Ribonucleotide Reductase Induced by Herpes Simplex Virus has a Virus-specified Constituent

References

1. Anderson K. P., Frink R. J., Devi G. B., Gaylord B. H., Costa R. H., Wagner E. K. 1981; Detailed characterisation of the mRNA mapping in the Hind III fragment K region of the herpes simplex virus type 1 genome. Journal of Virology 37:1011–1027
   [Google Scholar]
2. Brown S. M., Ritchie D. A., Subak-Sharpe J. H. 1973; Genetic studies with herpes simplex type 1. The isolation of temperature sensitive mutants, their arrangement into complementation groups and recombination analysis leading to a linkage map. Journal of General Virology 18:329–346
   [Google Scholar]
3. Cohen G. H. 1972; Ribonucleotide reductase activity of synchronised KB cells infected with herpes simplex virus. Journal of Virology 9:408–418
   [Google Scholar]
4. Crombie I. K. 1975 Genetic and biochemical studies with herpes simplex virus type 1 Ph.D. thesis University of Glasgow;
   [Google Scholar]
5. Dubbs D. R., Kit S. 1964; Mutant strains of herpes simplex deficient in thymidine kinase-inducing activity. Virology 22:493–502
   [Google Scholar]
6. Elford H. L. 1968; Effect of hydroxyurea on ribonucleotide reductase. Biochemical and Biophysical Research Communications 33:129–135
   [Google Scholar]
7. Eriksson S., Martin D. W. 1981; Ribonucleotide reductase in cultured mouse lymphoma cells. Cell cycle-dependent variation in the activity of subunit protein M2. Journal of Biological Chemistry 256:9436–9440
   [Google Scholar]
8. Francke B., Moss H., Timbury M. C., Hay J. 1978; Alkaline DNAase activity in cells infected with a temperature sensitive mutant of herpes simplex virus type 2. Journal of Virology 26:209–213
   [Google Scholar]
9. Hay J., Subak-Sharpe J. H. 1976; Mutants of herpes simplex virus that are resistant to phosphonoacetic acid induce altered DNA polymerase activities in infected cells. Journal of General Virology 31:145–148
   [Google Scholar]
10. Hay J., Moss H., Jamieson A. T., Timbury M. C. 1976; Herpesvirus proteins: DNA polymerase and pyrimidine deoxynucleoside kinase activities in temperature sensitive mutants of herpes simplex virus type 2. Journal of General Virology 31:65–73
    [Google Scholar]
11. Huszar D., Bacchetti S. 1981; Partial purification and characterization of the ribonucleotide reductase induced by herpes simplex virus infection of mammalian cells. Journal of Virology 37:580–588
    [Google Scholar]
12. Jamieson A. T., Bjursell G. 1976a; Deoxyribonucleoside triphosphate pools in herpes simplex type 1 infected cells. Journal of General Virology 31:101–113
    [Google Scholar]
13. Jamieson A. T., Bjursell G. 1976b; Deoxyribonucleoside triphosphate pools in cells infected with deoxypyrimidine kinaseless herpes simplex virus. Journal of General Virology 31:115–123
    [Google Scholar]
14. Jamieson A. T., Gentry G. A., Subak-Sharpe J. H. 1974; Induction of both thymidine and deoxycytidine kinase activity by herpes simplex viruses. Journal of General Virology 24:465–480
    [Google Scholar]
15. Keir H. M., Gold E. 1963; Deoxyribonucleic acid nucleotidyl transferase and deoxyribonuclease from cultured cells infected with herpes simplex virus. Biochimica et biophysica acta 72:263–276
    [Google Scholar]
16. Keir H. M., Subak-Sharpe J. H., Shedden W. J. H., Watson D. H., Wildy P. 1966; Immunological evidence for a specific DNA polymerase produced after infection by herpes simplex virus. Virology 30:154–157
    [Google Scholar]
17. Kit S., Dubbs D. R. 1963; Acquisition of thymidine kinase activity by herpes simplex infected mouse fibroblast cells. Biochemical and Biophysical Research Communications 11:55–59
    [Google Scholar]
18. Langelier Y., Buttin G. 1981; Characterization of ribonucleotide reductase induction in BHK-21/C13 Syrian hamster cell line upon infection by herpes simplex virus (HSV). Journal of General Virology 57:21–31
    [Google Scholar]
19. Langelier Y., Dechamps M., Buttin G. 1978; An analysis of dCMP deaminase and CDP reductase levels in hamster cells infected by herpes simplex virus. Journal of Virology 26:547–553
    [Google Scholar]
20. Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. 1951; Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193:265–275
    [Google Scholar]
21. Macdonald D. 1980 Herpes simplex virus-induced early proteins Ph D. thesis University of Glasgow;
    [Google Scholar]
22. Mclauchlan J., Clements J. B. 1982; A 3′ co-terminus of two early herpes simplex virus type 1 mRNAs. Nucleic Acids Research 10:501–512
    [Google Scholar]
23. Macpherson I., Stoker M. 1962; Polyoma transformation of hamster cell clones – an investigation of genetic factors affecting cell competence. Virology 16:147–151
    [Google Scholar]
24. Marsden H. S., Crombie I. K., Subak-Sharpe J. H. 1976; Control of protein synthesis in herpesvirus infected cells: analysis of the polypeptides induced by wild-type and sixteen temperature-sensitive mutants of HSV strain 17. Journal of General Virology 31:347–372
    [Google Scholar]
25. Ponce De Leon M., Eisenberg R. J., Cohen G. H. 1977; Ribonucleotide reductase from herpes simplex virus (types 1 and 2) infected and uninfected KB cells: properties of the partially purified enzymes. Journal of General Virology 36:163–173
    [Google Scholar]
26. Preston C. M. 1979; Control of herpes simplex virus type 1 mRNA synthesis in cells infected with wild type virus or the temperature sensitive mutant ts K. Journal of Virology 29:275–284
    [Google Scholar]
27. Reichard P. 1958; Chromatographic separations of cytosine containing compounds. Acta chemica scandinavica 12:2048
    [Google Scholar]
28. Thelander L., Reichard P. 1979; Reduction of ribonucleotides. Annual Review of Biochemistry 48:133–158
    [Google Scholar]
29. Thelander L., Eriksson S., Akerman M. 1980; Ribonucleotide reductase from calf thymus. Separation of the enzyme into two non-identical subunits, proteins M1 and M2. Journal of Biological Chemistry 255:7426–7432
    [Google Scholar]
30. Watson R. J., Clements J. B. 1978; Characterisation of transcription deficient temperature sensitive mutants of herpes simplex virus type 1. Virology 91:364–379
    [Google Scholar]