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Volumn 89, Issue 18, 2015, Pages 9288-9298

Exploring the balance between DNA pressure and capsid stability in herpesviruses and phages

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS DNA;

EID: 84940517444     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01172-15     Document Type: Article
Times cited : (50)

References (61)
  • 1
    • 0003715206 scopus 로고    scopus 로고
    • Principles of virology, 3rd ed
    • ASM Press, Washington, DC.
    • Flint SJ. 2009. Principles of virology, 3rd ed. ASM Press, Washington, DC.
    • (2009)
    • Flint, S.J.1
  • 2
    • 33747342874 scopus 로고    scopus 로고
    • Viruses' life history: towards a mechanistic basis of a trade-off between survival and reproduction among phages
    • De Paepe M, Taddei F. 2006. Viruses' life history: towards a mechanistic basis of a trade-off between survival and reproduction among phages. PLoS Biol 4:e193. http://dx.doi.org/10.1371/journal.pbio.0040193.
    • (2006) PLoS Biol , vol.4
    • De Paepe, M.1    Taddei, F.2
  • 3
    • 0035923664 scopus 로고    scopus 로고
    • DNA packaging and ejection forces in bacteriophage
    • Kindt J, Tzlil S, Ben-Shaul A, Gelbart WM. 2001. DNA packaging and ejection forces in bacteriophage. Proc Natl Acad Sci U S A 98:13671- 13674. http://dx.doi.org/10.1073/pnas.241486298.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13671-13674
    • Kindt, J.1    Tzlil, S.2    Ben-Shaul, A.3    Gelbart, W.M.4
  • 4
    • 0037340654 scopus 로고    scopus 로고
    • Forces and pressures inDNApackaging and release from viral capsids
    • Tzlil S, Kindt JT, Gelbart WM, Ben-Shaul A. 2003. Forces and pressures inDNApackaging and release from viral capsids. Biophys J 84:1616-1627. http://dx.doi.org/10.1016/S0006-3495(03)74971-6.
    • (2003) Biophys J , vol.84 , pp. 1616-1627
    • Tzlil, S.1    Kindt, J.T.2    Gelbart, W.M.3    Ben-Shaul, A.4
  • 5
    • 0026558204 scopus 로고
    • Direct measurement of the intermolecular forces between counterion-condensed DNA double helices Evidence for long range attractive hydration forces
    • Rau DC, Parsegian VA. 1992. Direct measurement of the intermolecular forces between counterion-condensed DNA double helices. Evidence for long range attractive hydration forces. Biophys J 61:246-259.
    • (1992) Biophys J , vol.61 , pp. 246-259
    • Rau, D.C.1    Parsegian, V.A.2
  • 6
    • 34447260515 scopus 로고    scopus 로고
    • Packaging of DNA by bacteriophage epsilon15: structure, forces, and thermodynamics
    • Petrov AS, Lim-Hing K, Harvey SC. 2007. Packaging of DNA by bacteriophage epsilon15: structure, forces, and thermodynamics. Structure 15: 807-812. http://dx.doi.org/10.1016/j.str.2007.05.005.
    • (2007) Structure , vol.15 , pp. 807-812
    • Petrov, A.S.1    Lim-Hing, K.2    Harvey, S.C.3
  • 8
    • 84878153984 scopus 로고    scopus 로고
    • DNA ejection from an archaeal virus-a single-molecule approach
    • Hanhijarvi KJ, Ziedaite G, Pietila MK, Haeggstrom E, Bamford DH. 2013. DNA ejection from an archaeal virus-a single-molecule approach. Biophys J 104:2264-2272. http://dx.doi.org/10.1016/j.bpj.2013.03.061.
    • (2013) Biophys J , vol.104 , pp. 2264-2272
    • Hanhijarvi, K.J.1    Ziedaite, G.2    Pietila, M.K.3    Haeggstrom, E.4    Bamford, D.H.5
  • 9
    • 84881078113 scopus 로고    scopus 로고
    • Herpes virus genome, the pressure is on
    • Bauer DW, Huffman JB, Homa FL, Evilevitch A. 2013. Herpes virus genome, the pressure is on. J Am Chem Soc 135:11216-11221. http://dx .doi.org/10.1021/ja404008r.
    • (2013) J Am Chem Soc , vol.135 , pp. 11216-11221
    • Bauer, D.W.1    Huffman, J.B.2    Homa, F.L.3    Evilevitch, A.4
  • 10
    • 84864817716 scopus 로고    scopus 로고
    • Viral connectors for DNA encapsulation
    • Cuervo A, Carrascosa JL. 2012. Viral connectors for DNA encapsulation. Curr Opin Biotechnol 23:529-536. http://dx.doi.org/10.1016/j.copbio .2011.11.029.
    • (2012) Curr Opin Biotechnol , vol.23 , pp. 529-536
    • Cuervo, A.1    Carrascosa, J.L.2
  • 11
    • 84908063758 scopus 로고    scopus 로고
    • Molecular architecture of tailed doublestranded DNA phages
    • Fokine A, Rossmann MG. 2014. Molecular architecture of tailed doublestranded DNA phages. Bacteriophage 4:e28281. http://dx.doi.org/10.4161 /bact.28281.
    • (2014) Bacteriophage , vol.4
    • Fokine, A.1    Rossmann, M.G.2
  • 12
    • 0037452426 scopus 로고    scopus 로고
    • New approach to stability assessment of protein solution formulations by differential scanning calorimetry
    • Cueto M, Dorta MJ, Munguia O, Llabres M. 2003. New approach to stability assessment of protein solution formulations by differential scanning calorimetry. Int J Pharm 252:159-166. http://dx.doi.org/10.1016 /S0378-5173(02)00627-0.
    • (2003) Int J Pharm , vol.252 , pp. 159-166
    • Cueto, M.1    Dorta, M.J.2    Munguia, O.3    Llabres, M.4
  • 13
    • 78650099292 scopus 로고    scopus 로고
    • Differential scanning calorimetry techniques: applications in biology and nanoscience
    • Gill P, Moghadam TT, Ranjbar B. 2010. Differential scanning calorimetry techniques: applications in biology and nanoscience. J Biomol Tech 21:167-193.
    • (2010) J Biomol Tech , vol.21 , pp. 167-193
    • Gill, P.1    Moghadam, T.T.2    Ranjbar, B.3
  • 15
    • 80051707836 scopus 로고    scopus 로고
    • The DNA-packaging nanomotor of tailed bacteriophages
    • Casjens SR. 2011. The DNA-packaging nanomotor of tailed bacteriophages. Nat Rev Microbiol 9:647-657. http://dx.doi.org/10.1038/nrmicro2632.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 647-657
    • Casjens, S.R.1
  • 16
    • 0017118828 scopus 로고
    • Assembly of the head of bacteriophage P22: x-ray diffraction from heads, proheads and related structures
    • Earnshaw W, Casjens S, Harrison SC. 1976. Assembly of the head of bacteriophage P22: x-ray diffraction from heads, proheads and related structures. J Mol Biol 104:387-410. http://dx.doi.org/10.1016/0022-2836(76)90278-3.
    • (1976) J Mol Biol , vol.104 , pp. 387-410
    • Earnshaw, W.1    Casjens, S.2    Harrison, S.C.3
  • 18
    • 84876815569 scopus 로고    scopus 로고
    • Function and horizontal transfer of the small terminase subunit of the tailed bacteriophage Sf6 DNA packaging nanomotor
    • Leavitt JC, Gilcrease EB, Wilson K, Casjens SR. 2013. Function and horizontal transfer of the small terminase subunit of the tailed bacteriophage Sf6 DNA packaging nanomotor. Virology 440:117-133. http://dx .doi.org/10.1016/j.virol.2013.02.023.
    • (2013) Virology , vol.440 , pp. 117-133
    • Leavitt, J.C.1    Gilcrease, E.B.2    Wilson, K.3    Casjens, S.R.4
  • 19
    • 84881531211 scopus 로고    scopus 로고
    • The tip of the tail needle affects the rate of DNA delivery by bacteriophage P22
    • Leavitt JC, Gogokhia L, Gilcrease EB, Bhardwaj A, Cingolani G, Casjens SR. 2013. The tip of the tail needle affects the rate of DNA delivery by bacteriophage P22. PLoS One 8:e70936. http://dx.doi.org/10.1371 /journal.pone.0070936.
    • (2013) PLoS One , vol.8
    • Leavitt, J.C.1    Gogokhia, L.2    Gilcrease, E.B.3    Bhardwaj, A.4    Cingolani, G.5    Casjens, S.R.6
  • 20
    • 0022504699 scopus 로고
    • Generation of an inverting herpes simplex virus 1 mutant lacking the L-S junction a sequences, an origin of DNA synthesis, and several genes including those specifying glycoprotein E and the alpha 47 gene
    • Longnecker R, Roizman B. 1986. Generation of an inverting herpes simplex virus 1 mutant lacking the L-S junction a sequences, an origin of DNA synthesis, and several genes including those specifying glycoprotein E and the alpha 47 gene. J Virol 58:583-591.
    • (1986) J Virol , vol.58 , pp. 583-591
    • Longnecker, R.1    Roizman, B.2
  • 21
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov PL, Potekhin SA. 1986. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 131:4-51. http://dx.doi.org/10.1016/0076-6879(86)31033-4.
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 22
    • 0031214756 scopus 로고    scopus 로고
    • A new ultrasensitive scanning calorimeter
    • Plotnikov VV, Brandts JM, Lin LN, Brandts JF. 1997. A new ultrasensitive scanning calorimeter. Anal Biochem 250:237-244. http://dx.doi.org /10.1006/abio.1997.2236.
    • (1997) Anal Biochem , vol.250 , pp. 237-244
    • Plotnikov, V.V.1    Brandts, J.M.2    Lin, L.N.3    Brandts, J.F.4
  • 24
    • 84863845580 scopus 로고    scopus 로고
    • Heat induced capsid disassembly and DNA release of bacteriophage lambda
    • Qiu X. 2012. Heat induced capsid disassembly and DNA release of bacteriophage lambda. PLoS One 7:e39793. http://dx.doi.org/10.1371/journal .pone.0039793.
    • (2012) PLoS One , vol.7
    • Qiu, X.1
  • 25
    • 67650697753 scopus 로고    scopus 로고
    • Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy
    • Duda RL, Ross PD, Cheng N, Firek BA, Hendrix RW, Conway JF, Steven AC. 2009. Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy. J Mol Biol 391:471-483. http://dx.doi.org/10.1016/j.jmb.2009 .06.035.
    • (2009) J Mol Biol , vol.391 , pp. 471-483
    • Duda, R.L.1    Ross, P.D.2    Cheng, N.3    Firek, B.A.4    Hendrix, R.W.5    Conway, J.F.6    Steven, A.C.7
  • 26
    • 73649136056 scopus 로고    scopus 로고
    • DNA heats up: energetics of genome ejection from phage revealed by isothermal titration calorimetry
    • Jeembaeva M, Jonsson B, Castelnovo M, Evilevitch A. 2010. DNA heats up: energetics of genome ejection from phage revealed by isothermal titration calorimetry. J Mol Biol 395:1079-1087. http://dx.doi.org/10.1016/j .jmb.2009.11.069.
    • (2010) J Mol Biol , vol.395 , pp. 1079-1087
    • Jeembaeva, M.1    Jonsson, B.2    Castelnovo, M.3    Evilevitch, A.4
  • 27
    • 35548972992 scopus 로고    scopus 로고
    • Real-time observations of single bacteriophage lambda DNA ejections in vitro
    • Grayson P, Han L, Winther T, Phillips R. 2007. Real-time observations of single bacteriophage lambda DNA ejections in vitro. Proc Natl Acad Sci U S A 104:14652-14657. http://dx.doi.org/10.1073/pnas.0703274104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 14652-14657
    • Grayson, P.1    Han, L.2    Winther, T.3    Phillips, R.4
  • 28
    • 77955190740 scopus 로고    scopus 로고
    • Is the in vitro ejection of bacteriophage DNA quasistatic? A bulk to single virus study
    • Chiaruttini N, de Frutos M, Augarde E, Boulanger P, Letellier L, Viasnoff V. 2010. Is the in vitro ejection of bacteriophage DNA quasistatic? A bulk to single virus study. Biophys J 99:447-455. http://dx.doi.org /10.1016/j.bpj.2010.04.048.
    • (2010) Biophys J , vol.99 , pp. 447-455
    • Chiaruttini, N.1    de Frutos, M.2    Augarde, E.3    Boulanger, P.4    Letellier, L.5    Viasnoff, V.6
  • 30
    • 0027320418 scopus 로고
    • Conformational transformations in the protein lattice of phage P22 procapsids
    • Galisteo ML, King J. 1993. Conformational transformations in the protein lattice of phage P22 procapsids. Biophys J 65:227-235. http://dx.doi .org/10.1016/S0006-3495(93)81073-7.
    • (1993) Biophys J , vol.65 , pp. 227-235
    • Galisteo, M.L.1    King, J.2
  • 31
  • 32
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • Sanchez-Ruiz JM, Lopez-Lacomba JL, Cortijo M, Mateo PL. 1988. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 27:1648-1652. http://dx.doi.org/10.1021 /bi00405a039.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 33
    • 84863994272 scopus 로고    scopus 로고
    • Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly
    • White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV. 2012. Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly. J Virol 86:6768-6777. http://dx.doi.org/10 .1128/JVI.00412-12.
    • (2012) J Virol , vol.86 , pp. 6768-6777
    • White, H.E.1    Sherman, M.B.2    Brasiles, S.3    Jacquet, E.4    Seavers, P.5    Tavares, P.6    Orlova, E.V.7
  • 34
    • 0141567910 scopus 로고    scopus 로고
    • Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy
    • Dzwolak W, Ravindra R, Lendermann J, Winter R. 2003. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 42:11347-11355. http://dx.doi.org/10.1021/bi034879h.
    • (2003) Biochemistry , vol.42 , pp. 11347-11355
    • Dzwolak, W.1    Ravindra, R.2    Lendermann, J.3    Winter, R.4
  • 35
    • 84859270120 scopus 로고    scopus 로고
    • Thermodynamic characterization of viral procapsid expansion into a functional capsid shell
    • Medina E, Nakatani E, Kruse S, Catalano CE. 2012. Thermodynamic characterization of viral procapsid expansion into a functional capsid shell. J Mol Biol 418:167-180. http://dx.doi.org/10.1016/j.jmb.2012.02 .020.
    • (2012) J Mol Biol , vol.418 , pp. 167-180
    • Medina, E.1    Nakatani, E.2    Kruse, S.3    Catalano, C.E.4
  • 37
    • 84890862396 scopus 로고    scopus 로고
    • Isolation and characterization of the herpes simplex virus 1 terminase complex
    • Heming JD, Huffman JB, Jones LM, Homa FL. 2014. Isolation and characterization of the herpes simplex virus 1 terminase complex. J Virol 88:225-236. http://dx.doi.org/10.1128/JVI.02632-13.
    • (2014) J Virol , vol.88 , pp. 225-236
    • Heming, J.D.1    Huffman, J.B.2    Jones, L.M.3    Homa, F.L.4
  • 38
    • 82355175265 scopus 로고    scopus 로고
    • Herpes simplex virus capsid assembly and DNA packaging: a present and future antiviral drug target
    • Baines JD. 2011. Herpes simplex virus capsid assembly and DNA packaging: a present and future antiviral drug target. Trends Microbiol 19: 606-613. http://dx.doi.org/10.1016/j.tim.2011.09.001.
    • (2011) Trends Microbiol , vol.19 , pp. 606-613
    • Baines, J.D.1
  • 39
    • 0030871678 scopus 로고    scopus 로고
    • Capsid assembly and DNA packaging in herpes simplex virus
    • Homa FL, Brown JC. 1997. Capsid assembly and DNA packaging in herpes simplex virus. Rev Med Virol 7:107-122. http://dx.doi.org/10.1002 /(SICI)1099-1654(199707)7:2107::AID-RMV191 3.0.CO;2-M.
    • (1997) Rev Med Virol , vol.7 , pp. 107-122
    • Homa, F.L.1    Brown, J.C.2
  • 40
    • 33751323827 scopus 로고    scopus 로고
    • Effects of condensing agent and nuclease on the extent of ejection from phage lambda
    • Evilevitch A. 2006. Effects of condensing agent and nuclease on the extent of ejection from phage lambda. J Phys Chem B 110:22261-22265. http: //dx.doi.org/10.1021/jp060573j.
    • (2006) J Phys Chem B , vol.110 , pp. 22261-22265
    • Evilevitch, A.1
  • 41
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage straight phi29 portal motor can package DNA against a large internal force
    • Smith DE, Tans SJ, Smith SB, Grimes S, Anderson DL, Bustamante C. 2001. The bacteriophage straight phi29 portal motor can package DNA against a large internal force. Nature 413:748-752. http://dx.doi.org/10 .1038/35099581.
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 42
    • 35148815738 scopus 로고    scopus 로고
    • Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations
    • Fuller DN, Raymer DM, Rickgauer JP, Robertson RM, Catalano CE, Anderson DL, Grimes S, Smith DE. 2007. Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations. J Mol Biol 373: 1113-1122. http://dx.doi.org/10.1016/j.jmb.2007.09.011.
    • (2007) J Mol Biol , vol.373 , 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
  • 43
    • 78651293238 scopus 로고    scopus 로고
    • Salt-dependent DNA-DNA spacings in intact bacteriophage lambda reflect relative importance of DNA self-repulsion and bending energies
    • Qiu X, Rau DC, Parsegian VA, Fang LT, Knobler CM, Gelbart WM. 2011. Salt-dependent DNA-DNA spacings in intact bacteriophage lambda reflect relative importance of DNA self-repulsion and bending energies. Phys Rev Lett 106:028102. http://dx.doi.org/10.1103/PhysRevLett.106 .028102.
    • (2011) Phys Rev Lett , vol.106 , pp. 028102
    • Qiu, X.1    Rau, D.C.2    Parsegian, V.A.3    Fang, L.T.4    Knobler, C.M.5    Gelbart, W.M.6
  • 44
    • 0001533502 scopus 로고
    • Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel DNA double helices
    • Rau DC, Lee B, Parsegian VA. 1984. Measurement of the repulsive force between polyelectrolyte molecules in ionic solution: hydration forces between parallel DNA double helices. Proc Natl Acad Sci U S A 81:2621- 2625. http://dx.doi.org/10.1073/pnas.81.9.2621.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 2621- 2625
    • Rau, D.C.1    Lee, B.2    Parsegian, V.A.3
  • 45
    • 84922061254 scopus 로고    scopus 로고
    • Solid-to-fluidDNAtransition inside HSV-1 capsid close to the temperature of infection
    • Sae-Ueng U, Li D, Zuo X, Huffman JB, Homa FL, Rau D, Evilevitch A. 2014. Solid-to-fluidDNAtransition inside HSV-1 capsid close to the temperature of infection. Nat Chem Biol 10:861-867. http://dx.doi.org/10 .1038/nchembio.1628.
    • (2014) Nat Chem Biol , vol.10 , pp. 861-867
    • Sae-Ueng, U.1    Li, D.2    Zuo, X.3    Huffman, J.B.4    Homa, F.L.5    Rau, D.6    Evilevitch, A.7
  • 46
    • 0020666329 scopus 로고
    • Stability and in vitro DNA packaging of bacteriophages: effects of dextrans, sugars, and polyols
    • Serwer P, Masker WE, Allen JL. 1983. Stability and in vitro DNA packaging of bacteriophages: effects of dextrans, sugars, and polyols. J Virol 45:665-671.
    • (1983) J Virol , vol.45 , pp. 665-671
    • Serwer, P.1    Masker, W.E.2    Allen, J.L.3
  • 47
    • 0015222711 scopus 로고
    • Deletion mutants of bacteriophage lambda. I. Isolation and initial characterization
    • Parkinson JS, Huskey RJ. 1971. Deletion mutants of bacteriophage lambda. I. Isolation and initial characterization. J Mol Biol 56:369-384.
    • (1971) J Mol Biol , vol.56 , pp. 369-384
    • Parkinson, J.S.1    Huskey, R.J.2
  • 48
    • 0015863735 scopus 로고
    • Visualization of thermal inactivation in phages lambda and phi80
    • Yamagishi H, Eguchi G, Matsuo H, Ozeki H. 1973. Visualization of thermal inactivation in phages lambda and phi80. Virology 53:277-282. http://dx.doi.org/10.1016/0042-6822(73)90486-8.
    • (1973) Virology , vol.53 , pp. 277-282
    • Yamagishi, H.1    Eguchi, G.2    Matsuo, H.3    Ozeki, H.4
  • 49
    • 57349125715 scopus 로고    scopus 로고
    • Engineering viable foot-and-mouth disease viruses with increased thermostability as a step in the development of improved vaccines
    • Mateo R, Luna E, Rincon V, Mateu MG. 2008. Engineering viable foot-and-mouth disease viruses with increased thermostability as a step in the development of improved vaccines. J Virol 82:12232-12240. http://dx .doi.org/10.1128/JVI.01553-08.
    • (2008) J Virol , vol.82 , pp. 12232-12240
    • Mateo, R.1    Luna, E.2    Rincon, V.3    Mateu, M.G.4
  • 50
    • 84876549863 scopus 로고    scopus 로고
    • Assembly, stability and dynamics of virus capsids
    • Mateu MG. 2013. Assembly, stability and dynamics of virus capsids. Arch Biochem Biophys 531:65-79. http://dx.doi.org/10.1016/j.abb.2012.10.015.
    • (2013) Arch Biochem Biophys , vol.531 , pp. 65-79
    • Mateu, M.G.1
  • 51
    • 0017657414 scopus 로고
    • DNA arrangement in isometric phage heads
    • Earnshaw WC, Harrison SC. 1977. DNA arrangement in isometric phage heads. Nature 268:598-602. http://dx.doi.org/10.1038/268598a0.
    • (1977) Nature , vol.268 , pp. 598-602
    • Earnshaw, W.C.1    Harrison, S.C.2
  • 52
    • 0034645746 scopus 로고    scopus 로고
    • Cryomicroscopy of human cytomegalovirus virions reveals more densely packed genomic DNA than in herpes simplex virus type 1
    • Bhella D, Rixon FJ, Dargan DJ. 2000. Cryomicroscopy of human cytomegalovirus virions reveals more densely packed genomic DNA than in herpes simplex virus type 1. J Mol Biol 295:155-161. http://dx.doi.org/10 .1006/jmbi.1999.3344.
    • (2000) J Mol Biol , vol.295 , pp. 155-161
    • Bhella, D.1    Rixon, F.J.2    Dargan, D.J.3
  • 53
    • 0026073819 scopus 로고
    • Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus
    • Booy FP, Newcomb WW, Trus BL, Brown JC, Baker TS, Steven AC. 1991. Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virus. Cell 64:1007-1015. http://dx.doi.org/10.1016/0092 -8674(91)90324-R.
    • (1991) Cell , vol.64 , pp. 1007-1015
    • Booy, F.P.1    Newcomb, W.W.2    Trus, B.L.3    Brown, J.C.4    Baker, T.S.5    Steven, A.C.6
  • 54
    • 34547444408 scopus 로고    scopus 로고
    • Internal DNA pressure modifies stability of WT phage
    • Ivanovska I, Wuite G, Jonsson B, Evilevitch A. 2007. Internal DNA pressure modifies stability of WT phage. Proc Natl Acad Sci U S A 104: 9603-9608. http://dx.doi.org/10.1073/pnas.0703166104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9603-9608
    • Ivanovska, I.1    Wuite, G.2    Jonsson, B.3    Evilevitch, A.4
  • 55
    • 42449112829 scopus 로고    scopus 로고
    • Biophysics of viral infectivity: matching genome length with capsid size
    • Nurmemmedov E, Castelnovo M, Catalano CE, Evilevitch A. 2007. Biophysics of viral infectivity: matching genome length with capsid size.Q Rev Biophys 40:327-356. http://dx.doi.org/10.1017/S0033583508004666.
    • (2007) Q Rev Biophys , vol.40 , pp. 327-356
    • Nurmemmedov, E.1    Castelnovo, M.2    Catalano, C.E.3    Evilevitch, A.4
  • 56
    • 0030298322 scopus 로고    scopus 로고
    • Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation
    • Newcomb WW, Homa FL, Thomsen DR, Booy FP, Trus BL, Steven AC, Spencer JV, Brown JC. 1996. Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation. J Mol Biol 263:432-446. http://dx.doi.org/10.1006/jmbi.1996.0587.
    • (1996) J Mol Biol , vol.263 , pp. 432-446
    • Newcomb, W.W.1    Homa, F.L.2    Thomsen, D.R.3    Booy, F.P.4    Trus, B.L.5    Steven, A.C.6    Spencer, J.V.7    Brown, J.C.8
  • 57
    • 50849118817 scopus 로고    scopus 로고
    • Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo- EM
    • Lander GC, Evilevitch A, Jeembaeva M, Potter CS, Carragher B, Johnson JE. 2008. Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo- EM. Structure 16:1399-1406. http://dx.doi.org/10.1016/j.str.2008.05.016.
    • (2008) Structure , vol.16 , pp. 1399-1406
    • Lander, G.C.1    Evilevitch, A.2    Jeembaeva, M.3    Potter, C.S.4    Carragher, B.5    Johnson, J.E.6
  • 58
    • 36849043686 scopus 로고    scopus 로고
    • Structure of phage P22 cell envelope-penetrating needle
    • Olia AS, Casjens S, Cingolani G. 2007. Structure of phage P22 cell envelope-penetrating needle. Nat Struct Mol Biol 14:1221-1226. http://dx .doi.org/10.1038/nsmb1317.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1221-1226
    • Olia, A.S.1    Casjens, S.2    Cingolani, G.3
  • 59
    • 84896522348 scopus 로고    scopus 로고
    • Elastic properties and heterogeneous stiffness of the phi29 motor connector channel
    • Kumar R, Grubmuller H. 2014. Elastic properties and heterogeneous stiffness of the phi29 motor connector channel. Biophys J 106:1338-1348. http://dx.doi.org/10.1016/j.bpj.2014.01.028.
    • (2014) Biophys J , vol.106 , pp. 1338-1348
    • Kumar, R.1    Grubmuller, H.2
  • 60
    • 69749108841 scopus 로고    scopus 로고
    • Polarized DNA ejection from the herpesvirus capsid
    • Newcomb WW, Cockrell SK, Homa FL, Brown JC. 2009. Polarized DNA ejection from the herpesvirus capsid. J Mol Biol 392:885-894. http://dx .doi.org/10.1016/j.jmb.2009.07.052.
    • (2009) J Mol Biol , vol.392 , pp. 885-894
    • Newcomb, W.W.1    Cockrell, S.K.2    Homa, F.L.3    Brown, J.C.4
  • 61
    • 84867350581 scopus 로고    scopus 로고
    • Viral fitness: definitions, measurement, and current insights
    • Wargo AR, Kurath G. 2012. Viral fitness: definitions, measurement, and current insights. Curr Opin Virol 2:538-545. http://dx.doi.org/10.1016/j .coviro.2012.07.007.
    • (2012) Curr Opin Virol , vol.2 , pp. 538-545
    • Wargo, A.R.1    Kurath, G.2


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