p53 de-ubiquitination: At the edge between life and death Journal Article


Authors: Salomoni, P.; Pandolfi, P. P.
Article Title: p53 de-ubiquitination: At the edge between life and death
Abstract: The tumour suppressor protein p53 is stabilized by the de-ubiquitination enzyme herpes-virus-associated ubiquitin-specific protease (HAUSP), which localizes to the promyelocytic leukaemia nuclear body (PML-NB). The pro-apoptotic activity of p53 is also induced by HAUSP. Therefore, p53 ubiquitination is a dynamic process, and HAUSP might function as a tumour suppressor by enhancing p53 stabilization.
Keywords: controlled study; unclassified drug; note; ubiquitin; protein function; animals; cell survival; apoptosis; protein stability; protein p53; tumor suppressor gene; promyelocytic leukemia; herpes virus; herpesviridae; tumor suppressor protein p53; proteinase; mammals; enzyme localization; cell nucleus inclusion body; priority journal; protein hausp
Journal Title: Nature Cell Biology
Volume: 4
Issue: 6
ISSN: 1465-7392
Publisher: Nature Publishing Group  
Date Published: 2002-06-01
Start Page: E152
End Page: E153
Language: English
DOI: 10.1038/ncb0602-e152
PUBMED: 12042830
PROVIDER: scopus
DOI/URL:
Notes: Export Date: 14 November 2014 -- Source: Scopus
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