HAUSP/USP7 as an Epstein–Barr virus target
MN Holowaty, L Frappier - Biochemical Society Transactions, 2004 - portlandpress.com
Biochemical Society Transactions, 2004•portlandpress.com
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.
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.
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.
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