TP53 and cancer: Many oncogenic mutations lower the stability of the DBD even further as a result of structural perturbations, causing it to rapidly unfold at body temperature while retaining native conformation at subphysiological temperature.24–28 Such temperature-sensitive cancer mutants are potential drug targets and can, in principle, be reactivated by small-molecule binders that preferentially bind to the native state, thus preventing unfolding.29,30 It has been suggested that aggregation of structurally destabilized p53 cancer mutants plays an important role in tumor induction or progression.31