Mutants aren't always bad. Mutant forms of prion proteins — found naturally in some species, including sheep, goats, and humans — can spur the aggregate of prion proteins to disassociate. Brown University's Tricia Serio and her team have been studying just how that works using two mutant prion proteins, Q24R and G58D. Once the cause of how the aggregate is destabilized is known, therapies could be developed that target protein misfolding.

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