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Elizabeth’s research at UNC utilized computational and experimental methods to explore the mechanism of protein aggregation in Amyotrophic Lateral Sclerosis.

Elizabeth Proctor, PhD

Elizabeth is being honored for her dissertation, titled: “Inhibiting the Formation of ALS-Relevant SOD1 Oligomers.” As the winner of the highly competitive Dean’s Distinguished Dissertation Award, she was presented with a plaque and $500 at the Graduate School’s Student Recognition Event on April 24, 2014.

Elizabeth Proctor grew up in the Chicago suburb of Libertyville, IL. After graduating from Purdue University with honors degrees in Physics and Russian Language and Literature in 2008, an interest in applied physics in biology and medicine led her to the Program in Molecular and Cellular Biophysics at UNC-Chapel Hill where she joined the lab of Nikolay Dokholyan, Professor of Biochemistry and Biophysics. Elizabeth’s research at UNC utilized computational and experimental methods to explore the mechanism of protein aggregation in the neurodegenerative disease, Amyotrophic Lateral Sclerosis. Elizabeth currently resides in Boston, MA, and is conducting post-doctoral research in the systems biology of Alzheimer’s disease with Professor Douglas Lauffenburger in the Department of Biological Engineering at the Massachusetts Institute of Technology. In her future independent career, Elizabeth aims to integrate the molecular and systems approaches to develop therapeutic strategies against neurodegenerative disease.

Abstract: Amyotrophic Lateral Sclerosis (ALS), an invariably fatal degenerative disease causing progressive paralysis, affects approximately 1 in 800 individuals. Despite decades of research, the cause of the disease remains unknown, preventing development of a cure or even an effective treatment. Aggregation of the protein Cu, Zn superoxide dismutase (SOD1) has been observed in ALS, and non-native SOD1 aggregates have been shown to participate in cytotoxic interactions. Structural knowledge of these aggregates could provide an avenue for therapeutic exploration, but their transient nature prevents traditional characterization. In my work, I develop a novel computational method to piece together low-resolution experimental data and construct the first-ever model of a meta-stable SOD1 oligomer as a toxic candidate in ALS. I use this structural model to identify non-native SOD1 aggregation interfaces and predict mutations that inhibit or promote aggregation, potentially contributing to knowledge of the molecular mechanism of ALS and elucidating pathways for future therapeutic intervention.