The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.

The herpes simplex virus type 1 (HSV-1) UL8 DNA replication protein is a component of a trimeric helicase-primase complex. Sixteen UL8-specific monoclonal antibodies (MAbs) were isolated and characterized. In initial immunoprecipitation experiments, one of these, MAb 804, was shown to coprecipitate...

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書誌詳細
出版年:	J Virol
主要な著者:	Marsden, H S, McLean, G W, Barnard, E C, Francis, G J, MacEachran, K, Murphy, M, McVey, G, Cross, A, Abbotts, A P, Stow, N D
フォーマット:	Artigo
言語:	Inglês
出版事項:	American Society for Microbiology (ASM) 1997
主題:	Research Article
オンライン･アクセス:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC191912/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9261356/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.71.9.6390-6397.1997
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The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.

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