메뉴 건너뛰기




Volumn 16, Issue 5, 2004, Pages 673-685

Does common architecture reveal a viral lineage spanning all three domains of life?

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; DOUBLE STRANDED DNA; VIRUS DNA;

EID: 9744228738     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.11.016     Document Type: Article
Times cited : (196)

References (96)
  • 6
    • 0028151167 scopus 로고
    • The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 Å resolution
    • Athappilly F.K., Murali R., Rux J.J., Cai Z., Burnett R.M. The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 Å resolution. J. Mol. Biol. 242:1994;430-455
    • (1994) J. Mol. Biol. , vol.242 , pp. 430-455
    • Athappilly, F.K.1    Murali, R.2    Rux, J.J.3    Cai, Z.4    Burnett, R.M.5
  • 7
    • 0038730770 scopus 로고    scopus 로고
    • Do viruses form lineages across different domains of life?
    • Bamford D.H. Do viruses form lineages across different domains of life? Res. Microbiol. 154:2003;231-236
    • (2003) Res. Microbiol. , vol.154 , pp. 231-236
    • Bamford, D.H.1
  • 8
    • 0021263434 scopus 로고
    • Characterization of the DNA-protein complex at the termini of the bacteriophage PRD1 genome
    • Bamford D.H., Mindich L. Characterization of the DNA-protein complex at the termini of the bacteriophage PRD1 genome. J. Virol. 50:1984;309-315
    • (1984) J. Virol. , vol.50 , pp. 309-315
    • Bamford, D.H.1    Mindich, L.2
  • 9
    • 0029159163 scopus 로고
    • Bacteriophage PRD1: A broad host range dsDNA tectivirus with an internal membrane
    • Bamford D.H., Caldentey J., Bamford J.K.H. Bacteriophage PRD1. A broad host range dsDNA tectivirus with an internal membrane Adv. Virus Res. 45:1995;281-319
    • (1995) Adv. Virus Res. , vol.45 , pp. 281-319
    • Bamford, D.H.1    Caldentey, J.2    Bamford, J.K.H.3
  • 12
    • 0042663851 scopus 로고
    • The presence of a copper/zinc superoxide dismutase in the bacterium Photobacterium leiognathi: A likely case of gene transfer from eukaryotes to prokaryotes
    • Bannister J.V., Parker M.W. The presence of a copper/zinc superoxide dismutase in the bacterium Photobacterium leiognathi. A likely case of gene transfer from eukaryotes to prokaryotes Proc. Natl. Acad. Sci. USA. 82:1985;149-152
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 149-152
    • Bannister, J.V.1    Parker, M.W.2
  • 13
    • 0027412196 scopus 로고
    • Alscript: A tool to format multiple sequence alignments
    • Barton G.J. Alscript. A tool to format multiple sequence alignments Protein Eng. 6:1993;37-40
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 14
    • 0034144697 scopus 로고    scopus 로고
    • Déjà vu all over again' the similar structures of bacteriophage PRD1 and adenovirus
    • Belnap D.M., Steven A.C. Déjà vu all over again'. The similar structures of bacteriophage PRD1 and adenovirus Trends Microbiol. 8:2000;91-93
    • (2000) Trends Microbiol. , vol.8 , pp. 91-93
    • Belnap, D.M.1    Steven, A.C.2
  • 15
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures
    • Benson S.D., Bamford J.K.H., Bamford D.H., Burnett R.M. Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell. 98:1999;825-833
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 16
    • 0036006764 scopus 로고    scopus 로고
    • The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 Å resolution
    • Benson S.D., Bamford J.K.H., Bamford D.H., Burnett R.M. The X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 Å resolution. Acta Crystallogr. D Biol. Crystallogr. 58:2002;39-59
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 39-59
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.M.4
  • 17
    • 0029633168 scopus 로고
    • Gromacs: A message-passing parallel molecular dynamics implementation
    • Berendsen H.J.C., van der Spoel D., van Drunen R. Gromacs. A message-passing parallel molecular dynamics implementation Com. Phys. Comm. 91:1995;43-56
    • (1995) Com. Phys. Comm. , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 18
    • 0022219750 scopus 로고
    • The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture
    • Burnett R.M. The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture. J. Mol. Biol. 185:1985;125-143
    • (1985) J. Mol. Biol. , vol.185 , pp. 125-143
    • Burnett, R.M.1
  • 19
    • 0029561893 scopus 로고
    • DNA packaging orders the membrane of bacteriophage PRD1
    • Butcher S.J., Bamford D.H., Fuller S.D. DNA packaging orders the membrane of bacteriophage PRD1. EMBO J. 14:1995;6078-6086
    • (1995) EMBO J. , vol.14 , pp. 6078-6086
    • Butcher, S.J.1    Bamford, D.H.2    Fuller, S.D.3
  • 21
    • 0037080985 scopus 로고    scopus 로고
    • Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber
    • Chappell J.D., Prota A.E., Dermody T.S., Stehle T. Crystal structure of reovirus attachment protein σ1 reveals evolutionary relationship to adenovirus fiber. EMBO J. 21:2002;1-11
    • (2002) EMBO J. , vol.21 , pp. 1-11
    • Chappell, J.D.1    Prota, A.E.2    Dermody, T.S.3    Stehle, T.4
  • 22
    • 0026489233 scopus 로고
    • Anatomy and evolution of proteins displaying the viral capsid jellyroll topology
    • Chelvanayagam G., Heringa J., Argos P. Anatomy and evolution of proteins displaying the viral capsid jellyroll topology. J. Mol. Biol. 228:1992;220-242
    • (1992) J. Mol. Biol. , vol.228 , pp. 220-242
    • Chelvanayagam, G.1    Heringa, J.2    Argos, P.3
  • 23
    • 0024289975 scopus 로고
    • The 14th barrel rolls out
    • Chothia C. The 14th barrel rolls out. Nature. 333:1988;598-599
    • (1988) Nature , vol.333 , pp. 598-599
    • Chothia, C.1
  • 25
    • 0242351787 scopus 로고    scopus 로고
    • Genetic content and evolution of adenoviruses
    • Davison A.J., Benkö M., Harrach B. Genetic content and evolution of adenoviruses. J. Gen. Virol. 84:2003;2895-2908
    • (2003) J. Gen. Virol. , vol.84 , pp. 2895-2908
    • Davison, A.J.1    Benkö, M.2    Harrach, B.3
  • 26
    • 0035881839 scopus 로고    scopus 로고
    • The complete DNA sequence of the Ectocarpus siliculosus virus EsV-1 genome
    • Delaroque N., Müller D.G., Bothe G., Pohl T., Knippers R., Boland W. The complete DNA sequence of the Ectocarpus siliculosus virus EsV-1 genome. Virology. 287:2001;112-132
    • (2001) Virology , vol.287 , pp. 112-132
    • Delaroque, N.1    Müller, D.G.2    Bothe, G.3    Pohl, T.4    Knippers, R.5    Boland, W.6
  • 27
    • 0019524018 scopus 로고
    • Structure of the linkage between adenovirus DNA and the 55,000 molecular weight terminal protein
    • Desiderio S.V., Kelly T.J. Jr. Structure of the linkage between adenovirus DNA and the 55,000 molecular weight terminal protein. J. Mol. Biol. 145:1981;319-337
    • (1981) J. Mol. Biol. , vol.145 , pp. 319-337
    • Desiderio, S.V.1    Kelly Jr., T.J.2
  • 28
    • 0034761101 scopus 로고    scopus 로고
    • The crystal structure of nucleoplasmin-core: Implications for histone binding and nucleosome assembly
    • Dutta S., Akey I.V., Dingwall C., Hartman K.L., Laue T., Nolte R.T., Head J.F., Akey C.W. The crystal structure of nucleoplasmin-core. Implications for histone binding and nucleosome assembly Mol. Cell. 8:2001;841-853
    • (2001) Mol. Cell , vol.8 , pp. 841-853
    • Dutta, S.1    Akey, I.V.2    Dingwall, C.3    Hartman, K.L.4    Laue, T.5    Nolte, R.T.6    Head, J.F.7    Akey, C.W.8
  • 29
    • 0024357657 scopus 로고
    • The structure of tumor necrosis factor-α at 2.6 Å resolution. Implications for receptor binding
    • Eck M.J., Sprang S.R. The structure of tumor necrosis factor-α at 2.6 Å resolution. Implications for receptor binding. J. Biol. Chem. 264:1989;17595-17605
    • (1989) J. Biol. Chem. , vol.264 , pp. 17595-17605
    • Eck, M.J.1    Sprang, S.R.2
  • 30
    • 0021015110 scopus 로고
    • Enveloped double-stranded DNA insect virus with novel structure and cytopathology
    • Federici B.A. Enveloped double-stranded DNA insect virus with novel structure and cytopathology. Proc. Natl. Acad. Sci. USA. 80:1983;7664-7668
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7664-7668
    • Federici, B.A.1
  • 31
    • 0037663674 scopus 로고    scopus 로고
    • Origin and evolution of polydnaviruses by symbiogenesis of insect DNA viruses in endoparasitic wasps
    • Federici B.A., Bigot Y. Origin and evolution of polydnaviruses by symbiogenesis of insect DNA viruses in endoparasitic wasps. J. Insect Physiol. 49:2003;419-432
    • (2003) J. Insect Physiol. , vol.49 , pp. 419-432
    • Federici, B.A.1    Bigot, Y.2
  • 32
    • 0030696044 scopus 로고    scopus 로고
    • Determining divergence times with a protein clock: Update and reevaluation
    • Feng D.-F., Cho G., Doolittle R.F. Determining divergence times with a protein clock. Update and reevaluation Proc. Natl. Acad. Sci. USA. 94:1997;13028-13033
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13028-13033
    • Feng, D.-F.1    Cho, G.2    Doolittle, R.F.3
  • 34
    • 0040984034 scopus 로고    scopus 로고
    • Inducible gene expression from African swine fever virus recombinants: Analysis of the major capsid protein p72
    • García-Escudero R., Andrés G., Almazán F., Viñuela E. Inducible gene expression from African swine fever virus recombinants. Analysis of the major capsid protein p72 J. Virol. 72:1998;3185-3195
    • (1998) J. Virol. , vol.72 , pp. 3185-3195
    • García-Escudero, R.1    Andrés, G.2    Almazán, F.3    Viñuela, E.4
  • 35
    • 0001526370 scopus 로고
    • A class of multi-symmetric polyhedra
    • Goldberg M. A class of multi-symmetric polyhedra. Tôhoku Math. J. 43:1937;104-108
    • (1937) Tôhoku Math. J. , vol.43 , pp. 104-108
    • Goldberg, M.1
  • 36
    • 0038758998 scopus 로고    scopus 로고
    • The tailless icosahedral membrane virus PRD1 localizes the proteins involved in genome packaging and injection at a unique vertex
    • Gowen B., Bamford J.K.H., Bamford D.H., Fuller S.D. The tailless icosahedral membrane virus PRD1 localizes the proteins involved in genome packaging and injection at a unique vertex. J. Virol. 77:2003;7863-7871
    • (2003) J. Virol. , vol.77 , pp. 7863-7871
    • Gowen, B.1    Bamford, J.K.H.2    Bamford, D.H.3    Fuller, S.D.4
  • 37
    • 0032745014 scopus 로고    scopus 로고
    • Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex
    • Grahn A.M., Caldentey J., Bamford J.K.H., Bamford D.H. Stable packaging of phage PRD1 DNA requires adsorption protein P2, which binds to the IncP plasmid-encoded conjugative transfer complex. J. Bacteriol. 181:1999;6689-6696
    • (1999) J. Bacteriol. , vol.181 , pp. 6689-6696
    • Grahn, A.M.1    Caldentey, J.2    Bamford, J.K.H.3    Bamford, D.H.4
  • 38
    • 0036887159 scopus 로고    scopus 로고
    • Sequential model of phage PRD1 DNA delivery: Active involvement of the viral membrane
    • Grahn A.M., Daugelavicius R., Bamford D.H. Sequential model of phage PRD1 DNA delivery. Active involvement of the viral membrane Mol. Microbiol. 46:2002;1199-1209
    • (2002) Mol. Microbiol. , vol.46 , pp. 1199-1209
    • Grahn, A.M.1    Daugelavicius, R.2    Bamford, D.H.3
  • 39
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer. An environment for comparative protein modeling Electrophoresis. 18:1997;2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 40
    • 0000885069 scopus 로고
    • Effects of the nonoccluded virus of Spodoptera frugiperda (Lepidoptera: Noctuidae) on the development of a parasitoid, Cotesia marginiventris (Hymenoptera: Braconidae)
    • Hamm J.J., Nordlund D.A., Marti O.G. Effects of the nonoccluded virus of Spodoptera frugiperda (Lepidoptera: Noctuidae) on the development of a parasitoid, Cotesia marginiventris (Hymenoptera: Braconidae). Environ. Entomol. 14:1985;258-261
    • (1985) Environ. Entomol. , vol.14 , pp. 258-261
    • Hamm, J.J.1    Nordlund, D.A.2    Marti, O.G.3
  • 42
    • 0033576564 scopus 로고    scopus 로고
    • Evolution: The long evolutionary reach of viruses
    • Hendrix R.W. Evolution. The long evolutionary reach of viruses Curr. Biol. 9:1999;R914-R917
    • (1999) Curr. Biol. , vol.9
    • Hendrix, R.W.1
  • 43
    • 0035167322 scopus 로고    scopus 로고
    • Common origin of four diverse families of large eukaryotic DNA viruses
    • Iyer L.M., Aravind L., Koonin E.V. Common origin of four diverse families of large eukaryotic DNA viruses. J. Virol. 75:2001;11720-11734
    • (2001) J. Virol. , vol.75 , pp. 11720-11734
    • Iyer, L.M.1    Aravind, L.2    Koonin, E.V.3
  • 44
    • 0024539057 scopus 로고
    • Structure of tumour necrosis factor
    • Jones E.Y., Stuart D.I., Walker N.P.C. Structure of tumour necrosis factor. Nature. 338:1989;225-228
    • (1989) Nature , vol.338 , pp. 225-228
    • Jones, E.Y.1    Stuart, D.I.2    Walker, N.P.C.3
  • 45
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet L., Agrain C., Broz P., Cornelis G.R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science. 302:2003;1757-1760
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 46
    • 0021712727 scopus 로고
    • Length determination in bacteriophage lambda tails
    • Katsura I., Hendrix R.W. Length determination in bacteriophage lambda tails. Cell. 39:1984;691-698
    • (1984) Cell , vol.39 , pp. 691-698
    • Katsura, I.1    Hendrix, R.W.2
  • 47
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley L.A., MacCallum R.M., Sternberg M.J.E. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol. 299:2000;499-520
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.E.3
  • 48
    • 0002608842 scopus 로고    scopus 로고
    • The procapsid-to-capsid transition in double-stranded DNA bacteriophages
    • W. Chiu, R.M. Burnett, & R.L. Garcea. New York: Oxford University Press
    • King J., Chiu W. The procapsid-to-capsid transition in double-stranded DNA bacteriophages. Chiu W., Burnett R.M., Garcea R.L. Structural Biology of Viruses. 1997;288-311 Oxford University Press, New York
    • (1997) Structural Biology of Viruses , pp. 288-311
    • King, J.1    Chiu, W.2
  • 49
    • 0023030811 scopus 로고
    • In vitro encapsidation of plasmid DNA into human adenovirus empty capsids
    • Kosturko L.D., Vanech M. In vitro encapsidation of plasmid DNA into human adenovirus empty capsids. Virus Res. 6:1986;123-132
    • (1986) Virus Res. , vol.6 , pp. 123-132
    • Kosturko, L.D.1    Vanech, M.2
  • 52
    • 0021920082 scopus 로고
    • Fish to bacterium gene transfer
    • Lewin R. Fish to bacterium gene transfer. Science. 277:1985;1020
    • (1985) Science , vol.277 , pp. 1020
    • Lewin, R.1
  • 53
    • 0034699383 scopus 로고    scopus 로고
    • Image reconstructions of helical assemblies of the HIV-1 CA protein
    • Li S., Hill C.P., Sundquist W.I., Finch J.T. Image reconstructions of helical assemblies of the HIV-1 CA protein. Nature. 407:2000;409-413
    • (2000) Nature , vol.407 , pp. 409-413
    • Li, S.1    Hill, C.P.2    Sundquist, W.I.3    Finch, J.T.4
  • 55
    • 0035789518 scopus 로고    scopus 로고
    • Gromacs 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E., Hess B., van der Spoel D. Gromacs 3.0. A package for molecular simulation and trajectory analysis J. Mol. Mod. 7:2001;306-317
    • (2001) J. Mol. Mod. , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 56
    • 0036183318 scopus 로고    scopus 로고
    • Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands
    • Liu Y., Xu L., Opalka N., Kappler J., Shu H.-B., Zhang G. Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands. Cell. 108:2002;383-394
    • (2002) Cell , vol.108 , pp. 383-394
    • Liu, Y.1    Xu, L.2    Opalka, N.3    Kappler, J.4    Shu, H.-B.5    Zhang, G.6
  • 57
    • 0025308438 scopus 로고
    • Mapping and sequence of the gene coding for protein p72, the major capsid protein of African swine fever virus
    • Lopez-Otin C., Freije J.M., Parra F., Mendez E., Viñuela E. Mapping and sequence of the gene coding for protein p72, the major capsid protein of African swine fever virus. Virology. 175:1990;477-484
    • (1990) Virology , vol.175 , pp. 477-484
    • Lopez-Otin, C.1    Freije, J.M.2    Parra, F.3    Mendez, E.4    Viñuela, E.5
  • 58
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., Bacon D.J. Raster3D. photorealistic molecular graphics Methods Enzymol. 277:1997;505-524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 61
    • 0028774531 scopus 로고
    • The three-dimensional structure of PNGase F, a glycosyl asparaginase from Flavobacterium meningosepticum
    • Norris G.E., Stillman T.J., Anderson B.F., Baker E.N. The three-dimensional structure of PNGase F, a glycosyl asparaginase from Flavobacterium meningosepticum. Structure. 2:1994;1049-1059
    • (1994) Structure , vol.2 , pp. 1049-1059
    • Norris, G.E.1    Stillman, T.J.2    Anderson, B.F.3    Baker, E.N.4
  • 62
    • 0016287852 scopus 로고
    • Characteristics of PRD1, a plasmid-dependent broad host range DNA bacteriophage
    • Olsen R.H., Siak J.-S., Gray R.H. Characteristics of PRD1, a plasmid-dependent broad host range DNA bacteriophage. J. Virol. 14:1974;689-699
    • (1974) J. Virol. , vol.14 , pp. 689-699
    • Olsen, R.H.1    Siak, J.-S.2    Gray, R.H.3
  • 63
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine α-hydroxylating monooxygenase
    • Prigge S.T., Kolhekar A.S., Eipper B.A., Mains R.E., Amzel L.M. Amidation of bioactive peptides. The structure of peptidylglycine α-hydroxylating monooxygenase Science. 278:1997;1300-1305
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 65
    • 0042887681 scopus 로고    scopus 로고
    • Comparative analysis of bacterial viruses Bam35, infecting a gram-positive host, and PRD1, infecting gram-negative hosts, demonstrates a viral lineage
    • Ravantti J.J., Gaidelyte A., Bamford D.H., Bamford J.K.H. Comparative analysis of bacterial viruses Bam35, infecting a gram-positive host, and PRD1, infecting gram-negative hosts, demonstrates a viral lineage. Virology. 313:2003;401-414
    • (2003) Virology , vol.313 , pp. 401-414
    • Ravantti, J.J.1    Gaidelyte, A.2    Bamford, D.H.3    Bamford, J.K.H.4
  • 68
    • 0031666742 scopus 로고    scopus 로고
    • The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F
    • Roelvink P.W., Lizonova A., Lee J.G.M., Li Y., Bergelson J.M., Finberg R.W., Brough D.E., Kovesdi I., Wickham T.J. The coxsackievirus-adenovirus receptor protein can function as a cellular attachment protein for adenovirus serotypes from subgroups A, C, D, E, and F. J. Virol. 72:1998;7909-7915
    • (1998) J. Virol. , vol.72 , pp. 7909-7915
    • Roelvink, P.W.1    Lizonova, A.2    Lee, J.G.M.3    Li, Y.4    Bergelson, J.M.5    Finberg, R.W.6    Brough, D.E.7    Kovesdi, I.8    Wickham, T.J.9
  • 70
    • 0033661024 scopus 로고    scopus 로고
    • Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon
    • Rux J.J., Burnett R.M. Type-specific epitope locations revealed by X-ray crystallographic study of adenovirus type 5 hexon. Mol. Ther. 1:2000;18-30
    • (2000) Mol. Ther. , vol.1 , pp. 18-30
    • Rux, J.J.1    Burnett, R.M.2
  • 71
    • 0042890357 scopus 로고    scopus 로고
    • Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods
    • Rux J.J., Kuser P.R., Burnett R.M. Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution X-ray crystallographic, molecular modeling, and sequence-based methods. J. Virol. 77:2003;9553-9566
    • (2003) J. Virol. , vol.77 , pp. 9553-9566
    • Rux, J.J.1    Kuser, P.R.2    Burnett, R.M.3
  • 73
    • 0035798386 scopus 로고    scopus 로고
    • A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly
    • Rydman P.S., Bamford J.K.H., Bamford D.H. A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly. J. Mol. Biol. 313:2001;785-795
    • (2001) J. Mol. Biol. , vol.313 , pp. 785-795
    • Rydman, P.S.1    Bamford, J.K.H.2    Bamford, D.H.3
  • 74
    • 0034797254 scopus 로고    scopus 로고
    • Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions
    • San Martín C., Burnett R.M., de Haas F., Heinkel R., Rutten T., Fuller S.D., Butcher S.J., Bamford D.H. Combined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions. Structure. 9:2001;917-930
    • (2001) Structure , vol.9 , pp. 917-930
    • San Martín, C.1    Burnett, R.M.2    De Haas, F.3    Heinkel, R.4    Rutten, T.5    Fuller, S.D.6    Butcher, S.J.7    Bamford, D.H.8
  • 76
    • 0027364732 scopus 로고
    • Identification of the gene encoding the major capsid protein of fish lymphocystis disease virus
    • Schnitzler P., Darai G. Identification of the gene encoding the major capsid protein of fish lymphocystis disease virus. J. Gen. Virol. 74:1993;2143-2150
    • (1993) J. Gen. Virol. , vol.74 , pp. 2143-2150
    • Schnitzler, P.1    Darai, G.2
  • 77
    • 0021152755 scopus 로고
    • Structural proteins and lipids in a virus, PBCV-1, which replicates in a Chlorella-like alga
    • Skrdla M.P., Burbank D.E., Xia Y., Meints R.H., Van Etten J.L. Structural proteins and lipids in a virus, PBCV-1, which replicates in a Chlorella-like alga. Virology. 135:1984;308-315
    • (1984) Virology , vol.135 , pp. 308-315
    • Skrdla, M.P.1    Burbank, D.E.2    Xia, Y.3    Meints, R.H.4    Van Etten, J.L.5
  • 79
    • 0026006259 scopus 로고
    • Image reconstruction reveals the complex molecular organization of adenovirus
    • Stewart P.L., Burnett R.M., Cyrklaff M., Fuller S.D. Image reconstruction reveals the complex molecular organization of adenovirus. Cell. 67:1991;145-154
    • (1991) Cell , vol.67 , pp. 145-154
    • Stewart, P.L.1    Burnett, R.M.2    Cyrklaff, M.3    Fuller, S.D.4
  • 81
    • 0038523777 scopus 로고    scopus 로고
    • The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane
    • a
    • Strömsten N.J., Bamford D.H., Bamford J.K.H. The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane. J. Virol. 77:2003;6314-6321. a
    • (2003) J. Virol. , vol.77 , pp. 6314-6321
    • Strömsten, N.J.1    Bamford, D.H.2    Bamford, J.K.H.3
  • 82
    • 0345687907 scopus 로고    scopus 로고
    • The Bacillus thuringiensis linear double-stranded DNA phage Bam35, which is highly similar to the Bacillus cereus linear plasmid pBClin15, has a prophage state
    • b
    • Strömsten N.J., Benson S.D., Burnett R.M., Bamford D.H., Bamford J.K.H. The Bacillus thuringiensis linear double-stranded DNA phage Bam35, which is highly similar to the Bacillus cereus linear plasmid pBClin15, has a prophage state. J. Bacteriol. 185:2003;6985-6989. b
    • (2003) J. Bacteriol. , vol.185 , pp. 6985-6989
    • Strömsten, N.J.1    Benson, S.D.2    Burnett, R.M.3    Bamford, D.H.4    Bamford, J.K.H.5
  • 83
    • 0032582665 scopus 로고    scopus 로고
    • Assembly of a tailed bacterial virus and its genome release studied in three dimensions
    • Tao Y., Olson N.H., Xu W., Anderson D.L., Rossmann M.G., Baker T.S. Assembly of a tailed bacterial virus and its genome release studied in three dimensions. Cell. 95:1998;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
  • 84
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface. Flexible strategies for multiple sequence alignment aided by quality analysis tools Nucleic Acids Res. 25:1997;4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 85
    • 0031881860 scopus 로고    scopus 로고
    • Is the major capsid protein of iridoviruses a suitable target for the study of viral evolution?
    • Tidona C.A., Schnitzler P., Kehm R., Darai G. Is the major capsid protein of iridoviruses a suitable target for the study of viral evolution? Virus Genes. 16:1998;59-66
    • (1998) Virus Genes , vol.16 , pp. 59-66
    • Tidona, C.A.1    Schnitzler, P.2    Kehm, R.3    Darai, G.4
  • 88
    • 0022348579 scopus 로고
    • Molecular composition of the adenovirus type 2 virion
    • van Oostrum J., Burnett R.M. Molecular composition of the adenovirus type 2 virion. J. Virol. 56:1985;439-448
    • (1985) J. Virol. , vol.56 , pp. 439-448
    • Van Oostrum, J.1    Burnett, R.M.2
  • 89
    • 0033613385 scopus 로고    scopus 로고
    • A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein
    • van Raaij M.J., Mitraki A., Lavigne G., Cusack S. A triple β-spiral in the adenovirus fibre shaft reveals a new structural motif for a fibrous protein. Nature. 401:1999;935-938
    • (1999) Nature , vol.401 , pp. 935-938
    • Van Raaij, M.J.1    Mitraki, A.2    Lavigne, G.3    Cusack, S.4
  • 90
    • 0003412657 scopus 로고    scopus 로고
    • M.H.V. van Regenmortel, C.M. Fauquet, D. Bishop, E. Carsten, M. Estes, S. Lemon, J. Maniloff, M.A. Mayo, D. McGeoch, C. Pringle, & R. Wickner. San Diego: Academic Press
    • van Regenmortel M.H.V., Fauquet C.M., Bishop D., Carsten E., Estes M., Lemon S., Maniloff J., Mayo M.A., McGeoch D., Pringle C., Wickner R. Seventh Report of the International Committee on Taxonomy of Viruses. 2000;Academic Press, San Diego
    • (2000) Seventh Report of the International Committee on Taxonomy of Viruses
  • 91
    • 0042925630 scopus 로고    scopus 로고
    • PGIL01, a linear tectiviral plasmid prophage originating from Bacillus thuringiensis serovar israelensis
    • Verheust C., Jensen G., Mahillon J. pGIL01, a linear tectiviral plasmid prophage originating from Bacillus thuringiensis serovar israelensis. Microbiol. 149:2003;2083-2092
    • (2003) Microbiol. , vol.149 , pp. 2083-2092
    • Verheust, C.1    Jensen, G.2    Mahillon, J.3
  • 92
    • 0030021332 scopus 로고    scopus 로고
    • The iridoviruses
    • Williams T. The iridoviruses. Adv. Virus Res. 46:1996;345-412
    • (1996) Adv. Virus Res. , vol.46 , pp. 345-412
    • Williams, T.1
  • 93
    • 0014546234 scopus 로고
    • An electron microscope study of the structure of Sericesthis iridescent virus
    • Wrigley N.G. An electron microscope study of the structure of Sericesthis iridescent virus. J. Gen. Virol. 5:1969;123-134
    • (1969) J. Gen. Virol. , vol.5 , pp. 123-134
    • Wrigley, N.G.1
  • 94
    • 0037334514 scopus 로고    scopus 로고
    • The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions
    • Xu L., Benson S.D., Butcher S.J., Bamford D.H., Burnett R.M. The receptor binding protein P2 of PRD1, a virus targeting antibiotic-resistant bacteria, has a novel fold suggesting multiple functions. Structure. 11:2003;309-322
    • (2003) Structure , vol.11 , pp. 309-322
    • Xu, L.1    Benson, S.D.2    Butcher, S.J.3    Bamford, D.H.4    Burnett, R.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.