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Volumn 466-467, Issue , 2014, Pages 15-26

Revisiting the genome packaging in viruses with lessons from the "Giants"

Author keywords

Classification; Encapsidation; Energy dependent; Energy independent; Genome packaging; NCLDV; Packaging ATPase

Indexed keywords

CARRIER PROTEIN; PROTEIN FTSK; PROTEIN HERA; UNCLASSIFIED DRUG; VIRUS PROTEIN; DNA VIRUS; VIRUS DNA;

EID: 84908258828     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.06.022     Document Type: Review
Times cited : (45)

References (153)
  • 1
    • 15244343074 scopus 로고    scopus 로고
    • Structure of the connector of bacteriophage T7 at 8Å resolution: structural homologies of a basic component of a DNA translocating machinery
    • Agirrezabala X., Martín-Benito J., Valle M., González J.M., Valencia A., Valpuesta J.M., Carrascosa J.L. Structure of the connector of bacteriophage T7 at 8Å resolution: structural homologies of a basic component of a DNA translocating machinery. J. Mol. Biol. 2005, 347(5):895-902.
    • (2005) J. Mol. Biol. , vol.347 , Issue.5 , pp. 895-902
    • Agirrezabala, X.1    Martín-Benito, J.2    Valle, M.3    González, J.M.4    Valencia, A.5    Valpuesta, J.M.6    Carrascosa, J.L.7
  • 2
    • 69949139694 scopus 로고    scopus 로고
    • The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor
    • Al-Zahrani A.S., Kondabagil K., Gao S., Kelly N., Ghosh-Kumar M., Rao V.B. The small terminase, gp16, of bacteriophage T4 is a regulator of the DNA packaging motor. J. Biol. Chem. 2009, 284(36):24490-24500.
    • (2009) J. Biol. Chem. , vol.284 , Issue.36 , pp. 24490-24500
    • Al-Zahrani, A.S.1    Kondabagil, K.2    Gao, S.3    Kelly, N.4    Ghosh-Kumar, M.5    Rao, V.B.6
  • 3
    • 0034636984 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the ψ-RNA packaging signal. Implications for genome recognition
    • Amarasinghe G.K., De Guzman R.N., Turner R.B., Chancellor K.J., Wu Z.R., Summers M.F. NMR structure of the HIV-1 nucleocapsid protein bound to stem-loop SL2 of the ψ-RNA packaging signal. Implications for genome recognition. J. Mol. Biol. 2000, 301(2):491-511.
    • (2000) J. Mol. Biol. , vol.301 , Issue.2 , pp. 491-511
    • Amarasinghe, G.K.1    De Guzman, R.N.2    Turner, R.B.3    Chancellor, K.J.4    Wu, Z.R.5    Summers, M.F.6
  • 4
    • 0037169328 scopus 로고    scopus 로고
    • FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases
    • Aussel L., Barre F.-X., Aroyo M., Stasiak A., Stasiak A.Z., Sherratt D. FtsK is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell 2002, 108(2):195-205.
    • (2002) Cell , vol.108 , Issue.2 , pp. 195-205
    • Aussel, L.1    Barre, F.-X.2    Aroyo, M.3    Stasiak, A.4    Stasiak, A.Z.5    Sherratt, D.6
  • 5
    • 0038751848 scopus 로고    scopus 로고
    • Isolation and characterization of T4 bacteriophage gp17 terminase, a large subunit multimer with enhanced ATPase activity
    • Baumann R.G., Black L.W. Isolation and characterization of T4 bacteriophage gp17 terminase, a large subunit multimer with enhanced ATPase activity. J. Biol. Chem. 2003, 278(7):4618-4627.
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 4618-4627
    • Baumann, R.G.1    Black, L.W.2
  • 6
    • 0037301362 scopus 로고    scopus 로고
    • Rotavirus nonstructural protein NSP5 interact with major core protein VP2
    • Berosis M., Sapin C., Erk I., Poncet D., Cohen J. Rotavirus nonstructural protein NSP5 interact with major core protein VP2. J. Virol. 2013, 77(3):1757-1763.
    • (2013) J. Virol. , vol.77 , Issue.3 , pp. 1757-1763
    • Berosis, M.1    Sapin, C.2    Erk, I.3    Poncet, D.4    Cohen, J.5
  • 7
    • 0029556888 scopus 로고
    • DNA packaging and cutting by phage terminases: control in phage T4 by a synaptic mechanism
    • Black L.W. DNA packaging and cutting by phage terminases: control in phage T4 by a synaptic mechanism. Bioessays 1995, 17(12):1025-1030.
    • (1995) Bioessays , vol.17 , Issue.12 , pp. 1025-1030
    • Black, L.W.1
  • 9
    • 0041691085 scopus 로고    scopus 로고
    • Determination of the protein composition of the occlusion-derived virus of Autographa californica nucleopolyhedrovirus
    • Braunagel S.C., Russell W.K., Rosas-Acosta G., Russell D.H., Summers M.D. Determination of the protein composition of the occlusion-derived virus of Autographa californica nucleopolyhedrovirus. Proc. Natl. Acad. Sci. 2003, 100(17):9797-9802.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , Issue.17 , pp. 9797-9802
    • Braunagel, S.C.1    Russell, W.K.2    Rosas-Acosta, G.3    Russell, D.H.4    Summers, M.D.5
  • 11
    • 1642529011 scopus 로고    scopus 로고
    • Genetic details, optimization and phage life histories
    • Bull J.J., Pfennig D.W., Wang I.-N. Genetic details, optimization and phage life histories. Trends Ecol. Evol. 2004, 19(2):76-82.
    • (2004) Trends Ecol. Evol. , vol.19 , Issue.2 , pp. 76-82
    • Bull, J.J.1    Pfennig, D.W.2    Wang, I.-N.3
  • 12
    • 48749086251 scopus 로고    scopus 로고
    • Comparative genomics and evolutionary trajectories of viral ATP dependent DNA-packaging systems
    • Burroughs A., Iyer L., Aravind L. Comparative genomics and evolutionary trajectories of viral ATP dependent DNA-packaging systems. Genome Dyn. 2007, 3:48-65.
    • (2007) Genome Dyn. , vol.3 , pp. 48-65
    • Burroughs, A.1    Iyer, L.2    Aravind, L.3
  • 13
    • 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. 1995, 14(24):6078-6086.
    • (1995) EMBO J. , vol.14 , Issue.24 , pp. 6078-6086
    • Butcher, S.J.1    Bamford, D.H.2    Fuller, S.D.3
  • 14
    • 0037931517 scopus 로고    scopus 로고
    • Bacillus subtilis bacteriophage SPP1 DNA packaging motor requires terminase and portal proteins
    • Camacho A.G., Gual A., Lurz R., Tavares P., Alonso J.C. Bacillus subtilis bacteriophage SPP1 DNA packaging motor requires terminase and portal proteins. J. Biol. Chem. 2003, 278(26):23251-23259.
    • (2003) J. Biol. Chem. , vol.278 , Issue.26 , pp. 23251-23259
    • Camacho, A.G.1    Gual, A.2    Lurz, R.3    Tavares, P.4    Alonso, J.C.5
  • 15
    • 59649084913 scopus 로고    scopus 로고
    • Visualization of a missing link in retrovirus capsid assembly
    • Cardone G., Purdy J.G., Cheng N., Craven R.C., Steven A.C. Visualization of a missing link in retrovirus capsid assembly. Nature 2009, 457(7230):694-698.
    • (2009) Nature , vol.457 , Issue.7230 , pp. 694-698
    • Cardone, G.1    Purdy, J.G.2    Cheng, N.3    Craven, R.C.4    Steven, A.C.5
  • 16
    • 33746799027 scopus 로고    scopus 로고
    • Viral genome packaging machines, viral genome packaging machines: genetics
    • Springer, US
    • Catalano C. Viral genome packaging machines, viral genome packaging machines: genetics. Structure, and Mechanism 2005, 1-4. Springer, US.
    • (2005) Structure, and Mechanism , pp. 1-4
    • Catalano, C.1
  • 17
    • 84899845883 scopus 로고    scopus 로고
    • Genome segregation and packaging machinery in acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus
    • Chelikani V., Ranjan T., Zade A., Shukla A., Kondabagil K. Genome segregation and packaging machinery in acanthamoeba polyphaga mimivirus is reminiscent of bacterial apparatus. J. Virol. 2014, 88(11):6069-6075.
    • (2014) J. Virol. , vol.88 , Issue.11 , pp. 6069-6075
    • Chelikani, V.1    Ranjan, T.2    Zade, A.3    Shukla, A.4    Kondabagil, K.5
  • 19
    • 0141570689 scopus 로고    scopus 로고
    • Packaging of brome mosaic virus RNA3 is mediated through a bipartite signal
    • Choi Y.G., Rao A.L.N. Packaging of brome mosaic virus RNA3 is mediated through a bipartite signal. J. Virol. 2003, 77(18):9750-9757.
    • (2003) J. Virol. , vol.77 , Issue.18 , pp. 9750-9757
    • Choi, Y.G.1    Rao, A.L.N.2
  • 21
    • 84866161112 scopus 로고    scopus 로고
    • Identification and characterization of a DNA binding domain on the adenovirus IVa2 protein
    • Christensen J.B., Ewing S.G., Imperiale M.J. Identification and characterization of a DNA binding domain on the adenovirus IVa2 protein. Virology 2012, 433(1):124-130.
    • (2012) Virology , vol.433 , Issue.1 , pp. 124-130
    • Christensen, J.B.1    Ewing, S.G.2    Imperiale, M.J.3
  • 22
    • 80051718223 scopus 로고    scopus 로고
    • Molecular determinants that regulate plasma membrane association of HIV-1 Gag
    • Chukkapalli V., Ono A. Molecular determinants that regulate plasma membrane association of HIV-1 Gag. J. Mol. Biol. 2011, 410(4):512-524.
    • (2011) J. Mol. Biol. , vol.410 , Issue.4 , pp. 512-524
    • Chukkapalli, V.1    Ono, A.2
  • 23
    • 0035838978 scopus 로고    scopus 로고
    • Bacteriophage λ DNA packaging: DNA site requirements for termination and processivity
    • Cue D., Feiss M. Bacteriophage λ DNA packaging: DNA site requirements for termination and processivity. J. Mol. Biol. 2001, 311(2):233-240.
    • (2001) J. Mol. Biol. , vol.311 , Issue.2 , pp. 233-240
    • Cue, D.1    Feiss, M.2
  • 24
    • 34548179538 scopus 로고    scopus 로고
    • Proteomics analysis of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, HA44 and HA100
    • Deng F., Wang R., Fang M., Jiang Y., Xu X., Wang H., Chen X., Arif B.M., Guo L., Wang H. Proteomics analysis of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus identified two new occlusion-derived virus-associated proteins, HA44 and HA100. J. Virol. 2007, 81(17):9377-9385.
    • (2007) J. Virol. , vol.81 , Issue.17 , pp. 9377-9385
    • Deng, F.1    Wang, R.2    Fang, M.3    Jiang, Y.4    Xu, X.5    Wang, H.6    Chen, X.7    Arif, B.M.8    Guo, L.9    Wang, H.10
  • 25
    • 79551683191 scopus 로고    scopus 로고
    • Structure of the HIV-1 full-length capsid protein in a conformationally trapped unassembled state induced by small-molecule binding
    • Du S., Betts L., Yang R., Shi H., Concel J., Ahn J., Aiken C., Zhang P., Yeh J.I. Structure of the HIV-1 full-length capsid protein in a conformationally trapped unassembled state induced by small-molecule binding. J. Mol. Biol. 2011, 406(3):371-386.
    • (2011) J. Mol. Biol. , vol.406 , Issue.3 , pp. 371-386
    • Du, S.1    Betts, L.2    Yang, R.3    Shi, H.4    Concel, J.5    Ahn, J.6    Aiken, C.7    Zhang, P.8    Yeh, J.I.9
  • 26
    • 36048969242 scopus 로고    scopus 로고
    • Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins
    • Ewing S.G., Byrd S.A., Christensen J.B., Tyler R.E., Imperiale M.J. Ternary complex formation on the adenovirus packaging sequence by the IVa2 and L4 22-kilodalton proteins. J. Virol. 2007, 81(22):12450-12457.
    • (2007) J. Virol. , vol.81 , Issue.22 , pp. 12450-12457
    • Ewing, S.G.1    Byrd, S.A.2    Christensen, J.B.3    Tyler, R.E.4    Imperiale, M.J.5
  • 28
    • 0020501606 scopus 로고
    • Structure of the bacteriophage lambda cohesive end site: location of the sites of terminase binding (cosB) and nicking (cosN)
    • Feiss M., Widner W., Miller G., Johnson G., Christiansen S. Structure of the bacteriophage lambda cohesive end site: location of the sites of terminase binding (cosB) and nicking (cosN). Gene 1983, 24(2):207-218.
    • (1983) Gene , vol.24 , Issue.2 , pp. 207-218
    • Feiss, M.1    Widner, W.2    Miller, G.3    Johnson, G.4    Christiansen, S.5
  • 29
    • 79953806385 scopus 로고    scopus 로고
    • A virophage at the origin of large DNA transposons
    • Fischer M.G., Suttle C.A. A virophage at the origin of large DNA transposons. Science 2011, 332(6026):231-234.
    • (2011) Science , vol.332 , Issue.6026 , pp. 231-234
    • Fischer, M.G.1    Suttle, C.A.2
  • 30
    • 36749028241 scopus 로고    scopus 로고
    • Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability
    • Fuller D.N., Raymer D.M., Kottadiel V.I., Rao V.B., Smith D.E. Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability. Proc. Natl. Acad. Sci. 2007, 104(43):16868-16873.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , Issue.43 , pp. 16868-16873
    • Fuller, D.N.1    Raymer, D.M.2    Kottadiel, V.I.3    Rao, V.B.4    Smith, D.E.5
  • 31
    • 35148815738 scopus 로고    scopus 로고
    • Measurements of single DNA molecule packaging dynamics in bacteriophage λ reveal high forces, high motor processivity, and capsid transformations
    • Fuller D.N., Raymer D.M., Rickgauer J.P., Robertson R.M., Catalano C.E., Anderson D.L., Grimes S., Smith D.E. Measurements of single DNA molecule packaging dynamics in bacteriophage λ reveal high forces, high motor processivity, and capsid transformations. J. Mol. Biol. 2007, 373(5):1113-1122.
    • (2007) J. Mol. Biol. , vol.373 , Issue.5 , pp. 1113-1122
    • Fuller, D.N.1    Raymer, D.M.2    Rickgauer, J.P.3    Robertson, R.M.4    Catalano, C.E.5    Anderson, D.L.6    Grimes, S.7    Smith, D.E.8
  • 33
    • 0026657924 scopus 로고
    • Protein P4 of the bacteriophage ϕ 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity
    • Gottlieb P., Strassman J., Mindich L. Protein P4 of the bacteriophage ϕ 6 procapsid has a nucleoside triphosphate-binding site with associated nucleoside triphosphate phosphohydrolase activity. J. Virol. 1992, 66(10):6220-6222.
    • (1992) J. Virol. , vol.66 , Issue.10 , pp. 6220-6222
    • Gottlieb, P.1    Strassman, J.2    Mindich, L.3
  • 34
    • 0026560654 scopus 로고
    • In vitro packaging and replication of individual genomic segments of bacteriophage ϕ 6 RNA
    • Gottlieb P., Strassman J., Qiao X., Frilander M., Frucht A., Mindich L. in vitro packaging and replication of individual genomic segments of bacteriophage ϕ 6 RNA. J. Virol. 1992, 66(5):2611-2616.
    • (1992) J. Virol. , vol.66 , Issue.5 , pp. 2611-2616
    • Gottlieb, P.1    Strassman, J.2    Qiao, X.3    Frilander, M.4    Frucht, A.5    Mindich, L.6
  • 35
    • 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., Strassman J., Qiao X.Y., Frucht A., Mindich L. 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. 1990, 172(10):5774-5782.
    • (1990) J. Bacteriol. , vol.172 , Issue.10 , pp. 5774-5782
    • Gottlieb, P.1    Strassman, J.2    Qiao, X.Y.3    Frucht, A.4    Mindich, L.5
  • 36
    • 0025265591 scopus 로고
    • Adenovirus type 5 packaging domain is composed of a repeated element that is functionally redundant
    • Gräble M., Hearing P. Adenovirus type 5 packaging domain is composed of a repeated element that is functionally redundant. J. Virol. 1990, 64(5):2047-2056.
    • (1990) J. Virol. , vol.64 , Issue.5 , pp. 2047-2056
    • Gräble, M.1    Hearing, P.2
  • 37
    • 0026584172 scopus 로고
    • Cis and trans requirements for the selective packaging of adenovirus type 5 DNA
    • Gräble M., Hearing P. cis and trans requirements for the selective packaging of adenovirus type 5 DNA. J. Virol. 1992, 66(2):723-731.
    • (1992) J. Virol. , vol.66 , Issue.2 , pp. 723-731
    • Gräble, M.1    Hearing, P.2
  • 38
    • 0036887159 scopus 로고    scopus 로고
    • Sequential model of phage PRD1 DNA delivery: active involvement of the viral membrane
    • Grahn A.M., Daugelavičius R., Bamford D.H. Sequential model of phage PRD1 DNA delivery: active involvement of the viral membrane. Mol. Microbiol. 2002, 46(5):1199-1209.
    • (2002) Mol. Microbiol. , vol.46 , Issue.5 , pp. 1199-1209
    • Grahn, A.M.1    Daugelavičius, R.2    Bamford, D.H.3
  • 39
    • 0025028872 scopus 로고
    • RNA dependence of the bacteriophage ϕ29 DNA packaging ATPase
    • Grimes S., Anderson D. RNA dependence of the bacteriophage ϕ29 DNA packaging ATPase. J. Mol. Biol. 1990, 215(4):559-566.
    • (1990) J. Mol. Biol. , vol.215 , Issue.4 , pp. 559-566
    • Grimes, S.1    Anderson, D.2
  • 40
    • 0036052845 scopus 로고    scopus 로고
    • Bacteriophage ϕ29 DNA packaging
    • Academic Press, California, USA, (Volume)
    • Grimes S., Jardine P.J., Anderson D. Bacteriophage ϕ29 DNA packaging, Advances in Virus Research 2002, 58:255-294. Academic Press, California, USA, (Volume). ed.
    • (2002) Advances in Virus Research , vol.58 , pp. 255-294
    • Grimes, S.1    Jardine, P.J.2    Anderson, D.3
  • 41
    • 34248333990 scopus 로고
    • Introduction: principles, perspectives and potential applications in viral assembly
    • Guo P. Introduction: principles, perspectives and potential applications in viral assembly. Semin. Virol. 1994, 5:1-3.
    • (1994) Semin. Virol. , vol.5 , pp. 1-3
    • Guo, P.1
  • 42
    • 34248340401 scopus 로고    scopus 로고
    • Viral nanomotors for packaging of dsDNA and dsRNA
    • Guo P., Lee T.J. Viral nanomotors for packaging of dsDNA and dsRNA. Mol. Microbiol. 2007, 64(4):886-903.
    • (2007) Mol. Microbiol. , vol.64 , Issue.4 , pp. 886-903
    • Guo, P.1    Lee, T.J.2
  • 43
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage ϕ29
    • Guo P., Peterson C., Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage ϕ29. J. Mol. Biol. 1987, 197(2):229-236.
    • (1987) J. Mol. Biol. , vol.197 , Issue.2 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 44
    • 0023225629 scopus 로고
    • A small viral RNA is required for in vitro packaging of bacteriophage ϕ 29 DNA
    • Guo P.X., Erickson S., Anderson D. A small viral RNA is required for in vitro packaging of bacteriophage ϕ 29 DNA. Science 1987, 236(4802):690-694.
    • (1987) Science , vol.236 , Issue.4802 , pp. 690-694
    • Guo, P.X.1    Erickson, S.2    Anderson, D.3
  • 45
    • 0017844502 scopus 로고
    • Identification of the protein firmly bound to the ends of bacteriophage ϕ29 DNA
    • Harding N.E., Ito J., David G.S. Identification of the protein firmly bound to the ends of bacteriophage ϕ29 DNA. Virology 1978, 84(2):279-292.
    • (1978) Virology , vol.84 , Issue.2 , pp. 279-292
    • Harding, N.E.1    Ito, J.2    David, G.S.3
  • 46
    • 84861350662 scopus 로고    scopus 로고
    • Portal-large terminase interactions of the bacteriophage T4 DNA packaging machine implicate a molecular lever mechanism for coupling ATPase to DNA translocation
    • Hegde S., Padilla-Sanchez V., Draper B., Rao V.B. Portal-large terminase interactions of the bacteriophage T4 DNA packaging machine implicate a molecular lever mechanism for coupling ATPase to DNA translocation. J. Virol. 2012, 86(8):4046-4057.
    • (2012) J. Virol. , vol.86 , Issue.8 , pp. 4046-4057
    • Hegde, S.1    Padilla-Sanchez, V.2    Draper, B.3    Rao, V.B.4
  • 47
    • 0023042015 scopus 로고
    • Morphogenesis of f1 filamentous bacteriophage: increased expression of gene I inhibits bacterial growth
    • Horabin J.I., Webster R.E. Morphogenesis of f1 filamentous bacteriophage: increased expression of gene I inhibits bacterial growth. J. Mol. Biol. 1986, 188(3):403-413.
    • (1986) J. Mol. Biol. , vol.188 , Issue.3 , pp. 403-413
    • Horabin, J.I.1    Webster, R.E.2
  • 49
    • 33645076499 scopus 로고    scopus 로고
    • Evolutionary genomics of nucleo-cytoplasmic large DNA viruses
    • Iyer L.M., Balaji S., Koonin E.V., Aravind L. Evolutionary genomics of nucleo-cytoplasmic large DNA viruses. Virus Res. 2006, 117(1):156-184.
    • (2006) Virus Res. , vol.117 , Issue.1 , pp. 156-184
    • Iyer, L.M.1    Balaji, S.2    Koonin, E.V.3    Aravind, L.4
  • 50
    • 5144223072 scopus 로고    scopus 로고
    • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging
    • Iyer L.M., Makarova K.S., Koonin E.V., Aravind L. Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging. Nucleic Acids Res. 2004, 32(17):5260-5279.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.17 , pp. 5260-5279
    • Iyer, L.M.1    Makarova, K.S.2    Koonin, E.V.3    Aravind, L.4
  • 51
    • 0032484035 scopus 로고    scopus 로고
    • Capsid expansion follows the initiation of DNA packaging in bacteriophage T4
    • Jardine P.J., Coombs D.H. Capsid expansion follows the initiation of DNA packaging in bacteriophage T4. J. Mol. Biol. 1998, 284(3):661-672.
    • (1998) J. Mol. Biol. , vol.284 , Issue.3 , pp. 661-672
    • Jardine, P.J.1    Coombs, D.H.2
  • 52
    • 0037118101 scopus 로고    scopus 로고
    • Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold
    • Jayaram H., Taraporewala Z., Patton J.T., Prasad B.V.V. Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold. Nature 2002, 417(6886):311-315.
    • (2002) Nature , vol.417 , Issue.6886 , pp. 311-315
    • Jayaram, H.1    Taraporewala, Z.2    Patton, J.T.3    Prasad, B.V.V.4
  • 53
    • 0029740399 scopus 로고    scopus 로고
    • Journey to the core of HIV.
    • Jones I., Stuart D. Journey to the core of HIV. Nat. Struct. Mol. Biol. 1996, 3(10):818-820.
    • (1996) Nat. Struct. Mol. Biol. , vol.3 , Issue.10 , pp. 818-820
    • Jones, I.1    Stuart, D.2
  • 54
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • Jouvenet N., Bieniasz P.D., Simon S.M. Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 2008, 454(7201):236-240.
    • (2008) Nature , vol.454 , Issue.7201 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 55
    • 73149122533 scopus 로고    scopus 로고
    • Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles
    • Jouvenet N., Simon S.M., Bieniasz P.D. Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles. Proc. Natl. Acad. Sci. 2009, 106(45):19114-19119.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , Issue.45 , pp. 19114-19119
    • Jouvenet, N.1    Simon, S.M.2    Bieniasz, P.D.3
  • 56
    • 0029060842 scopus 로고
    • RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage ϕ6
    • Juuti J.T., Bamford D.H. RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage ϕ6. J. Mol. Biol. 1995, 249(3):545-554.
    • (1995) J. Mol. Biol. , vol.249 , Issue.3 , pp. 545-554
    • Juuti, J.T.1    Bamford, D.H.2
  • 57
    • 0031567131 scopus 로고    scopus 로고
    • Protein P7 of phage ϕ6 RNA polymerase complex, acquiring of RNA packaging activity by in vitro assembly of the purified protein onto deficient particles
    • Juuti J.T., Bamford D.H. Protein P7 of phage ϕ6 RNA polymerase complex, acquiring of RNA packaging activity by in vitro assembly of the purified protein onto deficient particles. J. Mol. Biol. 1997, 266(5):891-900.
    • (1997) J. Mol. Biol. , vol.266 , Issue.5 , pp. 891-900
    • Juuti, J.T.1    Bamford, D.H.2
  • 58
    • 0032486109 scopus 로고    scopus 로고
    • Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage ϕ6
    • Juuti J.T., Bamford D.H., Tuma R., Thomas G.J. Structure and NTPase activity of the RNA-translocating protein (P4) of bacteriophage ϕ6. J. Mol. Biol. 1998, 279(2):347-359.
    • (1998) J. Mol. Biol. , vol.279 , Issue.2 , pp. 347-359
    • Juuti, J.T.1    Bamford, D.H.2    Tuma, R.3    Thomas, G.J.4
  • 59
    • 33745293696 scopus 로고    scopus 로고
    • Hexameric molecular motors: P4 packaging ATPase unravels the mechanism
    • Kainov D.E., Tuma R., Mancini E.J. Hexameric molecular motors: P4 packaging ATPase unravels the mechanism. Cell. Mol. Life Sci. 2006, 63(10):1095-1105.
    • (2006) Cell. Mol. Life Sci. , vol.63 , Issue.10 , pp. 1095-1105
    • Kainov, D.E.1    Tuma, R.2    Mancini, E.J.3
  • 61
    • 8844274078 scopus 로고    scopus 로고
    • Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage ϕ29
    • Kamtekar S., Berman A.J., Wang J., Lázaro J.M., de Vega M., Blanco L., Salas M., Steitz T.A. Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage ϕ29. Mol. Cell 2004, 16(4):609-618.
    • (2004) Mol. Cell , vol.16 , Issue.4 , pp. 609-618
    • Kamtekar, S.1    Berman, A.J.2    Wang, J.3    Lázaro, J.M.4    de Vega, M.5    Blanco, L.6    Salas, M.7    Steitz, T.A.8
  • 62
    • 33947382214 scopus 로고    scopus 로고
    • Efficient DNA packaging of bacteriophage PRD1 requires the unique vertex protein P6
    • Karhu N.J., Ziedaite G., Bamford D.H., Bamford J.K.H. Efficient DNA packaging of bacteriophage PRD1 requires the unique vertex protein P6. J. Virol. 2007, 81(6):2970-2979.
    • (2007) J. Virol. , vol.81 , Issue.6 , pp. 2970-2979
    • Karhu, N.J.1    Ziedaite, G.2    Bamford, D.H.3    Bamford, J.K.H.4
  • 63
    • 33749561425 scopus 로고    scopus 로고
    • The DNA translocating ATPase of bacteriophage T4 packaging motor
    • Kondabagil K.R., Zhang Z., Rao V.B. The DNA translocating ATPase of bacteriophage T4 packaging motor. J. Mol. Biol. 2006, 363(4):786-799.
    • (2006) J. Mol. Biol. , vol.363 , Issue.4 , pp. 786-799
    • Kondabagil, K.R.1    Zhang, Z.2    Rao, V.B.3
  • 64
    • 0029013585 scopus 로고
    • The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity
    • Kräusslich H.G., Fäcke M., Heuser A.M., Konvalinka J., Zentgraf H. The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivity. J. Virol. 1995, 69(6):3407-3419.
    • (1995) J. Virol. , vol.69 , Issue.6 , pp. 3407-3419
    • Kräusslich, H.G.1    Fäcke, M.2    Heuser, A.M.3    Konvalinka, J.4    Zentgraf, H.5
  • 65
    • 79251506313 scopus 로고    scopus 로고
    • Analysis of the initiating events in HIV-1 particle assembly and genome packaging
    • Kutluay S.B., Bieniasz P.D. Analysis of the initiating events in HIV-1 particle assembly and genome packaging. PLoS Pathog. 2010, 6(11):e1001200.
    • (2010) PLoS Pathog. , vol.6 , Issue.11 , pp. e1001200
    • Kutluay, S.B.1    Bieniasz, P.D.2
  • 69
    • 67749104678 scopus 로고    scopus 로고
    • Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: evidence that NBs are sites of viral transcription and replication
    • Lahaye X., Vidy A., Pomier C., Obiang L., Harper F., Gaudin Y., Blondel D. Functional characterization of Negri bodies (NBs) in rabies virus-infected cells: evidence that NBs are sites of viral transcription and replication. J. Virol. 2009, 83(16):7948-7958.
    • (2009) J. Virol. , vol.83 , Issue.16 , pp. 7948-7958
    • Lahaye, X.1    Vidy, A.2    Pomier, C.3    Obiang, L.4    Harper, F.5    Gaudin, Y.6    Blondel, D.7
  • 71
    • 0016139684 scopus 로고
    • The bromoviruses
    • Lane L.C. The bromoviruses. Adv. Virus Res. 1974, 19:151-220.
    • (1974) Adv. Virus Res. , vol.19 , pp. 151-220
    • Lane, L.C.1
  • 73
    • 0034711268 scopus 로고    scopus 로고
    • Biochemical characterization of an ATPase activity associated with the large packaging subunit gp17 from bacteriophage T4
    • Leffers G., Rao V.B. Biochemical characterization of an ATPase activity associated with the large packaging subunit gp17 from bacteriophage T4. J. Biol. Chem. 2000, 275(47):37127-37136.
    • (2000) J. Biol. Chem. , vol.275 , Issue.47 , pp. 37127-37136
    • Leffers, G.1    Rao, V.B.2
  • 74
    • 0032030444 scopus 로고    scopus 로고
    • DNA requirementsin vivofor phage T4 packaging
    • Lin H., Black L.W. DNA requirementsin vivofor phage T4 packaging. Virology 1998, 242(1):118-127.
    • (1998) Virology , vol.242 , Issue.1 , pp. 118-127
    • Lin, H.1    Black, L.W.2
  • 75
    • 44949202636 scopus 로고    scopus 로고
    • Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites of viral replication and assembly
    • Lin Y.C.J., Li J., Irwin C.R., Jenkins H., DeLange L., Evans D.H. Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites of viral replication and assembly. J. Virol. 2008, 82(12):5922-5932.
    • (2008) J. Virol. , vol.82 , Issue.12 , pp. 5922-5932
    • Lin, Y.C.J.1    Li, J.2    Irwin, C.R.3    Jenkins, H.4    DeLange, L.5    Evans, D.H.6
  • 76
    • 80051766524 scopus 로고    scopus 로고
    • Structural determinants and mechanism of HIV-1 genome packaging
    • Lu K., Heng X., Summers M.F. Structural determinants and mechanism of HIV-1 genome packaging. J. Mol. Biol. 2011, 410(4):609-633.
    • (2011) J. Mol. Biol. , vol.410 , Issue.4 , pp. 609-633
    • Lu, K.1    Heng, X.2    Summers, M.F.3
  • 77
    • 1542268890 scopus 로고    scopus 로고
    • RNA-dependent RNA polymerases of dsRNA bacteriophages
    • Makeyev E.V., Grimes J.M. RNA-dependent RNA polymerases of dsRNA bacteriophages. Virus Res. 2004, 101(1):45-55.
    • (2004) Virus Res. , vol.101 , Issue.1 , pp. 45-55
    • Makeyev, E.V.1    Grimes, J.M.2
  • 78
    • 0000391309 scopus 로고
    • Structural diversity in filamentous bacteriophages. Biological macromolecules and assemblies
    • Wiley-Interscience, New York
    • Makowski L.S. Structural diversity in filamentous bacteriophages. Biological macromolecules and assemblies. Virus Structures 1984, vol. 1:203-253. Wiley-Interscience, New York.
    • (1984) Virus Structures , vol.1 , pp. 203-253
    • Makowski, L.S.1
  • 79
    • 4544386863 scopus 로고    scopus 로고
    • Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation
    • Mancini E.J., Kainov D.E., Grimes J.M., Tuma R., Bamford D.H., Stuart D.I. Atomic snapshots of an RNA packaging motor reveal conformational changes linking ATP hydrolysis to RNA translocation. Cell 2004, 118(6):743-755.
    • (2004) Cell , vol.118 , Issue.6 , pp. 743-755
    • Mancini, E.J.1    Kainov, D.E.2    Grimes, J.M.3    Tuma, R.4    Bamford, D.H.5    Stuart, D.I.6
  • 80
    • 0035918974 scopus 로고    scopus 로고
    • Specific packaging of nodaviral RNA2 requires the N-terminus of the capsid protein
    • Marshall D., Schneemann A. Specific packaging of nodaviral RNA2 requires the N-terminus of the capsid protein. Virology 2001, 285(1):165-175.
    • (2001) Virology , vol.285 , Issue.1 , pp. 165-175
    • Marshall, D.1    Schneemann, A.2
  • 81
    • 0019907224 scopus 로고
    • DNA packaging in vitro by an isolated bacteriophage T7 procapsid
    • Masker W.E., Serwer P. DNA packaging in vitro by an isolated bacteriophage T7 procapsid. J. Virol. 1982, 43(3):1138-1142.
    • (1982) J. Virol. , vol.43 , Issue.3 , pp. 1138-1142
    • Masker, W.E.1    Serwer, P.2
  • 82
    • 79952101724 scopus 로고    scopus 로고
    • Assortment and packaging of the segmented rotavirus genome
    • McDonald S.M., Patton J.T. Assortment and packaging of the segmented rotavirus genome. Trends Microbiol. 2011, 19(3):136-144.
    • (2011) Trends Microbiol. , vol.19 , Issue.3 , pp. 136-144
    • McDonald, S.M.1    Patton, J.T.2
  • 83
    • 81755172911 scopus 로고    scopus 로고
    • Terminal protein-primed amplification of heterologous DNA with a minimal replication system based on phage ϕ29
    • Mencia M., Gella P., Camacho A., de Vega M., Salas M. Terminal protein-primed amplification of heterologous DNA with a minimal replication system based on phage ϕ29. Proc. Natl. Acad. Sci. 2011, 108(46):18655-18660.
    • (2011) Proc. Natl. Acad. Sci. , vol.108 , Issue.46 , pp. 18655-18660
    • Mencia, M.1    Gella, P.2    Camacho, A.3    de Vega, M.4    Salas, M.5
  • 86
    • 84861427386 scopus 로고    scopus 로고
    • The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease
    • Moodley S., Maxwell K.L., Kanelis V. The protein gp74 from the bacteriophage HK97 functions as a HNH endonuclease. Protein Sci. 2012, 2(16):809-818.
    • (2012) Protein Sci. , vol.2 , Issue.16 , pp. 809-818
    • Moodley, S.1    Maxwell, K.L.2    Kanelis, V.3
  • 87
  • 88
    • 0018362508 scopus 로고
    • Comparative studies on two satellite RNAs of cucumber mosaic virus
    • Mossop D.W., Francki R.I.B. Comparative studies on two satellite RNAs of cucumber mosaic virus. Virology 1979, 95(2):395-404.
    • (1979) Virology , vol.95 , Issue.2 , pp. 395-404
    • Mossop, D.W.1    Francki, R.I.B.2
  • 89
    • 84878481589 scopus 로고    scopus 로고
    • Membrane assembly during the infection cycle of the giant mimivirus
    • MutsafiY., Shimoni E., Shimon A., Minsky A. Membrane assembly during the infection cycle of the giant mimivirus. PLoS Pathog. 2013, 9(5):e1003367.
    • (2013) PLoS Pathog. , vol.9 , Issue.5 , pp. e1003367
    • Mutsafi, Y.1    Shimoni, E.2    Shimon, A.3    Minsky, A.4
  • 91
    • 0032567311 scopus 로고    scopus 로고
    • Isolation of a mutant that changes genomic packaging specificity in ϕ6
    • Onodera S., Qiao X., Qiao J., Mindich L. Isolation of a mutant that changes genomic packaging specificity in ϕ6. Virology 1998, 252(2):438-442.
    • (1998) Virology , vol.252 , Issue.2 , pp. 438-442
    • Onodera, S.1    Qiao, X.2    Qiao, J.3    Mindich, L.4
  • 92
    • 84876678181 scopus 로고    scopus 로고
    • Mechanisms of genome packaging
    • RSC Publishing, London, UK
    • Oram M., Black L.W. Mechanisms of genome packaging. Structural Virology 2011, 213-219. RSC Publishing, London, UK.
    • (2011) Structural Virology , pp. 213-219
    • Oram, M.1    Black, L.W.2
  • 93
    • 33645986125 scopus 로고    scopus 로고
    • Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively bind and bend viral DNA: implications for the assembly of a genome-packaging motor
    • Ortega M.E., Catalano C.E. Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively bind and bend viral DNA: implications for the assembly of a genome-packaging motor. Biochemistry 2006, 45(16):5180-5189.
    • (2006) Biochemistry , vol.45 , Issue.16 , pp. 5180-5189
    • Ortega, M.E.1    Catalano, C.E.2
  • 94
    • 0037405145 scopus 로고    scopus 로고
    • Minimal cis-acting elements required for adenovirus genome packaging
    • Ostapchuk P., Hearing P. Minimal cis-acting elements required for adenovirus genome packaging. J. Virol. 2003, 77(9):5127-5135.
    • (2003) J. Virol. , vol.77 , Issue.9 , pp. 5127-5135
    • Ostapchuk, P.1    Hearing, P.2
  • 95
    • 33745780727 scopus 로고    scopus 로고
    • The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome
    • Ostapchuk P., Anderson M.E., Chandrasekhar S., Hearing P. The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome. J. Virol. 2006, 80(14):6973-6981.
    • (2006) J. Virol. , vol.80 , Issue.14 , pp. 6973-6981
    • Ostapchuk, P.1    Anderson, M.E.2    Chandrasekhar, S.3    Hearing, P.4
  • 96
    • 0031774382 scopus 로고    scopus 로고
    • Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage ϕ6
    • Paatero A.O., Mindich L., Bamford D.H. Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage ϕ6. J. Virol. 1998, 72(12):10058-10065.
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 10058-10065
    • Paatero, A.O.1    Mindich, L.2    Bamford, D.H.3
  • 97
    • 0343276268 scopus 로고
    • Initiation of phage ϕ 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP
    • Peñalva M.A., Salas M. Initiation of phage ϕ 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP. Proc. Natl. Acad. Sci. 1982, 79(18):5522-5526.
    • (1982) Proc. Natl. Acad. Sci. , vol.79 , Issue.18 , pp. 5522-5526
    • Peñalva, M.A.1    Salas, M.2
  • 98
    • 0034041604 scopus 로고    scopus 로고
    • RNA secondary structures of the bacteriophage ϕ6 packaging regions
    • Pirttimaa M.J., Bamford D.H. RNA secondary structures of the bacteriophage ϕ6 packaging regions. RNA 2000, 6(6):880-889.
    • (2000) RNA , vol.6 , Issue.6 , pp. 880-889
    • Pirttimaa, M.J.1    Bamford, D.H.2
  • 99
    • 0036786440 scopus 로고    scopus 로고
    • Nonspecific nucleoside triphosphatase P4 of double-stranded RNA bacteriophage ϕ6 is required for single-stranded RNA packaging and transcription
    • Pirttimaa M.J., Paatero A.O., Frilander M.J., Bamford D.H. Nonspecific nucleoside triphosphatase P4 of double-stranded RNA bacteriophage ϕ6 is required for single-stranded RNA packaging and transcription. J. Virol. 2002, 76(20):10122-10127.
    • (2002) J. Virol. , vol.76 , Issue.20 , pp. 10122-10127
    • Pirttimaa, M.J.1    Paatero, A.O.2    Frilander, M.J.3    Bamford, D.H.4
  • 100
    • 0016703827 scopus 로고
    • Location of histones on simian virus 40 DNA
    • Polisky B., McCarthy B. Location of histones on simian virus 40 DNA. Proc. Natl. Acad. Sci. 1975, 72(8):2895-2899.
    • (1975) Proc. Natl. Acad. Sci. , vol.72 , Issue.8 , pp. 2895-2899
    • Polisky, B.1    McCarthy, B.2
  • 101
    • 0035002345 scopus 로고    scopus 로고
    • Self-assembly of a viral molecular machine from purified protein and RNA constituents
    • Poranen M.M., Paatero A.O., Tuma R., Bamford D.H. Self-assembly of a viral molecular machine from purified protein and RNA constituents. Mol. Cell 2001, 7(4):845-854.
    • (2001) Mol. Cell , vol.7 , Issue.4 , pp. 845-854
    • Poranen, M.M.1    Paatero, A.O.2    Tuma, R.3    Bamford, D.H.4
  • 102
    • 84899088004 scopus 로고    scopus 로고
    • Staphylococcal pathogenicity island DNA packaging system involving cos-site packaging and phage-encoded HNH endonucleases
    • Quiles-Puchalt N., Carpena N., Alonso J.C., Novick R.P., Marina A., Penadés J.R. Staphylococcal pathogenicity island DNA packaging system involving cos-site packaging and phage-encoded HNH endonucleases. Proc. Natl. Acad. Sci. 2014, 111(16):6016-6021.
    • (2014) Proc. Natl. Acad. Sci. , vol.111 , Issue.16 , pp. 6016-6021
    • Quiles-Puchalt, N.1    Carpena, N.2    Alonso, J.C.3    Novick, R.P.4    Marina, A.5    Penadés, J.R.6
  • 104
    • 33748940970 scopus 로고    scopus 로고
    • Genome packaging by spherical plant RNA viruses
    • Rao A.L.N. Genome packaging by spherical plant RNA viruses. Annu. Rev. Phytopathol. 2006, 44:61-87.
    • (2006) Annu. Rev. Phytopathol. , vol.44 , pp. 61-87
    • Rao, A.L.N.1
  • 106
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao V.B., Feiss M. The bacteriophage DNA packaging motor. Annu. Rev. Genet. 2008, 42:647-681.
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 108
    • 0027992332 scopus 로고
    • Characterization of the prohead-pRNA interaction of bacteriophage ϕ29
    • Reid R.J., Bodley J.W., Anderson D. Characterization of the prohead-pRNA interaction of bacteriophage ϕ29. J. Biolo. Chem. 1994, 269(7):5157-5162.
    • (1994) J. Biolo. Chem. , vol.269 , Issue.7 , pp. 5157-5162
    • Reid, R.J.1    Bodley, J.W.2    Anderson, D.3
  • 110
    • 37749051185 scopus 로고    scopus 로고
    • Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage ϕ29
    • Rickgauer J.P., Fuller D.N., Grimes S., Jardine P.J., Anderson D.L., Smith D.E. Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage ϕ29. Biophys. J. 2008, 94(1):159-167.
    • (2008) Biophys. J. , vol.94 , Issue.1 , pp. 159-167
    • Rickgauer, J.P.1    Fuller, D.N.2    Grimes, S.3    Jardine, P.J.4    Anderson, D.L.5    Smith, D.E.6
  • 111
    • 0001315638 scopus 로고
    • Structure and assembly of herpesviruses
    • Rixon F.J. Structure and assembly of herpesviruses. Semin. Virol. 1993, 4:135-144.
    • (1993) Semin. Virol. , vol.4 , pp. 135-144
    • Rixon, F.J.1
  • 112
    • 65549134398 scopus 로고    scopus 로고
    • National Center for Biotechnology Information (US), Bethesda (MD), (Bookshelf ID: NBK49492)
    • Rohrmann G.F. Baculovirus Molecular Biology: second edition 2011, National Center for Biotechnology Information (US), Bethesda (MD), (Bookshelf ID: NBK49492).
    • (2011) Baculovirus Molecular Biology: second edition
    • Rohrmann, G.F.1
  • 113
    • 0028999019 scopus 로고
    • Moving through the membrane with filamentous phages
    • Russel M. Moving through the membrane with filamentous phages. Trends Microbiol. 1995, 3(6):223-228.
    • (1995) Trends Microbiol. , vol.3 , Issue.6 , pp. 223-228
    • Russel, M.1
  • 114
    • 0023035960 scopus 로고
    • The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins
    • Russel M., Model P. The role of thioredoxin in filamentous phage assembly. Construction, isolation, and characterization of mutant thioredoxins. J. Biol. Chem. 1986, 261(32):14997-15005.
    • (1986) J. Biol. Chem. , vol.261 , Issue.32 , pp. 14997-15005
    • Russel, M.1    Model, P.2
  • 115
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad J.S., Miller J., Tai J., Kim A., Ghanam R.H., Summers M.F. Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc. Natl. Acad. Sci. 2006, 103(30):11364-11369.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , Issue.30 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 116
    • 0017893449 scopus 로고
    • Characterization of a protein covalently linked to the 5' termini of the DNA of Bacillus subtilis phage ϕ29
    • Salas M., Mellado R.P., Viñuela E., Sogo J.M. Characterization of a protein covalently linked to the 5' termini of the DNA of Bacillus subtilis phage ϕ29. J. Mol. Biol. 1978, 119(2):269-291.
    • (1978) J. Mol. Biol. , vol.119 , Issue.2 , pp. 269-291
    • Salas, M.1    Mellado, R.P.2    Viñuela, E.3    Sogo, J.M.4
  • 117
    • 0002277375 scopus 로고    scopus 로고
    • Mechanisms for priming DNA synthesis
    • Cold Spring Harbor Laboratory Press, NY, (Cold Spring Harbor)
    • Salas M., Miller J.T., Leis J., Depamphilis M.L. Mechanisms for priming DNA synthesis. DNA Replication in Eukaryotic Cells 1996, 131-176. Cold Spring Harbor Laboratory Press, NY, (Cold Spring Harbor).
    • (1996) DNA Replication in Eukaryotic Cells , pp. 131-176
    • Salas, M.1    Miller, J.T.2    Leis, J.3    Depamphilis, M.L.4
  • 118
    • 84873629694 scopus 로고    scopus 로고
    • Effect of capsid confinement on the chromatin organization of the SV40 minichromosome
    • Saper G., Kler S., Asor R., Oppenheim A., Raviv U., Harries D. Effect of capsid confinement on the chromatin organization of the SV40 minichromosome. Nucleic Acids Res. 2013, 41(3):1569-1580.
    • (2013) Nucleic Acids Res. , vol.41 , Issue.3 , pp. 1569-1580
    • Saper, G.1    Kler, S.2    Asor, R.3    Oppenheim, A.4    Raviv, U.5    Harries, D.6
  • 119
    • 0029095624 scopus 로고
    • Natural selection on the gag, pol, and env genes of human immunodeficiency virus 1 (HIV-1)
    • Seibert S.A., Howell C.Y., Hughes M.K., Hughes A.L. Natural selection on the gag, pol, and env genes of human immunodeficiency virus 1 (HIV-1). Mol. Biol. Evol. 1995, 12(5):803-813.
    • (1995) Mol. Biol. Evol. , vol.12 , Issue.5 , pp. 803-813
    • Seibert, S.A.1    Howell, C.Y.2    Hughes, M.K.3    Hughes, A.L.4
  • 120
    • 4744355827 scopus 로고    scopus 로고
    • Plant virus satellite and defective interfering RNAs: new paradigms for a new century
    • Simon A.E., Roossinck M.J., Havelda Z. Plant virus satellite and defective interfering RNAs: new paradigms for a new century. Annu. Rev. Phytopathol. 2004, 42:415-437.
    • (2004) Annu. Rev. Phytopathol. , vol.42 , pp. 415-437
    • Simon, A.E.1    Roossinck, M.J.2    Havelda, Z.3
  • 123
    • 84862945655 scopus 로고    scopus 로고
    • Single-molecule studies of viral DNA packaging
    • Smith D.E. Single-molecule studies of viral DNA packaging. Curr. Opin. Virol. 2011, 1(2):134-141.
    • (2011) Curr. Opin. Virol. , vol.1 , Issue.2 , pp. 134-141
    • Smith, D.E.1
  • 124
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage ϕ29 portal motor can package DNA against a large internal force
    • Smith D.E., Tans S.J., Smith S.B., Grimes S., Anderson D.L., Bustamante C. The bacteriophage ϕ29 portal motor can package DNA against a large internal force. Nature 2001, 413(6857):748-751.
    • (2001) Nature , vol.413 , Issue.6857 , pp. 748-751
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 125
    • 0038523777 scopus 로고    scopus 로고
    • The unique vertex of bacterial virus PRD1 is connected to the viral internal membrane
    • 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. 2003, 77(11):6314-6321.
    • (2003) J. Virol. , vol.77 , Issue.11 , pp. 6314-6321
    • Strömsten, N.J.1    Bamford, D.H.2    Bamford, J.K.H.3
  • 126
    • 17144366252 scopus 로고    scopus 로고
    • Invitro DNA packaging of PRD1: a common mechanism for internal-membrane viruses
    • Strömsten N.J., Bamford D.H., Bamford J.K.H. Invitro DNA packaging of PRD1: a common mechanism for internal-membrane viruses. J. Mol. Biol. 2005, 348(3):617-629.
    • (2005) J. Mol. Biol. , vol.348 , Issue.3 , pp. 617-629
    • Strömsten, N.J.1    Bamford, D.H.2    Bamford, J.K.H.3
  • 127
    • 84856402988 scopus 로고    scopus 로고
    • Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages
    • Sun S., Gao S., Kondabagil K., Xiang Y., Rossmann M.G., Rao V.B. Structure and function of the small terminase component of the DNA packaging machine in T4-like bacteriophages. Proc. Natl. Acad. Sci. 2012, 109(3):817-822.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , Issue.3 , pp. 817-822
    • Sun, S.1    Gao, S.2    Kondabagil, K.3    Xiang, Y.4    Rossmann, M.G.5    Rao, V.B.6
  • 129
    • 41249097397 scopus 로고    scopus 로고
    • Ultrastructural characterization of the giant volcano-like virus factory of Acanthamoeba polyphaga mimivirus
    • Suzan-Monti M., La Scola B., Barrassi L., Espinosa L., Raoult D. Ultrastructural characterization of the giant volcano-like virus factory of Acanthamoeba polyphaga mimivirus. PLoS One 2007, 2(3):e328.
    • (2007) PLoS One , vol.2 , Issue.3 , pp. e328
    • Suzan-Monti, M.1    La Scola, B.2    Barrassi, L.3    Espinosa, L.4    Raoult, D.5
  • 130
    • 0020318765 scopus 로고
    • Function of adenovirus terminal protein in the initiation of DNA replication
    • Tamanoi F., Stillman B.W. Function of adenovirus terminal protein in the initiation of DNA replication. Proc. Natl. Acad. Sci. 1982, 79(7):2221-2225.
    • (1982) Proc. Natl. Acad. Sci. , vol.79 , Issue.7 , pp. 2221-2225
    • Tamanoi, F.1    Stillman, B.W.2
  • 131
    • 79954421946 scopus 로고    scopus 로고
    • Condensed DNA: condensing the concepts
    • Teif V.B., Bohinc K. Condensed DNA: condensing the concepts. Prog. Biophys. Mol. Biol. 2011, 105(3):208-222.
    • (2011) Prog. Biophys. Mol. Biol. , vol.105 , Issue.3 , pp. 208-222
    • Teif, V.B.1    Bohinc, K.2
  • 133
    • 0000793742 scopus 로고    scopus 로고
    • Poxvirus DNA replication, DNA Replication in Eukaryotic Cells
    • Cold Spring Harbor Laboratory Press, NY, (Cold Spring Harbor)
    • Traktman P. Poxvirus DNA replication, DNA Replication in Eukaryotic Cells 1996, 775:775-795. Cold Spring Harbor Laboratory Press, NY, (Cold Spring Harbor).
    • (1996) , vol.775 , pp. 775-795
    • Traktman, P.1
  • 134
    • 33947427084 scopus 로고    scopus 로고
    • Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein
    • Tyler R.E., Ewing S.G., Imperiale M.J. Formation of a multiple protein complex on the adenovirus packaging sequence by the IVa2 protein. J. Virol. 2007, 81(7):3447-3454.
    • (2007) J. Virol. , vol.81 , Issue.7 , pp. 3447-3454
    • Tyler, R.E.1    Ewing, S.G.2    Imperiale, M.J.3
  • 138
    • 84908252278 scopus 로고
    • Chromatin
    • Van Holde K.E. Chromatin. Cell 1989, 59(2):243-244.
    • (1989) Cell , vol.59 , Issue.2 , pp. 243-244
    • Van Holde, K.E.1
  • 139
    • 0042889581 scopus 로고    scopus 로고
    • Rotavirus NSP2 interferes with the core lattice protein VP2 in initiation of minus-strand synthesis
    • Vende P., Tortorici M.A., Taraporewala Z.F., Patton J.T. Rotavirus NSP2 interferes with the core lattice protein VP2 in initiation of minus-strand synthesis. Virology 2003, 313(1):261-273.
    • (2003) Virology , vol.313 , Issue.1 , pp. 261-273
    • Vende, P.1    Tortorici, M.A.2    Taraporewala, Z.F.3    Patton, J.T.4
  • 140
    • 63149184752 scopus 로고    scopus 로고
    • Dual roles for an arginine-rich motif in specific genome recognition and localization of viral coat protein to RNA replication sites in flock house virus-infected cells
    • Venter P.A., Marshall D., Schneemann A. Dual roles for an arginine-rich motif in specific genome recognition and localization of viral coat protein to RNA replication sites in flock house virus-infected cells. J. Virol. 2009, 83(7):2872-2882.
    • (2009) J. Virol. , vol.83 , Issue.7 , pp. 2872-2882
    • Venter, P.A.1    Marshall, D.2    Schneemann, A.3
  • 141
    • 0015876365 scopus 로고
    • Bacteriophage ϕ6: a lipid-containing virus of Pseudomonas phaseolicola
    • Vidaver A.K., Koski R.K., Van Etten J.L. Bacteriophage ϕ6: a lipid-containing virus of Pseudomonas phaseolicola. J. Virol. 1973, 11(5):799-805.
    • (1973) J. Virol. , vol.11 , Issue.5 , pp. 799-805
    • Vidaver, A.K.1    Koski, R.K.2    Van Etten, J.L.3
  • 142
    • 0023042762 scopus 로고
    • Role of the N-terminal part of the coat protein in the assembly of cowpea chlorotic mottle virus: a 500MHz proton nuclear magnetic resonance study and structural calculations
    • Vriend G., Verduin B.J.M., Hemminga M.A. Role of the N-terminal part of the coat protein in the assembly of cowpea chlorotic mottle virus: a 500MHz proton nuclear magnetic resonance study and structural calculations. J. Mol. Biol. 1986, 191(3):453-460.
    • (1986) J. Mol. Biol. , vol.191 , Issue.3 , pp. 453-460
    • Vriend, G.1    Verduin, B.J.M.2    Hemminga, M.A.3
  • 143
    • 0004021544 scopus 로고
    • Structure and Assembly of the Class I Filamentous Bacteriophage
    • Jones & Bartlett, Boston
    • Webster R., Lopez J. Structure and Assembly of the Class I Filamentous Bacteriophage 1985, 235-268. Jones & Bartlett, Boston.
    • (1985) , pp. 235-268
    • Webster, R.1    Lopez, J.2
  • 145
    • 77950455981 scopus 로고    scopus 로고
    • Strong intranucleoid interactions organize the Escherichia coli chromosome into a nucleoid filament
    • Wiggins P.A., Cheveralls K.C., Martin J.S., Lintner R., Kondev J. Strong intranucleoid interactions organize the Escherichia coli chromosome into a nucleoid filament. Proc. Natl. Acad. Sci. 2010, 107(11):4991-4995.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , Issue.11 , pp. 4991-4995
    • Wiggins, P.A.1    Cheveralls, K.C.2    Martin, J.S.3    Lintner, R.4    Kondev, J.5
  • 146
    • 84869001469 scopus 로고    scopus 로고
    • The adenovirus L4-22K protein is multifunctional and is an integral component of crucial aspects of infection
    • Wu K., Orozco D., Hearing P. The adenovirus L4-22K protein is multifunctional and is an integral component of crucial aspects of infection. J. Virol. 2012, 86(19):10474-10483.
    • (2012) J. Virol. , vol.86 , Issue.19 , pp. 10474-10483
    • Wu, K.1    Orozco, D.2    Hearing, P.3
  • 149
    • 78149456074 scopus 로고    scopus 로고
    • Self-association of the adenoviral L4-22K protein
    • Yang T.-C., Maluf N.K. Self-association of the adenoviral L4-22K protein. Biochemistry 2010, 49(45):9830-9838.
    • (2010) Biochemistry , vol.49 , Issue.45 , pp. 9830-9838
    • Yang, T.-C.1    Maluf, N.K.2
  • 151
    • 84862878463 scopus 로고    scopus 로고
    • Push through one-way valve mechanism of viral DNA packaging
    • Zhang H., Schwartz C., De Donatis G.M., Guo P. Push through one-way valve mechanism of viral DNA packaging. Adv. Virus Res. 2012, 83:415-465.
    • (2012) Adv. Virus Res. , vol.83 , pp. 415-465
    • Zhang, H.1    Schwartz, C.2    De Donatis, G.M.3    Guo, P.4
  • 153
    • 14744274896 scopus 로고    scopus 로고
    • Newly identified host factors modulate HIV replication
    • Zheng Y.-H., Lovsin N., Peterlin B.M. Newly identified host factors modulate HIV replication. Immunol. Lett. 2005, 97(2):225-234.
    • (2005) Immunol. Lett. , vol.97 , Issue.2 , pp. 225-234
    • Zheng, Y.-H.1    Lovsin, N.2    Peterlin, B.M.3


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