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Volumn 387, Issue 1, 2009, Pages 11-15

Single-particle cryo-electron microscopy of Rift Valley fever virus

Author keywords

Bunyaviridae; Cryo electron microscopy; Inter capsomer contacts; Rift Valley fever virus; Single particle averaging

Indexed keywords

VIRUS GLYCOPROTEIN; VIRUS VACCINE;

EID: 63549107008     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.02.038     Document Type: Article
Times cited : (85)

References (21)
  • 1
    • 0029665272 scopus 로고    scopus 로고
    • A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy
    • Baker T.S., and Cheng R.H. A model-based approach for determining orientations of biological macromolecules imaged by cryoelectron microscopy. J. Struct. Biol. 116 1 (1996) 120-130
    • (1996) J. Struct. Biol. , vol.116 , Issue.1 , pp. 120-130
    • Baker, T.S.1    Cheng, R.H.2
  • 2
    • 0037292883 scopus 로고    scopus 로고
    • Rift Valley fever: an uninvited zoonosis in the Arabian peninsula
    • Balkhy H.H., and Memish Z.A. Rift Valley fever: an uninvited zoonosis in the Arabian peninsula. Int. J. Antimicrob. Agents 21 2 (2003) 153-157
    • (2003) Int. J. Antimicrob. Agents , vol.21 , Issue.2 , pp. 153-157
    • Balkhy, H.H.1    Memish, Z.A.2
  • 3
    • 0026044403 scopus 로고
    • Oligomerization, transport, and Golgi retention of Punta Toro virus glycoproteins
    • Chen S.Y., and Compans R.W. Oligomerization, transport, and Golgi retention of Punta Toro virus glycoproteins. J. Virol. 65 11 (1991) 5902-5909
    • (1991) J. Virol. , vol.65 , Issue.11 , pp. 5902-5909
    • Chen, S.Y.1    Compans, R.W.2
  • 4
    • 55249110450 scopus 로고    scopus 로고
    • Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    • Freiberg A.N., Sherman M.B., Morais M.C., Holbrook M.R., and Watowich S.J. Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography. J. Virol. 82 21 (2008) 10341-10348
    • (2008) J. Virol. , vol.82 , Issue.21 , pp. 10341-10348
    • Freiberg, A.N.1    Sherman, M.B.2    Morais, M.C.3    Holbrook, M.R.4    Watowich, S.J.5
  • 5
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)
    • Garry C.E., and Garry R.F. Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes). Theor. Biol. Med. Model 1 (2004) 10
    • (2004) Theor. Biol. Med. Model , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 6
    • 33751440340 scopus 로고    scopus 로고
    • Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins
    • Gerrard S.R., and Nichol S.T. Synthesis, proteolytic processing and complex formation of N-terminally nested precursor proteins of the Rift Valley fever virus glycoproteins. Virology 357 2 (2007) 124-133
    • (2007) Virology , vol.357 , Issue.2 , pp. 124-133
    • Gerrard, S.R.1    Nichol, S.T.2
  • 7
    • 64049094507 scopus 로고    scopus 로고
    • Cryo-Microscopy and Single-Particle Averaging of Rift Valley Fever Virus: Evidence for GN-GC Glycoprotein Heterodimers. J. Virol. doi:10.1128/JVI.02483-08, in press
    • Huiskonen, J.T., Overby, A.K., Weber, F., Grunewald, K., in press. Electron Cryo-Microscopy and Single-Particle Averaging of Rift Valley Fever Virus: Evidence for GN-GC Glycoprotein Heterodimers. J. Virol. doi:10.1128/JVI.02483-08.
    • Electron
    • Huiskonen, J.T.1    Overby, A.K.2    Weber, F.3    Grunewald, K.4
  • 8
    • 33644995874 scopus 로고    scopus 로고
    • A model-based parallel origin and orientation refinement algorithm for cryoTEM and its application to the study of virus structures
    • Ji Y., Marinescu D.C., Zhang W., Zhang X., Yan X., and Baker T.S. A model-based parallel origin and orientation refinement algorithm for cryoTEM and its application to the study of virus structures. J. Struct. Biol. 154 1 (2006) 1-19
    • (2006) J. Struct. Biol. , vol.154 , Issue.1 , pp. 1-19
    • Ji, Y.1    Marinescu, D.C.2    Zhang, W.3    Zhang, X.4    Yan, X.5    Baker, T.S.6
  • 9
    • 48349131507 scopus 로고    scopus 로고
    • Rift Valley fever virus structural proteins: expression, characterization and assembly of recombinant proteins
    • Liu L., Celma C.C., and Roy P. Rift Valley fever virus structural proteins: expression, characterization and assembly of recombinant proteins. Virol. J. 5 (2008) 82
    • (2008) Virol. J. , vol.5 , pp. 82
    • Liu, L.1    Celma, C.C.2    Roy, P.3
  • 10
    • 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 1 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 11
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 2 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , Issue.2 , pp. 491-497
    • Matthews, B.W.1
  • 12
    • 33750374298 scopus 로고    scopus 로고
    • Generation and analysis of infectious virus-like particles of Uukuniemi virus (Bunyaviridae): a useful system for studying bunyaviral packaging and budding
    • Overby A.K., Popov V., Neve E.P., and Pettersson R.F. Generation and analysis of infectious virus-like particles of Uukuniemi virus (Bunyaviridae): a useful system for studying bunyaviral packaging and budding. J. Virol. 80 21 (2006) 10428-10435
    • (2006) J. Virol. , vol.80 , Issue.21 , pp. 10428-10435
    • Overby, A.K.1    Popov, V.2    Neve, E.P.3    Pettersson, R.F.4
  • 13
    • 33947383002 scopus 로고    scopus 로고
    • The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae) interacts with ribonucleoproteins and is critical for genome packaging
    • Overby A.K., Pettersson R.F., and Neve E.P. The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae) interacts with ribonucleoproteins and is critical for genome packaging. J. Virol. 81 7 (2007) 3198-3205
    • (2007) J. Virol. , vol.81 , Issue.7 , pp. 3198-3205
    • Overby, A.K.1    Pettersson, R.F.2    Neve, E.P.3
  • 14
    • 40649115227 scopus 로고    scopus 로고
    • Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus
    • Overby A.K., Pettersson R.F., Grunewald K., and Huiskonen J.T. Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus. Proc. Natl. Acad. Sci. U.S.A. 105 7 (2008) 2375-2379
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , Issue.7 , pp. 2375-2379
    • Overby, A.K.1    Pettersson, R.F.2    Grunewald, K.3    Huiskonen, J.T.4
  • 16
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., and Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375 6529 (1995) 291-298
    • (1995) Nature , vol.375 , Issue.6529 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 17
    • 0029163526 scopus 로고
    • Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus
    • Ronka H., Hilden P., Von Bonsdorff C.H., and Kuismanen E. Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus. Virology 211 1 (1995) 241-250
    • (1995) Virology , vol.211 , Issue.1 , pp. 241-250
    • Ronka, H.1    Hilden, P.2    Von Bonsdorff, C.H.3    Kuismanen, E.4
  • 18
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal P.B., and Henderson R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333 4 (2003) 721-745
    • (2003) J. Mol. Biol. , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 19
    • 34948862521 scopus 로고    scopus 로고
    • Bunyaviridae
    • Knipe D.M., and Howley P.M. (Eds), Wolters Kluwer, Philadelphia, PA
    • Schmaljohn C.S., and Nichol S.T. Bunyaviridae. In: Knipe D.M., and Howley P.M. (Eds). Fields Virology. Fifth ed. Vol. 2 (2007), Wolters Kluwer, Philadelphia, PA 1741-1790
    • (2007) Fields Virology. Fifth ed. , vol.2 , pp. 1741-1790
    • Schmaljohn, C.S.1    Nichol, S.T.2
  • 20
    • 35348871306 scopus 로고    scopus 로고
    • Role of the cytoplasmic tail domains of Bunyamwera orthobunyavirus glycoproteins Gn and Gc in virus assembly and morphogenesis
    • Shi X., Kohl A., Li P., and Elliott R.M. Role of the cytoplasmic tail domains of Bunyamwera orthobunyavirus glycoproteins Gn and Gc in virus assembly and morphogenesis. J. Virol. 81 18 (2007) 10151-10160
    • (2007) J. Virol. , vol.81 , Issue.18 , pp. 10151-10160
    • Shi, X.1    Kohl, A.2    Li, P.3    Elliott, R.M.4
  • 21
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A
    • Zhang X., Walker S.B., Chipman P.R., Nibert M.L., and Baker T.S. Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 A. Nat. Struct. Biol. 10 12 (2003) 1011-1018
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.12 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.