메뉴 건너뛰기




Volumn 305, Issue 1, 2003, Pages 138-152

Influenza a virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza a virus in polarized MDCK cells

Author keywords

Endocytosis; Influenza virus; Mutated (Cys561 Tyr561) hemagglutinin; Polarized budding; Raft association

Indexed keywords

GLYCOPROTEIN; HEMAGGLUTININ; META TYROSINE; SIALIDASE; VIRUS ENVELOPE PROTEIN;

EID: 0037225270     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.2002.1731     Document Type: Article
Times cited : (21)

References (48)
  • 1
    • 85031249978 scopus 로고    scopus 로고
    • Role of influenza virus hemagglutinin in determining the budding site of influenza virus
    • Abstract number W40-1. University of Wisconsin-Madison, Madison, WI
    • Adhikary, L., Barman, S., Kawaoka, Y., and Nayak, D. P. (2001). Role of influenza virus hemagglutinin in determining the budding site of influenza virus. Abstract number W40-1. 20th Annual Meeting of American Society for Virology. University of Wisconsin-Madison, Madison, WI.
    • (2001) 20th Annual Meeting of American Society for Virology
    • Adhikary, L.1    Barman, S.2    Kawaoka, Y.3    Nayak, D.P.4
  • 2
    • 0033858756 scopus 로고    scopus 로고
    • Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein
    • Ali, A., Avalos, R. T., Ponimaskin, E., and Nayak, D. P. (2000). Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein. J. Virol. 74, 8709-8719.
    • (2000) J. Virol. , vol.74 , pp. 8709-8719
    • Ali, A.1    Avalos, R.T.2    Ponimaskin, E.3    Nayak, D.P.4
  • 3
    • 0034939645 scopus 로고    scopus 로고
    • Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses
    • Barman, S., Ali, A., Hui, E. K., Adhikary, L., and Nayak, D. P. (2001). Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses. Virus Res. 77, 61-69.
    • (2001) Virus Res. , vol.77 , pp. 61-69
    • Barman, S.1    Ali, A.2    Hui, E.K.3    Adhikary, L.4    Nayak, D.P.5
  • 4
    • 0033934725 scopus 로고    scopus 로고
    • Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association
    • Barman, S., and Nayak, D. P. (2000). Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association. J. Virol. 74, 6538-6545.
    • (2000) J. Virol. , vol.74 , pp. 6538-6545
    • Barman, S.1    Nayak, D.P.2
  • 5
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer, C. B., and Roth, M. G. (1991). A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114, 413-421.
    • (1991) J. Cell Biol , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 6
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A., and London, E. (1998a). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 7
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D. A, and London, E. (1998b). Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164, 103-114.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 8
    • 0029123983 scopus 로고
    • Virus entry and release in polarized epithelial cells
    • Compans, R. W. (1995). Virus entry and release in polarized epithelial cells. Curr. Top. Microbiol. Immunol. 202, 209-219.
    • (1995) Curr. Top. Microbiol. Immunol. , vol.202 , pp. 209-219
    • Compans, R.W.1
  • 9
    • 0032994155 scopus 로고    scopus 로고
    • Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission
    • Deschambeault, J., Lalonde, J. P., Cervantes-Acosta, G., Lodge, R., Cohen, E. A., and Lemay, G. (1999). Polarized human immunodeficiency virus budding in lymphocytes involves a tyrosine-based signal and favors cell-to-cell viral transmission. J. Virol. 73, 5010-5017.
    • (1999) J. Virol. , vol.73 , pp. 5010-5017
    • Deschambeault, J.1    Lalonde, J.P.2    Cervantes-Acosta, G.3    Lodge, R.4    Cohen, E.A.5    Lemay, G.6
  • 11
    • 0034468745 scopus 로고    scopus 로고
    • Influenza virus matrix protein is the major driving force in virus budding
    • Gomez-Puertas, P., Albo, C., Perez-Pastrana, E., Vivo, A., and Portela, A. (2000). Influenza virus matrix protein is the major driving force in virus budding. J. Virol. 74, 11538-11547.
    • (2000) J. Virol. , vol.74 , pp. 11538-11547
    • Gomez-Puertas, P.1    Albo, C.2    Perez-Pastrana, E.3    Vivo, A.4    Portela, A.5
  • 12
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • Goto, H., and Kawaoka, Y. (1998). A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. USA 95, 10224-1022.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10224-11022
    • Goto, H.1    Kawaoka, Y.2
  • 13
    • 0033856584 scopus 로고    scopus 로고
    • Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging
    • Hermida-Matsumoto, L., and Resh, M. D. (2000). Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging. J. Virol. 74, 8670-8679.
    • (2000) J. Virol. , vol.74 , pp. 8670-8679
    • Hermida-Matsumoto, L.1    Resh, M.D.2
  • 14
    • 0027190727 scopus 로고
    • Targeting of viral glycoproteins to the Golgi complex
    • Hobman, T. C. (1993). Targeting of viral glycoproteins to the Golgi complex. Trends Microbiol. 1, 124-130.
    • (1993) Trends Microbiol. , vol.1 , pp. 124-130
    • Hobman, T.C.1
  • 15
    • 0026802981 scopus 로고
    • Expression of the influenza A virus M2 protein is restricted to apical surfaces of polarized epithelial cells
    • Hughey, P. G., Compans, R. W., Zebedee, S. L., and Lamb, R. A. (1992). Expression of the influenza A virus M2 protein is restricted to apical surfaces of polarized epithelial cells. J. Virol. 66, 5542-5552.
    • (1992) J. Virol. , vol.66 , pp. 5542-5552
    • Hughey, P.G.1    Compans, R.W.2    Zebedee, S.L.3    Lamb, R.A.4
  • 16
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • Jin, H., Leser, G. P., Zhang, J., and Lamb, R. A. (1997). Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J. 16, 1236-1247.
    • (1997) EMBO J. , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 17
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu, A., Avalos, R. T., Sanderson, C. M., and Nayak, D. P. (1996). Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70, 6508-6515.
    • (1996) J. Virol. , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 18
    • 0026328853 scopus 로고
    • Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoproteins: Role of cytoplasmic and anchor domains
    • Kundu, A., Jabbar, M. A., and Nayak, D. P. (1991). Cell surface transport, oligomerization, and endocytosis of chimeric type II glycoproteins: Role of cytoplasmic and anchor domains. Mol. Cell. Biol. 11, 2675-2685.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 2675-2685
    • Kundu, A.1    Jabbar, M.A.2    Nayak, D.P.3
  • 19
    • 0028069680 scopus 로고
    • Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins
    • Kundu, A., and Nayak, D. P. (1994). Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins. J. Virol. 68, 1812-1818.
    • (1994) J. Virol. , vol.68 , pp. 1812-1818
    • Kundu, A.1    Nayak, D.P.2
  • 20
    • 0033568078 scopus 로고    scopus 로고
    • The signal for clathrin-mediated endocytosis of the paramyxovirus SV5 HN protein resides at the transmembrane domain-ectodomain boundary region
    • Leser, G. P., Ector, K. J., Ng, D. T., Shaughnessy, M. A., and Lamb, R. A. (1999). The signal for clathrin-mediated endocytosis of the paramyxovirus SV5 HN protein resides at the transmembrane domain-ectodomain boundary region. Virology 262, 79-92.
    • (1999) Virology , vol.262 , pp. 79-92
    • Leser, G.P.1    Ector, K.J.2    Ng, D.T.3    Shaughnessy, M.A.4    Lamb, R.A.5
  • 21
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin, S., Naim, H. Y., Rodriguez, A. C., and Roth, M. G. (1998). Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell Biol. 142, 51-57.
    • (1998) J. Cell Biol. , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 22
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C., eichelberger, M. C., Compans, R. W., and Air, G. M. (1995). Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J Virol. 69, 1099-1106.
    • (1995) J Virol. , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 23
    • 0028229632 scopus 로고
    • The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells
    • Lodge, R., Gottlinger, H., Gabuzda, D., Cohen, E. A., and Lemay, G. (1994). The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells. J. Virol. 68, 4857-4861.
    • (1994) J. Virol. , vol.68 , pp. 4857-4861
    • Lodge, R.1    Gottlinger, H.2    Gabuzda, D.3    Cohen, E.A.4    Lemay, G.5
  • 24
    • 0031039756 scopus 로고    scopus 로고
    • The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells
    • Lodge, R., Lalonde, J. P., Lemay, G., and Cohen, E. A. (1997). The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells. EMBO J. 16, 695-705.
    • (1997) EMBO J. , vol.16 , pp. 695-705
    • Lodge, R.1    Lalonde, J.P.2    Lemay, G.3    Cohen, E.A.4
  • 25
    • 0031925785 scopus 로고    scopus 로고
    • Polarized budding of measles virus is not determined by viral surface glycoproteins
    • Maisner, A., Klenk, H., and Herrler, G. (1998). Polarized budding of measles virus is not determined by viral surface glycoproteins. J. Virol. 72, 5276-5278.
    • (1998) J. Virol. , vol.72 , pp. 5276-5278
    • Maisner, A.1    Klenk, H.2    Herrler, G.3
  • 26
    • 0030069140 scopus 로고    scopus 로고
    • The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication
    • Mitnaul, L. J., Castrucci, M. R., Murti, K. G., and Kawaoka, Y. (1996). The cytoplasmic tail of influenza A virus neuraminidase (NA) affects NA incorporation into virions, virion morphology, and virulence in mice but is not essential for virus replication. J. Virol. 70, 873-879.
    • (1996) J. Virol. , vol.70 , pp. 873-879
    • Mitnaul, L.J.1    Castrucci, M.R.2    Murti, K.G.3    Kawaoka, Y.4
  • 27
    • 0036124420 scopus 로고    scopus 로고
    • Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal
    • Mora, R., Rodriguez-Boulan, E., Palese, P., and Garcia-Sastre, A. (2002). Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal. J. Virol. 76, 3544-3553.
    • (2002) J. Virol. , vol.76 , pp. 3544-3553
    • Mora, R.1    Rodriguez-Boulan, E.2    Palese, P.3    Garcia-Sastre, A.4
  • 28
    • 0002738750 scopus 로고    scopus 로고
    • Virus morphology, replication and assembly
    • C. J. Hurst, Ed. Academic Press, San Diego
    • Nayak, D. P. (2000). Virus morphology, replication and assembly. In "Viral Ecology" (C. J. Hurst, Ed.), pp. 64-123. Academic Press, San Diego.
    • (2000) Viral Ecology , pp. 64-123
    • Nayak, D.P.1
  • 29
    • 0034679785 scopus 로고    scopus 로고
    • Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells
    • Naim, H. Y., Ehler, E., and Billeter, M. A. (2000). Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells. EMBO J. 19, 3576-3585.
    • (2000) EMBO J. , vol.19 , pp. 3576-3585
    • Naim, H.Y.1    Ehler, E.2    Billeter, M.A.3
  • 31
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen, O. H., and Hildreth, J. E. K. (2000). Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 74, 3264-3272.
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, O.H.1    Hildreth, J.E.K.2
  • 32
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., Yamamura, K., and Miyazaki, J. (1991). Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108, 193-199.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 33
    • 0025822399 scopus 로고
    • Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells
    • Owens, R. J., Dubay, J. W., Hunter, E., and Compans, R. W. (1991). Human immunodeficiency virus envelope protein determines the site of virus release in polarized epithelial cells. Proc. Natl. Acad. Sci. USA 88, 3987-3991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3987-3991
    • Owens, R.J.1    Dubay, J.W.2    Hunter, E.3    Compans, R.W.4
  • 34
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., Tobita, K., Ueda, M., and Compans, R. W. (1974). Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61, 397-410.
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 35
    • 0023021602 scopus 로고
    • Formation of influenza virus particles lacking hemagglutinin on the viral envelope
    • Pattnaik, A. K., Brown, D. J., and Nayak, D. P. (1986). Formation of influenza virus particles lacking hemagglutinin on the viral envelope. J. Virol. 60, 994-1001.
    • (1986) J. Virol. , vol.60 , pp. 994-1001
    • Pattnaik, A.K.1    Brown, D.J.2    Nayak, D.P.3
  • 36
    • 0031846868 scopus 로고    scopus 로고
    • Retention of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum does not redirect virus assembly from the plasma membrane
    • Salzwedel, K., West, J. T., Jr., Mulligan, M. J., and Hunter, E. (1998). Retention of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum does not redirect virus assembly from the plasma membrane. J. Virol. 72, 7523-7531.
    • (1998) J. Virol. , vol.72 , pp. 7523-7531
    • Salzwedel, K.1    West J.T., Jr.2    Mulligan, M.J.3    Hunter, E.4
  • 37
    • 0033989064 scopus 로고    scopus 로고
    • Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: Characterization of a potential site of virus assembly
    • Sanchez, V., Greis, K. D., Sztul, E., and Britt, W. J. (2000). Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: Characterization of a potential site of virus assembly. J. Virol. 74, 975-986.
    • (2000) J. Virol. , vol.74 , pp. 975-986
    • Sanchez, V.1    Greis, K.D.2    Sztul, E.3    Britt, W.J.4
  • 38
    • 0035148474 scopus 로고    scopus 로고
    • Sorting of marburg virus surface protein and virus release take place at opposite surfaces of infected polarized epithelial cells
    • Sanger, C., Muhlberger, E., Ryabchikova, E., Kolesnikova, L., Klenk, H. D., and Becker, S. (2001). Sorting of marburg virus surface protein and virus release take place at opposite surfaces of infected polarized epithelial cells. J. Virol. 75, 1274-1283.
    • (2001) J. Virol. , vol.75 , pp. 1274-1283
    • Sanger, C.1    Muhlberger, E.2    Ryabchikova, E.3    Kolesnikova, L.4    Klenk, H.D.5    Becker, S.6
  • 39
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and Sommer, S. S. (1990). The "megaprimer" method of site-directed mutagenesis. Biotechniques 8, 404-407.
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 40
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., Rietveld, A., Wilk, T., and Simons, K. (1999). Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. BioI. Chem. 274, 2038-2044.
    • (1999) J. BioI. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 41
    • 0000874599 scopus 로고
    • Growing Madin-Darby canine kidney cells for studying epithelial cell biology
    • J. E. Celis, Ed. Academic Press, New York
    • Simon, K., and Virta, H. (1994). Growing Madin-Darby canine kidney cells for studying epithelial cell biology. In "Cell Biology: A Laboratory Handbook" (J. E. Celis, Ed.), pp. 225-231. Academic Press, New York.
    • (1994) Cell Biology: A Laboratory Handbook , pp. 225-231
    • Simon, K.1    Virta, H.2
  • 42
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas, D. C., Brewer, C. B., and Roth, M. G. (1993). Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J. Biol. Chem. 268, 3313-3320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 43
    • 0016801782 scopus 로고
    • Plaque assay and primary isolation of influenza A viruses in an established line of canine kidney cells (MDCK) in the presence of trypsin
    • Tobita, K., Sugiura, A., Enomote, C., and Furuyama, M. (1975). Plaque assay and primary isolation of influenza A viruses in an established line of canine kidney cells (MDCK) in the presence of trypsin. Med. Microbiol. Immunol. (Berl.) 30, 9-14.
    • (1975) Med. Microbiol. Immunol. (Berl.) , vol.30 , pp. 9-14
    • Tobita, K.1    Sugiura, A.2    Enomote, C.3    Furuyama, M.4
  • 44
    • 0035017262 scopus 로고    scopus 로고
    • Influenza A virus can undergo multiple cycles of replication without M2 ion channel activity
    • Watanabe, T., Watanabe, S., Ito, H., Kida, H., and Kawaoka, Y. (2001). Influenza A virus can undergo multiple cycles of replication without M2 ion channel activity. J. Virol. 75, 5656-5662.
    • (2001) J. Virol. , vol.75 , pp. 5656-5662
    • Watanabe, T.1    Watanabe, S.2    Ito, H.3    Kida, H.4    Kawaoka, Y.5
  • 45
    • 0034630492 scopus 로고    scopus 로고
    • The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging
    • Zhang, J., Leser, G. P., Pekosz, A., and Lamb, R. A. (2000a). The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging. Virology 269, 325-334.
    • (2000) Virology , vol.269 , pp. 325-334
    • Zhang, J.1    Leser, G.P.2    Pekosz, A.3    Lamb, R.A.4
  • 46
    • 0033995067 scopus 로고    scopus 로고
    • Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins
    • Zhang, J., Pekosz, A., and Lamb, R. A. (2000b). Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins. J. Virol. 74, 4634-4644.
    • (2000) J. Virol. , vol.74 , pp. 4634-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3
  • 47
    • 0036199454 scopus 로고    scopus 로고
    • Vesicular somatitis virus glycoprotein does not determine the site of virus release in polarized epithelial cells
    • Zimmer, G., Zimmer K.-P., Trotz, I., and Herrler, G. (2002). Vesicular somatitis virus glycoprotein does not determine the site of virus release in polarized epithelial cells. J. Virol. 76, 4103-4107.
    • (2002) J. Virol. , vol.76 , pp. 4103-4107
    • Zimmer, G.1    Zimmer, K.-P.2    Trotz, I.3    Herrler, G.4
  • 48
    • 0026557513 scopus 로고
    • Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues
    • Zurzolo, C., Polistina, C., Saini, M., Gentile, R., Aloj, L., Migliaccio, G., Bonatti, S., and Nitsch, L. (1992). Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues. J. Cell Biol. 117, 551-564.
    • (1992) J. Cell Biol. , vol.117 , pp. 551-564
    • Zurzolo, C.1    Polistina, C.2    Saini, M.3    Gentile, R.4    Aloj, L.5    Migliaccio, G.6    Bonatti, S.7    Nitsch, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.