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Do Complex Neurodegenerative Diseases Follow Simple Chemical Rules?

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Neurodegenerative diseases like Alzheimer’s, Parkinson’s, and Huntington’s have proved particularly challenging to study because they involve the disruption of a wide variety of cellular processes for reasons that are often not obvious. While it is thought that the initiating event of these diseases and many others is the folding of specific proteins into an incorrect and toxic shape, it remains an open question how this leads to a general collapse of protein homeostasis. Over the last 15 years, however, it has become apparent that the principles that govern the misfolding of proteins are general, leading to the intriguing possibility that even seemingly random disease processes follow from simple chemical principles. Our current efforts are to bring this knowledge to scale, seeking to identify bottom-up rules and top-down heuristics to help make sense of disease complexity. Our systems biology effort has recently revealed that supersaturated proteins — those whose concentrations are likely too high to remain soluble in the cell — are particularly at risk for misfolding, and that these proteins are overrepresented in the disparate disease pathways of Alzheimer’s, Parkinson’s, and Huntington’s diseases. As Alan Turing postulated 60 years ago, biological complexity — both in function and dysfunction — can emerge from relative simplicity. Applying physicochemical intuition to the large-scale analysis of biological data has the potential to yield important insights about complex disease, and to help us track the progression of neurodegenerative diseases across whole proteomes in patients over their lifetimes.

This talk is part of the King's Occasional Lectures series.

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