메뉴 건너뛰기




Volumn 101, Issue 1, 2004, Pages 57-66

Nonstructural proteins involved in genome packaging and replication of rotaviruses and other members of the Reoviridae

Author keywords

Cryoelectron; Icosahedrons; Replication intermediates

Indexed keywords

BASIC PROTEIN; DOUBLE STRANDED RNA; MESSENGER RNA; RIBOZYME; SINGLE STRANDED DNA BINDING PROTEIN; SMALL SUBUNIT RIBOSOMAL RNA; VIRUS ENZYME; VIRUS PROTEIN;

EID: 1542268891     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2003.12.006     Document Type: Article
Times cited : (70)

References (78)
  • 2
    • 0031736033 scopus 로고    scopus 로고
    • Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2
    • Afrikanova I., Fabretti E., Miozzo M.C., Burrone O.R. Rotavirus NSP5 phosphorylation is up-regulated by interaction with NSP2. J. Gen. Virol. 79:1998;2679-2686.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2679-2686
    • Afrikanova, I.1    Fabretti, E.2    Miozzo, M.C.3    Burrone, O.R.4
  • 3
    • 0026529484 scopus 로고
    • Reovirus genome segment assortment into progeny genomes studied by the use of monoclonal antibodies directed against reovirus proteins
    • Antczak J.B., Joklik W.K. Reovirus genome segment assortment into progeny genomes studied by the use of monoclonal antibodies directed against reovirus proteins. Virology. 187:1992;760-776.
    • (1992) Virology , vol.187 , pp. 760-776
    • Antczak, J.B.1    Joklik, W.K.2
  • 5
    • 0031060310 scopus 로고    scopus 로고
    • Serine protein kinase activity associated with rotavirus phosphoprotein NSP5
    • Blackhall J., Fuentes A., Hansen K., Magnusson G. Serine protein kinase activity associated with rotavirus phosphoprotein NSP5. J. Virol. 71:1997;138-144.
    • (1997) J. Virol. , vol.71 , pp. 138-144
    • Blackhall, J.1    Fuentes, A.2    Hansen, K.3    Magnusson, G.4
  • 6
    • 2642702588 scopus 로고    scopus 로고
    • Analysis of rotavirus nonstructural protein NSP5 phosphorylation
    • Blackhall J., Munoz M., Fuentes A., Magnusson G. Analysis of rotavirus nonstructural protein NSP5 phosphorylation. J. Virol. 72:1998;6398-6405.
    • (1998) J. Virol. , vol.72 , pp. 6398-6405
    • Blackhall, J.1    Munoz, M.2    Fuentes, A.3    Magnusson, G.4
  • 7
    • 0027452772 scopus 로고
    • Herpes simplex virus type1 ICP8: Helix destabilizing properties
    • Boehmer P.E., Lehman I.R. Herpes simplex virus type1 ICP8: helix destabilizing properties. J. Virol. 67:1993;711-715.
    • (1993) J. Virol. , vol.67 , pp. 711-715
    • Boehmer, P.E.1    Lehman, I.R.2
  • 8
    • 0031595933 scopus 로고    scopus 로고
    • The reovirus protein mu2* encoded by the M1 gene* is an RNA-binding protein
    • Brentano L., Noah D.L., Brown E.G., Sherry B. The reovirus protein mu2* encoded by the M1 gene* is an RNA-binding protein. J. Virol. 72:1998;8354-8357.
    • (1998) J. Virol. , vol.72 , pp. 8354-8357
    • Brentano, L.1    Noah, D.L.2    Brown, E.G.3    Sherry, B.4
  • 9
    • 0027420113 scopus 로고
    • Characterization of virus inclusion bodies in bluetongue virus-infected cells
    • Brookes S.M., Hyatt A.D., Eaton B.T. Characterization of virus inclusion bodies in bluetongue virus-infected cells. J. Gen. Virol. 74:1993;525-530.
    • (1993) J. Gen. Virol. , vol.74 , pp. 525-530
    • Brookes, S.M.1    Hyatt, A.D.2    Eaton, B.T.3
  • 10
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double-stranded RNA virus phi6
    • Butcher S.J., Dokland T., Ojala P.M., Bamford D.H., Fuller S.D. Intermediates in the assembly pathway of the double-stranded RNA virus phi6. EMBO J. 16:1997;4477-4487.
    • (1997) EMBO J. , vol.16 , pp. 4477-4487
    • Butcher, S.J.1    Dokland, T.2    Ojala, P.M.3    Bamford, D.H.4    Fuller, S.D.5
  • 11
    • 0025041270 scopus 로고
    • Intracellular RNA synthesis directed by temperature-sensitive mutants of simian rotavirus SA11
    • Chen D., Gombold J.L., Ramig R.F. Intracellular RNA synthesis directed by temperature-sensitive mutants of simian rotavirus SA11. Virology. 178:1990;143-151.
    • (1990) Virology , vol.178 , pp. 143-151
    • Chen, D.1    Gombold, J.L.2    Ramig, R.F.3
  • 12
    • 0033527897 scopus 로고    scopus 로고
    • Rotavirus open cores catalyze 5′-capping and methylation of exogenous RNA: Evidence that VP3 is a methyltransferase
    • Chen D., Luongo C.L., Nibert M.L., Patton J.T. Rotavirus open cores catalyze 5′-capping and methylation of exogenous RNA: evidence that VP3 is a methyltransferase. Virology. 265:1999;120-130.
    • (1999) Virology , vol.265 , pp. 120-130
    • Chen, D.1    Luongo, C.L.2    Nibert, M.L.3    Patton, J.T.4
  • 14
    • 0017757633 scopus 로고
    • Ribonucleic acid polymerase activity associated with purified calf rotavirus
    • Cohen J. Ribonucleic acid polymerase activity associated with purified calf rotavirus. J. Gen. Virol. 36:1977;395-402.
    • (1977) J. Gen. Virol. , vol.36 , pp. 395-402
    • Cohen, J.1
  • 15
    • 0033607480 scopus 로고    scopus 로고
    • A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage phi6
    • de Haas F., Paatero A.O., Mindich L., Bamford D.H., Fuller S.D. A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage phi6. J. Mol. Biol. 294:1999;357-372.
    • (1999) J. Mol. Biol. , vol.294 , pp. 357-372
    • De Haas, F.1    Paatero, A.O.2    Mindich, L.3    Bamford, D.H.4    Fuller, S.D.5
  • 16
    • 0024082836 scopus 로고
    • Characterization of a nonstructural phosphoprotein of two orbiviruses
    • Devaney M.A., Kendall J., Grubman M.J. Characterization of a nonstructural phosphoprotein of two orbiviruses. Virus Res. 11:1988;151-164.
    • (1988) Virus Res. , vol.11 , pp. 151-164
    • Devaney, M.A.1    Kendall, J.2    Grubman, M.J.3
  • 17
    • 0036122465 scopus 로고    scopus 로고
    • Rotavirus NSP5: Mapping phosphorylation sites and kinase activation and viroplasm localization domains
    • Eichwald C., Vascotto F., Fabbretti E., Burrone O.R. Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains. J. Virol. 76:2002;3461-3470.
    • (2002) J. Virol. , vol.76 , pp. 3461-3470
    • Eichwald, C.1    Vascotto, F.2    Fabbretti, E.3    Burrone, O.R.4
  • 18
    • 0001581287 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • Knipe D., Howley M., et al. (Eds.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Estes, M.K., 2001. Rotaviruses and their replication, In: Knipe D., Howley M., et al. (Eds.), Fields Virology, 4th edition. Lippincott Williams & Wilkins, Philadelphia, PA, pp. 1747-1785.
    • (2001) Fields Virology, 4th Edition , pp. 1747-1785
    • Estes, M.K.1
  • 19
    • 0032970118 scopus 로고    scopus 로고
    • Two nonstructural rotavirus proteins* NSP2 and NSP5* form viroplasm-like structures in vivo
    • Fabbretti E., Afrikanova I., Vascotto F., Burrone O.R. Two nonstructural rotavirus proteins* NSP2 and NSP5* form viroplasm-like structures in vivo. J. Gen. Virol. 80:1999;333-339.
    • (1999) J. Gen. Virol. , vol.80 , pp. 333-339
    • Fabbretti, E.1    Afrikanova, I.2    Vascotto, F.3    Burrone, O.R.4
  • 20
    • 0026627864 scopus 로고
    • Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage phi 6
    • Frilander M., Gottlieb P., Strassman J., Bamford D.H., Mindich L. Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage phi 6. J. Virol. 66:1992;5013-5017.
    • (1992) J. Virol. , vol.66 , pp. 5013-5017
    • Frilander, M.1    Gottlieb, P.2    Strassman, J.3    Bamford, D.H.4    Mindich, L.5
  • 21
    • 0024317561 scopus 로고
    • Characterization of rotavirus replication intermediates: A model for the assembly of single-shelled particles
    • Gallegos C.O., Patton J.T. Characterization of rotavirus replication intermediates: a model for the assembly of single-shelled particles. Virology. 172:1989;616-627.
    • (1989) Virology , vol.172 , pp. 616-627
    • Gallegos, C.O.1    Patton, J.T.2
  • 22
    • 0032484483 scopus 로고    scopus 로고
    • Amino terminus of reovirus nonstructural protein σnS is important for ssRNA binding and nucleoprotein complex formation
    • Gillian A.L., Nibert M.L. Amino terminus of reovirus nonstructural protein σNS is important for ssRNA binding and nucleoprotein complex formation. Virology. 240:1998;1-11.
    • (1998) Virology , vol.240 , pp. 1-11
    • Gillian, A.L.1    Nibert, M.L.2
  • 23
    • 0033625344 scopus 로고    scopus 로고
    • Reovirus protein sigmaNS binds in multiple copies to single-stranded RNA and shares properties with single-stranded DNA binding proteins
    • Gillian A.L., Schmechel S.C., Livny J., Schiff L.A., Nibert M.L. Reovirus protein sigmaNS binds in multiple copies to single-stranded RNA and shares properties with single-stranded DNA binding proteins. J. Virol. 74:2000;5939-5948.
    • (2000) J. Virol. , vol.74 , pp. 5939-5948
    • Gillian, A.L.1    Schmechel, S.C.2    Livny, J.3    Schiff, L.A.4    Nibert, M.L.5
  • 24
    • 0019391135 scopus 로고
    • Small reovirus particle composed solely of sigma NS with specificity for binding different nucleic acids
    • Gomatos P.J., Prakash O., Stamatos N.M. Small reovirus particle composed solely of sigma NS with specificity for binding different nucleic acids. J. Virol. 39:1981;115-124.
    • (1981) J. Virol. , vol.39 , pp. 115-124
    • Gomatos, P.J.1    Prakash, O.2    Stamatos, N.M.3
  • 25
    • 0018928388 scopus 로고
    • Small reovirus-specific particle with polycytidylate-dependent RNA polymerase activity
    • Gomatos P.J., Stamatos N.M., Sarkar N.H. Small reovirus-specific particle with polycytidylate-dependent RNA polymerase activity. J. Virol. 36:1980;556-565.
    • (1980) J. Virol. , vol.36 , pp. 556-565
    • Gomatos, P.J.1    Stamatos, N.M.2    Sarkar, N.H.3
  • 26
  • 27
    • 0025810911 scopus 로고
    • Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine
    • Gonzalez S.A., Burrone O.R. Rotavirus NS26 is modified by addition of single O-linked residues of N-acetylglucosamine. Virology. 182:1991;8-16.
    • (1991) Virology , vol.182 , pp. 8-16
    • Gonzalez, S.A.1    Burrone, O.R.2
  • 28
    • 0026657924 scopus 로고
    • Protein P4 of the bacteriophage phi 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity
    • Gottlieb P., Strassman J., Mindich L. Protein P4 of the bacteriophage phi 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity. J. Virol. 66:1992;6220-6222.
    • (1992) J. Virol. , vol.66 , pp. 6220-6222
    • Gottlieb, P.1    Strassman, J.2    Mindich, L.3
  • 29
    • 0025893698 scopus 로고
    • In vitro packaging of the bacteriophage phi 6 ssRNA genomic precursors
    • Gottlieb P., Strassman J., Frucht A., Qiao X.Y., Mindich L. In vitro packaging of the bacteriophage phi 6 ssRNA genomic precursors. Virology. 181:1991;589-594.
    • (1991) Virology , vol.181 , pp. 589-594
    • Gottlieb, P.1    Strassman, J.2    Frucht, A.3    Qiao, X.Y.4    Mindich, L.5
  • 30
  • 31
    • 0022872976 scopus 로고
    • Characterization of subviral particles in cells infected with simian rotavirus SA11
    • Helmberger-Jones M., Patton J.T. Characterization of subviral particles in cells infected with simian rotavirus SA11. Virology. 155:1986;655-665.
    • (1986) Virology , vol.155 , pp. 655-665
    • Helmberger-Jones, M.1    Patton, J.T.2
  • 32
    • 0033865718 scopus 로고    scopus 로고
    • NTP binding and phosphohydrolase activity associated with purified bluetongue virus nonstructural protein NS2
    • Horscroft N.J., Roy P. NTP binding and phosphohydrolase activity associated with purified bluetongue virus nonstructural protein NS2. J. Gen. Virol. 81:2000;1961-1965.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1961-1965
    • Horscroft, N.J.1    Roy, P.2
  • 33
    • 0016302387 scopus 로고
    • Denaturation of T4 DNA by an in vitro processed gene 32 protein
    • Hosoda J., Takacs B., Brack C. Denaturation of T4 DNA by an in vitro processed gene 32 protein. FEBS Lett. 47:1974;338-342.
    • (1974) FEBS Lett. , vol.47 , pp. 338-342
    • Hosoda, J.1    Takacs, B.2    Brack, C.3
  • 34
    • 0017253105 scopus 로고
    • Reovirus-coded polypeptides in infected cells: Isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively
    • Huismans H., Joklik W.K. Reovirus-coded polypeptides in infected cells: Isolation of two native monomeric polypeptides with affinity for single-stranded and double-stranded RNA, respectively. Virology. 70:1976;411-424.
    • (1976) Virology , vol.70 , pp. 411-424
    • Huismans, H.1    Joklik, W.K.2
  • 35
    • 0023270054 scopus 로고
    • In vitro phosphorylation and purification of a nonstructural protein of bluetongue virus with affinity for their single stranded RNA
    • Huismans H., Van Dijk A.A., Bauskin A.R. In vitro phosphorylation and purification of a nonstructural protein of bluetongue virus with affinity for their single stranded RNA. J. Virol. 61:1987;3589-3595.
    • (1987) J. Virol. , vol.61 , pp. 3589-3595
    • Huismans, H.1    Van Dijk, A.A.2    Bauskin, A.R.3
  • 36
    • 0037118101 scopus 로고    scopus 로고
    • X-ray structure of rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold
    • Jayaram H., Taraporewala Z., Patton J.T., Venkataram Prasad B.V. X-ray structure of rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold. Nature. 417:2002;311-315.
    • (2002) Nature , vol.417 , pp. 311-315
    • Jayaram, H.1    Taraporewala, Z.2    Patton, J.T.3    Venkataram Prasad, B.V.4
  • 37
    • 0001659603 scopus 로고    scopus 로고
    • Rotaviruses
    • Knipe D., Howley M., et al. (Eds.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Kapikian A.Z., 2001. Rotaviruses. In: Knipe D., Howley M., et al. (Eds.), Fields Virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA, pp. 1787-1833.
    • (2001) Fields Virology, 4th Ed. , pp. 1787-1833
    • Kapikian, A.Z.1
  • 38
    • 0027932436 scopus 로고
    • The rotavirus RNA binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase
    • Kattoura M.D., Chen X., Patton J.T. The rotavirus RNA binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase. Virology. 202:1994;803-813.
    • (1994) Virology , vol.202 , pp. 803-813
    • Kattoura, M.D.1    Chen, X.2    Patton, J.T.3
  • 39
    • 0027093812 scopus 로고
    • The rotavirus nonstructural protein* NS35* is a nonspecific RNA-binding protein
    • Kattoura M., Clapp L.L., Patton J.T. The rotavirus nonstructural protein* NS35* is a nonspecific RNA-binding protein. Virology. 191:1992;698-708.
    • (1992) Virology , vol.191 , pp. 698-708
    • Kattoura, M.1    Clapp, L.L.2    Patton, J.T.3
  • 41
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • Lawton J.A., Estes M.K., Prasad B.V.V. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 2:1997a;118-121.
    • (1997) Nat. Struct. Biol. , vol.2 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.V.3
  • 42
    • 0030768785 scopus 로고    scopus 로고
    • Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal deleted VP2: Implications for the architecture of the VP2 capsid layer
    • Lawton J.A., Zeng C.Q.-Y., Mukherjee S.K., Cohen J., Estes M.K., Prasad B.V.V. Three-dimensional structural analysis of recombinant rotavirus-like particles with intact and amino-terminal deleted VP2: implications for the architecture of the VP2 capsid layer. J. Virol. 71:1997b;7353-7360.
    • (1997) J. Virol. , vol.71 , pp. 7353-7360
    • Lawton, J.A.1    Zeng, C.Q.-Y.2    Mukherjee, S.K.3    Cohen, J.4    Estes, M.K.5    Prasad, B.V.V.6
  • 43
    • 0026766537 scopus 로고
    • Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity
    • Lui M., Mattion N.M., Estes M.K. Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity. Virology. 188:1992;77-84.
    • (1992) Virology , vol.188 , pp. 77-84
    • Lui, M.1    Mattion, N.M.2    Estes, M.K.3
  • 44
    • 0025980112 scopus 로고
    • Expression of rotavirus proteins encoded by alternative open reading frames of genome segment 11*
    • Mattion N.M., Mitchell D.B., Both G.W., Estes M.K. Expression of rotavirus proteins encoded by alternative open reading frames of genome segment 11*. Virology. 181:1991;295-304.
    • (1991) Virology , vol.181 , pp. 295-304
    • Mattion, N.M.1    Mitchell, D.B.2    Both, G.W.3    Estes, M.K.4
  • 45
    • 0034690808 scopus 로고    scopus 로고
    • Reovirus mu2 protein determines strain-specific differences in the rate of viral inclusion formation in L929 cells
    • Mbisa J.L., Becker M.M., Zou S., Dermody T.S., Brown E.G. Reovirus mu2 protein determines strain-specific differences in the rate of viral inclusion formation in L929 cells. Virology. 272:2000;16-26.
    • (2000) Virology , vol.272 , pp. 16-26
    • Mbisa, J.L.1    Becker, M.M.2    Zou, S.3    Dermody, T.S.4    Brown, E.G.5
  • 46
    • 0028285251 scopus 로고
    • Adenovirus DNA binding protein: Helix-destabilizing activity
    • Monaghan A., Webster A., Ronald T.H. Adenovirus DNA binding protein: helix-destabilizing activity. Nucleic Acids Res. 22:1994;742-748.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 742-748
    • Monaghan, A.1    Webster, A.2    Ronald, T.H.3
  • 47
    • 0001123624 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • Knipe, D., Howley, M., et al. (Eds.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Nibert, M.L., Schiff, L.A., 2001. Reoviruses and their replication, In: Knipe, D., Howley, M., et al. (Eds.), Fields Virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA, pp. 1679-1728.
    • (2001) Fields Virology, 4th Ed. , pp. 1679-1728
    • Nibert, M.L.1    Schiff, L.A.2
  • 48
    • 0031055059 scopus 로고    scopus 로고
    • Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein lambda1
    • Noble S., 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
  • 49
    • 0028805187 scopus 로고
    • Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions
    • Paatero A.O., Syvaoja J.E., Bamford D.H. Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions. J Virol. 69:1995;6729-6734.
    • (1995) J Virol. , vol.69 , pp. 6729-6734
    • Paatero, A.O.1    Syvaoja, J.E.2    Bamford, D.H.3
  • 50
    • 0022883817 scopus 로고
    • Synthesis of simian rotavirus SA11 double-stranded RNA in a cell-free system
    • Patton J.T. Synthesis of simian rotavirus SA11 double-stranded RNA in a cell-free system. Virus Res. 6:1986;217-233.
    • (1986) Virus Res. , vol.6 , pp. 217-233
    • Patton, J.T.1
  • 51
    • 0023677273 scopus 로고
    • Structure and protein composition of the rotavirus replicase particle
    • Patton J.T., Gallegos C.O. Structure and protein composition of the rotavirus replicase particle. Virology. 166:1988;358-365.
    • (1988) Virology , vol.166 , pp. 358-365
    • Patton, J.T.1    Gallegos, C.O.2
  • 52
    • 0025281467 scopus 로고
    • Rotavirus RNA replication: Single-stranded RNA extends form the replicase particle
    • Patton J.T., Gallegos C.O. Rotavirus RNA replication: single-stranded RNA extends form the replicase particle. J. Gen. Virol. 71:1990;1087-1094.
    • (1990) J. Gen. Virol. , vol.71 , pp. 1087-1094
    • Patton, J.T.1    Gallegos, C.O.2
  • 53
    • 0030831560 scopus 로고    scopus 로고
    • Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome
    • Patton J.T., Jones M.T., Kalbach A.N., He Y.W., Xiaobo J. Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome. J. Virol. 71:1997;9618-9626.
    • (1997) J. Virol. , vol.71 , pp. 9618-9626
    • Patton, J.T.1    Jones, M.T.2    Kalbach, A.N.3    He, Y.W.4    Xiaobo, J.5
  • 54
    • 1542274427 scopus 로고    scopus 로고
    • Rotavirus genome replication: Role of the RNA-binding proteins
    • Gray J., Desselberger U. (Eds.), Elsevier, Amsterdam, in press.
    • Patton, J.T., Kearney, K., Taraporewala, Z., 2002. Rotavirus genome replication: role of the RNA-binding proteins. In: Gray J., Desselberger U. (Eds.), Perspectives in Medical Virology: Viral Gastroenteritis. Elsevier, Amsterdam, in press.
    • (2002) Perspectives in Medical Virology: Viral Gastroenteritis
    • Patton, J.T.1    Kearney, K.2    Taraporewala, Z.3
  • 55
    • 0021238996 scopus 로고
    • Ultrastructural localization of rotavirus antigens using colloidal gold
    • Petrie B.L., Greenberg H.B., Graham D.Y., Estes M.K. Ultrastructural localization of rotavirus antigens using colloidal gold. Virus Res. 1:1984;133-152.
    • (1984) Virus Res. , vol.1 , pp. 133-152
    • Petrie, B.L.1    Greenberg, H.B.2    Graham, D.Y.3    Estes, M.K.4
  • 57
    • 0031060143 scopus 로고    scopus 로고
    • In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms
    • Poncet D., Lindenbaum P., Haridon R.L., Cohen J. In vivo and in vitro phosphorylation of rotavirus NSP5 correlates with its localization in viroplasms. J. Virol. 71:1997;34-41.
    • (1997) J. Virol. , vol.71 , pp. 34-41
    • Poncet, D.1    Lindenbaum, P.2    Haridon, R.L.3    Cohen, J.4
  • 59
    • 0028984351 scopus 로고
    • Interference with bacteriophage phi6 genomic RNA packaging by hairpin structures
    • Qiao X., Qiao J., Mindich L. Interference with bacteriophage phi6 genomic RNA packaging by hairpin structures. J. Virol. 69:1995;5502-5505.
    • (1995) J. Virol. , vol.69 , pp. 5502-5505
    • Qiao, X.1    Qiao, J.2    Mindich, L.3
  • 60
    • 0020066537 scopus 로고
    • Isolation and genetic characterization of temperature-sensitive mutants of simian rotavirus SA11
    • Ramig R.F. Isolation and genetic characterization of temperature- sensitive mutants of simian rotavirus SA11. Virology. 120:1982;93-105.
    • (1982) Virology , vol.120 , pp. 93-105
    • Ramig, R.F.1
  • 61
    • 0021367347 scopus 로고
    • Characterization of temperature-sensitive mutants of simian rotavirus SA11: Protein synthesis and morphogenesis
    • Ramig R.F., Petrie B.L. Characterization of temperature-sensitive mutants of simian rotavirus SA11: protein synthesis and morphogenesis. J. Virol. 49:1984;665-673.
    • (1984) J. Virol. , vol.49 , pp. 665-673
    • Ramig, R.F.1    Petrie, B.L.2
  • 62
    • 0008512898 scopus 로고    scopus 로고
    • Orbiviruses
    • Knipe, D., Howley, M. et al. (Eds.), Lippincott Williams & Wilkins, Philadelphia, PA
    • Roy, P., 2001. Orbiviruses, In: Knipe, D., Howley, M. et al. (Eds.), Fields Virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA, pp. 1835-1870.
    • (2001) Fields Virology, 4th Ed. , pp. 1835-1870
    • Roy, P.1
  • 63
    • 0035971072 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes
    • Schuck P., Taraporewala Z., McPhie P., Patton J.T. Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes. J. Biol. Chem. 276:2001;9679-9687.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9679-9687
    • Schuck, P.1    Taraporewala, Z.2    McPhie, P.3    Patton, J.T.4
  • 64
    • 0035034563 scopus 로고    scopus 로고
    • Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2
    • Taraporewala Z.F., Patton J.T. Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2. J. Virol. 75:2001;4519-4527.
    • (2001) J. Virol. , vol.75 , pp. 4519-4527
    • Taraporewala, Z.F.1    Patton, J.T.2
  • 65
    • 0035866324 scopus 로고    scopus 로고
    • Multimers of the bluetongue virus nonstructural protein, NS2, possess nucleotidyl phosphatase activity: Similarities between NS2 and rotavirus NSP2*
    • Taraporewala Z.F., Chen D., Patton J.T. Multimers of the bluetongue virus nonstructural protein, NS2, possess nucleotidyl phosphatase activity: similarities between NS2 and rotavirus NSP2*. Virology. 280:2001;221-231.
    • (2001) Virology , vol.280 , pp. 221-231
    • Taraporewala, Z.F.1    Chen, D.2    Patton, J.T.3
  • 66
    • 0032759060 scopus 로고    scopus 로고
    • Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity
    • Taraporewala Z.F., Chen D., Patton J.T. Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity. J. Virol. 73:1999;9934-9943.
    • (1999) J. Virol. , vol.73 , pp. 9934-9943
    • Taraporewala, Z.F.1    Chen, D.2    Patton, J.T.3
  • 67
    • 0036634873 scopus 로고    scopus 로고
    • Analysis of a rotavirus temperature-sensitive mutant indicates that NSP2 octamers are the functional form of the protein
    • Taraporewala Z.F., Schuck P., Ramig R.F., Patton J.T. Analysis of a rotavirus temperature-sensitive mutant indicates that NSP2 octamers are the functional form of the protein. J. Virol. 76:2002;7082-7093.
    • (2002) J. Virol. , vol.76 , pp. 7082-7093
    • Taraporewala, Z.F.1    Schuck, P.2    Ramig, R.F.3    Patton, J.T.4
  • 68
    • 0031550798 scopus 로고    scopus 로고
    • Stable protein-RNA interaction involves the terminal domains of bluetongue virus mRNA* but not the terminally conserved sequences
    • Theron J., Nel L.H. Stable protein-RNA interaction involves the terminal domains of bluetongue virus mRNA* but not the terminally conserved sequences. Virology. 229:1997;134-142.
    • (1997) Virology , vol.229 , pp. 134-142
    • Theron, J.1    Nel, L.H.2
  • 69
    • 0028641318 scopus 로고
    • Comparison of the expression and phosphorylation of the nonstructural protein NS2 of three orbiviruses: Evidence for the involvement of an ubiquitous cellular kinase
    • Theron J., Uitenweerde J.M., Huismans H., Nel L.H. Comparison of the expression and phosphorylation of the nonstructural protein NS2 of three orbiviruses: evidence for the involvement of an ubiquitous cellular kinase. J. Gen. Virol. 75:1994;3401-3411.
    • (1994) J. Gen. Virol. , vol.75 , pp. 3401-3411
    • Theron, J.1    Uitenweerde, J.M.2    Huismans, H.3    Nel, L.H.4
  • 70
    • 0025144003 scopus 로고
    • Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: It binds the single-stranded RNA species
    • Thomas C.P., Booth T.F., Roy P. Synthesis of bluetongue virus-encoded phosphoprotein and formation of inclusion bodies by recombinant baculovirus in insect cells: it binds the single-stranded RNA species. J. Gen. Virol. 71:1990;2073-2083.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2073-2083
    • Thomas, C.P.1    Booth, T.F.2    Roy, P.3
  • 71
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 72
    • 17344390304 scopus 로고    scopus 로고
    • The C-terminal domain of rotavirus NSP5 is essential for its multimerization, hyperphosphorylation and interaction with NSP6
    • Torres-Vega M.A., González R.A., Duarte M., Poncet D., López S., Arias C.F. The C-terminal domain of rotavirus NSP5 is essential for its multimerization, hyperphosphorylation and interaction with NSP6. J. Gen. Virol. 81:2000;821-830.
    • (2000) J. Gen. Virol. , vol.81 , pp. 821-830
    • Torres-Vega, M.A.1    González, R.A.2    Duarte, M.3    Poncet, D.4    López, S.5    Arias, C.F.6
  • 75
    • 0036237304 scopus 로고    scopus 로고
    • RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA
    • Vende P., Taraporewala Z., Poncet D., Patton J.T. RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA. J. Virol. 10:2002;5291-5299.
    • (2002) J. Virol. , vol.10 , pp. 5291-5299
    • Vende, P.1    Taraporewala, Z.2    Poncet, D.3    Patton, J.T.4
  • 76
    • 0024381234 scopus 로고
    • Rotavirus SA11 genome segment 11 protein is a nonstructural phosphoprotein
    • Welch S.K., Crawford S.E., Estes M.K. Rotavirus SA11 genome segment 11 protein is a nonstructural phosphoprotein. J. Virol. 63:1989;3974-3982.
    • (1989) J. Virol. , vol.63 , pp. 3974-3982
    • Welch, S.K.1    Crawford, S.E.2    Estes, M.K.3
  • 77
    • 0029017156 scopus 로고
    • The multimeric nonstructural NS2 proteins of bluetongue virus, African horsesickness virus and epizootic hemorrhagic disease virus differ in their single-stranded RNA-binding ability
    • Uitenweerde J.M., Theron J., Stoltz M.A., Huismans H. The multimeric nonstructural NS2 proteins of bluetongue virus, African horsesickness virus and epizootic hemorrhagic disease virus differ in their single-stranded RNA-binding ability. Virology. 209:1995;624-632.
    • (1995) Virology , vol.209 , pp. 624-632
    • Uitenweerde, J.M.1    Theron, J.2    Stoltz, M.A.3    Huismans, H.4
  • 78
    • 0029998886 scopus 로고    scopus 로고
    • Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants
    • Zeng C.Q., Wentz M.J., Cohen J., Estes M.K., Ramig R.F. Characterization and replicase activity of double-layered and single-layered rotavirus-like particles expressed from baculovirus recombinants. J. Virol. 70:1996;2736-2742.
    • (1996) J. Virol. , vol.70 , pp. 2736-2742
    • Zeng, C.Q.1    Wentz, M.J.2    Cohen, J.3    Estes, M.K.4    Ramig, R.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.