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Volumn 85, Issue 10, 2011, Pages 4691-4697

Structure of Bombyx mori densovirus 1, a silkworm pathogen

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN VP3;

EID: 79955425835     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02688-10     Document Type: Article
Times cited : (24)

References (36)
  • 2
    • 0021740133 scopus 로고
    • Virion orientation in cubic crystals of the human common cold virus HRV14
    • Arnold, E., et al. 1984. Virion orientation in cubic crystals of the human common cold virus HRV14. J. Mol. Biol. 177:417-430.
    • (1984) J. Mol. Biol. , vol.177 , pp. 417-430
    • Arnold, E.1
  • 4
    • 9744228738 scopus 로고    scopus 로고
    • Does common architecture reveal a viral lineage spanning all three domains of life?
    • Benson, S. D., J. K. Bamford, D. H. Bamford, and R. M. Burnett. 2004. Does common architecture reveal a viral lineage spanning all three domains of life? Mol. Cell 16:673-685.
    • (2004) Mol. Cell , vol.16 , pp. 673-685
    • Benson, S.D.1    Bamford, J.K.2    Bamford, D.H.3    Burnett, R.M.4
  • 5
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brünger, A. T. 2007. Version 1.2 of the Crystallography and NMR system. Nat. Protoc. 2:2728-2733.
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brünger, A.T.1
  • 6
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brünger, A. T., et al. 1998. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54:905-921.
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 7
    • 2442507712 scopus 로고    scopus 로고
    • Interfacial enzymology of parvovirus phospholipases A2
    • Canaan, S., et al. 2004. Interfacial enzymology of parvovirus phospholipases A2. J. Biol. Chem. 279:14502-14508.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14502-14508
    • Canaan, S.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50:760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 10
    • 28044448698 scopus 로고    scopus 로고
    • Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry
    • Farr, G. A., L. G. Zhang, and P. Tattersall. 2005. Parvoviral virions deploy a capsid-tethered lipolytic enzyme to breach the endosomal membrane during cell entry. Proc. Natl. Acad. Sci. U. S. A. 102:17148-17153.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17148-17153
    • Farr, G.A.1    Zhang, L.G.2    Tattersall, P.3
  • 11
    • 0036246727 scopus 로고    scopus 로고
    • The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity
    • Girod, A., et al. 2002. The VP1 capsid protein of adeno-associated virus type 2 is carrying a phospholipase A2 domain required for virus infectivity. J. Gen. Virol. 83:973-978.
    • (2002) J. Gen. Virol. , vol.83 , pp. 973-978
    • Girod, A.1
  • 12
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 13
    • 77957940075 scopus 로고    scopus 로고
    • The structure of Penaeus stylirostris densovirus, a shrimp pathogen
    • Kaufmann, B., et al. 2010. The structure of Penaeus stylirostris densovirus, a shrimp pathogen. J. Virol. 84:11289-11296.
    • (2010) J. Virol. , vol.84 , pp. 11289-11296
    • Kaufmann, B.1
  • 15
    • 0031574325 scopus 로고    scopus 로고
    • Not your average density
    • Kleywegt, G. J., and R. J. Read. 1997. Not your average density. Structure 5:1557-1569.
    • (1997) Structure , vol.5 , pp. 1557-1569
    • Kleywegt, G.J.1    Read, R.J.2
  • 16
    • 0000243829 scopus 로고
    • Procheck-a program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. Procheck-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 17
    • 0034782919 scopus 로고    scopus 로고
    • Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid
    • Li, Y., et al. 2001. Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid. J. Gen. Virol. 82:2821-2825.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2821-2825
    • Li, Y.1
  • 19
    • 17644446136 scopus 로고    scopus 로고
    • A beta-stranded motif drives capsid protein oligomers of the parvovi-rus minute virus of mice into the nucleus for viral assembly
    • Lombardo, E., J. C. Ramírez, M. Agbandje-McKenna, and J. M. Almendral. 2000. A beta-stranded motif drives capsid protein oligomers of the parvovi-rus minute virus of mice into the nucleus for viral assembly. J. Virol. 74: 3804-3814.
    • (2000) J. Virol. , vol.74 , pp. 3804-3814
    • Lombardo, E.1    Ramírez, J.C.2    Agbandje-Mckenna, M.3    Almendral, J.M.4
  • 20
    • 0037069358 scopus 로고    scopus 로고
    • The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus
    • Nandhagopal, N., et al. 2002. The structure and evolution of the major capsid protein of a large, lipid-containing DNA virus. Proc. Natl. Acad. Sci. U. S. A. 99:14758-14763.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 14758-14763
    • Nandhagopal, N.1
  • 21
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Charles W. Carter, Jr. (ed.), Academic Press, San Diego, CA
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode, p. 307-326. In Charles W. Carter, Jr. (ed.), Methods Enzymol., vol. 276. Academic Press, San Diego, CA.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F., et al. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Computat. Chem. 25:1605-1612.
    • (2004) J. Computat. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 23
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. Sect. A 42:140-149.
    • (1986) Acta Crystallogr. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 24
    • 33644943804 scopus 로고    scopus 로고
    • Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid
    • Riolobos, L., J. Reguera, M. G. Mateu, and J. M. Almendral. 2006. Nuclear transport of trimeric assembly intermediates exerts a morphogenetic control on the icosahedral parvovirus capsid. J. Mol. Biol. 357:1026-1038.
    • (2006) J. Mol. Biol. , vol.357 , pp. 1026-1038
    • Riolobos, L.1    Reguera, J.2    Mateu, M.G.3    Almendral, J.M.4
  • 25
    • 78649992830 scopus 로고    scopus 로고
    • The human rhinovirus: Human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery
    • Rollinger, J. M., and M. Schmidtke. 2011. The human rhinovirus: human-pathological impact, mechanisms of antirhinoviral agents, and strategies for their discovery. Med. Res. Rev. 31:42-92.
    • (2011) Med. Res. Rev. , vol.31 , pp. 42-92
    • Rollinger, J.M.1    Schmidtke, M.2
  • 26
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann, M. G., and D. M. Blow. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr. 15:24-31.
    • (1962) Acta Crystallogr , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 28
    • 85010233872 scopus 로고
    • Pathogenicity of an infectious flacherie virus of the silkworm, Bombyx mori, obtained from sericultural farms in the suburbs of Ina city
    • Shimizu, T. 1975. Pathogenicity of an infectious flacherie virus of the silkworm, Bombyx mori, obtained from sericultural farms in the suburbs of Ina city. J. Seric. Sci. Jpn. 44:45-48.
    • (1975) J. Seric. Sci. Jpn. , vol.44 , pp. 45-48
    • Shimizu, T.1
  • 29
    • 0032533456 scopus 로고    scopus 로고
    • The structure of an insect parvovirus (Galleria mellonella denso-virus) at 3.7 Å resolution
    • Simpson, A. A., P. R. Chipman, T. S. Baker, P. Tijssen, and M. G. Rossmann. 1998. The structure of an insect parvovirus (Galleria mellonella denso-virus) at 3.7 Å resolution. Structure 6:1355-1367.
    • (1998) Structure , vol.6 , pp. 1355-1367
    • Simpson, A.A.1    Chipman, P.R.2    Baker, T.S.3    Tijssen, P.4    Rossmann, M.G.5
  • 30
    • 0036304301 scopus 로고    scopus 로고
    • The structure of porcine parvovirus: Comparison with related viruses
    • Simpson, A. A., et al. 2002. The structure of porcine parvovirus: comparison with related viruses. J. Mol. Biol. 315:1189-1198.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1189-1198
    • Simpson, A.A.1
  • 31
    • 79955410210 scopus 로고    scopus 로고
    • Parvoviridae
    • A. M. Q. King, M. J. Adams, E. Carstens, and E. J. Lefkowitz (ed.), Ninth report of the International Committee on Taxonomy of Viruses, in press. Elsevier, San Diego, CA
    • Tijssen, P., et al. Parvoviridae. In A. M. Q. King, M. J. Adams, E. Carstens, and E. J. Lefkowitz (ed.), Virus taxonomy: classification and nomenclature of viruses. Ninth report of the International Committee on Taxonomy of Viruses, in press. Elsevier, San Diego, CA.
    • Virus taxonomy: Classification and nomenclature of viruses
    • Tijssen, P.1
  • 33
    • 0025774451 scopus 로고
    • The three-dimensional structure of canine parvovirus and its functional implications
    • Tsao, J., et al. 1991. The three-dimensional structure of canine parvovirus and its functional implications. Science 251:1456-1464.
    • (1991) Science , vol.251 , pp. 1456-1464
    • Tsao, J.1
  • 34
    • 0036678455 scopus 로고    scopus 로고
    • The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy
    • Xie, Q., et al. 2002. The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy. Proc. Natl. Acad. Sci. U. S. A. 99:10405- 10410.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10405-10410
    • Xie, Q.1
  • 35
    • 0030573015 scopus 로고    scopus 로고
    • Canine parvovirus capsid structure, analyzed at 2.9 Å resolution
    • Xie, Q., and M. S. Chapman. 1996. Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol. 264:497-520.
    • (1996) J. Mol. Biol. , vol.264 , pp. 497-520
    • Xie, Q.1    Chapman, M.S.2
  • 36
    • 0035431876 scopus 로고    scopus 로고
    • A viral phospholipase A2 is required for parvovirus infectivity
    • Zadori, Z., et al. 2001. A viral phospholipase A2 is required for parvovirus infectivity. Dev. Cell 1:291-302.
    • (2001) Dev. Cell , vol.1 , pp. 291-302
    • Zadori, Z.1


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