|Jeffery W. Kelly|
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The central theme of our research is to understand the chemistry and biology of protein folding and the competition between protein folding, misfolding and aggregation, the latter two processes being associated with a spectrum of human diseases. A recent focus has been on adapting the innate biology of protein maintenance carried out by the protein homeostasis, or proteostasis, network within the cell to enhance the folding and trafficking or clearance of aggregation-prone and/or misfolding-prone proteins. Protein maintenance is influenced by the energetics of protein folding, misfolding and aggregation as well as by numerous regulated networks of interacting and competing biological pathways; including ribosomal protein synthesis, chaperone (chaperonin) and enzyme-mediated folding, vesicular trafficking, disaggregation, and proteasome- and autophagy-mediated degradation pathways. Knowledge gained from our investigations is used to conceive of new therapeutic strategies that in one case have lead to the discovery of a first-in-class small molecule drug for the amelioration of gain-of-toxic-function transthyretin amyloid diseases that result in degeneration of the peripheral nervous system and/or the heart. We are also currently developing novel therapeutic strategies based on our basic research for Alzheimer’s disease and for loss-of-function diseases such as Gaucher disease and related lysosomal storage diseases.
We currently collaborate with the Balch, Dillin, Wiseman, Wilson, Ron, Yates, Wong and Buxbaum Laboratories.
Ongoing projects in the Kelly Laboratory include:
For a more detailed overview of our laboratory with a historical perspective, click here.
Last Modified on 05/09/2013