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Temperature-Sensitive Mutations in the Putative Herpes Simplex Virus Type 1 Terminase Subunits pU(L)15 and pU(L)33 Preclude Viral DNA Cleavage/Packaging and Interaction with pU(L)28 at the Nonpermissive Temperature
Terminases comprise essential components of molecular motors required to package viral DNA into capsids in a variety of DNA virus systems. Previous studies indicated that the herpes simplex virus type 1 U(L)15 protein (pU(L)15) interacts with the pU(L)28 moiety of a pU(L)28-pU(L)33 complex to form t...
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| Autors principals: | , , , |
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| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
American Society for Microbiology (ASM)
2008
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2224384/ https://ncbi.nlm.nih.gov/pubmed/17913813 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.01875-07 |
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