Regulation and Function of the Original p53- Inducible p21 Gene (2010)
Book Chapter
Fraser, J. A. (2010). Regulation and Function of the Original p53- Inducible p21 Gene. In p53; Molecular Biology Intelligence Unit, 100-116. Springer Science + Business Media. https://doi.org/10.1007/978-1-4419-8231-5_7

P21 is a well known regulator of cell cycle progression through its inhibitory actions on Cyclin dependent kinases, (Cdk)/cyclin complexes, and DNA replication via its binding to proliferating cell nuclear antigen (PCNA). p21 also has a role in many... Read More about Regulation and Function of the Original p53- Inducible p21 Gene.

A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER269 IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION. (2010)
Journal Article
Fraser, J. A., Vojtesek, B., & Hupp, T. R. (2010). A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER269 IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION. Journal of Biological Chemistry, 285, 37762-37772. https://doi.org/10.1074/jbc.M110.143099

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 o... Read More about A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: I. PHOSPHORYLATION AT SER269 IN VIVO IS LINKED TO INACTIVATION OF p53 FUNCTION..

A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: II. A MODEL IN WHICH PHOSPHORYLATION AT SER269 INDUCES A MUTANT CONFORMATION TO p53. (2010)
Journal Article
Fraser, J. A., Madhumalar, A., Blackburn, E., Bramham, J., Walkinshaw, M. D., Verma, C., & Hupp, T. R. (2010). A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: II. A MODEL IN WHICH PHOSPHORYLATION AT SER269 INDUCES A MUTANT CONFORMATION TO p53. Journal of Biological Chemistry, 285, 37773-37786. https://doi.org/10.1074/jbc.M110.143107

The p53 DNA-binding domain harbors a conformationally flexible multiprotein binding site that regulates p53 ubiquitination. A novel phosphorylation site exists within this region at Ser269, whose phosphomimetic mutation inactivates p53. The phosphomi... Read More about A Novel p53 Phosphorylation Site within the MDM2 Ubiquitination Signal: II. A MODEL IN WHICH PHOSPHORYLATION AT SER269 INDUCES A MUTANT CONFORMATION TO p53..