Education
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
  • Molecular mechanisms of enzyme activation by monovalent cations.
    Gohara DW, Di Cera E. J Biol Chem. (2016) Jul 26 [Epub ahead of print].
  • Structural architecture of prothrombin in solution revealed by single molecule spectroscopy.
    Pozzi N, Bystranowska D, et al. J Biol Chem. (2016) Jul 19 [Epub ahead of print].
  • Dual effect of histone H4 on prothrombin activation.
    Pozzi N, Di Cera E. J Thromb Haemost. (2016) June 30 [Epub ahead of print].
  • Loop electrostatics asymmetry modulates the preexisting conformational equilibrium in thrombin.
    Pozzi N, Zerbetto M, et al. Biochemistry. (2016) 55(28):3984-3994.
  • Potassium and the K+/H+ exchanger Kha1p promote binding of copper to ApoFet3p multi-copper ferroxidase.
    Wu X, Kim H, et al. J Biol Chem. (2016) 291(18):9796-9806.
  • Data publication with the structural biology data grid supports live analysis.
    Meyer PA, Socias S, et al. Nat Commun. (2016) 7:10882.
  • How the linker connecting the two Kringles influences activation and conformational plasticity of prothrombin.
    Pozzi N, Chen Z, et al. J Biol Chem. (2016) 291(12):6071-6082.
  • 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) pii:S0301.
  • Why ser and not thr brokers catalysis in the trypsin fold.
    Pelc LA, Chen Z, et al. Biochemistry. (2015) 54(7):1457-64.