In a variety of systems, proteins have been linked to processes historically limited to nucleic acids, such as infectivity and inheritance. Such proteins, termed prions, adopt multiple physical and therefore functional states in vivo, an attribute underlying their atypical roles in the cell. Our work seeks to elucidate the molecular mechanisms that module prion protein conformational flexibility in vivo using the yeast Saccharomyces cerevisiae as an experimental model.
Professor Serio received her B.S. in Molecular Biology from Lehigh University in 1991 and completed her graduate work in Molecular Biochemistry and Biophysics as a fellow of the Howard Hughes Medical Institute at Yale University (M.Phil 1995, Ph.D. 1997). From 1997 through 2002, she was a post-doctoral fellow of the Damon Runyon-Walter Winchell Cancer Research Fund at the University of Chicago and a recipient of the Howard Temin Award from the National Cancer Institute at Yale University. She joined the faculty at Brown University as an assistant professor in 2002 and was promoted to associate professor in 2008. Her research focuses on self-perpetuating protein conformations in the yeast Saccharomyces cerevisiae as model for severe neurodegenerative diseases in mammals.
TRICIA SERIO, Ph.D.
On The Web:
Tricia Serio one of 2003 Pew Scholars
Prions Rapidly "Remodel" Good Protein Into Bad
Brown Team Finds Crucial Protein Role in Deadly Prion Spread
Size of protein aggregates, not abundance, drives spread of prion-based disease
Mutant prions help cells foil harmful protein misfolding
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