Enrico Di Cera, M.D.
Alice A. Doisy Professor and Chairman
Structure and function of trypsin-like proteases, such as thrombin, and the molecular determinants of substrate specificity and allosteric regulation.
Office: DRC, Room 533
Voice: (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.
- Special issue on conformational selection.
Di Cera E. Biophys. Chem. (2013) 186:1-2.
- Histone h4 promotes prothrombin autoactivation.
Barranco-Medina S, Pozzi N, et al. J. Biol. Chem. (2013) 288(50):35749-57.
- Essential role of conformational selection in ligand binding.
Vogt AD, Pozzi N, et al. Biophys Chem. (2013) 186:13-21.
- In vitro veritas: 90 years of biochemistry at Saint Louis University.
Eissenberg JC, Di Cera E. Mo Med. (2013) 110(4):297-301.
- Conformational selection is a dominant mechanism of ligand binding.
Vogt AD, Di Cera E. Biochemistry. (2013) 52(34):5723-9.
- Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation.
Pozzi N, Chen Z, et al. J Biol Chem. (2013) 288(31):22734-44.
- Autoactivation of thrombin precursors.
Pozzi N, Chen Z, et al. J Biol Chem. (2013) 288(16):11601-10.