The Carroll Lab

RESEARCH

Updated 7/26/2011

Redox Biology and Cancer

New methods for comprehensive and quantitative analysis of the thiol proteome are being developed and applied to the discovery of cellular signaling networks and regulatory mechanisms that involve oxidation of protein cysteine residues in cancer biology.

Reviews:

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:

Depuydt, M.; Leonard, S. E.; Vertommen, D.; Denoncin, K.; Morsomme, P.; Wahni, K.; Messens, J.; Carroll, K. S.; Collet, J. F. “A periplasmic reducing system protects single cysteine residues from oxidation.” Science. 2009, 326(5956), 1109-11. [PubMed Link]

Leonard, S. E.; Reddie, K. G.; Carroll, K. S. “Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells.” ACS Chem. Biol. 2009, 4(9), 783-99. [PubMed Link]

Research image

Paulsen, C. E.; Carroll, K. S. “Chemical dissection of an essential redox switch in yeast.” Chem. Biol. 2009, 16(2), 217-25. [PubMed Link]