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Faculty
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Kate S. Carroll
Assistant Professor of Chemistry
Ph.D., Stanford University
Postdoctoral Fellow, University of California, Berkeley
Research Focus: Sulfur Metabolism in Mycobacteria and Chemical Tools to Study Oxidation Biology
Phone: 734.615.2739
E-mail: katesc@umich.edu
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Kate Carroll is an Assistant Professor of Chemistry and a Research Assistant Professor in the Life Sciences Institute at the University of Michigan. She completed her undergraduate degree in Biochemistry with honors from Mills College in 1996. She received her Ph.D. in 2003 from Stanford University for research on the selectivity mechanisms of vesicle cargo selection during protein transport and spent three years at the University of California at Berkeley as a Damon Runyon Postdoctoral Fellow studying sulfur pathways that are essential for infection and long-term survival of human pathogens such as Mycobacterium tuberculosis. In 2006 she joined the Chemistry Department at the University of Michigan where her laboratory develops and applies chemical tools to study the role of oxidants as signaling molecules and the biological basis of aging. Kate Carroll has received a Special Fellow Award from the Leukemia and Lymphoma Society and is a Biological Sciences Scholar at the University of Michigan.
The Carroll group in the Life Sciences Institute and the Department of Chemistry at the University of Michigan integrates biochemistry, organic chemistry, and chemical biology approaches to address problems relevant to human health and disease. Our research has two major focuses: Microbial sulfur metabolism and oxidation biology. In the host-pathogen arena, we are investigating sulfur metabolic pathways that allow Mycobacteria to persist in the human host. Our efforts in oxidation biology are directed at developing new chemical and immunological tools to identify and study post-translational modifications associated with cellular redox signaling and oxidative stress. A hallmark of our program is the ability to make new molecules and use them for a targeted function. This philosophy allows students and postdocs in the group to take their own chemistry-based projects all the way to the biological finish line. We synthesize a variety of molecules ranging from activity-based chemical probes, small-molecule inhibitors, novel haptens, and also use directed evolution to generate new catalysts. In turn, we apply a variety of biological, structural, and spectroscopic techniques to evaluate the properties and capabilities of newly synthesized molecules and catalysts in living cells.
Awards
2006 Leukemia and Lymphoma Society Special Fellow Award
2003 Damon Runyon Postdoctoral Fellow Award
Representative Publications
1. Reddie, K.G, Seo, Y.H., Muse III, W.B., Leonard, S.E. and Carroll, K.S., "A chemical approach for detecting sulfenic acid-modified proteins in living cells", Mol. BioSyst., 2008, DOI: 10.1039/b719986d.
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Chang, M.W., Belew, R.K., Carroll, K.S., Olson, A.J., Goodsell, D.S., "Empirical entropic contributions in computational docking: Evaluation in APS reductase complexes", Mol. BioSyst., 2008, DOI: 10.1002/jcc.20936a.
3. Bhave, D.P., Muse III, W.B., Carroll, K.S., "Drug Targets in mycobacterial sulfur metabolism", Infectious Disorders- Drug Targets, 2007, 140.
4. Chartron, J., Shiau, C., Stout, C.D., Carroll, K.S., "3'-Phopspoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle", Biochemistry, 2007, 46, 3942.
5. Gao, H., Leary, J.A., Carroll, K.S., Bertozzi, C.R., Chen, H., "Noncovalent complexes of APS Reductase from Mycobacterium tuberculosis: delineating a mechanistic model using ESI-FTICR MS", J. Am. Chem. Soc., 2007, 18, 167.
6. Charton, J., Carroll, K.S., Shiau, C., Gao, H., Leary, J.A., Bertozzi, C.R., Stout, C.D., "Substrate recognition protein dynamics adn novel iron-sulfur cluster in Pseudomonas aeruginosa APS reductase", J. Mol. Biol., 2006, 364, 152.
7. Carroll, K.S., Gao, H., Chen, H., Leary, J.A. and Bertozzi, C.R., "Investigation of the iron-sulfur cluster in Mycobacterium tuberculosis APS reductase: Implications for substrate binding and catalysis", Biochem., 2005, 44, 14647.
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