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S. cerevisiae cells expressing the human adenosine A1 receptor (blue) and an endoplasmic reticulum (ER) marker (green) show significant co-localization, indicating primary localization within the ER during A1R protein expression. The Robinson laboratory is interested in understanding the fundamental interactions between molecules, both in isolation and in the complex environment of the cell. We use our growing understanding to design proteins with more robust or novel properties and to engineer cellular systems for improved production or drug screening applications. To this end, we are investigating the determinants of protein folding and misfolding, on both atomic and molecular levels. We have developed several novel approaches to inhibit protein misfolding and aggregation. Additionally, we are designing cellular systems for optimal expression of membrane proteins and antibodies.

A major goal of this research is to establish a set of cellular systems that could express any protein of interest. Recently, we have begun studies to understand the cellular interactions that lead to hyperphosphorylation and aggregation of tau protein, which is relevant to Alzheimer’s disease, and several other neurodegenerative diseases including corticobasal degeneration.

Our approach uses techniques in molecular biology, genetic engineering, and biophysical chemistry to identify and study macromolecules at both an atomic and cellular level. Mechanistic modeling guides us in experimental design and analysis. We use both prokaryotic (bacterial) systems as well as eukaryotic systems, such as yeast or mammalian cells. The research in the laboratory has focus areas in protein stability, expression, and aggregation for biotechnology and biomedical applications.

Anne Skaja Robinson to Chair Tulane University Department  


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