Identification of a dimerization domain in the C-terminal segment of the IE110 transactivator protein from herpes simplex virus.
The 775-amino-acid IE110 (or ICP0) phosphoprotein of herpes simplex virus (HSV) functions as an accessory transcription factor during the lytic cycle and plays a critical role in reactivation from latent infection. By immunofluorescence analysis, IE110 localizes in a novel pattern consisting of seve...
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| Pubblicato in: | J Virol |
|---|---|
| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
American Society for Microbiology (ASM)
1994
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC236817/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8151788/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.68.5.3267-3282.1994 |
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