M.D., 1985, Catholic University School of Medicine, Rome, Italy.
Research Interests
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.
Recent Publications
  • 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.
  • 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.