Tetramer Stability and Functional Regulation of Tumor Suppressor Protein p53

This book presents the first report of the comprehensive and quantitative analysis of the effects of tumor-derived mutations on the tetrameric structure of tumor suppressor protein p53, which plays a central role in maintaining genomic integrity.

Nominated by Hokkaido University as an outstanding thesis in chemistry First report that comprehensively and quantitatively analyzes the effects of tumor-derived mutations on tetrameric structure of tumor suppressor p53 Reports the development of a new stabilizer and inhibitor of p53, which could enhance or decrease p53 transcriptional activity via regulation of tetramer formation of p53 Includes supplementary material: sn.pub/extras

Autorentext

Dr. Rui Kamada
Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University

Inhalt
Quantitative analysis for p53 tetramerization domain mutants reveals a low threshold for tumor suppressor inactivation.- Stabilization of mutant tetrameric structures by calixarene derivatives.- Inhibition of the transcriptional activity of p53 through hetero-oligomerization.