Structural biology of the tumor suppressor p53.

By A. Joerger, Alan R. Fersht. Annual Review of Biochemistry, 2008

681 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/1c2352fcbed36dca9e717dc8e44e7181ff9e7e1d

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Citations in the corpus

Targeting p53 pathways: mechanisms, structures and advances in therapy (2023, background): “259 The exact structure and interaction mechanism of PRD are largely unknown.”
Awakening guardian angels: drugging the p53 pathway (2009, background): “Strategies for reactivating mutant p53 The core domain of wild-type p53 is rather unstable, with a melting temperature of 44 °C and a short half-life of 9 minutes at body temperatur”
p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept (2016, background): “Human p53 is a 393 residue-long protein, which has three functional/structural domains, the N-terminal region (residues 1–92), the central DNA-binding domain (DBD; residues 94–292), and the C-terminal region (residues 293–393) [110].”
Mutant p53 gain-of-function in cancer. (2010, background): “…perhaps in response to particular proliferative signals, but cancer-associated mutations “fix” the protein in the altered conformational state and prevent it from engaging in sequence-specific interactions with DNA elements recognized by wtp53 (Joerger and Fersht 2007; Joerger and Fersht 2008).”
Mutant p53 in Cancer: New Functions and Therapeutic Opportunities (2014, background): “Interestingly, loss of wild-type function introduced by some destabilizing tumor-derived mutations can be rescued by additional point mutations that serve to stabilize the conformation of p53 protein, showing that the loss of structure is intrinsically reversible (Joerger and Fersht, 2008).”