Jeffrey R. Peterson, PhD
Office Phone: 215-728-3568
1. Kinase regulation and inhibition with small molecules
We are studying a number of kinases with respect to how they are regulated, what proteins they phosphorylate, and how they become dysregulated in cancer. We have a particular interest in the power of small, drug-like molecules to inactivate kinase function both as a tool to study kinases and as a therapeutic approach in cancer.Top
2. Kinase function in triple negative breast cancer
TNBC is a poorly understood but malignant type of breast cancer that disproportionately affects younger women and African-American women. There are currently no targeted therapies for TNBC but they are desperately needed. We developed a novel tool to probe kinase function in cultured cells (Anastassiadis et al., 2012, Nat Biotech). This set of highly characterized small-molecule kinase inhibitors has allowed us to systematically inactivate protein kinases in cell models of triple negative (estrogen receptor, progesterone receptor, and HER2 negative) breast cancer (TNBC) in order to identify kinase-mediated signaling pathways that contribute to TNBC. In addition, we are investigating changes in basal metabolism that are associated with TNBC and the role of kinases in controlling cancer cell metabolism. We are testing the therapeutic potential of manipulating kinase activity using drugs that target kinases that could lead to new targeted therapies for TNBC.