메뉴 건너뛰기




Volumn 356, Issue 1-2, 2006, Pages 4-11

Quantitative dissociation of archaeal virus SH1 reveals distinct capsid proteins and a lipid core

Author keywords

Archaea; Archaeal virus; Haloarchaea; Haloarcula hispanica; Halobacteria

Indexed keywords

CAPSID PROTEIN;

EID: 33750991064     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2006.07.027     Document Type: Article
Times cited : (32)

References (31)
  • 2
    • 0038392706 scopus 로고    scopus 로고
    • Bacteriophage observations and evolution
    • Ackermann H.W. Bacteriophage observations and evolution. Res. Microbiol. 154 (2003) 245-251
    • (2003) Res. Microbiol. , vol.154 , pp. 245-251
    • Ackermann, H.W.1
  • 3
    • 0019166535 scopus 로고
    • Electron microscopy of cells infected with nonsense mutants of bacteriophage φ{symbol}6
    • Bamford D.H., and Mindich L. Electron microscopy of cells infected with nonsense mutants of bacteriophage φ{symbol}6. Virology 107 (1980) 222-228
    • (1980) Virology , vol.107 , pp. 222-228
    • Bamford, D.H.1    Mindich, L.2
  • 7
    • 9744228738 scopus 로고    scopus 로고
    • Does common architecture reveal a viral lineage spanning all three domains of life?
    • Benson S.D., Bamford J.K., Bamford D.H., and Burnett R.M. Does common architecture reveal a viral lineage spanning all three domains of life?. Mol. Cell 16 (2004) 673-685
    • (2004) Mol. Cell , vol.16 , pp. 673-685
    • Benson, S.D.1    Bamford, J.K.2    Bamford, D.H.3    Burnett, R.M.4
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 9
    • 0034730067 scopus 로고    scopus 로고
    • Assembly of bacteriophage PRD1 spike complex: role of the multidomain protein P5
    • Caldentey J., Tuma R., and Bamford D.H. Assembly of bacteriophage PRD1 spike complex: role of the multidomain protein P5. Biochemistry 39 (2000) 10566-10573
    • (2000) Biochemistry , vol.39 , pp. 10566-10573
    • Caldentey, J.1    Tuma, R.2    Bamford, D.H.3
  • 12
    • 0037716583 scopus 로고    scopus 로고
    • Haloarchaeal viruses: how diverse are they?
    • Dyall-Smith M., Tang S.L., and Bath C. Haloarchaeal viruses: how diverse are they?. Res. Microbiol. 154 (2003) 309-313
    • (2003) Res. Microbiol. , vol.154 , pp. 309-313
    • Dyall-Smith, M.1    Tang, S.L.2    Bath, C.3
  • 13
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch J., Lees M., and Sloane-Stanley G.H. A simple method for the isolation and purification of total lipides from animal tissues. J. Biol. Chem. 226 (1957) 497-509
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane-Stanley, G.H.3
  • 14
    • 4344559453 scopus 로고    scopus 로고
    • The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes
    • Huiskonen J.T., Kivelä H.M., Bamford D.H., and Butcher S.J. The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat. Struct. Mol. Biol. 11 (2004) 850-856
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 850-856
    • Huiskonen, J.T.1    Kivelä, H.M.2    Bamford, D.H.3    Butcher, S.J.4
  • 15
    • 0003146009 scopus 로고
    • Haloarcula hispanica spec. nov. and Haloferax gibbonsii spec. nov., two new species of extremely halophilic archaebacteria
    • Juez G., Rodriquez-Valera F., Ventosa A., and Kushner D.J. Haloarcula hispanica spec. nov. and Haloferax gibbonsii spec. nov., two new species of extremely halophilic archaebacteria. System. Appl. Microbiol. 8 (1986) 75-79
    • (1986) System. Appl. Microbiol. , vol.8 , pp. 75-79
    • Juez, G.1    Rodriquez-Valera, F.2    Ventosa, A.3    Kushner, D.J.4
  • 17
    • 30044450170 scopus 로고    scopus 로고
    • Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses
    • Khayat R., Tang L., Larson E.T., Lawrence C.M., Young M., and Johnson J.E. Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 18944-18949
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18944-18949
    • Khayat, R.1    Tang, L.2    Larson, E.T.3    Lawrence, C.M.4    Young, M.5    Johnson, J.E.6
  • 18
    • 0036319176 scopus 로고    scopus 로고
    • Bacteriophage PM2 has a protein capsid surrounding a spherical proteinaceous lipid core
    • Kivelä H.M., Kalkkinen N., and Bamford D.H. Bacteriophage PM2 has a protein capsid surrounding a spherical proteinaceous lipid core. J. Virol. 76 (2002) 8169-8178
    • (2002) J. Virol. , vol.76 , pp. 8169-8178
    • Kivelä, H.M.1    Kalkkinen, N.2    Bamford, D.H.3
  • 19
    • 27944481316 scopus 로고    scopus 로고
    • Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35
    • Laurinmäki P.A., Huiskonen J.T., Bamford D.H., and Butcher S.J. Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35. Structure 13 (2005) 1819-1828
    • (2005) Structure , vol.13 , pp. 1819-1828
    • Laurinmäki, P.A.1    Huiskonen, J.T.2    Bamford, D.H.3    Butcher, S.J.4
  • 20
    • 17044438215 scopus 로고    scopus 로고
    • The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture
    • Merckel M.C., Huiskonen J.T., Bamford D.H., Goldman A., and Tuma R. The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol. Cell 18 (2005) 161-170
    • (2005) Mol. Cell , vol.18 , pp. 161-170
    • Merckel, M.C.1    Huiskonen, J.T.2    Bamford, D.H.3    Goldman, A.4    Tuma, R.5
  • 22
    • 0027374807 scopus 로고
    • HF1 and HF2: novel bacteriophages of halophilic archaea
    • Nuttall S.D., and Dyall-Smith M.L. HF1 and HF2: novel bacteriophages of halophilic archaea. Virology 197 (1993) 678-684
    • (1993) Virology , vol.197 , pp. 678-684
    • Nuttall, S.D.1    Dyall-Smith, M.L.2
  • 23
    • 0031196664 scopus 로고    scopus 로고
    • Occurrence of virus-like particles in the Dead Sea
    • Oren A., Bratbak G., and Heldal M. Occurrence of virus-like particles in the Dead Sea. Extremophiles 1 (1997) 143-149
    • (1997) Extremophiles , vol.1 , pp. 143-149
    • Oren, A.1    Bratbak, G.2    Heldal, M.3
  • 25
    • 27144541842 scopus 로고    scopus 로고
    • Viruses of hyperthermophilic crenarchaea
    • Prangishvili D., and Garrett R.A. Viruses of hyperthermophilic crenarchaea. Trends Microbiol. 13 (2005) 535-542
    • (2005) Trends Microbiol. , vol.13 , pp. 535-542
    • Prangishvili, D.1    Garrett, R.A.2
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 31
    • 17144366252 scopus 로고    scopus 로고
    • In vitro DNA packaging of PRD1: a common mechanism for internal-membrane viruses
    • Strömsten N.J., Bamford D.H., and Bamford J.K. In vitro DNA packaging of PRD1: a common mechanism for internal-membrane viruses. J. Mol. Biol. 348 (2005) 617-629
    • (2005) J. Mol. Biol. , vol.348 , pp. 617-629
    • Strömsten, N.J.1    Bamford, D.H.2    Bamford, J.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.