Protein misfolding and aggregation are the hallmark of several neurodegenerative diseases and other disorders. Protein misfolding can be sporadic or due to genetic mutations that alter folding. In addition, chaperones that normally assist in protein folding have been linked to inherited diseases (chaperonopathies) when mutated. My research investigates how the process of protein misfolding occurs, how it propagates, and how these problems can be corrected in the cell. We are specifically interested in prions, toxic protein aggregates and amyloid associated with neurodegenerative diseases, and chaperone mutants linked to a form of muscular dystrophy. We use a yeast model system and biochemical approaches to uncover important cellular contributors and elucidate mechanisms to prevent or rescue protein misfolding and aggregation.
- BS: University of Wisconsin – Parkside, Kenosha, WI, 1992, Molecular Biology
- MS: University of Illinois, Urbana, IL, 1995, Microbiology
- PhD: University of Illinois, Urbana, IL, 1998, Microbiology
- Postdoc: The University of Chicago, Chicago, IL, 1998-2001, Genetics
- Postdoc: The Whitehead Institute/MIT, Cambridge, MA, 2001-2003, Genetics
Graduate & Fellowship Program Affiliations
Pullen MY, Weihl CC, and True HL