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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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| Hlavní autoři: | , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
American Society for Biochemistry and Molecular Biology
2010
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| Témata: | |
| On-line přístup: | 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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