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We determined high-resolution crystal structures of multiple DARPin\u2013mutant p53 complexes, providing mechanistic insights into this mode of stabilization. Reporter gene assays across a comprehensive panel of cancer-associated mutants revealed reactivation of the majority of TS mutants, whereas DNA-contact mutants and those with local misfolding of the DNA-binding surface remained inactive, as expected. We demonstrate that this reactivation induces the transcription of canonical p53 target genes and elicits antiproliferative effects in cancer cell lines. A combination of this DARPin with an mRNA\/lipid nanoparticle-based transfection approach may have the potential to reactivate most TS p53 mutants and resensitize cancer cells to chemotherapy.<\/jats:p>","DOI":"10.1073\/pnas.2531747123","type":"journal-article","created":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T17:59:57Z","timestamp":1777399197000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":1,"title":["DARPins as pan-reactivators of temperature-sensitive p53 cancer mutants"],"prefix":"10.1073","volume":"123","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0548-0897","authenticated-orcid":false,"given":"Philipp","family":"M\u00fcnick","sequence":"first","affiliation":[{"name":"Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University","place":["Frankfurt, 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