ArticleThe Biochemical journal1995
Human papillomavirus type 6 E7 protein is a substrate in vitro of protein kinase C.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Article
- The papillomavirus E7 proteins.Virology · 2013Review
- Phosphorylation events during viral infections provide potential therapeutic targets.Reviews in medical virology · 2012Article
- Cellular transformation by human papillomaviruses: lessons learned by comparing high- and low-risk viruses.Virology · 2012Review
- Nonconserved lysine residues attenuate the biological function of the low-risk human papillomavirus E7 protein.Journal of virology · 2011Article
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Authors and funding
2 authors.
Funding
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Abstract
The E7 proteins of 'low-risk' and 'high-risk' human papillomaviruses (HPV) are phosphorylated by casein kinase II. In this study, we report that the 'low-risk' HPV 6 E7 protein, but not the 'high-risk' HPV 16 E7 protein, can be phosphorylated in vitro on threonine at amino acid position 7 by protein kinase C. This is the first example of a qualitative biochemical difference between the HPV 6 E7 and HPV 16 E7 proteins.
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