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- W4238771447 abstract "(Molecular Cell 18, 565–576; May 27, 2005) In our recent article, the labeling of Figure 6B was misprinted. The correct Figure 6 is printed here. Loss of HAUSP-Mediated Deubiquitination Contributes to DNA Damage-Induced Destabilization of Hdmx and Hdm2Meulmeester et al.Molecular CellMay 27, 2005In BriefThe p53 tumor suppressor protein has a major role in protecting the integrity of the genome. In unstressed cells, p53 is maintained at low levels by the ubiquitin-proteasome pathway. A balance between ubiquitin ligase activity (Hdm2, COP1, and Pirh2) and the ubiquitin protease activity of the Herpes virus-associated ubiquitin-specific protease (HAUSP) determines the half-life of p53. HAUSP also modulates p53 stability indirectly by deubiquitination and stabilization of Hdm2. The Hdmx protein affects p53 stability as well through its interaction with and regulation of Hdm2. Full-Text PDF Open Archive" @default.
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- W4238771447 date "2005-07-01" @default.
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- W4238771447 title "Loss of HAUSP-Mediated Deubiquitination Contributes to DNA Damage-Induced Destabilization of Hdmx and Hdm2" @default.
- W4238771447 doi "https://doi.org/10.1016/j.molcel.2005.06.002" @default.
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