A glutamine residue in the membrane-associating domain of the bovine papillomavirus type 1 E5 oncoprotein mediates its binding to a transmembrane component of the vacuolar H(+)-ATPase.
The 44-amino-acid E5 oncoprotein is the major transforming protein of bovine papillomavirus type 1. It is a highly hydrophobic polypeptide which dimerizes and localizes to the Golgi apparatus and endoplasmic reticulum membranes. Recent evidence suggests that E5 modulates the phosphorylation and inte...
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| 出版年: | J Virol |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American Society for Microbiology (ASM)
1992
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC238300/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1370089/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jvi.66.1.405-413.1992 |
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