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Volumn 9, Issue 2, 2005, Pages 83-92

Structures involved in the replication and transcription of non-segmented negative strand RNA viruses;Structures impliquées dans la réplication et la transcription des virus à ARN non segmenté de sens négatif

Author keywords

Antiviral drug; Measles virus; Negative strand RNA viruses; Nucleocapsid; Rabies virus; Replication

Indexed keywords

RNA POLYMERASE; VIRUS NUCLEOPROTEIN; VIRUS RNA;

EID: 18344382350     PISSN: 12678694     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (18)

References (40)
  • 1
    • 0028065169 scopus 로고
    • An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation
    • Curran J, Pelet T, Kolakofsky D. An acidic activation-like domain of the Sendai virus P protein is required for RNA synthesis and encapsidation. Virology 1994; 202: 875-84.
    • (1994) Virology , vol.202 , pp. 875-884
    • Curran, J.1    Pelet, T.2    Kolakofsky, D.3
  • 2
    • 0026527737 scopus 로고
    • Sequence analysis of the Marburg virus nucleoprotein gene: Comparison to Ebola virus and the other non-segmented negative-strand RNA viruses
    • Sanchez A, Kiley MP, Klenk HD, Feldmann H. Sequence analysis of the Marburg virus nucleoprotein gene: comparison to Ebola virus and the other non-segmented negative-strand RNA viruses. J Gen Virol 1992; 73: 347-57.
    • (1992) J Gen Virol , vol.73 , pp. 347-357
    • Sanchez, A.1    Kiley, M.P.2    Klenk, H.D.3    Feldmann, H.4
  • 3
    • 0027260606 scopus 로고
    • The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly
    • Buchholz CJ, Spehner D, Drillien R, Neubert WJ, Homann HE. The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly. J Virol 1993; 67: 5803-12.
    • (1993) J Virol , vol.67 , pp. 5803-5812
    • Buchholz, C.J.1    Spehner, D.2    Drillien, R.3    Neubert, W.J.4    Homann, H.E.5
  • 4
    • 0037705413 scopus 로고    scopus 로고
    • The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein
    • Longhi S, Receveur-Brechot V, Karlin D, et al. The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein. J Biol Chem 2003; 278: 18638-48.
    • (2003) J Biol Chem , vol.278 , pp. 18638-18648
    • Longhi, S.1    Receveur-Brechot, V.2    Karlin, D.3
  • 5
    • 0034749347 scopus 로고    scopus 로고
    • Structure of recombinant rabies virus N-RNA and identification of the phosphoprotein binding site
    • Schoehn G, Iseni F, Mavrakis M, Blondel D, Ruigrok RWH. Structure of recombinant rabies virus N-RNA and identification of the phosphoprotein binding site. J Virol 2001; 75: 490-8.
    • (2001) J Virol , vol.75 , pp. 490-498
    • Schoehn, G.1    Iseni, F.2    Mavrakis, M.3    Blondel, D.4    Ruigrok, R.W.H.5
  • 6
    • 0033965262 scopus 로고    scopus 로고
    • Structure of the RNA inside the vesicular stomatitis virus nucleocapsid
    • Iseni F, Baudin F, Blondel D, Ruigrok RWH. Structure of the RNA inside the vesicular stomatitis virus nucleocapsid. RNA 2000; 6: 270-81.
    • (2000) RNA , vol.6 , pp. 270-281
    • Iseni, F.1    Baudin, F.2    Blondel, D.3    Ruigrok, R.W.H.4
  • 7
    • 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 RWH, Kolakofsky D. Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids. RNA 2002; 8: 1056-67.
    • (2002) RNA , vol.8 , pp. 1056-1067
    • Iseni, F.1    Baudin, F.2    Garcin, D.3    Marq, J.-B.4    Ruigrok, R.W.H.5    Kolakofsky, D.6
  • 8
    • 17244373335 scopus 로고    scopus 로고
    • Dans le génome des paramyxovirinae, les promoteurs et leur activité sont façonnés par la règle des six
    • Roux L. Dans le génome des paramyxovirinae, les promoteurs et leur activité sont façonnés par la règle des six. Virologie 2005; 9: 19-34.
    • (2005) Virologie , vol.9 , pp. 19-34
    • Roux, L.1
  • 9
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman EH, Wu SS, Amrein M, Portner A, Murti G. The Sendai virus nucleocapsid exists in at least four different helical states. J Virol 1989; 63: 2233-43.
    • (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
  • 10
    • 0021885051 scopus 로고
    • Mass and molecular composition of vesicular stomatitis virus: A scanning transmission electron microscopy analysis
    • Thomas D, Newcomb WW, Brown JC, et al. Mass and molecular composition of vesicular stomatitis virus: a scanning transmission electron microscopy analysis. J Virol 1985; 54: 598-607.
    • (1985) J Virol , vol.54 , pp. 598-607
    • Thomas, D.1    Newcomb, W.W.2    Brown, J.C.3
  • 13
    • 0027291943 scopus 로고
    • The rule of six, a basic feature for efficient replication of Sendai virus defective interfering RNA
    • Calain P, Roux L. The rule of six, a basic feature for efficient replication of Sendai virus defective interfering RNA. J Virol 1993; 67: 4822-30.
    • (1993) J Virol , vol.67 , pp. 4822-4830
    • Calain, P.1    Roux, L.2
  • 14
    • 0025983571 scopus 로고
    • Assembly of nucleocapsid like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein
    • Spehner D, Kirn A, Drillien R. Assembly of nucleocapsid like structures in animal cells infected with a vaccinia virus recombinant encoding the measles virus nucleoprotein. J Virol 1991; 65: 6296-300.
    • (1991) J Virol , vol.65 , pp. 6296-6300
    • Spehner, D.1    Kirn, A.2    Drillien, R.3
  • 15
    • 0029163410 scopus 로고
    • High-level expression of the measles virus nucleocapsid protein by using a replication-deficient adenovirus vector: Induction of an MHC-1-restricted CTL response and protection in a murine model
    • Fooks AR, Schadeck E, Liebert UG, et al. High-level expression of the measles virus nucleocapsid protein by using a replication-deficient adenovirus vector: induction of an MHC-1-restricted CTL response and protection in a murine model. Virology 1995; 210: 456-65.
    • (1995) Virology , vol.210 , pp. 456-465
    • Fooks, A.R.1    Schadeck, E.2    Liebert, U.G.3
  • 16
    • 0032425151 scopus 로고    scopus 로고
    • Characterization of Rabies Virus nucleocapsids and recombinant nucleocapsid-like structures
    • Iseni F, Barge A, Baudin F, Blondel D, Ruigrok RWH. Characterization of Rabies Virus nucleocapsids and recombinant nucleocapsid-like structures. J Gen Virol 1998; 79: 2909-19.
    • (1998) J Gen Virol , vol.79 , pp. 2909-2919
    • Iseni, F.1    Barge, A.2    Baudin, F.3    Blondel, D.4    Ruigrok, R.W.H.5
  • 17
    • 0035983614 scopus 로고    scopus 로고
    • Significant differences in nucleocapsid morphology within the Paramyxoviridae
    • Bhella D, Ralph A, Murphy LB, Yeo RP. Significant differences in nucleocapsid morphology within the Paramyxoviridae. J Gen Virol 2002; 83: 1831-9.
    • (2002) J Gen Virol , vol.83 , pp. 1831-1839
    • Bhella, D.1    Ralph, A.2    Murphy, L.B.3    Yeo, R.P.4
  • 19
    • 0347719363 scopus 로고    scopus 로고
    • 3D structure of the influenza virus polymerase complex: Localization of subunit domains
    • Area E, Martin-Benito J, Gastaminza P, et al. 3D structure of the influenza virus polymerase complex: localization of subunit domains. Proc Natl Acad Sci USA 2004; 101: 308-13.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 308-313
    • Area, E.1    Martin-Benito, J.2    Gastaminza, P.3
  • 20
    • 1242328675 scopus 로고    scopus 로고
    • Visualizing the RNA molecule in the bacterially expressed vesicular stomatitis virus nucleoprotein-RNA complex
    • Chen Z, Green TJ, Luo M, Li H. Visualizing the RNA molecule in the bacterially expressed vesicular stomatitis virus nucleoprotein-RNA complex. Structure 2004; 12: 227-35.
    • (2004) Structure , vol.12 , pp. 227-235
    • Chen, Z.1    Green, T.J.2    Luo, M.3    Li, H.4
  • 21
    • 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, Tordo N. Identification of a region of the rabies virus N protein involved in direct binding to the viral RNA. J Gen Virol 1998; 79: 1005-13.
    • (1998) J Gen Virol , vol.79 , pp. 1005-1013
    • Kouznetzoff, A.1    Buckle, M.2    Tordo, N.3
  • 22
    • 0031003878 scopus 로고    scopus 로고
    • Roles of the Influenza Virus Polymerase and Nucleoprotein in forming a functional RNP structure
    • Klumpp K, Ruigrok RWH, Baudin F. Roles of the Influenza Virus Polymerase and Nucleoprotein in forming a functional RNP structure. EMBO J 1997; 16: 1248-57.
    • (1997) EMBO J , vol.16 , pp. 1248-1257
    • Klumpp, K.1    Ruigrok, R.W.H.2    Baudin, F.3
  • 23
    • 22844442335 scopus 로고    scopus 로고
    • La protéine P du virus rabique: Une protéine multifonctionnelle à l'interface entre le virus et son hôte
    • sous presse
    • Blondel D, Ruigrok R, Chelbi-Alix M, Tordo N. La protéine P du virus rabique: une protéine multifonctionnelle à l'interface entre le virus et son hôte. Virologie 2005; (sous presse).
    • (2005) Virologie
    • Blondel, D.1    Ruigrok, R.2    Chelbi-Alix, M.3    Tordo, N.4
  • 24
    • 0036299393 scopus 로고    scopus 로고
    • The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins
    • Karlin D, Longhi S, Receveur V, Canard B. The N-terminal domain of the phosphoprotein of Morbilliviruses belongs to the natively unfolded class of proteins. Virology 2002; 296: 251-62.
    • (2002) Virology , vol.296 , pp. 251-262
    • Karlin, D.1    Longhi, S.2    Receveur, V.3    Canard, B.4
  • 25
    • 0028895953 scopus 로고
    • An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
    • Curran J, Marq JB, Kolakofsky D. An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication. J Virol 1995; 69: 849-55.
    • (1995) J Virol , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 26
    • 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, et al. Structure and dynamics of the nucleocapsid-binding domain of the Sendai virus phosphoprotein in solution. Virology 2004; 319: 201-11.
    • (2004) Virology , vol.319 , pp. 201-211
    • Blanchard, L.1    Tarbouriech, N.2    Blackledge, M.3
  • 28
    • 0346752214 scopus 로고    scopus 로고
    • Structural disorder and modular organization in Paramyxovirinae N and P
    • Karlin D, Ferron F, Canard B, Longhi S. Structural disorder and modular organization in Paramyxovirinae N and P. J Gen Virol 2003; 84: 3239-52.
    • (2003) J Gen Virol , vol.84 , pp. 3239-3252
    • Karlin, D.1    Ferron, F.2    Canard, B.3    Longhi, S.4
  • 29
    • 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 JM, Campanacci V, Cambillau C, Canard B, Longhi S. Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J Biol Chem 2003; 278: 44567-73.
    • (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
  • 31
    • 3543139986 scopus 로고    scopus 로고
    • Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins
    • Kingston RL, Baase WA, Gay LS. Characterization of nucleocapsid binding by the measles virus and mumps virus phosphoproteins. J Virol 2004; 78: 8630-40.
    • (2004) J Virol , vol.78 , pp. 8630-8640
    • Kingston, R.L.1    Baase, W.A.2    Gay, L.S.3
  • 32
    • 1242283916 scopus 로고    scopus 로고
    • Viral RNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis
    • Kolakofsky D, Le Mercier P, Iseni F, Garcin D. Viral RNA polymerase scanning and the gymnastics of Sendai virus RNA synthesis. Virology 2004; 318: 463-73.
    • (2004) Virology , vol.318 , pp. 463-473
    • Kolakofsky, D.1    Le Mercier, P.2    Iseni, F.3    Garcin, D.4
  • 33
    • 0032651115 scopus 로고    scopus 로고
    • Replication of paramyxoviruses
    • Curran J, Kolakofsky D. Replication of paramyxoviruses. Adv Virus Res 1999; 54: 403-22.
    • (1999) Adv Virus Res , vol.54 , pp. 403-422
    • Curran, J.1    Kolakofsky, D.2
  • 34
    • 0028961740 scopus 로고
    • Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II
    • Gao Y, Lenard J. Multimerization and transcriptional activation of the phosphoprotein (P) of vesicular stomatitis virus by casein kinase-II. EMBO J 1995; 14: 1240-7.
    • (1995) EMBO J , vol.14 , pp. 1240-1247
    • Gao, Y.1    Lenard, J.2
  • 35
    • 0034811975 scopus 로고    scopus 로고
    • Functional interaction map of lyssavirus phosphoprotein: Identification of the minimal transcription domains
    • Jacob Y, Real E, Tordo N. Functional interaction map of lyssavirus phosphoprotein: identification of the minimal transcription domains. J Virol 2001; 75: 9613-22.
    • (2001) J Virol , vol.75 , pp. 9613-9622
    • Jacob, Y.1    Real, E.2    Tordo, N.3
  • 36
    • 5144222412 scopus 로고    scopus 로고
    • Structure and function of the C-terminal domain of the polymerase cofactor of Rabies virus
    • Mavrakis M, McCarthy AA, Roche S, Blondel D, Ruigrok RWH. Structure and function of the C-terminal domain of the polymerase cofactor of Rabies virus. J Mol Biol 2004; 343: 819-31.
    • (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.H.5
  • 37
    • 0024784519 scopus 로고
    • Identification of four conserved motifs among the RNA-dependent polymerase encoding elements
    • Poch O, Sauvaget I, Delarue M, Tordo N. Identification of four conserved motifs among the RNA-dependent polymerase encoding elements. EMBO J 1989; 8: 3867-74.
    • (1989) EMBO J , vol.8 , pp. 3867-3874
    • Poch, O.1    Sauvaget, I.2    Delarue, M.3    Tordo, N.4
  • 38
    • 0033539482 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus
    • Bressanelli S, Tomei L, Roussel A, et al. Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Proc Natl Acad Sci USA 1999; 96: 13034-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13034-13039
    • Bressanelli, S.1    Tomei, L.2    Roussel, A.3
  • 39
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 2002; 296: 2218-22.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 40
    • 0036943952 scopus 로고    scopus 로고
    • Intragenic complementation and oligomerization of the L subunit of the sendai virus RNA polymerase
    • Smallwood S, Cevik B, Moyer SA. Intragenic complementation and oligomerization of the L subunit of the sendai virus RNA polymerase. Virology 2002; 304: 235-45.
    • (2002) Virology , vol.304 , pp. 235-245
    • Smallwood, S.1    Cevik, B.2    Moyer, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.