Education
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
  • 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.