메뉴 건너뛰기




Volumn 157, Issue 2, 2007, Pages 356-364

Structural analysis of viral nucleocapsids by subtraction of partial projections

Author keywords

Flaviviruses; Nucleocapsid; Structure; Symmetry mismatch

Indexed keywords

GLYCOPROTEIN;

EID: 33846232731     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2006.09.002     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 0029162425 scopus 로고
    • Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form
    • Allison S.L., Stadler K., Mandl C.W., Kunz C., and Heinz F.X. Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form. J. Virol. 69 (1995) 5816-5820
    • (1995) J. Virol. , vol.69 , pp. 5816-5820
    • Allison, S.L.1    Stadler, K.2    Mandl, C.W.3    Kunz, C.4    Heinz, F.X.5
  • 2
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 (1996) 120-130
    • (1996) J. Struct. Biol. , vol.116 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 3
    • 0025060289 scopus 로고
    • Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy
    • Baker T.S., Newcomb W.W., Booy F.P., Brown J.C., and Steven A.C. Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy. J. Virol. 64 (1990) 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
  • 4
    • 0032712359 scopus 로고    scopus 로고
    • Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs
    • Baker T.S., Olson N.H., and Fuller S.D. Adding the third dimension to virus life cycles: three-dimensional reconstruction of icosahedral viruses from cryo-electron micrographs. Microbiol. Mol. Biol. Rev. 63 (1999) 862-922
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 862-922
    • Baker, T.S.1    Olson, N.H.2    Fuller, S.D.3
  • 5
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • Booy F.P., Newcomb W.W., Trus B.L., Brown J.C., Baker T.S., and Steven A.C. Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64 (1991) 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
  • 7
    • 0015242164 scopus 로고
    • Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs
    • Crowther R.A. Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. Roy. Soc. Lond. B 261 (1971) 221-230
    • (1971) Phil. Trans. Roy. Soc. Lond. B , vol.261 , pp. 221-230
    • Crowther, R.A.1
  • 8
    • 3142611054 scopus 로고    scopus 로고
    • West Nile virus core protein: tetramer structure and ribbon formation
    • Dokland T., Walsh M., Mackenzie J.M., Khromykh A.A., Ee K., and Wang S. West Nile virus core protein: tetramer structure and ribbon formation. Structure 12 (2004) 1157-1163
    • (2004) Structure , vol.12 , pp. 1157-1163
    • Dokland, T.1    Walsh, M.2    Mackenzie, J.M.3    Khromykh, A.A.4    Ee, K.5    Wang, S.6
  • 9
    • 0028039833 scopus 로고
    • Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice
    • Fonseca B.A., Pincus S., Shope R.E., Paoletti E., and Mason P.W. Recombinant vaccinia viruses co-expressing dengue-1 glycoproteins prM and E induce neutralizing antibodies in mice. Vaccine 12 (1994) 279-285
    • (1994) Vaccine , vol.12 , pp. 279-285
    • Fonseca, B.A.1    Pincus, S.2    Shope, R.E.3    Paoletti, E.4    Mason, P.W.5
  • 11
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., and Leith A. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116 (1996) 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
  • 12
    • 0019802812 scopus 로고
    • Computer averaging of electron micrographs of 40S ribosomal subunits
    • Frank J., Verschoor A., and Boublik M. Computer averaging of electron micrographs of 40S ribosomal subunits. Science 214 (1981) 1353-1355
    • (1981) Science , vol.214 , pp. 1353-1355
    • Frank, J.1    Verschoor, A.2    Boublik, M.3
  • 13
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles-the uncommon line
    • Fuller S.D., Butcher S.J., Cheng R.H., and Baker T.S. Three-dimensional reconstruction of icosahedral particles-the uncommon line. J. Struct. Biol. 116 (1996) 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
  • 14
    • 0041736713 scopus 로고    scopus 로고
    • Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 Å resolution
    • Furst J., Sutton R.B., Chen J., Brunger A.T., and Grigorieff N. Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 Å resolution. EMBO J. 22 (2003) 4365-4374
    • (2003) EMBO J. , vol.22 , pp. 4365-4374
    • Furst, J.1    Sutton, R.B.2    Chen, J.3    Brunger, A.T.4    Grigorieff, N.5
  • 15
    • 34248171243 scopus 로고    scopus 로고
    • Huiskonen, J.T., Jäälinoja, H.T., Briggs, J.A.G., Fuller, S.D., Butcher, S.J., 2006. Structure of a hexameric RNA packaging motor in a viral polymerase complex. J. Struct. Biol., in press.
  • 16
    • 0026766722 scopus 로고
    • Mice immunized with a subviral particle containing the Japanese encephalitis virus prM/M and E proteins are protected from lethal JEV infection
    • Konishi E., Pincus S., Paoletti E., Shope R.E., Burrage T., and Mason P.W. Mice immunized with a subviral particle containing the Japanese encephalitis virus prM/M and E proteins are protected from lethal JEV infection. Virology 188 (1992) 714-720
    • (1992) Virology , vol.188 , pp. 714-720
    • Konishi, E.1    Pincus, S.2    Paoletti, E.3    Shope, R.E.4    Burrage, T.5    Mason, P.W.6
  • 20
    • 0000163169 scopus 로고    scopus 로고
    • Flaviviridae: the viruses and their replication
    • Knipe D.M., and Howley P.M. (Eds), Lippincott Williams and Wilkins, Philadelphia
    • Lindenbach B.D., and Rice C.M. Flaviviridae: the viruses and their replication. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology Vol. 1 (2001), Lippincott Williams and Wilkins, Philadelphia 991-1042
    • (2001) Fields Virology , vol.1 , pp. 991-1042
    • Lindenbach, B.D.1    Rice, C.M.2
  • 21
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 24
    • 0035211731 scopus 로고    scopus 로고
    • Transport and budding at two distinct sites of visible nucleocapsids of West Nile (Sarafend) virus
    • Ng M.L., Tan S.H., and Chu J.J. Transport and budding at two distinct sites of visible nucleocapsids of West Nile (Sarafend) virus. J. Med. Virol. 65 (2001) 758-764
    • (2001) J. Med. Virol. , vol.65 , pp. 758-764
    • Ng, M.L.1    Tan, S.H.2    Chu, J.J.3
  • 25
    • 0026505138 scopus 로고
    • Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis
    • Pincus S., Mason P.W., Konishi E., Fonseca B.A., Shope R.E., Rice C.M., and Paoletti E. Recombinant vaccinia virus producing the prM and E proteins of yellow fever virus protects mice from lethal yellow fever encephalitis. Virology 187 (1992) 290-297
    • (1992) Virology , vol.187 , pp. 290-297
    • Pincus, S.1    Mason, P.W.2    Konishi, E.3    Fonseca, B.A.4    Shope, R.E.5    Rice, C.M.6    Paoletti, E.7
  • 27
    • 1542347791 scopus 로고    scopus 로고
    • Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length
    • Tihova M., Dryden K.A., Le T.L., Harvey S.C., Johnson J.E., Yeager M., and Schneemann A. Nodavirus coat protein imposes dodecahedral RNA structure independent of nucleotide sequence and length. J. Virol. 78 (2004) 2897-2905
    • (2004) J. Virol. , vol.78 , pp. 2897-2905
    • Tihova, M.1    Dryden, K.A.2    Le, T.L.3    Harvey, S.C.4    Johnson, J.E.5    Yeager, M.6    Schneemann, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.