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Volumn 63, Issue 4, 1999, Pages 862-922

Adding the third dimension to virus life cycles: Three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE; BIRNAVIRIDAE; CRYOELECTRON MICROSCOPY; IMAGE ANALYSIS; IMAGE RECONSTRUCTION; LIFE CYCLE; NONHUMAN; ORBIVIRUS; ORTHOREOVIRUS; REOVIRUS; REVIEW; ROTAVIRUS; THREE DIMENSIONAL IMAGING; VIROGENESIS; VIRUS TRANSMISSION;

EID: 0032712359     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/mmbr.63.4.862-922.1999     Document Type: Review
Times cited : (479)

References (366)
  • 2
    • 0025271666 scopus 로고
    • Regulation of icosahedral virion capsid size by the in vitro activity of a cloned gene product
    • Agarwal, M., M. Arthur, R. D. Arbeit, and R. Goldstein. 1990. Regulation of icosahedral virion capsid size by the in vitro activity of a cloned gene product. Proc. Natl. Acad. Sci. USA 87:2428-2432.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2428-2432
    • Agarwal, M.1    Arthur, M.2    Arbeit, R.D.3    Goldstein, R.4
  • 3
    • 0026564434 scopus 로고
    • Magnification mismatches between micrographs: Corrective procedures and implications for structural analysis
    • Aldroubi, U., B. L. Trus, M. Unser, F. P. Booy, and A. C. Steven. 1992. Magnification mismatches between micrographs: corrective procedures and implications for structural analysis. Ultramicroscopy 46:175-188.
    • (1992) Ultramicroscopy , vol.46 , pp. 175-188
    • Aldroubi, U.1    Trus, B.L.2    Unser, M.3    Booy, F.P.4    Steven, A.C.5
  • 4
    • 0014106334 scopus 로고
    • Structure of simian virus 40. II. Symmetry and components of the virus particle
    • Anderer, F. A., H. D. Schlumberger, M. A. Koch, H. Frank, and H. J. Eggers. 1967. Structure of simian virus 40. II. Symmetry and components of the virus particle. Virology 32:511-523.
    • (1967) Virology , vol.32 , pp. 511-523
    • Anderer, F.A.1    Schlumberger, H.D.2    Koch, M.A.3    Frank, H.4    Eggers, H.J.5
  • 5
    • 0026066977 scopus 로고
    • Protein-protein interactions in an alphavirus membrane
    • Anthony, R. P., and D. T. Brown. 1991. Protein-protein interactions in an alphavirus membrane. J. Virol. 65:1187-1194.
    • (1991) J. Virol. , vol.65 , pp. 1187-1194
    • Anthony, R.P.1    Brown, D.T.2
  • 6
    • 0026802051 scopus 로고
    • Disulphide bonds are essential for the stability of the Sindbis virus envelope
    • Anthony, R. P., A. M. Paredes, and D. T. Brown. 1992. Disulphide bonds are essential for the stability of the Sindbis virus envelope. Virology 190:330-336.
    • (1992) Virology , vol.190 , pp. 330-336
    • Anthony, R.P.1    Paredes, A.M.2    Brown, D.T.3
  • 7
    • 0013457150 scopus 로고
    • Preirradiation and minimum beam microscopy of periodic biological specimens
    • Toronto, Canada
    • Baker, T. S. 1978. Preirradiation and minimum beam microscopy of periodic biological specimens, p. 2-3. In Proceedings of the Ninth International Congress on Electron Microscopy, Toronto, Canada, vol. 2.
    • (1978) Proceedings of the Ninth International Congress on Electron Microscopy , vol.2 , pp. 2-3
    • Baker, T.S.1
  • 8
    • 0018173893 scopus 로고
    • Structure of the tubulin dimer in zinc-induced sheets
    • Baker, T. S., and L. A. Amos. 1978. Structure of the tubulin dimer in zinc-induced sheets. J. Mol. Biol. 123:89-106.
    • (1978) J. Mol. Biol. , vol.123 , pp. 89-106
    • Baker, T.S.1    Amos, L.A.2
  • 9
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker, T. S., and R. H. Cheng. 1996. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116:120-130.
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 10
    • 0344386221 scopus 로고
    • Organized packing of RNA inside viruses as revealed by cryo-electron microscopy and x-ray diffraction analysis
    • Boston San Francisco Press, Inc., San Francisco, Calif
    • Baker, T. S., R. H. Cheng, J. E. Johnson, N. H. Olson, G. J. Wang, and T. S. Schmidt. 1992. Organized packing of RNA inside viruses as revealed by cryo-electron microscopy and X-ray diffraction analysis. Proc. Electron Microsc. Soc. Am. (Boston) 50:454-455. San Francisco Press, Inc., San Francisco, Calif.
    • (1992) Proc. Electron Microsc. Soc. Am. , vol.50 , pp. 454-455
    • Baker, T.S.1    Cheng, R.H.2    Johnson, J.E.3    Olson, N.H.4    Wang, G.J.5    Schmidt, T.S.6
  • 11
    • 0345680664 scopus 로고
    • Cryo-electron microscopy and x-ray crystallographic studies of flock house virus, a T=3 icosahedral animal virus (invited)
    • Paris, France
    • Baker, T. S., R. H. Cheng, V. S. Reddy, N. H. Olson, A. J. Fisher, and J. E. Johnson. 1994. Cryo-electron microscopy and X-ray crystallographic studies of flock house virus, a T=3 icosahedral animal virus (invited), p. 525-526. In International Congress on Electron Microscopy 13, Paris, France, vol. 3A.
    • (1994) International Congress on Electron Microscopy 13 , vol.3 A , pp. 525-526
    • Baker, T.S.1    Cheng, R.H.2    Reddy, V.S.3    Olson, N.H.4    Fisher, A.J.5    Johnson, J.E.6
  • 13
    • 0343995343 scopus 로고
    • The structure of SV40 virus by electron microscopy of unstained frozen hydrated suspensions and negatively stained crystalline arrays
    • Baker, T. S., J. Drak, and M. Bina. 1985. The structure of SV40 virus by electron microscopy of unstained frozen hydrated suspensions and negatively stained crystalline arrays. Biophys. J. 47:50a.
    • (1985) Biophys. J. , vol.47
    • Baker, T.S.1    Drak, J.2    Bina, M.3
  • 14
    • 0023704386 scopus 로고
    • Reconstruction of the three-dimensional structure of simian virus 40 and visualization of the chromatin core
    • Baker, T. S., J. Drak, and M. Bina. 1988. Reconstruction of the three-dimensional structure of simian virus 40 and visualization of the chromatin core. Proc. Natl. Acad. Sci. USA 85:422-426.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 422-426
    • Baker, T.S.1    Drak, J.2    Bina, M.3
  • 15
    • 0024533224 scopus 로고
    • The capsid of small papova viruses contains 72 pentameric capsomeres: Direct evidence from cryo-electron microscopy of simian virus 40
    • Baker, T. S., J. Drak, and M. Bina. 1989. The capsid of small papova viruses contains 72 pentameric capsomeres: direct evidence from cryo-electron microscopy of simian virus 40. Biophys. J. 55:243-253.
    • (1989) Biophys. J. , vol.55 , pp. 243-253
    • Baker, T.S.1    Drak, J.2    Bina, M.3
  • 16
    • 0030272365 scopus 로고    scopus 로고
    • Low resolution meets high: Towards a resolution continuum from cells to atoms
    • Baker, T. S., and J. E. Johnson. 1996. Low resolution meets high: towards a resolution continuum from cells to atoms. Curr. Opin. Struct. Biol. 6: 585-594.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 585-594
    • Baker, T.S.1    Johnson, J.E.2
  • 17
    • 0343796086 scopus 로고
    • Three-dimensional reconstructions of 'light' and 'intermediate' capsids of equine herpes virus
    • Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven. 1989. Three-dimensional reconstructions of 'light' and 'intermediate' capsids of equine herpes virus. Electron Microsc. Soc. Am. Proc. 47:822-823.
    • (1989) Electron Microsc. Soc. Am. Proc. , vol.47 , pp. 822-823
    • Baker, T.S.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 18
    • 0025060289 scopus 로고
    • Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy
    • Baker, T. S., W. W. Newcomb, F. P. Booy, J. C. Brown, and A. C. Steven. 1990. Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J. Virol. 64:563-573.
    • (1990) J. Virol. , vol.64 , pp. 563-573
    • Baker, T.S.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 19
    • 0026329210 scopus 로고
    • Structures of bovine and human papilloma viruses: Analysis by cryoelectron microscopy and three-dimensional image reconstruction
    • Baker, T. S., W. W. Newcomb, N. H. Olson, L. M. Cowsert, C. Olson, and J. C. Brown. 1991. Structures of bovine and human papilloma viruses: analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys. J. 60:1445-1456.
    • (1991) Biophys. J. , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 20
    • 0345249064 scopus 로고
    • Electron microscopy of stained and unstained bovine papilloma virus: Comparison with polyoma virus
    • Baker, T. S., N. H. Olson, W. W. Newcomb, J. C. Brown, and C. Olson. 1989. Electron microscopy of stained and unstained bovine papilloma virus: comparison with polyoma virus. Electron Microsc. Soc. Am. Proc. 47:820-821.
    • (1989) Electron Microsc. Soc. Am. Proc. , vol.47 , pp. 820-821
    • Baker, T.S.1    Olson, N.H.2    Newcomb, W.W.3    Brown, J.C.4    Olson, C.5
  • 21
    • 0014051277 scopus 로고
    • A study of the self-assembly process in a small spherical virus: Formation of organized structures from protein subunits in vitro
    • Bancroft, J. B., G. J. Hills, and R. Markham. 1967. A study of the self-assembly process in a small spherical virus: formation of organized structures from protein subunits in vitro. Virology 31:354-379.
    • (1967) Virology , vol.31 , pp. 354-379
    • Bancroft, J.B.1    Hills, G.J.2    Markham, R.3
  • 22
    • 0017139928 scopus 로고
    • Interactions between a satellite bacteriophage and its helper
    • Barrett, K. J., M. L. Marsh, and R. Calandar. 1976. Interactions between a satellite bacteriophage and its helper. J. Mol. Biol. 106:683-707.
    • (1976) J. Mol. Biol. , vol.106 , pp. 683-707
    • Barrett, K.J.1    Marsh, M.L.2    Calandar, R.3
  • 23
    • 0031571121 scopus 로고    scopus 로고
    • Structures of orbivirus VP7: Implications for the role of this protein in the viral life cycle
    • Basak, A. K., J. M. Grimes, P. Gouet, P. Roy, and D. I. Stuart. 1997. Structures of orbivirus VP7: implications for the role of this protein in the viral life cycle. Structure 5:871-883.
    • (1997) Structure , vol.5 , pp. 871-883
    • Basak, A.K.1    Grimes, J.M.2    Gouet, P.3    Roy, P.4    Stuart, D.I.5
  • 24
    • 0021783271 scopus 로고
    • The DNA translocating vertex of dsDNA bacteriophage
    • Bazinet, C., and J. King. 1985. The DNA translocating vertex of dsDNA bacteriophage. Annu. Rev. Microbiol. 39:109-129.
    • (1985) Annu. Rev. Microbiol. , vol.39 , pp. 109-129
    • Bazinet, C.1    King, J.2
  • 25
    • 0032516070 scopus 로고    scopus 로고
    • The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand
    • Bella, J., P. R. Kolatkar, C. W. Marlor, J. M. Greve, and M. G. Rossmann. 1998. The structure of the two amino-terminal domains of human ICAM-1 suggests how it functions as a rhinovirus receptor and as an LFA-1 integrin ligand. Proc. Natl. Acad. Sci. USA 95:4140-4145.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4140-4145
    • Bella, J.1    Kolatkar, P.R.2    Marlor, C.W.3    Greve, J.M.4    Rossmann, M.G.5
  • 26
    • 0027556541 scopus 로고
    • Use of radial density plots to calibrate image magnification for frozen-hydrated specimens
    • Belnap, D. M., W. D. Grochulski, N. H. Olson, and T. S. Baker. 1993 Use of radial density plots to calibrate image magnification for frozen-hydrated specimens. Ultramicroscopy 48:347-358.
    • (1993) Ultramicroscopy , vol.48 , pp. 347-358
    • Belnap, D.M.1    Grochulski, W.D.2    Olson, N.H.3    Baker, T.S.4
  • 27
    • 0032809077 scopus 로고    scopus 로고
    • Low-resolution density maps from atomic models: How stepping "back" can be a step "forward."
    • Belnap, D. M., A. Kumar, J. T. Folk, T. J. Smith, and T. S. Baker. 1999. Low-resolution density maps from atomic models: how stepping "back" can be a step "forward." J. Struct. Biol. 125:166-175.
    • (1999) J. Struct. Biol. , vol.125 , pp. 166-175
    • Belnap, D.M.1    Kumar, A.2    Folk, J.T.3    Smith, T.J.4    Baker, T.S.5
  • 28
    • 0031257718 scopus 로고    scopus 로고
    • A method for establishing the handedness of biological macromolecules
    • Belnap, D. M., N. H. Olson, and T. S. Baker. 1997. A method for establishing the handedness of biological macromolecules. J. Struct. Biol. 120: 44-51.
    • (1997) J. Struct. Biol. , vol.120 , pp. 44-51
    • Belnap, D.M.1    Olson, N.H.2    Baker, T.S.3
  • 30
    • 0344817899 scopus 로고
    • The use of radial density plots to calibrate images of frozen-hydrated specimens
    • San Francisco Press. Inc., San Francisco, Calif.
    • Belnap, D. M., N. H. Olson, W. D. Grochulski, and T. S. Baker. 1992. The use of radial density plots to calibrate images of frozen-hydrated specimens, p. 998-999. In Proceedings of the Electron Microscopy Society of America, vol. 50. San Francisco Press. Inc., San Francisco, Calif.
    • (1992) Proceedings of the Electron Microscopy Society of America , vol.50 , pp. 998-999
    • Belnap, D.M.1    Olson, N.H.2    Grochulski, W.D.3    Baker, T.S.4
  • 31
    • 0028659872 scopus 로고
    • Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets
    • Berriman, J., and N. Unwin. 1994. Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets. Ultramicroscopy 56:241-252.
    • (1994) Ultramicroscopy , vol.56 , pp. 241-252
    • Berriman, J.1    Unwin, N.2
  • 32
    • 0002567358 scopus 로고
    • The P2-like pliages and their parasite P4
    • R. Calender (ed.). Plenum Press, New York, N.Y.
    • Bertani, L. E., and E. Six. 1988. The P2-like pliages and their parasite P4. p. 73-143. In R. Calender (ed.). The bacteriophages, vol. 2. Plenum Press, New York, N.Y.
    • (1988) The Bacteriophages , vol.2 , pp. 73-143
    • Bertani, L.E.1    Six, E.2
  • 33
    • 0012229502 scopus 로고    scopus 로고
    • Identification of spherical virus particles in digitized images of entire electron micrographs
    • Boier-Martin, I. M., D. C. Marinescu, R. E. Lynch, and T. S. Baker. 1997. Identification of spherical virus particles in digitized images of entire electron micrographs. J. Struct. Biol. 120:146-157.
    • (1997) J. Struct. Biol. , vol.120 , pp. 146-157
    • Boier-Martin, I.M.1    Marinescu, D.C.2    Lynch, R.E.3    Baker, T.S.4
  • 35
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • Booy, F. P., W. W. Newcomb, B. L. Trus, J. C. Brown, T. S. Baker, and A. C. Steven. 1991. Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64:1007-1015.
    • (1991) Cell , vol.64 , pp. 1007-1015
    • Booy, F.P.1    Newcomb, W.W.2    Trus, B.L.3    Brown, J.C.4    Baker, T.S.5    Steven, A.C.6
  • 36
    • 0032493679 scopus 로고    scopus 로고
    • Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 Å resolution
    • Booy, F. P., R. B. S. Roden, H. L. Greenstone, J. T. Schiller, and B. L. Trus. 1998. Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 Å resolution. J. Mol. Biol. 281: 95-106.
    • (1998) J. Mol. Biol. , vol.281 , pp. 95-106
    • Booy, F.P.1    Roden, R.B.S.2    Greenstone, H.L.3    Schiller, J.T.4    Trus, B.L.5
  • 37
    • 0030040630 scopus 로고    scopus 로고
    • The capsid architecture of channel catfish virus, an evolutionary distant herpesvirus, is largely conserved in the absence of discernable sequence homology with herpes simplex virus
    • Booy, F. P., B. L. Trus, A. J. Davison, and A. C. Steven. 1996. The capsid architecture of channel catfish virus, an evolutionary distant herpesvirus, is largely conserved in the absence of discernable sequence homology with herpes simplex virus. Virology 215:134-141.
    • (1996) Virology , vol.215 , pp. 134-141
    • Booy, F.P.1    Trus, B.L.2    Davison, A.J.3    Steven, A.C.4
  • 38
    • 0028261190 scopus 로고
    • Finding a needle in a haystack: Detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of the herpes simplex virus)
    • Booy, F. P., B. L. Trus, W. W. Newcomb, J. C. Brown, J. F. Conway, and A. C. Steven. 1994. Finding a needle in a haystack: detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of the herpes simplex virus). Proc. Natl. Acad. Sci. USA 91:5652-5656.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5652-5656
    • Booy, F.P.1    Trus, B.L.2    Newcomb, W.W.3    Brown, J.C.4    Conway, J.F.5    Steven, A.C.6
  • 39
    • 0030584685 scopus 로고    scopus 로고
    • Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus
    • Böttcher, B., and R. A. Crowther. 1996. Difference imaging reveals ordered regions of RNA in turnip yellow mosaic virus. Structure 4:387-394.
    • (1996) Structure , vol.4 , pp. 387-394
    • Böttcher, B.1    Crowther, R.A.2
  • 41
    • 0343147172 scopus 로고    scopus 로고
    • Peptides that block hepatitis B virus assembly: Analysis by cryomicroscopy, mutagenesis and transfection
    • Böttcher, B., N. Tsuji, H. Takahashi, M. R. Dyson, S. Zhao, R. A. Crowther, and K. Murray. 1998. Peptides that block hepatitis B virus assembly: analysis by cryomicroscopy, mutagenesis and transfection. EMBO J. 17:6839-6845.
    • (1998) EMBO J. , vol.17 , pp. 6839-6845
    • Böttcher, B.1    Tsuji, N.2    Takahashi, H.3    Dyson, M.R.4    Zhao, S.5    Crowther, R.A.6    Murray, K.7
  • 42
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron microscopy
    • Böttcher, B., S. A. Wynne, and R. A. Crowther. 1997. Determination of the fold of the core protein of hepatitis B virus by electron microscopy. Nature 386:88-91.
    • (1997) Nature , vol.386 , pp. 88-91
    • Böttcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 43
    • 0345249062 scopus 로고
    • The determination of parameters in crystal structures by means of Fourier series
    • Bragg, W. L. 1929. The determination of parameters in crystal structures by means of Fourier series. Proc. R. Soc. Lond. Ser. A 123:537-559.
    • (1929) Proc. R. Soc. Lond. Ser. A , vol.123 , pp. 537-559
    • Bragg, W.L.1
  • 44
    • 0015076981 scopus 로고
    • The structure of heated poliovirus particles
    • Breindl, M. 1971. The structure of heated poliovirus particles. J. Gen. Virol. 11:147-156.
    • (1971) J. Gen. Virol. , vol.11 , pp. 147-156
    • Breindl, M.1
  • 45
    • 0022658115 scopus 로고
    • Swelling of isometric and of bacilliform plant virus nucleocapsids is required for virus-specific protein synthesis in vitro
    • Brisco, M., R. Hull, and T. M. A. Wilson. 1986. Swelling of isometric and of bacilliform plant virus nucleocapsids is required for virus-specific protein synthesis in vitro. Virology 148:210-217.
    • (1986) Virology , vol.148 , pp. 210-217
    • Brisco, M.1    Hull, R.2    Wilson, T.M.A.3
  • 46
    • 0000244715 scopus 로고
    • Structural changes in alphaviruses accompanying the process of membrane penetration
    • Brown, D. T., and J. Edwards. 1992. Structural changes in alphaviruses accompanying the process of membrane penetration. Semin. Virol. 3:519-527.
    • (1992) Semin. Virol. , vol.3 , pp. 519-527
    • Brown, D.T.1    Edwards, J.2
  • 47
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., J. Kuriyan, and M. Karplus. 1987. Crystallographic R factor refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 48
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double stranded RNA virus φ6
    • Butcher, S., T. Dokland, P. Ojala, D. Bamford, and S. Fuller. 1997. Intermediates in the assembly pathway of the double stranded RNA virus φ6. EMBO J. 16:4477-4487.
    • (1997) EMBO J. , vol.16 , pp. 4477-4487
    • Butcher, S.1    Dokland, T.2    Ojala, P.3    Bamford, D.4    Fuller, S.5
  • 49
    • 0032434645 scopus 로고    scopus 로고
    • Structure of the human cytomegalovirus B capsid by electron cryomicroscopy and image reconstruction
    • Butcher, S. J., J. Aitken, J. Mitchell, B. Gowen, and D. J. Dargan. 1998. Structure of the human cytomegalovirus B capsid by electron cryomicroscopy and image reconstruction. J. Struct. Biol. 124:70-76.
    • (1998) J. Struct. Biol. , vol.124 , pp. 70-76
    • Butcher, S.J.1    Aitken, J.2    Mitchell, J.3    Gowen, B.4    Dargan, D.J.5
  • 50
    • 0029561893 scopus 로고
    • DNA packaging orders the membrane of bacteriophage PRD1
    • Butcher, S. J., D. H. Bamford, and S. D. Fuller. 1995. DNA packaging orders the membrane of bacteriophage PRD1. EMBO J. 14:6078-6086.
    • (1995) EMBO J. , vol.14 , pp. 6078-6086
    • Butcher, S.J.1    Bamford, D.H.2    Fuller, S.D.3
  • 51
    • 0016290968 scopus 로고
    • Localization and amounts of the major structural proteins in bacteriophage lambda
    • Casjens, S., and R. W. Hendrix. 1974. Localization and amounts of the major structural proteins in bacteriophage lambda. J. Mol. Biol. 88:535-545.
    • (1974) J. Mol. Biol. , vol.88 , pp. 535-545
    • Casjens, S.1    Hendrix, R.W.2
  • 52
    • 0025712187 scopus 로고
    • Bacteriorhodopsin - At last!
    • London
    • Caspar, D. L. D. 1990. Bacteriorhodopsin - at last! Nature (London) 345: 666-667.
    • (1990) Nature , vol.345 , pp. 666-667
    • Caspar, D.L.D.1
  • 53
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar, D. L. D., and A. Klug. 1962. Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. Quant. Biol. 27:1-24.
    • (1962) Cold Spring Harbor Symp. Quant. Biol. , vol.27 , pp. 1-24
    • Caspar, D.L.D.1    Klug, A.2
  • 54
    • 0032798976 scopus 로고    scopus 로고
    • A strategy for determining the orientations of refractory particles for reconstruction from cryo-electron micrographs with particular reference to round, smooth-surfaced, icosahedral viruses
    • Castón, J. R., D. M. Belnap, A. C. Steven, and B. L. Trus. 1999. A strategy for determining the orientations of refractory particles for reconstruction from cryo-electron micrographs with particular reference to round, smooth-surfaced, icosahedral viruses. J. Struct. Biol. 125:209-215.
    • (1999) J. Struct. Biol. , vol.125 , pp. 209-215
    • Castón, J.R.1    Belnap, D.M.2    Steven, A.C.3    Trus, B.L.4
  • 55
    • 0030924019 scopus 로고    scopus 로고
    • Structure of L-A virus: A specialized compartment for the transcription and replication of double-stranded RNA
    • Caston, J. R., B. L. Trus, F. P. Booy, R. B. Wickner, J. S. Wall, and A. C. Steven. 1997. Structure of L-A virus: a specialized compartment for the transcription and replication of double-stranded RNA. J. Cell Biol. 138: 975-985.
    • (1997) J. Cell Biol. , vol.138 , pp. 975-985
    • Caston, J.R.1    Trus, B.L.2    Booy, F.P.3    Wickner, R.B.4    Wall, J.S.5    Steven, A.C.6
  • 57
    • 0032899595 scopus 로고    scopus 로고
    • In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins μ1 and σ3
    • Chandran, K., S. B. Walker, Y. Chen, C. M. Contreras, L. A. Schiff, T. S. Baker, and M. L. Nibert. 1999. In vitro recoating of reovirus cores with baculovirus-expressed outer-capsid proteins μ1 and σ3. J. Virol. 73:3941-3950.
    • (1999) J. Virol. , vol.73 , pp. 3941-3950
    • Chandran, K.1    Walker, S.B.2    Chen, Y.3    Contreras, C.M.4    Schiff, L.A.5    Baker, T.S.6    Nibert, M.L.7
  • 58
    • 0031902570 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and x-ray crystallography of virus-Fab complexes
    • Che, Z., N. H. Olson, D. Leippe, W.-M. Lee, A. G. Mosser, R. R. Rueckert, T. S. Baker, and T. J. Smith. 1998. Antibody-mediated neutralization of human rhinovirus 14 explored by means of cryoelectron microscopy and X-ray crystallography of virus-Fab complexes. J. Virol. 72:4610-4622.
    • (1998) J. Virol. , vol.72 , pp. 4610-4622
    • Che, Z.1    Olson, N.H.2    Leippe, D.3    W-M, L.4    Mosser, A.G.5    Rueckert, R.R.6    Baker, T.S.7    Smith, T.J.8
  • 59
    • 0002838985 scopus 로고
    • RNA packaging in bean pod mottle virus
    • M. A. Brinton and F. X. Heinz (ed.), American Society for Microbiology, Washington, D.C.
    • Chen, Z., C. Stauffacher, T. Schmidt, A. Fisher, and J. E. Johnson. 1990. RNA packaging in bean pod mottle virus, p. 218-226. In M. A. Brinton and F. X. Heinz (ed.), New aspects of positive-strand RNA viruses. American Society for Microbiology, Washington, D.C.
    • (1990) New Aspects of Positive-strand RNA Viruses , pp. 218-226
    • Chen, Z.1    Stauffacher, C.2    Schmidt, T.3    Fisher, A.4    Johnson, J.E.5
  • 60
    • 0001384655 scopus 로고
    • Capsid structure and RNA packaging in comoviruses
    • Chen, Z., C. V. Stauffacher, and J. E. Johnson. 1990. Capsid structure and RNA packaging in comoviruses. Semin. Virol. 1:453-466.
    • (1990) Semin. Virol. , vol.1 , pp. 453-466
    • Chen, Z.1    Stauffacher, C.V.2    Johnson, J.E.3
  • 62
    • 0342655563 scopus 로고
    • Correlation of cryo-electron microscopic and x-ray data and compensation of the contrast transfer function
    • Boston
    • Cheng, R. H. 1992. Correlation of cryo-electron microscopic and X-ray data and compensation of the contrast transfer function. Proc. Electron Microsc. Soc. Am. (Boston) 50:996-997.
    • (1992) Proc. Electron Microsc. Soc. Am. , vol.50 , pp. 996-997
    • Cheng, R.H.1
  • 65
    • 0026540521 scopus 로고
    • Cauliflower mosaic virus, a 420 subunit (T=7), multi-layer structure
    • Cheng, R. H., N. H. Olson, and T. S. Baker. 1992. Cauliflower mosaic virus, a 420 subunit (T=7), multi-layer structure. Virology 186:655-668.
    • (1992) Virology , vol.186 , pp. 655-668
    • Cheng, R.H.1    Olson, N.H.2    Baker, T.S.3
  • 66
    • 0028773272 scopus 로고
    • Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and x-ray crystallography
    • Cheng, R. H., V. S. Reddy, N. H. Olson, A. J. Fisher, T. S. Baker, and J. E. Johnson. 1994. Functional implications of quasi-equivalence in a T=3 icosahedral animal virus established by cryo-electron microscopy and X-ray crystallography. Structure 2:271-282.
    • (1994) Structure , vol.2 , pp. 271-282
    • Cheng, R.H.1    Reddy, V.S.2    Olson, N.H.3    Fisher, A.J.4    Baker, T.S.5    Johnson, J.E.6
  • 68
    • 0032520196 scopus 로고    scopus 로고
    • Structural analysis of the spiroplasma virus, SpV4: Implications for evolutionary variation to obtain host diversity among the Microviridae
    • Chipman, P. R., M. Agbandje-McKenna, J. Renaudin, T. S. Baker, and R. McKenna. 1998. Structural analysis of the spiroplasma virus, SpV4: implications for evolutionary variation to obtain host diversity among the Microviridae. Structure 6:135-145.
    • (1998) Structure , vol.6 , pp. 135-145
    • Chipman, P.R.1    Agbandje-McKenna, M.2    Renaudin, J.3    Baker, T.S.4    McKenna, R.5
  • 69
    • 0344817890 scopus 로고    scopus 로고
    • Cryo-electron microscopy of spiroplasma virus SpV4
    • Springer-Verlag, New York, N.Y.
    • Chipman, P. R., R. McKenna, J. Renaudin, and T. S. Baker. 1997. Cryo-electron microscopy of spiroplasma virus SpV4. Proc. Microsc. Microanal. 3:87-88. Springer-Verlag, New York, N.Y.
    • (1997) Proc. Microsc. Microanal. , vol.3 , pp. 87-88
    • Chipman, P.R.1    McKenna, R.2    Renaudin, J.3    Baker, T.S.4
  • 71
    • 0022539461 scopus 로고
    • Electron microscopy of frozen, hydrated biological specimens
    • Chiu, W. 1986. Electron microscopy of frozen, hydrated biological specimens. Annu. Rev. Biophys. Biophys. Chem. 15:237-257.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 237-257
    • Chiu, W.1
  • 72
    • 0030888403 scopus 로고    scopus 로고
    • Pushing back the limits of electron cryomicroscopy
    • Chiu, W., and M. F. Schmid. 1997. Pushing back the limits of electron cryomicroscopy. Nat. Struct. Biol. 4:331-333.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 331-333
    • Chiu, W.1    Schmid, M.F.2
  • 73
    • 0028221575 scopus 로고
    • Structural studies of virus-antibody complexes by electron microscopy and x-ray crystallography
    • Chiu, W., and T. J. Smith. 1994. Structural studies of virus-antibody complexes by electron microscopy and X-ray crystallography. Curr. Opin. Struct. Biol. 4:219-224.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 219-224
    • Chiu, W.1    Smith, T.J.2
  • 74
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine protease and the organization of the virion
    • London
    • Choi, H.-K., L. Tong, W. Minor, P. Dumas, U. Boege, M. G. Rossmann, and G. Wengler. 1991. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine protease and the organization of the virion. Nature (London) 354:37-43.
    • (1991) Nature , vol.354 , pp. 37-43
    • Choi, H.-K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 75
    • 0026667023 scopus 로고
    • Lattice defects in microtubules: Protofilament numbers vary within individual microtubules
    • Chrétien, D., F. Metoz, K. Verde, and E. Karsenti. 1992. Lattice defects in microtubules: protofilament numbers vary within individual microtubules. J. Cell Biol. 117:1031-1040.
    • (1992) J. Cell Biol. , vol.117 , pp. 1031-1040
    • Chrétien, D.1    Metoz, F.2    Verde, K.3    Karsenti, E.4
  • 76
    • 0031570295 scopus 로고    scopus 로고
    • Virus versus antibody
    • Colman, P. M. 1997. Virus versus antibody. Structure 5:591-593.
    • (1997) Structure , vol.5 , pp. 591-593
    • Colman, P.M.1
  • 77
    • 0024496565 scopus 로고
    • Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments
    • Colonno, R. J., P. L. Callahan, D. M. Leippe, R. R. Rueckert, and J. E. Tomassini. 1989. Inhibition of rhinovirus attachment by neutralizing monoclonal antibodies and their Fab fragments. J. Virol. 63:36-42.
    • (1989) J. Virol. , vol.63 , pp. 36-42
    • Colonno, R.J.1    Callahan, P.L.2    Leippe, D.M.3    Rueckert, R.R.4    Tomassini, J.E.5
  • 78
    • 0032568864 scopus 로고    scopus 로고
    • Hepatitis B virus capsid: Localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens
    • Conway, J. F., N. Cheng, A. Zlotnick, S. J. Stahl, P. T. Wingneld, D. M. Belnap, U. Kanngiesser, M. Noah, and A. C. Steven. 1998. Hepatitis B virus capsid: localization of the putative immunodominant loop (residues 78 to 83) on the capsid surface, and implications for the distinction between c and e-antigens. J. Mol. Biol. 279:1111-1121.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1111-1121
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingneld, P.T.5    Belnap, D.M.6    Kanngiesser, U.7    Noah, M.8    Steven, A.C.9
  • 79
    • 0032428377 scopus 로고    scopus 로고
    • Localization of the N terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy
    • Conway, J. F., N. Cheng, A. Zlotnick, S. J. Stahl, P. T. Wingneld, and A. C. Steven. 1998. Localization of the N terminus of hepatitis B virus capsid protein by peptide-based difference mapping from cryoelectron microscopy. Proc. Natl. Acad. Sci. USA 95:14622-14627.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14622-14627
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Stahl, S.J.4    Wingneld, P.T.5    Steven, A.C.6
  • 80
    • 0030937751 scopus 로고    scopus 로고
    • Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy
    • London
    • Conway, J. F., N. Cheng, A. Zlotnick, P. T. Wingneld, S. J. Stahl, and A. C. Steven. 1997. Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy. Nature (London) 386:91-94.
    • (1997) Nature , vol.386 , pp. 91-94
    • Conway, J.F.1    Cheng, N.2    Zlotnick, A.3    Wingneld, P.T.4    Stahl, S.J.5    Steven, A.C.6
  • 82
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: The bacteriophage HK97 system
    • Conway, J. F., R. L. Duda, N. Cheng, R. W. Hendrix, and A. C. Steven. 1995. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J. Mol. Biol. 253:86-99.
    • (1995) J. Mol. Biol. , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Cheng, N.3    Hendrix, R.W.4    Steven, A.C.5
  • 85
    • 0029964659 scopus 로고    scopus 로고
    • Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids
    • Conway, J. F., B. L. Trus, F. P. Booy, W. W. Newcomb, J. C. Brown, and A. C. Steven. 1996. Visualization of three-dimensional density maps reconstructed from cryoelectron micrographs of viral capsids. J. Struct. Biol. 116: 200-208.
    • (1996) J. Struct. Biol. , vol.116 , pp. 200-208
    • Conway, J.F.1    Trus, B.L.2    Booy, F.P.3    Newcomb, W.W.4    Brown, J.C.5    Steven, A.C.6
  • 86
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther, R. A. 1971. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. R. Soc. Lond. Ser. B 261:221-230.
    • (1971) Phil. Trans. R. Soc. Lond. Ser. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 87
    • 0015120186 scopus 로고
    • Three-dimensional reconstruction and the architecture of spherical viruses
    • Crowther, R. A. 1971. Three-dimensional reconstruction and the architecture of spherical viruses. Endeavour 30:124-129.
    • (1971) Endeavour , vol.30 , pp. 124-129
    • Crowther, R.A.1
  • 88
    • 0015441377 scopus 로고
    • Three-dimensional image reconstruction of some small spherical viruses
    • Crowther, R. A., and L. A. Amos. 1972. Three-dimensional image reconstruction of some small spherical viruses. Cold Spring Harbor Symp. Quant. Biol. 36:489-494.
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.36 , pp. 489-494
    • Crowther, R.A.1    Amos, L.A.2
  • 89
    • 0014930077 scopus 로고
    • Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs
    • London
    • Crowther, R. A., L. A. Amos, J. T. Finch, D. J. DeRosier, and A. Klug. 1970. Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs. Nature (London) 226:421-425.
    • (1970) Nature , vol.226 , pp. 421-425
    • Crowther, R.A.1    Amos, L.A.2    Finch, J.T.3    DeRosier, D.J.4    Klug, A.5
  • 91
    • 0014894609 scopus 로고
    • The reconstruction of a three-dimensional structure from projections and its application to electron microscopy
    • Crowther, R. A., D. J. DeRosier, and A. Klug. 1970. The reconstruction of a three-dimensional structure from projections and its application to electron microscopy. Proc. R. Soc. Lond. Ser. A 317:319-340.
    • (1970) Proc. R. Soc. Lond. Ser. A , vol.317 , pp. 319-340
    • Crowther, R.A.1    DeRosier, D.J.2    Klug, A.3
  • 93
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • Crowther, R. A., N. A. Kiselev, B. Böttcher, J. A. Berriman, G. P. Borisova, V. Ose, and P. Pumpens. 1994. Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77:943-950.
    • (1994) Cell , vol.77 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Böttcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 94
    • 0345680645 scopus 로고
    • Three dimensional image reconstruction on an extended field - A fast, stable algorithm
    • London
    • Crowther, R. A., and A. Klug. 1974. Three dimensional image reconstruction on an extended field - a fast, stable algorithm. Nature (London) 251: 490-492.
    • (1974) Nature , vol.251 , pp. 490-492
    • Crowther, R.A.1    Klug, A.2
  • 95
    • 0016419773 scopus 로고
    • Structural analysis of macromolccular assemblies by image reconstruction from electron micrographs
    • Crowther, R. A., and A. Klug. 1975. Structural analysis of macromolccular assemblies by image reconstruction from electron micrographs. Annu. Rev. Biochem. 44:161-182.
    • (1975) Annu. Rev. Biochem. , vol.44 , pp. 161-182
    • Crowther, R.A.1    Klug, A.2
  • 96
    • 0029844847 scopus 로고    scopus 로고
    • The poliovirus 135S particle is infectious
    • Curry, S., M. Chow, and J. Hogle. 1996. The poliovirus 135S particle is infectious. J. Virol. 70:7125-7131.
    • (1996) J. Virol. , vol.70 , pp. 7125-7131
    • Curry, S.1    Chow, M.2    Hogle, J.3
  • 97
    • 0033607480 scopus 로고    scopus 로고
    • A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage φ6
    • de Haas, F., A. O. Paatero, L. Mindich, D. H. Bamford, and S. D. Fuller. 1999. A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage φ6. J. Mol. Biol. 294:357-372.
    • (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
  • 98
    • 0344386211 scopus 로고
    • Structure of a dehydrogenase enzyme complex by electron microscopy and x-ray diffraction
    • DeRosier, D. J. 1973. Structure of a dehydrogenase enzyme complex by electron microscopy and X-ray diffraction. Am. Crystallogr. Assoc. Trans. 9: 1-9.
    • (1973) Am. Crystallogr. Assoc. Trans. , vol.9 , pp. 1-9
    • DeRosier, D.J.1
  • 99
    • 0027225537 scopus 로고
    • Capsid localization of the bacteriophage-P4 Psu protein
    • Dokland, T., M. L. Isaksen, S. D. Fuller, and B. H. Lindqvist. 1993. Capsid localization of the bacteriophage-P4 Psu protein. Virology 194:682-687.
    • (1993) Virology , vol.194 , pp. 682-687
    • Dokland, T.1    Isaksen, M.L.2    Fuller, S.D.3    Lindqvist, B.H.4
  • 100
    • 0027366430 scopus 로고
    • Structural transitions during maturation of bacteriophage lambda capsids
    • Dokland, T., and H. Murialdo. 1993. Structural transitions during maturation of bacteriophage lambda capsids. J. Mol. Biol. 233:682-694.
    • (1993) J. Mol. Biol. , vol.233 , pp. 682-694
    • Dokland, T.1    Murialdo, H.2
  • 101
    • 0026579790 scopus 로고
    • Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system
    • Dokland, T. E., B. H. Lindqvist, and S. D. Fuller. 1992. Image reconstruction from cryo-electron micrographs reveals the morphopoietic mechanism in the P2-P4 bacteriophage system. EMBO J. 11:839-846.
    • (1992) EMBO J. , vol.11 , pp. 839-846
    • Dokland, T.E.1    Lindqvist, B.H.2    Fuller, S.D.3
  • 102
    • 0023839543 scopus 로고
    • Observations of restricted beam-induced specimen motion with small-spot illumination
    • Downing, K. H. 1988. Observations of restricted beam-induced specimen motion with small-spot illumination. Ultramicroscopy 24:387-398.
    • (1988) Ultramicroscopy , vol.24 , pp. 387-398
    • Downing, K.H.1
  • 103
    • 0026031904 scopus 로고
    • Spot-scan imaging in transmission electron microscopy
    • Downing, K. H. 1991. Spot-scan imaging in transmission electron microscopy. Science 251:53-59.
    • (1991) Science , vol.251 , pp. 53-59
    • Downing, K.H.1
  • 104
    • 0345680653 scopus 로고
    • Progress in design and applications of ccd cameras for electron microscopy
    • Downing, K. H. 1995. Progress in design and applications of CCD cameras for electron microscopy. Microsc. Today 95:12.
    • (1995) Microsc. Today , vol.95 , pp. 12
    • Downing, K.H.1
  • 105
    • 0025583463 scopus 로고
    • Cold stage design for high resolution electron microscopy of biological materials
    • Downing, K. H., and W. Chiu. 1990. Cold stage design for high resolution electron microscopy of biological materials. Electron Microsc. Rev. 3:213-226.
    • (1990) Electron Microsc. Rev. , vol.3 , pp. 213-226
    • Downing, K.H.1    Chiu, W.2
  • 106
    • 0344386209 scopus 로고
    • A computer graphic method to enhance the display and interpretation of three-dimensional data
    • Seattle, Wash, San Francisco Press, Inc., San Francisco. Calif.
    • Dryden, K. A. 1990. A computer graphic method to enhance the display and interpretation of three-dimensional data, p. 540-541. In Proceedings of the XIIth International Congress on Electron Microscopy, Seattle, Wash, vol. 1. San Francisco Press, Inc., San Francisco. Calif.
    • (1990) Proceedings of the XIIth International Congress on Electron Microscopy , vol.1 , pp. 540-541
    • Dryden, K.A.1
  • 107
    • 0032565725 scopus 로고    scopus 로고
    • Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus
    • Dryden, K. A., D. L. Farsetta, G. Wang, J. M. Keegan, B. N. Fields, T. S. Baker, and M. L. Nibert. 1998. Internal structures containing transcriptase-related proteins in top component particles of mammalian orthoreovirus. Virology 245:33-46.
    • (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
  • 108
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis ot virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden, K. A., G. Wang, M. Yeager, M. L. Nibert, K. M. Coombs, D. B. Furlong, B. N. Fields, and T. S. Baker. 1993. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis ot virions and subviral particles by cryoelectron microscopy and image reconstruction. J. Cell Biol. 122:1023-1041.
    • (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
  • 112
    • 0020220722 scopus 로고
    • The mounting of macromolecules tor electron microscopy with particular reference to surface phenomena and the treatment of support films by glow discharge
    • Dubochet, J., M. Groom, and S. Müller-Neuteboom. 1982. The mounting of macromolecules tor electron microscopy with particular reference to surface phenomena and the treatment of support films by glow discharge. Adv. Opt. Electron Microsc. 8:107-135.
    • (1982) Adv. Opt. Electron Microsc. , vol.8 , pp. 107-135
    • Dubochet, J.1    Groom, M.2    Müller-Neuteboom, S.3
  • 114
    • 0019836642 scopus 로고
    • Vitrification of pure water for electron microscopy
    • Dubochet, J., and A. W. McDowell. 1981. Vitrification of pure water for electron microscopy. J. Microsc. 124:RP3-RP4.
    • (1981) J. Microsc. , vol.124
    • Dubochet, J.1    McDowell, A.W.2
  • 115
    • 0018232414 scopus 로고
    • Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein
    • Earnshaw, W., and J. King. 1978. Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. J. Mol. Biol. 126:721-747.
    • (1978) J. Mol. Biol. , vol.126 , pp. 721-747
    • Earnshaw, W.1    King, J.2
  • 116
    • 0000186608 scopus 로고
    • Measurement and compensation of defocusing and aberrations by Fourier processing of micrographs
    • Erickson, H. P., and A. Klug. 1971. Measurement and compensation of defocusing and aberrations by Fourier processing of micrographs. Phil. Trans. R. Soc. Lond. Ser. B 261:105-118.
    • (1971) Phil. Trans. R. Soc. Lond. Ser. B , vol.261 , pp. 105-118
    • Erickson, H.P.1    Klug, A.2
  • 117
    • 0000730162 scopus 로고    scopus 로고
    • Rotaviruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven, Philadelphia, Pa
    • Estes, M. K. 1996. Rotaviruses and their replication, p. 1627-1655. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Fields virology. 3rd ed., vol. 2. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology. 3rd Ed. , vol.2 , pp. 1627-1655
    • Estes, M.K.1
  • 118
    • 0032538274 scopus 로고    scopus 로고
    • The first step: Maturation of the Semliki forest virus spike occurs through a dramatic localized conformational change
    • Ferlenghi, I., B. Gowen, F. de Haas, E. J. Mancini, H. Garoff, M. Sjöberg, and S. D. Fuller. 1998. The first step: maturation of the Semliki Forest virus spike occurs through a dramatic localized conformational change. J. Mol. Biol. 283:71-81.
    • (1998) J. Mol. Biol. , vol.283 , pp. 71-81
    • Ferlenghi, I.1    Gowen, B.2    De Haas, F.3    Mancini, E.J.4    Garoff, H.5    Sjöberg, M.6    Fuller, S.D.7
  • 119
    • 0016193324 scopus 로고
    • The surface structure of polyoma
    • Finch, J. T. 1974. The surface structure of polyoma. J. Gen. Virol. 24: 359-364.
    • (1974) J. Gen. Virol. , vol.24 , pp. 359-364
    • Finch, J.T.1
  • 120
    • 0016222110 scopus 로고
    • The structure of Nudaurelia capensis β virus: The first example of a capsid with icosahedral surface symmetry T=4
    • Finch, J. T., R. A. Crowther, D. A. Hendry, and J. K. Struthers. 1974. The structure of Nudaurelia capensis β virus: the first example of a capsid with icosahedral surface symmetry T=4. J. Gen. Virol. 24:191-200.
    • (1974) J. Gen. Virol. , vol.24 , pp. 191-200
    • Finch, J.T.1    Crowther, R.A.2    Hendry, D.A.3    Struthers, J.K.4
  • 121
    • 0013795002 scopus 로고
    • The structure of viruses of the papillomapolyoma type. III. Structure of rabbit papilloma virus
    • Finch, J. T., and A. Klug. 1965. The structure of viruses of the papillomapolyoma type. III. Structure of rabbit papilloma virus. J. Mol. Biol. 13:1-12.
    • (1965) J. Mol. Biol. , vol.13 , pp. 1-12
    • Finch, J.T.1    Klug, A.2
  • 122
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • London
    • Fisher, A. J., and J. E. Johnson. 1993. Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature (London) 361:176-179.
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 123
    • 0032565439 scopus 로고    scopus 로고
    • Comparison of the native CCMV virion with in vitro assembled CCMV virions by cryoelectron microscopy and image reconstruction
    • Fox, J. M., G. Wang, J. A. Speir, N. H. Olson, J. E. Johnson, T. S. Baker, and M. J. Young. 1998. Comparison of the native CCMV virion with in vitro assembled CCMV virions by cryoelectron microscopy and image reconstruction. Virology 244:212-218.
    • (1998) Virology , vol.244 , pp. 212-218
    • Fox, J.M.1    Wang, G.2    Speir, J.A.3    Olson, N.H.4    Johnson, J.E.5    Baker, T.S.6    Young, M.J.7
  • 125
    • 0030990359 scopus 로고    scopus 로고
    • The ribosome at higher resolution - The donut takes shape
    • Frank, J. 1997. The ribosome at higher resolution - the donut takes shape. Curr. Opin. Struct. Biol. 7:266-272.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 266-272
    • Frank, J.1
  • 126
    • 0029975088 scopus 로고    scopus 로고
    • Spider and web: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith. 1996. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 127
    • 84909895726 scopus 로고
    • High-resolution cryo-electron microscopy of biological macromolecules
    • Seattle, Wash., San Francisco Press, Inc., San Francisco, Calif.
    • Fujiyoshi, Y. 1990. High-resolution cryo-electron microscopy of biological macromolecules, p. 126-127. In Proceedings of the XIIth International Congress on Electron Microscopy, Seattle, Wash., vol. 1. San Francisco Press, Inc., San Francisco, Calif.
    • (1990) Proceedings of the XIIth International Congress on Electron Microscopy , vol.1 , pp. 126-127
    • Fujiyoshi, Y.1
  • 130
    • 0023666171 scopus 로고
    • The T=4 envelope of Sindbis virus is organized by complementary interactions with a T=3 icosahedral capsid
    • Fuller, S. D. 1987. The T=4 envelope of Sindbis virus is organized by complementary interactions with a T=3 icosahedral capsid. Cell 48:923-934.
    • (1987) Cell , vol.48 , pp. 923-934
    • Fuller, S.D.1
  • 131
    • 0023317718 scopus 로고
    • Is Sindbis a simple picornavirus with an envelope?
    • Fuller, S. D., and P. Argos. 1987. Is Sindbis a simple picornavirus with an envelope? EMBO J. 6:1099-1105.
    • (1987) EMBO J. , vol.6 , pp. 1099-1105
    • Fuller, S.D.1    Argos, P.2
  • 132
    • 0029052283 scopus 로고
    • Low pH induces the swivelling of the glycoprotein heterodimers in the Semliki forest virus spike complex
    • Fuller, S. D., J. A. Berriman, S. J. Butcher, and B. E. Gowen. 1995. Low pH induces the swivelling of the glycoprotein heterodimers in the Semliki Forest virus spike complex. Cell 81:715-725.
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3    Gowen, B.E.4
  • 133
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles: The uncommon line
    • Fuller, S. D., S. J. Butcher, R. H. Cheng, and T. S. Baker. 1996. Three-dimensional reconstruction of icosahedral particles: the uncommon line. J. Struct. Biol. 116:48-55.
    • (1996) J. Struct. Biol. , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 134
    • 0031260436 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals ordered domains within the immature HIV-1 particle
    • Fuller, S. D., T. Wilk, B. E. Gowen, H.-G. Krausslich, and V. E. Vogt. 1997. Cryo-electron microscopy reveals ordered domains within the immature HIV-1 particle. Curr. Biol. 7:729-738.
    • (1997) Curr. Biol. , vol.7 , pp. 729-738
    • Fuller, S.D.1    Wilk, T.2    Gowen, B.E.3    Krausslich, H.-G.4    Vogt, V.E.5
  • 135
    • 0024819017 scopus 로고
    • Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography
    • Furcinitti, P. S., J. van Oostrum, and R. M. Burnett. 1991. Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography. EMBO J. 12:3563-3570.
    • (1991) EMBO J. , vol.12 , pp. 3563-3570
    • Furcinitti, P.S.1    Van Oostrum, J.2    Burnett, R.M.3
  • 136
    • 0023945392 scopus 로고
    • Sigma 1 protein of mammalian reoviruses extends from the surface of viral particles
    • Furlong, D. B., M. L. Nibert, and B. N. Fields. 1988. Sigma 1 protein of mammalian reoviruses extends from the surface of viral particles. J. Virol. 62:246-256.
    • (1988) J. Virol. , vol.62 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 137
    • 0024075239 scopus 로고
    • Assembly-dependent maturation cleavage in provirions of a small icosahedral insect ribovirus
    • Gallagher, T. M., and R. R. Rueckert. 1988. Assembly-dependent maturation cleavage in provirions of a small icosahedral insect ribovirus. J. Virol. 62:3399-3406.
    • (1988) J. Virol. , vol.62 , pp. 3399-3406
    • Gallagher, T.M.1    Rueckert, R.R.2
  • 138
    • 0018270186 scopus 로고
    • Transcriptional control of capsid size in the P2:P4 bacteriophage system
    • Geisselsoder, J., M. Chidambaram, and R. Goldstein. 1978. Transcriptional control of capsid size in the P2:P4 bacteriophage system. J. Mol. Biol. 126: 447-456.
    • (1978) J. Mol. Biol. , vol.126 , pp. 447-456
    • Geisselsoder, J.1    Chidambaram, M.2    Goldstein, R.3
  • 139
    • 0023675432 scopus 로고
    • Production of a polyhedral particle in Escherichia coli from a cDNA copy of the large genome segment of φ6
    • Gottlieb, P., J. Strassman, D. Bamford, and L. Mindich. 1988. Production of a polyhedral particle in Escherichia coli from a cDNA copy of the large genome segment of φ6. J. Virol. 62:181-187.
    • (1988) J. Virol. , vol.62 , pp. 181-187
    • Gottlieb, P.1    Strassman, J.2    Bamford, D.3    Mindich, L.4
  • 140
    • 0025030197 scopus 로고
    • In vitro replication, packaging, and transcription of the segmented double-stranded RNA genome of bacteriophage φ6: Studies with procapsids assembled from plasmid-encoded proteins
    • Gottlieb, P., J. Strassman, X. Y. Qiao, A. Frucht, and L. Mindich. 1990. In vitro replication, packaging, and transcription of the segmented double-stranded RNA genome of bacteriophage φ6: studies with procapsids assembled from plasmid-encoded proteins. J. Bacteriol. 172:5774-5782.
    • (1990) J. Bacteriol. , vol.172 , pp. 5774-5782
    • Gottlieb, P.1    Strassman, J.2    Qiao, X.Y.3    Frucht, A.4    Mindich, L.5
  • 143
    • 0028874050 scopus 로고
    • The crystal structure of bluetongue virus VP7
    • London
    • Grimes, J., A. K. Basak, P. Roy, and D. Stuart. 1995. The crystal structure of bluetongue virus VP7. Nature (London) 373:167-170.
    • (1995) Nature , vol.373 , pp. 167-170
    • Grimes, J.1    Basak, A.K.2    Roy, P.3    Stuart, D.4
  • 145
    • 0031571162 scopus 로고    scopus 로고
    • An atomic model of the outer layer of the bluetongue virus core derived from x-ray crystallography and electron cryomicroscopy
    • Grimes, J. M., J. Jakana, M. Ghosh, A. K. Basak, P. Roy, W. Chiu, D. I. Stuart, and B. V. V. Prasad. 1997. 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) Structure , vol.5 , pp. 885-893
    • Grimes, J.M.1    Jakana, J.2    Ghosh, M.3    Basak, A.K.4    Roy, P.5    Chiu, W.6    Stuart, D.I.7    Prasad, B.V.V.8
  • 146
    • 0028300962 scopus 로고
    • Three-dimensional structure of vaccinia virus-produced human papilloma-virus type 1 capsids
    • Hagensee, M. E., N. H. Olson, T. S. Baker, and D. A. Galloway. 1994. Three-dimensional structure of vaccinia virus-produced human papilloma-virus type 1 capsids. J. Virol. 68:4503-4505.
    • (1994) J. Virol. , vol.68 , pp. 4503-4505
    • Hagensee, M.E.1    Olson, N.H.2    Baker, T.S.3    Galloway, D.A.4
  • 148
    • 0021006743 scopus 로고
    • Virus structure: High resolution perspectives
    • Harrison, S. C. 1983. Virus structure: high resolution perspectives. Adv. Virus Res. 28:175-240.
    • (1983) Adv. Virus Res. , vol.28 , pp. 175-240
    • Harrison, S.C.1
  • 149
    • 0001801780 scopus 로고
    • Principles of virus structure
    • B. N. Fields, D. M. Knipe, R. M. Chanock, et al. (ed.), Raven Press, New York, N.Y.
    • Harrison, S. C. 1990. Principles of virus structure, p. 37-61. In B. N. Fields, D. M. Knipe, R. M. Chanock, et al. (ed.), Fields virology, vol. 2. Raven Press, New York, N.Y.
    • (1990) Fields Virology , vol.2 , pp. 37-61
    • Harrison, S.C.1
  • 151
    • 0344386206 scopus 로고
    • A cryo-transfer system for EM400 electron microscopes
    • Hax, W. M. A., and S. Lichtenegger. 1983. A cryo-transfer system for EM400 electron microscopes. Electron Opt. Rep. 30:57-60.
    • (1983) Electron Opt. Rep. , vol.30 , pp. 57-60
    • Hax, W.M.A.1    Lichtenegger, S.2
  • 152
    • 0016287569 scopus 로고
    • Eine tiefkuhlkette zum uberfuhren von wasserhaltigen biologischen objekten ins elektronenmikroskop
    • Heide, H. G., and S. Grund. 1974. Eine tiefkuhlkette zum uberfuhren von wasserhaltigen biologischen Objekten ins elektronenmikroskop. J. Ultrastruct. Res. 48:259-268.
    • (1974) J. Ultrastruct. Res. , vol.48 , pp. 259-268
    • Heide, H.G.1    Grund, S.2
  • 153
    • 0029003107 scopus 로고
    • The potential and limitations of neutrons, electrons, and x-rays for atomic resolution microscopy of unstained biological molecules
    • Henderson, R. 1995. The potential and limitations of neutrons, electrons, and X-rays for atomic resolution microscopy of unstained biological molecules. Q. Rev. Biophys. 28:171-193.
    • (1995) Q. Rev. Biophys. , vol.28 , pp. 171-193
    • Henderson, R.1
  • 154
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213:899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 155
    • 0025978870 scopus 로고
    • A side-entry cold holder for cryo-electron microscopy
    • Henderson, R., C. Raeburn, and G. Vigers. 1991. A side-entry cold holder for cryo-electron microscopy. Ultramicroscopy 35:45-53.
    • (1991) Ultramicroscopy , vol.35 , pp. 45-53
    • Henderson, R.1    Raeburn, C.2    Vigers, G.3
  • 156
    • 0030007379 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound bivalently to human rhinovirus 2
    • Hewat, E. A., and D. Blaas. 1996. Structure of a neutralizing antibody bound bivalently to human rhinovirus 2. EMBO J. 15:1515-1523.
    • (1996) EMBO J. , vol.15 , pp. 1515-1523
    • Hewat, E.A.1    Blaas, D.2
  • 157
    • 0026719673 scopus 로고
    • Three-dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy
    • Hewat, E. A., T. F. Booth, P. T. Loudon, and P. Roy. 1992. Three-dimensional reconstruction of baculovirus expressed bluetongue virus core-like particles by cryo-electron microscopy. Virology 189:10-20.
    • (1992) Virology , vol.189 , pp. 10-20
    • Hewat, E.A.1    Booth, T.F.2    Loudon, P.T.3    Roy, P.4
  • 158
    • 0027008546 scopus 로고
    • Structure of bluetongue virus particles by cryoelectron microscopy
    • Hewat, E. A., T. F. Booth, and P. Roy. 1992. Structure of bluetongue virus particles by cryoelectron microscopy. J. Struct. Biol. 109:61-69.
    • (1992) J. Struct. Biol. , vol.109 , pp. 61-69
    • Hewat, E.A.1    Booth, T.F.2    Roy, P.3
  • 159
    • 0028600626 scopus 로고
    • Structure of correctly self-assembled bluetongue virus-like particles
    • Hewat, E. A., T. F. Booth, and P. Roy. 1994. Structure of correctly self-assembled bluetongue virus-like particles. J. Struct. Biol. 112:183-191.
    • (1994) J. Struct. Biol. , vol.112 , pp. 183-191
    • Hewat, E.A.1    Booth, T.F.2    Roy, P.3
  • 160
    • 0026521446 scopus 로고
    • 3-D reconstruction of bluetongue virus tubules using cryoelectron microscopy
    • Hewat, E. A., T. F. Booth, R. W. Wade, and P. Roy. 1992. 3-D reconstruction of bluetongue virus tubules using cryoelectron microscopy. J. Struct. Biol. 108:35-48.
    • (1992) J. Struct. Biol. , vol.108 , pp. 35-48
    • Hewat, E.A.1    Booth, T.F.2    Wade, R.W.3    Roy, P.4
  • 161
    • 0031967887 scopus 로고    scopus 로고
    • Structure of a neutralizing antibody bound monovalently to human rhinovirus 2
    • Hewat, E. A., T. C. Marlovits, and D. Blaas. 1998. Structure of a neutralizing antibody bound monovalently to human rhinovirus 2. J. Virol. 72: 4396-4402.
    • (1998) J. Virol. , vol.72 , pp. 4396-4402
    • Hewat, E.A.1    Marlovits, T.C.2    Blaas, D.3
  • 162
    • 8244249460 scopus 로고    scopus 로고
    • Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: Positioning of a highly mobile antigenic group
    • Hewat, E. A., N. Verdaguer, I. Fita, W. Blakemore, S. Brookes, A. King, J. Newman, E. Domingo, M. G. Mateu, and D. I. Stuart. 1997. Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic group. EMBO J. 16: 1492-1500.
    • (1997) EMBO J. , vol.16 , pp. 1492-1500
    • Hewat, E.A.1    Verdaguer, N.2    Fita, I.3    Blakemore, W.4    Brookes, S.5    King, A.6    Newman, J.7    Domingo, E.8    Mateu, M.G.9    Stuart, D.I.10
  • 163
    • 0000490047 scopus 로고
    • The viral canyon
    • Hogle, J. M. 1993. The viral canyon. Curr. Biol. 3:278-281.
    • (1993) Curr. Biol. , vol.3 , pp. 278-281
    • Hogle, J.M.1
  • 164
    • 84985225810 scopus 로고
    • Improved anticontaminator for cryo-electron microscopy with a philips EM 400
    • Homo, J.-C., F. Booy, P. Labouesse, J. Lepault, and J. Dubochet. 1984. Improved anticontaminator for cryo-electron microscopy with a Philips EM 400. J. Microsc. 136:337-340.
    • (1984) J. Microsc. , vol.136 , pp. 337-340
    • Homo, J.-C.1    Booy, F.2    Labouesse, P.3    Lepault, J.4    Dubochet, J.5
  • 167
    • 0019304084 scopus 로고
    • Outer capsid protein of bacteriophage lambda
    • Imber, R., A. Tsugita, M. Wurtz, and T. Hohn. 1980. Outer capsid protein of bacteriophage lambda. J. Mol. Biol. 139:277-295.
    • (1980) J. Mol. Biol. , vol.139 , pp. 277-295
    • Imber, R.1    Tsugita, A.2    Wurtz, M.3    Hohn, T.4
  • 168
    • 0026751260 scopus 로고
    • The polarity suppression factor of bacteriophage P4 is also a decoration protein of the P4 capsid
    • Isaksen, M., S. Rishovd, R. Calendar, and B. H. Lindqvist. 1992. The polarity suppression factor of bacteriophage P4 is also a decoration protein of the P4 capsid. Virology 188:831-839.
    • (1992) Virology , vol.188 , pp. 831-839
    • Isaksen, M.1    Rishovd, S.2    Calendar, R.3    Lindqvist, B.H.4
  • 169
    • 0027161709 scopus 로고
    • Characterization of the capsid associating activity of bacteriophage P4's Psu protein
    • Isaksen, M. I., T. Dokland, and B. H. Lindqvist. 1993. Characterization of the capsid associating activity of bacteriophage P4's Psu protein. Virology 194:674-681.
    • (1993) Virology , vol.194 , pp. 674-681
    • Isaksen, M.I.1    Dokland, T.2    Lindqvist, B.H.3
  • 170
    • 0016791695 scopus 로고
    • Structure of tomato bushy stunt virus. II. Comparison of results obtained by electron microscopy and x-ray diffraction
    • Jack, A., S. C. Harrison, and R. A. Crowther. 1975. Structure of tomato bushy stunt virus. II. Comparison of results obtained by electron microscopy and X-ray diffraction. J. Mol. Biol. 97:163-172.
    • (1975) J. Mol. Biol. , vol.97 , pp. 163-172
    • Jack, A.1    Harrison, S.C.2    Crowther, R.A.3
  • 171
    • 0345196599 scopus 로고    scopus 로고
    • Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: An approach for analyzing σ3 functions during virus entry
    • Jané-Valbuena, J., M. L. Nibert, S. M. Spencer, S. B. Walker, T. S. Baker, Y. Chen, V. E. Centonze, and L. A. Schiff. 1999. Reovirus virion-like particles obtained by recoating infectious subvirion particles with baculovirus-expressed σ3 protein: an approach for analyzing σ3 functions during virus entry. J. Virol. 73:2963-2973.
    • (1999) J. Virol. , vol.73 , pp. 2963-2973
    • Jané-Valbuena, J.1    Nibert, M.L.2    Spencer, S.M.3    Walker, S.B.4    Baker, T.S.5    Chen, Y.6    Centonze, V.E.7    Schiff, L.A.8
  • 172
    • 0033608952 scopus 로고    scopus 로고
    • An animal virus-derived peptide switches membrane morphology: Possible relevance to nodaviral transfection process
    • Janshoff, A., D. Bong, C. Steinem, J. Johnson, and M. Ghadiri. 1999. An animal virus-derived peptide switches membrane morphology: possible relevance to nodaviral transfection process. Biochemistry 38:5328-5336.
    • (1999) Biochemistry , vol.38 , pp. 5328-5336
    • Janshoff, A.1    Bong, D.2    Steinem, C.3    Johnson, J.4    Ghadiri, M.5
  • 173
    • 0023077720 scopus 로고
    • High resolution cryo system designed for JEM 100CX electron microscope
    • Jeng, T.-W., and W. Chiu. 1987. High resolution cryo system designed for JEM 100CX electron microscope. Ultramicroscopy 23:61-66.
    • (1987) Ultramicroscopy , vol.23 , pp. 61-66
    • Jeng, T.-W.1    Chiu, W.2
  • 174
    • 0023889015 scopus 로고
    • Containment system for the preparation of vitrified-hydrated virus specimens
    • Jeng, T.-W., Y. Talmon, and W. Chiu. 1988. Containment system for the preparation of vitrified-hydrated virus specimens. J. Electron Microsc. Tech. 8:343-348.
    • (1988) J. Electron Microsc. Tech. , vol.8 , pp. 343-348
    • Jeng, T.-W.1    Talmon, Y.2    Chiu, W.3
  • 175
    • 0030026807 scopus 로고    scopus 로고
    • Functional implications of protein-protein interactions in icosahedral viruses
    • Johnson, J. E. 1996. Functional implications of protein-protein interactions in icosahedral viruses. Proc. Natl. Acad. Sci. USA 93:27-33.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 27-33
    • Johnson, J.E.1
  • 176
    • 0011463689 scopus 로고
    • Principles of virus structure
    • R. G. Webster and A. Granoff (ed.), Academic Press. London. United Kingdom
    • Johnson, J. E., and A. J. Fisher. 1994. Principles of virus structure, p. 1573-1586. In R. G. Webster and A. Granoff (ed.), Encyclopedia of virology. vol. 3. Academic Press. London. United Kingdom.
    • (1994) Encyclopedia of Virology. , vol.3 , pp. 1573-1586
    • Johnson, J.E.1    Fisher, A.J.2
  • 178
    • 0031588020 scopus 로고    scopus 로고
    • Quasi-equivalent viruses: A paradigm for protein assemblies
    • Johnson, J. E., and J. A. Speir. 1997. Quasi-equivalent viruses: a paradigm for protein assemblies. J. Mol. Biol. 269:665-675.
    • (1997) J. Mol. Biol. , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 179
    • 0015398520 scopus 로고
    • Studies on the effect of chymotrypsin on reoviruses
    • Joklik, W. K. 1972. Studies on the effect of chymotrypsin on reoviruses. Virology 49:700-715.
    • (1972) Virology , vol.49 , pp. 700-715
    • Joklik, W.K.1
  • 180
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47:110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 181
    • 0023860024 scopus 로고
    • Infectious rotavirus enters cells by direct cell membrane penetration, not by endocytosis
    • Kaljot, K. T., R. D. Shaw, D. H. Rubin, and H. B. Greenberg. 1988. Infectious rotavirus enters cells by direct cell membrane penetration, not by endocytosis. J. Virol. 62:1136-1144.
    • (1988) J. Virol. , vol.62 , pp. 1136-1144
    • Kaljot, K.T.1    Shaw, R.D.2    Rubin, D.H.3    Greenberg, H.B.4
  • 182
    • 0025329955 scopus 로고
    • Structure and inherent properties of the bacteriophage lambda head shell. VII. Molecular design of the form determining major capsid protein
    • Katsura, I., and H. Kobayashi. 1990. Structure and inherent properties of
    • (1990) J. Mol. Biol. , vol.213 , pp. 503-511
    • Katsura, I.1    Kobayashi, H.2
  • 183
    • 0017882467 scopus 로고
    • Structure and inherent properties of the bacteriophage lambda head shell. I. Polyheads formed by two defective mutants in the major head protein
    • Katsura, I. 1978. Structure and inherent properties of the bacteriophage lambda head shell. I. Polyheads formed by two defective mutants in the major head protein. J. Mol. Biol. 121:71-93.
    • (1978) J. Mol. Biol. , vol.121 , pp. 71-93
    • Katsura, I.1
  • 184
    • 0029645618 scopus 로고
    • Evolutionary conservation in the hepatitis B core structure: Comparison of human and duck cores
    • Kenney, J. M., C.-H. von Bonsdorf, M. Nassal, and S. D. Fuller. 1995. Evolutionary conservation in the hepatitis B core structure: comparison of human and duck cores. Structure 3:1009-1019.
    • (1995) Structure , vol.3 , pp. 1009-1019
    • Kenney, J.M.1    Von Bonsdorf, C.-H.2    Nassal, M.3    Fuller, S.D.4
  • 185
    • 0026664623 scopus 로고
    • Bacteriophage φ-6 envelope elucidated by chemical crosslinking, immunodetection and cryo-electron microscopy
    • Kenney, J. M., J. Hantula, S. D. Fuller, L. Mindich, P. M. Ojala, and D. H. Bamford. 1992. Bacteriophage φ-6 envelope elucidated by chemical crosslinking, immunodetection and cryo-electron microscopy. Virology 190: 635-644.
    • (1992) Virology , vol.190 , pp. 635-644
    • Kenney, J.M.1    Hantula, J.2    Fuller, S.D.3    Mindich, L.4    Ojala, P.M.5    Bamford, D.H.6
  • 186
    • 0028774176 scopus 로고
    • Visualization of fusion activation of the Semliki forest virus spike
    • Kenney, J. M., M. Sjöberg, H. Garoff, and S. D. Fuller. 1994. Visualization of fusion activation of the Semliki Forest virus spike. Structure 2:823-832.
    • (1994) Structure , vol.2 , pp. 823-832
    • Kenney, J.M.1    Sjöberg, M.2    Garoff, H.3    Fuller, S.D.4
  • 187
    • 0029108852 scopus 로고
    • Membrane fusion and the alphavirus life cycle
    • Kielian, M. 1995. Membrane fusion and the alphavirus life cycle. Adv. Virus Res. 45:113-151.
    • (1995) Adv. Virus Res. , vol.45 , pp. 113-151
    • Kielian, M.1
  • 188
    • 0001292454 scopus 로고
    • Structure of viruses of the papillomapolyoma type. I. Human wart virus
    • Klug, A., and J. T. Finch. 1965. Structure of viruses of the papillomapolyoma type. I. Human wart virus. J. Mol. Biol. 11:403-423.
    • (1965) J. Mol. Biol. , vol.11 , pp. 403-423
    • Klug, A.1    Finch, J.T.2
  • 189
    • 0014413307 scopus 로고
    • Structure of viruses of the papillomapolyoma type. IV. Analysis of tilting experiments in the electron microscope
    • Klug, A., and J. T. Finch. 1968. Structure of viruses of the papillomapolyoma type. IV. Analysis of tilting experiments in the electron microscope. J. Mol. Biol. 31:1-12.
    • (1968) J. Mol. Biol. , vol.31 , pp. 1-12
    • Klug, A.1    Finch, J.T.2
  • 190
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • London
    • Kuhlbrandt, W., D. N. Wang, and Y. Fujiyoshi. 1994. Atomic model of plant light-harvesting complex by electron crystallography. Nature (London) 367: 614-621.
    • (1994) Nature , vol.367 , pp. 614-621
    • Kuhlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 192
    • 0026499195 scopus 로고
    • Quantitative energy-filtered electron microscopy of biological molecules in ice
    • Langmore, J. P., and M. F. Smith. 1992. Quantitative energy-filtered electron microscopy of biological molecules in ice. Ultramicroscopy 46:349-373.
    • (1992) Ultramicroscopy , vol.46 , pp. 349-373
    • Langmore, J.P.1    Smith, M.F.2
  • 193
    • 0031031329 scopus 로고    scopus 로고
    • Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles
    • Lawton, J. A., M. K. Estes, and B. V. V. Prasad. 1997. Three-dimensional visualization of mRNA release from actively transcribing rotavirus particles. Nat. Struct. Biol. 4:118-121.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 118-121
    • Lawton, J.A.1    Estes, M.K.2    Prasad, B.V.V.3
  • 194
    • 0029916491 scopus 로고    scopus 로고
    • Automated software package for icosahedral virus reconstruction
    • Lawton, J. A., and B. V. V. Prasad. 1996. Automated software package for icosahedral virus reconstruction. J. Struct. Biol. 116:209-215.
    • (1996) J. Struct. Biol. , vol.116 , pp. 209-215
    • Lawton, J.A.1    Prasad, B.V.V.2
  • 195
    • 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., C. Q.-Y. Zeng, S. K. Mukherjee, J. Cohen, M. K. Estes, and B. V. V. Prasad. 1997. 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. 71:7353-7360.
    • (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
  • 196
    • 0344817872 scopus 로고
    • Projected structure of the surface protein of Sulfolobus spec B12 determined to a resolution of 1.0 nm by cryo-electron microscopy
    • Seattle, Wash., San Francisco Press, Inc., San Francisco, Calif.
    • Lembeke, G., and F. Zemlin. 1990. Projected structure of the surface protein of Sulfolobus spec B12 determined to a resolution of 1.0 nm by cryo-electron microscopy, p. 102-103. In Proceedings of the XIIth International Congress on Electron Microscopy, Seattle, Wash., vol. 1. San Francisco Press, Inc., San Francisco, Calif.
    • (1990) Proceedings of the XIIth International Congress on Electron Microscopy , vol.1 , pp. 102-103
    • Lembeke, G.1    Zemlin, F.2
  • 197
    • 0020691376 scopus 로고
    • Electron microscopy of frozen biological specimens
    • Lepault, J., F. P. Booy, and J. Dubochet. 1983. Electron microscopy of frozen biological specimens. J. Microsc. 129:89-102.
    • (1983) J. Microsc. , vol.129 , pp. 89-102
    • Lepault, J.1    Booy, F.P.2    Dubochet, J.3
  • 198
    • 0022511350 scopus 로고
    • Electron microscopy of frozen hydrated specimens: Preparation and characteristics
    • Lepault, J., and J. Dubochet. 1986. Electron microscopy of frozen hydrated specimens: preparation and characteristics. Methods Enzymol. 127:719-730.
    • (1986) Methods Enzymol. , vol.127 , pp. 719-730
    • Lepault, J.1    Dubochet, J.2
  • 199
    • 0023341103 scopus 로고
    • Organization of double-stranded DNA in bacteriophages: A study by cryo-electron microscopy of vitrified samples
    • Lepault, J., J. Dubochet, W. Baschong, and E. Kellenberger. 1987. Organization of double-stranded DNA in bacteriophages: a study by cryo-electron microscopy of vitrified samples. EMBO J. 6:1507-1512.
    • (1987) EMBO J. , vol.6 , pp. 1507-1512
    • Lepault, J.1    Dubochet, J.2    Baschong, W.3    Kellenberger, E.4
  • 200
  • 202
    • 0023015186 scopus 로고
    • The structure of spherical viruses
    • Liljas, L. 1986. The structure of spherical viruses. Prog. Biophys. Mol. Biol. 48:1-36.
    • (1986) Prog. Biophys. Mol. Biol. , vol.48 , pp. 1-36
    • Liljas, L.1
  • 204
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full-length cDNA clone of Semliki forest virus: The small 6,000 molecules bright membrane protein modulates virus release
    • Liljestrom, P., S. Lusa, D. Huylebroeck, and H. Garoff. 1991. In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000 molecules bright membrane protein modulates virus release. J. Virol. 65:4107-4113.
    • (1991) J. Virol. , vol.65 , pp. 4107-4113
    • Liljestrom, P.1    Lusa, S.2    Huylebroeck, D.3    Garoff, H.4
  • 205
    • 0028260521 scopus 로고
    • Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex
    • Liu, H., T. J. Smith, W.-M. Lee, A. G. Mosser, R. R. Rueckert, N. H. Olson, R. H. Cheng, and T. S. Baker. 1994. Structure determination of an Fab fragment that neutralizes human rhinovirus 14 and analysis of the Fab-virus complex. J. Mol. Biol. 240:127-137.
    • (1994) J. Mol. Biol. , vol.240 , pp. 127-137
    • Liu, H.1    Smith, T.J.2    Lee, W.-M.3    Mosser, A.G.4    Rueckert, R.R.5    Olson, N.H.6    Cheng, R.H.7    Baker, T.S.8
  • 206
    • 0022477384 scopus 로고
    • Conservation in rotaviruses of the protein region containing the two sites associated with trypsin enhancement of infectivity
    • Lopez, S., C. F. Arias, E. Méndez, and R. T. Espejo. 1986. Conservation in rotaviruses of the protein region containing the two sites associated with trypsin enhancement of infectivity. Virology 154:224-227.
    • (1986) Virology , vol.154 , pp. 224-227
    • Lopez, S.1    Arias, C.F.2    Méndez, E.3    Espejo, R.T.4
  • 208
    • 0027180931 scopus 로고
    • Isolation of a phospholipid-free protein shell of hacteriophage PRD1, an Escherichia coli virus with an internal membrane
    • Luo, C., S. Butcher, and D. H. Bamford. 1993. Isolation of a phospholipid-free protein shell of hacteriophage PRD1, an Escherichia coli virus with an internal membrane. Virology 194:564-569.
    • (1993) Virology , vol.194 , pp. 564-569
    • Luo, C.1    Butcher, S.2    Bamford, D.H.3
  • 210
    • 0031570712 scopus 로고    scopus 로고
    • High resolution icosahedral reconstruction: Fulfilling the promise of cryo-electron microscopy
    • Mancini, E. J., F. de Haas, and S. D. Fuller. 1997. High resolution icosahedral reconstruction: fulfilling the promise of cryo-electron microscopy. Structure 5:741-750.
    • (1997) Structure , vol.5 , pp. 741-750
    • Mancini, E.J.1    De Haas, F.2    Fuller, S.D.3
  • 211
    • 0022384496 scopus 로고
    • Unstained microtubules studied by cryo-electron microscopy: Substructure, supertwist and disassembly
    • Mandelkow, E.-M., and E. Mandelkow. 1985. Unstained microtubules studied by cryo-electron microscopy: substructure, supertwist and disassembly. J. Mol. Biol. 181:123-135.
    • (1985) J. Mol. Biol. , vol.181 , pp. 123-135
    • Mandelkow, E.-M.1    Mandelkow, E.2
  • 212
    • 0025868445 scopus 로고
    • Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study
    • Mandelkow, E.-M., E. Mandelkow, and R. A. Milligan. 1991. Microtubule dynamics and microtubule caps: a time-resolved cryo-electron microscopy study. J. Cell Biol. 114:977-991.
    • (1991) J. Cell Biol. , vol.114 , pp. 977-991
    • Mandelkow, E.-M.1    Mandelkow, E.2    Milligan, R.A.3
  • 213
  • 215
    • 0020197316 scopus 로고
    • A double Faraday cup attachment for relative intensity measurements on an electron microscope
    • McMath, T. A., A. E. Curzon, and R. F. Frindt. 1982. A double Faraday cup attachment for relative intensity measurements on an electron microscope. J. Phys. E Sci. Instrum. 15:988-990.
    • (1982) J. Phys. E Sci. Instrum. , vol.15 , pp. 988-990
    • McMath, T.A.1    Curzon, A.E.2    Frindt, R.F.3
  • 216
    • 0015530173 scopus 로고
    • Three-dimensional image reconstruction of turnip yellow mosaic virus
    • Mellema, J. E., and L. A. Amos. 1972. Three-dimensional image reconstruction of turnip yellow mosaic virus. J. Mol. Biol. 72:819-822.
    • (1972) J. Mol. Biol. , vol.72 , pp. 819-822
    • Mellema, J.E.1    Amos, L.A.2
  • 217
    • 0026072563 scopus 로고
    • The three-dimensional structure of reovirus obtained by cryo-electron microscopy
    • Metcalf, P., M. Cyrklaff, and M. Adrian. 1991. The three-dimensional structure of reovirus obtained by cryo-electron microscopy. EMBO J. 10: 3129-3136.
    • (1991) EMBO J. , vol.10 , pp. 3129-3136
    • Metcalf, P.1    Cyrklaff, M.2    Adrian, M.3
  • 218
    • 0021153153 scopus 로고
    • Molecular structure determination of crystalline specimens in frozen aqueous solutions
    • Milligan, R. A., A. Brisson, and P. N. T. Unwin. 1984. Molecular structure determination of crystalline specimens in frozen aqueous solutions. Ultramicroscopy 13:1-10.
    • (1984) Ultramicroscopy , vol.13 , pp. 1-10
    • Milligan, R.A.1    Brisson, A.2    Unwin, P.N.T.3
  • 219
    • 0000364302 scopus 로고
    • Lipid containing bacteriophages
    • R. Calendar (ed.), Plenum Press, New York, N.Y.
    • Mindich, L., and D. H. Bamford. 1988. Lipid containing bacteriophages, p. 475-520. In R. Calendar (ed.), The bacteriophages, vol. 2. Plenum Press, New York, N.Y.
    • (1988) The Bacteriophages , vol.2 , pp. 475-520
    • Mindich, L.1    Bamford, D.H.2
  • 220
    • 0025899211 scopus 로고
    • Bacteriophage lambda DNA maturation and packaging
    • Murialdo, H. 1991. Bacteriophage lambda DNA maturation and packaging. Annu. Rev. Biochem. 60:125-153.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 125-153
    • Murialdo, H.1
  • 221
    • 0016776711 scopus 로고
    • Model for arrangement of minor structural proteins in the head of bacteriophage X
    • London
    • Murialdo, H., and P. N. Ray. 1975. Model for arrangement of minor structural proteins in the head of bacteriophage X. Nature (London) 257: 815-817.
    • (1975) Nature , vol.257 , pp. 815-817
    • Murialdo, H.1    Ray, P.N.2
  • 222
    • 0001923913 scopus 로고    scopus 로고
    • Virus taxonomy
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven, Philadelphia, Pa
    • Murphy, F. A. 1996. Virus taxonomy, p. 15-57. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Fields virology, 3rd ed., vol. 2. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , vol.2 , pp. 15-57
    • Murphy, F.A.1
  • 223
    • 0024332497 scopus 로고
    • Nucleocapsid mass and capsomer protein stoichiometry in equine herpesvirus 1: Scanning transmission electron microscopic study
    • Newcomb, W. W., J. C. Brown, F. P. Booy, and A. C. Steven. 1989. Nucleocapsid mass and capsomer protein stoichiometry in equine herpesvirus 1: scanning transmission electron microscopic study. J. Virol. 63:3777-3783.
    • (1989) J. Virol. , vol.63 , pp. 3777-3783
    • Newcomb, W.W.1    Brown, J.C.2    Booy, F.P.3    Steven, A.C.4
  • 224
    • 0027291013 scopus 로고
    • Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes
    • Newcomb, W. W., B. L. Trus, F. P. Booy, A. C. Steven, J. S. Wall, and J. C. Brown. 1993. Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. J. Mol. Biol. 232:499-511.
    • (1993) J. Mol. Biol. , vol.232 , pp. 499-511
    • Newcomb, W.W.1    Trus, B.L.2    Booy, F.P.3    Steven, A.C.4    Wall, J.S.5    Brown, J.C.6
  • 225
    • 0000432516 scopus 로고    scopus 로고
    • Reoviruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven, Philadelphia, Pa
    • Nibert, M. L., L. A. Schiff, and B. N. Fields. 1996. Reoviruses and their replication, p. 1557-1596. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Fields virology, 3rd ed., vol. 2. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , vol.2 , pp. 1557-1596
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 226
    • 0026088718 scopus 로고
    • Mammalian reoviruses contain a myristoylated structural protein
    • Nibert, M. L., L. A. Schiff, and B. N. Fields. 1991. Mammalian reoviruses contain a myristoylated structural protein. J. Virol. 65:1960-1967.
    • (1991) J. Virol. , vol.65 , pp. 1960-1967
    • Nibert, M.L.1    Schiff, L.A.2    Fields, B.N.3
  • 227
    • 0025606353 scopus 로고
    • In vitro assembly of infectious nucleocapsids of φ6: Formation of a recombinant double stranded RNA virus
    • Olkonnen, V. M., P. Gottlieb, J. Strassman, X. Qiao, D. H. Bamford, and L. Mindich. 1990. In vitro assembly of infectious nucleocapsids of φ6: formation of a recombinant double stranded RNA virus. Proc. Natl. Acad. Sci. USA 87:9173-9177.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 9173-9177
    • Olkonnen, V.M.1    Gottlieb, P.2    Strassman, J.3    Qiao, X.4    Bamford, D.H.5    Mindich, L.6
  • 228
    • 0024475524 scopus 로고
    • Magnification calibration and the determination of spherical virus diameters using cryo-microscopy
    • Olson, N. H., and T. S. Baker. 1989. Magnification calibration and the determination of spherical virus diameters using cryo-microscopy. Ultramicroscopy 30:281-298.
    • (1989) Ultramicroscopy , vol.30 , pp. 281-298
    • Olson, N.H.1    Baker, T.S.2
  • 230
    • 0025569309 scopus 로고
    • The three-dimensional structure of frozen-hydrated Nudaurelia capensis β virus, a T=4 insect virus j
    • Olson, N. H., T. S. Baker, J. E. Johnson, and D. A. Hendry. 1990. The three-dimensional structure of frozen-hydrated Nudaurelia capensis β virus, a T=4 insect virus J. Struct. Biol. 105:111-122.
    • (1990) Struct. Biol. , vol.105 , pp. 111-122
    • Olson, N.H.1    Baker, T.S.2    Johnson, J.E.3    Hendry, D.A.4
  • 231
    • 0026520513 scopus 로고
    • The three-dimensional structure of frozen-hydrated bacteriophage φX174
    • Olson, N. H., T. S. Baker, P. Willingham, and N. L. Incardona. 1992. The three-dimensional structure of frozen-hydrated bacteriophage φX174. J. Struct. Biol. 108:168-175.
    • (1992) J. Struct. Biol. , vol.108 , pp. 168-175
    • Olson, N.H.1    Baker, T.S.2    Willingham, P.3    Incardona, N.L.4
  • 234
    • 85029992573 scopus 로고
    • Cryoelectron microscopy and image reconstruction of spherical viruses with spot scan and FEG technologies
    • Olson, N. H., U. Lücken, S. B. Walker, M. T. Otten, and T. S. Baker. 1995. Cryoelectron microscopy and image reconstruction of spherical viruses with spot scan and FEG technologies. Proc. Microsc. Microanal. 1:1086-1087.
    • (1995) Proc. Microsc. Microanal. , vol.1 , pp. 1086-1087
    • Olson, N.H.1    Lücken, U.2    Walker, S.B.3    Otten, M.T.4    Baker, T.S.5
  • 238
  • 239
    • 0021314590 scopus 로고
    • Structure and assembly of adenoviruses
    • Philipson, L. 1983. Structure and assembly of adenoviruses. Curr. Top. Microbiol. Immunol. 109:1-52.
    • (1983) Curr. Top. Microbiol. Immunol. , vol.109 , pp. 1-52
    • Philipson, L.1
  • 240
    • 0027974229 scopus 로고
    • Direct imaging of interactions between an icosahedral virus conjugate Fab fragments by cryo-electron microscopy and x-ray crystallography
    • Porta, C., G. Wang, R. H. Cheng, Z. Chen, T. S. Baker, and J. E. Johnson. 1994. Direct imaging of interactions between an icosahedral virus conjugate Fab fragments by cryo-electron microscopy and X-ray crystallography. Virology 204:777-788.
    • (1994) Virology , vol.204 , pp. 777-788
    • Porta, C.1    Wang, G.2    Cheng, R.H.3    Chen, Z.4    Baker, T.S.5    Johnson, J.E.6
  • 241
    • 0026583836 scopus 로고
    • Three-dimensional structure of single-shelled bluetongue virus
    • Prasad, B. V., S. Yamaguchi, and S. Roy. 1992. Three-dimensional structure of single-shelled bluetongue virus. J. Virol. 66:2135-2142.
    • (1992) J. Virol. , vol.66 , pp. 2135-2142
    • Prasad, B.V.1    Yamaguchi, S.2    Roy, S.3
  • 242
    • 0025178591 scopus 로고
    • Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy
    • London
    • Prasad, B. V. V., J. W. Burns, E. Marietta, M. K. Estes, and W. Chiu. 1990 Localization of VP4 neutralization sites in rotavirus by three-dimensional cryo-electron microscopy. Nature (London) 343:476-479.
    • (1990) Nature , vol.343 , pp. 476-479
    • Prasad, B.V.V.1    Burns, J.W.2    Marietta, E.3    Estes, M.K.4    Chiu, W.5
  • 243
    • 0345680644 scopus 로고
    • Three-dimensional structure of rotavirus-Fab complex
    • Seattle, Wash., San Francisco Press, Inc., San Francisco, Calif.
    • Prasad, B. V. V., E. Marietta, J. W. Burns, M. K. Estes, and W. Chiu. 1990. Three-dimensional structure of rotavirus-FAB complex, p. 238-239. In Proc. XIIth Int. Cong. Electron Microscopy, Seattle, Wash., vol. 1. San Francisco Press, Inc., San Francisco, Calif.
    • (1990) Proc. XIIth Int. Cong. Electron Microscopy , vol.1 , pp. 238-239
    • Prasad, B.V.V.1    Marietta, E.2    Burns, J.W.3    Estes, M.K.4    Chiu, W.5
  • 244
    • 0028136813 scopus 로고
    • Three-dimensional structure of calicivirus
    • Prasad, B. V. V., D. O. Matson, and A. W. Smith. 1994. Three-dimensional structure of calicivirus. J. Mol. Biol. 240:256-264.
    • (1994) J. Mol. Biol. , vol.240 , pp. 256-264
    • Prasad, B.V.V.1    Matson, D.O.2    Smith, A.W.3
  • 245
    • 0027278758 scopus 로고
    • Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus
    • Prasad, B. V. V., P. E. Prevelige, E. Marietta, R. O. Chen, D. Thomas, J. King, and W. Chiu. 1993. Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus. J. Mol. Biol. 231: 65-74.
    • (1993) J. Mol. Biol. , vol.231 , pp. 65-74
    • Prasad, B.V.V.1    Prevelige, P.E.2    Marietta, E.3    Chen, R.O.4    Thomas, D.5    King, J.6    Chiu, W.7
  • 246
    • 0028321481 scopus 로고
    • Three-dimensional structure of baculovirus-expressed Norwalk virus capsids
    • Prasad, B. V. V., R. Rothnagel, X. Jiang, and M. K. Estes. 1994. Three-dimensional structure of baculovirus-expressed Norwalk virus capsids. J. Virol. 68:5117-5125.
    • (1994) J. Virol. , vol.68 , pp. 5117-5125
    • Prasad, B.V.V.1    Rothnagel, R.2    Jiang, X.3    Estes, M.K.4
  • 247
    • 0029839752 scopus 로고    scopus 로고
    • Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus
    • London
    • Prasad, B. V. V., R. Rothnagel, C. Q.-Y. Zeng, J. Jakana, J. A. Lawton, W. Chiu, and M. K. Estes. 1996. Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature (London) 382: 471-473.
    • (1996) Nature , vol.382 , pp. 471-473
    • Prasad, B.V.V.1    Rothnagel, R.2    Zeng, C.Q.-Y.3    Jakana, J.4    Lawton, J.A.5    Chiu, W.6    Estes, M.K.7
  • 248
    • 0023554031 scopus 로고
    • Cryo-electron microscopy of spherical viruses: An application to rotaviruses
    • Prasad, B. V. V., G. J. Wang, J. P. M. Clerx, and W. Chiu. 1987. Cryo-electron microscopy of spherical viruses: an application to rotaviruses. Micron 18:327-331.
    • (1987) Micron , vol.18 , pp. 327-331
    • Prasad, B.V.V.1    Wang, G.J.2    Clerx, J.P.M.3    Chiu, W.4
  • 250
  • 251
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher, M., T. Wagenknecht, A. Verschoor, and J. Frank. 1987. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 146:113-136.
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 252
    • 0020031457 scopus 로고
    • Polyoma virus capsid structure at 22.5Å resolution
    • London
    • Rayment, I., T. S. Baker, D. L. D. Caspar, and W. T. Murakami. 1982. Polyoma virus capsid structure at 22.5Å resolution. Nature (London) 295: 110-115.
    • (1982) Nature , vol.295 , pp. 110-115
    • Rayment, I.1    Baker, T.S.2    Caspar, D.L.D.3    Murakami, W.T.4
  • 253
    • 0017189552 scopus 로고
    • Characteristics of sindbis virus temperature-sensitive mutants in cultured BHK-21 and Aedes albopictus (mosquito) cells
    • Renz, D., and D. T. Brown. 1976. Characteristics of Sindbis virus temperature-sensitive mutants in cultured BHK-21 and Aedes albopictus (mosquito) cells. J. Virol. 19:775-781.
    • (1976) J. Virol. , vol.19 , pp. 775-781
    • Renz, D.1    Brown, D.T.2
  • 254
    • 0029014434 scopus 로고
    • The structure of the envelope protein of tick-borne encephalitis virus
    • London
    • Rey, F., and S. Harrison. 1995. The structure of the envelope protein of tick-borne encephalitis virus. Nature (London) 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.1    Harrison, S.2
  • 255
    • 0023059423 scopus 로고
    • Three-dimensional structure of the adenovirus major coat protein hexon
    • Roberts, M. M., J. L. White, M. G. Grütter, and R. M. Burnett. 1986. Three-dimensional structure of the adenovirus major coat protein hexon. Science 232:1148-1151.
    • (1986) Science , vol.232 , pp. 1148-1151
    • Roberts, M.M.1    White, J.L.2    Grütter, M.G.3    Burnett, R.M.4
  • 256
    • 0000640156 scopus 로고
    • Structure of the expanded state of tomato bushy stunt virus
    • London
    • Robinson, I. K., and S. C. Harrison. 1982. Structure of the expanded state of tomato bushy stunt virus. Nature (London) 297:563-568.
    • (1982) Nature , vol.297 , pp. 563-568
    • Robinson, I.K.1    Harrison, S.C.2
  • 257
    • 0028032395 scopus 로고
    • Viral cell recognition and entry
    • Rossmann, M. G. 1994. Viral cell recognition and entry. Protein Sci. 3: 1712-1725.
    • (1994) Protein Sci. , vol.3 , pp. 1712-1725
    • Rossmann, M.G.1
  • 262
    • 0002992717 scopus 로고    scopus 로고
    • Orbiviruses and their replication
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Lippincott-Raven, Philadelphia. Pa
    • Roy, P. 1996. Orbiviruses and their replication, p. 1709-1734. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.), Fields virology, 3rd ed., vol. 2. Lippincott-Raven, Philadelphia. Pa.
    • (1996) Fields Virology, 3rd Ed. , vol.2 , pp. 1709-1734
    • Roy, P.1
  • 266
    • 0344817869 scopus 로고    scopus 로고
    • Reconstructions tridimensionnelles de virus icosaédriques par cryomicroscopie èlectronique: Application au virus Broadhaven et à l'adenovirus humain de sérotype 3
    • Université Joseph Fourier-Grenoble I, Grenoble, France
    • Schoehn, G. 1997. Reconstructions tridimensionnelles de virus icosaédriques par cryomicroscopie èlectronique: application au virus Broadhaven et à l'adenovirus humain de sérotype 3. Physique. Université Joseph Fourier-Grenoble I, Grenoble, France.
    • (1997) Physique
    • Schoehn, G.1
  • 267
    • 0030465607 scopus 로고    scopus 로고
    • Adenovirus 3 penton dodecahedron exhibits structural changes of the base on fibre binding
    • Schoehn, G., P. Fender, J. Chroboczek, and E. A. Hewat. 1996. Adenovirus 3 penton dodecahedron exhibits structural changes of the base on fibre binding. EMBO J. 15:6841-6848.
    • (1996) EMBO J. , vol.15 , pp. 6841-6848
    • Schoehn, G.1    Fender, P.2    Chroboczek, J.3    Hewat, E.A.4
  • 268
    • 0030778980 scopus 로고    scopus 로고
    • Structure of Broadhaven virus by cryoelectron microscopy: Correlation of structural and antigenic properties of Broadhaven virus and Bluelongue virus outer capsid proteins
    • Schoehn, G., S. R. Moss, P. A. Nuttall, and E. A. Hewat. 1997. Structure of Broadhaven virus by cryoelectron microscopy: correlation of structural and antigenic properties of Broadhaven virus and Bluelongue virus outer capsid proteins. Virology 235:191-200.
    • (1997) Virology , vol.235 , pp. 191-200
    • Schoehn, G.1    Moss, S.R.2    Nuttall, P.A.3    Hewat, E.A.4
  • 269
    • 0024552611 scopus 로고
    • Three-dimensional structure of the HSV1 nucleocapsid
    • Schrag, J. D., B. V. V. Prasad, F. J. Rixon, and W. Chiu. 1989. Three-dimensional structure of the HSV1 nucleocapsid. Cell 56:651-660.
    • (1989) Cell , vol.56 , pp. 651-660
    • Schrag, J.D.1    Prasad, B.V.V.2    Rixon, F.J.3    Chiu, W.4
  • 270
    • 84911837213 scopus 로고
    • Communication in the presence of noise
    • Shannon, C. E. 1949. Communication in the presence of noise. Proc. Inst. Radio Eng. 37:10-20.
    • (1949) Proc. Inst. Radio Eng. , vol.37 , pp. 10-20
    • Shannon, C.E.1
  • 271
    • 0027220677 scopus 로고
    • Three-dimensional visualization of the rotavirus hemagglutinin structure
    • Shaw, A. L., R. Rothnagel, D. Chen, R. F. Ramig, W. Chiu, and B. V. V. Prasad. 1993. Three-dimensional visualization of the rotavirus hemagglutinin structure. Cell 74:693-701.
    • (1993) Cell , vol.74 , pp. 693-701
    • Shaw, A.L.1    Rothnagel, R.2    Chen, D.3    Ramig, R.F.4    Chiu, W.5    Prasad, B.V.V.6
  • 272
    • 0030586878 scopus 로고    scopus 로고
    • The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization
    • Shaw, A. L., S. K. Samal, K. Subramanian, and B. V. V. Prasad. 1996. The structure of aquareovirus shows how the different geometries of the two layers of the capsid are reconciled to provide symmetrical interactions and stabilization. Structure 4:957-967.
    • (1996) Structure , vol.4 , pp. 957-967
    • Shaw, A.L.1    Samal, S.K.2    Subramanian, K.3    Prasad, B.V.V.4
  • 273
    • 0029930519 scopus 로고    scopus 로고
    • AVS software for visualization in molecular microscopy
    • Sheehan, B., S. D. Fuller, M. E. Pique, and M. Yeager. 1996. AVS software for visualization in molecular microscopy. J. Struct. Biol. 116:99-105.
    • (1996) J. Struct. Biol. , vol.116 , pp. 99-105
    • Sheehan, B.1    Fuller, S.D.2    Pique, M.E.3    Yeager, M.4
  • 274
    • 0022644644 scopus 로고
    • Use of monoclonal antibodies on a common cold picornavirus, human rhinovirus 14
    • Sherry, B., A. G. Mosser, R. J. Colonno, and R. R. Rueckert. 1986. Use of monoclonal antibodies on a common cold picornavirus, human rhinovirus 14. J. Virol. 57:246-257.
    • (1986) J. Virol. , vol.57 , pp. 246-257
    • Sherry, B.1    Mosser, A.G.2    Colonno, R.J.3    Rueckert, R.R.4
  • 276
    • 0019066885 scopus 로고
    • The budding mechanisms of envelope animal viruses
    • Simons, K., and H. Garoff. 1980. The budding mechanisms of envelope animal viruses. J. Gen. Virol. 50:1-21.
    • (1980) J. Gen. Virol. , vol.50 , pp. 1-21
    • Simons, K.1    Garoff, H.2
  • 279
    • 0028822560 scopus 로고
    • Expression of tobacco ringspot virus capsid protein and satellite RNA in insect cells and three-dimensional structure of tobacco ringspot virus-like particles
    • Singh, S., R. Rothnagel, B. V. V. Prasad, and B. Buckley. 1995. Expression of tobacco ringspot virus capsid protein and satellite RNA in insect cells and three-dimensional structure of tobacco ringspot virus-like particles. Virology 213:472-481.
    • (1995) Virology , vol.213 , pp. 472-481
    • Singh, S.1    Rothnagel, R.2    Prasad, B.V.V.3    Buckley, B.4
  • 280
    • 0016697207 scopus 로고
    • The helper dependence of satellite bacteriophage P4: Which gene functions of bacteriophage P2 are needed by P4?
    • Six, E. W. 1975. The helper dependence of satellite bacteriophage P4: which gene functions of bacteriophage P2 are needed by P4? Virology 67:249-263.
    • (1975) Virology , vol.67 , pp. 249-263
    • Six, E.W.1
  • 281
    • 0015579384 scopus 로고
    • Bacteriophage P4: A satellite virus depending on a helper such as prophage P2
    • Six, E. W., and C. A. C. Klug. 1973. Bacteriophage P4: a satellite virus depending on a helper such as prophage P2. Virology 51:327-347.
    • (1973) Virology , vol.51 , pp. 327-347
    • Six, E.W.1    Klug, C.A.C.2
  • 282
    • 0030295008 scopus 로고    scopus 로고
    • Maximum-entropy three-dimensional reconstruction with deconvolution of the contrast transfer function: A test application with adenovirus
    • Skoglund, U., L.-G. Öfverstedt, R. M. Burnett, and G. Bricogne. 1996. Maximum-entropy three-dimensional reconstruction with deconvolution of the contrast transfer function: a test application with adenovirus. J. Struct. Biol. 117:173-188.
    • (1996) J. Struct. Biol. , vol.117 , pp. 173-188
    • Skoglund, U.1    Öfverstedt, L.-G.2    Burnett, R.M.3    Bricogne, G.4
  • 283
    • 0026663109 scopus 로고
    • Quantitation of molecular densities by cryo-electron microscopy: Determination of the radial density distribution of tobacco mosaic virus
    • Smith, M. F., and J. P. Langmore. 1992. Quantitation of molecular densities by cryo-electron microscopy: determination of the radial density distribution of tobacco mosaic virus. J. Mol. Biol. 226:763-774.
    • (1992) J. Mol. Biol. , vol.226 , pp. 763-774
    • Smith, M.F.1    Langmore, J.P.2
  • 284
    • 0032616823 scopus 로고    scopus 로고
    • Picornaviruses: Epitopes, canyons, and pockets
    • Smith, T. J., and T. S. Baker. 1999. Picornaviruses: epitopes, canyons, and pockets. Adv. Virus Res. 52:1-23.
    • (1999) Adv. Virus Res. , vol.52 , pp. 1-23
    • Smith, T.J.1    Baker, T.S.2
  • 285
    • 0029743275 scopus 로고    scopus 로고
    • Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon
    • London
    • Smith, T. J., E. S. Chase, T. J. Schmidt, N. H. Olson, and T. S. Baker. 1996. Neutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon. Nature (London) 383:350-354.
    • (1996) Nature , vol.383 , pp. 350-354
    • Smith, T.J.1    Chase, E.S.2    Schmidt, T.J.3    Olson, N.H.4    Baker, T.S.5
  • 287
    • 0028831519 scopus 로고
    • Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus
    • Smith, T. J., A. G. Mosser, and T. S. Baker. 1995. Structural studies on the mechanisms of antibody-mediated neutralization of human rhinovirus. Semin. Virol. 6:233-242.
    • (1995) Semin. Virol. , vol.6 , pp. 233-242
    • Smith, T.J.1    Mosser, A.G.2    Baker, T.S.3
  • 288
    • 0027306163 scopus 로고
    • Structure of a human rhinovirus-bivalently bound antibody complex: Implications for viral neutralization and antibody flexibility
    • Smith, T. J., N. H. Olson, R. H. Cheng, E. S. Chase, and T. S. Baker. 1993. Structure of a human rhinovirus-bivalently bound antibody complex: implications for viral neutralization and antibody flexibility. Proc. Natl. Acad. Sci. USA 90:7015-7018.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7015-7018
    • Smith, T.J.1    Olson, N.H.2    Cheng, R.H.3    Chase, E.S.4    Baker, T.S.5
  • 290
    • 0029643791 scopus 로고
    • Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by x-ray crystallography and cryo-electron microscopy
    • Speir, J. A., S. Munshi, G. Wang, T. S. Baker, and J. E. Johnson. 1995. Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy. Structure 3:63-78.
    • (1995) Structure , vol.3 , pp. 63-78
    • Speir, J.A.1    Munshi, S.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 291
    • 18544402853 scopus 로고    scopus 로고
    • Structure of the herpes simplex virus capsid: Peptide A862-H880 of the major capsid protein is displayed on the rim of the capsomer protrusions
    • Spencer, J. V., B. L. Trus, F. P. Booy, A. C. Steven, W. W. Newcomb, and J. C. Brown. 1997. Structure of the herpes simplex virus capsid: peptide A862-H880 of the major capsid protein is displayed on the rim of the capsomer protrusions. Virology 228:229-235.
    • (1997) Virology , vol.228 , pp. 229-235
    • Spencer, J.V.1    Trus, B.L.2    Booy, F.P.3    Steven, A.C.4    Newcomb, W.W.5    Brown, J.C.6
  • 292
    • 0031257722 scopus 로고    scopus 로고
    • IRIS explorer software for radial-depth cueing reovirus particles and other macromolecular structures determined by cryoelectron microscopy and image reconstruction
    • Spencer, S. M., J.-Y. Sgro, K. A. Dryden, T. S. Baker, and M. L. Nibert. 1997. 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) J. Struct. Biol. , vol.120 , pp. 11-21
    • Spencer, S.M.1    Sgro, J.-Y.2    Dryden, K.A.3    Baker, T.S.4    Nibert, M.L.5
  • 293
    • 0028303852 scopus 로고
    • Structure of murine polyoma virus complexed with an oligosaccharide receptor fragment
    • London
    • Stehle, T., Y. Yan, T. L. Benjamin, and S. C. Harrison. 1994. Structure of murine polyoma virus complexed with an oligosaccharide receptor fragment. Nature (London) 369:160-163.
    • (1994) Nature , vol.369 , pp. 160-163
    • Stehle, T.1    Yan, Y.2    Benjamin, T.L.3    Harrison, S.C.4
  • 294
    • 0030790280 scopus 로고    scopus 로고
    • The making and breaking of symmetry in virus capsid assembly: Glimpses of capsid biology from cryoelectron microscopy
    • Steven, A. C., B. L. Trus, F. P. Booy, N. Cheng, A. Zlotnick, J. R. Caston, and J. F. Conway. 1997. The making and breaking of symmetry in virus capsid assembly: glimpses of capsid biology from cryoelectron microscopy. FASEB J. 11:733-742.
    • (1997) FASEB J. , vol.11 , pp. 733-742
    • Steven, A.C.1    Trus, B.L.2    Booy, F.P.3    Cheng, N.4    Zlotnick, A.5    Caston, J.R.6    Conway, J.F.7
  • 295
    • 0345249035 scopus 로고
    • Electron microscopy of biological macromolecules: Frozen hydrated methods and computer image processing, 9-39
    • P. J. Duke and A. G. Michette (ed.). Plenum Press, New York, N.Y.
    • Stewart, M. 1990. Electron microscopy of biological macromolecules: frozen hydrated methods and computer image processing, p. 9-39. In P. J. Duke and A. G. Michette (ed.). Modern microscopies: techniques and applications. Plenum Press, New York, N.Y.
    • (1990) Modern Microscopies: Techniques and Applications
    • Stewart, M.1
  • 296
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organization of adenovirus
    • Stewart, P. L., R. M. Burnett, M. Cyrklaff, and S. D. Fuller. 1991. Image reconstruction reveals the complex molecular organization of adenovirus. Cell 67:145-154.
    • (1991) Cell , vol.67 , pp. 145-154
    • Stewart, P.L.1    Burnett, R.M.2    Cyrklaff, M.3    Fuller, S.D.4
  • 297
    • 0031003549 scopus 로고    scopus 로고
    • Cryo-EM visualization of an exposed RGD epitope on adenovirus that escapes antibody neutralization
    • Stewart, P. L., C. Y. Chiu, S. Huang, T. Muir, Y. Zhao, B. Chait. P. Mathias, and G. R. Nemerow. 1997. Cryo-EM visualization of an exposed RGD epitope on adenovirus that escapes antibody neutralization. EMBO J. 16:1189-1198.
    • (1997) EMBO J. , vol.16 , pp. 1189-1198
    • Stewart, P.L.1    Chiu, C.Y.2    Huang, S.3    Muir, T.4    Zhao, Y.5    Chait, B.6    Mathias, P.7    Nemerow, G.R.8
  • 298
    • 0027184774 scopus 로고
    • Difference imaging of adenovirus: Bridging the resolution gap between x-ray crystallography and electron microscopy
    • Stewart, P. L., S. D. Fuller, and R. M. Burnett. 1993. Difference imaging of adenovirus: bridging the resolution gap between X-ray crystallography and electron microscopy. EMBO J. 12:2589-2599.
    • (1993) EMBO J. , vol.12 , pp. 2589-2599
    • Stewart, P.L.1    Fuller, S.D.2    Burnett, R.M.3
  • 299
    • 0345680643 scopus 로고
    • Combining structures from cryo-electron microscopy and x-ray crystallography
    • Stewart, P. L., and G. R. Nemerow. 1995. Combining structures from cryo-electron microscopy and x-ray crystallography. JMSA Proc. Microsc. Microanal. 53:44-45.
    • (1995) JMSA Proc. Microsc. Microanal. , vol.53 , pp. 44-45
    • Stewart, P.L.1    Nemerow, G.R.2
  • 300
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • Tao, Y., N. H. Olson, W. Xu, D. L. Anderson, M. G. Rossmann, and T. S. Baker. 1998. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell 95:431-437.
    • (1998) Cell , vol.95 , pp. 431-437
    • Tao, Y.1    Olson, N.H.2    Xu, W.3    Anderson, D.L.4    Rossmann, M.G.5    Baker, T.S.6
  • 301
    • 0344817868 scopus 로고
    • Electron microscopy of frozen, hydrated biological specimens
    • Taylor, K. A. 1975. Electron microscopy of frozen, hydrated biological specimens. Electron Microsc. Soc. Am. Proc. 33:300-301.
    • (1975) Electron Microsc. Soc. Am. Proc. , vol.33 , pp. 300-301
    • Taylor, K.A.1
  • 302
    • 0345680639 scopus 로고
    • A method for maintaining specimen hydration by sandwiching between thin films
    • Taylor, K. A., and R. M. Glaeser. 1973. A method for maintaining specimen hydration by sandwiching between thin films. Electron Microsc. Soc. Am. Proc. 31:342-343.
    • (1973) Electron Microsc. Soc. Am. Proc. , vol.31 , pp. 342-343
    • Taylor, K.A.1    Glaeser, R.M.2
  • 303
    • 0017140343 scopus 로고
    • Electron microscopy of frozen hydrated biological specimens
    • Taylor, K. A., and R. M. Glaeser. 1976. Electron microscopy of frozen hydrated biological specimens. J. Ultrastruct. Res. 55:448-456.
    • (1976) J. Ultrastruct. Res. , vol.55 , pp. 448-456
    • Taylor, K.A.1    Glaeser, R.M.2
  • 304
    • 0002228874 scopus 로고
    • Phase contrast electron microscopy
    • U. Valdre (ed.), Academic Press, New York, N.Y.
    • Thon, F. 1971. Phase contrast electron microscopy, p. 570-625. In U. Valdre (ed.), Electron microscopy in material science. Academic Press, New York, N.Y.
    • (1971) Electron Microscopy in Material Science , pp. 570-625
    • Thon, F.1
  • 305
    • 0030739033 scopus 로고    scopus 로고
    • Bivalent binding of neutralising antibody to a calicivirus involves the torsional flexibility of the antibody hinge
    • Thouvenin, E., S. Laurent, M.-F. Madelaine, D. Rasschaert, J.-F. Vautherot, and E. A. Hewat. 1997. Bivalent binding of neutralising antibody to a calicivirus involves the torsional flexibility of the antibody hinge. J. Mol. Biol. 270:238-246.
    • (1997) J. Mol. Biol. , vol.270 , pp. 238-246
    • Thouvenin, E.1    Laurent, S.2    Madelaine, M.-F.3    Rasschaert, D.4    Vautherot, J.-F.5    Hewat, E.A.6
  • 306
    • 0029991984 scopus 로고    scopus 로고
    • PTOOL: A software package for the selection of particles from electron cyromicroscopy spot-scan images
    • Thuman-Commike, P. A., and W. Chiu. 1996. PTOOL: a software package for the selection of particles from electron cyromicroscopy spot-scan images. J. Struct. Biol. 116:41-47.
    • (1996) J. Struct. Biol. , vol.116 , pp. 41-47
    • Thuman-Commike, P.A.1    Chiu, W.2
  • 307
    • 0031214838 scopus 로고    scopus 로고
    • Improved common line-based icosahedral particle image orientation estimation algorithms
    • Thuman-Commike, P. A., and W. Chiu. 1997. Improved common line-based icosahedral particle image orientation estimation algorithms. Ultramicroscopy 68:231-255.
    • (1997) Ultramicroscopy , vol.68 , pp. 231-255
    • Thuman-Commike, P.A.1    Chiu, W.2
  • 309
    • 0031982564 scopus 로고    scopus 로고
    • Role of the scaffolding protein in P22 procapsid size determination suggested by T=4 and T=7 procapsid structures
    • Thuman-Commike, P. A., B. Greene, J. A. Malinski, J. King, and W. Chiu. 1998. Role of the scaffolding protein in P22 procapsid size determination suggested by T=4 and T=7 procapsid structures. Biophys. J. 74:559-568.
    • (1998) Biophys. J. , vol.74 , pp. 559-568
    • Thuman-Commike, P.A.1    Greene, B.2    Malinski, J.A.3    King, J.4    Chiu, W.5
  • 310
    • 0025074665 scopus 로고
    • Concentration of solutes during preparation of aqueous suspensions for cryo-electron microscopy
    • Trinick, J., and J. Cooper. 1990. Concentration of solutes during preparation of aqueous suspensions for cryo-electron microscopy. J. Microsc. 159: 215-222.
    • (1990) J. Microsc. , vol.159 , pp. 215-222
    • Trinick, J.1    Cooper, J.2
  • 311
    • 0029908793 scopus 로고    scopus 로고
    • The herpes simplex virus procapsid: Structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly
    • Trus, B. L., F. P. Booy, W. W. Newcomb, J. C. Brown, F. L. Homa, D. R. Thomsen, and A. C. Steven. 1996. The herpes simplex virus procapsid: structure, conformational changes upon maturation, and roles of the triplex proteins VP19c and VP23 in assembly. J. Mol. Biol. 263:447-462.
    • (1996) J. Mol. Biol. , vol.263 , pp. 447-462
    • Trus, B.L.1    Booy, F.P.2    Newcomb, W.W.3    Brown, J.C.4    Homa, F.L.5    Thomsen, D.R.6    Steven, A.C.7
  • 312
    • 0028783737 scopus 로고
    • Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: Structural authenticity and localization of vp26
    • Trus, B. L., F. L. Homa, F. P. Booy, W. W. Newcomb, D. R. Thompson, N. Cheng, J. C. Brown, and A. C. Steven. 1995. Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of vp26. J. Virol. 69:7362-7366.
    • (1995) J. Virol. , vol.69 , pp. 7362-7366
    • Trus, B.L.1    Homa, F.L.2    Booy, F.P.3    Newcomb, W.W.4    Thompson, D.R.5    Cheng, N.6    Brown, J.C.7    Steven, A.C.8
  • 313
    • 0026490068 scopus 로고
    • Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid
    • Trus, B. L., W. W. Newcomb, F. P. Booy. J. C. Brown, and A. C. Steven. 1992. Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid. Proc. Natl. Acad. Sci. USA 89: 11508-11512.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11508-11512
    • Trus, B.L.1    Newcomb, W.W.2    Booy, F.P.3    Brown, J.C.4    Steven, A.C.5
  • 314
    • 0030931283 scopus 로고    scopus 로고
    • Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 A resolution
    • Trus, B. L., R. B. S. Roden, H. L. Greenstone, M. Vrhel, J. T. Schiller, and F. P. Booy. 1997. Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 A resolution. Nat. Struct. Biol. 4:413-420.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 413-420
    • Trus, B.L.1    Roden, R.B.S.2    Greenstone, H.L.3    Vrhel, M.4    Schiller, J.T.5    Booy, F.P.6
  • 316
    • 0344386192 scopus 로고
    • An optimized Faraday cage design for electron beam current measurements
    • Turner, J. N., G. G. J. Hausner, and D. F. Parsons. 1975. An optimized Faraday cage design for electron beam current measurements. J. Phys. E Sci. Instrum. 8:954-957.
    • (1975) J. Phys. E Sci. Instrum. , vol.8 , pp. 954-957
    • Turner, J.N.1    Hausner, G.G.J.2    Parsons, D.F.3
  • 317
    • 0016688080 scopus 로고
    • Molecular structure determination by electron microscopy of unstained crystalline specimens
    • Unwin, P. N. T., and R. Henderson. 1975. Molecular structure determination by electron microscopy of unstained crystalline specimens. J. Mol. Biol. 94:425-440.
    • (1975) J. Mol. Biol. , vol.94 , pp. 425-440
    • Unwin, P.N.T.1    Henderson, R.2
  • 318
    • 0016296364 scopus 로고
    • Electron microscopy of the stacked discaggregate of tobacco mosaic virus protein. I. Three-dimensional image reconstruction
    • Unwin, P. N. T., and A. Klug. 1974. Electron microscopy of the stacked discaggregate of tobacco mosaic virus protein. I. Three-dimensional image reconstruction. J. Mol. Biol. 87:641-656.
    • (1974) J. Mol. Biol. , vol.87 , pp. 641-656
    • Unwin, P.N.T.1    Klug, A.2
  • 319
    • 0017183621 scopus 로고
    • Comparative properties of bacteriophage φ6 and φ6 nuclcocapsid
    • Van Etten, J. L., L. Lane, C. Gonzales, J. Partridge, and A. Vidaver. 1976. Comparative properties of bacteriophage φ6 and φ6 nuclcocapsid. J. Virol. 18:652-658.
    • (1976) J. Virol. , vol.18 , pp. 652-658
    • Van Etten, J.L.1    Lane, L.2    Gonzales, C.3    Partridge, J.4    Vidaver, A.5
  • 320
    • 0015858583 scopus 로고
    • RNA polymerase activity associated with bacteriophage φ6
    • Van Etten, J. L., A. K. Vidaver, R. K. Koski, and J. S. Semancik. 1973. RNA polymerase activity associated with bacteriophage φ6. J. Virol. 12:464-471.
    • (1973) J. Virol. , vol.12 , pp. 464-471
    • Van Etten, J.L.1    Vidaver, A.K.2    Koski, R.K.3    Semancik, J.S.4
  • 321
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel, M. 1987. Similarity measures between images. Ultramicroscopy 21:95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 322
    • 0029916485 scopus 로고    scopus 로고
    • A new generation of the IMAGIC image processing system
    • van Heel, M., G. Harauz, and E. V. Orlova. 1996. A new generation of the IMAGIC image processing system. J. Struct. Biol. 116:17-24.
    • (1996) J. Struct. Biol. , vol.116 , pp. 17-24
    • Van Heel, M.1    Harauz, G.2    Orlova, E.V.3
  • 323
    • 0022348579 scopus 로고
    • Molecular composition of the adenovirus type 2 virion
    • van Oostrum, J., and R. M. Burnett. 1985. Molecular composition of the adenovirus type 2 virion. J. Virol. 56:439-448.
    • (1985) J. Virol. , vol.56 , pp. 439-448
    • Van Oostrum, J.A.1    Burnett, R.M.2
  • 324
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9A resolution
    • London
    • Varghese, J. N., W. G. Laver, and P. M. Colman. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9A resolution. Nature (London) 303:35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 325
    • 0028316182 scopus 로고
    • The organization of the spike complex of Semliki forest virus
    • Vénien-Bryan, C., and S. D. Fuller. 1994. The organization of the spike complex of Semliki Forest virus. J. Mol. Biol. 236:572-583.
    • (1994) J. Mol. Biol. , vol.236 , pp. 572-583
    • Vénien-Bryan, C.1    Fuller, S.D.2
  • 326
    • 0024220731 scopus 로고
    • Three-dimensional reconstruction from electron micrographs of disordered specimens. II. Implementation and results
    • Vogel, R. H., and S. W. Provencher. 1988. Three-dimensional reconstruction from electron micrographs of disordered specimens. II. Implementation and results. Ultramicroscopy 25:223-240.
    • (1988) Ultramicroscopy , vol.25 , pp. 223-240
    • Vogel, R.H.1    Provencher, S.W.2
  • 327
    • 0022539125 scopus 로고
    • Envelope structure of Semliki forest virus reconstructed from cryo-electron micrographs
    • London
    • Vogel, R. H., S. W. Provencher, C.-H. Bonsdorff, M. Adrian, and J. Dubochet. 1986. Envelope structure of Semliki Forest virus reconstructed from cryo-electron micrographs. Nature (London) 320:533-535.
    • (1986) Nature , vol.320 , pp. 533-535
    • Vogel, R.H.1    Provencher, S.W.2    Bonsdorff, C.-H.3    Adrian, M.4    Dubochet, J.5
  • 328
    • 0032949985 scopus 로고    scopus 로고
    • A helper-independent adenovirus vector with E1, E3, and fiber deleted: Structure and intectivity of fiberless particles
    • Von Seggern, D. J., C. Y. Chiu, S. K. Fleck, P. L. Stewart, and G. R. Nemerow. 1999. A helper-independent adenovirus vector with E1, E3, and fiber deleted: structure and intectivity of fiberless particles. J. Virol. 73: 1601-1608.
    • (1999) J. Virol. , vol.73 , pp. 1601-1608
    • Von Seggern, D.J.1    Chiu, C.Y.2    Fleck, S.K.3    Stewart, P.L.4    Nemerow, G.R.5
  • 329
    • 0026566945 scopus 로고
    • A brief look at imaging and contrast transfer
    • Wade, R. H. 1992. A brief look at imaging and contrast transfer. Ultramicroscopy 46:145-156.
    • (1992) Ultramicroscopy , vol.46 , pp. 145-156
    • Wade, R.H.1
  • 330
    • 0027164079 scopus 로고
    • Cryo-electron microscopy of microtubules
    • Wade, R. H., and D. Chrétien. 1993. Cryo-electron microscopy of microtubules. J. Struct. Biol. 110:1-27.
    • (1993) J. Struct. Biol. , vol.110 , pp. 1-27
    • Wade, R.H.1    Chrétien, D.2
  • 331
    • 0017541997 scopus 로고
    • Electron microscope transfer functions for partially coherent axial illumination and chromatic defocus spread
    • Wade, R. H., and J. Frank. 1977. Electron microscope transfer functions for partially coherent axial illumination and chromatic defocus spread. Optik 49:81-92.
    • (1977) Optik , vol.49 , pp. 81-92
    • Wade, R.H.1    Frank, J.2
  • 332
    • 0028041141 scopus 로고
    • Cryoelectron microscopy of macromolecular complexes
    • Wade, R. H., and E. A. Hewat. 1994. Cryoelectron microscopy of macromolecular complexes. Biol. Cell 80:211-220.
    • (1994) Biol. Cell , vol.80 , pp. 211-220
    • Wade, R.H.1    Hewat, E.A.2
  • 333
    • 0026495818 scopus 로고
    • Membrane fusion of Semliki forest virus involves homotrimers of the fusion protein
    • Wahlberg, J. M., R. Bron, J. Wilschut, and H. Garoff. 1992. Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein. J. Virol. 66:7309-7318.
    • (1992) J. Virol. , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 334
    • 0033582235 scopus 로고    scopus 로고
    • Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: Evidence that the start of the crossbridge power stroke; in muscle has variable geometry
    • Walker, M., X.-Z. Zhang, W. Jiang, J. Trinick, and H. D. White. 1999. Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the crossbridge power stroke; in muscle has variable geometry. Proc. Natl. Acad. Sci. USA 96:465-470.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 465-470
    • Walker, M.1    Zhang, X.-Z.2    Jiang, W.3    Trinick, J.4    White, H.D.5
  • 336
    • 0345680635 scopus 로고    scopus 로고
    • Personal communication
    • Wang, G. J. Personal communication.
    • Wang, G.J.1
  • 337
    • 0027121512 scopus 로고
    • Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and x-ray crystallography
    • London
    • Wang, G.-J., C. Porta, Z. Chen, T. S. Baker, and J. E. Johnson. 1992. Identification of a Fab interaction footprint site on an icosahedral virus by cryoelectron microscopy and X-ray crystallography. Nature (London) 355: 275-278.
    • (1992) Nature , vol.355 , pp. 275-278
    • Wang, G.-J.1    Porta, C.2    Chen, Z.3    Baker, T.S.4    Johnson, J.E.5
  • 338
    • 0345680634 scopus 로고
    • The analysis of a spherical virus-Fab interaction by cryo-electron microscopy and x-ray crystallography
    • K. H. Kuo and Z. H. Zhai (ed.), World Scientific Publishing, River Edge. N.J.
    • Wang, G.-J., C. Porta, Z. Chen, R. H. Cheng, T. S. Baker, and J. E. Johnson. 1992. The analysis of a spherical virus-Fab interaction by cryo-electron microscopy and X-ray crystallography, p. 158-159. In K. H. Kuo and Z. H. Zhai (ed.), Electron microscopy II. 5th Asian Pacific Electron Microscopy Conference. World Scientific Publishing, River Edge. N.J.
    • (1992) Electron Microscopy II. 5th Asian Pacific Electron Microscopy Conference , pp. 158-159
    • Wang, G.-J.1    Porta, C.2    Chen, Z.3    Cheng, R.H.4    Baker, T.S.5    Johnson, J.E.6
  • 340
    • 0027953618 scopus 로고
    • The refined three-dimensional structure of an insect virus at 2.8 A resolution
    • Wery, J.-P., V. S. Reddy, M. V. Hosur, and J. E. Johnson. 1994. The refined three-dimensional structure of an insect virus at 2.8 A resolution. J. Mol. Biol. 235:565-586.
    • (1994) J. Mol. Biol. , vol.235 , pp. 565-586
    • Wery, J.-P.1    Reddy, V.S.2    Hosur, M.V.3    Johnson, J.E.4
  • 341
    • 0028169584 scopus 로고
    • Integrin αvβ5 selectively promotes adenovirus mediated cell membrane permeabilization
    • Wickham, T. J., E. J. Filardo, D. A. Cheresh, and G. R. Nemerow. 1994. Integrin αvβ5 selectively promotes adenovirus mediated cell membrane permeabilization. J. Cell Biol. 127:257-264.
    • (1994) J. Cell Biol. , vol.127 , pp. 257-264
    • Wickham, T.J.1    Filardo, E.J.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 343
    • 0000256849 scopus 로고    scopus 로고
    • Viruses of yeasts, fungi and parasitic microorganisms
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.). Lippincott-Raven, Philadelphia, Pa
    • Wickner, R. B. 1996. Viruses of yeasts, fungi and parasitic microorganisms, p. 557-585. In B. N. Fields, D. M. Knipe, P. M. Howley, et al. (ed.). Fields virology, 3rd ed., vol. 1. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , vol.1 , pp. 557-585
    • Wickner, R.B.1
  • 344
    • 0342981744 scopus 로고    scopus 로고
    • The structure of cucumber mosaic virus: Cryoelectron microscopy. X-ray crystallography, and sequence analysis
    • Wikoff, W. R., C. J. Tsai, G. Wang, T. S. Baker, and J. E. Johnson. 1997. The structure of cucumber mosaic virus: cryoelectron microscopy. X-ray crystallography, and sequence analysis. Virology 232:91-97.
    • (1997) Virology , vol.232 , pp. 91-97
    • Wikoff, W.R.1    Tsai, C.J.2    Wang, G.3    Baker, T.S.4    Johnson, J.E.5
  • 345
    • 0028773903 scopus 로고
    • The structure of a neutralized virus: Canine parvovirus complexed with neutralizing antibody fragment
    • Wikoff, W. R., G. Wang, C. R. Parrish, R. H. Cheng, M. L. Strassheim, T. S. Baker, and M. G. Rossmann, 1994. The structure of a neutralized virus: canine parvovirus complexed with neutralizing antibody fragment. Structure 2:595-607.
    • (1994) Structure , vol.2 , pp. 595-607
    • Wikoff, W.R.1    Wang, G.2    Parrish, C.R.3    Cheng, R.H.4    Strassheim, M.L.5    Baker, T.S.6    Rossmann, M.G.7
  • 346
    • 0014966182 scopus 로고
    • Electron microscopy of tobacco mosaic virus under conditions of minimal beam exposure. 1
    • Williams, R. C., and H. W. Fisher. 1970. Electron microscopy of tobacco mosaic virus under conditions of minimal beam exposure. 1. Mol. Biol. 52: 121-123.
    • (1970) Mol. Biol. , vol.52 , pp. 121-123
    • Williams, R.C.1    Fisher, H.W.2
  • 347
    • 0016393817 scopus 로고
    • Capsid structure of bacteriophage lambda
    • Williams, R. C., and K. E. Richards. 1974. Capsid structure of bacteriophage lambda. J. Mol. Biol. 88:547-550.
    • (1974) J. Mol. Biol. , vol.88 , pp. 547-550
    • Williams, R.C.1    Richards, K.E.2
  • 348
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • London
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature (London) 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 349
    • 0030774226 scopus 로고    scopus 로고
    • Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virus
    • Wingfield, P. T., S. J. Stahl, D. R. Thomsen, F. L. Homa, F. P. Booy, B. L. Trus, and A. C. Steven. 1997. Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virus. J. Virol. 71:8955-8961.
    • (1997) J. Virol. , vol.71 , pp. 8955-8961
    • Wingfield, P.T.1    Stahl, S.J.2    Thomsen, D.R.3    Homa, F.L.4    Booy, F.P.5    Trus, B.L.6    Steven, A.C.7
  • 350
    • 0025741668 scopus 로고
    • Three-dimensional structure of myosin subfragment-1 from electron microscopy of sectioned crystals
    • Winkelmann, D. A., T. S. Baker, and I. Rayment. 1991. Three-dimensional structure of myosin subfragment-1 from electron microscopy of sectioned crystals. J. Cell Biol. 114:701-713.
    • (1991) J. Cell Biol. , vol.114 , pp. 701-713
    • Winkelmann, D.A.1    Baker, T.S.2    Rayment, I.3
  • 351
    • 0017359170 scopus 로고
    • Tomato bushy stunt virus at 5.5 Å resolution
    • London
    • Winkler, F. K., C. E. Schutt, S. C. Harrison, and G. Bricogne. 1977. Tomato bushy stunt virus at 5.5 Å resolution. Nature (London) 265:509-513.
    • (1977) Nature , vol.265 , pp. 509-513
    • Winkler, F.K.1    Schutt, C.E.2    Harrison, S.C.3    Bricogne, G.4
  • 352
    • 0344386189 scopus 로고    scopus 로고
    • Cryo-electron microscopy and image reconstruction of PBCV-1, an algal virus with T=169, icosahedral lattice symmetry
    • Springer-Verlag, New York, N.Y.
    • Yan, X., N. Olson, J. Van Etten, and T. Baker. 1998. Cryo-electron microscopy and image reconstruction of PBCV-1, an algal virus with T=169, icosahedral lattice symmetry. Proc. Microsc. Microanal. 4:948-949. Springer-Verlag, New York, N.Y.
    • (1998) Proc. Microsc. Microanal. , vol.4 , pp. 948-949
    • Yan, X.1    Olson, N.2    Van Etten, J.3    Baker, T.4
  • 353
    • 0028205688 scopus 로고
    • Three-dimensional structure of the rotavirus hemagglutinin VP4 by cryo-electron microscopy and difference map analysis
    • Yeager, M., J. A. Berrimann, T. S. Baker, and A. R. Bellamy. 1994. Three-dimensional structure of the rotavirus hemagglutinin VP4 by cryo-electron microscopy and difference map analysis. EMBO J. 13:1011-1018.
    • (1994) EMBO J. , vol.13 , pp. 1011-1018
    • Yeager, M.1    Berrimann, J.A.2    Baker, T.S.3    Bellamy, A.R.4
  • 354
    • 0025371944 scopus 로고
    • Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction
    • Yeager, M., K. A. Dryden, N. H. Olson, H. B. Greenberg, and T. S. Baker. 1990. Three-dimensional structure of rhesus rotavirus by cryoelectron microscopy and image reconstruction. J. Cell Biol. 110:2133-2144.
    • (1990) J. Cell Biol. , vol.110 , pp. 2133-2144
    • Yeager, M.1    Dryden, K.A.2    Olson, N.H.3    Greenberg, H.B.4    Baker, T.S.5
  • 355
    • 0026932437 scopus 로고
    • Desired features of cryoelectron microscope for the electron crystallography of biological material
    • Zemlin, F. 1992. Desired features of cryoelectron microscope for the electron crystallography of biological material. Ultramicroscopy 46:25-32.
    • (1992) Ultramicroscopy , vol.46 , pp. 25-32
    • Zemlin, F.1
  • 356
    • 0344817866 scopus 로고
    • High-resolution cryo-electron microscopy of 2-D protein crystals
    • Seattle. Wash., San Francisco Press, San Francisco. Calif.
    • Zemlin, F., and E. Beckmann. 1990. High-resolution cryo-electron microscopy of 2-D protein crystals, p. 84-85. In Proceedings of the XIIth International Congress on Electron Microscopy, Seattle. Wash., vol. 1. San Francisco Press, San Francisco. Calif.
    • (1990) Proceedings of the XIIth International Congress on Electron Microscopy , vol.1 , pp. 84-85
    • Zemlin, F.1    Beckmann, E.2
  • 358
    • 0344386188 scopus 로고    scopus 로고
    • Cryo-electron microscopy of aura viruses
    • Springer-Verlag, New York, N.Y.
    • Zhang, W., N. Olson, B. McKinney, R. Kuhn, and T. Baker. 1998. Cryo-electron microscopy of aura viruses. Proc. Microsc. Microanal. 4:946-947. Springer-Verlag, New York, N.Y.
    • (1998) Proc. Microsc. Microanal. , vol.4 , pp. 946-947
    • Zhang, W.1    Olson, N.2    McKinney, B.3    Kuhn, R.4    Baker, T.5
  • 359
    • 0028919805 scopus 로고
    • In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA
    • Zhao, X., J. M. Fox, N. H. Olson, T. S. Baker, and M. J. Young. 1995. In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA. Virology 207:486-494.
    • (1995) Virology , vol.207 , pp. 486-494
    • Zhao, X.1    Fox, J.M.2    Olson, N.H.3    Baker, T.S.4    Young, M.J.5
  • 360
    • 0345471494 scopus 로고    scopus 로고
    • Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions
    • Zhou, Z. H., D. H. Chen, J. Jakana, F. J. Rixon, and W. Chiu. 1999. Visualization of tegument-capsid interactions and DNA in intact herpes simplex virus type 1 virions. J. Virol. 73:3210-3218.
    • (1999) J. Virol. , vol.73 , pp. 3210-3218
    • Zhou, Z.H.1    Chen, D.H.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 361
    • 0027543395 scopus 로고
    • Prospects for using an IVEM with a FEG for imaging macromoleculcs towards atomic resolution
    • Zhou, Z. H., and W. Chiu. 1993. Prospects for using an IVEM with a FEG for imaging macromoleculcs towards atomic resolution. Ultramicroscopy 49:407-416.
    • (1993) Ultramicroscopy , vol.49 , pp. 407-416
    • Zhou, Z.H.1    Chiu, W.2
  • 363
    • 0028804828 scopus 로고
    • Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids
    • Zhou, Z. H., J. He, J. Jakana, J. D. Tatman, F. J. Rixon, and W. Chiu. 1995. Assembly of VP26 in herpes simplex virus-1 inferred from structures of wild-type and recombinant capsids. Nat. Struct. Biol. 2:1026-1030.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1026-1030
    • Zhou, Z.H.1    He, J.2    Jakana, J.3    Tatman, J.D.4    Rixon, F.J.5    Chiu, W.6
  • 364
    • 0028151168 scopus 로고
    • Protein subunit structures in the herpes simplex virus A-capsid determined from 400kV spot-scan electron cryomicroscopy
    • Zhou, Z. H., B. V. V. Prasad, J. Jakana, F. J. Rixon, and W. Chiu. 1994. Protein subunit structures in the herpes simplex virus A-capsid determined from 400kV spot-scan electron cryomicroscopy. J. Mol. Biol. 242:456-469.
    • (1994) J. Mol. Biol. , vol.242 , pp. 456-469
    • Zhou, Z.H.1    Prasad, B.V.V.2    Jakana, J.3    Rixon, F.J.4    Chiu, W.5
  • 365
    • 0030930426 scopus 로고    scopus 로고
    • Localization of the C terminus of the assembly domain of hepatitis B capsid protein: Implications for morphogenesis and organization of encapsidated RNA
    • Zlotnick, A. 1997. Localization of the C terminus of the assembly domain of hepatitis B capsid protein: implications for morphogenesis and organization of encapsidated RNA. Proc. Natl. Acad. Sci. USA 94:9556-9561.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9556-9561
    • Zlotnick, A.1
  • 366
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick, A., N. Cheng, J. F. Conway, F. P. Booy, A. C. Steven, S. J. Stahl, and P. T. Wingfleld. 1996. Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35:7412-7421.
    • (1996) Biochemistry , vol.35 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfleld, P.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.