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.
- How the linker connecting the two Kringles influences activation and conformational plasticity of prothrombin.
Pozzi N, Chen Z, et al. J Biol Chem. (2016) Jan 12 [Epub ahead of print].
- 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.