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Enrico Di Cera
Roy and Diana Vagelos Professor of Biochemistry and Molecular Biophysics
Professor of Medicine
Dept. of Biochemistry and
Molecular Biophysics |
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Mailing Address:
WUSM - Biochemistry Dept.
660 S. Euclid Ave., MS8231
St. Louis, MO 63110
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Research
The Di Cera laboratory is interested in the structure and function of serine proteases, especially in the molecular determinants of substrate specificity and allosteric regulation by monovalent cations. Their main focus is on thrombin, the key enzyme of blood coagulation and the prototypic allosteric protease. Emphasis is on X-ray structural studies of these forms in complex with relevant physiological substrates.
Selected Publications
- Niu, W., Chen, Z., Busch-Pelc, L.A., Bah, A., Gandhi, P.S. and Di Cera, E. The mutant N143P reveals how Na+ activates thrombin. J Biol Chem (E-pub ahead of print.) (2009).
- Gandhi, P.S., Page, M.J., Chen, Z., Bush-Pelc, L.A. and Di Cera, E. Mechanism of the anticoagulant activity of the thrombin mutant W215A/E217A. J Biol Chem 284-24098-24105 (2009).
- Di Cera, E. Know your APC. Blood 113:5970-5978 (2009).
- Bah, A., Carrell, C.J., Chen, Z., Gandhi, P.S. and Di Cera, E. Stabilization of the E* form turns thrombin into an anticoagulant. J Biol Chem 284:24098-24105 (2009).
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Di Cera, E. Serine proteases. IUBMB Life 61:510-515 (2009)
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Papaconstantinou, M.E., Gandhi, P.S., Chen, Z., Bah, A. and Di Cera, E. Na(+) Binding to meizothrombin desF1. Cell Mol Life Sci. 65:3688-3697 (2008).
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Page, M.J. and Di Cera, E. Evolution of peptidase diversity. J Biol Chem 283:30010-30014 (2008).
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Di Cera, E. How I became a biochemist. IUBMB Life 60:859-861 (2008).
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Tanaka, K.A., Gruber, A., Szlam, F., Bush, L.A., Hanson, S.R. and Di Cera, E. Interaction between thrombin mutant W215A/E217A and direct thrombin I\inhibitor. Blood Coagul Fibrinolysis 19:465-468 (2008).
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Papaconstantinou, M.E., Bah, A. and Di Cera, E. Role of the A chain in thrombin function.
Cell Mol Life Sci.65:1943-1947 (2008)
