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 are interested in the structure, function and engineering of trypsin-like proteases and their zymogen forms. The main focus of the lab is on thrombin and prothrombin as key components of the blood coagulation system. Our experimental approach includes kinetics, thermodynamics, site-directed mutagenesis, X-ray structural biology and single molecule spectroscopy.
- Kinetic dissection of the pre-existing conformational equilibrium in the trypsin fold.
Vogt AD, Chakraborty 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.