A proteomic approach to identify yeast proteins responding to accumulation of misfolded proteins inside the cells

In growing number of diseases it has been shown that aggregation of specific proteins has an important role in pathogenesis of the disorder. This has been demonstrated in structural details with the liver cirrhosis of ${\alpha}$$_1$-antitrypsin deficiency, and it is now believed that similar protein aggregation underlies many neurodegenerative disorders such as autosomal dominant Parkinson disease, prion diseases, Alzheimer disease, and Huntington disease. ${\alpha}$$_1$-Antieypsin, a member of serine pretense inhibitor (serpin) family, functions as an inhibitor of neutrophil elastase.