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Volumn 1, Issue 3, 2013, Pages

Complete genome sequence of a rabies virus isolate from a ferret badger (Melogale moschata) in Jiangxi, China

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EID: 84997235743     PISSN: None     EISSN: 21698287     Source Type: Journal    
DOI: 10.1128/genomeA.00192-13     Document Type: Article
Times cited : (4)

References (12)
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  • 4
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    • Characterization of a rabies virus isolate from a ferret badger (Melogale moschata) with unique molecular differences in glycoprotein antigenic site III
    • Zhang S, Zhao J, Liu Y, Fooks AR, Zhang F, Hu R. 2010. Characterization of a rabies virus isolate from a ferret badger (Melogale moschata) with unique molecular differences in glycoprotein antigenic site III. Virus Res. 149:143-151.
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    • Zhang, S.1    Zhao, J.2    Liu, Y.3    Fooks, A.R.4    Zhang, F.5    Hu, R.6
  • 7
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    • Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein
    • Seif I, Coulon P, Rollin PE, Flamand A. 1985. Rabies virulence: effect on pathogenicity and sequence characterization of rabies virus mutations affecting antigenic site III of the glycoprotein. J. Virol. 53:926-934.
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    • Seif, I.1    Coulon, P.2    Rollin, P.E.3    Flamand, A.4
  • 8
    • 27644521445 scopus 로고    scopus 로고
    • A single amino acid change in rabies virus glycoprotein increases virus spread and enhances virus pathogenicity
    • Faber M, Faber ML, Papaneri A, Bette M, Weihe E, Dietzschold B, Schnell MJ. 2005. A single amino acid change in rabies virus glycoprotein increases virus spread and enhances virus pathogenicity. J. Virol. 79: 14141-14148.
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    • 33646803010 scopus 로고    scopus 로고
    • A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein
    • Takayama-Ito M, Inoue K, Shoji Y, Inoue S, Iijima T, Sakai T, Kurane I, Morimoto K. 2006. A highly attenuated rabies virus HEP-Flury strain reverts to virulent by single amino acid substitution to arginine at position 333 in glycoprotein. Virus Res. 119:208-215.
    • (2006) Virus Res , vol.119 , pp. 208-215
    • Takayama-Ito, M.1    Inoue, K.2    Shoji, Y.3    Inoue, S.4    Iijima, T.5    Sakai, T.6    Kurane, I.7    Morimoto, K.8
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    • Faber, M.1    Faber, M.L.2    Li, J.3    Preuss, M.A.4    Schnell, M.J.5    Dietzschold, B.6
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    • Molecular basis of neurovirulence of Flury rabies virus vaccine strains: importance of the polymerase and the glycoprotein R333Q mutation
    • Tao L, Ge J, Wang X, Zhai H, Hua T, Zhao B, Kong D, Yang C, Chen H, Bu Z. 2010. Molecular basis of neurovirulence of Flury rabies virus vaccine strains: importance of the polymerase and the glycoprotein R333Q mutation. J. Virol. 84:8926-8936.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.