메뉴 건너뛰기




Volumn 71, Issue 11, 1997, Pages 8475-8481

Proteolytic activation of tick-borne encephalitis virus by furin

Author keywords

[No Author keywords available]

Indexed keywords

FURIN; VIRUS ENVELOPE PROTEIN;

EID: 0030764780     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.11.8475-8481.1997     Document Type: Article
Times cited : (437)

References (48)
  • 1
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • Allison, S. L., J. Schalich, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J. Virol. 69:695-700.
    • (1995) J. Virol. , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 2
    • 0029162425 scopus 로고
    • Synthesis and secretion of recombinant tick-borne encephalitis virus protein e in soluble and particulate form
    • Allison, S. L., K. Stadler, C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol. 69:5816-5820.
    • (1995) J. Virol. , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 3
    • 0023841862 scopus 로고
    • A view of acidic intracellular compartments
    • Anderson, R. G. W., and L. Orci. 1988. A view of acidic intracellular compartments. J. Cell Biol. 106:539-543.
    • (1988) J. Cell Biol. , vol.106 , pp. 539-543
    • Anderson, R.G.W.1    Orci, L.2
  • 5
  • 6
    • 70449217974 scopus 로고
    • Techniques for hemagglutination and hemagglutination inhibition with arthropod-borne viruses
    • Clarke, D. A., and J. Casals. 1958. Techniques for hemagglutination and hemagglutination inhibition with arthropod-borne viruses. Am. J. Trop. Med. Hyg. 7:561-573.
    • (1958) Am. J. Trop. Med. Hyg. , vol.7 , pp. 561-573
    • Clarke, D.A.1    Casals, J.2
  • 7
    • 0030048594 scopus 로고    scopus 로고
    • Furin/PACE/SPC1: A convertase involved in exocytic and endocytic processing of precursor proteins
    • Denault, J.-B., and R. Leduc. 1996. Furin/PACE/SPC1: a convertase involved in exocytic and endocytic processing of precursor proteins. FEBS Lett. 379:113-116.
    • (1996) FEBS Lett. , vol.379 , pp. 113-116
    • Denault, J.-B.1    Leduc, R.2
  • 8
    • 0027081630 scopus 로고
    • The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
    • Guirakhoo, F., R. A. Bolin, and J. T. Roehrig. 1992. The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 191:921-931.
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 9
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: Comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • Guirakhoo, F., F. X. Heinz, C. W. Mandl, H. Holzmann, and C. Kunz. 1991. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J. Gen. Virol. 72:1323-1329.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3    Holzmann, H.4    Kunz, C.5
  • 10
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger, S., V. Bosch, H. Angliker, E. Shaw, H.-D. Klenk, and W. Garten. 1992. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature 360:358-361.
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.-D.5    Garten, W.6
  • 11
    • 0019835410 scopus 로고
    • Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: Comparison with other flaviviruses
    • Heinz, F. X., and C. Kunz. 1981. Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: comparison with other flaviviruses. J. Gen. Virol. 57:263-274.
    • (1981) J. Gen. Virol. , vol.57 , pp. 263-274
    • Heinz, F.X.1    Kunz, C.2
  • 12
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM
    • Heinz, F. X., K. Stiasny, G. Püschner-Auer, H. Holzmann, S. L. Allison, C. W. Mandl, and C. Kunz. 1994. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198:109-117.
    • (1994) Virology , vol.198 , pp. 109-117
    • Heinz, F.X.1    Stiasny, K.2    Püschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6    Kunz, C.7
  • 13
    • 0031014304 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice
    • Holzmann, H., K. Stiasny, M. Ecker, C. Kunz, and F. X. Heinz. 1997. Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J. Gen. Virol. 78: 31-37.
    • (1997) J. Gen. Virol. , vol.78 , pp. 31-37
    • Holzmann, H.1    Stiasny, K.2    Ecker, M.3    Kunz, C.4    Heinz, F.X.5
  • 14
    • 0028095251 scopus 로고
    • Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses
    • Horimoto, T., K. Nakayama, S. P. Smeekens, and Y. Kawaoka. 1994. Proprotein-processing endoproteases PC6 and furin both activate hemagglutinin of virulent avian influenza viruses. J. Virol. 68:6074-6078.
    • (1994) J. Virol. , vol.68 , pp. 6074-6078
    • Horimoto, T.1    Nakayama, K.2    Smeekens, S.P.3    Kawaoka, Y.4
  • 15
    • 0028871001 scopus 로고
    • Endoproteolytic cleavage of HIV-gp160 envelope precursor occurs after exit from the trans-Golgi network (TGN)
    • Kantanen, M. L., P. Leinikki, and E. Kuismanen. 1995. Endoproteolytic cleavage of HIV-gp160 envelope precursor occurs after exit from the trans-Golgi network (TGN). Arch. Virol. 140:1441-1449.
    • (1995) Arch. Virol. , vol.140 , pp. 1441-1449
    • Kantanen, M.L.1    Leinikki, P.2    Kuismanen, E.3
  • 16
    • 0001561789 scopus 로고
    • Activation cleavage of viral spike proteins by host proteases
    • E. Wimmer (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Klenk, H.-D., and W. Garten. 1994. Activation cleavage of viral spike proteins by host proteases, p. 241-280. In E. Wimmer (ed.), Cellular receptors for animal viruses. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) Cellular Receptors for Animal Viruses , pp. 241-280
    • Klenk, H.-D.1    Garten, W.2
  • 17
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • Laemmli, U. K., and M. Favre. 1973. Maturation of the head of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80:575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 18
    • 0025219313 scopus 로고
    • Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
    • Lobigs, M., and H. Garoff. 1990. Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62. J. Virol. 64:1233-1240.
    • (1990) J. Virol. , vol.64 , pp. 1233-1240
    • Lobigs, M.1    Garoff, H.2
  • 19
    • 0023811062 scopus 로고
    • Sequence of the structural proteins of tick-borne encephalitis virus (Western subtype) and comparative analysis with other flaviviruses
    • Mandl, C. W., F. X. Heinz, and C. Kunz. 1988. Sequence of the structural proteins of tick-borne encephalitis virus (Western subtype) and comparative analysis with other flaviviruses. Virology 166:197-205.
    • (1988) Virology , vol.166 , pp. 197-205
    • Mandl, C.W.1    Heinz, F.X.2    Kunz, C.3
  • 20
    • 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., P. A. Bresnahan, S. H. Leppla, K. R. Klimpel, and G. Thomas. 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. 267:16396-16402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 21
    • 0028107656 scopus 로고
    • Intracellular trafficking and activation of the furin proprotein convertase: Localization to the TGN and recycling from the cell surface
    • Molloy, S. S., L. Thomas, J. K. VanSlyke, P. E. Stenberg, and G. Thomas. 1994. Intracellular trafficking and activation of the furin proprotein convertase: localization to the TGN and recycling from the cell surface. EMBO J. 13:18-33.
    • (1994) EMBO J. , vol.13 , pp. 18-33
    • Molloy, S.S.1    Thomas, L.2    VanSlyke, J.K.3    Stenberg, P.E.4    Thomas, G.5
  • 22
    • 0001925194 scopus 로고    scopus 로고
    • Flaviviruses
    • B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Monath, T. P., and F. X. Heinz. 1996. Flaviviruses, p. 961-1034. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Virology, 3rd Ed. , pp. 961-1034
    • Monath, T.P.1    Heinz, F.X.2
  • 23
    • 0027530821 scopus 로고
    • Processing of the dengue virus type 2 proteins prM and C-prM
    • Murray, J. M., J. G. Aaskov, and P. J. Wright. 1993. Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol. 74:175-182.
    • (1993) J. Gen. Virol. , vol.74 , pp. 175-182
    • Murray, J.M.1    Aaskov, J.G.2    Wright, P.J.3
  • 24
    • 0028229822 scopus 로고
    • A furin-defective cell line is able to process correctly the gp160 of human immunodeficiency virus type 1
    • Ohnishi, Y., T. Shioda, K. Nakayama, S. Iwata, B. Gotoh, M. Hamaguchi, and Y. Nagai. 1994. A furin-defective cell line is able to process correctly the gp160 of human immunodeficiency virus type 1. J. Virol. 68:4075-4079.
    • (1994) J. Virol. , vol.68 , pp. 4075-4079
    • Ohnishi, Y.1    Shioda, T.2    Nakayama, K.3    Iwata, S.4    Gotoh, B.5    Hamaguchi, M.6    Nagai, Y.7
  • 26
    • 0028196642 scopus 로고
    • Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2
    • Ortmann, D., M. Ohuchi, H. Angliker, E. Shaw, W. Garten, and H.-D. Klenk. 1994. Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2. J. Virol. 68:2772-2776.
    • (1994) J. Virol. , vol.68 , pp. 2772-2776
    • Ortmann, D.1    Ohuchi, M.2    Angliker, H.3    Shaw, E.4    Garten, W.5    Klenk, H.-D.6
  • 27
    • 0025064269 scopus 로고
    • Acidotropic amines inhibit proteolytic processing of flavivirus prM protein
    • Randolph, V. B., G. Winkler, and V. Stollar. 1990. Acidotropic amines inhibit proteolytic processing of flavivirus prM protein. Virology 174:450-458.
    • (1990) Virology , vol.174 , pp. 450-458
    • Randolph, V.B.1    Winkler, G.2    Stollar, V.3
  • 28
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: the viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, P. M. Howley, R. M. Chanock, J. L. Melnick, T. P. Monath, B. Roizman, and S. E. Straus (ed.), Virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 29
    • 0026567676 scopus 로고
    • Membrane fusion process of Semliki Forest virus. II. Cleavage-dependent reorganization of the spike protein complex controls virus entry
    • Salminen, A., J. M. Wahlberg, M. Lobigs, P. Liljeström, and H. Garoff. 1992. Membrane fusion process of Semliki Forest virus. II. Cleavage-dependent reorganization of the spike protein complex controls virus entry. J. Cell Biol. 116:349-357.
    • (1992) J. Cell Biol. , vol.116 , pp. 349-357
    • Salminen, A.1    Wahlberg, J.M.2    Lobigs, M.3    Liljeström, P.4    Garoff, H.5
  • 30
    • 0029011658 scopus 로고
    • Communication of post-Golgi elements with early endocytic pathway: Regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor
    • Sariola, M., J. Saraste, and E. Kuismanen. 1995. Communication of post-Golgi elements with early endocytic pathway: regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor. J. Cell Sci. 108:2465-2475.
    • (1995) J. Cell Sci. , vol.108 , pp. 2465-2475
    • Sariola, M.1    Saraste, J.2    Kuismanen, E.3
  • 31
    • 0029071584 scopus 로고
    • Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin
    • Schäfer, W., A. Stroh, S. Berghöfer, J. Seiler, M. Vey, M.-L. Kruse, H.-F. Kern, H.-D. Klenk, and W. Garten. 1995. Two independent targeting signals in the cytoplasmic domain determine trans-Golgi network localization and endosomal trafficking of the proprotein convertase furin. EMBO J. 14:2424-2435.
    • (1995) EMBO J. , vol.14 , pp. 2424-2435
    • Schäfer, W.1    Stroh, A.2    Berghöfer, S.3    Seiler, J.4    Vey, M.5    Kruse, M.-L.6    Kern, H.-F.7    Klenk, H.-D.8    Garten, W.9
  • 32
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • Schalich, J., S. L. Allison, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1996. Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J. Virol. 70:4549-4557.
    • (1996) J. Virol. , vol.70 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 33
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek, O., J. Biwersi, and A. S. Verkman. 1995. Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J. Biol. Chem. 270:4967-4970.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 34
    • 0015462429 scopus 로고
    • Change involving a viral membrane glycoprotein during morphogenesis of group B arboviruses
    • Shapiro, D., W. E. Brandt, and P. K. Russell. 1972. Change involving a viral membrane glycoprotein during morphogenesis of group B arboviruses. Virology 50:906-911.
    • (1972) Virology , vol.50 , pp. 906-911
    • Shapiro, D.1    Brandt, W.E.2    Russell, P.K.3
  • 35
    • 14744293993 scopus 로고
    • Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases
    • Smeekens, S. P. 1993. Processing of protein precursors by a novel family of subtilisin-related mammalian endoproteases. Bio/Technology 11:182-186.
    • (1993) Bio/Technology , vol.11 , pp. 182-186
    • Smeekens, S.P.1
  • 36
    • 0026643396 scopus 로고
    • Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease
    • Stieneke-Gröber, A., M. Vey, H. Angliker, E. Shaw, G. Thomas, C. Roberts, H.-D. Klenk, and W. Garten. 1992. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 11:2407-2414.
    • (1992) EMBO J. , vol.11 , pp. 2407-2414
    • Stieneke-Gröber, A.1    Vey, M.2    Angliker, H.3    Shaw, E.4    Thomas, G.5    Roberts, C.6    Klenk, H.-D.7    Garten, W.8
  • 39
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin: Compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey, M., W. Schäfer, S. Berghöfer, H.-D. Klenk, and W. Garten. 1994. Maturation of the trans-Golgi network protease furin: compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J. Cell Biol. 127:1829-1842.
    • (1994) J. Cell Biol. , vol.127 , pp. 1829-1842
    • Vey, M.1    Schäfer, W.2    Berghöfer, S.3    Klenk, H.-D.4    Garten, W.5
  • 40
    • 0028801453 scopus 로고
    • Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin
    • Vey, M., W. Schäfer, B. Reis, R. Ohuchi, W. Britt, W. Garten, H.-D. Klenk, and K. Radsak. 1995. Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediated by the human endoprotease furin. Virology 206:746-749.
    • (1995) Virology , vol.206 , pp. 746-749
    • Vey, M.1    Schäfer, W.2    Reis, B.3    Ohuchi, R.4    Britt, W.5    Garten, W.6    Klenk, H.-D.7    Radsak, K.8
  • 41
    • 0027295514 scopus 로고
    • Characterization of a secreted form of human furin endoprotease
    • Vidricaire, G., J.-B. Denault, and R. Leduc. 1993. Characterization of a secreted form of human furin endoprotease. Biochem. Biophys. Res. Commun. 195:1011-1018.
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 1011-1018
    • Vidricaire, G.1    Denault, J.-B.2    Leduc, R.3
  • 42
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg, J. M., W. A. M. Boere, and H. Garoff. 1989. The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation. J. Virol. 63:4991-4997.
    • (1989) J. Virol. , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.M.2    Garoff, H.3
  • 43
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein
    • Wahlberg, J. M., R. Bron, J. Wilschut, and H. Garoff. 1992. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 66:7309-7318.
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 44
    • 0025866211 scopus 로고
    • A mutant CHO-K1 strain with resistance to Pseudomonas exotoxin A and alphaviruses fails to cleave Sindbis virus glycoprotein PE2
    • Watson, D. G., J. M. Moehring, and T. J. Moehring. 1991. A mutant CHO-K1 strain with resistance to Pseudomonas exotoxin A and alphaviruses fails to cleave Sindbis virus glycoprotein PE2. J. Virol. 65:2332-2339.
    • (1991) J. Virol. , vol.65 , pp. 2332-2339
    • Watson, D.G.1    Moehring, J.M.2    Moehring, T.J.3
  • 45
    • 0024327726 scopus 로고
    • Cell-associated West Nile flavivirus is covered with E + Pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release
    • Wengler, G., and G. Wengler. 1989. Cell-associated West Nile flavivirus is covered with E + Pre-M protein heterodimers which are destroyed and reorganized by proteolytic cleavage during virus release. J. Virol. 63:2521-2526.
    • (1989) J. Virol. , vol.63 , pp. 2521-2526
    • Wengler, G.1    Wengler, G.2
  • 46
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. M. 1990. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:675-697.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 47
    • 0010296944 scopus 로고
    • Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160
    • Willey, R. L., J. S. Bonifacino, B. J. Potts, M. A. Martin, and R. D. Klausner. 1988. Biosynthesis, cleavage, and degradation of the human immunodeficiency virus 1 envelope glycoprotein gp160. Proc. Natl. Acad. Sci. USA 85:9580-9584.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9580-9584
    • Willey, R.L.1    Bonifacino, J.S.2    Potts, B.J.3    Martin, M.A.4    Klausner, R.D.5
  • 48
    • 0024412303 scopus 로고
    • Endoproteolytic activation of Newcastle disease virus fusion proteins requires an intracellular acidic environment
    • Yoshida, T., S. Takao, K. Kiyotani, and T. Sakaguchi. 1989. Endoproteolytic activation of Newcastle disease virus fusion proteins requires an intracellular acidic environment. Virology 170:571-574.
    • (1989) Virology , vol.170 , pp. 571-574
    • Yoshida, T.1    Takao, S.2    Kiyotani, K.3    Sakaguchi, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.