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A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER(269) IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION

p53 is a thermodynamically unstable protein containing a conformationally flexible multiprotein docking site within the DNA-binding domain. A combinatorial peptide chip used to identify the novel kinase consensus site RXSΦ(K/D) led to the discovery of a homologous phosphorylation site in the S10 β-s...

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書目詳細資料
Main Authors: Fraser, Jennifer A., Vojtesek, Borivoj, Hupp, Ted R.
格式: Artigo
語言:Inglês
出版: American Society for Biochemistry and Molecular Biology 2010
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC2988381/
https://ncbi.nlm.nih.gov/pubmed/20851891
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.143099
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