메뉴 건너뛰기




Volumn , Issue , 2008, Pages 321-328

Birnaviruses

(1)  Delmas, B a  


Author keywords

Birnavirus; BSNV; Capsid protein; DsRNA genome; DXV; IBDV; IPNV; Picobirnavirus; Polyprotein; Polyprotein processing; RNA polymerase; Taxonomy; Viral evoltion; Viral peptide; Viral protease

Indexed keywords


EID: 84860142368     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012374410-4.00350-2     Document Type: Chapter
Times cited : (5)

References (16)
  • 1
    • 0034602847 scopus 로고    scopus 로고
    • A non-canonical Lon proteinase lacking the ATPase domain employs the ser-lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus
    • Birghan C., Mundt E., Gorbalenya A.E. A non-canonical Lon proteinase lacking the ATPase domain employs the ser-lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus. EMBO Journal 2000, 19:114.
    • (2000) EMBO Journal , vol.19 , pp. 114
    • Birghan, C.1    Mundt, E.2    Gorbalenya, A.E.3
  • 2
    • 25144487718 scopus 로고    scopus 로고
    • Structural peptides of a nonenveloped virus are involved in assembly and membrane translocation
    • Chevalier C., Galloux M., Pous J., et al. Structural peptides of a nonenveloped virus are involved in assembly and membrane translocation. Journal of Virology 2005, 79:12253.
    • (2005) Journal of Virology , vol.79 , pp. 12253
    • Chevalier, C.1    Galloux, M.2    Pous, J.3
  • 3
    • 17644376907 scopus 로고    scopus 로고
    • The birnavirus crystal structure reveals structural relationships among icosahedral viruses
    • Coulibaly F., Chevalier C., Gutsche I., et al. The birnavirus crystal structure reveals structural relationships among icosahedral viruses. Cell 2005, 120:761.
    • (2005) Cell , vol.120 , pp. 761
    • Coulibaly, F.1    Chevalier, C.2    Gutsche, I.3
  • 5
    • 33745041491 scopus 로고    scopus 로고
    • Crystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism
    • Feldman A.R., Lee J., Delmas B., et al. Crystal structure of a novel viral protease with a serine/lysine catalytic dyad mechanism. Journal of Molecular Biology 2006, 358:1378.
    • (2006) Journal of Molecular Biology , vol.358 , pp. 1378
    • Feldman, A.R.1    Lee, J.2    Delmas, B.3
  • 7
    • 2642653222 scopus 로고    scopus 로고
    • Prevalence of enteric viruses in human immunodeficiency virus seropositive patients in Venezuela
    • Gonzalez G.G., Pujol F.H., Liprandi F., et al. Prevalence of enteric viruses in human immunodeficiency virus seropositive patients in Venezuela. Journal of Medical Virology 1998, 55:288.
    • (1998) Journal of Medical Virology , vol.55 , pp. 288
    • Gonzalez, G.G.1    Pujol, F.H.2    Liprandi, F.3
  • 8
    • 0036434498 scopus 로고    scopus 로고
    • The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage
    • Gorbalenya A.E., Pringle F.M., Zeddam J.-L., et al. The palm subdomain-based active site is internally permuted in viral RNA-dependent RNA polymerases of an ancient lineage. Journal of Molecular Biology 2002, 324:47.
    • (2002) Journal of Molecular Biology , vol.324 , pp. 47
    • Gorbalenya, A.E.1    Pringle, F.M.2    Zeddam, J.-L.3
  • 9
    • 33645218567 scopus 로고    scopus 로고
    • Nonstructural protein of infectious bursal disease virus inhibits apoptosis at the early stage of virus infection
    • Liu M., Vakharia V.N. Nonstructural protein of infectious bursal disease virus inhibits apoptosis at the early stage of virus infection. Journal of Virology 2006, 80:3369.
    • (2006) Journal of Virology , vol.80 , pp. 3369
    • Liu, M.1    Vakharia, V.N.2
  • 10
    • 0034715855 scopus 로고    scopus 로고
    • VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane and induces cell lysis
    • Lombardo E., Maraver A., Espinosa I., et al. VP5, the nonstructural polypeptide of infectious bursal disease virus, accumulates within the host plasma membrane and induces cell lysis. Virology 2000, 277:345.
    • (2000) Virology , vol.277 , pp. 345
    • Lombardo, E.1    Maraver, A.2    Espinosa, I.3
  • 13
    • 21744450430 scopus 로고    scopus 로고
    • The structural polymorphism of the major capsid protein of a double-stranded RNA virus: An amphipathic helix as a molecular switch
    • Saugar I., Luque D., Ona A., et al. The structural polymorphism of the major capsid protein of a double-stranded RNA virus: An amphipathic helix as a molecular switch. Structure 2005, 13:1007.
    • (2005) Structure , vol.13 , pp. 1007
    • Saugar, I.1    Luque, D.2    Ona, A.3
  • 14
    • 0036828149 scopus 로고    scopus 로고
    • Infectious bursal disease virus capsid protein VP3 interacts both with VP1, the RNA-dependent RNA polymerase, and with viral double-stranded RNA
    • Tacken M.G., Peeters B.P., Thomas A.A., et al. Infectious bursal disease virus capsid protein VP3 interacts both with VP1, the RNA-dependent RNA polymerase, and with viral double-stranded RNA. Journal of Virology 2002, 76:11301.
    • (2002) Journal of Virology , vol.76 , pp. 11301
    • Tacken, M.G.1    Peeters, B.P.2    Thomas, A.A.3
  • 15
    • 31144459030 scopus 로고    scopus 로고
    • RNA viral community in human feces: Prevalence of plant pathogenic viruses
    • Zhang T., Breitbart M., Lee W.H., et al. RNA viral community in human feces: Prevalence of plant pathogenic viruses. PLoS Biology 2006, 4:108.
    • (2006) PLoS Biology , vol.4 , pp. 108
    • Zhang, T.1    Breitbart, M.2    Lee, W.H.3
  • 16
    • 85069924159 scopus 로고    scopus 로고
    • MEROPS, Peptidase Database
    • MEROPS, Peptidase Database. http://merops.sanger.ac.uk.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.