Kenneth Tew, Ph.D.

My research is aimed at identifying drug discovery/development strategies with a platform of redox pathways. Earlier studies on resistance mechanisms to alkylating agents and anti-microtubule drugs led to prevalent focus on redox pathways, particularly those linked to glutathione and glutathione S-transferases (GST). For example, evidence that attachment of glutathione to cysteine residues influenced enzyme activity and laid the groundwork for more recent work on how drugs and/or stress influence post-translational S-glutathionylation and its associated cycle. These led to defining how redox mechanisms interconnect with essential signaling pathways such as how GSTP regulates Jun NH2-terminal kinase (JNK)-related signaling events and acts as a catalyst for the forward reaction of S-glutathionylation. Through clinical trials, we identified S-glutathionylated proteins as plasma biomarkers for responses to drugs and radiation. The redox proteome and its associated pathways therefore form a platform for discovery and development that continues to drive our present-day research.