4.4 Article Proceedings Paper

HAUSP/USP7 as an Epstein-Barr virus target

期刊

BIOCHEMICAL SOCIETY TRANSACTIONS
卷 32, 期 -, 页码 731-732

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BST0320731

关键词

affinity chromatography; DNA replication; EBNA1; immortalization; p53; tandem affinity purification (TAP) tagging

向作者/读者索取更多资源

USP7 (also called HAUSP) is a de-ubiquitinating enzyme recently identified as a key regulator of the p53-mdm2 pathway, which stabilizes both p53 and mdm2. We have discovered that the Epstein-Barr nuclear antigen 1 protein of Epstein-Barr virus binds with high affinity to USP7 and disrupts the USP7-p53 interaction. The results have important implications for the role of Epstein-Barr nuclear antigen 1 in the cellular immortalization that is typical of an Epstein-Barr virus latent infection.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.4
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据