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Induction of Both Thymidine and Deoxycytidine Kinase Activity by Herpes Viruses
Abstract
SUMMARY Genetical and biochemical evidence indicates that herpes simplex virus (types 1 and 2) specifies a unique kinase activity which is able to phosphorylate both thymidine and deoxycytidine. Pseudorabies virus specifies an enzyme which has only thymidine kinase activity and so does vaccinia virus, while equine abortion virus does not induce either activity. It is shown that the HSV specified deoxypyrimidine kinase is indispensable for virus growth in serum starved cells but not important for virus replication in actively growing culture cells.
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Cited by
Experimental Therapy of Human Glioma by Means of a Genetically Engineered Virus Mutant
Martuza, R. L., Malick, A., Markert, J. M., Ruffner, K. L., & Coen, D. M. (1991) · Science · doi:10.1126/science.1851332 · Cited by 1,050
Buller, R. M. L., & Palumbo, G. J. (1991) · Microbiological Reviews · doi:10.1128/mmbr.55.1.80-122.1991 · Cited by 452
Identification and Cloning of the Fowlpox Virus Thymidine Kinase Gene Using Vaccinia Virus
Boyle, D. B., & Coupar, B. E. H. (1986) · Journal of General Virology · doi:10.1099/0022-1317-67-8-1591 · Cited by 51
Metadata
- Authors
- Jamieson, A. T., Gentry, G. A., & Subak-Sharpe, J. H.
- Venue
- Journal of General Virology
- Publisher
- Microbiology Society
- Published
- 1974-09-01
- Volume
- 24
- Issue
- 3
- Pages
- 465-480
- ISSN
- 0022-1317 (ISSN-L)
- 1465-2099
- OpenAlex
- W2114240169
- Cited by
- 288
- References
- 0
- FWCI
- 17.44
- Type
- journal article
- Language
- en
- Open access
- closed
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- Jamieson, A. T., Gentry, G. A., & Subak-Sharpe, J. H. (1974). Induction of Both Thymidine and Deoxycytidine Kinase Activity by Herpes Viruses. Journal of General Virology. https://doi.org/10.1099/0022-1317-24-3-465
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
