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Gene Review

J2R  -  temporal expression: early

Vaccinia virus

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Disease relevance of J2R

  • The thymidine kinase (ATP:thymidine 5'-phosphotransferase, EC gene of vaccinia virus has previously been mapped near the middle of the viral DNA, within the 4.85-kilobase HindIII J fragment, and shown to encode a Mr 19,000 polypeptide [Hruby, D. E. & Ball, L. A. (1982) J. Virol. 43, 403-409] [1].
  • Because hybridization of vaccinia virus DNA to partially purified thymidine kinase mRNA detected only a single 670-nucleotide RNA species capable of hybridizing to this region of the genome, nuclease S1 mapping experiments were carried out with thymidine kinase mRNA to protect DNA fragments that were terminally labeled at this EcoRI site [1].
  • Nevertheless a fowlpox virus gene corresponding to the vaccinia virus thymidine kinase gene was apparently lacking within the region studied and is probably located elsewhere in the genome [2].
  • As to HSV-1, most of the selected compounds were markedly less effective against the TK(-) strains, suggesting that this enzyme was required for the activation of these nucleoside analogs [3].
  • Additional screening against orthopoxviruses will be required to identify nucleoside analogs that are efficiently activated by their type II TK [3].

High impact information on J2R


Chemical compound and disease context of J2R


Biological context of J2R


Anatomical context of J2R


Associations of J2R with chemical compounds

  • This differs from the results for CV where only idoxuridine and bromodeoxyuridine appeared to be activated, putatively by the type II TK expressed by this virus [3].

Analytical, diagnostic and therapeutic context of J2R


  1. Fine structure analysis and nucleotide sequence of the vaccinia virus thymidine kinase gene. Hruby, D.E., Maki, R.A., Miller, D.B., Ball, L.A. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  2. Similar genetic organization between a region of fowlpox virus DNA and the vaccinia virus HindIII J fragment despite divergent location of the thymidine kinase gene. Drillien, R., Spehner, D., Villeval, D., Lecocq, J.P. Virology (1987) [Pubmed]
  3. Distinct thymidine kinases encoded by cowpox virus and herpes simplex virus contribute significantly to the differential antiviral activity of nucleoside analogs. Prichard, M.N., Williams, A.D., Keith, K.A., Harden, E.A., Kern, E.R. Antiviral Res. (2006) [Pubmed]
  4. Prevention of vaccinia virus infection in immunodeficient mice by vector-directed IL-2 expression. Flexner, C., Hügin, A., Moss, B. Nature (1987) [Pubmed]
  5. Epitopes derived by incidental translational frameshifting give rise to a protective CTL response. Zook, M.B., Howard, M.T., Sinnathamby, G., Atkins, J.F., Eisenlohr, L.C. J. Immunol. (2006) [Pubmed]
  6. A single amino acid substitution abolishes feedback inhibition of vaccinia virus thymidine kinase. Black, M.E., Hruby, D.E. J. Biol. Chem. (1992) [Pubmed]
  7. The nucleotide sequence of the chicken thymidine kinase gene and the relationship of its predicted polypeptide to that of the vaccinia virus thymidine kinase. Kwoh, T.J., Engler, J.A. Nucleic Acids Res. (1984) [Pubmed]
  8. Dominant negative selection of vaccinia virus using a thymidine kinase/thymidylate kinase fusion gene and the prodrug azidothymidine. Holzer, G.W., Mayrhofer, J., Gritschenberger, W., Falkner, F.G. Virology (2005) [Pubmed]
  9. Inhibition of vaccinia virus thymidine kinase by the distal products of its own metabolic pathway. Hruby, D.E. Virus Res. (1985) [Pubmed]
  10. Nucleotide sequence of the vaccinia virus thymidine kinase gene and the nature of spontaneous frameshift mutations. Weir, J.P., Moss, B. J. Virol. (1983) [Pubmed]
  11. Dominant host range selection of vaccinia recombinants by rescue of an essential gene. Holzer, G.W., Gritschenberger, W., Mayrhofer, J.A., Wieser, V., Dorner, F., Falkner, F.G. Virology (1998) [Pubmed]
  12. Synthesis of vaccinia virus thymidine kinase in microinjected Xenopus oocytes. Hruby, D.E., Miller, D.B., Ball, L.A. Virology (1982) [Pubmed]
  13. Site-directed mutagenesis of a conserved domain in vaccinia virus thymidine kinase. Evidence for a potential role in magnesium binding. Black, M.E., Hruby, D.E. J. Biol. Chem. (1992) [Pubmed]
  14. Introduction of foreign DNA into the vaccinia virus genome by in vitro ligation: recombination-independent selectable cloning vectors. Merchlinsky, M., Moss, B. Virology (1992) [Pubmed]
  15. Quaternary structure of vaccinia virus thymidine kinase. Black, M.E., Hruby, D.E. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  16. Expression and single-step purification of enzymatically active vaccinia virus thymidine kinase containing an engineered oligohistidine domain by immobilized metal affinity chromatography. Franke, C.A., Hruby, D.E. Protein Expr. Purif. (1993) [Pubmed]
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