Updated 7/26/2011
Our lab is taking a rational design approach toward the development of irreversible, small-molecule inhibitors that target the oxidized forms of functionally important cysteine residues in kinases and phosphatases using a nucleophilic warhead.
Reviews:
Leonard, S. E.; Carroll, K. S. “Chemical ‘omics’ approaches for understanding protein cysteine oxidation in biology.” Curr. Opin. Chem. Biol. 2011, 15(1), 88-102. [PubMed Link]
Paulsen, C. E.; Carroll, K. S. “Orchestrating redox signaling networks through regulatory cysteine switches.” ACS Chem. Biol. 2010, 5(1), 47-62. [PubMed Link]
Reddie, K. G.; Carroll, K. S. “Expanding the functional diversity of proteins through cysteine oxidation.” Curr. Opin. Chem. Biol. 2008, 12(6), 746-54. [PubMed Link]
Research Articles:
Leonard, S. E.; Garcia, F. J.; Goodsell, D. S.; Carroll, K. S. “Redox-Based Probes for Protein Tyrosine Phosphatases.” Angew. Chem. Int. Ed. Engl. 2011, 50. [PubMed Link]

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