I study the stress or heat shock protein response, which is a highly conserved reaction to physical trauma and metabolic stress in most cells and organisms. It is a key feature of the way stressed or damaged cells and tissues can mitigate damage, retain or restore normal function, and even become more resistant to future stresses. The group of proteins that are part of this response are commonly referred to as heat shock proteins (Hsps). Because neurons are difficult to replace, this response is very important in the nervous system.

My collaborators and I have shown that some isoforms of the 70 kiloDalton Hsp (Hsp70) have potential as therapeutic agents that can rescue injured neurons and other cells.

About Me 

I investigate how cells protect themselves from physical trauma and metabolic stress, especially in the nervous system. My research has focused on understanding the role of a highly conserved family of proteins, commonly referred to as heat shock proteins or Hsps, in making cells more resistant to injury or promote their survival injury. Over more than 30 years, I and collaborators at Wake Forest and elsewhere have documented that one of the more abundant of the Hsps, called Hsp70, can be used as a therapeutic agent to rescue damaged retinal and neural cells. We now understand that the cytoprotective activity of Hsp70 results from its ability to keep other cellular proteins properly folded and to modulate the immune response.

I have also been involved in graduate student professional training. I contributed to the development of classes in research ethics and to an internship program for Ph.D. and M.S. students to gain work experience beyond the conventional lab bench research.