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Article

The E3 ubiquitin protein ligase HERC2 modulates the activity of tumor protein p53 by regulating its oligomerization.

The Journal of biological chemistry - 23 May 2014

Cubillos-Rojas Monica, Amair-Pinedo Fabiola, Peiró-Jordán Roser, Bartrons Ramon, Ventura Francesc, Rosa Jose Luis

Abstract excerpt

The tumor suppressor p53 is a transcription factor that coordinates the cellular response to several kinds of stress. p53 inactivation is an important step in tumor progression. Oligomerization of p53 is critical for its posttranslational modification and its ability to regulate the transcription...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 24722987
DOI: 10.1074/jbc.M113.527978
PMCID: PMC4031533

Genes

HERC2
MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24722987-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

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The E3 ubiquitin protein ligase HERC2 modulates the activity of tumor protein p53 by regulating its oligomerization.PMID 24722987Read ↗

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MDM2-C Functions as an E3 Ubiquitin LigaseSemantic proximity Read ↗

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Functional analysis and consequences of Mdm2 E3 ligase inhibition in human tumor cells.Semantic proximity Read ↗

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