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.
- Essential role of conformational selection in ligand binding.
Vogt AD, Pozzi N, et al. Biophys Chem. (2013) Sept 25 [Epub ahead of print].
- 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.
- Conformational selection or induced fit? A critical appraisal of the kinetic mechanism.
Vogt AD and Di Cera E. Biochemistry. (2012) 51(30):5894-902.
- Conformational selection in trypsin-like proteases.
Pozzi N, Vogt AD, et al. Curr Opin Struct Biol. (2012) 22(4):421-31.
- Exposure of R169 controls protein C activation and auto activation.
Pozzi N, Barranco-Medina S, et al. Blood. (2012) 120(3):664-70.
- Thrombomodulin is required for the antithrombotic activity of thrombin mutant W215A/E217A in a mouse model of arterial thrombosis.
Vicente CP, et al. Thromb Res. (2012) 130(4):646-8.