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Cited by 459

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300

Grossman, Steven R., Deato, Maria E., Brignone, Chrystelle, Chan, Ho Man, Kung, Andrew L., Tagami, Hideaki, Nakatani, Yoshihiro, Livingston, David M.·2003·Science

Abstract

Rapid turnover of the tumor suppressor protein p53 requires the MDM2 ubiquitin ligase, and both interact with p300–CREB-binding protein transcriptional coactivator proteins. p53 is stabilized by the binding of p300 to the oncoprotein E1A, suggesting that p300 regulates p53 degradation. Purified p300 exhibited intrinsic ubiquitin ligase activity that was inhibited by E1A. In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 catalyzed p53 monoubiquitination. E1A expression caused a decrease in polyubiquitinated but not monoubiquitinated p53 in cells. Thus, generation of the polyubiquitinated forms of p53 that are targeted for proteasome degradation requires the intrinsic ubiquitin ligase activities of MDM2 and p300.

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Metadata

Authors
Grossman, S. R., Deato, M. E., Brignone, C., Chan, H. M., Kung, A. L., Tagami, H., Nakatani, Y., & Livingston, D. M.
Venue
Science
Published
2003-04-11
Volume
300
Issue
5617
Pages
342-344
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2094494461
Cited by
459
References
4
FWCI
18.12
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300. https://app.cochat.ai/papers/10.1126/science.1080386
The paper
Grossman, S. R., Deato, M. E., Brignone, C., Chan, H. M., Kung, A. L., Tagami, H., Nakatani, Y., & Livingston, D. M. (2003). Polyubiquitination of p53 by a Ubiquitin Ligase Activity of p300. Science. https://doi.org/10.1126/science.1080386

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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