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Volumn 110, Issue 45, 2013, Pages

Isolation and characterization of the positive-sense replicative intermediate of a negative-strand RNA virus

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RNA DIRECTED RNA POLYMERASE; SINGLE STRANDED RNA; SMALL CYTOPLASMIC RIBONUCLEOPROTEIN;

EID: 84887265188     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1315068110     Document Type: Article
Times cited : (107)

References (40)
  • 2
    • 84871460710 scopus 로고    scopus 로고
    • The structure of native influenza virion ribonucleoproteins
    • Arranz R, et al. (2012) The structure of native influenza virion ribonucleoproteins. Science 338(6114):1634-1637.
    • (2012) Science , vol.338 , Issue.6114 , pp. 1634-1637
    • Arranz, R.1
  • 4
    • 84880367286 scopus 로고    scopus 로고
    • The RNA polymerase of influenza a virus: Mechanisms of viral transcription and replication
    • Fodor E (2013) The RNA polymerase of influenza a virus: Mechanisms of viral transcription and replication. Acta Virol 57(2):113-122.
    • (2013) Acta Virol , vol.57 , Issue.2 , pp. 113-122
    • Fodor, E.1
  • 5
    • 84883076935 scopus 로고    scopus 로고
    • The virus genome and its replication
    • Webster RG, Monto AS, Braciale TJ, Lamb RA (John Wiley & Sons, New York), 2nd Ed
    • Krug RM, Fodor E (2013) The virus genome and its replication. Textbook of Influenza, eds Webster RG, Monto AS, Braciale TJ, Lamb RA (John Wiley & Sons, New York), 2nd Ed, pp 57-66.
    • (2013) Textbook of Influenza , pp. 57-66
    • Krug, R.M.1    Fodor, E.2
  • 6
    • 84974694553 scopus 로고    scopus 로고
    • Orthomyxoviridae
    • Knipe DM, Howley PM (Lippincott Williams and Wilkins, Philadelphia), 6th Ed
    • Palese P, Shaw ML (2013) Orthomyxoviridae. Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams and Wilkins, Philadelphia), 6th Ed, pp 1151-1185.
    • (2013) Fields Virology , pp. 1151-1185
    • Palese, P.1    Shaw, M.L.2
  • 7
    • 4143153932 scopus 로고    scopus 로고
    • Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates
    • Vreede FT, Jung TE, Brownlee GG (2004) Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates. J Virol 78(17): 9568-9572.
    • (2004) J Virol , vol.78 , Issue.17 , pp. 9568-9572
    • Vreede, F.T.1    Jung, T.E.2    Brownlee, G.G.3
  • 8
    • 0024535928 scopus 로고
    • Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells
    • Hatada E, Hasegawa M, Mukaigawa J, Shimizu K, Fukuda R (1989) Control of influenza virus gene expression: Quantitative analysis of each viral RNA species in infected cells. J Biochem 105(4):537-546.
    • (1989) J Biochem , vol.105 , Issue.4 , pp. 537-546
    • Hatada, E.1    Hasegawa, M.2    Mukaigawa, J.3    Shimizu, K.4    Fukuda, R.5
  • 9
    • 0036799597 scopus 로고    scopus 로고
    • RNA recognition site of PP7 coat protein
    • Lim F, Peabody DS (2002) RNA recognition site of PP7 coat protein. Nucleic Acids Res 30(19):4138-4144.
    • (2002) Nucleic Acids Res , vol.30 , Issue.19 , pp. 4138-4144
    • Lim, F.1    Peabody, D.S.2
  • 10
    • 34249053165 scopus 로고    scopus 로고
    • RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation
    • Hogg JR, Collins K (2007) RNA-based affinity purification reveals 7SK RNPs with distinct composition and regulation. RNA 13(6):868-880.
    • (2007) RNA , vol.13 , Issue.6 , pp. 868-880
    • Hogg, J.R.1    Collins, K.2
  • 11
    • 0032844790 scopus 로고    scopus 로고
    • Rescue of influenza A virus from recombinant DNA
    • Fodor E, et al. (1999) Rescue of influenza A virus from recombinant DNA. J Virol 73 (11):9679-9682.
    • (1999) J Virol , vol.73 , Issue.11 , pp. 9679-9682
    • Fodor, E.1
  • 12
    • 84862003840 scopus 로고    scopus 로고
    • Influenza neuraminidase
    • Air GM (2012) Influenza neuraminidase. Influenza Other Respi Viruses 6(4):245-256.
    • (2012) Influenza Other Respi Viruses , vol.6 , Issue.4 , pp. 245-256
    • Air, G.M.1
  • 13
    • 0027236107 scopus 로고
    • Alterations of the stalk of the influenza virus neuraminidase: Deletions and insertions
    • Luo G, Chung J, Palese P (1993) Alterations of the stalk of the influenza virus neuraminidase: Deletions and insertions. Virus Res 29(2):141-153.
    • (1993) Virus Res , vol.29 , Issue.2 , pp. 141-153
    • Luo, G.1    Chung, J.2    Palese, P.3
  • 14
    • 0027397591 scopus 로고
    • Biologic importance of neuraminidase stalk length in influenza A virus
    • Castrucci MR, Kawaoka Y (1993) Biologic importance of neuraminidase stalk length in influenza A virus. J Virol 67(2):759-764.
    • (1993) J Virol , vol.67 , Issue.2 , pp. 759-764
    • Castrucci, M.R.1    Kawaoka, Y.2
  • 15
    • 78049509775 scopus 로고    scopus 로고
    • A 27-amino-acid deletion in the neuraminidase stalk supports replication of an avian H2N2 influenza A virus in the respiratory tract of chickens
    • Sorrell EM, Song H, Pena L, Perez DR (2010) A 27-amino-acid deletion in the neuraminidase stalk supports replication of an avian H2N2 influenza A virus in the respiratory tract of chickens. J Virol 84(22):11831-11840.
    • (2010) J Virol , vol.84 , Issue.22 , pp. 11831-11840
    • Sorrell, E.M.1    Song, H.2    Pena, L.3    Perez, D.R.4
  • 16
    • 73849099951 scopus 로고    scopus 로고
    • A genetically engineered waterfowl influenza virus with a deletion in the stalk of the neuraminidase has increased virulence for chickens
    • Munier S, et al. (2010) A genetically engineered waterfowl influenza virus with a deletion in the stalk of the neuraminidase has increased virulence for chickens. J Virol 84(2):940-952.
    • (2010) J Virol , vol.84 , Issue.2 , pp. 940-952
    • Munier, S.1
  • 17
    • 0015414910 scopus 로고
    • Structure of the ribonucleoprotein of influenza virus
    • Compans RW, Content J, Duesberg PH (1972) Structure of the ribonucleoprotein of influenza virus. J Virol 10(4):795-800.
    • (1972) J Virol , vol.10 , Issue.4 , pp. 795-800
    • Compans, R.W.1    Content, J.2    Duesberg, P.H.3
  • 18
    • 67649227447 scopus 로고    scopus 로고
    • NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome
    • Robb NC, Smith M, Vreede FT, Fodor E (2009) NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J Gen Virol 90(Pt 6):1398-1407.
    • (2009) J Gen Virol , vol.90 , Issue.PART 6 , pp. 1398-1407
    • Robb, N.C.1    Smith, M.2    Vreede, F.T.3    Fodor, E.4
  • 19
    • 33847195002 scopus 로고    scopus 로고
    • Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro
    • Vreede FT, Brownlee GG (2007) Influenza virion-derived viral ribonucleoproteins synthesize both mRNA and cRNA in vitro. J Virol 81(5):2196-2204.
    • (2007) J Virol , vol.81 , Issue.5 , pp. 2196-2204
    • Vreede, F.T.1    Brownlee, G.G.2
  • 20
    • 67249108203 scopus 로고    scopus 로고
    • Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication
    • Jorba N, Coloma R, Ortín J (2009) Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication. PLoS Pathog 5(5):e1000462.
    • (2009) PLoS Pathog , vol.5 , Issue.5
    • Jorba, N.1    Coloma, R.2    Ortín, J.3
  • 21
    • 33144488409 scopus 로고    scopus 로고
    • Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication
    • Deng T, Vreede FT, Brownlee GG (2006) Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication. J Virol 80(5):2337-2348.
    • (2006) J Virol , vol.80 , Issue.5 , pp. 2337-2348
    • Deng, T.1    Vreede, F.T.2    Brownlee, G.G.3
  • 22
    • 31444441789 scopus 로고    scopus 로고
    • Architecture of ribonucleoprotein complexes in influenza A virus particles
    • Noda T, et al. (2006) Architecture of ribonucleoprotein complexes in influenza A virus particles. Nature 439(7075):490-492.
    • (2006) Nature , vol.439 , Issue.7075 , pp. 490-492
    • Noda, T.1
  • 24
    • 84863393147 scopus 로고    scopus 로고
    • A supramolecular assembly formed by influenza A virus genomic RNA segments
    • Fournier E, et al. (2012) A supramolecular assembly formed by influenza A virus genomic RNA segments. Nucleic Acids Res 40(5):2197-2209.
    • (2012) Nucleic Acids Res , vol.40 , Issue.5 , pp. 2197-2209
    • Fournier, E.1
  • 25
    • 84856704565 scopus 로고    scopus 로고
    • Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus
    • Noda T, et al. (2012) Three-dimensional analysis of ribonucleoprotein complexes in influenza A virus. Nat Commun 3:639.
    • (2012) Nat Commun , vol.3 , pp. 639
    • Noda, T.1
  • 26
    • 84883124285 scopus 로고    scopus 로고
    • Biogenesis, assembly and export of viral messenger ribonucleoproteins in the influenza A virus infected cell
    • York A, Fodor E (2013) Biogenesis, assembly and export of viral messenger ribonucleoproteins in the influenza A virus infected cell. RNA Biol 10(8):1274-1282.
    • (2013) RNA Biol , vol.10 , Issue.8 , pp. 1274-1282
    • York, A.1    Fodor, E.2
  • 27
    • 80051781196 scopus 로고    scopus 로고
    • Nucleoproteins and nucleocapsids of negative-strand RNA viruses
    • Ruigrok RW, Crépin T, Kolakofsky D (2011) Nucleoproteins and nucleocapsids of negative-strand RNA viruses. Curr Opin Microbiol 14(4):504-510.
    • (2011) Curr Opin Microbiol , vol.14 , Issue.4 , pp. 504-510
    • Ruigrok, R.W.1    Crépin, T.2    Kolakofsky, D.3
  • 28
    • 41649087655 scopus 로고    scopus 로고
    • Oligomerization of the influenza virus polymerase complex in vivo
    • Jorba N, Area E, Ortín J (2008) Oligomerization of the influenza virus polymerase complex in vivo. J Gen Virol 89(Pt 2):520-524.
    • (2008) J Gen Virol , vol.89 , Issue.PART 2 , pp. 520-524
    • Jorba, N.1    Area, E.2    Ortín, J.3
  • 29
    • 0024395266 scopus 로고
    • Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes
    • Digard P, Blok VC, Inglis SC (1989) Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes. Virology 171(1):162-169.
    • (1989) Virology , vol.171 , Issue.1 , pp. 162-169
    • Digard, P.1    Blok, V.C.2    Inglis, S.C.3
  • 30
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle JM, Bullitt E, Bienz K, Kirkegaard K (2002) Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296(5576):2218-2222.
    • (2002) Science , vol.296 , Issue.5576 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 31
    • 0036194639 scopus 로고    scopus 로고
    • Oligomerization and cooperative RNA synthesis activity of hepatitis C virus RNA-dependent RNA polymerase
    • Wang QM, et al. (2002) Oligomerization and cooperative RNA synthesis activity of hepatitis C virus RNA-dependent RNA polymerase. J Virol 76(8):3865-3872.
    • (2002) J Virol , vol.76 , Issue.8 , pp. 3865-3872
    • Wang, Q.M.1
  • 32
    • 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 (2002) Intragenic complementation and oligomerization of the L subunit of the sendai virus RNA polymerase. Virology 304(2):235-245.
    • (2002) Virology , vol.304 , Issue.2 , pp. 235-245
    • Smallwood, S.1    Cevik, B.2    Moyer, S.A.3
  • 33
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt LA, Wang J, Friedman JM, Rice PA, Steitz TA (1992) Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science 256 (5065):1783-1790.
    • (1992) Science , vol.256 , Issue.5065 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 34
    • 0036720769 scopus 로고    scopus 로고
    • A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs
    • Fodor E, et al. (2002) A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs. J Virol 76 (18):8989-9001.
    • (2002) J Virol , vol.76 , Issue.18 , pp. 8989-9001
    • Fodor, E.1
  • 36
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SHW (2012) RELION: Implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180(3):519-530.
    • (2012) J Struct Biol , vol.180 , Issue.3 , pp. 519-530
    • Scheres, S.H.W.1
  • 37
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig O, et al. (2001) The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods 24(3):218-229.
    • (2001) Methods , vol.24 , Issue.3 , pp. 218-229
    • Puig, O.1
  • 38
    • 75749152978 scopus 로고    scopus 로고
    • MultiBac: Multigene baculovirus-based eukaryotic protein complex production
    • Unit 5.20
    • Bieniossek C, Richmond TJ, Berger I (2008) MultiBac: Multigene baculovirus-based eukaryotic protein complex production. Curr Protoc Protein Sci Chapter 5:Unit 5.20.
    • (2008) Curr Protoc Protein Sci Chapter , vol.5
    • Bieniossek, C.1    Richmond, T.J.2    Berger, I.3
  • 39
    • 17444430403 scopus 로고    scopus 로고
    • Association of the influenza A virus RNAdependent RNA polymerase with cellular RNA polymerase II
    • Engelhardt OG, Smith M, Fodor E (2005) Association of the influenza A virus RNAdependent RNA polymerase with cellular RNA polymerase II. J Virol 79(9):5812-5818.
    • (2005) J Virol , vol.79 , Issue.9 , pp. 5812-5818
    • Engelhardt, O.G.1    Smith, M.2    Fodor, E.3
  • 40
    • 0036635342 scopus 로고    scopus 로고
    • The RNA polymerase of influenza A virus is stabilized by interaction with its viral RNA promoter
    • Brownlee GG, Sharps JL (2002) The RNA polymerase of influenza A virus is stabilized by interaction with its viral RNA promoter. J Virol 76(14):7103-7113.
    • (2002) J Virol , vol.76 , Issue.14 , pp. 7103-7113
    • Brownlee, G.G.1    Sharps, J.L.2


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