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http://purl.uniprot.org/citations/24143256http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24143256http://www.w3.org/2000/01/rdf-schema#comment"

Background

The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulators ubiquitin ligase MDM2.

Principal findings

In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress.

Conclusions

As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0077682"xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Chen L."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Cao J."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Lu X."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Luo J."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Lu Z."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Zhou X."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/author"Ling Y."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/name"PLoS One"xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/pages"e77682"xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/title"OTUD5 regulates p53 stability by deubiquitinating p53."xsd:string
http://purl.uniprot.org/citations/24143256http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/24143256http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24143256
http://purl.uniprot.org/citations/24143256http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24143256
http://purl.uniprot.org/uniprot/#_A0A0M4B4Y9-mappedCitation-24143256http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24143256
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http://purl.uniprot.org/uniprot/#_A0A087X1Q1-mappedCitation-24143256http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24143256
http://purl.uniprot.org/uniprot/#_A0A218MJE5-mappedCitation-24143256http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24143256
http://purl.uniprot.org/uniprot/#_A0A087WT22-mappedCitation-24143256http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24143256
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