An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo

@article{Midgley2000AnNP,
  title={An N-terminal p14ARF peptide blocks Mdm2-dependent ubiquitination in vitro and can activate p53 in vivo},
  author={Carol A Midgley and Joana M. P. Desterro and Mark K. Saville and Stephanie F. Howard and Alison Sparks and Ronald Thomas Hay and D. P. Lane},
  journal={Oncogene},
  year={2000},
  volume={19},
  pages={2312-2323}
}
The p53 tumour suppressor protein is down-regulated by the action of Mdm2, which targets p53 for rapid degradation by the ubiquitin-proteasome pathway. The p14ARF protein is also a potent tumour suppressor that acts by binding to Mdm2 and blocking Mdm2-dependent p53 degradation and transcriptional silencing. We have screened a series of overlapping synthetic peptides derived from the p14ARF protein sequence and found that a peptide corresponding to the first 20 amino acids of ARF (Peptide 3… CONTINUE READING
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