Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization

By Muyang Li, Delin Chen, A. Shiloh, Jianyuan Luo, A. Nikolaev, J. Qin, W. Gu. Nature, 2002

1,067 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/f86b1201c0bdda42fc99fc4e0938f74466b35e3a

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Citations in the corpus

Ubiquitination, phosphorylation and acetylation: the molecular basis for p53 regulation. (2003, background): “The importance of deubiquitination in the p53 pathway was recently shown by the discovery of a herpesvirusassociated ubiquitin-specific protease, or HAUSP [25 ].”
HIF-1 as a target for drug development (2003, background): “The precedence for such a paradigm has recently been reported for the p53 tumour-suppressor gene through the identification of HAUSP, a herpes virus ubiquitin-specific proteas”
p53 ubiquitination: Mdm2 and beyond. (2006, background): “The finding that the herpesvirus-associated ubiquitin-specific protease (HAUSP) could bind to and stabilize p53 added yet another layer of regulation to the p53 ubiquitination pathway and was one of the first indications that DUBs exhibited substrate specificity (Hu et al., 2002; Li et al., 2002a).”
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO (2004, methodology): “Binding and elution of proteins as well as immunoprecipitation with Bcl10 antibody were performed as previously describe”
The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway. (2005, background): “…DUB substrates shRNA vectors efficiently suppressed GFP-USP1 ex-have been identified (Brummelkamp et al., 2003; Cumpression (Figure 2C).mings et al., 2004; Graner et al., 2004; Kovalenko et al., To study endogenous USP1 protein, a polyclonal anti-2003; Li et al., 2002; Trompouki et al., 2003).”
USP10 Regulates p53 Localization and Stability by Deubiquitinating p53 (2010, methodology): “The ubiquitin-specific protease HAUSP has been shown to deubiquitinate p53, with overexpression of HAUSP resulting in p53 stabilization (Li et al., 2002).”
The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “HAUSP, which is localized in the nucleus, can prevent the degradation of p53 by deubiquitinating even under the circumstance of highly expressed Mdm2.”
Mechanism and function of deubiquitinating enzymes. (2004, background): “[74] identified HAUSP (see earlier) as a novel p53-interacting protein.”
Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. (2004, background): “H1299 cells (genetically negative for p53) were trans- et al., 1997; Li et al., 2002).”
The emerging roles of forkhead box (Fox) proteins in cancer (2007, background): “, and HAUSP may function as a tumour suppressor by promoting p53 stabilit”