(1) Ozaki, T., & Nakagawara, A. (2011). Role of p53 in Cell Death and Human Cancers. Cancers, 3(1), 994.
(2) Hassin, O., & Oren, M. (2022). Drugging p53 in cancer: one protein, many targets. Nature Reviews Drug Discovery 2022 22:2, 22(2), 127–144.
(3) Pilley, S., Rodriguez, T. A., & Vousden, K. H. (2021). Mutant p53 in cell-cell interactions. Genes & Development, 35(7–8), 433–448.
(4) Joerger, A. C., Allen, M. D., & Fersht, A. R. (2004). Crystal Structure of a Superstable Mutant of Human p53 Core Domain: INSIGHTS INTO THE MECHANISM OF RESCUING ONCOGENIC MUTATIONS. Journal of Biological Chemistry, 279(2), 1291–1296.
(5) Blanden, A. R., Yu, X., Wolfe, A. J., Gilleran, J. A., Augeri, D. J., O’Dell, R. S., Olson, E. C., Kimball, S. D., Emge, T. J., Movileanu, L., Carpizo, D. R., & Loh, S. N. (2015). Synthetic metallochaperone ZMC1 rescues mutant p53 conformation by transporting zinc into cells as an ionophore. Molecular Pharmacology, 87(5), 825–831.
(6) Degtjarik, O., Golovenko, D., Diskin-Posner, Y., Abrahmsén, L., Rozenberg, H., & Shakked, Z. (2021). Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Nature Communications, 12(1).
(7) Chasov, V., Mirgayazova, R., Zmievskaya, E., Khadiullina, R., Valiullina, A., Stephenson Clarke, J., Rizvanov, A., Baud, M. G. J., & Bulatov, E. (2020). Key Players in the Mutant p53 Team: Small Molecules, Gene Editing, Immunotherapy. Frontiers in Oncology, 10, 555069.
(8) Brulet, J. W., Borne, A. L., Yuan, K., Libby, A. H., & Hsu, K. L. (2020). Liganding Functional Tyrosine Sites on Proteins Using Sulfur-Triazole Exchange Chemistry. Journal of the American Chemical Society, 142(18), 8270–8280.
(9) Hahm, H. S., Toroitich, E. K., Borne, A. L., Brulet, J. W., Libby, A. H., Yuan, K., Ware, T. B., McCloud, R. L., Ciancone, A. M., & Hsu, K. L. (2020). Global targeting of functional tyrosines using sulfur-triazole exchange chemistry. Nature Chemical Biology, 16(2), 150–159.
(10) Emamzadah, S., Tropia, L., & Halazonetis, T. D. (2011). Crystal structure of a multidomain human p53 tetramer bound to the natural CDKN1A (p21) p53-response element. Molecular Cancer Research, 9(11), 1493–1499.