Associate Professor, Department of Chemistry, Florida Campus Scripps Research Institute
"Cysteine-mediated Redox Signaling: Chemical Tools for Biological Discovery"
Kate S Carroll is an Associate Professor with Tenure in the Department of Chemistry at The Scripps Research Institute in Jupiter, Florida. She received her BA degree in Biochemistry from Mills College in 1996 and PhD in Biochemistry from Stanford University in 2003. Her postdoctoral work was completed at the University of California, Berkeley, where she was a Damon Runyon-Walter Winchell Chancer Fund Fellow with Prof. Carolyn Bertozzi. She was an assistant professor at the University of Michigan until 2010, when she joined the Chemistry faculty at Scripps. Her research interests span the disciplines of chemistry and biology with an emphasis on studies of sulfur biochemistry pertinent to disease states. Her lab focuses on the development of novel tools to study redox modifications of cysteine thiols, profiling changes in protein oxidation associated with disease, and exploiting this information for development of diagnostic and therapeutic approaches. In addition, her group investigates sulfur pathways that are essential for infection and long-term survival of human pathogens such as Mycobacterium tuberculosis. Dr. Carroll currently serves on the editorial board of Cell Chemical Biology, Molecular Biosystems, Journal of Biology Chemistry, and is a contributing member of ‘Faculty of 1000’. She is also the recipient of the ACS Pfizer Award in Enzyme Chemistry (2013), Camille Dreyfus Teacher-Scholar Award (2010), Scientist Development Award from American Heart Association (2008), and Special Fellow Award from the Leukemia and Lymphoma Society (2006).
The Carroll lab has an established record of attacking fundamental problems in redox biology through a powerful, interdisciplinary approach that integrates synthetic chemistry with proteomics, biochemistry, and cell biology. An overarching goal of our research program is to understand the biological chemistry and molecular mechanisms of redox-based cellular regulation and signal transduction, with particular emphasis on the role of cysteine oxidation, a ubiquitous and conserved mechanism for controlling protein function. We are also exploring the therapeutic potential of redox-regulated protein function by developing an entirely new class of inhibitors that targets oxidized cysteine residues of key proteins involved in human disease. Ultimately, our goal is to accelerate the discovery of key regulatory nodes of redox-signaling networks, profile changes in protein cysteine oxidation associated with disease, and harness this information for the development of new diagnostic and therapeutic approaches.