Protein Misfolding and Disease
The overall goal of our research program is to probe the folding of ALS-linked proteins in order to provide a molecular level understanding of how misfolding contributes to disease. A thermodynamic analysis of the molecular interactions stabilizing the native, functional conformation is a key first step to the development of small molecule screening assays for identifying therapeutic compounds that prevent misfolding. Current research efforts focus on utilizing biophysical methods to probe the folding, misfolding and aberrant aggregation processes in ALS variants of SOD1 and TDP-43. It is our expectation that these studies will not only lead to new insights into how to prevent misfolding in a set of human diseases, they will also provide guidelines for the biotechnological development of therapeutic small molecules and antibodies to treat disease.
Jill Zitzewitz received her B.A. in Chemistry from Carthage College in 1986 and her PhD in Bioorganic Chemistry from Washington University in St. Louis in 1991. She completed postdoctoral training in protein folding at The Pennsylvania State University, where she was awarded an NIH fellowship. Jill joined the faculty of Biochemistry and Molecular Pharmacology at UMass Medical School in 2001.