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Volumn 82, Issue 19, 2008, Pages 9577-9590

The crystal structure of coxsackievirus B3 RNA-dependent RNA polymerase in complex with its protein primer VPg confirms the existence of a second VPg binding site on Picornaviridae polymerases

Author keywords

[No Author keywords available]

Indexed keywords

PYROPHOSPHATE; RNA DIRECTED RNA POLYMERASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; VPG PROTEIN;

EID: 52649173300     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.00631-08     Document Type: Article
Times cited : (76)

References (71)
  • 1
  • 2
    • 33744990410 scopus 로고    scopus 로고
    • Current status of anti-picornavirus therapies
    • Barnard, D. L. 2006. Current status of anti-picornavirus therapies. Curr. Pharm. Des. 12:1379-1390.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 1379-1390
    • Barnard, D.L.1
  • 5
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • Bressanelli, S., L. Tomei, F. A. Rey, and R. De Francesco. 2002. Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J. Virol. 76:3482-3492.
    • (2002) J. Virol , vol.76 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 6
    • 0037386414 scopus 로고    scopus 로고
    • A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases
    • Bruenn, J. A. 2003. A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases. Nucleic Acids Res. 31:1821-1829.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1821-1829
    • Bruenn, J.A.1
  • 9
    • 0021017976 scopus 로고
    • Genome-linked protein VPg of poliovirus is present as free VPg and VPg-pUpU in poliovirus-infected cells
    • Crawford, N. M., and D. Baltimore. 1983. Genome-linked protein VPg of poliovirus is present as free VPg and VPg-pUpU in poliovirus-infected cells. Proc. Natl. Acad. Sci. USA 80:7452-7455.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7452-7455
    • Crawford, N.M.1    Baltimore, D.2
  • 10
    • 0033080970 scopus 로고    scopus 로고
    • An open and closed case for all polymerases
    • Doublie, S., M. R. Sawaya, and T. Ellenberger. 1999. An open and closed case for all polymerases. Structure 7:R31-R35.
    • (1999) Structure , vol.7
    • Doublie, S.1    Sawaya, M.R.2    Ellenberger, T.3
  • 11
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 12
  • 15
    • 8744222695 scopus 로고    scopus 로고
    • Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
    • Ferrer-Orta, C., A. Arias, R. Perez-Luque, C. Escarmis, E. Domingo, and N. Verdaguer. 2004. Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA. J. Biol. Chem. 279:47212-47221.
    • (2004) J. Biol. Chem , vol.279 , pp. 47212-47221
    • Ferrer-Orta, C.1    Arias, A.2    Perez-Luque, R.3    Escarmis, C.4    Domingo, E.5    Verdaguer, N.6
  • 16
    • 34247567806 scopus 로고    scopus 로고
    • Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication
    • Fujita, K., S. S. Krishnakumar, D. Franco, A. V. Paul, E. London, and E. Wimmer. 2007. Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication. Biochemistry 46:5185-5199.
    • (2007) Biochemistry , vol.46 , pp. 5185-5199
    • Fujita, K.1    Krishnakumar, S.S.2    Franco, D.3    Paul, A.V.4    London, E.5    Wimmer, E.6
  • 18
    • 0031565730 scopus 로고    scopus 로고
    • Modelling protein docking using shape complementarity, electrostatics, and biochemical information
    • Gabb, H. A., R. M. Jackson, and M. J. Sternberg. 1997. Modelling protein docking using shape complementarity, electrostatics, and biochemical information. J. Mol. Biol. 272:106-120.
    • (1997) J. Mol. Biol , vol.272 , pp. 106-120
    • Gabb, H.A.1    Jackson, R.M.2    Sternberg, M.J.3
  • 19
    • 3142765526 scopus 로고    scopus 로고
    • Coxsackievirus experimental heart diseases
    • Gauntt, C., and S. Huber. 2003. Coxsackievirus experimental heart diseases. Front. Biosci. 8:e23-e35.
    • (2003) Front. Biosci , vol.8
    • Gauntt, C.1    Huber, S.2
  • 20
    • 0041351978 scopus 로고    scopus 로고
    • The poliovirus 2C cis-acting replication element-mediated uridylylation of VPg is not required for synthesis of negative-sense genomes
    • Goodfellow, I. G., C. Polacek, R. Andino, and D. J. Evans. 2003. The poliovirus 2C cis-acting replication element-mediated uridylylation of VPg is not required for synthesis of negative-sense genomes. J. Gen. Virol. 84:2359-2363.
    • (2003) J. Gen. Virol , vol.84 , pp. 2359-2363
    • Goodfellow, I.G.1    Polacek, C.2    Andino, R.3    Evans, D.J.4
  • 22
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • Gouet, P., X. Robert, and E. Courcelle. 2003. ESPript/ENDscript: extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31:3320-3323.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3
  • 23
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J. L., A. M. Long, and S. C. Schultz. 1997. Structure of the RNA-dependent RNA polymerase of poliovirus. Structure 5:1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 24
    • 0033919960 scopus 로고    scopus 로고
    • Poliovirus requires a precise 5′ end for efficient positive-strand RNA synthesis
    • Herold, J., and R. Andino. 2000. Poliovirus requires a precise 5′ end for efficient positive-strand RNA synthesis. J. Virol. 74:6394-6400.
    • (2000) J. Virol , vol.74 , pp. 6394-6400
    • Herold, J.1    Andino, R.2
  • 26
    • 0030732120 scopus 로고    scopus 로고
    • Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB
    • Hope, D. A., S. E. Diamond, and K. Kirkegaard. 1997. Genetic dissection of interaction between poliovirus 3D polymerase and viral protein 3AB. J. Virol. 71:9490-9498.
    • (1997) J. Virol , vol.71 , pp. 9490-9498
    • Hope, D.A.1    Diamond, S.E.2    Kirkegaard, K.3
  • 28
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch. 1988. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallogr. 21:916-924.
    • (1988) J. Appl. Crystallogr , vol.21 , pp. 916-924
    • Kabsch1
  • 29
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., and K. Henrick. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr. 60:2256-2268.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 30
    • 0034711772 scopus 로고    scopus 로고
    • Enteroviral capsid protein VP1 is present in myocardial tissues from some patients with myocarditis or dilated cardiomyopathy
    • Li, Y., T. Bourlet, L. Andreoletti, J. F. Mosnier, T. Peng, Y. Yang, L. C. Archard, B. Pozzetto, and H. Zhang. 2000. Enteroviral capsid protein VP1 is present in myocardial tissues from some patients with myocarditis or dilated cardiomyopathy. Circulation 101:231-234.
    • (2000) Circulation , vol.101 , pp. 231-234
    • Li, Y.1    Bourlet, T.2    Andreoletti, L.3    Mosnier, J.F.4    Peng, T.5    Yang, Y.6    Archard, L.C.7    Pozzetto, B.8    Zhang, H.9
  • 31
    • 34249799046 scopus 로고    scopus 로고
    • Tyrosine 3 of poliovirus terminal peptide VPg(3B) has an essential function in RNA replication in the context of its precursor protein, 3AB
    • Liu, Y., D. Franco, A. V. Paul, and E. Wimmer. 2007. Tyrosine 3 of poliovirus terminal peptide VPg(3B) has an essential function in RNA replication in the context of its precursor protein, 3AB. J. Virol. 81:5669-5684.
    • (2007) J. Virol , vol.81 , pp. 5669-5684
    • Liu, Y.1    Franco, D.2    Paul, A.V.3    Wimmer, E.4
  • 32
    • 4143147318 scopus 로고    scopus 로고
    • The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: A dual function target for common cold antiviral therapy
    • Love, R. A., K. A. Maegley, X. Yu, R. A. Ferre, L. K. Lingardo, W. Diehl, H. E. Parge, P. S. Dragovich, and S. A. Fuhrman. 2004. The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy. Structure 12:1533-1544.
    • (2004) Structure , vol.12 , pp. 1533-1544
    • Love, R.A.1    Maegley, K.A.2    Yu, X.3    Ferre, R.A.4    Lingardo, L.K.5    Diehl, W.6    Parge, H.E.7    Dragovich, P.S.8    Fuhrman, S.A.9
  • 33
    • 0037150679 scopus 로고    scopus 로고
    • Visualization and functional analysis of RNA-dependent RNA polymerase lattices
    • Lyle, J. M., E. Bullitt, K. Bienz, and K. Kirkegaard. 2002. Visualization and functional analysis of RNA-dependent RNA polymerase lattices. Science 296:2218-2222.
    • (2002) Science , vol.296 , pp. 2218-2222
    • Lyle, J.M.1    Bullitt, E.2    Bienz, K.3    Kirkegaard, K.4
  • 34
    • 0037013317 scopus 로고    scopus 로고
    • Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase
    • Lyle, J. M., A. Clewell, K. Richmond, O. C. Richards, D. A. Hope, S. C. Schultz, and K. Kirkegaard. 2002. Similar structural basis for membrane localization and protein priming by an RNA-dependent RNA polymerase. J. Biol. Chem. 277:16324-16331.
    • (2002) J. Biol. Chem , vol.277 , pp. 16324-16331
    • Lyle, J.M.1    Clewell, A.2    Richmond, K.3    Richards, O.C.4    Hope, D.A.5    Schultz, S.C.6    Kirkegaard, K.7
  • 36
    • 33947386595 scopus 로고    scopus 로고
    • Crystal structure of poliovirus 3CD protein: Virally encoded protease and precursor to the RNA-dependent RNA polymerase
    • Marcotte, L. L., A. B. Wass, D. W. Gohara, H. B. Pathak, J. J. Arnold, D. J. Filman, C. E. Cameron, and J. M. Hogle. 2007. Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. J. Virol. 81:3583-3596.
    • (2007) J. Virol , vol.81 , pp. 3583-3596
    • Marcotte, L.L.1    Wass, A.B.2    Gohara, D.W.3    Pathak, H.B.4    Arnold, J.J.5    Filman, D.J.6    Cameron, C.E.7    Hogle, J.M.8
  • 37
    • 0037405928 scopus 로고    scopus 로고
    • Poliovirus cre(2C)-dependent synthesis of VPgpUpU is required for positive- but not negative-strand RNA synthesis
    • Morasco, B. J., N. Sharma, J. Parilla, and J. B. Flanegan. 2003. Poliovirus cre(2C)-dependent synthesis of VPgpUpU is required for positive- but not negative-strand RNA synthesis. J. Virol. 77:5136-5144.
    • (2003) J. Virol , vol.77 , pp. 5136-5144
    • Morasco, B.J.1    Sharma, N.2    Parilla, J.3    Flanegan, J.B.4
  • 38
    • 0037383425 scopus 로고    scopus 로고
    • Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negative-strand RNA synthesis
    • Murray, K. E., and D. J. Barton. 2003. Poliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negative-strand RNA synthesis. J. Virol. 77:4739-4750.
    • (2003) J. Virol , vol.77 , pp. 4739-4750
    • Murray, K.E.1    Barton, D.J.2
  • 40
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza, J. 2001. Implementation of molecular replacement in AMoRe. Acta Crystallogr. D Biol. Crystallogr. 57:1367-1372.
    • (2001) Acta Crystallogr. D Biol. Crystallogr , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 41
    • 0027991249 scopus 로고
    • Identification of terminal adenylyl transferase activity of the poliovirus polymerase 3Dpol
    • Neufeld, K. L., J. M. Galarza, O. C. Richards, D. F. Summers, and E. Ehrenfeld. 1994. Identification of terminal adenylyl transferase activity of the poliovirus polymerase 3Dpol. J. Virol. 68:5811-5818.
    • (1994) J. Virol , vol.68 , pp. 5811-5818
    • Neufeld, K.L.1    Galarza, J.M.2    Richards, O.C.3    Summers, D.F.4    Ehrenfeld, E.5
  • 42
    • 0037059758 scopus 로고    scopus 로고
    • Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase
    • Ng, K. K., M. M. Cherney, A. L. Vazquez, A. Machin, J. M. Alonso, F. Parra, and M. N. James. 2002. Crystal structures of active and inactive conformations of a caliciviral RNA-dependent RNA polymerase. J. Biol. Chem. 277:1381-1387.
    • (2002) J. Biol. Chem , vol.277 , pp. 1381-1387
    • Ng, K.K.1    Cherney, M.M.2    Vazquez, A.L.3    Machin, A.4    Alonso, J.M.5    Parra, F.6    James, M.N.7
  • 43
    • 34250643613 scopus 로고    scopus 로고
    • The structure of a birnavirus polymerase reveals a distinct active site topology
    • Pan, J., V. N. Vakharia, and Y. J. Tao. 2007. The structure of a birnavirus polymerase reveals a distinct active site topology. Proc. Natl. Acad. Sci. USA 104:7385-7390.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7385-7390
    • Pan, J.1    Vakharia, V.N.2    Tao, Y.J.3
  • 44
    • 34447536284 scopus 로고    scopus 로고
    • Picornavirus genome replication: Assembly and organization of the VPg uridylylation ribonucleoprotein (initiation) complex
    • Pathak, H. B., J. J. Arnold, P. N. Wiegand, M. R. Hargittai, and C. E. Cameron. 2007. Picornavirus genome replication: assembly and organization of the VPg uridylylation ribonucleoprotein (initiation) complex. J. Biol. Chem. 282:16202-16213.
    • (2007) J. Biol. Chem , vol.282 , pp. 16202-16213
    • Pathak, H.B.1    Arnold, J.J.2    Wiegand, P.N.3    Hargittai, M.R.4    Cameron, C.E.5
  • 45
    • 0037200001 scopus 로고    scopus 로고
    • Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol): A surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation
    • Pathak, H. B., S. K. Ghosh, A. W. Roberts, S. D. Sharma, J. D. Yoder, J. J. Arnold, D. W. Gohara, D. J. Barton, A. V. Paul, and C. E. Cameron. 2002. Structure-function relationships of the RNA-dependent RNA polymerase from poliovirus (3Dpol): a surface of the primary oligomerization domain functions in capsid precursor processing and VPg uridylylation. J. Biol. Chem. 277:31551-31562.
    • (2002) J. Biol. Chem , vol.277 , pp. 31551-31562
    • Pathak, H.B.1    Ghosh, S.K.2    Roberts, A.W.3    Sharma, S.D.4    Yoder, J.D.5    Arnold, J.J.6    Gohara, D.W.7    Barton, D.J.8    Paul, A.V.9    Cameron, C.E.10
  • 46
    • 0037223676 scopus 로고    scopus 로고
    • Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus
    • Paul, A. V., J. Peters, J. Mugavero, J. Yin, J. H. van Boom, and E. Wimmer. 2003. Biochemical and genetic studies of the VPg uridylylation reaction catalyzed by the RNA polymerase of poliovirus. J. Virol. 77:891-904.
    • (2003) J. Virol , vol.77 , pp. 891-904
    • Paul, A.V.1    Peters, J.2    Mugavero, J.3    Yin, J.4    van Boom, J.H.5    Wimmer, E.6
  • 47
    • 0033766003 scopus 로고    scopus 로고
    • Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg
    • Paul, A. V., E. Rieder, D. W. Kim, J. H. van Boom, and E. Wimmer. 2000. Identification of an RNA hairpin in poliovirus RNA that serves as the primary template in the in vitro uridylylation of VPg. J. Virol. 74:10359-10370.
    • (2000) J. Virol , vol.74 , pp. 10359-10370
    • Paul, A.V.1    Rieder, E.2    Kim, D.W.3    van Boom, J.H.4    Wimmer, E.5
  • 48
    • 0032554886 scopus 로고    scopus 로고
    • Protein-primed RNA synthesis by purified poliovirus RNA polymerase
    • Paul, A. V., J. H. van Boom, D. Filippov, and E. Wimmer. 1998. Protein-primed RNA synthesis by purified poliovirus RNA polymerase. Nature 393:280-284.
    • (1998) Nature , vol.393 , pp. 280-284
    • Paul, A.V.1    van Boom, J.H.2    Filippov, D.3    Wimmer, E.4
  • 49
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., R. Morris, and V. S. Lamzin. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:458-463.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 50
    • 84974728057 scopus 로고    scopus 로고
    • Racaniello, V. R. 2001. Picornaviridae: the viruses and their replication, p. 685-722. In D. M. Knipe and P. M. Howley (ed.), Fields' virology, 4th ed., 1. Lippincott/The Williams & Wilkins Co., Philadelphia, PA.
    • Racaniello, V. R. 2001. Picornaviridae: the viruses and their replication, p. 685-722. In D. M. Knipe and P. M. Howley (ed.), Fields' virology, 4th ed., vol. 1. Lippincott/The Williams & Wilkins Co., Philadelphia, PA.
  • 51
    • 0033762467 scopus 로고    scopus 로고
    • Quantitative analysis of viral RNA kinetics in coxsackievirus B3-induced murine myocarditis: Biphasic pattern of clearance following acute infection, with persistence of residual viral RNA throughout and beyond the inflammatory phase of disease
    • Reetoo, K. N., S. A. Osman, S. J. Illavia, C. L. Cameron-Wilson, J. E. Banatvala, and P. Muir. 2000. Quantitative analysis of viral RNA kinetics in coxsackievirus B3-induced murine myocarditis: biphasic pattern of clearance following acute infection, with persistence of residual viral RNA throughout and beyond the inflammatory phase of disease. J. Gen. Virol. 81:2755-2762.
    • (2000) J. Gen. Virol , vol.81 , pp. 2755-2762
    • Reetoo, K.N.1    Osman, S.A.2    Illavia, S.J.3    Cameron-Wilson, C.L.4    Banatvala, J.E.5    Muir, P.6
  • 52
    • 0029974113 scopus 로고    scopus 로고
    • Mutation of lysine residues in the nucleotide binding segments of the poliovirus RNA-dependent RNA polymerase
    • Richards, O. C., S. Baker, and E. Ehrenfeld. 1996. Mutation of lysine residues in the nucleotide binding segments of the poliovirus RNA-dependent RNA polymerase. J. Virol. 70:8564-8570.
    • (1996) J. Virol , vol.70 , pp. 8564-8570
    • Richards, O.C.1    Baker, S.2    Ehrenfeld, E.3
  • 53
    • 33746215114 scopus 로고    scopus 로고
    • Intramolecular and intermolecular uridylylation by poliovirus RNA-dependent RNA polymerase
    • Richards, O. C., J. F. Spagnolo, J. M. Lyle, S. E. Vleck, R. D. Kuchta, and K. Kirkegaard. 2006. Intramolecular and intermolecular uridylylation by poliovirus RNA-dependent RNA polymerase. J. Virol. 80:7405-7415.
    • (2006) J. Virol , vol.80 , pp. 7405-7415
    • Richards, O.C.1    Spagnolo, J.F.2    Lyle, J.M.3    Vleck, S.E.4    Kuchta, R.D.5    Kirkegaard, K.6
  • 54
    • 0033755326 scopus 로고    scopus 로고
    • Genetic and biochemical studies of poliovirus cis-acting replication element cre in relation to VPg uridylylation
    • Rieder, E., A. V. Paul, D. W. Kim, J. H. van Boom, and E. Wimmer. 2000. Genetic and biochemical studies of poliovirus cis-acting replication element cre in relation to VPg uridylylation. J. Virol. 74:10371-10380.
    • (2000) J. Virol , vol.74 , pp. 10371-10380
    • Rieder, E.1    Paul, A.V.2    Kim, D.W.3    van Boom, J.H.4    Wimmer, E.5
  • 58
    • 33744984790 scopus 로고    scopus 로고
    • NMR structure of the viral peptide linked to the genome (VPg) of poliovirus
    • Schein, C. H., N. Oezguen, D. E. Volk, R. Garimella, A. Paul, and W. Braun. 2006. NMR structure of the viral peptide linked to the genome (VPg) of poliovirus. Peptides 27:1676-1684.
    • (2006) Peptides , vol.27 , pp. 1676-1684
    • Schein, C.H.1    Oezguen, N.2    Volk, D.E.3    Garimella, R.4    Paul, A.5    Braun, W.6
  • 59
    • 43649090340 scopus 로고    scopus 로고
    • Coxsackievirus B RNA replication: Lessons from poliovirus
    • Sean, P., and B. L. Semler. 2008. Coxsackievirus B RNA replication: lessons from poliovirus. Curr. Top. Microbiol. Immunol. 323:89-121.
    • (2008) Curr. Top. Microbiol. Immunol , vol.323 , pp. 89-121
    • Sean, P.1    Semler, B.L.2
  • 60
    • 0036580905 scopus 로고    scopus 로고
    • FDA panel rejects common cold treatment
    • Senior, K. 2002. FDA panel rejects common cold treatment. Lancet Infect. Dis. 2:264.
    • (2002) Lancet Infect. Dis , vol.2 , pp. 264
    • Senior, K.1
  • 61
    • 52649093188 scopus 로고    scopus 로고
    • Smart, O. S., M. Brandl, C. Flensburg, P. Keller, W. Paciorek, C. Vonrhein, T. O. Womack, and G. Bricogne. 2008. Refinement with local structure similarity restraints (LSSR) enables exploitation of information from related structures and facilitates use of NCS, abstr. TP139. Abstr. Annu. Meet. Am. Crystallogr. Assoc., Knoxville, TN.
    • Smart, O. S., M. Brandl, C. Flensburg, P. Keller, W. Paciorek, C. Vonrhein, T. O. Womack, and G. Bricogne. 2008. Refinement with local structure similarity restraints (LSSR) enables exploitation of information from related structures and facilitates use of NCS, abstr. TP139. Abstr. Annu. Meet. Am. Crystallogr. Assoc., Knoxville, TN.
  • 62
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz, T. A. 1998. A mechanism for all polymerases. Nature 391:231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 63
    • 34249932386 scopus 로고    scopus 로고
    • Characterization of protein-protein interactions critical for poliovirus replication: Analysis of 3AB and VPg binding to the RNA-dependent RNA polymerase
    • Strauss, D. M., and D. S. Wuttke. 2007. Characterization of protein-protein interactions critical for poliovirus replication: analysis of 3AB and VPg binding to the RNA-dependent RNA polymerase. J. Virol. 81:6369-6378.
    • (2007) J. Virol , vol.81 , pp. 6369-6378
    • Strauss, D.M.1    Wuttke, D.S.2
  • 65
    • 33846833843 scopus 로고    scopus 로고
    • Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions
    • Thompson, A. A., R. A. Albertini, and O. B. Peersen. 2007. Stabilization of poliovirus polymerase by NTP binding and fingers-thumb interactions. J. Mol. Biol. 366:1459-1474.
    • (2007) J. Mol. Biol , vol.366 , pp. 1459-1474
    • Thompson, A.A.1    Albertini, R.A.2    Peersen, O.B.3
  • 66
    • 4644238112 scopus 로고    scopus 로고
    • Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase
    • Thompson, A. A., and O. B. Peersen. 2004. Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. EMBO J. 23:3462-3471.
    • (2004) EMBO J , vol.23 , pp. 3462-3471
    • Thompson, A.A.1    Peersen, O.B.2
  • 68
    • 27244434501 scopus 로고    scopus 로고
    • Host and virus determinants of picornavirus pathogenesis and tropism
    • Whitton, J. L., C. T. Cornell, and R. Feuer. 2005. Host and virus determinants of picornavirus pathogenesis and tropism. Nat. Rev. Microbiol. 3:765-776.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 765-776
    • Whitton, J.L.1    Cornell, C.T.2    Feuer, R.3
  • 69
    • 1842424947 scopus 로고    scopus 로고
    • Genetic evidence for an interaction between a picornaviral cis-acting RNA replication element and 3CD protein
    • Yang, Y., R. Rijnbrand, S. Watowich, and S. M. Lemon. 2004. Genetic evidence for an interaction between a picornaviral cis-acting RNA replication element and 3CD protein. J. Biol. Chem. 279:12659-12667.
    • (2004) J. Biol. Chem , vol.279 , pp. 12659-12667
    • Yang, Y.1    Rijnbrand, R.2    Watowich, S.3    Lemon, S.M.4
  • 70
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-Å resolution
    • Yap, T. L., T. Xu, Y. L. Chen, H. Malet, M. P. Egloff, B. Canard, S. G. Vasudevan, and J. Lescar. 2007. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-Å resolution. J. Virol. 81:4753-4765.
    • (2007) J. Virol , vol.81 , pp. 4753-4765
    • Yap, T.L.1    Xu, T.2    Chen, Y.L.3    Malet, H.4    Egloff, M.P.5    Canard, B.6    Vasudevan, S.G.7    Lescar, J.8
  • 71
    • 34547556207 scopus 로고    scopus 로고
    • Viral load in blood is correlated with disease severity of neonatal coxsackievirus B3 infection: Early diagnosis and predicting disease severity is possible in severe neonatal enterovirus infection
    • Yen, M. H., K. C. Tsao, Y. C. Huang, C. G. Huang, Y. L. Huang, R. Lin, M. L. Chang, C. C. Huang, D. C. Yan, and T. Y. Lin. 2007. Viral load in blood is correlated with disease severity of neonatal coxsackievirus B3 infection: early diagnosis and predicting disease severity is possible in severe neonatal enterovirus infection. Clin. Infect. Dis. 44:e78-e81.
    • (2007) Clin. Infect. Dis , vol.44
    • Yen, M.H.1    Tsao, K.C.2    Huang, Y.C.3    Huang, C.G.4    Huang, Y.L.5    Lin, R.6    Chang, M.L.7    Huang, C.C.8    Yan, D.C.9    Lin, T.Y.10


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