The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Inactivation of HAUSP in vivo modulates p53 function.
Open accessAbstract
Hausp is a deubiquitinase that has been shown to regulate the p53-Mdm2 pathway. Cotransfection of p53 and Hausp stabilizes p53 through the removal of ubiquitin moieties from polyubiquitinated p53. Interestingly, knockout or RNA interference-mediated knockdown of Hausp in human cells also resulted in the stabilization of p53 due to the destabilization of Mdm2, suggesting a dynamic role of Hausp in p53 activation. To understand the physiological functions of Hausp, we generated hausp knockout mice. Hausp knockout mice die during early embryonic development between embryonic days E6.5 and E7.5. The hausp knockout embryos showed p53 activation, but no apparent increase in apoptosis. Embryonic lethality was caused by a dramatic reduction in proliferation and termination in development, in part due to p53 activation and/or abrogation of p53-independent functions. Although deletion of p53 did not completely rescue the embryonic lethality of the hausp knockout, embryonic development was extended in both hausp and p53 double knockout embryos. These data show that Hausp has a critical role in regulating the p53-Mdm2 pathway.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“USP7 is an essential enzyme; its homozygous knockout in mice results is early embryonic lethality (Kon et al., 2010)”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Kon et al., 2010
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
Li, E., Bestor, T. H., & Jaenisch, R. (1992) · Cell · doi:10.1016/0092-8674(92)90611-f · Cited by 3,984
A genomic and functional inventory of deubiquitinating enzymes.
Nijman, S. M. B., Luna-Vargas, M. P. A., Velds, A., Brummelkamp, T. R., Dirac, A. M. G., Sixma, T. K., & Bernards, R. (2005) · Cell · doi:10.1016/j.cell.2005.11.007 · Cited by 1,854
Defining the Human Deubiquitinating Enzyme Interaction Landscape
Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523
Ubiquitin: structures, functions, mechanisms
Pickart, C. M., & Eddins, M. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.09.019 · Cited by 1,491
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
de Oca Luna, R. M., Wagner, D. S., & Lozano, G. (1995) · Nature · doi:10.1038/378203a0 · Cited by 1,420 · cited 1×
“However, combining a p53-null background with the mdm2 knockout rescues this phenotype, suggesting that Mdm2 is a major negative regulator of p53 (Jones et al., 1995; Montes de Oca Luna et al., 1995).”
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
Jones, S. N., Roe, A. E., Donehower, L. A., & Bradley, A. (1995) · Nature · doi:10.1038/378206a0 · Cited by 1,280 · cited 1×
“However, combining a p53-null background with the mdm2 knockout rescues this phenotype, suggesting that Mdm2 is a major negative regulator of p53 (Jones et al., 1995; Montes de Oca Luna et al., 1995).”
Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
Li, M., Chen, D., Shiloh, A., Luo, J., Nikolaev, A. Y., Qin, J., & Gu, W. J. (2002) · Nature · doi:10.1038/nature737 · Cited by 1,048
Chen, X., Ko, L. J., Jayaraman, L., & Prives, C. (1996) · Genes & Development · doi:10.1101/gad.10.19.2438 · Cited by 735
Pirh2, a p53-Induced Ubiquitin-Protein Ligase, Promotes p53 Degradation
Leng, R. P., Lin, Y., Ma, W., Wu, H., Lemmers, B., Chung, S., Parant, J. M., Lozano, G., Hakem, R., & Benchimol, S. (2003) · Cell · doi:10.1016/s0092-8674(03)00193-4 · Cited by 731
Cited by
Sorted by citations
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398
Self-citationChauhan, D., Tian, Z., Nicholson, B., Kumar, K. G. S., Zhou, B., Carrasco, R., McDermott, J. L., Leach, C. A., Fulcinniti, M., Kodrasov, M. P., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.08.007 · Cited by 589
p53 post-translational modification: deregulated in tumorigenesis
Dai, C., & Gu, W. J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.09.002 · Cited by 547
Deubiquitinases in cancer: new functions and therapeutic options
Fraile, J. M., Quesada, V., Rodríguez, D., Freije, J. M. P., & López-Otín, C. (2011) · Oncogene · doi:10.1038/onc.2011.443 · Cited by 463
Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death
Vucic, D., Dixit, V. M., & Wertz, I. E. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3143 · Cited by 468
Metadata
- Authors
- Kon, N., Kobayashi, Y., Li, M., Brooks, C. L., Ludwig, T., & Gu, W.
- Affiliations
- Columbia University (US)
- Venue
- Oncogene
- Published
- 2009-11-30
- Volume
- 29
- Issue
- 9
- Pages
- 1270-1279
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC2857765
- OpenAlex
- W2037667982
- Cited by
- 176
- References
- 31
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 8 · 2023: 7 · 2022: 10 · 2021: 12 · 2020: 28 · 2019: 14 · 2018: 15 · 2017: 15 · 2016: 10 · 2015: 10 · 2014: 8 · 2013: 10 · 2012: 8
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Oncogene (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (P01CA097403, R01CA129627)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
- Keywords
- USP7, p53, MDM2, deubiquitinase, p53 stabilization, MDM2-p53 pathway, embryonic lethality, cell proliferation, knockout mice, p53-independent function, apoptosis
- MeSH terms
- Ubiquitin-Specific Peptidase 7, Animals, Female, HeLa Cells, Humans, Substrate Specificity, Genes, p53, Tumor Suppressor Protein p53, Apoptosis, Mice, Knockout, Tumor Suppressor Proteins, Ubiquitin, RNA Interference, RNA, Small Interfering, Ubiquitin Thiolesterase, Ubiquitin-Protein Ligases, Cell Line, Tumor, Mice, Proto-Oncogene Proteins c-mdm2
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
