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Volumn 65, Issue 2, 2008, Pages 282-294

Structural aspects of rabies virus replication

Author keywords

Influenza virus; Nucleocapsid; Nucleoprotein N; Phosphoprotein P; Rabies virus; VSV

Indexed keywords

PHOSPHOPROTEIN; RNA POLYMERASE; VIRUS NUCLEOPROTEIN; VIRUS RNA;

EID: 38549175260     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-007-7298-1     Document Type: Review
Times cited : (65)

References (81)
  • 1
    • 21344473205 scopus 로고    scopus 로고
    • Replication strategies of rabies virus
    • Finke, S. and Conzelmann, K. K. (2005) Replication strategies of rabies virus. Virus Res. 111, 120-131.
    • (2005) Virus Res , vol.111 , pp. 120-131
    • Finke, S.1    Conzelmann, K.K.2
  • 6
    • 34250658504 scopus 로고    scopus 로고
    • Synchronous cycles of domestic dog rabies in sub-Saharan Africa and the impact of control efforts
    • Hampson, K., Dushoff, J., Bingham, J., Bruckner, G., Ali, Y. H. and Dobson, A. (2007) Synchronous cycles of domestic dog rabies in sub-Saharan Africa and the impact of control efforts. Proc. Natl. Acad. Sci. USA 104, 7717-7722.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7717-7722
    • Hampson, K.1    Dushoff, J.2    Bingham, J.3    Bruckner, G.4    Ali, Y.H.5    Dobson, A.6
  • 7
    • 2342531185 scopus 로고    scopus 로고
    • Vesicular stomatitis virus: Re-inventing the bullet
    • Lichty, B. D., Power, A. T., Stojdl, D. F. and Bell, J. C. (2004) Vesicular stomatitis virus: re-inventing the bullet. Trends Mol. Med. 10, 210-216.
    • (2004) Trends Mol. Med , vol.10 , pp. 210-216
    • Lichty, B.D.1    Power, A.T.2    Stojdl, D.F.3    Bell, J.C.4
  • 8
    • 0032425151 scopus 로고    scopus 로고
    • Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures
    • Iseni, F., Barge, A., Baudin, F., Blondel, D. and Ruigrok, R. W. (1998) Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures. J. Gen. Virol. 79 (Pt 12), 2909-2919.
    • (1998) J. Gen. Virol , vol.79 , Issue.PART 12 , pp. 2909-2919
    • Iseni, F.1    Barge, A.2    Baudin, F.3    Blondel, D.4    Ruigrok, R.W.5
  • 9
    • 0021885051 scopus 로고
    • Mass and molecular composition of vesicular stomatitis virus: A scanning transmission electron microscopy analysis
    • Thomas, D., Newcomb, W. W., Brown, J. C., Wall, J. S., Hainfeld, J. F., Trus, B. L. and Steven, A. C. (1985) Mass and molecular composition of vesicular stomatitis virus: a scanning transmission electron microscopy analysis. J. Virol. 54, 598-607.
    • (1985) J. Virol , vol.54 , pp. 598-607
    • Thomas, D.1    Newcomb, W.W.2    Brown, J.C.3    Wall, J.S.4    Hainfeld, J.F.5    Trus, B.L.6    Steven, A.C.7
  • 10
    • 0023388295 scopus 로고
    • Location of the binding domains for the RNA polymerase L and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus
    • Emerson, S. U. and Schubert, M. (1987) Location of the binding domains for the RNA polymerase L and the ribonucleocapsid template within different halves of the NS phosphoprotein of vesicular stomatitis virus. Proc. Natl. Acad. Sci. USA 84, 5655-5659.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5655-5659
    • Emerson, S.U.1    Schubert, M.2
  • 12
    • 0034617991 scopus 로고    scopus 로고
    • Rabies virus-induced membrane fusion pathway
    • Gaudin, Y. (2000) Rabies virus-induced membrane fusion pathway. J. Cell. Biol. 150, 601-612.
    • (2000) J. Cell. Biol , vol.150 , pp. 601-612
    • Gaudin, Y.1
  • 14
    • 33845992557 scopus 로고    scopus 로고
    • Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus
    • Ogino, T. and Banerjee, A. K. (2007) Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol. Cell 25, 85-97.
    • (2007) Mol. Cell , vol.25 , pp. 85-97
    • Ogino, T.1    Banerjee, A.K.2
  • 15
    • 0019276997 scopus 로고
    • 5′-terminal cap structure in eucaryotic messenger ribonucleic acids
    • Banerjee, A. K. (1980) 5′-terminal cap structure in eucaryotic messenger ribonucleic acids. Microbiol. Rev. 44, 175-205.
    • (1980) Microbiol. Rev , vol.44 , pp. 175-205
    • Banerjee, A.K.1
  • 16
    • 0019524183 scopus 로고
    • Localized attenuation and discontinuous synthesis during vesicular stomatitis virus transcription
    • Iverson, L. E. and Rose, J. K. (1981) Localized attenuation and discontinuous synthesis during vesicular stomatitis virus transcription. Cell 23, 477-484.
    • (1981) Cell , vol.23 , pp. 477-484
    • Iverson, L.E.1    Rose, J.K.2
  • 17
    • 2442666665 scopus 로고    scopus 로고
    • Transcription and replication of nonsegmented negative-strand RNA viruses
    • Whelan, S. P., Barr, J. N. and Wertz, G. W. (2004) Transcription and replication of nonsegmented negative-strand RNA viruses. Curr. Top. Microbiol. Immunol. 283, 61-119.
    • (2004) Curr. Top. Microbiol. Immunol , vol.283 , pp. 61-119
    • Whelan, S.P.1    Barr, J.N.2    Wertz, G.W.3
  • 18
    • 0021794043 scopus 로고
    • Role of the nucleocapsid protein in regulating vesicular stomatitis virus RNA synthesis
    • Arnheiter, H., Davis, N. L., Wertz, G., Schubert, M. and Lazzarini, R. A. (1985) Role of the nucleocapsid protein in regulating vesicular stomatitis virus RNA synthesis. Cell 41, 259-267.
    • (1985) Cell , vol.41 , pp. 259-267
    • Arnheiter, H.1    Davis, N.L.2    Wertz, G.3    Schubert, M.4    Lazzarini, R.A.5
  • 19
    • 0021335460 scopus 로고
    • N protein alone satisfies the requirement for protein synthesis during RNA replication of vesicular stomatitis virus
    • Patton, J. T., Davis, N. L. and Wertz, G. W. (1984) N protein alone satisfies the requirement for protein synthesis during RNA replication of vesicular stomatitis virus. J. Virol. 49, 303-309.
    • (1984) J. Virol , vol.49 , pp. 303-309
    • Patton, J.T.1    Davis, N.L.2    Wertz, G.W.3
  • 20
    • 0023792843 scopus 로고
    • Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA
    • Masters, P. S. and Banerjee, A. K. (1988) Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA. J. Virol. 62, 2658-2664.
    • (1988) J. Virol , vol.62 , pp. 2658-2664
    • Masters, P.S.1    Banerjee, A.K.2
  • 21
    • 0023812912 scopus 로고
    • Kinetic, quantitative, and functional analysis of multiple forms of the vesicular stomatitis virus nucleocapsid protein in infected cells
    • Peluso, R. W. (1988) Kinetic, quantitative, and functional analysis of multiple forms of the vesicular stomatitis virus nucleocapsid protein in infected cells. J. Virol. 62, 2799-2807.
    • (1988) J. Virol , vol.62 , pp. 2799-2807
    • Peluso, R.W.1
  • 22
    • 0023856783 scopus 로고
    • Viral proteins required for the in vitro replication of vesicular stomatitis virus defective interfering particle genome RNA
    • Peluso, R. W. and Moyer, S. A. (1988) Viral proteins required for the in vitro replication of vesicular stomatitis virus defective interfering particle genome RNA. Virology 162, 369-376.
    • (1988) Virology , vol.162 , pp. 369-376
    • Peluso, R.W.1    Moyer, S.A.2
  • 23
    • 35148863197 scopus 로고    scopus 로고
    • Gerard, F. C., Jr., E. D., Albertini, A. A., Gutsche, I., Zaccai, G., Ruigrok, R. W. and Jamin, M. (2007) Unphosphorylated Rhabdoviridae phosphoproteins form elongated dimers in solution. Biochemistry, in press.
    • Gerard, F. C., Jr., E. D., Albertini, A. A., Gutsche, I., Zaccai, G., Ruigrok, R. W. and Jamin, M. (2007) Unphosphorylated Rhabdoviridae phosphoproteins form elongated dimers in solution. Biochemistry, in press.
  • 24
    • 0037455564 scopus 로고    scopus 로고
    • Isolation and characterisation of the rabies virus N degrees-P complex produced in insect cells
    • Mavrakis, M., Iseni, F., Mazza, C., Schoehn, G., Ebel, C., Gentzel, M., Franz, T. and Ruigrok, R. W. (2003) Isolation and characterisation of the rabies virus N degrees-P complex produced in insect cells. Virology 305, 406-414.
    • (2003) Virology , vol.305 , pp. 406-414
    • Mavrakis, M.1    Iseni, F.2    Mazza, C.3    Schoehn, G.4    Ebel, C.5    Gentzel, M.6    Franz, T.7    Ruigrok, R.W.8
  • 25
    • 5144222412 scopus 로고    scopus 로고
    • Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus
    • Mavrakis, M., McCarthy, A. A., Roche, S., Blondel, D. and Ruigrok, R. W. (2004) Structure and function of the C-terminal domain of the polymerase cofactor of rabies virus. J. Mol. Biol. 343, 819-831.
    • (2004) J. Mol. Biol , vol.343 , pp. 819-831
    • Mavrakis, M.1    McCarthy, A.A.2    Roche, S.3    Blondel, D.4    Ruigrok, R.W.5
  • 26
    • 33646861788 scopus 로고    scopus 로고
    • Rabies virus chaperone: Identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA
    • Mavrakis, M., Mehouas, S., Real, E., Iseni, F., Blondel, D., Tordo, N. and Ruigrok, R. W. (2006) Rabies virus chaperone: identification of the phosphoprotein peptide that keeps nucleoprotein soluble and free from non-specific RNA. Virology 349(2), 422-429.
    • (2006) Virology , vol.349 , Issue.2 , pp. 422-429
    • Mavrakis, M.1    Mehouas, S.2    Real, E.3    Iseni, F.4    Blondel, D.5    Tordo, N.6    Ruigrok, R.W.7
  • 27
    • 0028117909 scopus 로고
    • In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): Existence of two N-binding sites on P protein
    • Chenik, M., Chebli, K., Gaudin, Y. and Blondel, D. (1994) In vivo interaction of rabies virus phosphoprotein (P) and nucleoprotein (N): existence of two N-binding sites on P protein. J. Gen. Virol. 75 (Pt 11), 2889-2896.
    • (1994) J. Gen. Virol , vol.75 , Issue.PART 11 , pp. 2889-2896
    • Chenik, M.1    Chebli, K.2    Gaudin, Y.3    Blondel, D.4
  • 28
    • 2442662593 scopus 로고    scopus 로고
    • Association of rabies virus nominal phosphoprotein (P) with viral nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein (N)
    • Toriumi, H. and Kawai, A. (2004) Association of rabies virus nominal phosphoprotein (P) with viral nucleocapsid (NC) is enhanced by phosphorylation of the viral nucleoprotein (N). Microbiol. Immunol. 48, 399-409.
    • (2004) Microbiol. Immunol , vol.48 , pp. 399-409
    • Toriumi, H.1    Kawai, A.2
  • 29
    • 0034749347 scopus 로고    scopus 로고
    • Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site
    • Schoehn, G., Iseni, F., Mavrakis, M., Blondel, D. and Ruigrok, R. W. (2001) Structure of recombinant rabies virus nucleoprotein-RNA complex and identification of the phosphoprotein binding site. J. Virol. 75, 490-498.
    • (2001) J. Virol , vol.75 , pp. 490-498
    • Schoehn, G.1    Iseni, F.2    Mavrakis, M.3    Blondel, D.4    Ruigrok, R.W.5
  • 30
    • 33646539800 scopus 로고    scopus 로고
    • Resolution improvement of X-ray diffraction data of crystals of a vesicular stomatitis virus nucleocapsid protein oligomer complexed with RNA
    • Green, T. J. and Luo, M. (2006) Resolution improvement of X-ray diffraction data of crystals of a vesicular stomatitis virus nucleocapsid protein oligomer complexed with RNA. Acta Crystallogr. D Biol. Crystallogr. 62, 498-504.
    • (2006) Acta Crystallogr. D Biol. Crystallogr , vol.62 , pp. 498-504
    • Green, T.J.1    Luo, M.2
  • 31
    • 0027166165 scopus 로고
    • Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures
    • Fooks, A. R., Stephenson, J. R., Warnes, A., Dowsett, A. B., Rima, B. K. and Wilkinson, G. W. (1993) Measles virus nucleocapsid protein expressed in insect cells assembles into nucleocapsid-like structures. J. Gen. Virol. 74 (Pt 7), 1439-1444.
    • (1993) J. Gen. Virol , vol.74 , Issue.PART 7 , pp. 1439-1444
    • Fooks, A.R.1    Stephenson, J.R.2    Warnes, A.3    Dowsett, A.B.4    Rima, B.K.5    Wilkinson, G.W.6
  • 33
    • 0025983571 scopus 로고
    • Assembly of nucleocapsidlike structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein
    • Spehner, D., Kirn, A. and Drillien, R. (1991) Assembly of nucleocapsidlike structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein. J. Virol. 65, 6296-6300.
    • (1991) J. Virol , vol.65 , pp. 6296-6300
    • Spehner, D.1    Kirn, A.2    Drillien, R.3
  • 36
    • 33947316410 scopus 로고    scopus 로고
    • Isolation and crystallization of a unique size category of recombinant Rabies virus Nucleoprotein-RNA rings
    • Albertini, A. A., Clapier, C. R., Wernimont, A. K., Schoehn, G., Weissenhorn, W. and Ruigrok, R. W. (2007) Isolation and crystallization of a unique size category of recombinant Rabies virus Nucleoprotein-RNA rings. J. Struct. Biol. 158, 129-133.
    • (2007) J. Struct. Biol , vol.158 , pp. 129-133
    • Albertini, A.A.1    Clapier, C.R.2    Wernimont, A.K.3    Schoehn, G.4    Weissenhorn, W.5    Ruigrok, R.W.6
  • 38
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green, T. J., Zhang, X., Wertz, G. W. and Luo, M. (2006) Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313, 357-360.
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 39
    • 33750984771 scopus 로고    scopus 로고
    • Pichlmair, A., Schulz, O., Tan, C. P., Naslund, T. I., Liljestrom, P., Weber, F. and Reis e Sousa, C. (2006) RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science 314, 997-1001.
    • Pichlmair, A., Schulz, O., Tan, C. P., Naslund, T. I., Liljestrom, P., Weber, F. and Reis e Sousa, C. (2006) RIG-I-mediated antiviral responses to single-stranded RNA bearing 5′-phosphates. Science 314, 997-1001.
  • 42
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S., Uematsu, S. and Takeuchi, O. (2006) Pathogen recognition and innate immunity. Cell 124, 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 43
    • 0020714002 scopus 로고
    • N protein of vesicular stomatitis virus selectively encapsidates leader RNA in vitro
    • Blumberg, B. M., Giorgi, C. and Kolakofsky, D. (1983) N protein of vesicular stomatitis virus selectively encapsidates leader RNA in vitro. Cell 32, 559-567.
    • (1983) Cell , vol.32 , pp. 559-567
    • Blumberg, B.M.1    Giorgi, C.2    Kolakofsky, D.3
  • 44
    • 0031924057 scopus 로고    scopus 로고
    • Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA
    • Kouznetzoff, A., Buckle, M. and Tordo, N. (1998) Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA. J. Gen. Virol. 79 (Pt 5), 1005-1013.
    • (1998) J. Gen. Virol , vol.79 , Issue.PART 5 , pp. 1005-1013
    • Kouznetzoff, A.1    Buckle, M.2    Tordo, N.3
  • 46
    • 33646535836 scopus 로고    scopus 로고
    • Initiation of encapsidation as evidenced by deoxycholate-treated Nucleocapsid protein in the Chandipura virus life cycle
    • Bhattacharya, R., Basak, S. and Chattopadhyay, D. J. (2006) Initiation of encapsidation as evidenced by deoxycholate-treated Nucleocapsid protein in the Chandipura virus life cycle. Virology 349, 197-211.
    • (2006) Virology , vol.349 , pp. 197-211
    • Bhattacharya, R.1    Basak, S.2    Chattopadhyay, D.J.3
  • 47
    • 0019490310 scopus 로고
    • Role of the vesicular stomatitis virus matrix protein in maintaining the viral nucleocapsid in the condensed form found in native virions
    • Newcomb, W. W. and Brown, J. C. (1981) Role of the vesicular stomatitis virus matrix protein in maintaining the viral nucleocapsid in the condensed form found in native virions. J. Virol. 39, 295-299.
    • (1981) J. Virol , vol.39 , pp. 295-299
    • Newcomb, W.W.1    Brown, J.C.2
  • 48
    • 0020062026 scopus 로고
    • In vitro reassembly of vesicular stomatitis virus skeletons
    • Newcomb, W. W., Tobin, G. J., McGowan, J. J. and Brown, J. C. (1982) In vitro reassembly of vesicular stomatitis virus skeletons. J. Virol. 41, 1055-1062.
    • (1982) J. Virol , vol.41 , pp. 1055-1062
    • Newcomb, W.W.1    Tobin, G.J.2    McGowan, J.J.3    Brown, J.C.4
  • 50
    • 0030198563 scopus 로고    scopus 로고
    • Reexamination of the Sendai virus P protein domains required for RNA synthesis: A possible supplemental role for the P protein
    • Curran, J. (1996) Reexamination of the Sendai virus P protein domains required for RNA synthesis: a possible supplemental role for the P protein. Virology 221, 130-140.
    • (1996) Virology , vol.221 , pp. 130-140
    • Curran, J.1
  • 51
    • 0015953348 scopus 로고
    • Phosphorylation of vesicular stomatitis virus in vivo and in vitro
    • Moyer, S. A. and Summers, D. F. (1974) Phosphorylation of vesicular stomatitis virus in vivo and in vitro. J. Virol. 13, 455-465.
    • (1974) J. Virol , vol.13 , pp. 455-465
    • Moyer, S.A.1    Summers, D.F.2
  • 53
    • 21444456320 scopus 로고    scopus 로고
    • Paramyxovirus mRNA editing, the 'rule of six' and error catastrophe: A hypothesis
    • Kolakofsky, D., Roux, L., Garcin, D. and Ruigrok, R. W. (2005) Paramyxovirus mRNA editing, the 'rule of six' and error catastrophe: a hypothesis. J. Gen. Virol. 86, 1869-1877.
    • (2005) J. Gen. Virol , vol.86 , pp. 1869-1877
    • Kolakofsky, D.1    Roux, L.2    Garcin, D.3    Ruigrok, R.W.4
  • 54
    • 0034811975 scopus 로고    scopus 로고
    • Functional interaction map of lyssavirus phosphoprotein: Identification of the minimal transcription domains
    • Jacob, Y., Real, E. and Tordo, N. (2001) Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains. J. Virol. 75, 9613-9622.
    • (2001) J. Virol , vol.75 , pp. 9613-9622
    • Jacob, Y.1    Real, E.2    Tordo, N.3
  • 55
    • 0031888561 scopus 로고    scopus 로고
    • Mapping the interacting domains between the rabies virus polymerase and phosphoprotein
    • Chenik, M., Schnell, M., Conzelmann, K. K. and Blondel, D. (1998) Mapping the interacting domains between the rabies virus polymerase and phosphoprotein. J. Virol. 72, 1925-1930.
    • (1998) J. Virol , vol.72 , pp. 1925-1930
    • Chenik, M.1    Schnell, M.2    Conzelmann, K.K.3    Blondel, D.4
  • 57
    • 7644222274 scopus 로고    scopus 로고
    • Tracking fluorescence-labeled rabies virus: Enhanced green fluorescent protein-tagged phosphoprotein P supports virus gene expression and formation of infectious particles
    • Finke, S., Brzozka, K. and Conzelmann, K. K. (2004) Tracking fluorescence-labeled rabies virus: enhanced green fluorescent protein-tagged phosphoprotein P supports virus gene expression and formation of infectious particles. J. Virol. 78, 12333-12343.
    • (2004) J. Virol , vol.78 , pp. 12333-12343
    • Finke, S.1    Brzozka, K.2    Conzelmann, K.K.3
  • 58
    • 33644774586 scopus 로고    scopus 로고
    • Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus
    • Ding, H., Green, T. J., Lu, S. and Luo, M. (2006) Crystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus. J. Virol. 80, 2808-2814.
    • (2006) J. Virol , vol.80 , pp. 2808-2814
    • Ding, H.1    Green, T.J.2    Lu, S.3    Luo, M.4
  • 61
    • 0242582329 scopus 로고    scopus 로고
    • Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein
    • Johansson, K., Bourhis, J. M., Campanacci, V., Cambillau, C., Canard, B. and Longhi, S. (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J. Biol. Chem. 278, 44567-44573.
    • (2003) J. Biol. Chem , vol.278 , pp. 44567-44573
    • Johansson, K.1    Bourhis, J.M.2    Campanacci, V.3    Cambillau, C.4    Canard, B.5    Longhi, S.6
  • 62
    • 34250849555 scopus 로고    scopus 로고
    • Interaction of the C-terminal domains of Sendai virus N and P proteins: Comparison of polymerase-nucleocapsid interactions within the paramyxovirus family
    • Houben, K., Marion, D., Tarbouriech, N., Ruigrok, R. W. and Blanchard, L. (2007) Interaction of the C-terminal domains of Sendai virus N and P proteins: comparison of polymerase-nucleocapsid interactions within the paramyxovirus family. J. Virol. 81, 6807-6816.
    • (2007) J. Virol , vol.81 , pp. 6807-6816
    • Houben, K.1    Marion, D.2    Tarbouriech, N.3    Ruigrok, R.W.4    Blanchard, L.5
  • 63
    • 1342321890 scopus 로고    scopus 로고
    • Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution
    • Blanchard, L., Tarbouriech, N., Blackledge, M., Timmins, P., Burmeister, W. P., Ruigrok, R. W. and Marion, D. (2004) Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. Virology 319, 201-211.
    • (2004) Virology , vol.319 , pp. 201-211
    • Blanchard, L.1    Tarbouriech, N.2    Blackledge, M.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6    Marion, D.7
  • 64
    • 0033776043 scopus 로고    scopus 로고
    • Interaction of the rabies virus P protein with the LC8 dynein light chain
    • Raux, H., Flamand, A. and Blondel, D. (2000) Interaction of the rabies virus P protein with the LC8 dynein light chain. J. Virol. 74, 10212-10216.
    • (2000) J. Virol , vol.74 , pp. 10212-10216
    • Raux, H.1    Flamand, A.2    Blondel, D.3
  • 65
    • 0033775766 scopus 로고    scopus 로고
    • Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein
    • Jacob, Y., Badrane, H., Ceccaldi, P. E. and Tordo, N. (2000) Cytoplasmic dynein LC8 interacts with lyssavirus phosphoprotein. J. Virol. 74, 10217-10222.
    • (2000) J. Virol , vol.74 , pp. 10217-10222
    • Jacob, Y.1    Badrane, H.2    Ceccaldi, P.E.3    Tordo, N.4
  • 66
    • 33745260979 scopus 로고    scopus 로고
    • Visualization of intracellular transport of vesicular stomatitis virus nucleocapsids in living cells
    • Das, S. C., Nayak, D., Zhou, Y. and Pattnaik, A. K. (2006) Visualization of intracellular transport of vesicular stomatitis virus nucleocapsids in living cells. J. Virol. 80, 6368-6377.
    • (2006) J. Virol , vol.80 , pp. 6368-6377
    • Das, S.C.1    Nayak, D.2    Zhou, Y.3    Pattnaik, A.K.4
  • 67
    • 34249851501 scopus 로고    scopus 로고
    • The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription
    • Tan, G. S., Preuss, M. A., Williams, J. C. and Schnell, M. J. (2007) The dynein light chain 8 binding motif of rabies virus phosphoprotein promotes efficient viral transcription. Proc. Natl. Acad. Sci. USA 104, 7229-7234.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7229-7234
    • Tan, G.S.1    Preuss, M.A.2    Williams, J.C.3    Schnell, M.J.4
  • 69
    • 27644546664 scopus 로고    scopus 로고
    • Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways
    • Vidy, A., Chelbi-Alix, M. and Blondel, D. (2005) Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways. J. Virol. 79, 14411-14420.
    • (2005) J. Virol , vol.79 , pp. 14411-14420
    • Vidy, A.1    Chelbi-Alix, M.2    Blondel, D.3
  • 70
    • 33644787054 scopus 로고    scopus 로고
    • Inhibition of interferon signaling by rabies virus phosphoprotein P: Activation-dependent binding of STAT1 and STAT2
    • Brzozka, K., Finke, S. and Conzelmann, K. K. (2006) Inhibition of interferon signaling by rabies virus phosphoprotein P: activation-dependent binding of STAT1 and STAT2. J. Virol. 80, 2675-2683.
    • (2006) J. Virol , vol.80 , pp. 2675-2683
    • Brzozka, K.1    Finke, S.2    Conzelmann, K.K.3
  • 71
    • 0033986999 scopus 로고    scopus 로고
    • The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C
    • Gupta, A. K., Blondel, D., Choudhary, S. and Banerjee, A. K. (2000) The phosphoprotein of rabies virus is phosphorylated by a unique cellular protein kinase and specific isomers of protein kinase C. J. Virol. 74, 91-98.
    • (2000) J. Virol , vol.74 , pp. 91-98
    • Gupta, A.K.1    Blondel, D.2    Choudhary, S.3    Banerjee, A.K.4
  • 72
    • 0028961740 scopus 로고
    • Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II
    • Gao, Y. and Lenard, J. (1995) Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II. Embo J. 14, 1240-1247.
    • (1995) Embo J , vol.14 , pp. 1240-1247
    • Gao, Y.1    Lenard, J.2
  • 73
    • 0026638841 scopus 로고
    • Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P
    • Barik, S. and Banerjee, A. K. (1992) Phosphorylation by cellular casein kinase II is essential for transcriptional activity of vesicular stomatitis virus phosphoprotein P. Proc. Natl. Acad. Sci. USA 89, 6570-6574.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6570-6574
    • Barik, S.1    Banerjee, A.K.2
  • 74
    • 0030000107 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the vesicular stomatitis virus P protein modulates polymerase complex formation but is not essential for transcription or replication
    • Spadafora, D., Canter, D. M., Jackson, R. L. and Perrault, J. (1996) Constitutive phosphorylation of the vesicular stomatitis virus P protein modulates polymerase complex formation but is not essential for transcription or replication. J. Virol. 70, 4538-4548.
    • (1996) J. Virol , vol.70 , pp. 4538-4548
    • Spadafora, D.1    Canter, D.M.2    Jackson, R.L.3    Perrault, J.4
  • 75
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q., Krug, R. M. and Tao, Y. J. (2006) The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444, 1078-1082.
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 76
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega, J., Martin-Benito, J., Zurcher, T., Valpuesta, J. M., Carrascosa, J. L. and Ortin, J. (2000) Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J. Virol. 74, 156-163.
    • (2000) J. Virol , vol.74 , pp. 156-163
    • Ortega, J.1    Martin-Benito, J.2    Zurcher, T.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Ortin, J.6
  • 77
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin, F., Bach, C., Cusack, S. and Ruigrok, R. W. (1994) Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J. 13, 3158-3165.
    • (1994) EMBO J , vol.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.4
  • 78
    • 0014693884 scopus 로고
    • Distinct subunits of the ribonucleoprotein of influenza virus
    • Duesberg, P. H. (1969) Distinct subunits of the ribonucleoprotein of influenza virus. J. Mol. Biol. 42, 485-499.
    • (1969) J. Mol. Biol , vol.42 , pp. 485-499
    • Duesberg, P.H.1
  • 79
    • 0033965262 scopus 로고    scopus 로고
    • Structure of the RNA inside the vesicular stomatitis virus nucleocapsid
    • Iseni, F., Baudin, F., Blondel, D. and Ruigrok, R. W. (2000) Structure of the RNA inside the vesicular stomatitis virus nucleocapsid. RNA 6, 270-281.
    • (2000) RNA , vol.6 , pp. 270-281
    • Iseni, F.1    Baudin, F.2    Blondel, D.3    Ruigrok, R.W.4
  • 80
    • 0036675180 scopus 로고    scopus 로고
    • Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids
    • Iseni, F., Baudin, F., Garcin, D., Marq, J. B., Ruigrok, R. W. and Kolakofsky, D. (2002) Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids. RNA 8, 1056-1067.
    • (2002) RNA , vol.8 , pp. 1056-1067
    • Iseni, F.1    Baudin, F.2    Garcin, D.3    Marq, J.B.4    Ruigrok, R.W.5    Kolakofsky, D.6
  • 81
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman, E. H., Wu, S. S., Amrein, M., Portner, A. and Murti, G. (1989) The Sendai virus nucleocapsid exists in at least four different helical states. J. Virol. 63, 2233-2243.
    • (1989) J. Virol , vol.63 , pp. 2233-2243
    • Egelman, E.H.1    Wu, S.S.2    Amrein, M.3    Portner, A.4    Murti, G.5


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