메뉴 건너뛰기




Volumn 162, Issue 2, 2008, Pages 277-289

Conformational changes accompany activation of reovirus RNA-dependent RNA transcription

Author keywords

Cryo microscopy; Electron microscopy; Image processing; Mass spectrometry; RNA; Transcription; Virus structure

Indexed keywords

DOUBLE STRANDED RNA; MESSENGER RNA; NUCLEIC ACID; RNA DIRECTED RNA POLYMERASE; RNA POLYMERASE; TRYPSIN;

EID: 43049118630     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.01.006     Document Type: Article
Times cited : (18)

References (67)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 (1996) 120-130
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 2
    • 0024110653 scopus 로고
    • The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1
    • Bartlett J.A., and Joklik W.K. The sequence of the reovirus serotype 3 L3 genome segment which encodes the major core protein lambda 1. Virology 167 (1988) 31-37
    • (1988) Virology , vol.167 , pp. 31-37
    • Bartlett, J.A.1    Joklik, W.K.2
  • 3
    • 0030800967 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein
    • Bisaillon M., Bergeron J., and Lemay G. Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein. J. Biol. Chem. 272 (1997) 18298-18303
    • (1997) J. Biol. Chem. , vol.272 , pp. 18298-18303
    • Bisaillon, M.1    Bergeron, J.2    Lemay, G.3
  • 4
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry
    • Bothner B., Dong X.F., Bibbs L., Johnson J.E., and Siuzdak G. Evidence of viral capsid dynamics using limited proteolysis and mass spectrometry. J. Biol. Chem. 273 (1998) 673-676
    • (1998) J. Biol. Chem. , vol.273 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 5
    • 0030584685 scopus 로고    scopus 로고
    • Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus
    • Bottcher B., and Crowther R.A. Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus. Structure 4 (1996) 387-394
    • (1996) Structure , vol.4 , pp. 387-394
    • Bottcher, B.1    Crowther, R.A.2
  • 6
    • 0014838436 scopus 로고
    • Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus
    • Borsa J., Grover J., and Chapman J.D. Presence of nucleoside triphosphate phosphohydrolase activity in purified virions of reovirus. J. Virol. 6 (1970) 295-302
    • (1970) J. Virol. , vol.6 , pp. 295-302
    • Borsa, J.1    Grover, J.2    Chapman, J.D.3
  • 7
    • 0035450448 scopus 로고    scopus 로고
    • Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing
    • Breun L.A., Broering T.J., McCutcheon A.M., Harrison S.J., Luongo C.L., and Nibert M.L. Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing. Virology 287 (2001) 333-348
    • (2001) Virology , vol.287 , pp. 333-348
    • Breun, L.A.1    Broering, T.J.2    McCutcheon, A.M.3    Harrison, S.J.4    Luongo, C.L.5    Nibert, M.L.6
  • 8
    • 0037386414 scopus 로고    scopus 로고
    • A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases
    • Bruenn J.A. A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases. Nucleic Acids Res. 31 (2003) 1821-1829
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1821-1829
    • Bruenn, J.A.1
  • 10
    • 0141907317 scopus 로고    scopus 로고
    • Animal cell invasion by a large nonenveloped virus: reovirus delivers the goods
    • Chandran K., and Nibert M.L. Animal cell invasion by a large nonenveloped virus: reovirus delivers the goods. Trends Microbiol. 11 (2003) 374-382
    • (2003) Trends Microbiol. , vol.11 , pp. 374-382
    • Chandran, K.1    Nibert, M.L.2
  • 11
    • 0015166005 scopus 로고
    • Fate of parental reovirus in infected cell
    • Chang C.T., and Zweerink H.J. Fate of parental reovirus in infected cell. Virology 46 (1971) 544-555
    • (1971) Virology , vol.46 , pp. 544-555
    • Chang, C.T.1    Zweerink, H.J.2
  • 12
    • 0033169004 scopus 로고    scopus 로고
    • Orthogonal-injection TOFMS for analyzing biomolecules
    • Chernushevich I.V., Ens W., and Standing K.G. Orthogonal-injection TOFMS for analyzing biomolecules. Anal. Chem. 71 (1999) 452A-461A
    • (1999) Anal. Chem. , vol.71
    • Chernushevich, I.V.1    Ens, W.2    Standing, K.G.3
  • 13
    • 0022478937 scopus 로고
    • Reovirus guanylyltransferase is L2 gene product lambda 2
    • Cleveland D.R., Zarbl H., and Millward S. Reovirus guanylyltransferase is L2 gene product lambda 2. J. Virol. 60 (1986) 307-311
    • (1986) J. Virol. , vol.60 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 14
    • 0032579850 scopus 로고    scopus 로고
    • Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles
    • Coombs K.M. Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles. Virology 243 (1998) 218-228
    • (1998) Virology , vol.243 , pp. 218-228
    • Coombs, K.M.1
  • 15
    • 0025003413 scopus 로고
    • Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein
    • Coombs K.M., Fields B.N., and Harrison S.C. Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein. J. Mol. Biol. 215 (1990) 1-5
    • (1990) J. Mol. Biol. , vol.215 , pp. 1-5
    • Coombs, K.M.1    Fields, B.N.2    Harrison, S.C.3
  • 16
    • 0028078574 scopus 로고
    • Studies of the major reovirus core protein sigma 2: reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn
    • Coombs K.M., Mak S.C., and Petrycky-Cox L.D. Studies of the major reovirus core protein sigma 2: reversion of the assembly-defective mutant tsC447 is an intragenic process and involves back mutation of Asp-383 to Asn. J. Virol. 68 (1994) 177-186
    • (1994) J. Virol. , vol.68 , pp. 177-186
    • Coombs, K.M.1    Mak, S.C.2    Petrycky-Cox, L.D.3
  • 17
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Philos. Trans. R. Soc. Lond. B Biol. Sci. 261 (1971) 221-230
    • (1971) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 18
    • 43049103627 scopus 로고    scopus 로고
    • DeLano, W.L., 2004. The PyMOL molecular graphics system. World Wide Web.
    • DeLano, W.L., 2004. The PyMOL molecular graphics system. World Wide Web.
  • 19
    • 0020079241 scopus 로고
    • Activation and characterization of the reovirus transcriptase: genetic analysis
    • Drayna D., and Fields B.N. Activation and characterization of the reovirus transcriptase: genetic analysis. J. Virol. 41 (1982) 110-118
    • (1982) J. Virol. , vol.41 , pp. 110-118
    • Drayna, D.1    Fields, B.N.2
  • 20
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus 1
    • Dryden K.A., Farsetta D.L., Wang G., Keegan J.M., Fields B.N., Baker T.S., and Nibert M.L. Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus 1. Virology 245 (1998) 33-46
    • (1998) Virology , vol.245 , pp. 33-46
    • Dryden, K.A.1    Farsetta, D.L.2    Wang, G.3    Keegan, J.M.4    Fields, B.N.5    Baker, T.S.6    Nibert, M.L.7
  • 21
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden K.A., Wang G., Yeager M., Nibert M.L., Coombs K.M., Furlong D.B., Fields B.N., and Baker T.S. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122 (1993) 1023-1041
    • (1993) J. Cell Biol. , vol.122 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 22
    • 0016442397 scopus 로고
    • Reovirus messenger RNA contains a methylated, blocked 5′-terminal structure: m-7G(5')ppp(5')G-MpCp-
    • Furuichi Y., Morgan M., Muthukrishnan S., and Shatkin A.J. Reovirus messenger RNA contains a methylated, blocked 5′-terminal structure: m-7G(5')ppp(5')G-MpCp-. Proc. Natl. Acad. Sci. USA 72 (1975) 362-366
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 362-366
    • Furuichi, Y.1    Morgan, M.2    Muthukrishnan, S.3    Shatkin, A.J.4
  • 23
    • 0015151975 scopus 로고
    • Viral RNA polymerases: electron microscopy of reovirus reaction cores
    • Gillies S., Bullivant S., and Bellamy A.R. Viral RNA polymerases: electron microscopy of reovirus reaction cores. Science 174 (1971) 694-696
    • (1971) Science , vol.174 , pp. 694-696
    • Gillies, S.1    Bullivant, S.2    Bellamy, A.R.3
  • 24
    • 43049109692 scopus 로고
    • Animal and plant viruses with double-helical RNA
    • Gomatos P.J., and Tamm I. Animal and plant viruses with double-helical RNA. Proc. Natl. Acad. Sci. USA 50 (1963) 878-885
    • (1963) Proc. Natl. Acad. Sci. USA , vol.50 , pp. 878-885
    • Gomatos, P.J.1    Tamm, I.2
  • 26
    • 0033602711 scopus 로고    scopus 로고
    • Mammalian reovirs L3 gene sequences and evidence for a distinct amino-terminal region of the λ1 protein
    • Harrison S.J., Farsetta D.L., Kim J., Noble S., Broering T.J., and Nibert M.L. Mammalian reovirs L3 gene sequences and evidence for a distinct amino-terminal region of the λ1 protein. Virology 258 (1999) 54-64
    • (1999) Virology , vol.258 , pp. 54-64
    • Harrison, S.J.1    Farsetta, D.L.2    Kim, J.3    Noble, S.4    Broering, T.J.5    Nibert, M.L.6
  • 27
    • 0019489532 scopus 로고
    • Biophysical studies of reovirus type 3. IV. Low-angle x-ray diffraction studies
    • Harvey J.D., Bellamy A.R., Earnshaw W.C., and Schutt C. Biophysical studies of reovirus type 3. IV. Low-angle x-ray diffraction studies. Virology 112 (1981) 240-249
    • (1981) Virology , vol.112 , pp. 240-249
    • Harvey, J.D.1    Bellamy, A.R.2    Earnshaw, W.C.3    Schutt, C.4
  • 28
    • 43049124962 scopus 로고    scopus 로고
    • Hilmer, J.K., Zlotnik, A., Bothner, B., 2007. Conformational equilibria and rates of localized motion within hepatitis B virus capsids. J. Mol. Biol. (available online 22 October 2007).
    • Hilmer, J.K., Zlotnik, A., Bothner, B., 2007. Conformational equilibria and rates of localized motion within hepatitis B virus capsids. J. Mol. Biol. (available online 22 October 2007).
  • 29
    • 0002420633 scopus 로고
    • The reovirus particle
    • Joklik W.K. (Ed), Plenum Press, New York
    • Joklik W.K. The reovirus particle. In: Joklik W.K. (Ed). The Reoviridae (1983), Plenum Press, New York 9-78
    • (1983) The Reoviridae , pp. 9-78
    • Joklik, W.K.1
  • 30
    • 0001146459 scopus 로고    scopus 로고
    • Packaging and release of the viral genome
    • Chiu W., Burnett R.M., and Garcea R.L. (Eds), Oxford University Press, New York
    • Johnson J., and Rueckert R. Packaging and release of the viral genome. In: Chiu W., Burnett R.M., and Garcea R.L. (Eds). Structural Biology of Viruses (1997), Oxford University Press, New York 269-287
    • (1997) Structural Biology of Viruses , pp. 269-287
    • Johnson, J.1    Rueckert, R.2
  • 31
    • 0014965089 scopus 로고
    • An extraordinary temperature dependence of the reovirus transcriptase
    • Kapuler A.M. An extraordinary temperature dependence of the reovirus transcriptase. Biochemistry 9 (1970) 4453-4457
    • (1970) Biochemistry , vol.9 , pp. 4453-4457
    • Kapuler, A.M.1
  • 32
    • 1042289782 scopus 로고    scopus 로고
    • Nucleoside and RNA triphosphatase activities of orthoreovirus transcriptase cofactor μ2
    • Kim J., Parker J.S.L., Murray K.E., and Nibert M.L. Nucleoside and RNA triphosphatase activities of orthoreovirus transcriptase cofactor μ2. J. Biol. Chem. 279 (2004) 4394-4403
    • (2004) J. Biol. Chem. , vol.279 , pp. 4394-4403
    • Kim, J.1    Parker, J.S.L.2    Murray, K.E.3    Nibert, M.L.4
  • 33
    • 0036889158 scopus 로고    scopus 로고
    • The hydrophobic amino-terminal arm of reovirus core shell protein λ1 is dispensable for particle assembly
    • Kim J., Zhang X., Centonze V.E., Bowman V.D., Noble S., Baker T.S., and Nibert M.L. The hydrophobic amino-terminal arm of reovirus core shell protein λ1 is dispensable for particle assembly. J. Virol. 76 (2002) 12211-12222
    • (2002) J. Virol. , vol.76 , pp. 12211-12222
    • Kim, J.1    Zhang, X.2    Centonze, V.E.3    Bowman, V.D.4    Noble, S.5    Baker, T.S.6    Nibert, M.L.7
  • 34
    • 0028200822 scopus 로고
    • Reovirus exists in the form of 13 particle species that differ in their content of protein sigma 1
    • Larson S.M., Antczak J.B., and Joklik W.K. Reovirus exists in the form of 13 particle species that differ in their content of protein sigma 1. Virology 201 (1994) 303-311
    • (1994) Virology , vol.201 , pp. 303-311
    • Larson, S.M.1    Antczak, J.B.2    Joklik, W.K.3
  • 35
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • Lawton J.A., Estes M.K., and Prasad B.V.V. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 4 (1997) 118-121
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.V.3
  • 36
    • 0019522275 scopus 로고
    • Protein sigma 1 is the reovirus cell attachment protein
    • Lee P.W., Hayes E.C., and Joklik W.K. Protein sigma 1 is the reovirus cell attachment protein. Virology 108 (1981) 156-163
    • (1981) Virology , vol.108 , pp. 156-163
    • Lee, P.W.1    Hayes, E.C.2    Joklik, W.K.3
  • 37
    • 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., Maegley K.A., Yu X., Ferre R.A., Lingardo L.K., Diehl W., Parge H.E., Dragovich P.S., and Fuhrman S.A. The crystal structure of the RNA-dependent RNA polymerase from human rhinovirus: a dual function target for common cold antiviral therapy. Structure 12 (2005) 1533-1544
    • (2005) 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
  • 38
    • 0015318401 scopus 로고
    • An ultrastructural study of virions and cores of reovirus type 3
    • Luftig R.B., Kilham S.S., Hay A.J., Zweerink H.J., and Joklik W.K. An ultrastructural study of virions and cores of reovirus type 3. Virology 48 (1972) 170-181
    • (1972) Virology , vol.48 , pp. 170-181
    • Luftig, R.B.1    Kilham, S.S.2    Hay, A.J.3    Zweerink, H.J.4    Joklik, W.K.5
  • 39
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2
    • Luongo C.L., Reinisch K.M., Harrison S.C., and Nibert M.L. Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2. J. Biol. Chem. 275 (2000) 2804-2810
    • (2000) J. Biol. Chem. , vol.275 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 40
    • 0025947194 scopus 로고
    • Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase
    • Mao Z.X., and Joklik W.K. Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase. Virology 185 (1991) 377-386
    • (1991) Virology , vol.185 , pp. 377-386
    • Mao, Z.X.1    Joklik, W.K.2
  • 41
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 42
    • 0029911783 scopus 로고    scopus 로고
    • Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells
    • McBride A.E., Schlegel A., and Kirkegaard K. Human protein Sam68 relocalization and interaction with poliovirus RNA polymerase in infected cells. Proc. Natl. Acad. Sci. USA 93 (1996) 2296-2301
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2296-2301
    • McBride, A.E.1    Schlegel, A.2    Kirkegaard, K.3
  • 43
    • 0033818477 scopus 로고    scopus 로고
    • A comparative analysis of freon substitutes in the purification of reovirus and calicivirus
    • Mendez I.I., Hermann L.L., Hazelton P.R., and Coombs K.M. A comparative analysis of freon substitutes in the purification of reovirus and calicivirus. J. Virol. Methods 90 (2000) 59-67
    • (2000) J. Virol. Methods , vol.90 , pp. 59-67
    • Mendez, I.I.1    Hermann, L.L.2    Hazelton, P.R.3    Coombs, K.M.4
  • 44
    • 0038045776 scopus 로고    scopus 로고
    • Digestion pattern of reovirus outer capsid protein sigma3 determined by mass spectrometry
    • Mendez I.I., She Y.M., Ens W., and Coombs K.M. Digestion pattern of reovirus outer capsid protein sigma3 determined by mass spectrometry. Virology 311 (2003) 289-304
    • (2003) Virology , vol.311 , pp. 289-304
    • Mendez, I.I.1    She, Y.M.2    Ens, W.3    Coombs, K.M.4
  • 45
    • 0026072563 scopus 로고
    • The three-dimensional structure of reovirus obtained by cryo-electron microscopy
    • Metcalf P., Cyrklaff M., and Adrian M. The three-dimensional structure of reovirus obtained by cryo-electron microscopy. EMBO J. 10 (1991) 3129-3136
    • (1991) EMBO J. , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 46
    • 0024401164 scopus 로고
    • A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses
    • Morozov S.Y. A possible relationship of reovirus putative RNA polymerase to polymerases of positive-strand RNA viruses. Nucleic Acids Res. 17 (1989) 5394
    • (1989) Nucleic Acids Res. , vol.17 , pp. 5394
    • Morozov, S.Y.1
  • 48
    • 0031950354 scopus 로고    scopus 로고
    • Structure of mammalian orthoreovirus particles
    • Nibert M.L. Structure of mammalian orthoreovirus particles. Curr. Top. Microbiol. Immunol. 233 I (1998) 1-30
    • (1998) Curr. Top. Microbiol. Immunol. , vol.233 , Issue.I , pp. 1-30
    • Nibert, M.L.1
  • 49
    • 0029834595 scopus 로고    scopus 로고
    • Nonrandom segregation of parental alleles in reovirus reassortants
    • Nibert M.L., Margraf R.L., and Coombs K.M. Nonrandom segregation of parental alleles in reovirus reassortants. J. Virol. 70 (1996) 7295-7300
    • (1996) J. Virol. , vol.70 , pp. 7295-7300
    • Nibert, M.L.1    Margraf, R.L.2    Coombs, K.M.3
  • 50
    • 0031055059 scopus 로고    scopus 로고
    • Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1
    • Noble S., and Nibert M.L. Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1. J. Virol. 71 (1997) 2182-2191
    • (1997) J. Virol. , vol.71 , pp. 2182-2191
    • Noble, S.1    Nibert, M.L.2
  • 51
    • 0032567393 scopus 로고    scopus 로고
    • Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure
    • O'Reilly E.K., and Kao C.C. Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure. Virology 252 (1998) 287-303
    • (1998) Virology , vol.252 , pp. 287-303
    • O'Reilly, E.K.1    Kao, C.C.2
  • 52
    • 34250643613 scopus 로고    scopus 로고
    • The structure of birnavirus polymerase reveals a distinct active site topology
    • Pan J., Vakharia V.N., and Tao Y.J. The structure of birnavirus polymerase reveals a distinct active site topology. Proc. Natl. Acad. Sci. USA 104 (2007) 7385-7390
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 7385-7390
    • Pan, J.1    Vakharia, V.N.2    Tao, Y.J.3
  • 54
    • 0021153754 scopus 로고
    • Reovirus RNA transcriptase: evidence for a conformational change during activation of the core particle
    • Powell K.F., Harvey J.D., and Bellamy A.R. Reovirus RNA transcriptase: evidence for a conformational change during activation of the core particle. Virology 137 (1984) 1-8
    • (1984) Virology , vol.137 , pp. 1-8
    • Powell, K.F.1    Harvey, J.D.2    Bellamy, A.R.3
  • 56
    • 34547753377 scopus 로고    scopus 로고
    • Picornaviridae: the viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippencott Williams & Wilkins, Philadelphia
    • Racaniello V.R. Picornaviridae: the viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. fifth ed. (2007), Lippencott Williams & Wilkins, Philadelphia 795-838
    • (2007) Fields Virology. fifth ed. , pp. 795-838
    • Racaniello, V.R.1
  • 57
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Ǻ resolution
    • Reinisch K.M., Nibert M.L., and Harrison S.C. Structure of the reovirus core at 3.6 Ǻ resolution. Nature 404 (2000) 960-967
    • (2000) Nature , vol.404 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 58
    • 34548650332 scopus 로고    scopus 로고
    • Orthoreoviruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippencott Williams & Wilkins, Philadelphia
    • Schiff L.A., Nibert M.L., and Tyler K.L. Orthoreoviruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. fifth ed. (2007), Lippencott Williams & Wilkins, Philadelphia 1853-1915
    • (2007) Fields Virology. fifth ed. , pp. 1853-1915
    • Schiff, L.A.1    Nibert, M.L.2    Tyler, K.L.3
  • 59
  • 60
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko A., Chernushevich I., Ens W., Standing K.G., Thomson B., Wilm M., and Mann M. Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom. 11 (1997) 1015-1024
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 61
    • 0027177215 scopus 로고
    • Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase
    • Starnes M.C., and Joklik W.K. Reovirus protein lambda 3 is a poly(C)-dependent poly(G) polymerase. Virology 193 (1993) 356-366
    • (1993) Virology , vol.193 , pp. 356-366
    • Starnes, M.C.1    Joklik, W.K.2
  • 62
    • 33747621427 scopus 로고    scopus 로고
    • Visualizing polynucleotide polymerase machines at work
    • Steitz T.A. Visualizing polynucleotide polymerase machines at work. EMBO J. 25 (2006) 3458-3468
    • (2006) EMBO J. , vol.25 , pp. 3458-3468
    • Steitz, T.A.1
  • 63
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage-structural studies of reovirus polymerase lambda3
    • Tao Y., Farsetta D.L., Nibert M.L., and Harrison S.C. RNA synthesis in a cage-structural studies of reovirus polymerase lambda3. Cell 111 (2002) 733-745
    • (2002) Cell , vol.111 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 65
    • 0027432147 scopus 로고
    • Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genomic segments L1, L2, L3, and S2
    • Xu P., Miller S.E., and Joklik W.K. Generation of reovirus core-like particles in cells infected with hybrid vaccinia viruses that express genomic segments L1, L2, L3, and S2. Virology 197 (1993) 726-731
    • (1993) Virology , vol.197 , pp. 726-731
    • Xu, P.1    Miller, S.E.2    Joklik, W.K.3
  • 66
    • 0030030595 scopus 로고    scopus 로고
    • The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles
    • Yin P., Cheang M., and Coombs K.M. The M1 gene is associated with differences in the temperature optimum of the transcriptase activity in reovirus core particles. J. Virol. 70 (1996) 1223-1227
    • (1996) J. Virol. , vol.70 , pp. 1223-1227
    • Yin, P.1    Cheang, M.2    Coombs, K.M.3
  • 67
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 76 angstrom
    • Zhang X., Walker S.B., Chipman P.R., Nibert M.L., and Baker T.S. Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 76 angstrom. Nat. Struct. Biol. 10 (2003) 1011-1018
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.