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		Jeffery W. Kelly
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Our major goal is to understand the molecular mechanisms of protein folding and misfolding in a test tube, and in the cytoplasm and secretory pathway of mammalian cells. To accomplish this, we employ cell biological, spectroscopic, and biophysical approaches, in combination with chemical synthesis. The latter is being utilized to discover small molecules that manipulate protein folding and misfolding at the protein level and systems biology level in mammals. Besides understanding protein misfolding diseases, we also aim to develop new small-molecule therapeutic strategies against these neurodegenerative disorders.

· Amyloid as a functional fold:

There appears to be a fine line between pathology and physiology. It is hard to imagine, given the spontaneity of amyloid fibril formation, that this structure was not selected as a functional fold at some point during evolution. We are amassing evidence that this structure is used commonly in organelle biogenesis, and have developed the reagents to identify new amyloid folds in mammalian cells and tissue.

 

 

• Introduction
• · Transthyretin amyloid diseases: understanding the mechanism of proteotoxicity and inhibition of amyloid fibril formation
• · Understanding Abeta aggregation and Alzheimer's disease
• · Gelsolin amyloid disease mechanism and therapeutics
• · β-Sheet folding
• · Parkinson's disease
• · Restoration of enzyme homeostasis in lysosomal storage diseases
• · Amyloid as a functional fold