메뉴 건너뛰기




Volumn 158, Issue 11, 2013, Pages 2273-2284

Characterization of Dak Nong virus, an insect nidovirus isolated from Culex mosquitoes in Vietnam

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS PROTEIN;

EID: 84886720152     PISSN: 03048608     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00705-013-1741-4     Document Type: Article
Times cited : (26)

References (49)
  • 2
    • 84863109422 scopus 로고    scopus 로고
    • Ratification vote on taxonomic proposals to the International Committee on Taxonomy of Viruses
    • Adams MJ, Carstens EB (2012) Ratification vote on taxonomic proposals to the International Committee on Taxonomy of Viruses. Arch Virol 157: 1411-1422.
    • (2012) Arch Virol , vol.157 , pp. 1411-1422
    • Adams, M.J.1    Carstens, E.B.2
  • 4
    • 84861148370 scopus 로고    scopus 로고
    • Genetic analysis of a novel nidovirus from fathead minnows
    • Batts WN, Goodwin AE, Winton JR (2012) Genetic analysis of a novel nidovirus from fathead minnows. J Gen Virol 93: 1247-1252.
    • (2012) J Gen Virol , vol.93 , pp. 1247-1252
    • Batts, W.N.1    Goodwin, A.E.2    Winton, J.R.3
  • 6
    • 33744789955 scopus 로고    scopus 로고
    • Nidovirus transcription: how to make sense?
    • Pasternak AO, Spaan WJ, Snijder EJ (2006) Nidovirus transcription: how to make sense? J Gen Virol 87: 1403-1421.
    • (2006) J Gen Virol , vol.87 , pp. 1403-1421
    • Pasternak, A.O.1    Spaan, W.J.2    Snijder, E.J.3
  • 13
    • 0009134123 scopus 로고
    • A new continuous cell line from larvae of the mosquito Aedes albopictus (Diptera Culicidae)
    • Mitsuhashi J (1981) A new continuous cell line from larvae of the mosquito Aedes albopictus (Diptera Culicidae). Biochem Res 2: 599-606.
    • (1981) Biochem Res , vol.2 , pp. 599-606
    • Mitsuhashi, J.1
  • 16
    • 0021324979 scopus 로고
    • Electron microscopic observation of a newly isolated flavivirus-like virus from field-captured mosquitoes
    • Okuno Y, Igarashi A, Fukunaga T, Tadano M, Fukai K (1984) Electron microscopic observation of a newly isolated flavivirus-like virus from field-captured mosquitoes. J Gen Virol 65: 803-807.
    • (1984) J Gen Virol , vol.65 , pp. 803-807
    • Okuno, Y.1    Igarashi, A.2    Fukunaga, T.3    Tadano, M.4    Fukai, K.5
  • 18
    • 77954110202 scopus 로고    scopus 로고
    • DotKnot: pseudoknot prediction using the probability dot plot under a refined energy model
    • Sperschneider J, Datta A (2010) DotKnot: pseudoknot prediction using the probability dot plot under a refined energy model. Nucleic Acids Res 38: e103.
    • (2010) Nucleic Acids Res , vol.38
    • Sperschneider, J.1    Datta, A.2
  • 19
    • 78650483876 scopus 로고    scopus 로고
    • Heuristic RNA pseudoknot prediction including intramolecular kissing hairpins
    • Sperschneider J, Datta A, Wise MJ (2011) Heuristic RNA pseudoknot prediction including intramolecular kissing hairpins. RNA 17: 27-38.
    • (2011) Rna , vol.17 , pp. 27-38
    • Sperschneider, J.1    Datta, A.2    Wise, M.J.3
  • 20
    • 0000207681 scopus 로고
    • TMbase-A database of membrane spanning proteins segments
    • Hofmann K, Stoffel W (1993) TMbase-A database of membrane spanning proteins segments. Biol Chem Hoppe-Seyler 374: 166.
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 21
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden markov model: application to complete genomes
    • Anders K, Bjorn L, Gunnar von H, Erik LLS (2001) Predicting transmembrane protein topology with a hidden markov model: application to complete genomes. J Mol Biol 305: 567-580.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Anders, K.1    Bjorn, L.2    von Gunnar, H.3    Erik, L.L.S.4
  • 22
    • 80053345905 scopus 로고    scopus 로고
    • SignalP 4.0: discriminating signal peptides from transmembrane regions
    • Petersen TN, Brunak S, von Heijne G, Nielsen H (2011) SignalP 4. 0: discriminating signal peptides from transmembrane regions. Nat Methods 8: 785-786.
    • (2011) Nat Methods , vol.8 , pp. 785-786
    • Petersen, T.N.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 23
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P, Brunak S, Blom N (2004) Prediction of proprotein convertase cleavage sites. Protein Eng Des Sel 17: 107-112.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 24
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, van Dyke M, Stock J (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164.
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    van Dyke, M.2    Stock, J.3
  • 25
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: Improved prediction of coiled coils from sequence
    • McDonnell AV, Jiang T, Keating AE, Berger B (2006) Paircoil2: Improved prediction of coiled coils from sequence. Bioinformatics 22: 356-358.
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.V.1    Jiang, T.2    Keating, A.E.3    Berger, B.4
  • 26
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: web server for predicting protein binding regions in disordered proteins
    • Dosztány Z, Mészáros B, Simon I (2009) ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics 15: 2745-2746.
    • (2009) Bioinformatics , vol.15 , pp. 2745-2746
    • Dosztány, Z.1    Mészáros, B.2    Simon, I.3
  • 27
    • 0001868907 scopus 로고
    • Comparative analysis of amino acid sequences of the key enzymes of the replication and expression of positive-strand RNA viruses: validity of the approach and functional and evolutionary implications
    • Gorbalenya AE, Koonin EV (1993) Comparative analysis of amino acid sequences of the key enzymes of the replication and expression of positive-strand RNA viruses: validity of the approach and functional and evolutionary implications. SoV Sci Rev D Physicochem Biol 11: 1-84.
    • (1993) SoV Sci Rev D Physicochem Biol , vol.11 , pp. 1-84
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 29
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F, Huelsenbeck JP (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19: 1572-1574.
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 30
    • 0035031966 scopus 로고    scopus 로고
    • A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach
    • Whelan S, Goldman N (2001) A general empirical model of protein evolution derived from multiple protein families using a maximum-likelihood approach. Mol Biol Evol 18: 691-699.
    • (2001) Mol Biol Evol , vol.18 , pp. 691-699
    • Whelan, S.1    Goldman, N.2
  • 31
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 32
    • 0003437302 scopus 로고    scopus 로고
    • Distributed by the author. Department of Genome Sciences, University of Washington, Seattle
    • Felsenstein J (2005) PHYLIP (Phylogeny Inference Package) version 3. 6. Distributed by the author. Department of Genome Sciences, University of Washington, Seattle.
    • (2005) PHYLIP (Phylogeny Inference Package) version 3. 6
    • Felsenstein, J.1
  • 33
    • 0000461280 scopus 로고
    • Confidence-limits on phylogenies - an approach using the bootstrap
    • Felsenstein J (1985) Confidence-limits on phylogenies - an approach using the bootstrap. Evolution 39: 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 34
    • 0013212130 scopus 로고    scopus 로고
    • University of Glasgow, Glasgow, UK
    • Page RDM (2001) TreeView Version 1. 6. 6. University of Glasgow, Glasgow, UK. http://taxonomy. zoology. gla. ac. uk/rod/treeview. html.
    • (2001) TreeView Version 1. 6. 6
    • Page, R.D.M.1
  • 36
  • 37
    • 66149091584 scopus 로고    scopus 로고
    • Biochemical characterization of arterivirus nonstructural protein 11 reveals the nidovirus-wide conservation of a replicative endoribonuclease
    • Nedialkova DD, Ulferts R, van den Born E, Lauber C, Gorbalenya AE, Ziebuhr J, Snijder EJ (2009) Biochemical characterization of arterivirus nonstructural protein 11 reveals the nidovirus-wide conservation of a replicative endoribonuclease. J Virol 83: 5671-5682.
    • (2009) J Virol , vol.83 , pp. 5671-5682
    • Nedialkova, D.D.1    Ulferts, R.2    van den Born, E.3    Lauber, C.4    Gorbalenya, A.E.5    Ziebuhr, J.6    Snijder, E.J.7
  • 38
    • 3543096771 scopus 로고    scopus 로고
    • The gene encoding the nucleocapsid protein of Gill-associated nidovirus of Penaeus monodon prawns is located upstream of the glycoprotein gene
    • Cowley JA, Cadogan LC, Spann KM, Sittidilokratna N, Walker PJ (2004) The gene encoding the nucleocapsid protein of Gill-associated nidovirus of Penaeus monodon prawns is located upstream of the glycoprotein gene. J Virol 78: 8935-8941.
    • (2004) J Virol , vol.78 , pp. 8935-8941
    • Cowley, J.A.1    Cadogan, L.C.2    Spann, K.M.3    Sittidilokratna, N.4    Walker, P.J.5
  • 39
    • 32344436343 scopus 로고    scopus 로고
    • Structural and antigenic analysis of the yellow head virus nucleocapsid protein p20
    • Sittidilokratna N, Phetchampai N, Boonsaeng V, Walker PJ (2006) Structural and antigenic analysis of the yellow head virus nucleocapsid protein p20. Virus Res 116: 21-29.
    • (2006) Virus Res , vol.116 , pp. 21-29
    • Sittidilokratna, N.1    Phetchampai, N.2    Boonsaeng, V.3    Walker, P.J.4
  • 40
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: structures, evolution, and diversification
    • Massova I, Kotra LP, Fridman R, Mobashery S (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB J 12: 1075-1095.
    • (1998) FASEB J , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 41
    • 0042208243 scopus 로고    scopus 로고
    • The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex
    • Bosch BJ, van der Zee R, de Haan CA, Rottier PJ (2003) The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J Virol 77: 8801-8811.
    • (2003) J Virol , vol.77 , pp. 8801-8811
    • Bosch, B.J.1    van der Zee, R.2    de Haan, C.A.3    Rottier, P.J.4
  • 42
    • 33645219694 scopus 로고    scopus 로고
    • Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of severe acute respiratory syndrome coronavirus
    • Chan WE, Chuang CK, Yeh SH, Chang MS, Chen SS (2006) Functional characterization of heptad repeat 1 and 2 mutants of the spike protein of severe acute respiratory syndrome coronavirus. J Virol 80: 3225-3237.
    • (2006) J Virol , vol.80 , pp. 3225-3237
    • Chan, W.E.1    Chuang, C.K.2    Yeh, S.H.3    Chang, M.S.4    Chen, S.S.5
  • 43
    • 2442680275 scopus 로고    scopus 로고
    • Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion
    • de Haan CA, Stadler K, Godeke GJ, Bosch BJ, Rottier PJ (2004) Cleavage inhibition of the murine coronavirus spike protein by a furin-like enzyme affects cell-cell but not virus-cell fusion. J Virol 78: 6048-6054.
    • (2004) J Virol , vol.78 , pp. 6048-6054
    • de Haan, C.A.1    Stadler, K.2    Godeke, G.J.3    Bosch, B.J.4    Rottier, P.J.5
  • 44
    • 44949129907 scopus 로고    scopus 로고
    • Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation
    • de Haan CA, Haijema BJ, Schellen P, Wichgers Schreur P, te Lintelo E, Vennema H, Rottier PJ (2008) Cleavage of group 1 coronavirus spike proteins: how furin cleavage is traded off against heparan sulfate binding upon cell culture adaptation. J Virol 82: 6078-6083.
    • (2008) J Virol , vol.82 , pp. 6078-6083
    • de Haan, C.A.1    Haijema, B.J.2    Schellen, P.3    Wichgers Schreur, P.4    te Lintelo, E.5    Vennema, H.6    Rottier, P.J.7
  • 47
    • 79961046297 scopus 로고    scopus 로고
    • RNA-binding domain in the nucleocapsid protein of gill-associated nidovirus of penaeid shrimp
    • Soowannayan C, Cowley JA, Michalski WP, Walker PJ (2011) RNA-binding domain in the nucleocapsid protein of gill-associated nidovirus of penaeid shrimp. PLoS One 6: e22156.
    • (2011) PLoS One , vol.6
    • Soowannayan, C.1    Cowley, J.A.2    Michalski, W.P.3    Walker, P.J.4
  • 48
    • 79960248955 scopus 로고    scopus 로고
    • Insect-specific flaviviruses from Culex mosquitoes in Colorado, with evidence of vertical transmission
    • Bolling BG, Eisen L, Moore CG, Blair CD (2011) Insect-specific flaviviruses from Culex mosquitoes in Colorado, with evidence of vertical transmission. Am J Trop Med Hyg 85: 169-177.
    • (2011) Am J Trop Med Hyg , vol.85 , pp. 169-177
    • Bolling, B.G.1    Eisen, L.2    Moore, C.G.3    Blair, C.D.4
  • 49
    • 80052774358 scopus 로고    scopus 로고
    • Evidence of efficient transovarial transmission of Culex flavivirus by Culex pipiens (Diptera: Culicidae)
    • Saiyasombat R, Bolling BG, Brault AC, Bartholomay LC, Blitvich BJ (2011) Evidence of efficient transovarial transmission of Culex flavivirus by Culex pipiens (Diptera: Culicidae). J Med Entomol 48: 1031-1038.
    • (2011) J Med Entomol , vol.48 , pp. 1031-1038
    • Saiyasombat, R.1    Bolling, B.G.2    Brault, A.C.3    Bartholomay, L.C.4    Blitvich, B.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.