Small molecule PRIMA-1 that covalently modifies the Cys124/135/141 of P53 inhibited P53 aggregation, and a cell-permeable peptide ReACp53 derived from the distorted region of P53 (252–268 amino acids) inhibited the amyloid-like aggregate formation by the pathogenic P53R248Q mutant in primary high grade serous ovarian carcinoma cells, rescuing wild type P53 function (i.e., cell cycle arrest and apoptosis induction) in ovarian cancer [158]. This evidence concerns the gene TP53 and ovarian carcinoma.