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.
- Loop electrostatics asymmetry modulates the preexisting conformational equilibrium in thrombin.
Pozzi N, Zerbetto M, et al. Biochemistry. (2016) Jul 6 [Epub ahead of print].
- Potassium and the K+/H+ exchanger Kha1p promote binding of copper to ApoFet3p multi-copper ferroxidase.
Wu X, Kim H, et al. J Biol Chem. (2016) 291(18):9796-9806.
- Data publication with the structural biology data grid supports live analysis.
Meyer PA, Socias S, et al. Nat Commun. (2016) 7:10882.
- How the linker connecting the two Kringles influences activation and conformational plasticity of prothrombin.
Pozzi N, Chen Z, et al. J Biol Chem. (2016) 291(12):6071-6082.
- 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) pii:S0301.
- Why ser and not thr brokers catalysis in the trypsin fold.
Pelc LA, Chen Z, et al. Biochemistry. (2015) 54(7):1457-64.