PRIMA-1 reactivates mutant p53 by covalent binding to the core domain.
By Jeremy M. R. Lambert, Petr Gorzov, Dimitry B Veprintsev, Maja Söderqvist, D. Segerbäck, J. Bergman, Alan R. Fersht, Pierre Hainaut, K. Wiman, V. Bykov. Cancer Cell, 2009
595 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/0c3797ef9c3afe352d2976c670b360893488a535
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Citations in the corpus
- Role of p53 in Cell Death and Human Cancers (2011, background): “DNA-binding domain of mutant p53 and covalently modifies the thiol groups in the central core DNA-binding domain, and thereby reactivates mutant p53 [134].”
- Targeting p53 pathways: mechanisms, structures and advances in therapy (2023, background): “MQ is a very active Michael receptor that preferentially and reversibly binds to the soft nucleophile cysteine thiol of p53.(422) Theoretically, all cysteines exposed on the surface of p53 are potential modification sites of Michael addition reaction(285,423) (Fig.”
- Awakening guardian angels: drugging the p53 pathway (2009, background): “Recent papers have demonstrated that although it has activity in p53-independent cell-based phenotypic assays it can nevertheless form adducts with p53 through a mechanism that involves the covalent modification of cysteine residue”
- Mutant p53 gain-of-function in cancer. (2010, background): “A number of such molecules have already been identified and described, and shown to exert antitumor effects in experimental mouse models (Bykov et al. 2002; Bykov et al. 2005; Foster et al. 1999; Lambert et al. 2009).”