메뉴 건너뛰기




Volumn 5, Issue 3, 2010, Pages

Polypyrimidine tract binding protein functions as a negative regulator of feline calicivirus translation

Author keywords

[No Author keywords available]

Indexed keywords

POLYPYRIMIDINE TRACT BINDING PROTEIN; RNA; RNA BINDING PROTEIN; SMALL INTERFERING RNA; VIRUS PROTEIN; VIRUS RNA; GREEN FLUORESCENT PROTEIN; RIBONUCLEASE H;

EID: 77949714892     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0009562     Document Type: Article
Times cited : (32)

References (64)
  • 1
    • 33847067590 scopus 로고    scopus 로고
    • Solving the structure of PTB in complex with pyrimidine tracts: An NMR study of protein-RNA complexes of weak affinities
    • Auweter SD, Oberstrass FC, Allain FH (2007) Solving the structure of PTB in complex with pyrimidine tracts: an NMR study of protein-RNA complexes of weak affinities. J Mol Biol 367: 174-186.
    • (2007) J Mol Biol , vol.367 , pp. 174-186
    • Auweter, S.D.1    Oberstrass, F.C.2    Allain, F.H.3
  • 2
    • 0037349339 scopus 로고    scopus 로고
    • The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr
    • Mitchell SA, Spriggs KA, Coldwell MJ, Jackson RJ, Willis AE (2003) The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol Cell 11: 757-771.
    • (2003) Mol Cell , vol.11 , pp. 757-771
    • Mitchell, S.A.1    Spriggs, K.A.2    Coldwell, M.J.3    Jackson, R.J.4    Willis, A.E.5
  • 3
    • 2942628000 scopus 로고    scopus 로고
    • Bag-1 internal ribosome entry segment activity is promoted by structural changes mediated by poly(rC) binding protein 1 and recruitment of polypyrimidine tract binding protein 1
    • Pickering BM, Mitchell SA, Spriggs KA, Stoneley M, Willis AE (2004) Bag-1 internal ribosome entry segment activity is promoted by structural changes mediated by poly(rC) binding protein 1 and recruitment of polypyrimidine tract binding protein 1. Mol Cell Biol 24: 5595-5605.
    • (2004) Mol Cell Biol , vol.24 , pp. 5595-5605
    • Pickering, B.M.1    Mitchell, S.A.2    Spriggs, K.A.3    Stoneley, M.4    Willis, A.E.5
  • 4
    • 59749097987 scopus 로고    scopus 로고
    • Role of RNA chaperones in virus replication
    • Zuniga S, Sola I, Cruz JL, Enjuanes L (2009) Role of RNA chaperones in virus replication. Virus Res 139: 253-266.
    • (2009) Virus Res , vol.139 , pp. 253-266
    • Zuniga, S.1    Sola, I.2    Cruz, J.L.3    Enjuanes, L.4
  • 5
    • 0041806593 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein
    • Xie J, Lee JA, Kress TL, Mowry KL, Black DL (2003) Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein. Proc Natl Acad Sci U S A 100: 8776-8781.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 8776-8781
    • Xie, J.1    Lee, J.A.2    Kress, T.L.3    Mowry, K.L.4    Black, D.L.5
  • 6
    • 70849127442 scopus 로고    scopus 로고
    • The Polypyrimidine-Tract Binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells
    • Agis-Juarez RA, Galvan I, Medina FJ, Daikoku T, Padmanabhan R, et al. (2009) The Polypyrimidine-Tract Binding protein is relocated to the cytoplasm and is required during dengue virus infection in Vero cells. J Gen Virol 90: 2893-2901.
    • (2009) J Gen Virol , vol.90 , pp. 2893-2901
    • Agis-Juarez, R.A.1    Galvan, I.2    Medina, F.J.3    Daikoku, T.4    Padmanabhan, R.5
  • 7
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition
    • Gustin KE, Sarnow P (2001) Effects of poliovirus infection on nucleocytoplasmic trafficking and nuclear pore complex composition. Embo J 20: 240-249.
    • (2001) Embo J , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 8
    • 23744492690 scopus 로고    scopus 로고
    • Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition
    • Izquierdo JM, Majos N, Bonnal S, Martinez C, Castelo R, et al. (2005) Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol Cell 19: 475-484.
    • (2005) Mol Cell , vol.19 , pp. 475-484
    • Izquierdo, J.M.1    Majos, N.2    Bonnal, S.3    Martinez, C.4    Castelo, R.5
  • 9
    • 2942629589 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein modulates efficiency of polyadenylation
    • Castelo-Branco P, Furger A, Wollerton M, Smith C, Moreira A, et al. (2004) Polypyrimidine tract binding protein modulates efficiency of polyadenylation. Mol Cell Biol 24: 4174-4183.
    • (2004) Mol Cell Biol , vol.24 , pp. 4174-4183
    • Castelo-Branco, P.1    Furger, A.2    Wollerton, M.3    Smith, C.4    Moreira, A.5
  • 10
    • 0033197874 scopus 로고    scopus 로고
    • A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization
    • Cote CA, Gautreau D, Denegre JM, Kress TL, Terry NA, et al. (1999) A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization. Mol Cell 4: 431-437.
    • (1999) Mol Cell , vol.4 , pp. 431-437
    • Cote, C.A.1    Gautreau, D.2    Denegre, J.M.3    Kress, T.L.4    Terry, N.A.5
  • 11
    • 47749090521 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein regulates IRES-mediated translation of p53 isoforms
    • Grover R, Ray PS, Das S (2008) Polypyrimidine tract binding protein regulates IRES-mediated translation of p53 isoforms. Cell Cycle 7: 2189-2198.
    • (2008) Cell Cycle , vol.7 , pp. 2189-2198
    • Grover, R.1    Ray, P.S.2    Das, S.3
  • 12
    • 4644286294 scopus 로고    scopus 로고
    • Molecular mechanisms of attenuation of the Sabin strain of poliovirus type 3
    • Guest S, Pilipenko E, Sharma K, Chumakov K, Roos RP (2004) Molecular mechanisms of attenuation of the Sabin strain of poliovirus type 3. J Virol 78: 11097-11107.
    • (2004) J Virol , vol.78 , pp. 11097-11107
    • Guest, S.1    Pilipenko, E.2    Sharma, K.3    Chumakov, K.4    Roos, R.P.5
  • 13
    • 0030766564 scopus 로고    scopus 로고
    • Functional involvement of polypyrimidine tract-binding protein in translation initiation complexes with the internal ribosome entry site of foot-and-mouth disease virus
    • Niepmann M, Petersen A, Meyer K, Beck E (1997) Functional involvement of polypyrimidine tract-binding protein in translation initiation complexes with the internal ribosome entry site of foot-and-mouth disease virus. J Virol 71: 8330-8339.
    • (1997) J Virol , vol.71 , pp. 8330-8339
    • Niepmann, M.1    Petersen, A.2    Meyer, K.3    Beck, E.4
  • 14
    • 0035803389 scopus 로고    scopus 로고
    • Cell-specific proteins regulate viral RNA translation and virus-induced disease
    • Pilipenko EV, Viktorova EG, Guest ST, Agol VI, Roos RP (2001) Cell-specific proteins regulate viral RNA translation and virus-induced disease. Embo J 20: 6899-6908.
    • (2001) Embo J , vol.20 , pp. 6899-6908
    • Pilipenko, E.V.1    Viktorova, E.G.2    Guest, S.T.3    Agol, V.I.4    Roos, R.P.5
  • 15
    • 0031746507 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein (PTB) requirement for internal initiation of translation of cardiovirus RNAs is conditional rather than absolute
    • Kaminski A, Jackson RJ (1998) The polypyrimidine tract binding protein (PTB) requirement for internal initiation of translation of cardiovirus RNAs is conditional rather than absolute. RNA 4: 626-638.
    • (1998) RNA , vol.4 , pp. 626-638
    • Kaminski, A.1    Jackson, R.J.2
  • 16
    • 0034602386 scopus 로고    scopus 로고
    • Demonstration of functional requirement of polypyrimidine tract-binding protein by SELEX RNA during hepatitis C virus internal ribosome entry site-mediated translation initiation
    • Anwar A, Ali N, Tanveer R, Siddiqui A (2000) Demonstration of functional requirement of polypyrimidine tract-binding protein by SELEX RNA during hepatitis C virus internal ribosome entry site-mediated translation initiation. J Biol Chem 275: 34231-34235.
    • (2000) J Biol Chem , vol.275 , pp. 34231-34235
    • Anwar, A.1    Ali, N.2    Tanveer, R.3    Siddiqui, A.4
  • 18
    • 7044269394 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein (PTB) inhibits Hepatitis C virus internal ribosome entry site (HCV IRES)-mediated translation, but does not affect HCV replication
    • Tischendorf JJ, Beger C, Korf M, Manns MP, Kruger M (2004) Polypyrimidine tract-binding protein (PTB) inhibits Hepatitis C virus internal ribosome entry site (HCV IRES)-mediated translation, but does not affect HCV replication. Arch Virol 149: 1955-1970.
    • (2004) Arch Virol , vol.149 , pp. 1955-1970
    • Tischendorf, J.J.1    Beger, C.2    Korf, M.3    Manns, M.P.4    Kruger, M.5
  • 19
    • 67650520190 scopus 로고    scopus 로고
    • The polypyrimidine tract-binding protein is required for efficient dengue virus propagation and associates with the viral replication machinery
    • Anwar A, Leong KM, Ng ML, Chu JJ, Garcia-Blanco MA (2009) The polypyrimidine tract-binding protein is required for efficient dengue virus propagation and associates with the viral replication machinery. J Biol Chem 284: 17021-17029.
    • (2009) J Biol Chem , vol.284 , pp. 17021-17029
    • Anwar, A.1    Leong, K.M.2    Ng, M.L.3    Chu, J.J.4    Garcia-Blanco, M.A.5
  • 20
    • 67349133117 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus
    • Jiang L, Yao H, Duan X, Lu X, Liu Y (2009) Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus. Biochem Biophys Res Commun 385: 187-192.
    • (2009) Biochem Biophys Res Commun , vol.385 , pp. 187-192
    • Jiang, L.1    Yao, H.2    Duan, X.3    Lu, X.4    Liu, Y.5
  • 21
    • 17344372905 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein binds to the leader RNA of mouse hepatitis virus and serves as a regulator of viral transcription
    • Li HP, Huang P, Park S, Lai MM (1999) Polypyrimidine tract-binding protein binds to the leader RNA of mouse hepatitis virus and serves as a regulator of viral transcription. J Virol 73: 772-777.
    • (1999) J Virol , vol.73 , pp. 772-777
    • Li, H.P.1    Huang, P.2    Park, S.3    Lai, M.M.4
  • 24
    • 33748853528 scopus 로고    scopus 로고
    • Stable expression of a Norwalk virus RNA replicon in a human hepatoma cell line
    • Chang K-O, Sosnovtsev SV, Belliot G, King AD, Green KY (2006) Stable expression of a Norwalk virus RNA replicon in a human hepatoma cell line. Virology 353: 463-473.
    • (2006) Virology , vol.353 , pp. 463-473
    • Chang, K.-O.1    Sosnovtsev, S.V.2    Belliot, G.3    King, A.D.4    Green, K.Y.5
  • 28
    • 0036635341 scopus 로고    scopus 로고
    • Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome
    • Sosnovtsev SV, Garfield M, Green KY (2002) Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genome. J Virol 76: 7060-7072.
    • (2002) J Virol , vol.76 , pp. 7060-7072
    • Sosnovtsev, S.V.1    Garfield, M.2    Green, K.Y.3
  • 29
    • 0030922351 scopus 로고    scopus 로고
    • Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation
    • Herbert TP, Brierley I, Brown TD (1997) Identification of a protein linked to the genomic and subgenomic mRNAs of feline calicivirus and its role in translation. J Gen Virol 78: 1033-1040.
    • (1997) J Gen Virol , vol.78 , pp. 1033-1040
    • Herbert, T.P.1    Brierley, I.2    Brown, T.D.3
  • 30
    • 33748756616 scopus 로고    scopus 로고
    • Caliciviruses differ in their functional requirements for eIF4F components
    • Chaudhry Y, Nayak A, Bordeleau M-E, Tanaka J, Pelletier J, et al. (2006) Caliciviruses differ in their functional requirements for eIF4F components. J Biol Chem 281: 25315-25325.
    • (2006) J Biol Chem , vol.281 , pp. 25315-25325
    • Chaudhry, Y.1    Nayak, A.2    Bordeleau, M.-E.3    Tanaka, J.4    Pelletier, J.5
  • 32
    • 33745301496 scopus 로고    scopus 로고
    • VPg of murine norovirus binds translation initiation factors in infected cells
    • Daughenbaugh KF, Wobus CE, Hardy ME (2006) VPg of murine norovirus binds translation initiation factors in infected cells. Virol J 3: 33.
    • (2006) Virol , vol.J 3 , pp. 33
    • Daughenbaugh, K.F.1    Wobus, C.E.2    Hardy, M.E.3
  • 33
    • 0037844744 scopus 로고    scopus 로고
    • The genomelinked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment
    • Daughenbaugh KF, Fraser CS, Hershey JW, Hardy ME (2003) The genomelinked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitment. Embo J 22: 2852-2859.
    • (2003) Embo J , vol.22 , pp. 2852-2859
    • Daughenbaugh, K.F.1    Fraser, C.S.2    Hershey, J.W.3    Hardy, M.E.4
  • 34
    • 33750228022 scopus 로고    scopus 로고
    • Feline calicivirus replication: Requirement for polypyrimidine tract-binding protein is temperature dependent
    • Karakasiliotis I, Chaudhry Y, Roberts LO, Goodfellow IG (2006) Feline calicivirus replication: requirement for polypyrimidine tract-binding protein is temperature dependent. J Gen Virol 87: 3339-3347.
    • (2006) J Gen Virol , vol.87 , pp. 3339-3347
    • Karakasiliotis, I.1    Chaudhry, Y.2    Roberts, L.O.3    Goodfellow, I.G.4
  • 35
    • 0029134714 scopus 로고
    • RNA transcripts derived from a cloned fulllength copy of the feline calicivirus genome do not require VPg for infectivity
    • Sosnovtsev S, Green KY (1995) RNA transcripts derived from a cloned fulllength copy of the feline calicivirus genome do not require VPg for infectivity. Virology 210: 383-390.
    • (1995) Virology , vol.210 , pp. 383-390
    • Sosnovtsev, S.1    Green, K.Y.2
  • 36
    • 0028177935 scopus 로고
    • trans complementation by RNA of defective foot-and-mouth disease virus internal ribosome entry site elements
    • Drew J, Belsham GJ (1994) trans complementation by RNA of defective foot-and-mouth disease virus internal ribosome entry site elements. J Virol 68: 697-703.
    • (1994) J Virol , vol.68 , pp. 697-703
    • Drew, J.1    Belsham, G.J.2
  • 37
    • 33646881280 scopus 로고    scopus 로고
    • RNA delivery by heat shock protein-70 into mammalian cells: A preliminary study
    • Henics T, Zimmer C (2006) RNA delivery by heat shock protein-70 into mammalian cells: a preliminary study. Cell Biol Int 30: 480-484.
    • (2006) Cell Biol Int , vol.30 , pp. 480-484
    • Henics, T.1    Zimmer, C.2
  • 38
    • 77649187275 scopus 로고    scopus 로고
    • Abente EJ, Sosnovtsev SV, Bok K, Green KY (2010) Visualization of feline calicivirus replication in real-time with recombinant viruses 2 engineered to express fluorescent reporter proteins. Virology: In press.
    • Abente EJ, Sosnovtsev SV, Bok K, Green KY (2010) Visualization of feline calicivirus replication in real-time with recombinant viruses 2 engineered to express fluorescent reporter proteins. Virology: In press.
  • 40
    • 0030878682 scopus 로고    scopus 로고
    • Mutation of PTB binding sites causes misregulation of alternative 39 splice site selection in vivo
    • Perez I, Lin CH, McAfee JG, Patton JG (1997) Mutation of PTB binding sites causes misregulation of alternative 39 splice site selection in vivo. RNA 3: 764-778.
    • (1997) RNA , vol.3 , pp. 764-778
    • Perez, I.1    Lin, C.H.2    McAfee, J.G.3    Patton, J.G.4
  • 41
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh R, Valcarcel J, Green MR (1995) Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science 268: 1173-1176.
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcarcel, J.2    Green, M.R.3
  • 42
    • 0019876473 scopus 로고
    • Optimal computer folding of large RNA sequences using thermodynamics and auxilliary information
    • Zucker M, Stiegler P (1981) Optimal computer folding of large RNA sequences using thermodynamics and auxilliary information. Nucleic Acids Research 9: 133-148.
    • (1981) Nucleic Acids Research , vol.9 , pp. 133-148
    • Zucker, M.1    Stiegler, P.2
  • 43
    • 0036338006 scopus 로고    scopus 로고
    • Isolation of enzymatically active replication complexes from feline calicivirus-infected cells
    • Green KY, Mory A, Fogg MH, Weisberg A, Belliot G, et al. (2002) Isolation of enzymatically active replication complexes from feline calicivirus-infected cells. J Virol 76: 8582-8595.
    • (2002) J Virol , vol.76 , pp. 8582-8595
    • Green, K.Y.1    Mory, A.2    Fogg, M.H.3    Weisberg, A.4    Belliot, G.5
  • 44
    • 0032888961 scopus 로고    scopus 로고
    • Feline calicivirus capsid protein expression and capsid assembly in cultured feline cells
    • Geissler K, Schneider K, Fleuchaus A, Parrish CR, Sutter G, et al. (1999) Feline calicivirus capsid protein expression and capsid assembly in cultured feline cells. J Virol 73: 834-838.
    • (1999) J Virol , vol.73 , pp. 834-838
    • Geissler, K.1    Schneider, K.2    Fleuchaus, A.3    Parrish, C.R.4    Sutter, G.5
  • 45
    • 0032821090 scopus 로고    scopus 로고
    • Feline calicivirus capsid protein expression and self-assembly in cultured feline cells
    • Geissler K, Parrish CR, Schneider K, Truyen U (1999) Feline calicivirus capsid protein expression and self-assembly in cultured feline cells. Vet Microbiol 69: 63-66.
    • (1999) Vet Microbiol , vol.69 , pp. 63-66
    • Geissler, K.1    Parrish, C.R.2    Schneider, K.3    Truyen, U.4
  • 47
    • 77949696861 scopus 로고    scopus 로고
    • Hepatitis C Virus Translation and Cell Cycle
    • Honda M (2004) Hepatitis C Virus Translation and Cell Cycle. Biomedical Reviews 15: 37-46.
    • (2004) Biomedical Reviews , vol.15 , pp. 37-46
    • Honda, M.1
  • 48
    • 0034235466 scopus 로고    scopus 로고
    • Picornavirus RNA translation: Roles for cellular proteins
    • Belsham GJ, Sonenberg N (2000) Picornavirus RNA translation: roles for cellular proteins. Trends Microbiol 8: 330-335.
    • (2000) Trends Microbiol , vol.8 , pp. 330-335
    • Belsham, G.J.1    Sonenberg, N.2
  • 49
    • 28344442948 scopus 로고    scopus 로고
    • Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation
    • Song Y, Tzima E, Ochs K, Bassili G, Trusheim H, et al. (2005) Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. RNA 11: 1809-1824.
    • (2005) RNA , vol.11 , pp. 1809-1824
    • Song, Y.1    Tzima, E.2    Ochs, K.3    Bassili, G.4    Trusheim, H.5
  • 50
    • 66449130983 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation
    • Kafasla P, Morgner N, Poyry TA, Curry S, Robinson CV, et al. (2009) Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation. Mol Cell 34: 556-568.
    • (2009) Mol Cell , vol.34 , pp. 556-568
    • Kafasla, P.1    Morgner, N.2    Poyry, T.A.3    Curry, S.4    Robinson, C.V.5
  • 51
    • 0036168869 scopus 로고    scopus 로고
    • Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro)
    • Back SH, Kim YK, Kim WJ, Cho S, Oh HR, et al. (2002) Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro). J Virol 76: 2529-2542.
    • (2002) J Virol , vol.76 , pp. 2529-2542
    • Back, S.H.1    Kim, Y.K.2    Kim, W.J.3    Cho, S.4    Oh, H.R.5
  • 52
    • 58849127937 scopus 로고    scopus 로고
    • Drosophila PTB promotes formation of high-order RNP particles and represses oskar translation
    • Besse F, Lopez de Quinto S, Marchand V, Trucco A, Ephrussi A (2009) Drosophila PTB promotes formation of high-order RNP particles and represses oskar translation. Genes Dev 23: 195-207.
    • (2009) Genes Dev , vol.23 , pp. 195-207
    • Besse, F.1    Lopez de Quinto, S.2    Marchand, V.3    Trucco, A.4    Ephrussi, A.5
  • 53
    • 0033859004 scopus 로고    scopus 로고
    • Interaction of cellular proteins with the 59 end of Norwalk virus genomic RNA
    • Gutierrez-Escolano AL, Brito ZU, del Angel RM, Jiang X (2000) Interaction of cellular proteins with the 59 end of Norwalk virus genomic RNA. J Virol 74: 8558-8562.
    • (2000) J Virol , vol.74 , pp. 8558-8562
    • Gutierrez-Escolano, A.L.1    Brito, Z.U.2    del Angel, R.M.3    Jiang, X.4
  • 55
    • 64849084931 scopus 로고    scopus 로고
    • Cellular proteins mediate 59-39 end contacts of Norwalk virus genomic RNA
    • Sandoval-Jaime C, Gutiérrez-Escolano A (2009) Cellular proteins mediate 59-39 end contacts of Norwalk virus genomic RNA. Virology 387: 322.
    • (2009) Virology , vol.387 , pp. 322
    • Sandoval-Jaime, C.1    Gutiérrez-Escolano, A.2
  • 56
    • 0032752998 scopus 로고    scopus 로고
    • Translating ribosomes inhibit poliovirus negative-strand RNA synthesis
    • Barton DJ, Morasco BJ, Flanegan JB (1999) Translating ribosomes inhibit poliovirus negative-strand RNA synthesis. Journal of Virology 73: 10104-10112.
    • (1999) Journal of Virology , vol.73 , pp. 10104-10112
    • Barton, D.J.1    Morasco, B.J.2    Flanegan, J.B.3
  • 57
    • 0032146721 scopus 로고    scopus 로고
    • Switch from translation to RNA replication in a positive-stranded RNA virus
    • Gamarnik AV, Andino R (1998) Switch from translation to RNA replication in a positive-stranded RNA virus. Genes Dev 12: 2293-2304.
    • (1998) Genes Dev , vol.12 , pp. 2293-2304
    • Gamarnik, A.V.1    Andino, R.2
  • 58
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • van Kuppeveld FJ, Hoenderop JG, Smeets RL, Willems PH, Dijkman HB, et al. (1997) Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. Embo J 16: 3519-3532.
    • (1997) Embo J , vol.16 , pp. 3519-3532
    • van Kuppeveld, F.J.1    Hoenderop, J.G.2    Smeets, R.L.3    Willems, P.H.4    Dijkman, H.B.5
  • 59
    • 0032889314 scopus 로고    scopus 로고
    • Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro
    • Joachims M, Van Breugel PC, Lloyd RE (1999) Cleavage of poly(A)-binding protein by enterovirus proteases concurrent with inhibition of translation in vitro. J Virol 73: 718-727.
    • (1999) J Virol , vol.73 , pp. 718-727
    • Joachims, M.1    Van Breugel, P.C.2    Lloyd, R.E.3
  • 60
    • 3242702220 scopus 로고    scopus 로고
    • Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein
    • Kuyumcu-Martinez M, Belliot G, Sosnovtsev SV, Chang KO, Green KY, et al. (2004) Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein. J Virol 78: 8172-8182.
    • (2004) J Virol , vol.78 , pp. 8172-8182
    • Kuyumcu-Martinez, M.1    Belliot, G.2    Sosnovtsev, S.V.3    Chang, K.O.4    Green, K.Y.5
  • 61
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin KE, Sarnow P (2002) Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J Virol 76: 8787-8796.
    • (2002) J Virol , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 62
    • 33749049426 scopus 로고    scopus 로고
    • The nuclear pore complex, nuclear transport, and apoptosis
    • Fahrenkrog B (2006) The nuclear pore complex, nuclear transport, and apoptosis. Can J Physiol Pharmacol 84: 279-286.
    • (2006) Can J Physiol Pharmacol , vol.84 , pp. 279-286
    • Fahrenkrog, B.1
  • 63
    • 1842333235 scopus 로고    scopus 로고
    • Attenuating mutations in the poliovirus 5′ untranslated region alter its interaction with polypyrimidine tract-binding protein
    • Gutierrez AL, DenovaOcampo M, Racaniello VR, delAngel RM (1997) Attenuating mutations in the poliovirus 5′ untranslated region alter its interaction with polypyrimidine tract-binding protein. J Virol 71: 3826-3833.
    • (1997) J Virol , vol.71 , pp. 3826-3833
    • Gutierrez, A.L.1    DenovaOcampo, M.2    Racaniello, V.R.3    delAngel, R.M.4
  • 64
    • 33746825431 scopus 로고    scopus 로고
    • Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells
    • Sosnovtsev SV, Belliot G, Chang K-OK, Prikhodko VG, Thackray LB, et al. (2006) Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells. J Virol 80: 7816-7831.
    • (2006) J Virol , vol.80 , pp. 7816-7831
    • Sosnovtsev, S.V.1    Belliot, G.2    Chang, K.-O.K.3    Prikhodko, V.G.4    Thackray, L.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.