M.D., 1985, Catholic University School of Medicine, Rome, Italy.
Research Interests
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.
Recent Publications
  • How the linker connecting the two Kringles influences activation and conformational plasticity of prothrombin.
    Pozzi N, Chen Z, et al. J Biol Chem. (2016) Jan 12 [Epub ahead of print].
  • 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) Jan 15 [Epub ahead of print].
  • Why ser and not thr brokers catalysis in the trypsin fold.
    Pelc LA, Chen Z, et al. Biochemistry. (2015) 54(7):1457-64.