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Volumn 94, Issue 2, 2012, Pages 111-125

Orthopoxvirus targets for the development of new antiviral agents

Author keywords

Cidofovir; CMX001; Drug targets; Nucleoside analog; Orthopoxvirus; ST 246

Indexed keywords

ACICLOVIR; ANTIVIRUS AGENT; CIDOFOVIR; CIDOFOVIR 3 HEXADECYLOXYPROPYL ESTER; DNA POLYMERASE; DOUBLE STRANDED DNA; GENOMIC DNA; MESSENGER RNA; NUCLEOSIDE DERIVATIVE; PHOSPHATASE; PROTEIN KINASE; THIOSEMICARBAZONE DERIVATIVE; VIRUS DNA; VIRUS ENVELOPE PROTEIN;

EID: 84860272496     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2012.02.012     Document Type: Review
Times cited : (38)

References (237)
  • 1
    • 35148861053 scopus 로고    scopus 로고
    • Rabbitpox virus and vaccinia virus infection of rabbits as a model for human smallpox
    • Adams M.M., Rice A.D., Moyer R.W. Rabbitpox virus and vaccinia virus infection of rabbits as a model for human smallpox. J. Virol. 2007, 81:11084-11095.
    • (2007) J. Virol. , vol.81 , pp. 11084-11095
    • Adams, M.M.1    Rice, A.D.2    Moyer, R.W.3
  • 3
    • 79952164514 scopus 로고    scopus 로고
    • Cidofovir activity against poxvirus infections
    • Andrei G., Snoeck R. Cidofovir activity against poxvirus infections. Viruses 2010, 2:2803-2830.
    • (2010) Viruses , vol.2 , pp. 2803-2830
    • Andrei, G.1    Snoeck, R.2
  • 5
    • 2942639514 scopus 로고    scopus 로고
    • Vaccinia virus G1 protein, a predicted metalloprotease, is essential for morphogenesis of infectious virions but not for cleavage of major core proteins
    • Ansarah-Sobrinho C., Moss B. Vaccinia virus G1 protein, a predicted metalloprotease, is essential for morphogenesis of infectious virions but not for cleavage of major core proteins. J. Virol. 2004, 78:6855-6863.
    • (2004) J. Virol. , vol.78 , pp. 6855-6863
    • Ansarah-Sobrinho, C.1    Moss, B.2
  • 7
    • 0037288073 scopus 로고    scopus 로고
    • Potential antiviral therapeutics for smallpox, monkeypox and other orthopoxvirus infections
    • Baker R.O., Bray M., Huggins J.W. Potential antiviral therapeutics for smallpox, monkeypox and other orthopoxvirus infections. Antiviral Res. 2003, 57:13-23.
    • (2003) Antiviral Res. , vol.57 , pp. 13-23
    • Baker, R.O.1    Bray, M.2    Huggins, J.W.3
  • 9
    • 33645401301 scopus 로고    scopus 로고
    • Synthesis and antiviral evaluation of alkoxyalkyl derivatives of 9-(S)-(3-hydroxy-2-phosphonomethoxypropyl)adenine against cytomegalovirus and orthopoxviruses
    • Beadle J.R., Wan W.B., Ciesla S.L., Keith K.A., Hartline C., Kern E.R., Hostetler K.Y. Synthesis and antiviral evaluation of alkoxyalkyl derivatives of 9-(S)-(3-hydroxy-2-phosphonomethoxypropyl)adenine against cytomegalovirus and orthopoxviruses. J. Med. Chem. 2006, 49:2010-2015.
    • (2006) J. Med. Chem. , vol.49 , pp. 2010-2015
    • Beadle, J.R.1    Wan, W.B.2    Ciesla, S.L.3    Keith, K.A.4    Hartline, C.5    Kern, E.R.6    Hostetler, K.Y.7
  • 11
    • 3142604952 scopus 로고    scopus 로고
    • Antibodies against the extracellular enveloped virus B5R protein are mainly responsible for the EEV neutralizing capacity of vaccinia immune globulin
    • Bell E., Shamim M., Whitbeck J.C., Sfyroera G., Lambris J.D., Isaacs S.N. Antibodies against the extracellular enveloped virus B5R protein are mainly responsible for the EEV neutralizing capacity of vaccinia immune globulin. Virology 2004, 325:425-431.
    • (2004) Virology , vol.325 , pp. 425-431
    • Bell, E.1    Shamim, M.2    Whitbeck, J.C.3    Sfyroera, G.4    Lambris, J.D.5    Isaacs, S.N.6
  • 12
    • 0029655746 scopus 로고    scopus 로고
    • Phenotypic characterization of mutants in vaccinia virus gene G2R, a putative transcription elongation factor
    • Black E.P., Condit R.C. Phenotypic characterization of mutants in vaccinia virus gene G2R, a putative transcription elongation factor. J. Virol. 1996, 70:47-54.
    • (1996) J. Virol. , vol.70 , pp. 47-54
    • Black, E.P.1    Condit, R.C.2
  • 13
    • 0026655908 scopus 로고
    • A single amino acid substitution abolishes feedback inhibition of vaccinia virus thymidine kinase
    • Black M.E., Hruby D.E. A single amino acid substitution abolishes feedback inhibition of vaccinia virus thymidine kinase. J. Biol. Chem. 1992, 267:9743-9748.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9743-9748
    • Black, M.E.1    Hruby, D.E.2
  • 14
    • 0026039370 scopus 로고
    • Extracellular vaccinia virus formation and cell-to-cell virus transmission are prevented by deletion of the gene encoding the 37,000-Dalton outer envelope protein
    • Blasco R., Moss B. Extracellular vaccinia virus formation and cell-to-cell virus transmission are prevented by deletion of the gene encoding the 37,000-Dalton outer envelope protein. J. Virol. 1991, 65:5910-5920.
    • (1991) J. Virol. , vol.65 , pp. 5910-5920
    • Blasco, R.1    Moss, B.2
  • 15
    • 0027191921 scopus 로고
    • Dissociation of progeny vaccinia virus from the cell membrane is regulated by a viral envelope glycoprotein: effect of a point mutation in the lectin homology domain of the A34R gene
    • Blasco R., Sisler J.R., Moss B. Dissociation of progeny vaccinia virus from the cell membrane is regulated by a viral envelope glycoprotein: effect of a point mutation in the lectin homology domain of the A34R gene. J. Virol. 1993, 67:3319-3325.
    • (1993) J. Virol. , vol.67 , pp. 3319-3325
    • Blasco, R.1    Sisler, J.R.2    Moss, B.3
  • 16
    • 31044438181 scopus 로고    scopus 로고
    • Novel and specific inhibitors of a poxvirus type I topoisomerase
    • Bond A., Reichert Z., Stivers J.T. Novel and specific inhibitors of a poxvirus type I topoisomerase. Mol. Pharmacol. 2006, 69:547-557.
    • (2006) Mol. Pharmacol. , vol.69 , pp. 547-557
    • Bond, A.1    Reichert, Z.2    Stivers, J.T.3
  • 17
    • 33846086914 scopus 로고    scopus 로고
    • Biochemical and genetic analysis of the vaccinia virus d5 protein: Multimerization-dependent ATPase activity is required to support viral DNA replication
    • Boyle K.A., Arps L., Traktman P. Biochemical and genetic analysis of the vaccinia virus d5 protein: Multimerization-dependent ATPase activity is required to support viral DNA replication. J. Virol. 2007, 81:844-859.
    • (2007) J. Virol. , vol.81 , pp. 844-859
    • Boyle, K.A.1    Arps, L.2    Traktman, P.3
  • 18
    • 79960147916 scopus 로고    scopus 로고
    • Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme
    • Boyle K.A., Stanitsa E.S., Greseth M.D., Lindgren J.K., Traktman P. Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme. J. Biol. Chem. 2011, 286:24702-24713.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24702-24713
    • Boyle, K.A.1    Stanitsa, E.S.2    Greseth, M.D.3    Lindgren, J.K.4    Traktman, P.5
  • 20
    • 0038059031 scopus 로고    scopus 로고
    • Pathogenesis and potential antiviral therapy of complications of smallpox vaccination
    • Bray M. Pathogenesis and potential antiviral therapy of complications of smallpox vaccination. Antiviral Res. 2003, 58:101-114.
    • (2003) Antiviral Res. , vol.58 , pp. 101-114
    • Bray, M.1
  • 21
    • 0032552231 scopus 로고    scopus 로고
    • Poxvirus dilemmas-monkeypox, smallpox, and biologic terrorism
    • Breman J.G., Henderson D.A. Poxvirus dilemmas-monkeypox, smallpox, and biologic terrorism. N. Engl. J. Med. 1998, 339:556-559.
    • (1998) N. Engl. J. Med. , vol.339 , pp. 556-559
    • Breman, J.G.1    Henderson, D.A.2
  • 22
    • 3142543150 scopus 로고    scopus 로고
    • Identification of sites phosphorylated by the vaccinia virus B1R kinase in viral protein H5R
    • Brown N.G., Nick Morrice D., Beaud G., Hardie G., Leader D.P. Identification of sites phosphorylated by the vaccinia virus B1R kinase in viral protein H5R. BMC Biochem. 2000, 1:2.
    • (2000) BMC Biochem. , vol.1 , pp. 2
    • Brown, N.G.1    Nick Morrice, D.2    Beaud, G.3    Hardie, G.4    Leader, D.P.5
  • 23
    • 33748944877 scopus 로고    scopus 로고
    • Vaccinia virus F9 virion membrane protein is required for entry but not virus assembly, in contrast to the related L1 protein
    • Brown E., Senkevich T.G., Moss B. Vaccinia virus F9 virion membrane protein is required for entry but not virus assembly, in contrast to the related L1 protein. J. Virol. 2006, 80:9455-9464.
    • (2006) J. Virol. , vol.80 , pp. 9455-9464
    • Brown, E.1    Senkevich, T.G.2    Moss, B.3
  • 24
    • 0042353728 scopus 로고    scopus 로고
    • Vaccinia virus transcription
    • Broyles S.S. Vaccinia virus transcription. J. Gen. Virol. 2003, 84:2293-2303.
    • (2003) J. Gen. Virol. , vol.84 , pp. 2293-2303
    • Broyles, S.S.1
  • 25
    • 1242283917 scopus 로고    scopus 로고
    • Efficacy of oral active ether lipid analogs of cidofovir in a lethal mousepox model
    • Buller R.M., Owens G., Schriewer J., Melman L., Beadle J.R., Hostetler K.Y. Efficacy of oral active ether lipid analogs of cidofovir in a lethal mousepox model. Virology 2004, 318:474-481.
    • (2004) Virology , vol.318 , pp. 474-481
    • Buller, R.M.1    Owens, G.2    Schriewer, J.3    Melman, L.4    Beadle, J.R.5    Hostetler, K.Y.6
  • 26
    • 33745002291 scopus 로고    scopus 로고
    • Vaccinia virus proteolysis - a review
    • Byrd C.M., Hruby D.E. Vaccinia virus proteolysis - a review. Rev. Med. Virol. 2006, 16:187-202.
    • (2006) Rev. Med. Virol. , vol.16 , pp. 187-202
    • Byrd, C.M.1    Hruby, D.E.2
  • 27
    • 0036338018 scopus 로고    scopus 로고
    • The vaccinia virus I7L gene product is the core protein proteinase
    • Byrd C.M., Bolken T.C., Hruby D.E. The vaccinia virus I7L gene product is the core protein proteinase. J. Virol. 2002, 76:8973-8976.
    • (2002) J. Virol. , vol.76 , pp. 8973-8976
    • Byrd, C.M.1    Bolken, T.C.2    Hruby, D.E.3
  • 30
    • 18144365075 scopus 로고    scopus 로고
    • Entry of the vaccinia virus intracellular mature virion and its interactions with glycosaminoglycans
    • Carter G.C., Law M., Hollinshead M., Smith G.L. Entry of the vaccinia virus intracellular mature virion and its interactions with glycosaminoglycans. J. Gen. Virol. 2005, 86:1279-1290.
    • (2005) J. Gen. Virol. , vol.86 , pp. 1279-1290
    • Carter, G.C.1    Law, M.2    Hollinshead, M.3    Smith, G.L.4
  • 31
    • 0031800615 scopus 로고    scopus 로고
    • DNA packaging mutant: repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles
    • Cassetti M.C., Merchlinsky M., Wolffe E.J., Weisberg A.S., Moss B. DNA packaging mutant: repression of the vaccinia virus A32 gene results in noninfectious, DNA-deficient, spherical, enveloped particles. J. Virol. 1998, 72:5769-5780.
    • (1998) J. Virol. , vol.72 , pp. 5769-5780
    • Cassetti, M.C.1    Merchlinsky, M.2    Wolffe, E.J.3    Weisberg, A.S.4    Moss, B.5
  • 32
    • 33846837294 scopus 로고    scopus 로고
    • Amino acid substitutions at multiple sites within the vaccinia virus D13 scaffold protein confer resistance to rifampicin
    • Charity J.C., Katz E., Moss B. Amino acid substitutions at multiple sites within the vaccinia virus D13 scaffold protein confer resistance to rifampicin. Virology 2007, 359:227-232.
    • (2007) Virology , vol.359 , pp. 227-232
    • Charity, J.C.1    Katz, E.2    Moss, B.3
  • 34
    • 66249115329 scopus 로고    scopus 로고
    • Vaccinia virus p37 interacts with host proteins associated with LE-derived transport vesicle biogenesis
    • Chen Y., Honeychurch K.M., Yang G., Byrd C.M., Harver C., Hruby D.E., Jordan R. Vaccinia virus p37 interacts with host proteins associated with LE-derived transport vesicle biogenesis. Virol. J. 2009, 6:44.
    • (2009) Virol. J. , vol.6 , pp. 44
    • Chen, Y.1    Honeychurch, K.M.2    Yang, G.3    Byrd, C.M.4    Harver, C.5    Hruby, D.E.6    Jordan, R.7
  • 35
    • 78650291480 scopus 로고    scopus 로고
    • Poxvirus interleukin-4 expression overcomes inherent resistance and vaccine-induced immunity: pathogenesis, prophylaxis, and antiviral therapy
    • Chen N., Bellone C.J., Schriewer J., Owens G., Fredrickson T., Parker S., Buller R.M. Poxvirus interleukin-4 expression overcomes inherent resistance and vaccine-induced immunity: pathogenesis, prophylaxis, and antiviral therapy. Virology 2011, 409:328-337.
    • (2011) Virology , vol.409 , pp. 328-337
    • Chen, N.1    Bellone, C.J.2    Schriewer, J.3    Owens, G.4    Fredrickson, T.5    Parker, S.6    Buller, R.M.7
  • 36
    • 0025101284 scopus 로고
    • Insertional inactivation of the large subunit of ribonucleotide reductase encoded by vaccinia virus is associated with reduced virulence in vivo
    • Child S.J., Palumbo G.J., Buller R.M., Hruby D.E. Insertional inactivation of the large subunit of ribonucleotide reductase encoded by vaccinia virus is associated with reduced virulence in vivo. Virology 1990, 174:625-629.
    • (1990) Virology , vol.174 , pp. 625-629
    • Child, S.J.1    Palumbo, G.J.2    Buller, R.M.3    Hruby, D.E.4
  • 37
    • 33847197146 scopus 로고    scopus 로고
    • Vaccinia virus 4c (A26L) protein on intracellular mature virus binds to the extracellular cellular matrix laminin
    • Chiu W.L., Lin C.L., Yang M.H., Tzou D.L., Chang W. Vaccinia virus 4c (A26L) protein on intracellular mature virus binds to the extracellular cellular matrix laminin. J. Virol. 2007, 81:2149-2157.
    • (2007) J. Virol. , vol.81 , pp. 2149-2157
    • Chiu, W.L.1    Lin, C.L.2    Yang, M.H.3    Tzou, D.L.4    Chang, W.5
  • 38
    • 0042632872 scopus 로고    scopus 로고
    • Esterification of cidofovir with alkoxyalkanols increases oral bioavailability and diminishes drug accumulation in kidney
    • Ciesla S.L., Trahan J., Wan W.B., Beadle J.R., Aldern K.A., Painter G.R., Hostetler K.Y. Esterification of cidofovir with alkoxyalkanols increases oral bioavailability and diminishes drug accumulation in kidney. Antiviral Res. 2003, 59:163-171.
    • (2003) Antiviral Res. , vol.59 , pp. 163-171
    • Ciesla, S.L.1    Trahan, J.2    Wan, W.B.3    Beadle, J.R.4    Aldern, K.A.5    Painter, G.R.6    Hostetler, K.Y.7
  • 39
    • 0037073058 scopus 로고    scopus 로고
    • Regulation of viral transcription elongation and termination during vaccinia virus infection
    • Condit R.C., Niles E.G. Regulation of viral transcription elongation and termination during vaccinia virus infection. Biochim. Biophys. Acta 2002, 1577:325-336.
    • (2002) Biochim. Biophys. Acta , vol.1577 , pp. 325-336
    • Condit, R.C.1    Niles, E.G.2
  • 40
    • 0026347518 scopus 로고
    • A vaccinia virus isatin-beta-thiosemicarbazone resistance mutation maps in the viral gene encoding the 132-kDa subunit of RNA polymerase
    • Condit R.C., Easterly R., Pacha R.F., Fathi Z., Meis R.J. A vaccinia virus isatin-beta-thiosemicarbazone resistance mutation maps in the viral gene encoding the 132-kDa subunit of RNA polymerase. Virology 1991, 185:857-861.
    • (1991) Virology , vol.185 , pp. 857-861
    • Condit, R.C.1    Easterly, R.2    Pacha, R.F.3    Fathi, Z.4    Meis, R.J.5
  • 41
    • 33746577836 scopus 로고    scopus 로고
    • In a nutshell: structure and assembly of the vaccinia virion
    • Condit R.C., Moussatche N., Traktman P. In a nutshell: structure and assembly of the vaccinia virion. Adv. Virus Res. 2006, 66:31-124.
    • (2006) Adv. Virus Res. , vol.66 , pp. 31-124
    • Condit, R.C.1    Moussatche, N.2    Traktman, P.3
  • 42
    • 34848818806 scopus 로고    scopus 로고
    • Vaccinia, Inc. - probing the functional substructure of poxviral replication factories
    • Condit R.C. Vaccinia, Inc. - probing the functional substructure of poxviral replication factories. Cell Host Microbe 2007, 2:205-207.
    • (2007) Cell Host Microbe , vol.2 , pp. 205-207
    • Condit, R.C.1
  • 43
    • 34248567670 scopus 로고    scopus 로고
    • A targeted approach to identification of vaccinia virus postreplicative transcription elongation factors: genetic evidence for a role of the H5R gene in vaccinia transcription
    • Cresawn S.G., Condit R.C. A targeted approach to identification of vaccinia virus postreplicative transcription elongation factors: genetic evidence for a role of the H5R gene in vaccinia transcription. Virology 2007, 363:333-341.
    • (2007) Virology , vol.363 , pp. 333-341
    • Cresawn, S.G.1    Condit, R.C.2
  • 44
    • 34248515264 scopus 로고    scopus 로고
    • Mapping and phenotypic analysis of spontaneous isatin-beta-thiosemicarbazone resistant mutants of vaccinia virus
    • Cresawn S.G., Prins C., Latner D.R., Condit R.C. Mapping and phenotypic analysis of spontaneous isatin-beta-thiosemicarbazone resistant mutants of vaccinia virus. Virology 2007, 363:319-332.
    • (2007) Virology , vol.363 , pp. 319-332
    • Cresawn, S.G.1    Prins, C.2    Latner, D.R.3    Condit, R.C.4
  • 46
    • 0030054976 scopus 로고    scopus 로고
    • Pharmacokinetics, bioavailability, metabolism, and tissue distribution of cidofovir (HPMPC) and cyclic HPMPC in rats
    • Cundy K.C., Bidgood A.M., Lynch G., Shaw J.P., Griffin L., Lee W.A. Pharmacokinetics, bioavailability, metabolism, and tissue distribution of cidofovir (HPMPC) and cyclic HPMPC in rats. Drug Metab. Dispos. 1996, 24:745-752.
    • (1996) Drug Metab. Dispos. , vol.24 , pp. 745-752
    • Cundy, K.C.1    Bidgood, A.M.2    Lynch, G.3    Shaw, J.P.4    Griffin, L.5    Lee, W.A.6
  • 47
    • 0141594578 scopus 로고    scopus 로고
    • Poxvirus DNA topoisomerase knockout mutant exhibits decreased infectivity associated with reduced early transcription
    • Da Fonseca F., Moss B. Poxvirus DNA topoisomerase knockout mutant exhibits decreased infectivity associated with reduced early transcription. Proc. Natl. Acad. Sci. USA 2003, 100:11291-11296.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11291-11296
    • Da Fonseca, F.1    Moss, B.2
  • 48
    • 0033854259 scopus 로고    scopus 로고
    • Characterization of the vaccinia virus H3L envelope protein: topology and posttranslational membrane insertion via the C-terminal hydrophobic tail
    • da Fonseca F.G., Wolffe E.J., Weisberg A., Moss B. Characterization of the vaccinia virus H3L envelope protein: topology and posttranslational membrane insertion via the C-terminal hydrophobic tail. J. Virol. 2000, 74:7508-7517.
    • (2000) J. Virol. , vol.74 , pp. 7508-7517
    • da Fonseca, F.G.1    Wolffe, E.J.2    Weisberg, A.3    Moss, B.4
  • 49
    • 18044389358 scopus 로고    scopus 로고
    • Using purine skews to predict genes in AT-rich poxviruses
    • Da Silva M., Upton C. Using purine skews to predict genes in AT-rich poxviruses. BMC Genomics 2005, 6:22.
    • (2005) BMC Genomics , vol.6 , pp. 22
    • Da Silva, M.1    Upton, C.2
  • 50
    • 4444250212 scopus 로고    scopus 로고
    • Therapeutic potential of nucleoside/nucleotide analogues against poxvirus infections
    • De Clercq E., Neyts J. Therapeutic potential of nucleoside/nucleotide analogues against poxvirus infections. Rev. Med. Virol. 2004, 14:289-300.
    • (2004) Rev. Med. Virol. , vol.14 , pp. 289-300
    • De Clercq, E.1    Neyts, J.2
  • 51
    • 0017080159 scopus 로고
    • Effect of cytosine, arabinoside, iododeoxyuridine, ethyldeoxyuridine, thiocyanatodeoxyuridine, and ribavirin on tail lesion formation in mice infected with vaccinia virus
    • De Clercq E., Luczak M., Shugar D., Torrence P.F., Waters J.A., Witkop B. Effect of cytosine, arabinoside, iododeoxyuridine, ethyldeoxyuridine, thiocyanatodeoxyuridine, and ribavirin on tail lesion formation in mice infected with vaccinia virus. Proc. Soc. Exp. Biol. Med. 1976, 151:487-490.
    • (1976) Proc. Soc. Exp. Biol. Med. , vol.151 , pp. 487-490
    • De Clercq, E.1    Luczak, M.2    Shugar, D.3    Torrence, P.F.4    Waters, J.A.5    Witkop, B.6
  • 53
    • 33645456955 scopus 로고
    • Inhibition of the replication of DNA viruses by phosphonylmethoxyalkyl-purines and -pyrimidines
    • De Clercq E. Inhibition of the replication of DNA viruses by phosphonylmethoxyalkyl-purines and -pyrimidines. J. Chemother. 1989, 1:1074-1076.
    • (1989) J. Chemother. , vol.1 , pp. 1074-1076
    • De Clercq, E.1
  • 54
    • 0035074340 scopus 로고    scopus 로고
    • Vaccinia virus inhibitors as a paradigm for the chemotherapy of poxvirus infections
    • De Clercq E. Vaccinia virus inhibitors as a paradigm for the chemotherapy of poxvirus infections. Clin. Microbiol. Rev. 2001, 14:382-397.
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 382-397
    • De Clercq, E.1
  • 55
    • 0142126681 scopus 로고    scopus 로고
    • Clinical potential of the acyclic nucleoside phosphonates cidofovir, adefovir, and tenofovir in treatment of DNA virus and retrovirus infections
    • De Clercq E. Clinical potential of the acyclic nucleoside phosphonates cidofovir, adefovir, and tenofovir in treatment of DNA virus and retrovirus infections. Clin. Microbiol. Rev. 2003, 16:569-596.
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 569-596
    • De Clercq, E.1
  • 56
    • 34247275133 scopus 로고    scopus 로고
    • The acyclic nucleoside phosphonates from inception to clinical use: historical perspective
    • De Clercq E. The acyclic nucleoside phosphonates from inception to clinical use: historical perspective. Antiviral Res. 2007, 75:1-13.
    • (2007) Antiviral Res. , vol.75 , pp. 1-13
    • De Clercq, E.1
  • 57
    • 78651509253 scopus 로고    scopus 로고
    • Historical Perspectives in the Development of Antiviral Agents Against Poxviruses
    • De Clercq E. Historical Perspectives in the Development of Antiviral Agents Against Poxviruses. Viruses 2010, 2:1322-1339.
    • (2010) Viruses , vol.2 , pp. 1322-1339
    • De Clercq, E.1
  • 58
    • 78651509253 scopus 로고    scopus 로고
    • Historical perspectives in the development of antiviral agents against poxviruses
    • De Clercq E. Historical perspectives in the development of antiviral agents against poxviruses. Viruses 2010, 2:1322-1339.
    • (2010) Viruses , vol.2 , pp. 1322-1339
    • De Clercq, E.1
  • 59
    • 0037213268 scopus 로고    scopus 로고
    • Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells
    • De Silva F.S., Moss B. Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells. J. Virol. 2003, 77:159-166.
    • (2003) J. Virol. , vol.77 , pp. 159-166
    • De Silva, F.S.1    Moss, B.2
  • 60
    • 0034785376 scopus 로고    scopus 로고
    • Vaccinia virus telomeres: interaction with the viral I1, I6, and K4 proteins
    • DeMasi J., Du S., Lennon D., Traktman P. Vaccinia virus telomeres: interaction with the viral I1, I6, and K4 proteins. J. Virol. 2001, 75:10090-10105.
    • (2001) J. Virol. , vol.75 , pp. 10090-10105
    • DeMasi, J.1    Du, S.2    Lennon, D.3    Traktman, P.4
  • 61
    • 0032519829 scopus 로고    scopus 로고
    • Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination
    • Deng L., Shuman S. Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA transcription termination. Genes Dev. 1998, 12:538-546.
    • (1998) Genes Dev. , vol.12 , pp. 538-546
    • Deng, L.1    Shuman, S.2
  • 62
    • 37048998961 scopus 로고    scopus 로고
    • Identification of novel antipoxviral agents: mitoxantrone inhibits vaccinia virus replication by blocking virion assembly
    • Deng L., Dai P., Ciro A., Smee D.F., Djaballah H., Shuman S. Identification of novel antipoxviral agents: mitoxantrone inhibits vaccinia virus replication by blocking virion assembly. J. Virol. 2007, 81:13392-13402.
    • (2007) J. Virol. , vol.81 , pp. 13392-13402
    • Deng, L.1    Dai, P.2    Ciro, A.3    Smee, D.F.4    Djaballah, H.5    Shuman, S.6
  • 63
    • 0032837827 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of A17 during vaccinia virus infection: involvement of the H1 phosphatase and the F10 kinase
    • Derrien M., Punjabi A., Khanna M., Grubisha O., Traktman P. Tyrosine phosphorylation of A17 during vaccinia virus infection: involvement of the H1 phosphatase and the F10 kinase. J. Virol. 1999, 73:7287-7296.
    • (1999) J. Virol. , vol.73 , pp. 7287-7296
    • Derrien, M.1    Punjabi, A.2    Khanna, M.3    Grubisha, O.4    Traktman, P.5
  • 64
    • 0034062061 scopus 로고    scopus 로고
    • The punctate sites of accumulation of vaccinia virus early proteins are precursors of sites of viral DNA synthesis
    • Domi A., Beaud G. The punctate sites of accumulation of vaccinia virus early proteins are precursors of sites of viral DNA synthesis. J. Gen. Virol. 2000, 81:1231-1235.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1231-1235
    • Domi, A.1    Beaud, G.2
  • 65
    • 42449131355 scopus 로고    scopus 로고
    • Vaccinia virus E2L null mutants exhibit a major reduction in extracellular virion formation and virus spread
    • Domi A., Weisberg A.S., Moss B. Vaccinia virus E2L null mutants exhibit a major reduction in extracellular virion formation and virus spread. J. Virol. 2008, 82:4215-4226.
    • (2008) J. Virol. , vol.82 , pp. 4215-4226
    • Domi, A.1    Weisberg, A.S.2    Moss, B.3
  • 67
    • 29744441203 scopus 로고    scopus 로고
    • Vaccinia virus nicking-joining enzyme is encoded by K4L (VACWR035)
    • Eckert D., Williams O., Meseda C.A., Merchlinsky M. Vaccinia virus nicking-joining enzyme is encoded by K4L (VACWR035). J. Virol. 2005, 79:15084-15090.
    • (2005) J. Virol. , vol.79 , pp. 15084-15090
    • Eckert, D.1    Williams, O.2    Meseda, C.A.3    Merchlinsky, M.4
  • 68
    • 33750999341 scopus 로고    scopus 로고
    • Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design
    • El Omari K., Solaroli N., Karlsson A., Balzarini J., Stammers D.K. Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design. BMC Struct. Biol. 2006, 6:22.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 22
    • El Omari, K.1    Solaroli, N.2    Karlsson, A.3    Balzarini, J.4    Stammers, D.K.5
  • 69
    • 0001459947 scopus 로고    scopus 로고
    • Poxviruses
    • Lippincott Williams & Wilkins, Philadelphia, B.N. Fields, D.M. Knipe, P.M. Howley, D.E. Griffin (Eds.)
    • Esposito J., Fenner F. Poxviruses. Fields' virology 2001, 3087. Lippincott Williams & Wilkins, Philadelphia. fourth ed. B.N. Fields, D.M. Knipe, P.M. Howley, D.E. Griffin (Eds.).
    • (2001) Fields' virology , pp. 3087
    • Esposito, J.1    Fenner, F.2
  • 71
    • 0027099689 scopus 로고
    • Characterization of vaccinia virus DNA replication mutants with lesions in the D5 gene
    • Evans E., Traktman P. Characterization of vaccinia virus DNA replication mutants with lesions in the D5 gene. Chromosoma 1992, 102:S72-82.
    • (1992) Chromosoma , vol.102
    • Evans, E.1    Traktman, P.2
  • 72
    • 33745833395 scopus 로고    scopus 로고
    • Toward orthopoxvirus countermeasures: a novel heteromorphic nucleoside of unusual structure
    • Fan X., Zhang X., Zhou L., Keith K.A., Prichard M.N., Kern E.R., Torrence P.F. Toward orthopoxvirus countermeasures: a novel heteromorphic nucleoside of unusual structure. J. Med. Chem. 2006, 49:4052-4054.
    • (2006) J. Med. Chem. , vol.49 , pp. 4052-4054
    • Fan, X.1    Zhang, X.2    Zhou, L.3    Keith, K.A.4    Prichard, M.N.5    Kern, E.R.6    Torrence, P.F.7
  • 74
    • 33749987030 scopus 로고    scopus 로고
    • New peptide inhibitors of type IB topoisomerases: similarities and differences vis-a-vis inhibitors of tyrosine recombinases
    • Fujimoto D.F., Pinilla C., Segall A.M. New peptide inhibitors of type IB topoisomerases: similarities and differences vis-a-vis inhibitors of tyrosine recombinases. J. Mol. Biol. 2006, 363:891-907.
    • (2006) J. Mol. Biol. , vol.363 , pp. 891-907
    • Fujimoto, D.F.1    Pinilla, C.2    Segall, A.M.3
  • 75
    • 57349132991 scopus 로고    scopus 로고
    • Mechanism of antiviral drug resistance of vaccinia virus: identification of residues in the viral DNA polymerase conferring differential resistance to antipoxvirus drugs
    • Gammon D.B., Snoeck R., Fiten P., Krecmerova M., Holy A., De Clercq E., Opdenakker G., Evans D.H., Andrei G. Mechanism of antiviral drug resistance of vaccinia virus: identification of residues in the viral DNA polymerase conferring differential resistance to antipoxvirus drugs. J. Virol. 2008, 82:12520-12534.
    • (2008) J. Virol. , vol.82 , pp. 12520-12534
    • Gammon, D.B.1    Snoeck, R.2    Fiten, P.3    Krecmerova, M.4    Holy, A.5    De Clercq, E.6    Opdenakker, G.7    Evans, D.H.8    Andrei, G.9
  • 76
    • 77957676334 scopus 로고    scopus 로고
    • Vaccinia virus-encoded ribonucleotide reductase subunits are differentially required for replication and pathogenesis
    • Gammon D.B., Gowrishankar B., Duraffour S., Andrei G., Upton C., Evans D.H. Vaccinia virus-encoded ribonucleotide reductase subunits are differentially required for replication and pathogenesis. PLoS Pathog. 2010, 6:e1000984.
    • (2010) PLoS Pathog. , vol.6
    • Gammon, D.B.1    Gowrishankar, B.2    Duraffour, S.3    Andrei, G.4    Upton, C.5    Evans, D.H.6
  • 77
    • 0034988814 scopus 로고    scopus 로고
    • Repression of vaccinia virus Holliday junction resolvase inhibits processing of viral DNA into unit-length genomes
    • Garcia A.D., Moss B. Repression of vaccinia virus Holliday junction resolvase inhibits processing of viral DNA into unit-length genomes. J. Virol. 2001, 75:6460-6471.
    • (2001) J. Virol. , vol.75 , pp. 6460-6471
    • Garcia, A.D.1    Moss, B.2
  • 78
    • 33744954317 scopus 로고    scopus 로고
    • Quaternary structure and cleavage specificity of a poxvirus holliday junction resolvase
    • Garcia A.D., Otero J., Lebowitz J., Schuck P., Moss B. Quaternary structure and cleavage specificity of a poxvirus holliday junction resolvase. J. Biol. Chem. 2006, 281:11618-11626.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11618-11626
    • Garcia, A.D.1    Otero, J.2    Lebowitz, J.3    Schuck, P.4    Moss, B.5
  • 79
    • 0027391646 scopus 로고
    • Stimulation of poly(A) tail elongation by the VP39 subunit of the vaccinia virus-encoded poly(A) polymerase
    • Gershon P.D., Moss B. Stimulation of poly(A) tail elongation by the VP39 subunit of the vaccinia virus-encoded poly(A) polymerase. J. Biol. Chem. 1993, 268:2203-2210.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2203-2210
    • Gershon, P.D.1    Moss, B.2
  • 80
    • 0031026591 scopus 로고    scopus 로고
    • Palmitylation of the vaccinia virus 37-kDa major envelope antigen. Identification of a conserved acceptor motif and biological relevance
    • Grosenbach D.W., Ulaeto D.O., Hruby D.E. Palmitylation of the vaccinia virus 37-kDa major envelope antigen. Identification of a conserved acceptor motif and biological relevance. J. Biol. Chem. 1997, 272:1956-1964.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1956-1964
    • Grosenbach, D.W.1    Ulaeto, D.O.2    Hruby, D.E.3
  • 81
    • 0141677711 scopus 로고    scopus 로고
    • Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation
    • Grubisha O., Traktman P. Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation. J. Virol. 2003, 77:10929-10942.
    • (2003) J. Virol. , vol.77 , pp. 10929-10942
    • Grubisha, O.1    Traktman, P.2
  • 82
    • 0027049405 scopus 로고
    • A yeast protein phosphatase related to the vaccinia virus VH1 phosphatase is induced by nitrogen starvation
    • Guan K., Hakes D.J., Wang Y., Park H.D., Cooper T.G., Dixon J.E. A yeast protein phosphatase related to the vaccinia virus VH1 phosphatase is induced by nitrogen starvation. Proc. Natl. Acad. Sci. USA 1992, 89:12175-12179.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12175-12179
    • Guan, K.1    Hakes, D.J.2    Wang, Y.3    Park, H.D.4    Cooper, T.G.5    Dixon, J.E.6
  • 83
    • 0027154080 scopus 로고
    • A protein phosphatase related to the vaccinia virus VH1 is encoded in the genomes of several orthopoxviruses and a baculovirus
    • Hakes D.J., Martell K.J., Zhao W.G., Massung R.F., Esposito J.J., Dixon J.E. A protein phosphatase related to the vaccinia virus VH1 is encoded in the genomes of several orthopoxviruses and a baculovirus. Proc. Natl. Acad. Sci. USA 1993, 90:4017-4021.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4017-4021
    • Hakes, D.J.1    Martell, K.J.2    Zhao, W.G.3    Massung, R.F.4    Esposito, J.J.5    Dixon, J.E.6
  • 85
    • 0031751486 scopus 로고    scopus 로고
    • Re-emergence of monkeypox in Africa: a review of the past six years
    • Heymann D.L., Szczeniowski M., Esteves K. Re-emergence of monkeypox in Africa: a review of the past six years. Br. Med. Bull. 1998, 54:693-702.
    • (1998) Br. Med. Bull. , vol.54 , pp. 693-702
    • Heymann, D.L.1    Szczeniowski, M.2    Esteves, K.3
  • 86
    • 0019409526 scopus 로고
    • Characterization of intracellular and extracellular vaccinia virus variants: N1-isonicotinoyl-N2-3-methyl-4-chlorobenzoylhydrazine interferes with cytoplasmic virus dissemination and release
    • Hiller G., Eibl H., Weber K. Characterization of intracellular and extracellular vaccinia virus variants: N1-isonicotinoyl-N2-3-methyl-4-chlorobenzoylhydrazine interferes with cytoplasmic virus dissemination and release. J. Virol. 1981, 39:903-913.
    • (1981) J. Virol. , vol.39 , pp. 903-913
    • Hiller, G.1    Eibl, H.2    Weber, K.3
  • 87
    • 34250842469 scopus 로고    scopus 로고
    • The vaccinia virus F13L YPPL motif is required for efficient release of extracellular enveloped virus
    • Honeychurch K.M., Yang G., Jordan R., Hruby D.E. The vaccinia virus F13L YPPL motif is required for efficient release of extracellular enveloped virus. J. Virol. 2007, 81:7310-7315.
    • (2007) J. Virol. , vol.81 , pp. 7310-7315
    • Honeychurch, K.M.1    Yang, G.2    Jordan, R.3    Hruby, D.E.4
  • 88
    • 67349157073 scopus 로고    scopus 로고
    • Alkoxyalkyl prodrugs of acyclic nucleoside phosphonates enhance oral antiviral activity and reduce toxicity: current state of the art
    • Hostetler K.Y. Alkoxyalkyl prodrugs of acyclic nucleoside phosphonates enhance oral antiviral activity and reduce toxicity: current state of the art. Antiviral Res. 2009, 82:A84-98.
    • (2009) Antiviral Res. , vol.82
    • Hostetler, K.Y.1
  • 89
    • 0019979681 scopus 로고
    • Mapping and identification of the vaccinia virus thymidine kinase gene
    • Hruby D.E., Ball L.A. Mapping and identification of the vaccinia virus thymidine kinase gene. J. Virol. 1982, 43:403-409.
    • (1982) J. Virol. , vol.43 , pp. 403-409
    • Hruby, D.E.1    Ball, L.A.2
  • 90
    • 0036310248 scopus 로고    scopus 로고
    • Similarities in the induction of post-Golgi vesicles by the vaccinia virus F13L protein and phospholipase D
    • Husain M., Moss B. Similarities in the induction of post-Golgi vesicles by the vaccinia virus F13L protein and phospholipase D. J. Virol. 2002, 76:7777-7789.
    • (2002) J. Virol. , vol.76 , pp. 7777-7789
    • Husain, M.1    Moss, B.2
  • 91
    • 0041707720 scopus 로고    scopus 로고
    • Intracellular trafficking of a palmitoylated membrane-associated protein component of enveloped vaccinia virus
    • Husain M., Moss B. Intracellular trafficking of a palmitoylated membrane-associated protein component of enveloped vaccinia virus. J. Virol. 2003, 77:9008-9019.
    • (2003) J. Virol. , vol.77 , pp. 9008-9019
    • Husain, M.1    Moss, B.2
  • 93
    • 0036943963 scopus 로고    scopus 로고
    • Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex
    • Ishii K., Moss B. Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex. Virology 2002, 303:232-239.
    • (2002) Virology , vol.303 , pp. 232-239
    • Ishii, K.1    Moss, B.2
  • 94
    • 70350328591 scopus 로고    scopus 로고
    • Cidofovir inhibits genome encapsidation and affects morphogenesis during the replication of vaccinia virus
    • Jesus D.M., Costa L.T., Goncalves D.L., Achete C.A., Attias M., Moussatche N., Damaso C.R. Cidofovir inhibits genome encapsidation and affects morphogenesis during the replication of vaccinia virus. J. Virol. 2009, 83:11477-11490.
    • (2009) J. Virol. , vol.83 , pp. 11477-11490
    • Jesus, D.M.1    Costa, L.T.2    Goncalves, D.L.3    Achete, C.A.4    Attias, M.5    Moussatche, N.6    Damaso, C.R.7
  • 96
    • 79952132207 scopus 로고    scopus 로고
    • Development of ST-246(R) for Treatment of Poxvirus Infections
    • Jordan R., Leeds J.M., Tyavanagimatt S., Hruby D.E. Development of ST-246(R) for Treatment of Poxvirus Infections. Viruses 2010, 2:2409-2435.
    • (2010) Viruses , vol.2 , pp. 2409-2435
    • Jordan, R.1    Leeds, J.M.2    Tyavanagimatt, S.3    Hruby, D.E.4
  • 98
    • 4344678806 scopus 로고    scopus 로고
    • Fluoroquinolone-dependent DNA supercoiling by Vaccinia topoisomerase I
    • Kamau E., Grove A. Fluoroquinolone-dependent DNA supercoiling by Vaccinia topoisomerase I. J. Mol. Biol. 2004, 342:479-487.
    • (2004) J. Mol. Biol. , vol.342 , pp. 479-487
    • Kamau, E.1    Grove, A.2
  • 99
    • 0028981988 scopus 로고
    • Adenosine N1-oxide inhibits vaccinia virus replication by blocking translation of viral early mRNAs
    • Kane E.M., Shuman S. Adenosine N1-oxide inhibits vaccinia virus replication by blocking translation of viral early mRNAs. J. Virol. 1995, 69:6352-6358.
    • (1995) J. Virol. , vol.69 , pp. 6352-6358
    • Kane, E.M.1    Shuman, S.2
  • 100
    • 36949007602 scopus 로고    scopus 로고
    • Discovery of small molecule inhibitors of ubiquitin-like poxvirus proteinase I7L using homology modeling and covalent docking approaches
    • Katritch V., Byrd C.M., Tseitin V., Dai D., Raush E., Totrov M., Abagyan R., Jordan R., Hruby D.E. Discovery of small molecule inhibitors of ubiquitin-like poxvirus proteinase I7L using homology modeling and covalent docking approaches. J. Comput. Aided Mol. Des. 2007, 21:549-558.
    • (2007) J. Comput. Aided Mol. Des. , vol.21 , pp. 549-558
    • Katritch, V.1    Byrd, C.M.2    Tseitin, V.3    Dai, D.4    Raush, E.5    Totrov, M.6    Abagyan, R.7    Jordan, R.8    Hruby, D.E.9
  • 101
    • 34848865040 scopus 로고    scopus 로고
    • Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions
    • Katsafanas G.C., Moss B. Colocalization of transcription and translation within cytoplasmic poxvirus factories coordinates viral expression and subjugates host functions. Cell Host Microbe 2007, 2:221-228.
    • (2007) Cell Host Microbe , vol.2 , pp. 221-228
    • Katsafanas, G.C.1    Moss, B.2
  • 102
    • 0025286897 scopus 로고
    • Role of DNA replication in vaccinia virus gene expression: a naked template is required for transcription of three late trans-activator genes
    • Keck J.G., Baldick C.J., Moss B. Role of DNA replication in vaccinia virus gene expression: a naked template is required for transcription of three late trans-activator genes. Cell 1990, 61:801-809.
    • (1990) Cell , vol.61 , pp. 801-809
    • Keck, J.G.1    Baldick, C.J.2    Moss, B.3
  • 105
    • 0037282348 scopus 로고    scopus 로고
    • In vitro activity of potential anti-poxvirus agents
    • Kern E.R. In vitro activity of potential anti-poxvirus agents. Antiviral Res. 2003, 57:35-40.
    • (2003) Antiviral Res. , vol.57 , pp. 35-40
    • Kern, E.R.1
  • 106
    • 0035198155 scopus 로고    scopus 로고
    • The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymerase
    • Klemperer N., McDonald W., Boyle K., Unger B., Traktman P. The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymerase. J. Virol. 2001, 75:12298-12307.
    • (2001) J. Virol. , vol.75 , pp. 12298-12307
    • Klemperer, N.1    McDonald, W.2    Boyle, K.3    Unger, B.4    Traktman, P.5
  • 107
    • 79954592899 scopus 로고    scopus 로고
    • Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701
    • Koksal A.C., Cingolani G. Dimerization of Vaccinia virus VH1 is essential for dephosphorylation of STAT1 at tyrosine 701. J. Biol. Chem. 2011, 286:14373-14382.
    • (2011) J. Biol. Chem. , vol.286 , pp. 14373-14382
    • Koksal, A.C.1    Cingolani, G.2
  • 108
    • 33845245359 scopus 로고    scopus 로고
    • Mutations in the E9L polymerase gene of cidofovir-resistant vaccinia virus strain WR are associated with the drug resistance phenotype
    • Kornbluth R.S., Smee D.F., Sidwell R.W., Snarsky V., Evans D.H., Hostetler K.Y. Mutations in the E9L polymerase gene of cidofovir-resistant vaccinia virus strain WR are associated with the drug resistance phenotype. Antimicrob. Agents Chemother. 2006, 50:4038-4043.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 4038-4043
    • Kornbluth, R.S.1    Smee, D.F.2    Sidwell, R.W.3    Snarsky, V.4    Evans, D.H.5    Hostetler, K.Y.6
  • 109
    • 0033957173 scopus 로고    scopus 로고
    • Vaccinia virus gene A18R DNA helicase is a transcript release factor
    • Lackner C.A., Condit R.C. Vaccinia virus gene A18R DNA helicase is a transcript release factor. J. Biol. Chem. 2000, 275:1485-1494.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1485-1494
    • Lackner, C.A.1    Condit, R.C.2
  • 111
    • 0034630342 scopus 로고    scopus 로고
    • The vaccinia virus bifunctional gene J3 (nucleoside-2'-O-)-methyltransferase and poly(A) polymerase stimulatory factor is implicated as a positive transcription elongation factor by two genetic approaches
    • Latner D.R., Xiang Y., Lewis J.I., Condit J., Condit R.C. The vaccinia virus bifunctional gene J3 (nucleoside-2'-O-)-methyltransferase and poly(A) polymerase stimulatory factor is implicated as a positive transcription elongation factor by two genetic approaches. Virology 2000, 269:345-355.
    • (2000) Virology , vol.269 , pp. 345-355
    • Latner, D.R.1    Xiang, Y.2    Lewis, J.I.3    Condit, J.4    Condit, R.C.5
  • 112
    • 0036395075 scopus 로고    scopus 로고
    • The positive transcription elongation factor activity of the vaccinia virus J3 protein is independent from its (nucleoside-2'-O-) methyltransferase and poly(A) polymerase stimulatory functions
    • Latner D.R., Thompson J.M., Gershon P.D., Storrs C., Condit R.C. The positive transcription elongation factor activity of the vaccinia virus J3 protein is independent from its (nucleoside-2'-O-) methyltransferase and poly(A) polymerase stimulatory functions. Virology 2002, 301:64-80.
    • (2002) Virology , vol.301 , pp. 64-80
    • Latner, D.R.1    Thompson, J.M.2    Gershon, P.D.3    Storrs, C.4    Condit, R.C.5
  • 115
    • 0035234114 scopus 로고    scopus 로고
    • Strengthening national preparedness for smallpox: an update
    • LeDuc J.W., Jahrling P.B. Strengthening national preparedness for smallpox: an update. Emerg. Infect. Dis. 2001, 7:155-157.
    • (2001) Emerg. Infect. Dis. , vol.7 , pp. 155-157
    • LeDuc, J.W.1    Jahrling, P.B.2
  • 117
    • 13444283827 scopus 로고    scopus 로고
    • Poxvirus Bioinformatics Resource Center: a comprehensive Poxviridae informational and analytical resource
    • Lefkowitz E.J., Upton C., Changayil S.S., Buck C., Traktman P., Buller R.M. Poxvirus Bioinformatics Resource Center: a comprehensive Poxviridae informational and analytical resource. Nucleic Acids Res. 2005, 33:D311-316.
    • (2005) Nucleic Acids Res. , vol.33
    • Lefkowitz, E.J.1    Upton, C.2    Changayil, S.S.3    Buck, C.4    Traktman, P.5    Buller, R.M.6
  • 120
    • 0028136694 scopus 로고
    • Vaccinia protein kinase 2: a second essential serine/threonine protein kinase encoded by vaccinia virus
    • Lin S., Broyles S.S. Vaccinia protein kinase 2: a second essential serine/threonine protein kinase encoded by vaccinia virus. Proc. Natl. Acad. Sci. USA 1994, 91:7653-7657.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7653-7657
    • Lin, S.1    Broyles, S.S.2
  • 121
    • 0028840684 scopus 로고
    • The dual-specificity phosphatase encoded by vaccinia virus, VH1, is essential for viral transcription in vivo and in vitro
    • Liu K., Lemon B., Traktman P. The dual-specificity phosphatase encoded by vaccinia virus, VH1, is essential for viral transcription in vivo and in vitro. J. Virol. 1995, 69:7823-7834.
    • (1995) J. Virol. , vol.69 , pp. 7823-7834
    • Liu, K.1    Lemon, B.2    Traktman, P.3
  • 122
    • 23044457366 scopus 로고    scopus 로고
    • Mechanism of inhibition of vaccinia virus DNA polymerase by cidofovir diphosphate
    • Magee W.C., Hostetler K.Y., Evans D.H. Mechanism of inhibition of vaccinia virus DNA polymerase by cidofovir diphosphate. Antimicrob. Agents Chemother. 2005, 49:3153-3162.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 3153-3162
    • Magee, W.C.1    Hostetler, K.Y.2    Evans, D.H.3
  • 123
    • 38649102173 scopus 로고    scopus 로고
    • Cidofovir and (S)-9-[3-hydroxy-(2-phosphonomethoxy)propyl]adenine are highly effective inhibitors of vaccinia virus DNA polymerase when incorporated into the template strand
    • Magee W.C., Aldern K.A., Hostetler K.Y., Evans D.H. Cidofovir and (S)-9-[3-hydroxy-(2-phosphonomethoxy)propyl]adenine are highly effective inhibitors of vaccinia virus DNA polymerase when incorporated into the template strand. Antimicrob. Agents Chemother. 2008, 52:586-597.
    • (2008) Antimicrob. Agents Chemother. , vol.52 , pp. 586-597
    • Magee, W.C.1    Aldern, K.A.2    Hostetler, K.Y.3    Evans, D.H.4
  • 125
    • 79952412212 scopus 로고    scopus 로고
    • Participation of vaccinia virus l2 protein in the formation of crescent membranes and immature virions
    • Maruri-Avidal L., Domi A., Weisberg A.S., Moss B. Participation of vaccinia virus l2 protein in the formation of crescent membranes and immature virions. J. Virol. 2011, 85:2504-2511.
    • (2011) J. Virol. , vol.85 , pp. 2504-2511
    • Maruri-Avidal, L.1    Domi, A.2    Weisberg, A.S.3    Moss, B.4
  • 126
    • 0028099339 scopus 로고
    • Vaccinia virus DNA polymerase. In vitro analysis of parameters affecting processivity
    • McDonald W.F., Traktman P. Vaccinia virus DNA polymerase. In vitro analysis of parameters affecting processivity. J. Biol. Chem. 1994, 269:31190-31197.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31190-31197
    • McDonald, W.F.1    Traktman, P.2
  • 127
    • 33646737887 scopus 로고    scopus 로고
    • Vaccinia complications and methisazone therapy
    • McLean D.M. Vaccinia complications and methisazone therapy. Clin. Infect. Dis. 2006, 42:1653.
    • (2006) Clin. Infect. Dis. , vol.42 , pp. 1653
    • McLean, D.M.1
  • 128
    • 0025848811 scopus 로고
    • Genetic and molecular biological characterization of a vaccinia virus gene which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT)
    • Meis R.J., Condit R.C. Genetic and molecular biological characterization of a vaccinia virus gene which renders the virus dependent on isatin-beta-thiosemicarbazone (IBT). Virology 1991, 182:442-454.
    • (1991) Virology , vol.182 , pp. 442-454
    • Meis, R.J.1    Condit, R.C.2
  • 129
    • 0141570574 scopus 로고    scopus 로고
    • Plasma membrane budding as an alternative release mechanism of the extracellular enveloped form of vaccinia virus from HeLa cells
    • Meiser A., Sancho C., Krijnse Locker J. Plasma membrane budding as an alternative release mechanism of the extracellular enveloped form of vaccinia virus from HeLa cells. J. Virol. 2003, 77:9931-9942.
    • (2003) J. Virol. , vol.77 , pp. 9931-9942
    • Meiser, A.1    Sancho, C.2    Krijnse Locker, J.3
  • 130
    • 0038651056 scopus 로고    scopus 로고
    • Multistate outbreak of monkeypox - Illinois, Indiana, and Wisconsin, 2003
    • Melnick, et al. Multistate outbreak of monkeypox - Illinois, Indiana, and Wisconsin, 2003. MMWR Morb. Mortal. Wkly Rep. 2003, 52:537-540.
    • (2003) MMWR Morb. Mortal. Wkly Rep. , vol.52 , pp. 537-540
    • Melnick et, al.1
  • 131
    • 18744395205 scopus 로고    scopus 로고
    • Genetic and cell biological characterization of the vaccinia virus A30 and G7 phosphoproteins
    • Mercer J., Traktman P. Genetic and cell biological characterization of the vaccinia virus A30 and G7 phosphoproteins. J. Virol. 2005, 79:7146-7161.
    • (2005) J. Virol. , vol.79 , pp. 7146-7161
    • Mercer, J.1    Traktman, P.2
  • 132
    • 0035261891 scopus 로고    scopus 로고
    • Interaction between the J3R subunit of vaccinia virus poly(A) polymerase and the H4L subunit of the viral RNA polymerase
    • Mohamed M.R., Latner D.R., Condit R.C., Niles E.G. Interaction between the J3R subunit of vaccinia virus poly(A) polymerase and the H4L subunit of the viral RNA polymerase. Virology 2001, 280:143-152.
    • (2001) Virology , vol.280 , pp. 143-152
    • Mohamed, M.R.1    Latner, D.R.2    Condit, R.C.3    Niles, E.G.4
  • 133
    • 77649253974 scopus 로고    scopus 로고
    • Vaccinia protein F12 has structural similarity to kinesin light chain and contains a motor binding motif required for virion export
    • Morgan G.W., Hollinshead M., Ferguson B.J., Murphy B.J., Carpentier D.C., Smith G.L. Vaccinia protein F12 has structural similarity to kinesin light chain and contains a motor binding motif required for virion export. PLoS Pathog. 2010, 6:e1000785.
    • (2010) PLoS Pathog. , vol.6
    • Morgan, G.W.1    Hollinshead, M.2    Ferguson, B.J.3    Murphy, B.J.4    Carpentier, D.C.5    Smith, G.L.6
  • 134
    • 0001142643 scopus 로고    scopus 로고
    • Poxviridae: the viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, B.N. Fields, D.M. Knipe, P.M. Howley, D.E. Griffin (Eds.)
    • Moss B. Poxviridae: the viruses and their replication. Fields' Virology 2001, 3087. Lippincott Williams & Wilkins, Philadelphia. fourth ed. B.N. Fields, D.M. Knipe, P.M. Howley, D.E. Griffin (Eds.).
    • (2001) Fields' Virology , pp. 3087
    • Moss, B.1
  • 135
    • 29144519316 scopus 로고    scopus 로고
    • Poxvirus entry and membrane fusion
    • Moss B. Poxvirus entry and membrane fusion. Virology 2006, 344:48-54.
    • (2006) Virology , vol.344 , pp. 48-54
    • Moss, B.1
  • 136
    • 42449154473 scopus 로고    scopus 로고
    • Poxviridae: The viruses and Their Replication
    • Lippincott Williams & Wilkins, a Wolters Kluwer Business, Philadelphia, PA, D.M. Knipe, P.M. Howley (Eds.)
    • Moss B. Poxviridae: The viruses and Their Replication. Fields Virology 2007, 2905-2946. Lippincott Williams & Wilkins, a Wolters Kluwer Business, Philadelphia, PA. D.M. Knipe, P.M. Howley (Eds.).
    • (2007) Fields Virology , pp. 2905-2946
    • Moss, B.1
  • 137
    • 33646164166 scopus 로고    scopus 로고
    • Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity
    • Moure C.M., Bowman B.R., Gershon P.D., Quiocho F.A. Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity. Mol. Cell 2006, 22:339-349.
    • (2006) Mol. Cell , vol.22 , pp. 339-349
    • Moure, C.M.1    Bowman, B.R.2    Gershon, P.D.3    Quiocho, F.A.4
  • 138
    • 67650700335 scopus 로고    scopus 로고
    • When good vaccines go wild: Feral Orthopoxvirus in developing countries and beyond
    • Moussatche N., Damaso C.R., McFadden G. When good vaccines go wild: Feral Orthopoxvirus in developing countries and beyond. J. Infect. Dev. Ctries 2008, 2:156-173.
    • (2008) J. Infect. Dev. Ctries , vol.2 , pp. 156-173
    • Moussatche, N.1    Damaso, C.R.2    McFadden, G.3
  • 139
    • 33947397199 scopus 로고    scopus 로고
    • Aurintricarboxylic acid inhibits the early stage of vaccinia virus replication by targeting both cellular and viral factors
    • Myskiw C., Deschambault Y., Jefferies K., He R., Cao J. Aurintricarboxylic acid inhibits the early stage of vaccinia virus replication by targeting both cellular and viral factors. J. Virol. 2007, 81:3027-3032.
    • (2007) J. Virol. , vol.81 , pp. 3027-3032
    • Myskiw, C.1    Deschambault, Y.2    Jefferies, K.3    He, R.4    Cao, J.5
  • 140
    • 78650244224 scopus 로고    scopus 로고
    • Nigericin is a potent inhibitor of the early stage of vaccinia virus replication
    • Myskiw C., Piper J., Huzarewich R., Booth T.F., Cao J., He R. Nigericin is a potent inhibitor of the early stage of vaccinia virus replication. Antiviral Res. 2010, 88:304-310.
    • (2010) Antiviral Res. , vol.88 , pp. 304-310
    • Myskiw, C.1    Piper, J.2    Huzarewich, R.3    Booth, T.F.4    Cao, J.5    He, R.6
  • 141
    • 0031036704 scopus 로고    scopus 로고
    • HPMPC (cidofovir), PMEA (adefovir) and related acyclic nucleoside phosphonate analogues: a review of their pharmacology and clinical potential in the treatment of viral infections
    • Naesens L., Snoeck R., Andrei G., Balzarini J., Neyts J., De Clercq E. HPMPC (cidofovir), PMEA (adefovir) and related acyclic nucleoside phosphonate analogues: a review of their pharmacology and clinical potential in the treatment of viral infections. Antiviral Chem. Chemother. 1997, 8:1-23.
    • (1997) Antiviral Chem. Chemother. , vol.8 , pp. 1-23
    • Naesens, L.1    Snoeck, R.2    Andrei, G.3    Balzarini, J.4    Neyts, J.5    De Clercq, E.6
  • 142
    • 53249083929 scopus 로고    scopus 로고
    • Vaccinia virus entry/fusion complex subunit A28 is a target of neutralizing and protective antibodies
    • Nelson G.E., Sisler J.R., Chandran D., Moss B. Vaccinia virus entry/fusion complex subunit A28 is a target of neutralizing and protective antibodies. Virology 2008, 380:394-401.
    • (2008) Virology , vol.380 , pp. 394-401
    • Nelson, G.E.1    Sisler, J.R.2    Chandran, D.3    Moss, B.4
  • 143
  • 144
    • 6044223321 scopus 로고    scopus 로고
    • SRC mediates a switch from microtubule- to actin-based motility of vaccinia virus
    • Newsome T.P., Scaplehorn N., Way M. SRC mediates a switch from microtubule- to actin-based motility of vaccinia virus. Science 2004, 306:124-129.
    • (2004) Science , vol.306 , pp. 124-129
    • Newsome, T.P.1    Scaplehorn, N.2    Way, M.3
  • 145
    • 0027431547 scopus 로고
    • Efficacy of (S)-1-(3-hydroxy-2-phosphonylmethoxypropyl)cytosine for the treatment of lethal vaccinia virus infections in severe combined immune deficiency (SCID) mice
    • Neyts J., De Clercq E. Efficacy of (S)-1-(3-hydroxy-2-phosphonylmethoxypropyl)cytosine for the treatment of lethal vaccinia virus infections in severe combined immune deficiency (SCID) mice. J. Med. Virol. 1993, 41:242-246.
    • (1993) J. Med. Virol. , vol.41 , pp. 242-246
    • Neyts, J.1    De Clercq, E.2
  • 146
    • 0035162626 scopus 로고    scopus 로고
    • Efficacy of 2-amino-7-(1,3-dihydroxy-2-propoxymethyl)purine for treatment of vaccinia virus (orthopoxvirus) infections in mice
    • Neyts J., De Clercq E. Efficacy of 2-amino-7-(1,3-dihydroxy-2-propoxymethyl)purine for treatment of vaccinia virus (orthopoxvirus) infections in mice. Antimicrob. Agents Chemother. 2001, 45:84-87.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 84-87
    • Neyts, J.1    De Clercq, E.2
  • 147
    • 0037282284 scopus 로고    scopus 로고
    • Therapy and short-term prophylaxis of poxvirus infections: historical background and perspectives
    • Neyts J., De Clercq E. Therapy and short-term prophylaxis of poxvirus infections: historical background and perspectives. Antiviral Res. 2003, 57:25-33.
    • (2003) Antiviral Res. , vol.57 , pp. 25-33
    • Neyts, J.1    De Clercq, E.2
  • 148
    • 0036720998 scopus 로고    scopus 로고
    • Effect of 5-iodo-2'-deoxyuridine on vaccinia virus (orthopoxvirus) infections in mice
    • Neyts J., Verbeken E., De Clercq E. Effect of 5-iodo-2'-deoxyuridine on vaccinia virus (orthopoxvirus) infections in mice. Antimicrob. Agents Chemother. 2002, 46:2842-2847.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2842-2847
    • Neyts, J.1    Verbeken, E.2    De Clercq, E.3
  • 149
    • 29444454707 scopus 로고    scopus 로고
    • Entry of vaccinia virus and cell-cell fusion require a highly conserved cysteine-rich membrane protein encoded by the A16L gene
    • Ojeda S., Senkevich T.G., Moss B. Entry of vaccinia virus and cell-cell fusion require a highly conserved cysteine-rich membrane protein encoded by the A16L gene. J. Virol. 2006, 80:51-61.
    • (2006) J. Virol. , vol.80 , pp. 51-61
    • Ojeda, S.1    Senkevich, T.G.2    Moss, B.3
  • 151
    • 79952169957 scopus 로고    scopus 로고
    • Ectromelia virus infections of mice as a model to support the licensure of anti-orthopoxvirus therapeutics
    • Parker S., Siddiqui A.M., Painter G., Schriewer J., Buller R.M. Ectromelia virus infections of mice as a model to support the licensure of anti-orthopoxvirus therapeutics. Viruses 2010, 2:1918-1932.
    • (2010) Viruses , vol.2 , pp. 1918-1932
    • Parker, S.1    Siddiqui, A.M.2    Painter, G.3    Schriewer, J.4    Buller, R.M.5
  • 152
    • 33847779501 scopus 로고    scopus 로고
    • Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression
    • Parrish S., Resch W., Moss B. Vaccinia virus D10 protein has mRNA decapping activity, providing a mechanism for control of host and viral gene expression. Proc. Natl. Acad. Sci. USA 2007, 104:2139-2144.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2139-2144
    • Parrish, S.1    Resch, W.2    Moss, B.3
  • 153
    • 0021925847 scopus 로고
    • Extracellular release of enveloped vaccinia virus from mouse nasal epithelial cells in vivo
    • Payne L.G., Kristensson K. Extracellular release of enveloped vaccinia virus from mouse nasal epithelial cells in vivo. J. Gen. Virol. 1985, 66(Pt 3):643-646.
    • (1985) J. Gen. Virol. , vol.66 , Issue.PART 3 , pp. 643-646
    • Payne, L.G.1    Kristensson, K.2
  • 154
    • 0034075555 scopus 로고    scopus 로고
    • Characterization of vaccinia virus intracellular cores: implications for viral uncoating and core structure
    • Pedersen K., Snijder E.J., Schleich S., Roos N., Griffiths G., Locker J.K. Characterization of vaccinia virus intracellular cores: implications for viral uncoating and core structure. J. Virol. 2000, 74:3525-3536.
    • (2000) J. Virol. , vol.74 , pp. 3525-3536
    • Pedersen, K.1    Snijder, E.J.2    Schleich, S.3    Roos, N.4    Griffiths, G.5    Locker, J.K.6
  • 156
    • 33748671566 scopus 로고    scopus 로고
    • Interaction between vaccinia virus extracellular virus envelope A33 and B5 glycoproteins
    • Perdiguero B., Blasco R. Interaction between vaccinia virus extracellular virus envelope A33 and B5 glycoproteins. J. Virol. 2006, 80:8763-8777.
    • (2006) J. Virol. , vol.80 , pp. 8763-8777
    • Perdiguero, B.1    Blasco, R.2
  • 157
    • 39749149673 scopus 로고    scopus 로고
    • Vaccinia virus A34 glycoprotein determines the protein composition of the extracellular virus envelope
    • Perdiguero B., Lorenzo M.M., Blasco R. Vaccinia virus A34 glycoprotein determines the protein composition of the extracellular virus envelope. J. Virol. 2008, 82:2150-2160.
    • (2008) J. Virol. , vol.82 , pp. 2150-2160
    • Perdiguero, B.1    Lorenzo, M.M.2    Blasco, R.3
  • 158
    • 17444427138 scopus 로고    scopus 로고
    • Combinatorial optimization of isatin-beta-thiosemicarbazones as anti-poxvirus agents
    • Pirrung M.C., Pansare S.V., Sarma K.D., Keith K.A., Kern E.R. Combinatorial optimization of isatin-beta-thiosemicarbazones as anti-poxvirus agents. J. Med. Chem. 2005, 48:3045-3050.
    • (2005) J. Med. Chem. , vol.48 , pp. 3045-3050
    • Pirrung, M.C.1    Pansare, S.V.2    Sarma, K.D.3    Keith, K.A.4    Kern, E.R.5
  • 159
    • 78650254596 scopus 로고    scopus 로고
    • Inhibition of poxvirus growth by Terameprocol, a methylated derivative of nordihydroguaiaretic acid
    • Pollara J.J., Laster S.M., Petty I.T. Inhibition of poxvirus growth by Terameprocol, a methylated derivative of nordihydroguaiaretic acid. Antiviral Res. 2010, 88:287-295.
    • (2010) Antiviral Res. , vol.88 , pp. 287-295
    • Pollara, J.J.1    Laster, S.M.2    Petty, I.T.3
  • 160
    • 16344381518 scopus 로고    scopus 로고
    • Orthopoxvirus targets for the development of antiviral therapies
    • Prichard M.N., Kern E.R. Orthopoxvirus targets for the development of antiviral therapies. Curr. Drug Targets Infect. Disord. 2005, 5:17-28.
    • (2005) Curr. Drug Targets Infect. Disord. , vol.5 , pp. 17-28
    • Prichard, M.N.1    Kern, E.R.2
  • 162
    • 79952158137 scopus 로고    scopus 로고
    • Antiviral Activity of 4'-thioIDU and Thymidine Analogs against Orthopoxviruses
    • Prichard M.N., Kern E.R. Antiviral Activity of 4'-thioIDU and Thymidine Analogs against Orthopoxviruses. Viruses 2010, 2:1968-1983.
    • (2010) Viruses , vol.2 , pp. 1968-1983
    • Prichard, M.N.1    Kern, E.R.2
  • 163
    • 33645773912 scopus 로고    scopus 로고
    • Activity and mechanism of action of N-methanocarbathymidine against herpesvirus and orthopoxvirus infections
    • Prichard M.N., Keith K.A., Quenelle D.C., Kern E.R. Activity and mechanism of action of N-methanocarbathymidine against herpesvirus and orthopoxvirus infections. Antimicrob. Agents Chemother. 2006, 50:1336-1341.
    • (2006) Antimicrob. Agents Chemother. , vol.50 , pp. 1336-1341
    • Prichard, M.N.1    Keith, K.A.2    Quenelle, D.C.3    Kern, E.R.4
  • 165
    • 13444263330 scopus 로고    scopus 로고
    • Cell biological and functional characterization of the vaccinia virus F10 kinase: implications for the mechanism of virion morphogenesis
    • Punjabi A., Traktman P. Cell biological and functional characterization of the vaccinia virus F10 kinase: implications for the mechanism of virion morphogenesis. J. Virol. 2005, 79:2171-2190.
    • (2005) J. Virol. , vol.79 , pp. 2171-2190
    • Punjabi, A.1    Traktman, P.2
  • 166
    • 84855855161 scopus 로고    scopus 로고
    • Genomic analysis of the vaccinia virus strain variants found in Dryvax vaccine
    • Qin L., Upton C., Hazes B., Evans D.H. Genomic analysis of the vaccinia virus strain variants found in Dryvax vaccine. J. Virol. 2011.
    • (2011) J. Virol.
    • Qin, L.1    Upton, C.2    Hazes, B.3    Evans, D.H.4
  • 167
    • 0141994005 scopus 로고    scopus 로고
    • Efficacy of multiple- or single-dose cidofovir against vaccinia and cowpox virus infections in mice
    • Quenelle D.C., Collins D.J., Kern E.R. Efficacy of multiple- or single-dose cidofovir against vaccinia and cowpox virus infections in mice. Antimicrob. Agents Chemother. 2003, 47:3275-3280.
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 3275-3280
    • Quenelle, D.C.1    Collins, D.J.2    Kern, E.R.3
  • 168
    • 2942657054 scopus 로고    scopus 로고
    • Cutaneous infections of mice with vaccinia or cowpox viruses and efficacy of cidofovir
    • Quenelle D.C., Collins D.J., Kern E.R. Cutaneous infections of mice with vaccinia or cowpox viruses and efficacy of cidofovir. Antiviral Res. 2004, 63:33-40.
    • (2004) Antiviral Res. , vol.63 , pp. 33-40
    • Quenelle, D.C.1    Collins, D.J.2    Kern, E.R.3
  • 170
    • 33745211022 scopus 로고    scopus 로고
    • In vitro and in vivo evaluation of isatin-beta-thiosemicarbazone and marboran against vaccinia and cowpox virus infections
    • Quenelle D.C., Keith K.A., Kern E.R. In vitro and in vivo evaluation of isatin-beta-thiosemicarbazone and marboran against vaccinia and cowpox virus infections. Antiviral Res. 2006, 71:24-30.
    • (2006) Antiviral Res. , vol.71 , pp. 24-30
    • Quenelle, D.C.1    Keith, K.A.2    Kern, E.R.3
  • 173
    • 78349234678 scopus 로고    scopus 로고
    • Efficacy of CMX001 against herpes simplex virus infections in mice and correlations with drug distribution studies
    • Quenelle D.C., Lampert B., Collins D.J., Rice T.L., Painter G.R., Kern E.R. Efficacy of CMX001 against herpes simplex virus infections in mice and correlations with drug distribution studies. J. Infect. Dis. 2010, 202:1492-1499.
    • (2010) J. Infect. Dis. , vol.202 , pp. 1492-1499
    • Quenelle, D.C.1    Lampert, B.2    Collins, D.J.3    Rice, T.L.4    Painter, G.R.5    Kern, E.R.6
  • 176
    • 78650053134 scopus 로고    scopus 로고
    • Variola and monkeypox viruses utilize conserved mechanisms of virion motility and release that depend on abl and SRC family tyrosine kinases
    • Reeves P.M., Smith S.K., Olson V.A., Thorne S.H., Bornmann W., Damon I.K., Kalman D. Variola and monkeypox viruses utilize conserved mechanisms of virion motility and release that depend on abl and SRC family tyrosine kinases. J. Virol. 2011, 85:21-31.
    • (2011) J. Virol. , vol.85 , pp. 21-31
    • Reeves, P.M.1    Smith, S.K.2    Olson, V.A.3    Thorne, S.H.4    Bornmann, W.5    Damon, I.K.6    Kalman, D.7
  • 177
    • 0026777795 scopus 로고
    • Vaccinia virus B1 kinase: phenotypic analysis of temperature-sensitive mutants and enzymatic characterization of recombinant proteins
    • Rempel R.E., Traktman P. Vaccinia virus B1 kinase: phenotypic analysis of temperature-sensitive mutants and enzymatic characterization of recombinant proteins. J. Virol. 1992, 66:4413-4426.
    • (1992) J. Virol. , vol.66 , pp. 4413-4426
    • Rempel, R.E.1    Traktman, P.2
  • 178
    • 18744365510 scopus 로고    scopus 로고
    • Vaccinia virus nonstructural protein encoded by the A11R gene is required for formation of the virion membrane
    • Resch W., Weisberg A.S., Moss B. Vaccinia virus nonstructural protein encoded by the A11R gene is required for formation of the virion membrane. J. Virol. 2005, 79:6598-6609.
    • (2005) J. Virol. , vol.79 , pp. 6598-6609
    • Resch, W.1    Weisberg, A.S.2    Moss, B.3
  • 179
    • 53049097995 scopus 로고    scopus 로고
    • Vaccinia virus morphogenesis and dissemination
    • Roberts K.L., Smith G.L. Vaccinia virus morphogenesis and dissemination. Trends Microbiol. 2008, 16:472-479.
    • (2008) Trends Microbiol. , vol.16 , pp. 472-479
    • Roberts, K.L.1    Smith, G.L.2
  • 180
    • 0023002660 scopus 로고
    • Conserved TAAATG sequence at the transcriptional and translational initiation sites of vaccinia virus late genes deduced by structural and functional analysis of the HindIII H genome fragment
    • Rosel J.L., Earl P.L., Weir J.P., Moss B. Conserved TAAATG sequence at the transcriptional and translational initiation sites of vaccinia virus late genes deduced by structural and functional analysis of the HindIII H genome fragment. J. Virol. 1986, 60:436-449.
    • (1986) J. Virol. , vol.60 , pp. 436-449
    • Rosel, J.L.1    Earl, P.L.2    Weir, J.P.3    Moss, B.4
  • 183
    • 0033971767 scopus 로고    scopus 로고
    • The vaccinia virus A27L protein is needed for the microtubule-dependent transport of intracellular mature virus particles
    • Sanderson C.M., Hollinshead M., Smith G.L. The vaccinia virus A27L protein is needed for the microtubule-dependent transport of intracellular mature virus particles. J. Gen. Virol. 2000, 81:47-58.
    • (2000) J. Gen. Virol. , vol.81 , pp. 47-58
    • Sanderson, C.M.1    Hollinshead, M.2    Smith, G.L.3
  • 184
    • 5344223369 scopus 로고    scopus 로고
    • The vaccinia virus B1R kinase induces p53 downregulation by an Mdm2-dependent mechanism
    • Santos C.R., Vega F.M., Blanco S., Barcia R., Lazo P.A. The vaccinia virus B1R kinase induces p53 downregulation by an Mdm2-dependent mechanism. Virology 2004, 328:254-265.
    • (2004) Virology , vol.328 , pp. 254-265
    • Santos, C.R.1    Vega, F.M.2    Blanco, S.3    Barcia, R.4    Lazo, P.A.5
  • 185
    • 33746210118 scopus 로고    scopus 로고
    • Vaccinia virus B1R kinase interacts with JIP1 and modulates c-Jun-dependent signaling
    • Santos C.R., Blanco S., Sevilla A., Lazo P.A. Vaccinia virus B1R kinase interacts with JIP1 and modulates c-Jun-dependent signaling. J. Virol. 2006, 80:7667-7675.
    • (2006) J. Virol. , vol.80 , pp. 7667-7675
    • Santos, C.R.1    Blanco, S.2    Sevilla, A.3    Lazo, P.A.4
  • 186
    • 24344474790 scopus 로고    scopus 로고
    • In vitro activity of cycloSal-nucleoside monophosphates and polyhydroxycarboxylates against orthopoxviruses
    • Sauerbrei A., Meier C., Meerbach A., Schiel M., Helbig B., Wutzler P. In vitro activity of cycloSal-nucleoside monophosphates and polyhydroxycarboxylates against orthopoxviruses. Antiviral Res. 2005, 67:147-154.
    • (2005) Antiviral Res. , vol.67 , pp. 147-154
    • Sauerbrei, A.1    Meier, C.2    Meerbach, A.3    Schiel, M.4    Helbig, B.5    Wutzler, P.6
  • 187
    • 33344459771 scopus 로고    scopus 로고
    • Inhibitory efficacy of cyclosal-nucleoside monophosphates of aciclovir and brivudin on DNA synthesis of orthopoxvi ruses
    • Sauerbrei A., Meier C., Meerbach A., Wutzler P. Inhibitory efficacy of cyclosal-nucleoside monophosphates of aciclovir and brivudin on DNA synthesis of orthopoxvi ruses. Antiviral Chem. Chemother. 2006, 17:25-31.
    • (2006) Antiviral Chem. Chemother. , vol.17 , pp. 25-31
    • Sauerbrei, A.1    Meier, C.2    Meerbach, A.3    Wutzler, P.4
  • 188
    • 0025820492 scopus 로고
    • A mutation in the gene encoding the vaccinia virus 37,000-M(r) protein confers resistance to an inhibitor of virus envelopment and release
    • Schmutz C., Payne L.G., Gubser J., Wittek R. A mutation in the gene encoding the vaccinia virus 37,000-M(r) protein confers resistance to an inhibitor of virus envelopment and release. J. Virol. 1991, 65:3435-3442.
    • (1991) J. Virol. , vol.65 , pp. 3435-3442
    • Schmutz, C.1    Payne, L.G.2    Gubser, J.3    Wittek, R.4
  • 190
    • 33746518147 scopus 로고    scopus 로고
    • Genetic analysis of poxvirus mRNA cap methyltransferase: suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit
    • Schwer B., Shuman S. Genetic analysis of poxvirus mRNA cap methyltransferase: suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit. Virology 2006, 352:145-156.
    • (2006) Virology , vol.352 , pp. 145-156
    • Schwer, B.1    Shuman, S.2
  • 191
    • 0030813809 scopus 로고    scopus 로고
    • Nick sensing by vaccinia virus DNA ligase requires a 5' phosphate at the nick and occupancy of the adenylate binding site on the enzyme
    • Sekiguchi J., Shuman S. Nick sensing by vaccinia virus DNA ligase requires a 5' phosphate at the nick and occupancy of the adenylate binding site on the enzyme. J. Virol. 1997, 71:9679-9684.
    • (1997) J. Virol. , vol.71 , pp. 9679-9684
    • Sekiguchi, J.1    Shuman, S.2
  • 192
    • 0030801224 scopus 로고    scopus 로고
    • Novobiocin inhibits vaccinia virus replication by blocking virus assembly
    • Sekiguchi J., Shuman S. Novobiocin inhibits vaccinia virus replication by blocking virus assembly. Virology 1997, 235:129-137.
    • (1997) Virology , vol.235 , pp. 129-137
    • Sekiguchi, J.1    Shuman, S.2
  • 193
    • 0037076339 scopus 로고    scopus 로고
    • Complete pathway for protein disulfide bond formation encoded by poxviruses
    • Senkevich T.G., White C.L., Koonin E.V., Moss B. Complete pathway for protein disulfide bond formation encoded by poxviruses. Proc. Natl. Acad. Sci. USA 2002, 99:6667-6672.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6667-6672
    • Senkevich, T.G.1    White, C.L.2    Koonin, E.V.3    Moss, B.4
  • 195
    • 0015523596 scopus 로고
    • Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide
    • Sidwell R.W., Huffman J.H., Khare G.P., Allen L.B., Witkowski J.T., Robins R.K. Broad-spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide. Science 1972, 177:705-706.
    • (1972) Science , vol.177 , pp. 705-706
    • Sidwell, R.W.1    Huffman, J.H.2    Khare, G.P.3    Allen, L.B.4    Witkowski, J.T.5    Robins, R.K.6
  • 197
    • 0023001921 scopus 로고
    • Hydroxyurea-resistant vaccinia virus: overproduction of ribonucleotide reductase
    • Slabaugh M.B., Mathews C.K. Hydroxyurea-resistant vaccinia virus: overproduction of ribonucleotide reductase. J. Virol. 1986, 60:506-514.
    • (1986) J. Virol. , vol.60 , pp. 506-514
    • Slabaugh, M.B.1    Mathews, C.K.2
  • 198
    • 0033819235 scopus 로고    scopus 로고
    • Intranasal treatment of cowpox virus respiratory infections in mice with cidofovir
    • Smee D.F., Bailey K.W., Wong M., Sidwell R.W. Intranasal treatment of cowpox virus respiratory infections in mice with cidofovir. Antiviral Res. 2000, 47:171-177.
    • (2000) Antiviral Res. , vol.47 , pp. 171-177
    • Smee, D.F.1    Bailey, K.W.2    Wong, M.3    Sidwell, R.W.4
  • 199
    • 0034877280 scopus 로고    scopus 로고
    • Effects of cidofovir on the pathogenesis of a lethal vaccinia virus respiratory infection in mice
    • Smee D.F., Bailey K.W., Wong M.H., Sidwell R.W. Effects of cidofovir on the pathogenesis of a lethal vaccinia virus respiratory infection in mice. Antiviral Res. 2001, 52:55-62.
    • (2001) Antiviral Res. , vol.52 , pp. 55-62
    • Smee, D.F.1    Bailey, K.W.2    Wong, M.H.3    Sidwell, R.W.4
  • 200
    • 0036239724 scopus 로고    scopus 로고
    • Characterization of wild-type and cidofovir-resistant strains of camelpox, cowpox, monkeypox, and vaccinia viruses
    • Smee D.F., Sidwell R.W., Kefauver D., Bray M., Huggins J.W. Characterization of wild-type and cidofovir-resistant strains of camelpox, cowpox, monkeypox, and vaccinia viruses. Antimicrob. Agents Chemother. 2002, 46:1329-1335.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1329-1335
    • Smee, D.F.1    Sidwell, R.W.2    Kefauver, D.3    Bray, M.4    Huggins, J.W.5
  • 201
    • 34548609026 scopus 로고    scopus 로고
    • Efficacy of N-methanocarbathymidine in treating mice infected intranasally with the IHD and WR strains of vaccinia virus
    • Smee D.F., Hurst B.L., Wong M.H., Glazer R.I., Rahman A., Sidwell R.W. Efficacy of N-methanocarbathymidine in treating mice infected intranasally with the IHD and WR strains of vaccinia virus. Antiviral Res. 2007, 76:124-129.
    • (2007) Antiviral Res. , vol.76 , pp. 124-129
    • Smee, D.F.1    Hurst, B.L.2    Wong, M.H.3    Glazer, R.I.4    Rahman, A.5    Sidwell, R.W.6
  • 202
    • 33846137993 scopus 로고    scopus 로고
    • Cell line dependency for antiviral activity and in vivo efficacy of N-methanocarbathymidine against orthopoxvirus infections in mice
    • Smee D.F., Wandersee M.K., Bailey K.W., Wong M.H., Chu C.K., Gadthula S., Sidwell R.W. Cell line dependency for antiviral activity and in vivo efficacy of N-methanocarbathymidine against orthopoxvirus infections in mice. Antiviral Res. 2007, 73:69-77.
    • (2007) Antiviral Res. , vol.73 , pp. 69-77
    • Smee, D.F.1    Wandersee, M.K.2    Bailey, K.W.3    Wong, M.H.4    Chu, C.K.5    Gadthula, S.6    Sidwell, R.W.7
  • 203
    • 47049112478 scopus 로고    scopus 로고
    • Antiviral activities and phosphorylation of 5-halo-2'-deoxyuridines and N-methanocarbathymidine in cells infected with vaccinia virus
    • Smee D.F., Humphreys D.E., Hurst B.L., Barnard D.L. Antiviral activities and phosphorylation of 5-halo-2'-deoxyuridines and N-methanocarbathymidine in cells infected with vaccinia virus. Antiviral Chem. Chemother. 2008, 19:15-24.
    • (2008) Antiviral Chem. Chemother. , vol.19 , pp. 15-24
    • Smee, D.F.1    Humphreys, D.E.2    Hurst, B.L.3    Barnard, D.L.4
  • 204
    • 77951187151 scopus 로고    scopus 로고
    • Lack of efficacy of aurintricarboxylic acid and ethacrynic acid against vaccinia virus respiratory infections in mice
    • Smee D.F., Hurst B.L., Wong M.H. Lack of efficacy of aurintricarboxylic acid and ethacrynic acid against vaccinia virus respiratory infections in mice. Antiviral Chem. Chemother. 2010, 20:201-205.
    • (2010) Antiviral Chem. Chemother. , vol.20 , pp. 201-205
    • Smee, D.F.1    Hurst, B.L.2    Wong, M.H.3
  • 205
    • 80053305871 scopus 로고    scopus 로고
    • Topical treatment of cutaneous vaccinia virus infections in immunosuppressed hairless mice with selected antiviral substances
    • Smee D.F., Bailey K.W., Wong M.H., Tarbet E.B. Topical treatment of cutaneous vaccinia virus infections in immunosuppressed hairless mice with selected antiviral substances. Antiviral Chem. Chemother. 2011, 21:201-208.
    • (2011) Antiviral Chem. Chemother. , vol.21 , pp. 201-208
    • Smee, D.F.1    Bailey, K.W.2    Wong, M.H.3    Tarbet, E.B.4
  • 206
    • 9644262461 scopus 로고    scopus 로고
    • The exit of vaccinia virus from infected cells
    • Smith G.L., Law M. The exit of vaccinia virus from infected cells. Virus Res. 2004, 106:189-197.
    • (2004) Virus Res. , vol.106 , pp. 189-197
    • Smith, G.L.1    Law, M.2
  • 207
    • 0036932713 scopus 로고    scopus 로고
    • The formation and function of extracellular enveloped vaccinia virus
    • Smith G.L., Vanderplasschen A., Law M. The formation and function of extracellular enveloped vaccinia virus. J. Gen. Virol. 2002, 83:2915-2931.
    • (2002) J. Gen. Virol. , vol.83 , pp. 2915-2931
    • Smith, G.L.1    Vanderplasschen, A.2    Law, M.3
  • 208
    • 58149474787 scopus 로고    scopus 로고
    • Ethacrynic and alpha-lipoic acids inhibit vaccinia virus late gene expression
    • Spisakova M., Cizek Z., Melkova Z. Ethacrynic and alpha-lipoic acids inhibit vaccinia virus late gene expression. Antiviral Res. 2009, 81:156-165.
    • (2009) Antiviral Res. , vol.81 , pp. 156-165
    • Spisakova, M.1    Cizek, Z.2    Melkova, Z.3
  • 209
    • 33645639121 scopus 로고    scopus 로고
    • Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase
    • Stanitsa E.S., Arps L., Traktman P. Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase. J. Biol. Chem. 2006, 281:3439-3451.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3439-3451
    • Stanitsa, E.S.1    Arps, L.2    Traktman, P.3
  • 211
    • 0027418033 scopus 로고
    • A poxvirus-encoded uracil DNA glycosylase is essential for virus viability
    • Stuart D.T., Upton C., Higman M.A., Niles E.G., McFadden G. A poxvirus-encoded uracil DNA glycosylase is essential for virus viability. J. Virol. 1993, 67:2503-2512.
    • (1993) J. Virol. , vol.67 , pp. 2503-2512
    • Stuart, D.T.1    Upton, C.2    Higman, M.A.3    Niles, E.G.4    McFadden, G.5
  • 212
    • 0037334232 scopus 로고    scopus 로고
    • Vaccinia virus G7L protein Interacts with the A30L protein and is required for association of viral membranes with dense viroplasm to form immature virions
    • Szajner P., Jaffe H., Weisberg A.S., Moss B. Vaccinia virus G7L protein Interacts with the A30L protein and is required for association of viral membranes with dense viroplasm to form immature virions. J. Virol. 2003, 77:3418-3429.
    • (2003) J. Virol. , vol.77 , pp. 3418-3429
    • Szajner, P.1    Jaffe, H.2    Weisberg, A.S.3    Moss, B.4
  • 213
    • 9644303203 scopus 로고    scopus 로고
    • A complex of seven vaccinia virus proteins conserved in all chordopoxviruses is required for the association of membranes and viroplasm to form immature virions
    • Szajner P., Jaffe H., Weisberg A.S., Moss B. A complex of seven vaccinia virus proteins conserved in all chordopoxviruses is required for the association of membranes and viroplasm to form immature virions. Virology 2004, 330:447-459.
    • (2004) Virology , vol.330 , pp. 447-459
    • Szajner, P.1    Jaffe, H.2    Weisberg, A.S.3    Moss, B.4
  • 214
    • 24944546062 scopus 로고    scopus 로고
    • External scaffold of spherical immature poxvirus particles is made of protein trimers, forming a honeycomb lattice
    • Szajner P., Weisberg A.S., Lebowitz J., Heuser J., Moss B. External scaffold of spherical immature poxvirus particles is made of protein trimers, forming a honeycomb lattice. J. Cell Biol. 2005, 170:971-981.
    • (2005) J. Cell Biol. , vol.170 , pp. 971-981
    • Szajner, P.1    Weisberg, A.S.2    Lebowitz, J.3    Heuser, J.4    Moss, B.5
  • 215
    • 33847156030 scopus 로고    scopus 로고
    • Vaccinia topoisomerase mutants illuminate roles for Phe59, Gly73, Gln69 and Phe215
    • Tian L., Shuman S. Vaccinia topoisomerase mutants illuminate roles for Phe59, Gly73, Gln69 and Phe215. Virology 2007, 359:466-476.
    • (2007) Virology , vol.359 , pp. 466-476
    • Tian, L.1    Shuman, S.2
  • 216
    • 0035157752 scopus 로고    scopus 로고
    • Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei
    • Tolonen N., Doglio L., Schleich S., Krijnse Locker J. Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei. Mol. Biol. Cell 2001, 12:2031-2046.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2031-2046
    • Tolonen, N.1    Doglio, L.2    Schleich, S.3    Krijnse Locker, J.4
  • 219
    • 4043116119 scopus 로고    scopus 로고
    • Methods for analysis of poxvirus DNA replication
    • Traktman P., Boyle K. Methods for analysis of poxvirus DNA replication. Methods Mol. Biol. 2004, 269:169-186.
    • (2004) Methods Mol. Biol. , vol.269 , pp. 169-186
    • Traktman, P.1    Boyle, K.2
  • 220
    • 0021333525 scopus 로고
    • Transcriptional mapping of the DNA polymerase gene of vaccinia virus
    • Traktman P., Sridhar P., Condit R.C., Roberts B.E. Transcriptional mapping of the DNA polymerase gene of vaccinia virus. J. Virol. 1984, 49:125-131.
    • (1984) J. Virol. , vol.49 , pp. 125-131
    • Traktman, P.1    Sridhar, P.2    Condit, R.C.3    Roberts, B.E.4
  • 222
    • 0038128634 scopus 로고    scopus 로고
    • Poxvirus orthologous clusters: toward defining the minimum essential poxvirus genome
    • Upton C., Slack S., Hunter A.L., Ehlers A., Roper R.L. Poxvirus orthologous clusters: toward defining the minimum essential poxvirus genome. J. Virol. 2003, 77:7590-7600.
    • (2003) J. Virol. , vol.77 , pp. 7590-7600
    • Upton, C.1    Slack, S.2    Hunter, A.L.3    Ehlers, A.4    Roper, R.L.5
  • 224
    • 67049107832 scopus 로고    scopus 로고
    • Inhibition of vaccinia virus replication by two small interfering RNAs targeting B1R and G7L genes and their synergistic combination with cidofovir
    • Vigne S., Duraffour S., Andrei G., Snoeck R., Garin D., Crance J.M. Inhibition of vaccinia virus replication by two small interfering RNAs targeting B1R and G7L genes and their synergistic combination with cidofovir. Antimicrob. Agents Chemother. 2009, 53:2579-2588.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 2579-2588
    • Vigne, S.1    Duraffour, S.2    Andrei, G.3    Snoeck, R.4    Garin, D.5    Crance, J.M.6
  • 225
    • 0037379187 scopus 로고    scopus 로고
    • Mapping and functional analysis of interaction sites within the cytoplasmic domains of the vaccinia virus A33R and A36R envelope proteins
    • Ward B.M., Weisberg A.S., Moss B. Mapping and functional analysis of interaction sites within the cytoplasmic domains of the vaccinia virus A33R and A36R envelope proteins. J. Virol. 2003, 77:4113-4126.
    • (2003) J. Virol. , vol.77 , pp. 4113-4126
    • Ward, B.M.1    Weisberg, A.S.2    Moss, B.3
  • 227
    • 34248205172 scopus 로고    scopus 로고
    • Poxviral B1 kinase overcomes barrier to autointegration factor, a host defense against virus replication
    • Wiebe M.S., Traktman P. Poxviral B1 kinase overcomes barrier to autointegration factor, a host defense against virus replication. Cell Host Microbe 2007, 1:187-197.
    • (2007) Cell Host Microbe , vol.1 , pp. 187-197
    • Wiebe, M.S.1    Traktman, P.2
  • 228
    • 0027162408 scopus 로고
    • Deletion of the vaccinia virus B5R gene encoding a 42-kilodalton membrane glycoprotein inhibits extracellular virus envelope formation and dissemination
    • Wolffe E.J., Isaacs S.N., Moss B. Deletion of the vaccinia virus B5R gene encoding a 42-kilodalton membrane glycoprotein inhibits extracellular virus envelope formation and dissemination. J. Virol. 1993, 67:4732-4741.
    • (1993) J. Virol. , vol.67 , pp. 4732-4741
    • Wolffe, E.J.1    Isaacs, S.N.2    Moss, B.3
  • 229
    • 0013802325 scopus 로고
    • The inhibition of vaccinia virus multiplication by isatin-beta-thiosemicarbazone
    • Woodson B., Joklik W.K. The inhibition of vaccinia virus multiplication by isatin-beta-thiosemicarbazone. Proc. Natl. Acad. Sci. USA 1965, 54:946-953.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 946-953
    • Woodson, B.1    Joklik, W.K.2
  • 230
    • 0035798690 scopus 로고    scopus 로고
    • Vaccinia virus late transcription is activated in vitro by cellular heterogeneous nuclear ribonucleoproteins
    • Wright C.F., Oswald B.W., Dellis S. Vaccinia virus late transcription is activated in vitro by cellular heterogeneous nuclear ribonucleoproteins. J. Biol. Chem. 2001, 276:40680-40686.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40680-40686
    • Wright, C.F.1    Oswald, B.W.2    Dellis, S.3
  • 231
    • 2542452081 scopus 로고    scopus 로고
    • Benzo[c]phenanthrene adducts and nogalamycin inhibit DNA transesterification by vaccinia topoisomerase
    • Yakovleva L., Handy C.J., Sayer J.M., Pirrung M., Jerina D.M., Shuman S. Benzo[c]phenanthrene adducts and nogalamycin inhibit DNA transesterification by vaccinia topoisomerase. J. Biol. Chem. 2004, 279:23335-23342.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23335-23342
    • Yakovleva, L.1    Handy, C.J.2    Sayer, J.M.3    Pirrung, M.4    Jerina, D.M.5    Shuman, S.6
  • 232
    • 70450193225 scopus 로고    scopus 로고
    • Interaction of the vaccinia virus RNA polymerase-associated 94-kilodalton protein with the early transcription factor
    • Yang Z., Moss B. Interaction of the vaccinia virus RNA polymerase-associated 94-kilodalton protein with the early transcription factor. J. Virol. 2009, 83:12018-12026.
    • (2009) J. Virol. , vol.83 , pp. 12018-12026
    • Yang, Z.1    Moss, B.2
  • 234
    • 33747307897 scopus 로고    scopus 로고
    • Pox proteomics: mass spectrometry analysis and identification of Vaccinia virion proteins
    • Yoder J.D., Chen T.S., Gagnier C.R., Vemulapalli S., Maier C.S., Hruby D.E. Pox proteomics: mass spectrometry analysis and identification of Vaccinia virion proteins. Virol. J. 2006, 3:10.
    • (2006) Virol. J. , vol.3 , pp. 10
    • Yoder, J.D.1    Chen, T.S.2    Gagnier, C.R.3    Vemulapalli, S.4    Maier, C.S.5    Hruby, D.E.6
  • 235
    • 34547097537 scopus 로고    scopus 로고
    • Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition
    • Yoshizawa J.M., Li C., Gershon P.D. Saltatory forward movement of a poly(A) polymerase during poly(A) tail addition. J. Biol. Chem. 2007, 282:19144-19151.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19144-19151
    • Yoshizawa, J.M.1    Li, C.2    Gershon, P.D.3
  • 236
    • 0026506698 scopus 로고
    • Immature viral envelope formation is interrupted at the same stage by lac operator-mediated repression of the vaccinia virus D13L gene and by the drug rifampicin
    • Zhang Y., Moss B. Immature viral envelope formation is interrupted at the same stage by lac operator-mediated repression of the vaccinia virus D13L gene and by the drug rifampicin. Virology 1992, 187:643-653.
    • (1992) Virology , vol.187 , pp. 643-653
    • Zhang, Y.1    Moss, B.2
  • 237
    • 41649103338 scopus 로고    scopus 로고
    • Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase
    • Zheng S., Shuman S. Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase. RNA 2008, 14:696-705.
    • (2008) RNA , vol.14 , pp. 696-705
    • Zheng, S.1    Shuman, S.2


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