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Our mission is to build better tools and approaches to understand the mechanics of protein behaviour in situ in the cell.
Much is known from high resolution structural methods, as well as biophysical approaches, as to how proteins work in isolation or as static complexes. However, it is less clear how proteins operate in their natural environment and participate in large functional networks because the range of tools available for the study of processes in live cells is far more limited.
In the context of this broader theme, our research is divided into three major arms:
- Understanding how protein misfolding damages a cell. Protein misfolding is central to the pathogenesis of many diseases, in particular neurodegenerative diseases such as Alzheimer’s, Parkinson’s, Huntington’s and Amyotrophic Lateral Sclerosis (ALS). Questions were are investigating include how does a cell recognize misfolded proteins and respond; how do misfolded proteins actually aggregate in the cell; and how does misfolding and aggregation interfere with normal cell function? In this context, we are focused primarily on several proteins involved in Huntington’s and ALS.
- Building new biosensors and approaches to directly view the impact of the cellular quality control processes in keeping the proteome folded. This includes new fluorescence and flow cytometry methods to probe the physiological state of the cell before and after proteins have aggregated, and new methods to visualize the extent proteins are folded inside the cell.
- Developing methods to directly view the different on and off regulatory states of enzymes, such as kinases. Our goal here is to understand how important signaling proteins switch between regulatory states as signaling cascades are propagated in the cell.
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