J. Virol , vol.79 , pp. 1743-1752
    • Guillen, J.1    Perez-Berna, A.J.2    Moreno, M.R.3    Villalain, J.4
  • 20
    • 0242409119 scopus 로고    scopus 로고
    • The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity
    • Jeetendra, E., K. Ghosh, D. Odell, J. Li, H. P. Ghosh, and M. A. Whitt. 2003. The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity. J. Virol. 77:12807-12818.
    • (2003) J. Virol , vol.77 , pp. 12807-12818
    • Jeetendra, E.1    Ghosh, K.2    Odell, D.3    Li, J.4    Ghosh, H.P.5    Whitt, M.A.6
  • 21
    • 0036889342 scopus 로고    scopus 로고
    • The membrane-proximal domain of vesicular stomatitis virus G protein functions as a membrane fusion potentiator and can induce hemifusion
    • Jeetendra, E., C. S. Robison, L. M. Albritton, and M. A. Whitt. 2002. The membrane-proximal domain of vesicular stomatitis virus G protein functions as a membrane fusion potentiator and can induce hemifusion. J. Virol. 76:12300-12311.
    • (2002) J. Virol , vol.76 , pp. 12300-12311
    • Jeetendra, E.1    Robison, C.S.2    Albritton, L.M.3    Whitt, M.A.4
  • 22
    • 0027191913 scopus 로고
    • Truncations of the simian immunodeficiency virus transmembrane protein confer expanded virus host range by removing a block to virus entry into cells
    • Johnston, P. B., J. W. Dubay, and E. Hunter. 1993. Truncations of the simian immunodeficiency virus transmembrane protein confer expanded virus host range by removing a block to virus entry into cells. J. Virol. 67:3077-3086.
    • (1993) J. Virol , vol.67 , pp. 3077-3086
    • Johnston, P.B.1    Dubay, J.W.2    Hunter, E.3
  • 23
    • 0034284386 scopus 로고    scopus 로고
    • How proteins adapt to a membrane-water interface
    • Killian, J. A., and G. von Heijne. 2000. How proteins adapt to a membrane-water interface. Trends Biochem. Sci. 25:429-434.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 429-434
    • Killian, J.A.1    von Heijne, G.2
  • 24
    • 0037205452 scopus 로고    scopus 로고
    • Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors
    • Lewicki, D. N., and T. M. Gallagher. 2002. Quaternary structure of coronavirus spikes in complex with carcinoembryonic antigen-related cell adhesion molecule cellular receptors. J. Biol. Chem. 277:19727-19734.
    • (2002) J. Biol. Chem , vol.277 , pp. 19727-19734
    • Lewicki, D.N.1    Gallagher, T.M.2
  • 25
    • 33745794872 scopus 로고    scopus 로고
    • Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain
    • Li, F., M. Berardi, W. Li, M. Farzan, P. R. Dormitzer, and S. C. Harrison. 2006. Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain. J. Virol. 80:6794-6800.
    • (2006) J. Virol , vol.80 , pp. 6794-6800
    • Li, F.1    Berardi, M.2    Li, W.3    Farzan, M.4    Dormitzer, P.R.5    Harrison, S.C.6
  • 27
    • 12144287276 scopus 로고    scopus 로고
    • Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: Implications for virus fusogenic mechanism and identification of fusion inhibitors
    • Liu, S., G. Xiao, Y. Chen, Y. He, J. Niu, C. R. Escalante, H. Xiong, J. Farmar, A. K. Debnath, P. Tien, and S. Jiang. 2004. Interaction between heptad repeat 1 and 2 regions in spike protein of SARS-associated coronavirus: implications for virus fusogenic mechanism and identification of fusion inhibitors. Lancet 363:938-947.
    • (2004) Lancet , vol.363 , pp. 938-947
    • Liu, S.1    Xiao, G.2    Chen, Y.3    He, Y.4    Niu, J.5    Escalante, C.R.6    Xiong, H.7    Farmar, J.8    Debnath, A.K.9    Tien, P.10    Jiang, S.11
  • 28
    • 2442647673 scopus 로고    scopus 로고
    • Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site
    • Lontok, E., E. Corse, and C. E. Machamer. 2004. Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site. J. Virol. 78:5913-5922.
    • (2004) J. Virol , vol.78 , pp. 5913-5922
    • Lontok, E.1    Corse, E.2    Machamer, C.E.3
  • 29
    • 33845987097 scopus 로고    scopus 로고
    • Recognition and blocking of HIV-1 gp41 pre-transmembrane sequence by monoclonal 4E10 antibody in a Raft-like membrane environment
    • Lorizate, M., A. Cruz, N. Huarte, R. Kunert, J. Perez-Gil, and J. L. Nieva. 2006. Recognition and blocking of HIV-1 gp41 pre-transmembrane sequence by monoclonal 4E10 antibody in a Raft-like membrane environment. J. Biol. Chem. 281:39598-39606.
    • (2006) J. Biol. Chem , vol.281 , pp. 39598-39606
    • Lorizate, M.1    Cruz, A.2    Huarte, N.3    Kunert, R.4    Perez-Gil, J.5    Nieva, J.L.6
  • 30
    • 0141789697 scopus 로고    scopus 로고
    • Role of the mutation Q252R in activating membrane fusion in the murine leukemia virus surface envelope protein
    • Lu, C. W., and M. J. Roth. 2003. Role of the mutation Q252R in activating membrane fusion in the murine leukemia virus surface envelope protein. J. Virol. 77:10841-10849.
    • (2003) J. Virol , vol.77 , pp. 10841-10849
    • Lu, C.W.1    Roth, M.J.2
  • 31
    • 0036889416 scopus 로고    scopus 로고
    • Receptor-induced conformational changes of murine coronavirus spike protein
    • Matsuyama, S., and F. Taguchi. 2002. Receptor-induced conformational changes of murine coronavirus spike protein. J. Virol. 76:11819-11826.
    • (2002) J. Virol , vol.76 , pp. 11819-11826
    • Matsuyama, S.1    Taguchi, F.2
  • 32
    • 24644441711 scopus 로고    scopus 로고
    • Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection
    • Matsuyama, S., M. Ujike, S. Morikawa, M. Tashiro, and F. Taguchi. 2005. Protease-mediated enhancement of severe acute respiratory syndrome coronavirus infection. Proc. Natl. Acad. Sci. USA 102:12543-12547.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 12543-12547
    • Matsuyama, S.1    Ujike, M.2    Morikawa, S.3    Tashiro, M.4    Taguchi, F.5
  • 33
    • 33646672410 scopus 로고    scopus 로고
    • The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein
    • Moreno, M. R., M. Giudici, and J. Villalain. 2006. The membranotropic regions of the endo and ecto domains of HIV gp41 envelope glycoprotein. Biochim. Biophys. Acta 1758:111-123.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 111-123
    • Moreno, M.R.1    Giudici, M.2    Villalain, J.3
  • 34
    • 1042298782 scopus 로고    scopus 로고
    • Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan
    • Moreno, M. R., R. Pascual, and J. Villalain. 2004. Identification of membrane-active regions of the HIV-1 envelope glycoprotein gp41 using a 15-mer gp41-peptide scan. Biochim. Biophys. Acta 1661:97-105.
    • (2004) Biochim. Biophys. Acta , vol.1661 , pp. 97-105
    • Moreno, M.R.1    Pascual, R.2    Villalain, J.3
  • 35
    • 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., G. V. Yamshchikov, G. D. Ritter, Jr., F. Gao, M. J. Jin, C. D. Nail, C. P. Spies, B. H. Hahn, and R. W. Compans. 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 Jr., G.D.3    Gao, F.4    Jin, M.J.5    Nail, C.D.6    Spies, C.P.7    Hahn, B.H.8    Compans, R.W.9
  • 36
    • 26244466757 scopus 로고    scopus 로고
    • Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion
    • Petit, C. M., J. M. Melancon, V. N. Chouljenko, R. Colgrove, M. Farzan, D. M. Knipe, and K. G. Kousoulas. 2005. Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion. Virology 341:215-230.
    • (2005) Virology , vol.341 , pp. 215-230
    • Petit, C.M.1    Melancon, J.M.2    Chouljenko, V.N.3    Colgrove, R.4    Farzan, M.5    Knipe, D.M.6    Kousoulas, K.G.7
  • 37
    • 0030071620 scopus 로고    scopus 로고
    • Tetraoleoylpyrophosphatidic acid: A four acyl-chain lipid which forms a hexagonal II phase with high curvature
    • Powell, G. L., and S. W. Hui. 1996. Tetraoleoylpyrophosphatidic acid: a four acyl-chain lipid which forms a hexagonal II phase with high curvature. Biophys. J. 70:1402-1406.
    • (1996) Biophys. J , vol.70 , pp. 1402-1406
    • Powell, G.L.1    Hui, S.W.2
  • 39
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche, S., S. Bressanelli, F. A. Rey, and Y. Gaudin. 2006. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 313:187-191.
    • (2006) Science , vol.313 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 40
    • 0025348217 scopus 로고
    • Control of virus-induced cell fusion by host cell lipid composition
    • Roos, D. S., C. S. Duchala, C. B. Stephensen, K. V. Holmes, and P. W. Choppin. 1990. Control of virus-induced cell fusion by host cell lipid composition. Virology 175:345-357.
    • (1990) Virology , vol.175 , pp. 345-357
    • Roos, D.S.1    Duchala, C.S.2    Stephensen, C.B.3    Holmes, K.V.4    Choppin, P.W.5
  • 41
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., P. Fariselli, and R. Casadio. 1996. Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci. 5:1704-1718.
    • (1996) Protein Sci , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 43
    • 0037413864 scopus 로고    scopus 로고
    • Pre-transmembrane sequence of Ebola glycoprotein. Interfacial hydrophobicity distribution and interaction with membranes
    • Saez-Cirion, A., M. J. Gomara, A. Agirre, and J. L. Nieva. 2003. Pre-transmembrane sequence of Ebola glycoprotein. Interfacial hydrophobicity distribution and interaction with membranes. FEBS Lett. 533:47-53.
    • (2003) FEBS Lett , vol.533 , pp. 47-53
    • Saez-Cirion, A.1    Gomara, M.J.2    Agirre, A.3    Nieva, J.L.4
  • 44
    • 33745400398 scopus 로고    scopus 로고
    • Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
    • Sainz, B., Jr., E. C. Mossel, W. R. Gallaher, W. C. Wimley, C. J. Peters, R. B. Wilson, and R. F. Garry. 2006. Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein. Virus Res. 120:146-155.
    • (2006) Virus Res , vol.120 , pp. 146-155
    • Sainz Jr., B.1    Mossel, E.C.2    Gallaher, W.R.3    Wimley, W.C.4    Peters, C.J.5    Wilson, R.B.6    Garry, R.F.7
  • 45
    • 12344268838 scopus 로고    scopus 로고
    • The aromatic domain of the coronavirus class I viral fusion protein induces membrane permeabilization: Putative role during viral entry
    • Sainz, B., Jr., J. M. Rausch, W. R. Gallaher, R. F. Garry, and W. C. Wimley. 2005. The aromatic domain of the coronavirus class I viral fusion protein induces membrane permeabilization: putative role during viral entry. Biochemistry 44:947-958.
    • (2005) Biochemistry , vol.44 , pp. 947-958
    • Sainz Jr., B.1    Rausch, J.M.2    Gallaher, W.R.3    Garry, R.F.4    Wimley, W.C.5
  • 46
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel, K., J. T. West, and E. Hunter. 1999. A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 73:2469-2480.
    • (1999) J. Virol , vol.73 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 47
    • 0035859948 scopus 로고    scopus 로고
    • The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles
    • Schibli, D. J., R. C. Montelaro, and H. J. Vogel. 2001. The membrane-proximal tryptophan-rich region of the HIV glycoprotein, gp41, forms a well-defined helix in dodecylphosphocholine micelles. Biochemistry 40:9570-9578.
    • (2001) Biochemistry , vol.40 , pp. 9570-9578
    • Schibli, D.J.1    Montelaro, R.C.2    Vogel, H.J.3
  • 48
    • 11144340301 scopus 로고    scopus 로고
    • Class I and class II viral fusion protein structures reveal similar principles in membrane fusion
    • Schibli, D. J., and W. Weissenhorn. 2004. Class I and class II viral fusion protein structures reveal similar principles in membrane fusion. Mol. Membr. Biol. 21:361-371.
    • (2004) Mol. Membr. Biol , vol.21 , pp. 361-371
    • Schibli, D.J.1    Weissenhorn, W.2
  • 51
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry
    • 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) Proc. 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
  • 52
    • 33646729280 scopus 로고    scopus 로고
    • Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env
    • Sjoberg, M., M. Wallin, B. Lindqvist, and H. Garoff. 2006. Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env. J. Virol. 80:5540-5551.
    • (2006) J. Virol , vol.80 , pp. 5540-5551
    • Sjoberg, M.1    Wallin, M.2    Lindqvist, B.3    Garoff, H.4
  • 53
    • 0028054825 scopus 로고
    • Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain
    • Spies, C. P., G. D. Ritter, Jr., M. J. Mulligan, and R. W. Compans. 1994. Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain. J. Virol. 68:585-591.
    • (1994) J. Virol , vol.68 , pp. 585-591
    • Spies, C.P.1    Ritter Jr., G.D.2    Mulligan, M.J.3    Compans, R.W.4
  • 54
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez, T., W. R. Gallaher, A. Agirre, F. M. Goni, and J. L. Nieva. 2000. Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion. J. Virol. 74:8038-8047.
    • (2000) J. Virol , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 56
    • 0032561132 scopus 로고    scopus 로고
    • Principles governing amino acid composition of integral membrane proteins: Application to topology prediction
    • Tusnady, G. E., and I. Simon. 1998. Principles governing amino acid composition of integral membrane proteins: application to topology prediction. J. Mol. Biol. 283:489-506.
    • (1998) J. Mol. Biol , vol.283 , pp. 489-506
    • Tusnady, G.E.1    Simon, I.2
  • 57
    • 27144511135 scopus 로고    scopus 로고
    • Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection
    • Youn, S., E. W. Collision, and C. E. Machamer. 2005. Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection. J. Virol. 79:13209-13217.
    • (2005) J. Virol , vol.79 , pp. 13209-13217
    • Youn, S.1    Collision, E.W.2    Machamer, C.E.3
  • 58
    • 0037223630 scopus 로고    scopus 로고
    • Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8
    • Zelus, B. D., J. H. Schickli, D. M. Blau, S. R. Weiss, and K. V. Holmes. 2003. Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8. J. Virol. 77:830-840.
    • (2003) J. Virol , vol.77 , pp. 830-840
    • Zelus, B.D.1    Schickli, J.H.2    Blau, D.M.3    Weiss, S.R.4    Holmes, K.V.5
  • 59
    • 0242578444 scopus 로고    scopus 로고
    • Intracellular cleavage of human influenza A virus hemagglutinin and its inhibition
    • Zhirnov, O. P., I. V. Vorobjeva, A. V. Ovcharenko, and H. D. Klenk. 2003. Intracellular cleavage of human influenza A virus hemagglutinin and its inhibition. Biochemistry (Moscow) 68:1020-1026.
    • (2003) Biochemistry (Moscow) , vol.68 , pp. 1020-1026
    • Zhirnov, O.P.1    Vorobjeva, I.V.2    Ovcharenko, A.V.3    Klenk, H.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.