Enrico Di Cera, M.D.
Alice A. Doisy Professor and Chairman
Structure, function and regulation of trypsin-like proteases and their zymogens, protein engineering, and allostery.
Office: DRC, Room 533
Phone: (314) 977-9201
M.D., 1985, Catholic University School of Medicine, Rome, Italy.
We study function and regulation of proteins involved in blood coagulation, the molecular mechanism of zymogen activation and auto-activation, and the rational engineering of protease specificity for therapeutic and biotechnological purposes. Also of interest is ligand binding theory and kinetics. Our approach utilizes rapid kinetics, thermodynamics, spectroscopy and x-ray crystallography.
- Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.
Vogt AD, Chakrabortty P, Di Cera E. J Biol Chem. (2015) 290(37):22435-22445.
- John A. Schellman, 1924-2014.
Di Cera E. Biophys Chem. (2015) Jan 15 [Epub ahead of print].
- Why ser and not thr brokers catalysis in the trypsin fold.
Pelc LA, Chen Z, et al. Biochemistry. (2015) 54(7):1457-64.
- WEDGE: An anticoagulant thrombin mutant produced by autoactivation.
Wood DC, Pelc LA, et al. J Thromb Haemost. (2014) 13(1):111-4.
- Prothrombin structure: Unanticipated features and opportunities.
Pozzi N, Di Cera E. Expert Rev Proteomics. (2014) 11(6):653-5.
- The linker connecting the two kringles plays a key role in prothrombin activation.
Pozzi N, Chen Z, et al. Proc Natl Acad Sci USA. (2014) 111(21):7630-5.