Regulation of p53 function and stability by phosphorylation.

@article{Ashcroft1999RegulationOP,
  title={Regulation of p53 function and stability by phosphorylation.},
  author={Margaret Ashcroft and Michael H. G. Kubbutat and Karen H Vousden},
  journal={Molecular and cellular biology},
  year={1999},
  volume={19 3},
  pages={
          1751-8
        }
}
The p53 tumor suppressor protein can be phosphorylated at several sites within the N- and C-terminal domains, and several protein kinases have been shown to phosphorylate p53 in vitro. In this study, we examined the activity of p53 proteins with combined mutations at all of the reported N-terminal phosphorylation sites (p53N-term), all of the C-terminal phosphorylation sites (p53C-term), or all of the phosphorylation sites together (p53N/C-term). Each of these mutant proteins retained… CONTINUE READING
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