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Volumn 6, Issue 10, 2010, Pages

High-resolution functional mapping of the venezuelan equine encephalitis virus genome by insertional mutagenesis and massively parallel sequencing

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN E1; GLYCOPROTEIN E2; NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 3; VIRUS CAPSID ANTIGEN;

EID: 78449246344     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1001146     Document Type: Article
Times cited : (23)

References (52)
  • 1
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • Strauss JH, Strauss EG (1994) The alphaviruses: gene expression, replication, and evolution. Microbiol Rev 58: 491-562.
    • (1994) Microbiol Rev , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 2
    • 0036371127 scopus 로고    scopus 로고
    • Functions of alphavirus nonstructural proteins in RNA replication
    • Kaariainen L, Ahola T (2002) Functions of alphavirus nonstructural proteins in RNA replication. Prog Nucleic Acid Res Mol Biol 71: 187-222.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 187-222
    • Kaariainen, L.1    Ahola, T.2
  • 3
    • 0028319950 scopus 로고
    • Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes
    • Sawicki DL, Sawicki SG (1994) Alphavirus positive and negative strand RNA synthesis and the role of polyproteins in formation of viral replication complexes. Arch Virol Suppl 9: 393-405.
    • (1994) Arch Virol Suppl , vol.9 , pp. 393-405
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 4
    • 0001552353 scopus 로고    scopus 로고
    • Alphaviruses
    • In: Knipe DM, Howley PM, eds, 5th edition: Lippincott, Williams, and Wilkins
    • Griffin D (2007) Alphaviruses. In: Knipe DM, Howley PM, eds. Fields Virology, 5th edition: Lippincott, Williams, and Wilkins.
    • (2007) Fields Virology
    • Griffin, D.1
  • 5
    • 0032710835 scopus 로고    scopus 로고
    • Putative RNA capping activities encoded by brome mosaic virus: Methylation and covalent binding of guanylate by replicase protein 1a
    • Ahola T, Ahlquist P (1999) Putative RNA capping activities encoded by brome mosaic virus: methylation and covalent binding of guanylate by replicase protein 1a. J Virol 73: 10061-10069.
    • (1999) J Virol , vol.73 , pp. 10061-10069
    • Ahola, T.1    Ahlquist, P.2
  • 6
    • 0031060112 scopus 로고    scopus 로고
    • Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities
    • Ahola T, Laakkonen P, Vihinen H, Kaariainen L (1997) Critical residues of Semliki Forest virus RNA capping enzyme involved in methyltransferase and guanylyltransferase-like activities. J Virol 71: 392-397.
    • (1997) J Virol , vol.71 , pp. 392-397
    • Ahola, T.1    Laakkonen, P.2    Vihinen, H.3    Kaariainen, L.4
  • 7
    • 0028833053 scopus 로고
    • Reaction in alphavirus mRNA capping: Formation of a covalent complex of nonstructural protein nsP1 with 7-methyl- GMP
    • Ahola T, Kaariainen L (1995) Reaction in alphavirus mRNA capping: formation of a covalent complex of nonstructural protein nsP1 with 7-methyl- GMP. Proc Natl Acad Sci U S A 92: 507-511.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 507-511
    • Ahola, T.1    Kaariainen, L.2
  • 8
    • 0024328925 scopus 로고
    • Association of the Sindbis virus RNA methyltransferase activity with the nonstructural protein nsP1
    • Mi S, Durbin R, Huang HV, Rice CM, Stollar V (1989) Association of the Sindbis virus RNA methyltransferase activity with the nonstructural protein nsP1. Virology 170: 385-391.
    • (1989) Virology , vol.170 , pp. 385-391
    • Mi, S.1    Durbin, R.2    Huang, H.V.3    Rice, C.M.4    Stollar, V.5
  • 9
    • 0025851067 scopus 로고
    • Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli
    • Mi S, Stollar V (1991) Expression of Sindbis virus nsP1 and methyltransferase activity in Escherichia coli. Virology 184: 423-427.
    • (1991) Virology , vol.184 , pp. 423-427
    • Mi, S.1    Stollar, V.2
  • 10
    • 0022007185 scopus 로고
    • Functional analysis of the A complementation group mutants of Sindbis HR virus
    • Sawicki DL, Sawicki SG (1985) Functional analysis of the A complementation group mutants of Sindbis HR virus. Virology 144: 20-34.
    • (1985) Virology , vol.144 , pp. 20-34
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 12
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 59-triphosphatase activity of Nsp2
    • Vasiljeva L, Merits A, Auvinen P, Kaariainen L (2000) Identification of a novel function of the alphavirus capping apparatus. RNA 59-triphosphatase activity of Nsp2. J Biol Chem 275: 17281-17287.
    • (2000) J Biol Chem , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3    Kaariainen, L.4
  • 13
    • 0028018141 scopus 로고
    • ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2
    • Rikkonen M, Peranen J, Kaariainen L (1994) ATPase and GTPase activities associated with Semliki Forest virus nonstructural protein nsP2. J Virol 68: 5804-5810.
    • (1994) J Virol , vol.68 , pp. 5804-5810
    • Rikkonen, M.1    Peranen, J.2    Kaariainen, L.3
  • 14
    • 32344448603 scopus 로고    scopus 로고
    • Characterization of the cysteine protease domain of Semliki Forest virus replicase protein nsP2 by in vitro mutagenesis
    • Golubtsov A, Kaariainen L, Caldentey J (2006) Characterization of the cysteine protease domain of Semliki Forest virus replicase protein nsP2 by in vitro mutagenesis. FEBS Lett 580: 1502-1508.
    • (2006) FEBS Lett , vol.580 , pp. 1502-1508
    • Golubtsov, A.1    Kaariainen, L.2    Caldentey, J.3
  • 15
    • 0024315805 scopus 로고
    • Evidence that Sindbis virus NSP2 is an autoprotease which processes the virus nonstructural polyprotein
    • Ding MX, Schlesinger MJ (1989) Evidence that Sindbis virus NSP2 is an autoprotease which processes the virus nonstructural polyprotein. Virology 171: 280-284.
    • (1989) Virology , vol.171 , pp. 280-284
    • Ding, M.X.1    Schlesinger, M.J.2
  • 16
    • 0024421374 scopus 로고
    • Processing the nonstructural polyproteins of sindbis virus: Nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans
    • Hardy WR, Strauss JH (1989) Processing the nonstructural polyproteins of sindbis virus: nonstructural proteinase is in the C-terminal half of nsP2 and functions both in cis and in trans. J Virol 63: 4653-4664.
    • (1989) J Virol , vol.63 , pp. 4653-4664
    • Hardy, W.R.1    Strauss, J.H.2
  • 17
    • 0027067063 scopus 로고
    • Identification of the active site residues in the nsP2 proteinase of Sindbis virus
    • Strauss EG, De Groot RJ, Levinson R, Strauss JH (1992) Identification of the active site residues in the nsP2 proteinase of Sindbis virus. Virology 191: 932-940.
    • (1992) Virology , vol.191 , pp. 932-940
    • Strauss, E.G.1    De Groot, R.J.2    Levinson, R.3    Strauss, J.H.4
  • 18
    • 0036828075 scopus 로고    scopus 로고
    • Roles of nonstructural protein nsP2 and Alpha/Beta interferons in determining the outcome of Sindbis virus infection
    • Frolova EI, Fayzulin RZ, Cook SH, Griffin DE, Rice CM, et al. (2002) Roles of nonstructural protein nsP2 and Alpha/Beta interferons in determining the outcome of Sindbis virus infection. Journal of Virology 76: 11254-11264.
    • (2002) Journal of Virology , vol.76 , pp. 11254-11264
    • Frolova, E.I.1    Fayzulin, R.Z.2    Cook, S.H.3    Griffin, D.E.4    Rice, C.M.5
  • 19
    • 33744937066 scopus 로고    scopus 로고
    • Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription
    • Garmashova N, Gorchakov R, Frolova E, Frolov I (2006) Sindbis virus nonstructural protein nsP2 is cytotoxic and inhibits cellular transcription. J Virol 80: 5686-5696.
    • (2006) J Virol , vol.80 , pp. 5686-5696
    • Garmashova, N.1    Gorchakov, R.2    Frolova, E.3    Frolov, I.4
  • 20
    • 0025331987 scopus 로고
    • Nuclear localization of Semliki Forest virus-specific nonstructural protein nsP2
    • Peranen J, Rikkonen M, Liljestrom P, Kaariainen L (1990) Nuclear localization of Semliki Forest virus-specific nonstructural protein nsP2. J Virol 64: 1888-1896.
    • (1990) J Virol , vol.64 , pp. 1888-1896
    • Peranen, J.1    Rikkonen, M.2    Liljestrom, P.3    Kaariainen, L.4
  • 21
    • 0024582528 scopus 로고
    • Mapping of RNA- temperature-sensitive mutants of Sindbis virus: Complementation group F mutants have lesions in nsP4
    • Hahn YS, Grakoui A, Rice CM, Strauss EG, Strauss JH (1989) Mapping of RNA- temperature-sensitive mutants of Sindbis virus: complementation group F mutants have lesions in nsP4. J Virol 63: 1194-1202.
    • (1989) J Virol , vol.63 , pp. 1194-1202
    • Hahn, Y.S.1    Grakoui, A.2    Rice, C.M.3    Strauss, E.G.4    Strauss, J.H.5
  • 22
    • 0027504136 scopus 로고
    • Evolution and taxonomy of positive-strand RNA viruses: Implications of comparative analysis of amino acid sequences
    • Koonin EV, Dolja VV (1993) Evolution and taxonomy of positive-strand RNA viruses: implications of comparative analysis of amino acid sequences. Crit Rev Biochem Mol Biol 28: 375-430.
    • (1993) Crit Rev Biochem Mol Biol , vol.28 , pp. 375-430
    • Koonin, E.V.1    Dolja, V.V.2
  • 23
    • 0032567393 scopus 로고    scopus 로고
    • Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure
    • O'Reilly EK, Kao CC (1998) Analysis of RNA-dependent RNA polymerase structure and function as guided by known polymerase structures and computer predictions of secondary structure. Virology 252: 287-303.
    • (1998) Virology , vol.252 , pp. 287-303
    • O'Reilly, E.K.1    Kao, C.C.2
  • 24
    • 0021770887 scopus 로고
    • Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses
    • Kamer G, Argos P (1984) Primary structural comparison of RNA-dependent polymerases from plant, animal and bacterial viruses. Nucleic Acids Res 12: 7269-7282.
    • (1984) Nucleic Acids Res , vol.12 , pp. 7269-7282
    • Kamer, G.1    Argos, P.2
  • 25
    • 0027935902 scopus 로고
    • Genetic analysis of the nsP3 region of Sindbis virus: Evidence for roles in minus-strand and subgenomic RNA synthesis
    • LaStarza MW, Lemm JA, Rice CM (1994) Genetic analysis of the nsP3 region of Sindbis virus: evidence for roles in minus-strand and subgenomic RNA synthesis. J Virol 68: 5781-5791.
    • (1994) J Virol , vol.68 , pp. 5781-5791
    • LaStarza, M.W.1    Lemm, J.A.2    Rice, C.M.3
  • 26
    • 0028040383 scopus 로고
    • Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA
    • Wang YF, Sawicki SG, Sawicki DL (1994) Alphavirus nsP3 functions to form replication complexes transcribing negative-strand RNA. J Virol 68: 6466-6475.
    • (1994) J Virol , vol.68 , pp. 6466-6475
    • Wang, Y.F.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 27
    • 0027979138 scopus 로고
    • Regulation of Sindbis virus RNA replication: Uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis
    • Shirako Y, Strauss JH (1994) Regulation of Sindbis virus RNA replication: uncleaved P123 and nsP4 function in minus-strand RNA synthesis, whereas cleaved products from P123 are required for efficient plus-strand RNA synthesis. J Virol 68: 1874-1885.
    • (1994) J Virol , vol.68 , pp. 1874-1885
    • Shirako, Y.1    Strauss, J.H.2
  • 28
    • 27644505258 scopus 로고    scopus 로고
    • Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose- 10-phosphate dephosphorylation by a conserved domain of nsP3
    • Saikatendu KS, Joseph JS, Subramanian V, Clayton T, Griffith M, et al. (2005) Structural basis of severe acute respiratory syndrome coronavirus ADP-ribose- 10-phosphate dephosphorylation by a conserved domain of nsP3. Structure 13: 1665-1675.
    • (2005) Structure , vol.13 , pp. 1665-1675
    • Saikatendu, K.S.1    Joseph, J.S.2    Subramanian, V.3    Clayton, T.4    Griffith, M.5
  • 29
    • 33748665458 scopus 로고    scopus 로고
    • Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains
    • Egloff MP, Malet H, Putics A, Heinonen M, Dutartre H, et al. (2006) Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains. J Virol 80: 8493-8502.
    • (2006) J Virol , vol.80 , pp. 8493-8502
    • Egloff, M.P.1    Malet, H.2    Putics, A.3    Heinonen, M.4    Dutartre, H.5
  • 31
    • 26444559529 scopus 로고    scopus 로고
    • ADP-ribose-10- monophosphatase: A conserved coronavirus enzyme that is dispensable for viral replication in tissue culture
    • Putics A, Filipowicz W, Hall J, Gorbalenya AE, Ziebuhr J (2005) ADP-ribose-10- monophosphatase: a conserved coronavirus enzyme that is dispensable for viral replication in tissue culture. J Virol 79: 12721-12731.
    • (2005) J Virol , vol.79 , pp. 12721-12731
    • Putics, A.1    Filipowicz, W.2    Hall, J.3    Gorbalenya, A.E.4    Ziebuhr, J.5
  • 32
    • 67449102614 scopus 로고    scopus 로고
    • The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket
    • Malet H, Coutard B, Jamal S, Dutartre H, Papageorgiou N, et al. (2009) The crystal structures of Chikungunya and Venezuelan equine encephalitis virus nsP3 macro domains define a conserved adenosine binding pocket. Journal of Virology 83: 6534-6545.
    • (2009) Journal of Virology , vol.83 , pp. 6534-6545
    • Malet, H.1    Coutard, B.2    Jamal, S.3    Dutartre, H.4    Papageorgiou, N.5
  • 34
    • 0034623235 scopus 로고    scopus 로고
    • Phosphorylation site analysis of Semliki forest virus nonstructural protein 3
    • Vihinen H, Saarinen J (2000) Phosphorylation site analysis of Semliki forest virus nonstructural protein 3. J Biol Chem 275: 27775-27783.
    • (2000) J Biol Chem , vol.275 , pp. 27775-27783
    • Vihinen, H.1    Saarinen, J.2
  • 35
    • 0028142238 scopus 로고
    • Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: Effects on phosphorylation and on virus replication in vertebrate and invertebrate cells
    • Lastarza MW, Grakoui A, Rice CM (1994) Deletion and duplication mutations in the C-terminal nonconserved region of Sindbis virus nsP3: effects on phosphorylation and on virus replication in vertebrate and invertebrate cells. Virology 202: 224-232.
    • (1994) Virology , vol.202 , pp. 224-232
    • Lastarza, M.W.1    Grakoui, A.2    Rice, C.M.3
  • 36
    • 33748304343 scopus 로고    scopus 로고
    • The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease
    • Russo AT, White MA, Watowich SJ (2006) The crystal structure of the Venezuelan equine encephalitis alphavirus nsP2 protease. Structure 14: 1449-1458.
    • (2006) Structure , vol.14 , pp. 1449-1458
    • Russo, A.T.1    White, M.A.2    Watowich, S.J.3
  • 37
    • 0023780765 scopus 로고
    • Demonstration in vitro of temperature-sensitive elongation of RNA in Sindbis virus mutant ts6
    • Barton DJ, Sawicki SG, Sawicki DL (1988) Demonstration in vitro of temperature-sensitive elongation of RNA in Sindbis virus mutant ts6. J Virol 62: 3597-3602.
    • (1988) J Virol , vol.62 , pp. 3597-3602
    • Barton, D.J.1    Sawicki, S.G.2    Sawicki, D.L.3
  • 38
    • 0012471185 scopus 로고
    • Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease
    • Hahn CS, Strauss EG, Strauss JH (1985) Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease. Proc Natl Acad Sci U S A 82: 4648-4652.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4648-4652
    • Hahn, C.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 39
    • 0024358586 scopus 로고
    • Mapping of RNA- temperaturesensitive mutants of Sindbis virus: Assignment of complementation groups A, B, and G to nonstructural proteins
    • Hahn YS, Strauss EG, Strauss JH (1989) Mapping of RNA- temperaturesensitive mutants of Sindbis virus: assignment of complementation groups A, B, and G to nonstructural proteins. J Virol 63: 3142-3150.
    • (1989) J Virol , vol.63 , pp. 3142-3150
    • Hahn, Y.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 40
    • 0025277442 scopus 로고
    • Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus
    • Hardy WR, Hahn YS, de Groot RJ, Strauss EG, Strauss JH (1990) Synthesis and processing of the nonstructural polyproteins of several temperature-sensitive mutants of Sindbis virus. Virology 177: 199-208.
    • (1990) Virology , vol.177 , pp. 199-208
    • Hardy, W.R.1    Hahn, Y.S.2    de Groot, R.J.3    Strauss, E.G.4    Strauss, J.H.5
  • 41
    • 0018662782 scopus 로고
    • Functional defects of RNA-negative temperature-sensitive mutants of Sindbis and Semliki Forest viruses
    • Keranen S, Kaariainen L (1979) Functional defects of RNA-negative temperature-sensitive mutants of Sindbis and Semliki Forest viruses. J Virol 32: 19-29.
    • (1979) J Virol , vol.32 , pp. 19-29
    • Keranen, S.1    Kaariainen, L.2
  • 42
    • 0025141312 scopus 로고
    • Temperature sensitive shut-off of alphavirus minus strand RNA synthesis maps to a nonstructural protein, nsP4
    • Sawicki D, Barkhimer DB, Sawicki SG, Rice CM, Schlesinger S (1990) Temperature sensitive shut-off of alphavirus minus strand RNA synthesis maps to a nonstructural protein, nsP4. Virology 174: 43-52.
    • (1990) Virology , vol.174 , pp. 43-52
    • Sawicki, D.1    Barkhimer, D.B.2    Sawicki, S.G.3    Rice, C.M.4    Schlesinger, S.5
  • 43
    • 0027166774 scopus 로고
    • A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis
    • Sawicki DL, Sawicki SG (1993) A second nonstructural protein functions in the regulation of alphavirus negative-strand RNA synthesis. J Virol 67: 3605-3610.
    • (1993) J Virol , vol.67 , pp. 3605-3610
    • Sawicki, D.L.1    Sawicki, S.G.2
  • 44
    • 0017091647 scopus 로고
    • Mutants of sindbis virus. I. Isolation and partial characterization of 89 new temperature-sensitive mutants
    • Strauss EG, Lenches EM, Strauss JH (1976) Mutants of sindbis virus. I. Isolation and partial characterization of 89 new temperature-sensitive mutants. Virology 74: 154-168.
    • (1976) Virology , vol.74 , pp. 154-168
    • Strauss, E.G.1    Lenches, E.M.2    Strauss, J.H.3
  • 45
    • 0027475009 scopus 로고
    • Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription
    • Lemm JA, Rice CM (1993) Roles of nonstructural polyproteins and cleavage products in regulating Sindbis virus RNA replication and transcription. J Virol 67: 1916-1926.
    • (1993) J Virol , vol.67 , pp. 1916-1926
    • Lemm, J.A.1    Rice, C.M.2
  • 46
    • 77649206548 scopus 로고    scopus 로고
    • Novel Functions of the Alphavirus Nonstructural Protein nsP3 C-Terminal Region
    • Varjak M, Zusinaite E, Merits A (2010) Novel Functions of the Alphavirus Nonstructural Protein nsP3 C-Terminal Region. J Virol 84: 2352-2364.
    • (2010) J Virol , vol.84 , pp. 2352-2364
    • Varjak, M.1    Zusinaite, E.2    Merits, A.3
  • 47
    • 0345599124 scopus 로고    scopus 로고
    • Functional analysis of nsP3 phosphoprotein mutants of Sindbis virus
    • De I, Fata-Hartley C, Sawicki SG, Sawicki DL (2003) Functional analysis of nsP3 phosphoprotein mutants of Sindbis virus. J Virol 77: 13106-13116.
    • (2003) J Virol , vol.77 , pp. 13106-13116
    • de, I.1    Fata-Hartley, C.2    Sawicki, S.G.3    Sawicki, D.L.4
  • 49
    • 59649086888 scopus 로고    scopus 로고
    • Highresolution functional profiling of a gammaherpesvirus RTA locus in the context of the viral genome
    • Arumugaswami V, Sitapara R, Hwang S, Song MJ, Ho TN, et al. (2009) Highresolution functional profiling of a gammaherpesvirus RTA locus in the context of the viral genome. J Virol 83: 1811-1822.
    • (2009) J Virol , vol.83 , pp. 1811-1822
    • Arumugaswami, V.1    Sitapara, R.2    Hwang, S.3    Song, M.J.4    Ho, T.N.5
  • 50
    • 0031583842 scopus 로고    scopus 로고
    • Replicon-helper systems from attenuated Venezuelan equine encephalitis virus: Expression of heterologous genes in vitro and immunization against heterologous pathogens in vivo
    • Pushko P, Parker M, Ludwig GV, Davis NL, Johnston RE, et al. (1997) Replicon-helper systems from attenuated Venezuelan equine encephalitis virus: expression of heterologous genes in vitro and immunization against heterologous pathogens in vivo. Virology 239: 389-401.
    • (1997) Virology , vol.239 , pp. 389-401
    • Pushko, P.1    Parker, M.2    Ludwig, G.V.3    Davis, N.L.4    Johnston, R.E.5
  • 51
    • 0028895608 scopus 로고
    • Specific restrictions in the progression of Venezuelan equine encephalitis virus-induced disease resulting from single amino acid changes in the glycoproteins
    • Grieder FB, Davis NL, Aronson JF, Charles PC, Sellon DC, et al. (1995) Specific restrictions in the progression of Venezuelan equine encephalitis virus-induced disease resulting from single amino acid changes in the glycoproteins. Virology 206: 994-1006.
    • (1995) Virology , vol.206 , pp. 994-1006
    • Grieder, F.B.1    Davis, N.L.2    Aronson, J.F.3    Charles, P.C.4    Sellon, D.C.5
  • 52
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25: 3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5


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