Molecular chaperones are highly abundant proteins and are essential in all organisms. They regulate both the folding and degradation of many key signaling molecules. We are interested in the basic question of how molecular chaperone specificity is regulated. The ultimate goal of our work is to elicit greater control of chaperones to correct proteostatic defects that can arise in cancer and other illnesses.
Hsp70 Function (Source: Stressmarq Bioscience) :
The lab incorporates protein biochemistry, molecular biology, proteomics, systems biology, bacterial and yeast genetics and cell culture technologies.
Keywords: protein-protein interactions, protein folding, CRISPR-CAS9, cancer, signal transduction, phosphorylation, Hsp70, Hsp90, cell cycle, DNA damage response, yeast genetics.
Interested in working with CRISPR-CAS9?
Our lab utilizes CRISPR to knockout, mutate and epitope tag genes. If you are interested in collaborating on a CRISPR project, please click here for more details!
NIH-funded research opportunities for undergraduate and students available!
For more information, please click here.