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My lab is dedicated to the research of protein folding in health and disease. Specifically we are currently focussing on the folding pathways of α-synuclein. α-Synuclein (αSyn) is a small protein of unknown bodily function strongly linked to Parkinson’s disease (PD), Dementia with Lewy Bodies (DLB) and related fatal human diseases called “synucleinopathies”. Inherited changes in the production rate or structure of αSyn are known to invariably cause early-onset PD. Nevertheless, the precise biochemical nature of these changes in αSyn structure is still unknown despite the concerted effort of the field for almost two decades. Our lab recently discovered that the main form of αSyn in the human body appears to be a hitherto unrecognized structure that resists disease-associated changes. We believe this natural form has to be destabilized before disease can occur. Our main foci are to determine what factors cause this destabilization and therefore disease, to develop tools to detect these factors as potential diagnostic tools, and to stabilize the physiological forms of αSyn as a novel therapeutic approach. Additionally, we are currently extending our analysis of physiological αSyn species to pathological species isolated from human tissue to elucidate αSyn’s mechanism of neuronal toxicity.

CURRENT TEAM MEMBERS

Tim Bartels, PhD
Assistant Professor of Neurology

Matteo Rovere, MSc
Research Technician

Adam Cantlon, PhD
Post-doctoral fellow

Haiyang Jiang, MD
Post-doctoral fellow

Laura De Boni, MD
Post-doctoral fellow

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