메뉴 건너뛰기




Volumn 109, Issue 13, 2012, Pages 5046-5051

Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses

Author keywords

Structure biology; Virology

Indexed keywords

ANTIVIRUS AGENT; ENDONUCLEASE; SINGLE STRANDED RNA; VIRUS NUCLEOPROTEIN;

EID: 84859452102     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1200808109     Document Type: Article
Times cited : (95)

References (29)
  • 1
  • 2
    • 29444442652 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus
    • DOI 10.2174/156652405774962335
    • Flick R, Whitehouse CA (2005) Crimean-Congo hemorrhagic fever virus. Curr Mol Med 5:753-760. (Pubitemid 43009515)
    • (2005) Current Molecular Medicine , vol.5 , Issue.8 , pp. 753-760
    • Flick, R.1    Whitehouse, C.A.2
  • 3
    • 77249172863 scopus 로고    scopus 로고
    • Serial expression of the truncated fragments of the nucleocapsid protein of CCHFV and identification of the epitope region
    • Wei PF, et al. (2010) Serial expression of the truncated fragments of the nucleocapsid protein of CCHFV and identification of the epitope region. Virol Sin 25:45-51.
    • (2010) Virol Sin , vol.25 , pp. 45-51
    • Wei, P.F.1
  • 4
    • 37049039706 scopus 로고    scopus 로고
    • RNA binding domain of Jamestown Canyon virus S segment RNAs
    • Ogg MMPJ, Patterson JL (2007) RNA binding domain of Jamestown Canyon virus S segment RNAs. J Virol 81:13754-13760.
    • (2007) J Virol , vol.81 , pp. 13754-13760
    • Ogg, M.1    Patterson, J.L.2
  • 5
    • 0033771070 scopus 로고    scopus 로고
    • RNA binding properties of bunyamwera virus nucleocapsid protein and selective binding to an element in the 5′ terminus of the negative-sense S segment
    • Osborne JCER, Elliott RM (2000) RNA binding properties of bunyamwera virus nucleocapsid protein and selective binding to an element in the 5′ terminus of the negative-sense S segment. J Virol 74:9946-9952.
    • (2000) J Virol , vol.74 , pp. 9946-9952
    • Osborne, J.1    Elliott, R.M.2
  • 6
    • 33750682047 scopus 로고    scopus 로고
    • Hantavirus N protein exhibits genus-specific recognition of the viral RNA Panhandle
    • DOI 10.1128/JVI.00820-06
    • Mir MABB, Brown B, Hjelle B, Duran WA, Panganiban AT (2006) Hantavirus Nprotein exhibits genus-specific recognition of the viral RNA panhandle. J Virol 80:11283-11292. (Pubitemid 44706568)
    • (2006) Journal of Virology , vol.80 , Issue.22 , pp. 11283-11292
    • Mir, M.A.1    Brown, B.2    Hjelle, B.3    Duran, W.A.4    Panganiban, A.T.5
  • 7
    • 60849134280 scopus 로고    scopus 로고
    • Investigating the specificity and stoichiometry of RNA binding by the nucleocapsid protein of Bunyamwera virus
    • Mohl BPBJ, Barr JN (2009) Investigating the specificity and stoichiometry of RNA binding by the nucleocapsid protein of Bunyamwera virus. RNA 15:391-399.
    • (2009) RNA , vol.15 , pp. 391-399
    • Mohl, B.1    Barr, J.N.2
  • 9
    • 79958061217 scopus 로고    scopus 로고
    • The hexamer structure of Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes
    • Ferron F, et al. (2011) The hexamer structure of Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes. PLoS Pathog 7:e1002030.
    • (2011) PLoS Pathog , vol.7
    • Ferron, F.1
  • 10
    • 77955348510 scopus 로고    scopus 로고
    • Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation
    • Raymond DD, Piper ME, Gerrard SR, Smith JL (2010) Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation. Proc Natl Acad Sci USA 107:11769-11774.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 11769-11774
    • Raymond, D.D.1    Piper, M.E.2    Gerrard, S.R.3    Smith, J.L.4
  • 11
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design
    • Ng AK, et al. (2008) Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine design. FASEB J 22:3638-3647.
    • (2008) FASEB J , vol.22 , pp. 3638-3647
    • Ng, A.K.1
  • 12
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • DOI 10.1038/nature05379, PII NATURE05379
    • Ye Q, Krug RM, Tao YJ (2006) The mechanism bywhich influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444:1078-1082. (Pubitemid 46018528)
    • (2006) Nature , vol.444 , Issue.7122 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 14
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • DOI 10.1126/science.1126953
    • Green TJ, Zhang X, Wertz GW, Luo M (2006) Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313:357-360. (Pubitemid 44480961)
    • (2006) Science , vol.313 , Issue.5785 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wartz, G.W.3    Luo, M.4
  • 16
    • 79952303123 scopus 로고    scopus 로고
    • Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3′ to 5′ exonuclease activity essential for immune suppression
    • Hastie KM, Kimberlin CR, Zandonatti MA, MacRae IJ, Saphire EO (2011) Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3′ to 5′ exonuclease activity essential for immune suppression. Proc Natl Acad Sci USA 108:2396-2401.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2396-2401
    • Hastie, K.M.1    Kimberlin, C.R.2    Zandonatti, M.A.3    MacRae, I.J.4    Saphire, E.O.5
  • 17
    • 82755167958 scopus 로고    scopus 로고
    • Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding
    • Hastie KM, et al. (2011) Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding. Proc Natl Acad Sci USA 108:19365-19370.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 19365-19370
    • Hastie, K.M.1
  • 18
    • 78650132935 scopus 로고    scopus 로고
    • Cap binding and immune evasion revealed by Lassa nucleoprotein structure
    • Qi X, et al. (2010) Cap binding and immune evasion revealed by Lassa nucleoprotein structure. Nature 468:779-783.
    • (2010) Nature , vol.468 , pp. 779-783
    • Qi, X.1
  • 19
    • 84859465121 scopus 로고    scopus 로고
    • A scaffolded DNA origami algorithm for polygon network structures and hollow three-dimensional structures
    • Fu YM, Zeng DD, Huang Q, Fan CH (2010) A scaffolded DNA origami algorithm for polygon network structures and hollow three-dimensional structures. Acta Biophys Sin 26:750-758.
    • (2010) Acta Biophys Sin , vol.26 , pp. 750-758
    • Fu, Y.M.1    Zeng, D.D.2    Huang, Q.3    Fan, C.H.4
  • 20
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Holm, L.1    Rosenstrom, P.2
  • 21
    • 34447299235 scopus 로고    scopus 로고
    • Arenaviridae: The viruses and their replication
    • eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia), 5th Ed
    • Buchmeier MJ, Peters CJ, de la Torre JC (2007) Arenaviridae: The viruses and their replication. Fields Virology, eds Knipe DM, Howley PM (Lippincott Williams & Wilkins, Philadelphia), 5th Ed, pp 1791-1827.
    • (2007) Fields Virology , pp. 1791-1827
    • Buchmeier, M.J.1    Peters, C.J.2    De La Torre, J.C.3
  • 23
    • 36048934428 scopus 로고    scopus 로고
    • Differential inhibition of type I interferon induction by arenavirus nucleoproteins
    • DOI 10.1128/JVI.00882-07
    • Martínez-Sobrido L, Giannakas P, Cubitt B, García-Sastre A, de la Torre JC (2007) Differential inhibition of type I interferon induction by arenavirus nucleoproteins. J Virol 81:12696-12703. (Pubitemid 350085885)
    • (2007) Journal of Virology , vol.81 , Issue.22 , pp. 12696-12703
    • Martinez-Sobrido, L.1    Giannakas, P.2    Cubitt, B.3    Garcia-Sastre, A.4    De La, T.J.C.5
  • 24
    • 79952812440 scopus 로고    scopus 로고
    • Induction of caspase activation and cleavage of the viral nucleocapsid protein in different cell types during Crimean-Congo hemorrhagic fever virus infection
    • Karlberg H, Tan YJ, Mirazimi A (2011) Induction of caspase activation and cleavage of the viral nucleocapsid protein in different cell types during Crimean-Congo hemorrhagic fever virus infection. J Biol Chem 286:3227-3234.
    • (2011) J Biol Chem , vol.286 , pp. 3227-3234
    • Karlberg, H.1    Tan, Y.J.2    Mirazimi, A.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • eds Carter CW, Sweet RM (Academic, New York)
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography, Part A, Methods in Enzymology, eds Carter CW, Sweet RM (Academic, New York), Vol 276, pp 307-326.
    • (1997) Macromolecular Crystallography, Part A, Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 28
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R, MacArthur M, Moss D, Thornton J (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3    Thornton, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.