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Volumn 79, Issue 18, 2005, Pages 11901-11913

The carboxy-terminal sequence of the pestivirus glycoprotein E rns represents an unusual type of membrane anchor

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; GLYCOPROTEIN E; GLYCOPROTEIN E RNS; GREEN FLUORESCENT PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 24644472832     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.79.18.11901-11913.2005     Document Type: Article
Times cited : (48)

References (64)
  • 1
    • 3543016171 scopus 로고    scopus 로고
    • Signal recognition particle mediates post-translational targeting in eukaryotes
    • Abell, B. M., M. R. Pool, O. Schlenker, J. Sinning, and S. High. 2004. Signal recognition particle mediates post-translational targeting in eukaryotes. EMBO J. 23:2755-2764.
    • (2004) EMBO J. , vol.23 , pp. 2755-2764
    • Abell, B.M.1    Pool, M.R.2    Schlenker, O.3    Sinning, J.4    High, S.5
  • 2
    • 0023709836 scopus 로고
    • Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups
    • Bolin, S. R., V. Moennig, N. E. Kelso Gourley, and J. Ridpath. 1988. Monoclonal antibodies with neutralizing activity segregate isolates of bovine viral diarrhea virus into groups. Arch. Virol. 99:117-123.
    • (1988) Arch. Virol. , vol.99 , pp. 117-123
    • Bolin, S.R.1    Moennig, V.2    Kelso Gourley, N.E.3    Ridpath, J.4
  • 3
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 4
    • 0038153194 scopus 로고    scopus 로고
    • The tale of tail-anchored proteins: Coming from the cytosol and looking for a membrane
    • Borgese, N., S. Colombo, and E. Pedrazzini. 2003. The tale of tail-anchored proteins: coming from the cytosol and looking for a membrane. J. Cell Biol. 161:1013-1019.
    • (2003) J. Cell Biol. , vol.161 , pp. 1013-1019
    • Borgese, N.1    Colombo, S.2    Pedrazzini, E.3
  • 5
    • 0037040923 scopus 로고    scopus 로고
    • An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein SA
    • Brass, V., E. Bieck, R. Montserret, B. Wolk, J. A. Hellings, H. E. Blum, F. Penin, and D. Moradpour. 2002. An amino-terminal amphipathic alpha-helix mediates membrane association of the hepatitis C virus nonstructural protein SA. J. Biol. Chem. 277:8130-8139.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8130-8139
    • Brass, V.1    Bieck, E.2    Montserret, R.3    Wolk, B.4    Hellings, J.A.5    Blum, H.E.6    Penin, F.7    Moradpour, D.8
  • 6
    • 0024043662 scopus 로고
    • Proteins encoded by bovine viral diarrhea virus: The genome organization of a pestivirus
    • Collett, M. S., R. Larson, S. Belzer, and E. Retzel. 1988. Proteins encoded by bovine viral diarrhea virus: the genome organization of a pestivirus. Virology 165:200-208.
    • (1988) Virology , vol.165 , pp. 200-208
    • Collett, M.S.1    Larson, R.2    Belzer, S.3    Retzel, E.4
  • 8
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. A. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.A.3
  • 9
    • 0023850760 scopus 로고
    • Neutralizing monoclonal antibodies to bovine viral diarrhoea virus bind to the 56K to 58K glycoprotein
    • Donis, R. O., W. Corapi, and E. J. Dubovi. 1988. Neutralizing monoclonal antibodies to bovine viral diarrhoea virus bind to the 56K to 58K glycoprotein. J. Gen. Virol. 69:77-86.
    • (1988) J. Gen. Virol. , vol.69 , pp. 77-86
    • Donis, R.O.1    Corapi, W.2    Dubovi, E.J.3
  • 10
    • 0032052706 scopus 로고    scopus 로고
    • Amino-terminal region of poliovirus 2C protein is sufficient for membrane binding
    • Echeverri, A., R. Banerjee, and A, Dasgupta. 1998. Amino-terminal region of poliovirus 2C protein is sufficient for membrane binding. Virus Res. 54:217-223.
    • (1998) Virus Res. , vol.54 , pp. 217-223
    • Echeverri, A.1    Banerjee, R.2    Dasgupta, A.3
  • 11
    • 0033600935 scopus 로고    scopus 로고
    • Prediction of potential GPI-modification sites in proprotein sequences
    • Eisenhaber, B., P. Bork, and F. Eisenhaber. 1999. Prediction of potential GPI-modification sites in proprotein sequences. J. Mol. Biol. 292:741-758.
    • (1999) J. Mol. Biol. , vol.292 , pp. 741-758
    • Eisenhaber, B.1    Bork, P.2    Eisenhaber, F.3
  • 13
    • 0029893139 scopus 로고    scopus 로고
    • Processing in the pestivirus E2-NS2 region: Identification of the nonstructural proteins p7 and E2p7
    • Elbers, K., N. Tautz, P. Becher, T. Rümenapf, and H.-J. Thiel. 1996. Processing in the pestivirus E2-NS2 region: identification of the nonstructural proteins p7 and E2p7. J. Virol. 70:4131-4135.
    • (1996) J. Virol. , vol.70 , pp. 4131-4135
    • Elbers, K.1    Tautz, N.2    Becher, P.3    Rümenapf, T.4    Thiel, H.-J.5
  • 14
    • 0033819541 scopus 로고    scopus 로고
    • E2-p7 region of the bovine viral diarrhea virus polyprotein: Processing and functional studies
    • Harada, T., N. Tautz, and H. J. Thiel. 2000. E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies. J. Virol. 74:9498-9506.
    • (2000) J. Virol. , vol.74 , pp. 9498-9506
    • Harada, T.1    Tautz, N.2    Thiel, H.J.3
  • 16
    • 0002343237 scopus 로고    scopus 로고
    • Family Flaviviridae
    • M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carstens, M. K. Estes, S. M. Lemon, J. Maniloff, M. A. Mayo, D. J. McGeoch, C. R. Pringle, and R. B. Wickner (ed.). Seventh report of the International Committee on Taxonomy of Viruses. Academic Press, San Diego, Calif.
    • Heinz, F. X., M. S. Collett, R. H. Purcell, E. A. Gould, C. R. Howard, M. Houghton, J. M. Moormann, C. M. Rice, and H.-J. Thiel. 2000. Family Flaviviridae, p. 859-878. In M. H. V. van Regenmortel, C. M. Fauquet, D. H. L. Bishop, E. B. Carstens, M. K. Estes, S. M. Lemon, J. Maniloff, M. A. Mayo, D. J. McGeoch, C. R. Pringle, and R. B. Wickner (ed.), Virus taxonomy. Seventh report of the International Committee on Taxonomy of Viruses. Academic Press, San Diego, Calif.
    • (2000) Virus Taxonomy , pp. 859-878
    • Heinz, F.X.1    Collett, M.S.2    Purcell, R.H.3    Gould, E.A.4    Howard, C.R.5    Houghton, M.6    Moormann, J.M.7    Rice, C.M.8    Thiel, H.-J.9
  • 18
    • 0028294275 scopus 로고
    • Glycoprotein E2 of classical swine fever virus: Expression in insect cells and identification as a ribonuclease
    • Hulst, M. M., G. Himes, E. Newbigin, and R. J. M. Moormann. 1994. Glycoprotein E2 of classical swine fever virus: expression in insect cells and identification as a ribonuclease. Virology 200:558-565.
    • (1994) Virology , vol.200 , pp. 558-565
    • Hulst, M.M.1    Himes, G.2    Newbigin, E.3    Moormann, R.J.M.4
  • 19
    • 0030704752 scopus 로고    scopus 로고
    • Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors
    • Hulst, M. M., and R. J. Moormann. 1997. Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors. J. Gen. Virol. 78:2779-2787.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2779-2787
    • Hulst, M.M.1    Moormann, R.J.2
  • 20
    • 0034741189 scopus 로고    scopus 로고
    • Erns protein of pestiviruses
    • Hulst, M. M., and R. J. Moormann. 2001. Erns protein of pestiviruses. Methods Enzymol. 342:431-440.
    • (2001) Methods Enzymol. , vol.342 , pp. 431-440
    • Hulst, M.M.1    Moormann, R.J.2
  • 22
    • 0034807137 scopus 로고    scopus 로고
    • Interaction of classical swine fever virus with membrane-associated heparan sulfate: Role for virus replication in vivo and virulence
    • Hulst, M. M., H. G. van Gennip, A. C. Vlot, E. Schooten, A. J. de Smit, and R. J. Moormann. 2001. Interaction of classical swine fever virus with membrane-associated heparan sulfate: role for virus replication in vivo and virulence. J. Virol. 75:9585-9595.
    • (2001) J. Virol. , vol.75 , pp. 9585-9595
    • Hulst, M.M.1    Van Gennip, H.G.2    Vlot, A.C.3    Schooten, E.4    De Smit, A.J.5    Moormann, R.J.6
  • 23
    • 0027204176 scopus 로고
    • Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera
    • Hulst, M. M., D. F. Westra, G. Wensvoort, and R. J. Moormann. 1993. Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera. J. Virol. 67:5435-5442.
    • (1993) J. Virol. , vol.67 , pp. 5435-5442
    • Hulst, M.M.1    Westra, D.F.2    Wensvoort, G.3    Moormann, R.J.4
  • 24
    • 0033955991 scopus 로고    scopus 로고
    • Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell surface glycosaminoglycans
    • Iqbal, M., H. Flick-Smith, and J. W. McCauley. 2000. Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell surface glycosaminoglycans. J. Gen. Virol. 81:451-459.
    • (2000) J. Gen. Virol. , vol.81 , pp. 451-459
    • Iqbal, M.1    Flick-Smith, H.2    McCauley, J.W.3
  • 25
    • 0036714407 scopus 로고    scopus 로고
    • Identification of the glycosaminoglycan-binding site on the glycoprotein E(rns) of bovine viral diarrhoea virus by site-directed mutagenesis
    • Iqbal, M., and J. W. McCauley. 2002. Identification of the glycosaminoglycan-binding site on the glycoprotein E(rns) of bovine viral diarrhoea virus by site-directed mutagenesis. J. Gen. Virol. 83:2153-2159.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2153-2159
    • Iqbal, M.1    McCauley, J.W.2
  • 26
    • 0347626043 scopus 로고    scopus 로고
    • rns glycoprotein in the control of activation of beta interferon by double-stranded RNA
    • rns glycoprotein in the control of activation of beta interferon by double-stranded RNA. J. Virol. 78:135-145.
    • (2004) J. Virol. , vol.78 , pp. 135-145
    • Iqbal, M.1    Poole, E.2    Goodbourn, S.3    McCauley, J.W.4
  • 27
    • 0019739813 scopus 로고
    • Use of protein a bearing staphylococci for the immunoprecipitation and isolation of antigens from cells
    • Kessler, S. W. 1981. Use of protein A bearing staphylococci for the immunoprecipitation and isolation of antigens from cells. Methods Enzymol. 73:442-459.
    • (1981) Methods Enzymol. , vol.73 , pp. 442-459
    • Kessler, S.W.1
  • 28
    • 0029134624 scopus 로고
    • Classical swine fever virus: Independent induction of protective immunity by two structural glycoproteins
    • König, M., T. Lengsfeld, T. Pauly, R. Stark, and H.-J. Thiel. 1995. Classical swine fever virus: independent induction of protective immunity by two structural glycoproteins. J. Virol. 69:6479-0486.
    • (1995) J. Virol. , vol.69 , pp. 6479-10486
    • König, M.1    Lengsfeld, T.2    Pauly, T.3    Stark, R.4    Thiel, H.-J.5
  • 29
    • 0031834914 scopus 로고    scopus 로고
    • Membrane association and RNA binding of recombinant hepatitis a virus protein 2C
    • Kusov, Y. Y., C. Probst, M. Jecht, P. D. Jost, and V. Gauss-Muller. 1998. Membrane association and RNA binding of recombinant hepatitis A virus protein 2C. Arch. Virol. 143:931-944.
    • (1998) Arch. Virol. , vol.143 , pp. 931-944
    • Kusov, Y.Y.1    Probst, C.2    Jecht, M.3    Jost, P.D.4    Gauss-Muller, V.5
  • 30
    • 0027401769 scopus 로고
    • A class of membrane proteins with a C-terminal anchor
    • Kutay, U., E. Hartmann, and T. A. Rapoport. 1993. A class of membrane proteins with a C-terminal anchor. Trends Cell Biol. 3:72-75.
    • (1993) Trends Cell Biol. , vol.3 , pp. 72-75
    • Kutay, U.1    Hartmann, E.2    Rapoport, T.A.3
  • 31
    • 4544222881 scopus 로고    scopus 로고
    • Temporal modulation of an autoprotease is crucial for replication and pathogenicity of an RNA virus
    • Lackner, T., A. Muller, A. Pankraz, P. Becher, H. J. Thiel, A. E. Gorbalenya, and N. Tautz. 2004. Temporal modulation of an autoprotease is crucial for replication and pathogenicity of an RNA virus. J. Virol. 78:10765-10775.
    • (2004) J. Virol. , vol.78 , pp. 10765-10775
    • Lackner, T.1    Muller, A.2    Pankraz, A.3    Becher, P.4    Thiel, H.J.5    Gorbalenya, A.E.6    Tautz, N.7
  • 33
    • 0037085304 scopus 로고    scopus 로고
    • Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop
    • Langedijk, J. P. 2002. Translocation activity of C-terminal domain of pestivirus Erns and ribotoxin L3 loop. J. Biol. Chem. 277:5308-5314.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5308-5314
    • Langedijk, J.P.1
  • 34
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.). Lippincott-Raven Publishers, Philadelphia, Pa.
    • Lindenbach, B. D., and C. M. Rice. 2001. Flaviviridae: the viruses and their replication, p. 991-1042. In D. M. Knipe and P. M. Howley (ed.), Fields virology, vol. 1. Lippincott-Raven Publishers, Philadelphia, Pa.
    • (2001) Fields Virology , vol.1 , pp. 991-1042
    • Lindenbach, B.D.1    Rice, C.M.2
  • 35
    • 0842304523 scopus 로고    scopus 로고
    • CD46 is a cellular receptor for bovine viral diarrhea virus
    • Maurer, K., T. Krey, V. Moennig, H. J. Thiel, and T. Rumenapf. 2004. CD46 is a cellular receptor for bovine viral diarrhea virus. J. Virol. 78:1792-1799.
    • (2004) J. Virol. , vol.78 , pp. 1792-1799
    • Maurer, K.1    Krey, T.2    Moennig, V.3    Thiel, H.J.4    Rumenapf, T.5
  • 36
    • 0036315301 scopus 로고    scopus 로고
    • Recovery of virulent and RNase-negative attenuated type 2 bovine viral diarrhea viruses from infectious cDNA clones
    • Meyer, C., M. Von Freyburg, K. Elbers, and G. Meyers. 2002. Recovery of virulent and RNase-negative attenuated type 2 bovine viral diarrhea viruses from infectious cDNA clones. J. Virol. 76:8494-8503.
    • (2002) J. Virol. , vol.76 , pp. 8494-8503
    • Meyer, C.1    Von Freyburg, M.2    Elbers, K.3    Meyers, G.4
  • 37
    • 0345148344 scopus 로고    scopus 로고
    • rns of the pestivirus classical swine fever virus lead to virus attenuation
    • rns of the pestivirus classical swine fever virus lead to virus attenuation. J. Virol. 73:10224-10235.
    • (1999) J. Virol. , vol.73 , pp. 10224-10235
    • Meyers, G.1    Saalmüller, A.2    Büttner, M.3
  • 38
    • 0029861559 scopus 로고    scopus 로고
    • Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs
    • Meyers, G., N. Tautz, P. Becher, H.-J. Thiel, and B. Kümmerer. 1996. Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs. J. Virol. 70:8606-8613.
    • (1996) J. Virol. , vol.70 , pp. 8606-8613
    • Meyers, G.1    Tautz, N.2    Becher, P.3    Thiel, H.-J.4    Kümmerer, B.5
  • 39
    • 0033802790 scopus 로고    scopus 로고
    • Anchoring of a monotopic membrane protein: The binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer
    • Nina, M., S. Berneche, and B. Roux. 2000. Anchoring of a monotopic membrane protein: the binding of prostaglandin H2 synthase-1 to the surface of a phospholipid bilayer. Eur. Biophys. J. 29:439-454.
    • (2000) Eur. Biophys. J. , vol.29 , pp. 439-454
    • Nina, M.1    Berneche, S.2    Roux, B.3
  • 40
    • 0344692326 scopus 로고    scopus 로고
    • Analysis of the association of proteins with membranes
    • J. S. Bonifacino, M. Dasso, J. Lippincott-Schwartz, J. B. Harford, and K. M. Yamada (ed.). John Wiley & Sons, Inc., New York, N.Y.
    • Okamoto, T., R. B. S. P. E. Schwab, and M. P. Lisanti. 1999. Analysis of the association of proteins with membranes, p. 5.4.1-5.4.17. In J. S. Bonifacino, M. Dasso, J. Lippincott-Schwartz, J. B. Harford, and K. M. Yamada (ed.), Current protocols in cell biology. John Wiley & Sons, Inc., New York, N.Y.
    • (1999) Current Protocols in Cell Biology
    • Okamoto, T.1    Schwab, R.B.S.P.E.2    Lisanti, M.P.3
  • 41
    • 0028331981 scopus 로고
    • Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C
    • Paul, A. V., A. Molla, and E. Wimmer. 1994. Studies of a putative amphipathic helix in the N-terminus of poliovirus protein 2C. Virology 199:188-199.
    • (1994) Virology , vol.199 , pp. 188-199
    • Paul, A.V.1    Molla, A.2    Wimmer, E.3
  • 43
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., P. J. Loll, and R. M. Garavito. 1994. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367:243-249.
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 44
    • 0026032950 scopus 로고
    • Structural proteins of hog cholera virus expressed by vaccinia virus: Further characterization and induction of protective immunity
    • Rumenapf, T., R. Stark, G. Meyers, and H.-J. Thiel. 1991. Structural proteins of hog cholera virus expressed by vaccinia virus: further characterization and induction of protective immunity. J. Virol. 65:589-597.
    • (1991) J. Virol. , vol.65 , pp. 589-597
    • Rumenapf, T.1    Stark, R.2    Meyers, G.3    Thiel, H.-J.4
  • 45
    • 0027238125 scopus 로고
    • Processing of the envelope glycoproteins of pestiviruses
    • Rumenapf, T., G. Unger, J. H. Strauss, and H.-J. Thiel. 1993. Processing of the envelope glycoproteins of pestiviruses. J. Virol. 67:3288-3295.
    • (1993) J. Virol. , vol.67 , pp. 3288-3295
    • Rumenapf, T.1    Unger, G.2    Strauss, J.H.3    Thiel, H.-J.4
  • 46
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 47
    • 0027433731 scopus 로고
    • Identification of a structural glycoprotein of an RNA virus as a ribonuclease
    • Schneider, R., G. Unger, R. Stark, E. Schneider-Scherzer, and H.-J. Thiel. 1993. Identification of a structural glycoprotein of an RNA virus as a ribonuclease. Science 261:1169-1171.
    • (1993) Science , vol.261 , pp. 1169-1171
    • Schneider, R.1    Unger, G.2    Stark, R.3    Schneider-Scherzer, E.4    Thiel, H.-J.5
  • 48
    • 0034161496 scopus 로고    scopus 로고
    • A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses
    • Shmulevitz, M., and R. Duncan. 2000. A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses. EMBO J. 19:902-912.
    • (2000) EMBO J. , vol.19 , pp. 902-912
    • Shmulevitz, M.1    Duncan, R.2
  • 49
    • 0032705129 scopus 로고    scopus 로고
    • The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis
    • Spencer, A. G., E. Thuresson, J. C. Otto, I. Song, T. Smith, D. L. DeWitt, R. M. Garavito, and W. L. Smith. 1999. The membrane binding domains of prostaglandin endoperoxide H synthases 1 and 2. Peptide mapping and mutational analysis, J. Biol. Chem. 274:32936-32942.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32936-32942
    • Spencer, A.G.1    Thuresson, E.2    Otto, J.C.3    Song, I.4    Smith, T.5    DeWitt, D.L.6    Garavito, R.M.7    Smith, W.L.8
  • 50
    • 0027424003 scopus 로고
    • Processing of pestivirus polyprotein: Cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus
    • Stark, R., G. Meyers, T. Rümenapf, and H.-J. Thiel. 1993. Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus. J. Virol. 67:7088-7095.
    • (1993) J. Virol. , vol.67 , pp. 7088-7095
    • Stark, R.1    Meyers, G.2    Rümenapf, T.3    Thiel, H.-J.4
  • 51
    • 0030960350 scopus 로고    scopus 로고
    • Serine protease of pestiviruses: Determination of cleavage sites
    • Tautz, N., K. Elbers, D. Stell, G. Meyers, and H.-J. Thiel. 1997. Serine protease of pestiviruses: determination of cleavage sites. J. Virol. 71:5415-5422.
    • (1997) J. Virol. , vol.71 , pp. 5415-5422
    • Tautz, N.1    Elbers, K.2    Stell, D.3    Meyers, G.4    Thiel, H.-J.5
  • 52
    • 0030807887 scopus 로고    scopus 로고
    • Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells
    • Teterina, N. L., A. E. Gorbalenya, D. Egger, K. Bienz, and E. Ehrenfeld. 1997. Poliovirus 2C protein determinants of membrane binding and rearrangements in mammalian cells. J. Virol. 71:8962-8972.
    • (1997) J. Virol. , vol.71 , pp. 8962-8972
    • Teterina, N.L.1    Gorbalenya, A.E.2    Egger, D.3    Bienz, K.4    Ehrenfeld, E.5
  • 53
    • 0025955758 scopus 로고
    • Hog cholera virus: Molecular composition of virions from a pestivirus
    • Thiel, H.-J., R. Stark, E. Weiland, T. Rümenapf, and G. Meyers. 1991. Hog cholera virus: molecular composition of virions from a pestivirus. J. Virol. 65:4705-4712.
    • (1991) J. Virol. , vol.65 , pp. 4705-4712
    • Thiel, H.-J.1    Stark, R.2    Weiland, E.3    Rümenapf, T.4    Meyers, G.5
  • 54
    • 0025864175 scopus 로고
    • Live attenuated pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus protects swine against both pseudorabies and hog cholera
    • van Zijl, M., G. Wensvoort, E. de Kluyver, M. Hulst, H. van der Gulden, A. Gielkens, A. Berns, and R. Moormann. 1991. Live attenuated pseudorabies virus expressing envelope glycoprotein E1 of hog cholera virus protects swine against both pseudorabies and hog cholera. J. Virol. 65:2761-2765.
    • (1991) J. Virol. , vol.65 , pp. 2761-2765
    • Van Zijl, M.1    Wensvoort, G.2    De Kluyver, E.3    Hulst, M.4    Van Der Gulden, H.5    Gielkens, A.6    Berns, A.7    Moormann, R.8
  • 55
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne, G., and Y. Gavel. 1988. Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174:671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.1    Gavel, Y.2
  • 56
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • Wattenberg, B., and T. Lithgow. 2001. Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes. Traffic 2:66-71.
    • (2001) Traffic , vol.2 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 57
    • 0026665695 scopus 로고
    • A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus
    • Weiland, E., R. Ahl, R. Stark, F. Weiland, and H.-J. Thiel. 1992. A second envelope glycoprotein mediates neutralization of a pestivirus, hog cholera virus. J. Virol. 66:3677-3682.
    • (1992) J. Virol. , vol.66 , pp. 3677-3682
    • Weiland, E.1    Ahl, R.2    Stark, R.3    Weiland, F.4    Thiel, H.-J.5
  • 58
    • 0025307406 scopus 로고
    • Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide linked heterodimer
    • Weiland, E., R. Stark, B. Haas, T. Rümenapf, G. Meyers, and H.-J. Thiel. 1990. Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide linked heterodimer. J. Virol. 64:3563-3569.
    • (1990) J. Virol. , vol.64 , pp. 3563-3569
    • Weiland, E.1    Stark, R.2    Haas, B.3    Rümenapf, T.4    Meyers, G.5    Thiel, H.-J.6
  • 59
    • 0032904783 scopus 로고    scopus 로고
    • Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles
    • Weiland, F., E. Weiland, G. Unger, A. Saalmuller, and H. J. Thiel. 1999. Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles. J. Gen. Virol. 80:1157-1165.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1157-1165
    • Weiland, F.1    Weiland, E.2    Unger, G.3    Saalmuller, A.4    Thiel, H.J.5
  • 60
    • 0033548169 scopus 로고    scopus 로고
    • The structure of the membrane protein squalene-hopene cyclase at 2.0 a resolution
    • Wendt, K. U., A. Lenhart, and G. E. Schulz. 1999. The structure of the membrane protein squalene-hopene cyclase at 2.0 A resolution. J. Mol. Biol. 286:175-187.
    • (1999) J. Mol. Biol. , vol.286 , pp. 175-187
    • Wendt, K.U.1    Lenhart, A.2    Schulz, G.E.3
  • 61
    • 0029655758 scopus 로고    scopus 로고
    • RNase of classical swine fever virus: Biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies
    • Windisch, J. M., R. Schneider, R. Stark, E. Weiland, G. Meyers, and H.-J. Thiel. 1996. RNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies. J. Virol. 70:352-358.
    • (1996) J. Virol. , vol.70 , pp. 352-358
    • Windisch, J.M.1    Schneider, R.2    Stark, R.3    Weiland, E.4    Meyers, G.5    Thiel, H.-J.6
  • 62
    • 0025740555 scopus 로고
    • Pestivirus gene expression: The first protein product of the bovine viral diarrhea virus large open reading frame, p20, possesses proteolytic activity
    • Wiskerchen, M., S. K. Belzer, and M. S. Collett. 1991. Pestivirus gene expression: the first protein product of the bovine viral diarrhea virus large open reading frame, p20, possesses proteolytic activity. J. Virol. 65:4508-4514.
    • (1991) J. Virol. , vol.65 , pp. 4508-4514
    • Wiskerchen, M.1    Belzer, S.K.2    Collett, M.S.3
  • 63
    • 0029033825 scopus 로고
    • Replication-deficient vaccinia virus encoding bacteriophage T7 RNA polymerase for transient gene expression in mammalian cells
    • Wyatt, L. S., B. Moss, and S. Rozenblatt. 1995. Replication-deficient vaccinia virus encoding bacteriophage T7 RNA polymerase for transient gene expression in mammalian cells. Virology 210:202-205.
    • (1995) Virology , vol.210 , pp. 202-205
    • Wyatt, L.S.1    Moss, B.2    Rozenblatt, S.3
  • 64
    • 0031010133 scopus 로고    scopus 로고
    • Bovine viral diarrhea virus NS3 serine proteinase: Polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication
    • Xu, J., E. Mendez, P. R. Caron, C. Lin, M. A. Murcko, M. S. Collett, and C. M. Rice. 1997. Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication. J. Virol. 71:5312-5322.
    • (1997) J. Virol. , vol.71 , pp. 5312-5322
    • Xu, J.1    Mendez, E.2    Caron, P.R.3    Lin, C.4    Murcko, M.A.5    Collett, M.S.6    Rice, C.M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.