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Article

Phosphorylation of Pirh2 by Calmodulin‐dependent kinase II impairs its ability to ubiquitinate p53

14 Jun 2007

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 17568776
DOI: 10.1038/sj.emboj.7601749

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Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation of Pirh2 by Calmodulin‐dependent kinase II impairs its ability to ubiquitinate p53PMID 17568776Read ↗

Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation.Semantic proximity Read ↗

Pirh2Semantic proximity Read ↗

The Role of E3 Ligase Pirh2 in DiseaseSemantic proximity Read ↗

Differential response between the p53 ubiquitin–protein ligases Pirh2 and MdM2 following DNA damage in human cancer cellsSemantic proximity Read ↗

Pirh2 RING‐finger E3 ubiquitin ligase: Its role in tumorigenesis and cancer therapySemantic proximity Read ↗

Role of Pirh2 in Mediating the Regulation of p53 and c-MycSemantic proximity Read ↗

E3 ubiquitin ligase Pirh2 enhances tumorigenic properties of human non-small cell lung carcinoma cellsSemantic proximity Read ↗

Control of Human PIRH2 Protein StabilitySemantic proximity Read ↗

Enhanced Mdm2 activity inhibits pRB function via ubiquitin‐dependent degradationSemantic proximity Read ↗

Expression of Pirh2, a Newly Identified Ubiquitin Protein Ligase, in Lung CancerSemantic proximity Read ↗

Tumor Suppressor HIC1 Directly Regulates SIRT1 to Modulate p53-Dependent DNA-Damage ResponsesSemantic proximity Read ↗

High expression of Pirh2, an E3 ligase for p27, is associated with low expression of p27 and poor prognosis in head and neck cancersSemantic proximity Read ↗

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