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- W4310355255 endingPage "102230" @default.
- W4310355255 startingPage "102230" @default.
- W4310355255 abstract "The p53 protein plays a critical role in the prevention of genome mutations in the body, however, this protein is frequently mutated in cancer and almost all cancers exhibit malfunction along the p53 pathway. In addition to a loss of activity, mutant p53 protein is prone to unfolding and aggregation, eventually forming amyloid aggregates. There continues to be a considerable effort to develop strategies to restore normal p53 expression and activity and this review details recent advances in small-molecule stabilization of mutant p53 protein and the design of p53 aggregation inhibitors." @default.
- W4310355255 created "2022-12-09" @default.
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- W4310355255 date "2023-02-01" @default.
- W4310355255 modified "2023-10-01" @default.
- W4310355255 title "Inhibition of p53 protein aggregation as a cancer treatment strategy" @default.
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- W4310355255 doi "https://doi.org/10.1016/j.cbpa.2022.102230" @default.
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