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A little more than kin and less than kind: The origins of neurodegenerative disease.

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A fundamental requirement for life is that proteins remain soluble in the cell. When protein homeostasis fails to maintain solubility, toxic protein aggregates can form, leading to the dozens of protein conformational disorders, which include Alzheimer’s, Parkinson’s, and other diseases. These diseases, especially Alzheimer’s, have an incredible impact on health care in the developed world. Four million people in the United States currently suffer from Azheimer’s disease, a number expected to double by 2050. Because these diseases represent a dysfunction in a central process in biology—proteins folding into the correct shape—understanding them provides us insight into the foundations of living systems. Similarly, thinking about the basic principles that underlie life may yield important information about how the family of conformational disorders occur. Relying on one of these principles—that proteins must remain dissolved to work—has led to our first generation predictor of the the most dangerous proteins, those most susceptible to disease. Using our danger parameter, ∂, which relies on the gene expression of a given protein and the protein’s predicted tendency to form aggregates, we are able to identify groups of proteins in which the Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease pathways are overrepresented. This provides a first step at explaining the basis for human misfolding disease on a proteomic level.

This talk is part of the SBR Graduate Talks series.

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