메뉴 건너뛰기




Volumn 64, Issue , 2005, Pages 383-416

Influenza Virus Assembly and Budding at the Viral Budozone

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN;

EID: 26944491901     PISSN: 00653527     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3527(05)64012-2     Document Type: Review
Times cited : (88)

References (153)
  • 1
    • 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. Influenza virus assembly: Effect of influenza virus glycoproteins on the membrane association of M1 protein. J. Virol. 74 (2000) 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
    • 0035864293 scopus 로고    scopus 로고
    • Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer
    • Arzt S., Baudin F., Barge A., Timmins P., Burmeister W.P., and Ruigrok R.W. Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer. Virology 279 (2001) 439-446
    • (2001) Virology , vol.279 , pp. 439-446
    • Arzt, S.1    Baudin, F.2    Barge, A.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6
  • 4
    • 1642553530 scopus 로고    scopus 로고
    • Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2)
    • Arzt S., Petit I., Burmeister W.P., Ruigrok R.W., and Baudin F. Structure of a knockout mutant of influenza virus M1 protein that has altered activities in membrane binding, oligomerisation and binding to NEP (NS2). Virus Res. 99 (2004) 115-119
    • (2004) Virus Res. , vol.99 , pp. 115-119
    • Arzt, S.1    Petit, I.2    Burmeister, W.P.3    Ruigrok, R.W.4    Baudin, F.5
  • 5
    • 0030966390 scopus 로고    scopus 로고
    • Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells
    • Avalos R.T., Yu Z., and Nayak D.P. Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells. J. Virol. 71 (1997) 2947-2958
    • (1997) J. Virol. , vol.71 , pp. 2947-2958
    • Avalos, R.T.1    Yu, Z.2    Nayak, D.P.3
  • 6
    • 2342585501 scopus 로고    scopus 로고
    • Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding
    • Barman S., Adhikary L., Chakrabarti A.K., Bernas C., Kawaoka Y., and Nayak D.P. Role of transmembrane domain and cytoplasmic tail amino acid sequences of influenza a virus neuraminidase in raft association and virus budding. J. Virol. 78 (2004) 5258-5269
    • (2004) J. Virol. , vol.78 , pp. 5258-5269
    • Barman, S.1    Adhikary, L.2    Chakrabarti, A.K.3    Bernas, C.4    Kawaoka, Y.5    Nayak, D.P.6
  • 7
    • 0037225270 scopus 로고    scopus 로고
    • Influenza A virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza A virus in polarized MDCK cells
    • Barman S., Adhikary L., Kawaoka Y., and Nayak D.P. Influenza A virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza A virus in polarized MDCK cells. Virology 305 (2003) 138-152
    • (2003) Virology , vol.305 , pp. 138-152
    • Barman, S.1    Adhikary, L.2    Kawaoka, Y.3    Nayak, D.P.4
  • 8
    • 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. Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses. Virus Res. 77 (2001) 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
  • 9
    • 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. Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association. J. Virol. 74 (2000) 6538-6545
    • (2000) J. Virol. , vol.74 , pp. 6538-6545
    • Barman, S.1    Nayak, D.P.2
  • 10
    • 0035264603 scopus 로고    scopus 로고
    • In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein
    • Baudin F., Petit I., Weissenhorn W., and Ruigrok R.W. In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein. Virology 281 (2001) 102-108
    • (2001) Virology , vol.281 , pp. 102-108
    • Baudin, F.1    Petit, I.2    Weissenhorn, W.3    Ruigrok, R.W.4
  • 11
    • 0037370304 scopus 로고    scopus 로고
    • Reverse genetics studies on the filamentous morphology of influenza A virus
    • Bourmakina S.V., and Garcia-Sastre A. Reverse genetics studies on the filamentous morphology of influenza A virus. J. Gen. Virol. 84 (2003) 517-527
    • (2003) J. Gen. Virol. , vol.84 , pp. 517-527
    • Bourmakina, S.V.1    Garcia-Sastre, A.2
  • 12
    • 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. A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114 (1991) 413-421
    • (1991) J. Cell Biol. , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 13
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown D.A., and London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275 (2000) 17221-17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 14
    • 85047694808 scopus 로고    scopus 로고
    • A novel method for analysis of membrane microdomains: Vesicular stomatitis virus glycoprotein microdomains change in size during infection, and those outside of budding sites resemble sites of virus budding
    • Brown E.L., and Lyles D.S. A novel method for analysis of membrane microdomains: Vesicular stomatitis virus glycoprotein microdomains change in size during infection, and those outside of budding sites resemble sites of virus budding. Virology 310 (2003) 343-358
    • (2003) Virology , vol.310 , pp. 343-358
    • Brown, E.L.1    Lyles, D.S.2
  • 15
    • 0024347714 scopus 로고
    • M protein (M1) of influenza virus: Antigenic analysis and intracellular localization with monoclonal antibodies
    • Bucher D., Popple S., Baer M., Mikhail A., Gong Y.F., Whitaker C., Paoletti E., and Judd A. M protein (M1) of influenza virus: Antigenic analysis and intracellular localization with monoclonal antibodies. J. Virol. 63 (1989) 3622-3633
    • (1989) J. Virol. , vol.63 , pp. 3622-3633
    • Bucher, D.1    Popple, S.2    Baer, M.3    Mikhail, A.4    Gong, Y.F.5    Whitaker, C.6    Paoletti, E.7    Judd, A.8
  • 17
    • 0029861558 scopus 로고    scopus 로고
    • Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins
    • Bui M., Whittaker G., and Helenius A. Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteins. J. Virol. 70 (1996) 8391-8401
    • (1996) J. Virol. , vol.70 , pp. 8391-8401
    • Bui, M.1    Whittaker, G.2    Helenius, A.3
  • 18
    • 0033946767 scopus 로고    scopus 로고
    • Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins
    • Bui M., Wills E.G., Helenius A., and Whittaker G.R. Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins. J. Virol. 74 (2000) 1781-1786
    • (2000) J. Virol. , vol.74 , pp. 1781-1786
    • Bui, M.1    Wills, E.G.2    Helenius, A.3    Whittaker, G.R.4
  • 19
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • Chazal N., and Gerlier D. Virus entry, assembly, budding, and membrane rafts. Microbiol. Mol. Biol. Rev. 67 (2003) 226-237
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 226-237
    • Chazal, N.1    Gerlier, D.2
  • 20
    • 0000283734 scopus 로고
    • Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: Independence to morphological and functional traits
    • Choppin P.W., Murphy J.S., and Tamm I. Studies of two kinds of virus particles which comprise influenza A2 virus strains. III. Morphological characteristics: Independence to morphological and functional traits. J. Exp. Med. 112 (1960) 945-952
    • (1960) J. Exp. Med. , vol.112 , pp. 945-952
    • Choppin, P.W.1    Murphy, J.S.2    Tamm, I.3
  • 21
    • 0000443647 scopus 로고
    • Filamentous forms associated with newly isolated influenza virus
    • Chu C.M., Dawson I.M., and Elford W.J. Filamentous forms associated with newly isolated influenza virus. Lancet 1 (1949) 602-603
    • (1949) Lancet , vol.1 , pp. 602-603
    • Chu, C.M.1    Dawson, I.M.2    Elford, W.J.3
  • 22
    • 0029123983 scopus 로고
    • Virus entry and release in polarized epithelial cells
    • Compans R.W. Virus entry and release in polarized epithelial cells. Curr. Top. Microbiol. Immunol. 202 (1995) 209-219
    • (1995) Curr. Top. Microbiol. Immunol. , vol.202 , pp. 209-219
    • Compans, R.W.1
  • 23
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans R.W., Content J., and Duesberg P.H. Structure of the ribonucleoprotein of influenza virus. J. Virol. 10 (1972) 795-800
    • (1972) J. Virol. , vol.10 , pp. 795-800
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 24
    • 0033050343 scopus 로고    scopus 로고
    • Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras
    • Craven R.C., Harty R.N., Paragas J., Palese P., and Wills J.W. Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J. Virol. 73 (1999) 3359-3365
    • (1999) J. Virol. , vol.73 , pp. 3359-3365
    • Craven, R.C.1    Harty, R.N.2    Paragas, J.3    Palese, P.4    Wills, J.W.5
  • 25
    • 1642274781 scopus 로고    scopus 로고
    • The M1 matrix protein controls the filamentous phenotype of influenza A virus
    • Elleman C.J., and Barclay W.S. The M1 matrix protein controls the filamentous phenotype of influenza A virus. Virology 321 (2004) 144-153
    • (2004) Virology , vol.321 , pp. 144-153
    • Elleman, C.J.1    Barclay, W.S.2
  • 26
    • 0030749976 scopus 로고    scopus 로고
    • Influenza virus M1 protein binds to RNA through its nuclear localization signal
    • Elster C., Larsen K., Gagnon J., Ruigrok R.W., and Baudin F. Influenza virus M1 protein binds to RNA through its nuclear localization signal. J. Gen. Virol. 78 (1997) 1589-1596
    • (1997) J. Gen. Virol. , vol.78 , pp. 1589-1596
    • Elster, C.1    Larsen, K.2    Gagnon, J.3    Ruigrok, R.W.4    Baudin, F.5
  • 27
    • 0034749515 scopus 로고    scopus 로고
    • Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway
    • Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J., and Digard P. Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J. Virol. 75 (2001) 408-419
    • (2001) J. Virol. , vol.75 , pp. 408-419
    • Elton, D.1    Simpson-Holley, M.2    Archer, K.3    Medcalf, L.4    Hallam, R.5    McCauley, J.6    Digard, P.7
  • 28
    • 0029794377 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein
    • Enami M., and Enami K. Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein. J. Virol. 70 (1996) 6653-6657
    • (1996) J. Virol. , vol.70 , pp. 6653-6657
    • Enami, M.1    Enami, K.2
  • 29
    • 0025951699 scopus 로고
    • An influenza virus containing nine different RNA segments
    • Enami M., Sharma G., Benham C., and Palese P. An influenza virus containing nine different RNA segments. Virology 185 (1991) 291-298
    • (1991) Virology , vol.185 , pp. 291-298
    • Enami, M.1    Sharma, G.2    Benham, C.3    Palese, P.4
  • 30
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed E.O. Viral late domains. J. Virol. 76 (2002) 4679-4687
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 32
    • 0027999159 scopus 로고
    • Use of a mammalian internal ribosomal entry site element for expression of a foreign protein by a transfectant influenza virus
    • Garcia-Sastre A., Muster T., Barclay W.S., Percy N., and Palese P. Use of a mammalian internal ribosomal entry site element for expression of a foreign protein by a transfectant influenza virus. J. Virol. 68 (1994) 6254-6261
    • (1994) J. Virol. , vol.68 , pp. 6254-6261
    • Garcia-Sastre, A.1    Muster, T.2    Barclay, W.S.3    Percy, N.4    Palese, P.5
  • 33
    • 0029014741 scopus 로고
    • The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes
    • Garcia-Sastre A., and Palese P. The cytoplasmic tail of the neuraminidase protein of influenza A virus does not play an important role in the packaging of this protein into viral envelopes. Virus Res. 37 (1995) 37-47
    • (1995) Virus Res. , vol.37 , pp. 37-47
    • Garcia-Sastre, A.1    Palese, P.2
  • 35
    • 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. Influenza virus matrix protein is the major driving force in virus budding. J. Virol. 74 (2000) 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
  • 36
    • 0344654762 scopus 로고    scopus 로고
    • Efficient formation of influenza virus-like particles: Dependence on the expression levels of viral proteins
    • Gomez-Puertas P., Mena I., Castillo M., Vivo A., Perez-Pastrana E., and Portela A. Efficient formation of influenza virus-like particles: Dependence on the expression levels of viral proteins. J. Gen. Virol. 80 (1999) 1635-1645
    • (1999) J. Gen. Virol. , vol.80 , pp. 1635-1645
    • Gomez-Puertas, P.1    Mena, I.2    Castillo, M.3    Vivo, A.4    Perez-Pastrana, E.5    Portela, A.6
  • 37
    • 0026317877 scopus 로고
    • Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release
    • Gottlinger H.G., Dorfman T., Sodroski J.G., and Haseltine W.A. Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release. Proc. Natl. Acad. Sci. USA 88 (1991) 3195-3199
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3195-3199
    • Gottlinger, H.G.1    Dorfman, T.2    Sodroski, J.G.3    Haseltine, W.A.4
  • 38
    • 0018965999 scopus 로고
    • Interaction of influenza M protein with viral lipid and phosphatidylcholine vesicles
    • Gregoriades A. Interaction of influenza M protein with viral lipid and phosphatidylcholine vesicles. J. Virol. 36 (1980) 470-479
    • (1980) J. Virol. , vol.36 , pp. 470-479
    • Gregoriades, A.1
  • 39
    • 0019851016 scopus 로고
    • Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion
    • Gregoriades A., and Frangione B. Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion. J. Virol. 40 (1981) 323-328
    • (1981) J. Virol. , vol.40 , pp. 323-328
    • Gregoriades, A.1    Frangione, B.2
  • 40
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
    • Harris A., Forouhar F., Qiu S., Sha B., and Luo M. The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289 (2001) 34-44
    • (2001) Virology , vol.289 , pp. 34-44
    • Harris, A.1    Forouhar, F.2    Qiu, S.3    Sha, B.4    Luo, M.5
  • 42
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • Harty R.N., Brown M.E., Wang G., Huibregtse J., and Hayes F.P. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding. Proc. Natl. Acad. Sci. USA 97 (2000) 13871-13876
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 43
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty R.N., Paragas J., Sudol M., and Palese P. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding. J. Virol. 73 (1999) 2921-2929
    • (1999) J. Virol. , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 44
    • 0002988267 scopus 로고
    • 2 ion channel protein
    • 2 ion channel protein. Semin. Virol. 3 (1992) 21-30
    • (1992) Semin. Virol. , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 46
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius A. Unpacking the incoming influenza virus. Cell 69 (1992) 577-578
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 48
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease
    • Huang M., Orenstein J.M., Martin M.A., and Freed E.O. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing protease. J. Virol. 69 (1995) 6810-6818
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 49
    • 0035450255 scopus 로고    scopus 로고
    • Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
    • Huang X., Liu T., Muller J., Levandowski R.A., and Ye Z. Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology 287 (2001) 405-416
    • (2001) Virology , vol.287 , pp. 405-416
    • Huang, X.1    Liu, T.2    Muller, J.3    Levandowski, R.A.4    Ye, Z.5
  • 50
    • 0034121430 scopus 로고    scopus 로고
    • Influenza A viruses lacking sialidase activity can undergo multiple cycles of replication in cell culture, eggs, or mice
    • Hughes M.T., Matrosovich M., Rodgers M.E., McGregor M., and Kawaoka Y. Influenza A viruses lacking sialidase activity can undergo multiple cycles of replication in cell culture, eggs, or mice. J. Virol. 74 (2000) 5206-5212
    • (2000) J. Virol. , vol.74 , pp. 5206-5212
    • Hughes, M.T.1    Matrosovich, M.2    Rodgers, M.E.3    McGregor, M.4    Kawaoka, Y.5
  • 51
    • 0035080020 scopus 로고    scopus 로고
    • Adaptation of influenza A viruses to cells expressing low levels of sialic acid leads to loss of neuraminidase activity
    • Hughes M.T., McGregor M., Suzuki T., Suzuki Y., and Kawaoka Y. Adaptation of influenza A viruses to cells expressing low levels of sialic acid leads to loss of neuraminidase activity. J. Virol. 75 (2001) 3766-3770
    • (2001) J. Virol. , vol.75 , pp. 3766-3770
    • Hughes, M.T.1    McGregor, M.2    Suzuki, T.3    Suzuki, Y.4    Kawaoka, Y.5
  • 52
    • 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. Expression of the influenza A virus M2 protein is restricted to apical surfaces of polarized epithelial cells. J. Virol. 66 (1992) 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
  • 53
    • 0038618682 scopus 로고    scopus 로고
    • Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs
    • Hui E.K., Barman S., Yang T.Y., and Nayak D.P. Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs. J. Virol. 77 (2003) 7078-7092
    • (2003) J. Virol. , vol.77 , pp. 7078-7092
    • Hui, E.K.1    Barman, S.2    Yang, T.Y.3    Nayak, D.P.4
  • 54
    • 0035950932 scopus 로고    scopus 로고
    • Role of ATP in influenza virus budding
    • Hui E.K., and Nayak D.P. Role of ATP in influenza virus budding. Virology 290 (2001) 329-341
    • (2001) Virology , vol.290 , pp. 329-341
    • Hui, E.K.1    Nayak, D.P.2
  • 55
    • 0033775605 scopus 로고    scopus 로고
    • Mutations in the PPPY motif of vesicular stomatitis virus matrix protein reduce virus budding by inhibiting a late step in virion release
    • Jayakar H.R., Murti K.G., and Whitt M.A. Mutations in the PPPY motif of vesicular stomatitis virus matrix protein reduce virus budding by inhibiting a late step in virion release. J. Virol. 74 (2000) 9818-9827
    • (2000) J. Virol. , vol.74 , pp. 9818-9827
    • Jayakar, H.R.1    Murti, K.G.2    Whitt, M.A.3
  • 56
    • 0028102718 scopus 로고
    • The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity
    • Jin H., Leser G.P., and Lamb R.A. The influenza virus hemagglutinin cytoplasmic tail is not essential for virus assembly or infectivity. EMBO J. 13 (1994) 5504-5515
    • (1994) EMBO J. , vol.13 , pp. 5504-5515
    • Jin, H.1    Leser, G.P.2    Lamb, R.A.3
  • 57
    • 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. Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J. 16 (1997) 1236-1247
    • (1997) EMBO J. , vol.16 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 58
    • 0021809311 scopus 로고
    • Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells
    • Jones L.V., Compans R.W., Davis A.R., Bos T.J., and Nayak D.P. Surface expression of influenza virus neuraminidase, an amino-terminally anchored viral membrane glycoprotein, in polarized epithelial cells. Mol. Cell. Biol. 5 (1985) 2181-2189
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 2181-2189
    • Jones, L.V.1    Compans, R.W.2    Davis, A.R.3    Bos, T.J.4    Nayak, D.P.5
  • 59
    • 0347380840 scopus 로고    scopus 로고
    • The ubiquitin-vacuolar protein sorting system is selectively required during entry of influenza virus into host cells
    • Khor R., McElroy L.J., and Whittaker G.R. The ubiquitin-vacuolar protein sorting system is selectively required during entry of influenza virus into host cells. Traffic 4 (2003) 857-868
    • (2003) Traffic , vol.4 , pp. 857-868
    • Khor, R.1    McElroy, L.J.2    Whittaker, G.R.3
  • 60
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for Gag budding from cells
    • Kikonyogo A., Bouamr F., Vana M.L., Xiang Y., Aiyar A., Carter C., and Leis J. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for Gag budding from cells. Proc. Natl. Acad. Sci. USA 98 (2001) 11199-11204
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11199-11204
    • Kikonyogo, A.1    Bouamr, F.2    Vana, M.L.3    Xiang, Y.4    Aiyar, A.5    Carter, C.6    Leis, J.7
  • 61
    • 0000128765 scopus 로고
    • Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits: Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8
    • Kilbourne E.D., and Murphy J.S. Genetic studies of influenza viruses. I. Viral morphology and growth capacity as exchangeable genetic traits: Rapid in ovo adaptation of early passage Asian strain isolates by combination with PR8. J. Exp. Med. 111 (1960) 387-406
    • (1960) J. Exp. Med. , vol.111 , pp. 387-406
    • Kilbourne, E.D.1    Murphy, J.S.2
  • 62
    • 0029905294 scopus 로고    scopus 로고
    • Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins
    • Kretzschmar E., Bui M., and Rose J.K. Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins. Virology 220 (1996) 37-45
    • (1996) Virology , vol.220 , pp. 37-45
    • Kretzschmar, E.1    Bui, M.2    Rose, J.K.3
  • 63
    • 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. Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70 (1996) 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
  • 64
    • 0020696905 scopus 로고
    • The gene structure and replication of influenza virus
    • Lamb R.A., and Choppin P.W. The gene structure and replication of influenza virus. Annu. Rev. Biochem. 52 (1983) 467-506
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 467-506
    • Lamb, R.A.1    Choppin, P.W.2
  • 65
    • 0001178029 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Knipe D., and Howley P. (Eds), Lippincott Williams & Wilkins, Philadelphia, PA
    • Lamb R.A., and Krug R.M. Orthomyxoviridae: The viruses and their replication. In: Knipe D., and Howley P. (Eds). "Field's Virology". 4th Ed. (2001), Lippincott Williams & Wilkins, Philadelphia, PA 1487-1532
    • (2001) "Field's Virology". 4th Ed. , pp. 1487-1532
    • Lamb, R.A.1    Krug, R.M.2
  • 66
    • 0003156040 scopus 로고
    • 2 ion channel protein and its role in the influenza virus life cycle
    • Wimmer E. (Ed), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • 2 ion channel protein and its role in the influenza virus life cycle. In: Wimmer E. (Ed). "Receptor-mediated virus entry into cells" (1994), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 303-321
    • (1994) "Receptor-mediated virus entry into cells" , pp. 303-321
    • Lamb, R.A.1    Holsinger, L.J.2    Pinto, L.H.3
  • 67
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham T., and Galarza J.M. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J. Virol. 75 (2001) 6154-6165
    • (2001) J. Virol. , vol.75 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 68
    • 0029042229 scopus 로고
    • Electroporation of influenza virus ribonucleoprotein complexes for rescue of the nucleoprotein and matrix genes
    • Li S., Xu M., and Coelingh K. Electroporation of influenza virus ribonucleoprotein complexes for rescue of the nucleoprotein and matrix genes. Virus Res. 37 (1995) 153-161
    • (1995) Virus Res. , vol.37 , pp. 153-161
    • Li, S.1    Xu, M.2    Coelingh, K.3
  • 69
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Licata J.M., Simpson-Holley M., Wright N.T., Han Z., Paragas J., and Harty R.N. Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4. J. Virol. 77 (2003) 1812-1819
    • (2003) J. Virol. , vol.77 , pp. 1812-1819
    • Licata, J.M.1    Simpson-Holley, M.2    Wright, N.T.3    Han, Z.4    Paragas, J.5    Harty, R.N.6
  • 70
    • 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. 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 (1998) 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
  • 71
    • 0027261465 scopus 로고
    • Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes
    • Liu C., and Air G.M. Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194 (1993) 403-407
    • (1993) Virology , vol.194 , pp. 403-407
    • Liu, C.1    Air, G.M.2
  • 72
    • 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. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69 (1995) 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
  • 73
    • 0036935791 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins may control viral growth and morphology
    • Liu T., Muller J., and Ye Z. Association of influenza virus matrix protein with ribonucleoproteins may control viral growth and morphology. Virology 304 (2002) 89-96
    • (2002) Virology , vol.304 , pp. 89-96
    • Liu, T.1    Muller, J.2    Ye, Z.3
  • 74
    • 0036891870 scopus 로고    scopus 로고
    • Restriction of viral replication by mutation of the influenza virus matrix protein
    • Liu T., and Ye Z. Restriction of viral replication by mutation of the influenza virus matrix protein. J. Virol. 76 (2002) 13055-13061
    • (2002) J. Virol. , vol.76 , pp. 13055-13061
    • Liu, T.1    Ye, Z.2
  • 75
    • 0018330439 scopus 로고
    • Biosynthesis of the influenza virus envelope in abortive infection
    • Lohmeyer J., Talens L.T., and Klenk H.D. Biosynthesis of the influenza virus envelope in abortive infection. J. Gen. Virol. 42 (1979) 73-88
    • (1979) J. Gen. Virol. , vol.42 , pp. 73-88
    • Lohmeyer, J.1    Talens, L.T.2    Klenk, H.D.3
  • 76
    • 0024846089 scopus 로고
    • Amplification, expression, and packaging of foreign gene by influenza virus
    • Luytjes W., Krystal M., Enami M., Pavin J.D., and Palese P. Amplification, expression, and packaging of foreign gene by influenza virus. Cell 59 (1989) 1107-1113
    • (1989) Cell , vol.59 , pp. 1107-1113
    • Luytjes, W.1    Krystal, M.2    Enami, M.3    Pavin, J.D.4    Palese, P.5
  • 77
    • 0031925785 scopus 로고    scopus 로고
    • Polarized budding of measles virus is not determined by viral surface glycoproteins
    • Maisner A., Klenk H., and Herrler G. Polarized budding of measles virus is not determined by viral surface glycoproteins. J. Virol. 72 (1998) 5276-5278
    • (1998) J. Virol. , vol.72 , pp. 5276-5278
    • Maisner, A.1    Klenk, H.2    Herrler, G.3
  • 78
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import
    • Martin K., and Helenius A. Nuclear transport of influenza virus ribonucleoproteins: The viral matrix protein (M1) promotes export and inhibits import. Cell 67 (1991) 117-130
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 80
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • Martin-Serrano J., Perez-Caballero D., and Bieniasz P.D. Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78 (2004) 5554-5563
    • (2004) J. Virol. , vol.78 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 81
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano J., Yarovoy A., Perez-Caballero D., and Bieniasz P.D. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100 (2003) 12414-12419
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 82
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J., Zang T., and Bieniasz P.D. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7 (2001) 1313-1319
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 83
    • 0030001116 scopus 로고    scopus 로고
    • Rescue of a synthetic chloramphenicol acetyltransferase RNA into influenza virus-like particles obtained from recombinant plasmids
    • Mena I., Vivo A., Perez E., and Portela A. Rescue of a synthetic chloramphenicol acetyltransferase RNA into influenza virus-like particles obtained from recombinant plasmids. J. Virol. 70 (1996) 5016-5024
    • (1996) J. Virol. , vol.70 , pp. 5016-5024
    • Mena, I.1    Vivo, A.2    Perez, E.3    Portela, A.4
  • 84
    • 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. 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 (1996) 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
  • 85
    • 0035947572 scopus 로고    scopus 로고
    • A single amino acid change in the cytoplasmic domains of measles virus glycoproteins H and F alters targeting, endocytosis, and cell fusion in polarized Madin-Darby canine kidney cells
    • Moll M., Klenk H.D., Herrler G., and Maisner A. A single amino acid change in the cytoplasmic domains of measles virus glycoproteins H and F alters targeting, endocytosis, and cell fusion in polarized Madin-Darby canine kidney cells. J. Biol. Chem. 276 (2001) 17887-17894
    • (2001) J. Biol. Chem. , vol.276 , pp. 17887-17894
    • Moll, M.1    Klenk, H.D.2    Herrler, G.3    Maisner, A.4
  • 86
    • 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. Apical budding of a recombinant influenza A virus expressing a hemagglutinin protein with a basolateral localization signal. J. Virol. 76 (2002) 3544-3553
    • (2002) J. Virol. , vol.76 , pp. 3544-3553
    • Mora, R.1    Rodriguez-Boulan, E.2    Palese, P.3    Garcia-Sastre, A.4
  • 87
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S. Lipid rafts: Elusive or illusive?. Cell 115 (2003) 377-388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 88
    • 0026573109 scopus 로고
    • Composition of the helical internal components of influenza virus as revealed by immunogold labeling/electron microscopy
    • Murti K.G., Brown P.S., Bean Jr. W.J., and Webster R.G. Composition of the helical internal components of influenza virus as revealed by immunogold labeling/electron microscopy. Virology 186 (1992) 294-299
    • (1992) Virology , vol.186 , pp. 294-299
    • Murti, K.G.1    Brown, P.S.2    Bean Jr., W.J.3    Webster, R.G.4
  • 89
    • 0023821183 scopus 로고
    • Localization of RNA polymerases on influenza viral ribonucleoproteins by immunogold labeling
    • Murti K.G., Webster R.G., and Jones I.M. Localization of RNA polymerases on influenza viral ribonucleoproteins by immunogold labeling. Virology 164 (1988) 562-566
    • (1988) Virology , vol.164 , pp. 562-566
    • Murti, K.G.1    Webster, R.G.2    Jones, I.M.3
  • 90
    • 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. Measles virus matrix protein specifies apical virus release and glycoprotein sorting in epithelial cells. EMBO J. 19 (2000) 3576-3585
    • (2000) EMBO J. , vol.19 , pp. 3576-3585
    • Naim, H.Y.1    Ehler, E.2    Billeter, M.A.3
  • 91
    • 0027194751 scopus 로고
    • Basis for selective incorporation of glycoproteins into the influenza virus envelope
    • Naim H.Y., and Roth M.G. Basis for selective incorporation of glycoproteins into the influenza virus envelope. J. Virol. 67 (1993) 4831-4841
    • (1993) J. Virol. , vol.67 , pp. 4831-4841
    • Naim, H.Y.1    Roth, M.G.2
  • 92
    • 0036045120 scopus 로고    scopus 로고
    • Role of lipid rafts in virus assembly and budding
    • Nayak D.P., and Barman S. Role of lipid rafts in virus assembly and budding. Adv. Virus Res. 58 (2002) 1-28
    • (2002) Adv. Virus Res. , vol.58 , pp. 1-28
    • Nayak, D.P.1    Barman, S.2
  • 93
    • 0015456108 scopus 로고
    • Further investigation on the fine structure of influenza virus
    • Nermut M.V. Further investigation on the fine structure of influenza virus. J. Gen. Virol. 17 (1972) 317-331
    • (1972) J. Gen. Virol. , vol.17 , pp. 317-331
    • Nermut, M.V.1
  • 94
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1
    • Neumann G., Hughes M.T., and Kawaoka Y. Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J. 19 (2000) 6751-6758
    • (2000) EMBO J. , vol.19 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 95
    • 0033986824 scopus 로고    scopus 로고
    • Plasmid-driven formation of influenza virus-like particles
    • Neumann G., Watanabe T., and Kawaoka Y. Plasmid-driven formation of influenza virus-like particles. J. Virol. 74 (2000) 547-551
    • (2000) J. Virol. , vol.74 , pp. 547-551
    • Neumann, G.1    Watanabe, T.2    Kawaoka, Y.3
  • 96
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • O'Neill R.E., Talon J., and Palese P. The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J. 17 (1998) 288-296
    • (1998) EMBO J. , vol.17 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 97
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese P., Tobita K., Ueda M., and Compans R.W. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology 61 (1974) 397-410
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 98
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik A., Chau V., and Wills J.W. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. USA 97 (2000) 13069-13074
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 99
    • 0014591650 scopus 로고
    • Isolation and characterization of the ribonucleoprotein of influenza virus
    • Pons M.W., Schulze I.T., Hirst G.K., and Hauser R. Isolation and characterization of the ribonucleoprotein of influenza virus. Virology 39 (1969) 250-259
    • (1969) Virology , vol.39 , pp. 250-259
    • Pons, M.W.1    Schulze, I.T.2    Hirst, G.K.3    Hauser, R.4
  • 101
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle A., Keller P., Florin E.L., Simons K., and Horber J.K. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148 (2000) 997-1008
    • (2000) J. Cell Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 102
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer B.A., Parent L.J., Wills J.W., and Montelaro R.C. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71 (1997) 6541-6546
    • (1997) J. Virol. , vol.71 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 103
    • 0026726876 scopus 로고
    • Nuclear retention of M1 protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins
    • Rey O., and Nayak D.P. Nuclear retention of M1 protein in a temperature-sensitive mutant of influenza (A/WSN/33) virus does not affect nuclear export of viral ribonucleoproteins. J. Virol. 66 (1992) 5815-5824
    • (1992) J. Virol. , vol.66 , pp. 5815-5824
    • Rey, O.1    Nayak, D.P.2
  • 105
    • 0032484479 scopus 로고    scopus 로고
    • The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation
    • Roberts P.C., Lamb R.A., and Compans R.W. The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation. Virology 240 (1998) 127-137
    • (1998) Virology , vol.240 , pp. 127-137
    • Roberts, P.C.1    Lamb, R.A.2    Compans, R.W.3
  • 106
    • 0000747079 scopus 로고
    • Asymmetric budding of viruses in epithelial monlayers: A model system for study of epithelial polarity
    • Rodriguez-Boulan E., and Sabatini D.D. Asymmetric budding of viruses in epithelial monlayers: A model system for study of epithelial polarity. Proc. Natl. Acad. Sci. USA 75 (1978) 5071-5075
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5071-5075
    • Rodriguez-Boulan, E.1    Sabatini, D.D.2
  • 107
    • 0020770621 scopus 로고
    • Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA
    • Roth M.G., Compans R.W., Giusti L., Davis A.R., Nayak D.P., Gething M.J., and Sambrook J. Influenza virus hemagglutinin expression is polarized in cells infected with recombinant SV40 viruses carrying cloned hemagglutinin DNA. Cell 33 (1983) 435-443
    • (1983) Cell , vol.33 , pp. 435-443
    • Roth, M.G.1    Compans, R.W.2    Giusti, L.3    Davis, A.R.4    Nayak, D.P.5    Gething, M.J.6    Sambrook, J.7
  • 109
    • 0024443823 scopus 로고
    • Electron microscopy of the influenza virus submembranal structure
    • Ruigrok R.W., Calder L.J., and Wharton S.A. Electron microscopy of the influenza virus submembranal structure. Virology 173 (1989) 311-316
    • (1989) Virology , vol.173 , pp. 311-316
    • Ruigrok, R.W.1    Calder, L.J.2    Wharton, S.A.3
  • 110
    • 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. Sorting of Marburg virus surface protein and virus release take place at opposite surfaces of infected polarized epithelial cells. J. Virol. 75 (2001) 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
  • 111
    • 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. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274 (1999) 2038-2044
    • (1999) J. Biol. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 112
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele P., Roth M.G., and Simons K. Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16 (1997) 5501-5508
    • (1997) EMBO J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 113
    • 2442690486 scopus 로고    scopus 로고
    • Escaping from the cell: Assembly and budding of negative-strand RNA viruses
    • Schmitt A.P., and Lamb R.A. Escaping from the cell: Assembly and budding of negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 283 (2004) 145-196
    • (2004) Curr. Top. Microbiol. Immunol. , vol.283 , pp. 145-196
    • Schmitt, A.P.1    Lamb, R.A.2
  • 115
    • 0015251886 scopus 로고
    • The structure of influenza virus. II. A model based on the morphology and composition of subviral particles
    • Schulze I.T. The structure of influenza virus. II. A model based on the morphology and composition of subviral particles. Virology 47 (1972) 181-196
    • (1972) Virology , vol.47 , pp. 181-196
    • Schulze, I.T.1
  • 116
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha B., and Luo M. Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nat. Struct. Biol. 4 (1997) 239-244
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 118
    • 1542287451 scopus 로고    scopus 로고
    • Characterization of a neuraminidase-deficient influenza a virus as a potential gene delivery vector and a live vaccine
    • Shinya K., Fujii Y., Ito H., Ito T., and Kawaoka Y. Characterization of a neuraminidase-deficient influenza a virus as a potential gene delivery vector and a live vaccine. J. Virol. 78 (2004) 3083-3088
    • (2004) J. Virol. , vol.78 , pp. 3083-3088
    • Shinya, K.1    Fujii, Y.2    Ito, H.3    Ito, T.4    Kawaoka, Y.5
  • 119
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 120
    • 0036401535 scopus 로고    scopus 로고
    • A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions
    • Simpson-Holley M., Ellis D., Fisher D., Elton D., McCauley J., and Digard P. A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions. Virology 301 (2002) 212-225
    • (2002) Virology , vol.301 , pp. 212-225
    • Simpson-Holley, M.1    Ellis, D.2    Fisher, D.3    Elton, D.4    McCauley, J.5    Digard, P.6
  • 121
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel J.J., and Wiley D.C. Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin. Annu. Rev. Biochem. 69 (2000) 531-569
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 122
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens J.E., Roth M.G., and Matlin K.S. Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108 (1989) 821-832
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 123
    • 0025984080 scopus 로고
    • The genetic aspects of influenza virus filamentous particle formation
    • Smirnov Y.A., Kuznetsova M.A., and Kaverin N.V. The genetic aspects of influenza virus filamentous particle formation. Arch. Virol. 118 (1991) 279-284
    • (1991) Arch. Virol. , vol.118 , pp. 279-284
    • Smirnov, Y.A.1    Kuznetsova, M.A.2    Kaverin, N.V.3
  • 124
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B., Calistri A., Craig S., Popova E., and Gottlinger H.G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114 (2003) 689-699
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 125
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue R.J., and Hay A.J. Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel. Virology 180 (1991) 617-624
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 126
    • 0036789014 scopus 로고    scopus 로고
    • Lipid rafts and assembly of enveloped viruses
    • Suomalainen M. Lipid rafts and assembly of enveloped viruses. Traffic 3 (2002) 705-709
    • (2002) Traffic , vol.3 , pp. 705-709
    • Suomalainen, M.1
  • 127
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda M., Leser G.P., Russell C.J., and Lamb R.A. Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc. Natl. Acad. Sci. USA 100 (2003) 14610-14617
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 128
    • 0036007087 scopus 로고    scopus 로고
    • 2 ion channel activity is essential for efficient replication in tissue culture
    • 2 ion channel activity is essential for efficient replication in tissue culture. J. Virol. 76 (2002) 1391-1399
    • (2002) J. Virol. , vol.76 , pp. 1391-1399
    • Takeda, M.1    Pekosz, A.2    Shuck, K.3    Pinto, L.H.4    Lamb, R.A.5
  • 129
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL
    • Tall R.D., Alonso M.A., and Roth M.G. Features of influenza HA required for apical sorting differ from those required for association with DRMs or MAL. Traffic 4 (2003) 838-849
    • (2003) Traffic , vol.4 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 130
    • 0025194068 scopus 로고
    • Altered budding site of a pantropic mutant of Sendai virus, F1-R, in polarized epithelial cells
    • Tashiro M., Yamakawa M., Tobita K., Seto J.T., Klenk H.D., and Rott R. Altered budding site of a pantropic mutant of Sendai virus, F1-R, in polarized epithelial cells. J. Virol. 64 (1990) 4672-4677
    • (1990) J. Virol. , vol.64 , pp. 4672-4677
    • Tashiro, M.1    Yamakawa, M.2    Tobita, K.3    Seto, J.T.4    Klenk, H.D.5    Rott, R.6
  • 131
    • 0028217859 scopus 로고
    • The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities
    • Thomas D.C., and Roth M.G. The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities. J. Biol. Chem. 269 (1994) 15732-15739
    • (1994) J. Biol. Chem. , vol.269 , pp. 15732-15739
    • Thomas, D.C.1    Roth, M.G.2
  • 133
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., and Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394 (1998) 798-801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 135
    • 0037370013 scopus 로고    scopus 로고
    • YPXL/I is a protein interaction motif recognized by Aspergillus PalA and its human homologue, AIP1/Alix
    • Vincent O., Rainbow L., Tilburn J., Arst Jr. H.N., and Penalva M.A. YPXL/I is a protein interaction motif recognized by Aspergillus PalA and its human homologue, AIP1/Alix. Mol. Cell. Biol. 23 (2003) 1647-1655
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1647-1655
    • Vincent, O.1    Rainbow, L.2    Tilburn, J.3    Arst Jr., H.N.4    Penalva, M.A.5
  • 137
    • 0024454843 scopus 로고
    • RNA-binding properties of influenza A virus matrix protein M1
    • Wakefield L., and Brownlee G.G. RNA-binding properties of influenza A virus matrix protein M1. Nucleic Acids Res. 17 (1989) 8569-8580
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8569-8580
    • Wakefield, L.1    Brownlee, G.G.2
  • 138
    • 0029656043 scopus 로고    scopus 로고
    • Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein
    • Watanabe K., Handa H., Mizumoto K., and Nagata K. Mechanism for inhibition of influenza virus RNA polymerase activity by matrix protein. J. Virol. 70 (1996) 241-247
    • (1996) J. Virol. , vol.70 , pp. 241-247
    • Watanabe, K.1    Handa, H.2    Mizumoto, K.3    Nagata, K.4
  • 139
    • 0036139062 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of replication-incompetent influenza virus-like particles
    • Watanabe T., Watanabe S., Neumann G., Kida H., and Kawaoka Y. Immunogenicity and protective efficacy of replication-incompetent influenza virus-like particles. J. Virol. 76 (2002) 767-773
    • (2002) J. Virol. , vol.76 , pp. 767-773
    • Watanabe, T.1    Watanabe, S.2    Neumann, G.3    Kida, H.4    Kawaoka, Y.5
  • 140
    • 0141856265 scopus 로고    scopus 로고
    • Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes
    • Watanabe T., Watanabe S., Noda T., Fujii Y., and Kawaoka Y. Exploitation of nucleic acid packaging signals to generate a novel influenza virus-based vector stably expressing two foreign genes. J. Virol. 77 (2003) 10575-10583
    • (2003) J. Virol. , vol.77 , pp. 10575-10583
    • Watanabe, T.1    Watanabe, S.2    Noda, T.3    Fujii, Y.4    Kawaoka, Y.5
  • 141
    • 0030069730 scopus 로고    scopus 로고
    • The role of nuclear import and export in influenza virus infection
    • Whittaker G., Bui M., and Helenius A. The role of nuclear import and export in influenza virus infection. Trends Cell Biol. 6 (1996) 67-71
    • (1996) Trends Cell Biol. , vol.6 , pp. 67-71
    • Whittaker, G.1    Bui, M.2    Helenius, A.3
  • 142
    • 0028070639 scopus 로고
    • An assembly domain of the Rous sarcoma virus Gag protein required late in budding
    • Wills J.W., Cameron C.E., Wilson C.B., Xiang Y., Bennett R.P., and Leis J. An assembly domain of the Rous sarcoma virus Gag protein required late in budding. J. Virol. 68 (1994) 6605-6618
    • (1994) J. Virol. , vol.68 , pp. 6605-6618
    • Wills, J.W.1    Cameron, C.E.2    Wilson, C.B.3    Xiang, Y.4    Bennett, R.P.5    Leis, J.6
  • 143
    • 0029978648 scopus 로고    scopus 로고
    • Fine mapping and characterization of the Rous sarcoma virus Pr76gag late assembly domain
    • Xiang Y., Cameron C.E., Wills J.W., and Leis J. Fine mapping and characterization of the Rous sarcoma virus Pr76gag late assembly domain. J. Virol. 70 (1996) 5695-5700
    • (1996) J. Virol. , vol.70 , pp. 5695-5700
    • Xiang, Y.1    Cameron, C.E.2    Wills, J.W.3    Leis, J.4
  • 144
    • 0031550787 scopus 로고    scopus 로고
    • Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses
    • Yang P., Bansal A., Liu C., and Air G.M. Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses. Virology 229 (1997) 155-165
    • (1997) Virology , vol.229 , pp. 155-165
    • Yang, P.1    Bansal, A.2    Liu, C.3    Air, G.M.4
  • 145
    • 0024319381 scopus 로고
    • Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides
    • Ye Z.P., Baylor N.W., and Wagner R.R. Transcription-inhibition and RNA-binding domains of influenza A virus matrix protein mapped with anti-idiotypic antibodies and synthetic peptides. J. Virol. 63 (1989) 3586-3594
    • (1989) J. Virol. , vol.63 , pp. 3586-3594
    • Ye, Z.P.1    Baylor, N.W.2    Wagner, R.R.3
  • 146
    • 0032865668 scopus 로고    scopus 로고
    • Association of influenza virus matrix protein with ribonucleoproteins
    • Ye Z., Liu T., Offringa D.P., McInnis J., and Levandowski R.A. Association of influenza virus matrix protein with ribonucleoproteins. J. Virol. 73 (1999) 7467-7473
    • (1999) J. Virol. , vol.73 , pp. 7467-7473
    • Ye, Z.1    Liu, T.2    Offringa, D.P.3    McInnis, J.4    Levandowski, R.A.5
  • 147
    • 0023106182 scopus 로고
    • Functional and antigenic domains of the matrix (M1) protein of influenza A virus
    • Ye Z.P., Pal R., Fox J.W., and Wagner R.R. Functional and antigenic domains of the matrix (M1) protein of influenza A virus. J. Virol. 61 (1987) 239-246
    • (1987) J. Virol. , vol.61 , pp. 239-246
    • Ye, Z.P.1    Pal, R.2    Fox, J.W.3    Wagner, R.R.4
  • 148
    • 0028835724 scopus 로고
    • Nucleus-targeting domain of the matrix protein (M1) of influenza virus
    • Ye Z., Robinson D., and Wagner R.R. Nucleus-targeting domain of the matrix protein (M1) of influenza virus. J. Virol. 69 (1995) 1964-1970
    • (1995) J. Virol. , vol.69 , pp. 1964-1970
    • Ye, Z.1    Robinson, D.2    Wagner, R.R.3
  • 149
    • 0023820458 scopus 로고
    • Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions
    • Zebedee S.L., and Lamb R.A. Influenza A virus M2 protein: Monoclonal antibody restriction of virus growth and detection of M2 in virions. J. Virol. 62 (1988) 2762-2772
    • (1988) J. Virol. , vol.62 , pp. 2762-2772
    • Zebedee, S.L.1    Lamb, R.A.2
  • 150
    • 0030588962 scopus 로고    scopus 로고
    • Characterization of the membrane association of the influenza virus matrix protein in living cells
    • Zhang J., and Lamb R.A. Characterization of the membrane association of the influenza virus matrix protein in living cells. Virology 225 (1996) 255-266
    • (1996) Virology , vol.225 , pp. 255-266
    • Zhang, J.1    Lamb, R.A.2
  • 151
    • 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. The cytoplasmic tails of the influenza virus spike glycoproteins are required for normal genome packaging. Virology 269 (2000) 325-334
    • (2000) Virology , vol.269 , pp. 325-334
    • Zhang, J.1    Leser, G.P.2    Pekosz, A.3    Lamb, R.A.4
  • 152
    • 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. Influenza virus assembly and lipid raft microdomains: A role for the cytoplasmic tails of the spike glycoproteins. J. Virol. 74 (2000) 4634-4644
    • (2000) J. Virol. , vol.74 , pp. 4634-4644
    • Zhang, J.1    Pekosz, A.2    Lamb, R.A.3
  • 153
    • 0026517512 scopus 로고
    • Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent
    • Zhirnov O.P. Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent. Virology 186 (1992) 324-330
    • (1992) Virology , vol.186 , pp. 324-330
    • Zhirnov, O.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.