메뉴 건너뛰기




Volumn 84, Issue 18, 2010, Pages 9575-9583

The architecture and chemical stability of the archaeal Sulfolobus turreted icosahedral virus

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; MACROMOLECULE; VIRUS PROTEIN;

EID: 77956034102     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00708-10     Document Type: Article
Times cited : (33)

References (30)
  • 4
    • 0033578669 scopus 로고    scopus 로고
    • Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures
    • Benson, S. D., J. K. H. Bamford, D. H. Bamford, and R. Burnett. 1999. Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell 98:825-833.
    • (1999) Cell , vol.98 , pp. 825-833
    • Benson, S.D.1    Bamford, J.K.H.2    Bamford, D.H.3    Burnett, R.4
  • 5
    • 66149105112 scopus 로고    scopus 로고
    • Particle assembly and ultrastructural features associated with replication of the lytic archaeal virus sulfolobus turreted icosahedral virus
    • Brumfield, S. K., A. C. Ortmann, V. Ruigrok, P. Suci, T. Douglas, and M. J. Young. 2009. Particle assembly and ultrastructural features associated with replication of the lytic archaeal virus sulfolobus turreted icosahedral virus. J. Virol. 83:5964-5970.
    • (2009) J. Virol. , vol.83 , pp. 5964-5970
    • Brumfield, S.K.1    Ortmann, A.C.2    Ruigrok, V.3    Suci, P.4    Douglas, T.5    Young, M.J.6
  • 7
    • 0022219750 scopus 로고
    • The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture
    • Burnett, R. M. 1985. The structure of the adenovirus capsid. II. The packing symmetry of hexon and its implications for viral architecture. J. Mol. Biol. 185:125-143.
    • (1985) J. Mol. Biol. , vol.185 , pp. 125-143
    • Burnett, R.M.1
  • 8
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., M. Radermacher, P. Penczek, J. Zhu, Y. Li, M. Ladjadj, and A. Leith. 1996. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116:190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 9
    • 0036887159 scopus 로고    scopus 로고
    • Sequential model of phage PRD1 DNA delivery: Active involvement of the viral membrane
    • Grahn, A. M., R. Daugelavicius, and D. H. Bamford. 2002. Sequential model of phage PRD1 DNA delivery: active involvement of the viral membrane. Mol. Microbiol. 46:1199-1209.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1199-1209
    • Grahn, A.M.1    Daugelavicius, R.2    Bamford, D.H.3
  • 10
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber, U. F., M. Willetts, P. Webster, and A. Helenius. 1993. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 75:477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 12
    • 4344559453 scopus 로고    scopus 로고
    • The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes
    • Huiskonen, J. T., H. M. Kivela, D. H. Bamford, and S. J. Butcher. 2004. The PM2 virion has a novel organization with an internal membrane and pentameric receptor binding spikes. Nat. Struct. Mol. Biol. 11:850-856.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 850-856
    • Huiskonen, J.T.1    Kivela, H.M.2    Bamford, D.H.3    Butcher, S.J.4
  • 13
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali, B., and S. E. O'Connor. 1999. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3:643-649.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 14
    • 23144463912 scopus 로고    scopus 로고
    • FFAS03: A server for profile-profile sequence alignments
    • DOI 10.1093/nar/gki418
    • Jaroszewski, L., L. Rychlewski, Z. Li, W. Li, and A. Godzik. 2005. FFAS03: a server for profile-profile sequence alignments. Nucleic Acids Res. 33: W284-W288. (Pubitemid 44529927)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS
    • Jaroszewski, L.1    Rychlewski, L.2    Li, Z.3    Li, W.4    Godzik, A.5
  • 15
    • 30044450170 scopus 로고    scopus 로고
    • Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses
    • Khayat, R., L. Tang, E. T. Larson, C. M. Lawrence, M. Young, and J. E. Johnson. 2005. Structure of an archaeal virus capsid protein reveals a common ancestry to eukaryotic and bacterial viruses. Proc. Natl. Acad. Sci. U. S. A. 102:18944-18949.
    • (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
  • 16
    • 3843084996 scopus 로고    scopus 로고
    • Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts
    • Kivelä, H. M., R. Daugelavicius, R. H. Hankkio, J. K. Bamford, and D. H. Bamford. 2004. Penetration of membrane-containing double-stranded-DNA bacteriophage PM2 into Pseudoalteromonas hosts. J. Bacteriol. 186:5342-5354.
    • (2004) J. Bacteriol. , vol.186 , pp. 5342-5354
    • Kivelä, H.M.1    Daugelavicius, R.2    Hankkio, R.H.3    Bamford, J.K.4    Bamford, D.H.5
  • 18
    • 3242670863 scopus 로고    scopus 로고
    • Identification of glycosylation sites in the SU component of the avian sarcoma/leukosis virus envelope glycoprotein (subgroup A) by mass spectrometry
    • Kvaratskhelia, M., P. K. Clark, S. Hess, D. C. Melder, M. J. Federspiel, and S. H. Hughes. 2004. Identification of glycosylation sites in the SU component of the avian sarcoma/leukosis virus envelope glycoprotein (subgroup A) by mass spectrometry. Virology 326:171-181.
    • (2004) Virology , vol.326 , pp. 171-181
    • Kvaratskhelia, M.1    Clark, P.K.2    Hess, S.3    Melder, D.C.4    Federspiel, M.J.5    Hughes, S.H.6
  • 20
    • 27944481316 scopus 로고    scopus 로고
    • Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35
    • Laurinmäki, P. A., J. T. Huiskonen, D. H. Bamford, and S. J. Butcher. 2005. Membrane proteins modulate the bilayer curvature in the bacterial virus Bam35. Structure 13:1819-1828.
    • (2005) Structure , vol.13 , pp. 1819-1828
    • Laurinmäki, P.A.1    Huiskonen, J.T.2    Bamford, D.H.3    Butcher, S.J.4
  • 21
    • 0032190305 scopus 로고    scopus 로고
    • Analytical shape computation of macromolecules. I. Molecular area and volume through alpha shape
    • Liang, J., H. Edelsbrunner, P. Fu, P. V. Sudhakar, and S. Subramaniam. 1998. Analytical shape computation of macromolecules. I. Molecular area and volume through alpha shape. Proteins 33:1-17.
    • (1998) Proteins , vol.33 , pp. 1-17
    • Liang, J.1    Edelsbrunner, H.2    Fu, P.3    Sudhakar, P.V.4    Subramaniam, S.5
  • 22
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke, S. J., P. R. Baldwin, and W. Chiu. 1999. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 23
    • 33746210122 scopus 로고    scopus 로고
    • Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life
    • Maaty, W. S., A. C. Ortmann, M. Dlakic, K. Schulstad, J. K. Hilmer, L. Liepold, B. Weidenheft, R. Khayat, T. Douglas, M. J. Young, and B. Bothner. 2006. Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life. J. Virol. 80:7625-7635.
    • (2006) J. Virol. , vol.80 , pp. 7625-7635
    • Maaty, W.S.1    Ortmann, A.C.2    Dlakic, M.3    Schulstad, K.4    Hilmer, J.K.5    Liepold, L.6    Weidenheft, B.7    Khayat, R.8    Douglas, T.9    Young, M.J.10    Bothner, B.11
  • 26
    • 34248532415 scopus 로고    scopus 로고
    • PROMALS: Towards accurate multiple sequence alignments of distantly related proteins
    • Pei, J., and N. V. Grishin. 2007. PROMALS: towards accurate multiple sequence alignments of distantly related proteins. Bioinformatics 23:802-808.
    • (2007) Bioinformatics , vol.23 , pp. 802-808
    • Pei, J.1    Grishin, N.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.