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Prion diseases are fatal and currently untreatable neurodegenerative diseases of humans and animals. The central event underlying these diseases is the 3D conversion of the prion protein (PrPC) to a pathogenic shape, denoted PrPSc. It is often said that to understand a person, one should look at the company they keep. This is also true of proteins, as their interaction networks, or interactomes, define their functions. Although some information is available about the cellular partners of PrPC, almost nothing is known about the interaction network of PrPSc. Here, we propose to examine the PrPSc interactome for the first time, providing a wealth of new targets for therapeutic intervention.
About the Researcher:
Robert C.C. Mercer, Ph.D.
Instructor, Department of Biochemistry, Boston University School of Medicine
Dr. Mercer has over 10 years of experience in the prion field. First as a PhD student at the Centre for Prions and Protein Folding diseases at the University of Alberta under the tutelage of Dr. David Westaway and later as a Postdoctoral Associate and now Instructor at the Boston University Chobanian & Avedisian School of Medicine in the laboratory of Dr. David A. Harris. His work has focused primarily on the function of PrPC, modeling genetic forms of prion disease in mice, and the discovery and characterization of prion disease therapeutics.
Recipient Of:
- The Joanne (Jody) Atchison Memorial Research Grant, contributed by Dick Atchison
- The Robert Dodd Memorial Research Grant, contributed by Kathleen Dodd
- The Sherry Maxwell Fabian Memorial Grant, contributed by Tom Fabian
- The Chuck Fear Memorial Research Grant, contributed by Pamela Fear
- The Patrice Haggerty Memorial Grant, contributed by William Haggerty
- The Laura McElmurray Memorial Research Grant, contributed by Mike McElmurray
- The Lynda Morris Memorial Grant, contributed by David Morris
- The Nic Ziccardi Memorial Research Grant, contributed by Kandi Ziccardi
- The Strides for CJD Research Grant, contributed by the families of the CJD Foundation
- The CJD Foundation Grant, contributed by the families of the CJD Foundation