Matthew Steinsaltz

My research focuses on one of the most commonly mutated proteins across all cancers, p53. When functioning correctly, p53 helps suppress tumor formation; however, when mutated, it can drive the development and progression of cancers. Understanding how these mutations lead to poor clinical outcomes is crucial for developing effective therapies and, ultimately, saving lives.

Furthermore, thirty years of research have demonstrated that mutated p53 can misfold into amyloid-like aggregates—sticky clumps of misfolded proteins typically associated with unwanted deposits that accumulate in neurodegenerative diseases. What makes these clumps particularly concerning, especially in relation to cancer, is their ability to impair p53's function or create new harmful functions. Therefore, we focus not only on how these misfolded clumps form but also on how we can help stabilize p53 to prevent misfolding and potentially halt the development or progression of some diseases altogether.