Crossref journal-article
Springer Science and Business Media LLC
Nature Structural & Molecular Biology (297)
Authors 5
  1. Xing Zhang (first)
  2. Stephen B Walker (additional)
  3. Paul R Chipman (additional)
  4. Max L Nibert (additional)
  5. Timothy S Baker (additional)
References 58 Referenced 148
  1. Nibert, M.L., Schiff, L.A. & Fields, B.N. Reoviruses and their replication. in Fields Virology (eds. Fields, B.N., Knipe, D.M. & Howley, P.M.) 1679–1728 (Raven, Philadelphia, 2001). / Fields Virology by ML Nibert (2001)
  2. Dryden, K.A. et al. 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, 1023–1041 (1993). (10.1083/jcb.122.5.1023) / J. Cell Biol. by KA Dryden (1993)
  3. Liemann, S., Chandran, K., Baker, T.S., Nibert, M.L. & Harrison, S.C. Structure of the reovirus membrane-penetration protein, μ1, in a complex with its protector protein, σ3. Cell 108, 283–295 (2002). (10.1016/S0092-8674(02)00612-8) / Cell by S Liemann (2002)
  4. Furlong, D.B., Nibert, M.L. & Fields, B.N. Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles. J. Virol. 62, 246–256 (1988). (10.1128/JVI.62.1.246-256.1988) / J. Virol. by DB Furlong (1988)
  5. Strong, J.E., Leone, G., Duncan, R., Sharma, R.K. & Lee, P.W.K. Biochemical and biophysical characterization of the reovirus cell attachment protein σ1: evidence that it is a homotrimer. Virology 184, 23–32 (1991). (10.1016/0042-6822(91)90818-V) / Virology by JE Strong (1991)
  6. Larson, S.M., Antczak, J.B. & Joklik, W.K. Reovirus exists in the form of 13 particle species that differ in their content of protein σ1. Virology 201, 303–311 (1994). (10.1006/viro.1994.1295) / Virology by SM Larson (1994)
  7. Chappell, J.D., Porta, A.E., Dermody, T.S. & Stehle, T. Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 21, 1–11 (2002). (10.1093/emboj/21.1.1) / EMBO J. by JD Chappell (2002)
  8. Sturzenbecker, L.J., Nibert, M., Furlong, D. & Fields, B.N. Intracellular digestion of reovirus particles requires a low pH and is an essential step in the viral infectious cycle. J. Virol. 61, 2351–2361 (1987). (10.1128/JVI.61.8.2351-2361.1987) / J. Virol. by LJ Sturzenbecker (1987)
  9. Chandran, K., Farsetta, D.L. & Nibert, M.L. Strategy for nonenveloped virus entry: a hydrophobic conformer of reovirus penetration protein μ1 mediates membrane disruption. J. Virol. 76, 9920–9933 (2002). (10.1128/JVI.76.19.9920-9933.2002) / J. Virol. by K Chandran (2002)
  10. Chandran, K., Parker, J.S.L., Ehrlich, M., Kirchhausen, Y. & Nibert, M.L. The δ region of outer-capsid protein μ1 undergoes conformational change and release from reovirus particles during cell entry. J. Virol. (in the press). (10.1128/JVI.77.24.13361-13375.2003)
  11. Reinisch, K.M., Nibert, M.L. & Harrison, S.C. Structure of the reovirus core at 3.6 Å resolution. Nature 404, 960–967 (2000). (10.1038/35010041) / Nature by KM Reinisch (2000)
  12. Samuel, C.E. Reoviruses and the interferon system. Curr. Top. Microbiol. Immunol. 233, 125–145 (1998). / Curr. Top. Microbiol. Immunol. by CE Samuel (1998)
  13. Cullen, B.R. RNA interference: antiviral defense and genetic tool. Nat. Immunol. 3, 597–599 (2002). (10.1038/ni0702-597) / Nat. Immunol. by BR Cullen (2002)
  14. Coombs, K.M. Stoichiometry of reovirus structural proteins in virus, ISVP, and core particles. Virology 243, 218–228 (1998). (10.1006/viro.1998.9061) / Virology by KM Coombs (1998)
  15. Dryden, K.A. et al. Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245, 33–46 (1998). (10.1006/viro.1998.9146) / Virology by KA Dryden (1998)
  16. Drayna, D. & Fields, B.N. Activation and characterization of the reovirus transcriptase: genetic analysis. J. Virol. 41, 110–118 (1982). (10.1128/JVI.41.1.110-118.1982) / J. Virol. by D Drayna (1982)
  17. Starnes, M.C. & Joklik, W.K. Reovirus protein λ3 is a poly(C)-dependent poly(G) polymerase. Virology 193, 356–366 (1993). (10.1006/viro.1993.1132) / Virology by MC Starnes (1993)
  18. Tao, Y., Farsetta, D.L., Nibert, M.L. & Harrison, S.C. RNA synthesis in a cage—structural studies of reovirus polymerase λ3. Cell 111, 733–745 (2002). (10.1016/S0092-8674(02)01110-8) / Cell by Y Tao (2002)
  19. Yin, P., Cheang, M. & 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, 1223–1227 (1996). (10.1128/JVI.70.2.1223-1227.1996) / J. Virol. by P Yin (1996)
  20. Noble, S. & Nibert, M.L. Core protein μ2 is a second determinant of nucleoside triphosphatase activities by reovirus cores. J. Virol. 71, 7728–7735 (1997). (10.1128/JVI.71.10.7728-7735.1997) / J. Virol. by S Noble (1997)
  21. Noble, S. & Nibert, M.L. Characterization of an ATPase activity in reovirus cores and its genetic association with core-shell protein λ1. J. Virol. 71, 2182–2191 (1997). (10.1128/JVI.71.3.2182-2191.1997) / J. Virol. by S Noble (1997)
  22. Bisaillon, M., Bergeron, J. & Lemay, G. Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus λ1 protein. J. Biol. Chem. 272, 18298–18303 (1997). (10.1074/jbc.272.29.18298) / J. Biol. Chem. by M Bisaillon (1997)
  23. Bisaillon, M. & Lemay, G. Characterization of the reovirus λ1 protein RNA 5′-triphosphatase activity. J. Biol. Chem. 272, 29954–29957 (1997). (10.1074/jbc.272.47.29954) / J. Biol. Chem. by M Bisaillon (1997)
  24. Furuichi, Y., Muthukrishnan, S., Tomasz, J. & Shatkin, A.J. Caps in eukaryotic mRNAs: mechanism of formation of reovirus mRNA 5′-terminal m7GpppGm-C. Prog. Nucleic Acid Res. Mol. Biol. 19, 3–20 (1976). (10.1016/S0079-6603(08)60905-8) / Prog. Nucleic Acid Res. Mol. Biol. by Y Furuichi (1976)
  25. Cleveland, D.R., Zarbl, H. & Millward, S. Reovirus guanylyltransferase is L2 gene product λ2. J. Virol. 60, 307–311 (1986). (10.1128/JVI.60.1.307-311.1986) / J. Virol. by DR Cleveland (1986)
  26. Mao, Z.X. & Joklik, W.K. Isolation and enzymatic characterization of protein λ2, the reovirus guanylyltransferase. Virology 185, 377–386 (1991). (10.1016/0042-6822(91)90785-A) / Virology by ZX Mao (1991)
  27. Fausnaugh, J. & Shatkin, A.J. Active site localization in a viral mRNA capping enzyme. J. Biol. Chem. 265, 7669–7672 (1990). (10.1016/S0021-9258(19)39166-5) / J. Biol. Chem. by J Fausnaugh (1990)
  28. Luongo, C.L., Contreras, C.M., Farsetta, D.L. & Nibert, M.L. Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus λ2 protein. Evidence for activities in mRNA cap methylation. J. Biol. Chem. 273, 23773–23780 (1998). (10.1074/jbc.273.37.23773) / J. Biol. Chem. by CL Luongo (1998)
  29. Luongo, C.L., Reinisch, K.M., Harrison, S.C. & Nibert, M.L. Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein λ2. J. Biol. Chem. 275, 2804–2810 (2000). (10.1074/jbc.275.4.2804) / J. Biol. Chem. by CL Luongo (2000)
  30. Gillies, S., Bullivant, S. & Bellamy, A.R. Viral RNA polymerases: electron microscopy of reovirus reaction cores. Science 174, 694–696 (1971). (10.1126/science.174.4010.694) / Science by S Gillies (1971)
  31. Bartlett, N.M., Gillies, S.C., Bullivant, S. & Bellamy, A.R. Electron microscopy study of reovirus reaction cores. J. Virol. 14, 315–326 (1974). (10.1128/JVI.14.2.315-326.1974) / J. Virol. by NM Bartlett (1974)
  32. Yeager, M., Weiner, S. & Coombs, K.M. Transcriptionally active reovirus core particles visualized by electron cryo-microscopy and image reconstruction. Biophys. J. 70, A116 (1996). / Biophys. J. by M Yeager (1996)
  33. Furuichi, Y. & Shatkin, A.J. Viral and cellular mRNA capping: past and prospects. Adv. Virus Res. 55, 135–184 (2000). (10.1016/S0065-3527(00)55003-9) / Adv. Virus Res. by Y Furuichi (2000)
  34. Shuman, S. Structure, mechanism, and evolution of the mRNA capping apparatus. Prog. Nucleic Acid Res. Mol. Biol. 66, 1–40 (2001). / Prog. Nucleic Acid Res. Mol. Biol. by S Shuman (2001)
  35. Prasad, B.V.V. et al. Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature 382, 471–473 (1996). (10.1038/382471a0) / Nature by BVV Prasad (1996)
  36. Pesavento, J.B., Lawton, J.A., Estes, M.K. & Prasad, B.V.V. The reversible condensation and expansion of the rotavirus genome. Proc. Natl. Acad. Sci. USA 98, 1381–1386 (2001). (10.1073/pnas.98.4.1381) / Proc. Natl. Acad. Sci. USA by JB Pesavento (2001)
  37. Gouet, P. et al. The highly ordered double-stranded RNA genome of bluetongue virus revealed by crystallography. Cell 97, 481–490 (1999). (10.1016/S0092-8674(00)80758-8) / Cell by P Gouet (1999)
  38. Grimes, J.M. et al. The atomic structure of the bluetongue virus core. Nature 395, 470–478 (1998). (10.1038/26694) / Nature by JM Grimes (1998)
  39. Zhang, H. et al. Visualization of protein-RNA interactions in cytoplasmic polyhedrosis virus. J. Virol. 73, 1624–1629 (1999). (10.1128/JVI.73.2.1624-1629.1999) / J. Virol. by H Zhang (1999)
  40. Baker, T.S., Olson, N.H. & Fuller, S.D. Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol. Mol. Biol. Rev. 63, 862–922 (1999). (10.1128/MMBR.63.4.862-922.1999) / Microbiol. Mol. Biol. Rev. by TS Baker (1999)
  41. Rossmann, M.G., Bernal, R. & Pletnev, S.V. Combining electron microscopic with X-ray crystallographic structures. J. Struct. Biol. 136, 190–200 (2001). (10.1006/jsbi.2002.4435) / J. Struct. Biol. by MG Rossmann (2001)
  42. Chacón, P. & Wriggers, W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317, 375–384 (2002). (10.1006/jmbi.2002.5438) / J. Mol. Biol. by P Chacón (2002)
  43. Farsetta, D.L., Chandran, K. & Nibert, M.L. Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms. J. Biol. Chem. 275, 39693–39701 (2000). (10.1074/jbc.M004562200) / J. Biol. Chem. by DL Farsetta (2000)
  44. Joklik, W.K. The reovirus particle. In The Reoviridae (ed. Joklik, W.K.) 9–78 (Plenum, New York, 1983). (10.1007/978-1-4899-0580-2_2) / The Reoviridae by WK Joklik (1983)
  45. Shatkin, A.J. & Kozak, M. Biochemical aspects of reovirus transcription and translation. In The Reoviridae (ed. Joklik, W.K.) 79–106 (Plenum, New York, 1983). (10.1007/978-1-4899-0580-2_3) / The Reoviridae by AJ Shatkin (1983)
  46. Cheetham, G.M. & Steitz, T.A. Insights into transcription: structure and function of single-subunit DNA-dependent RNA polymerases. Curr. Opin. Struct. Biol. 10, 117–123 (2000). (10.1016/S0959-440X(99)00058-5) / Curr. Opin. Struct. Biol. by GM Cheetham (2000)
  47. Spencer, S.M., Sgro, J.-Y., Dryden, K.A., Baker, T.S. & Nibert, M.L. IRIS explorer software for radial-depth cueing reovirus particles and other macromolecular structures determined by cryoelectron microscopy and image reconstruction. J. Struct. Biol. 120, 11–21 (1997). (10.1006/jsbi.1997.3902) / J. Struct. Biol. by SM Spencer (1997)
  48. Luongo, C.L. et al. Loss of activities for mRNA synthesis accompanies loss of λ2 spikes from reovirus cores: an effect of λ2 on λ1 shell structure. Virology 296, 24–38 (2002). (10.1006/viro.2001.1258) / Virology by CL Luongo (2002)
  49. Diprose, J.M. et al. Translocation portals for the substrates and products of a viral transcription complex: the bluetongue virus core. EMBO J. 20, 7229–7239 (2001). (10.1093/emboj/20.24.7229) / EMBO J. by JM Diprose (2001)
  50. Lawton, J.A., Estes, M.K. & Prasad, B.V.V. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 4, 118–121 (1997). (10.1038/nsb0297-118) / Nat. Struct. Biol. by JA Lawton (1997)
  51. Le Blois, H., French, T., Mertens, P.P., Burroughs, J.N. & Roy, P. The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus. Virology 189, 757–761 (1992). (10.1016/0042-6822(92)90600-T) / Virology by H Le Blois (1992)
  52. Baker, T.S. & Cheng, R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116, 120–130 (1996). (10.1006/jsbi.1996.0020) / J. Struct. Biol. by TS Baker (1996)
  53. Bowman, V.D. et al. An antibody to the putative aphid recognition site on cucumber mosaic virus recognizes pentons but not hexons. J. Virol. 76, 12250–12258 (2002). (10.1128/JVI.76.23.12250-12258.2002) / J. Virol. by VD Bowman (2002)
  54. van Heel, M. et al. Single-particle electron cryo-microscopy: towards atomic resolution. Q. Rev. Biophys. 33, 371–424 (2000). (10.1017/S0033583500003644) / Q. Rev. Biophys. by M van Heel (2000)
  55. Esnouf, R.M. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132–134 (1997). (10.1016/S1093-3263(97)00021-1) / J. Mol. Graph. Model. by RM Esnouf (1997)
  56. Merritt, E.A. & Bacon, D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505–524 (1997). (10.1016/S0076-6879(97)77028-9) / Methods Enzymol. by EA Merritt (1997)
  57. Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998). (10.1107/S0907444998003254) / Acta Crystallogr. D by AT Brunger (1998)
  58. Grimes, J.M. et al. An atomic model of the outer layer of the bluetongue virus core derived from X-ray crystallography and electron cryomicroscopy. Structure 5, 885–893 (1997). (10.1016/S0969-2126(97)00243-8) / Structure by JM Grimes (1997)
Dates
Type When
Created 21 years, 9 months ago (Nov. 9, 2003, 2:19 p.m.)
Deposited 2 years, 3 months ago (May 19, 2023, 12:21 a.m.)
Indexed 1 month ago (July 28, 2025, 5:09 p.m.)
Issued 21 years, 9 months ago (Nov. 9, 2003)
Published 21 years, 9 months ago (Nov. 9, 2003)
Published Online 21 years, 9 months ago (Nov. 9, 2003)
Published Print 21 years, 8 months ago (Dec. 1, 2003)
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@article{Zhang_2003, title={Reovirus polymerase λ3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å}, volume={10}, ISSN={1545-9985}, url={http://dx.doi.org/10.1038/nsb1009}, DOI={10.1038/nsb1009}, number={12}, journal={Nature Structural & Molecular Biology}, publisher={Springer Science and Business Media LLC}, author={Zhang, Xing and Walker, Stephen B and Chipman, Paul R and Nibert, Max L and Baker, Timothy S}, year={2003}, month=nov, pages={1011–1018} }