Enrico Di Cera Lab

Selected Original 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.PubMed PMID: 24821807, PDF

  • Di Cera E. Special issue on conformational selection. (2013) Biophys. Chem. 186:1-2.
    PubMed PMID: 24315627, PDF

  • Barranco-Medina S et al. Histone h4 promotes prothrombin autoactivation. (2013) J. Biol. Chem. 288(50):35749-35757.
    PubMed PMID: 24178300 , PDF

  • Vogt AD et al. Essential role of conformational selection in ligand binding. (2013) Biophys Chem. 186:13-21.
    PubMed PMID: 241132848, PDF

  • Eissenberg JC, Di Cera E. In vitro veritas: 90 years of biochemistry at Saint Louis University. (2013) Mo Med. 110(4):297-301.
    PubMed PMID: 24003646, PDF

  • Vogt AD et al. Conformational selection is a dominant mechanism of ligand binding. (2013) Biochemistry. 52(34):5723-5729.
    PubMed PMID: 23947609, PDF

  • Pozzi N et al. Crystal structure of prothrombin reveals conformational flexibility and mechanism of action. (2013) J Biol Chem, 288(31):22734-22744.
    PubMed PMID: 23775088, PDF

  • Pozzi N et al. Autoactivation of thrombin precursors. (2013) J Biol Chem, 288, 11601-11610.
    PubMed PMID: 23467412, PDF

  • Vogt AD and Di Cera E. Conformational Selection or Induced Fit? A Critical Appraisal of the Kinetic Mechanism. (2012) Biochemistry, 51, 5894-5902.
    PubMed PMID: 22775458, PDF

  • Pozzi N et al. Conformational selection in trypsin-like proteases. (2012) Curr Opin Struct Biol, 22, 421-31.
    PubMed PMID: 22664096, PDF

  • Pozzi N et al. Exposure of R169 controls protein C activation and autoactivation. (2012) Blood, 120, 664-70.
    PubMed PMID: 22535660, PDF

  • Pozzi N et al. Crystal structures of prethrombin-2 reveal alternative conformations under identical solution conditions and the mechanism of zymogen activation. (2011) Biochemistry, 50, 10195-10202.
    PubMed PMID: 22049947, PDF

  • Niu W et al. Crystallographic and kinetic evidence of allostery in a trypsin-like protease. (2011) Biochemistry, 50, 6307-6307.
    PubMed PMID: 21707111, PDF

  • Pozzi N et al. Rigidification of the autolysis loop enhances Na(+) binding to thrombin. (2011) Biophys Chem, 159, 6-13.
    PubMed PMID: 21536369, PDF

  • Berny-Lang MA et al. Thrombin mutant W215A/E217A treatment improves neurological outcome and reduces cerebral infarct size in a mouse model of ischemic stroke. (2011) Stroke 42, 1736-1741.
    PubMed PMID: 21512172, PDF

  • Flick MJ et al. The development of inflammatory joint disease is attenuated in mice expressing the anticoagulant prothrombin mutant W215A/E217A. (2011) Blood 117, 6326-6337.
    PubMed PMID: 21436072, PDF

  • Rana S et al. Redesigning allosteric activation in an enzyme. (2011) Proc Natl Acad Sci USA 108, 5221-5225.
    PubMed PMID: 21368156, PDF

  • Chen Z et al. Crystal structure of prethrombin-1. (2010) Proc Natl Acad Sci USA 107, 19278-19283.
    PubMed PMID: 20974933, PDF

  • Gandhi PS et al. Crystal structure of thrombin bound to the uncleaved extracellular fragment of PAR1. (2010) J Biol Chem 285, 15393-15398.
    PubMed PMID: 20236938, PDF

  • Niu W et al. Mutant N143P reveals how Na+ activates thrombin. (2009) J Biol Chem 284, 36175-36185.
    PubMed PMID: 19846563, PDF

  • Bah A et al. Stabilization of the E* form turns thrombin into an anticoagulant. (2009) J Biol Chem 284, 20034-20040.
    PubMed PMID: 19473969, PDF

  • Gandhi PS et al. Structural identification of the pathway of long-range communication in an allosteric enzyme. (2008) Proc Natl Acad Sci USA 105, 1832-1837.
    PubMed PMID: 18250335, PDF

  • Bah A et al. Crystal structures of murine thrombin in complex with the extracellular fragments of protease-activated receptors PAR3 and PAR4. (2007) Proc Natl Acad Sci USA 104, 11603-11608.
    PubMed PMID: 17606903, PDF

  • Gruber A et al. Relative antithrombotic and antihemostatic effects of protein C activator versus low molecular weight heparin in primates. (2007) Blood 109, 3733-3740.
    PubMed PMID: 17227834, PDF

  • Bah A et al. Rapid kinetics of Na+ binding to thrombin. (2006) J Biol Chem 281, 40049-40056.
    PubMed PMID: 17074754, PDF

  • Pineda AO et al. Crystal structure of thrombin in a self-inhibited conformation. (2006) J Biol Chem 281, 32922-32928.
    PubMed PMID: 16962697, PDF

  • Prasad S et al. Redesigning the monovalent cation specificity of an enzyme. (2003) Proc Natl Acad Sci USA 100, 13785-13790.
    PubMed PMID: 14612565, PDF

  • Gruber A et al. The thrombin mutant W215A/E217A shows safe and potent anticoagulant and antithrombotic effects in vivo. (2002) J Biol Chem 277, 27581-27584.
    PubMed PMID: 12070133, PDF

  • Krem MM & Di Cera E. Molecular markers of serine protease evolution. (2001) EMBO J 20, 3036-3045.
    PubMed PMID: 11406580, PDF

  • Cantwell AM & Di Cera E. Rational design of a potent anticoagulant thrombin. (2000) J Biol Chem 275, 39827-39830.
    PubMed PMID: 11060281, PDF

  • Vindigni A et al. Site-specific dissection of substrate recognition by thrombin. (1997) Nat Biotechnol 15, 891-895.
    PubMed PMID: 9306406, PDF

  • Ido Y et al. Prevention of vascular and neural dysfunction in diabetic rats by C-peptide. (1997) Science 277, 563-566.
    PubMed PMID: 9228006, PDF

  • Dang QD et al. Rational engineering of catalytic activity and specificity in a serine protease. (1997) Nat Biotechnol 15, 146-149.
    PubMed PMID: 9035139, PDF

  • Dang QD & Di Cera E. Residue 225 determines the Na+-induced allosteric regulation of catalytic activity in serine proteases. (1996) Proc Natl Acad Sci USA 93, 10653-10656.
    PubMed PMID: 8855234, PDF

  • Nayal M & Di Cera E. Valence screening of water in protein crystals reveals potential Na+ binding sites. (1996) J Mol Biol 256, 228-234.
    PubMed PMID: 8594192, PDF

  • Di Cera E et al. The Na+ binding site of thrombin. (1995) J Biol Chem 270, 22089-22092.
    PubMed PMID: 7673182, PDF

  • Dang OD et al. An allosteric switch controls the procoagulant and anticoagulant activities of thrombin. (1995) Proc Natl Acad Sci USA 92, 5977-5981.
    PubMed PMID: 7597064, PDF

  • Nayal M & Di Cera E. Predicting Ca2+-binding sites in proteins. (1994) Proc Natl Acad Sci USA 91, 817-821.
    PubMed PMID: 8290605, PDF

  • Wells CM & Di Cera E. Thrombin is a Na+-activated enzyme. (1992) Biochemistry 31, 11721-11730.
    PubMed PMID: 1445907, PDF


Selected Reviews

  • Pozzi N et al. Conformational selection in trypsin-like proteases. (2012) Curr Opin Struct Biol, 22, 421-431.
    PubMed PMID: 22664096, PDF

  • Gohara DW and Di Cera E. Allostery in trypsin-like proteases suggests new therapeutic strategies. (2011) Trends Biotechnol, 29, 577-585.
    PubMed PMID: 21726912, PDF

  • Gandhi PS et al. Structural basis of thrombin-PAR interactions. (2011) IUBMB Life 63, 375-382.
    PubMed PMID: 21698746, PDF

  • Di Cera E. Thrombin as an anticoagulant. (2011) Prog Mol Biol Transl Sci 99, 145-184.
    PubMed PMID: 21238936, PDF

  • Di Cera E. Thrombin. (2008) Mol Aspects Med 29, 203-254.
    PubMed PMID: 18329094, PDF

  • Page MJ & Di Cera E. Serine peptidases: classification, structure and function. (2008) Cell Mol Life Sci 65, 1220-1236.
    PubMed PMID: 18259688, PDF

  • Page MJ & Di Cera E. Role of Na+ and K+ in enzyme function. (2006) Physiol Rev 86, 1049-1092.
    PubMed PMID: 17015484, PDF

  • Di Cera E. A structural perspective on enzymes activated by monovalent cations. (2006) J Biol Chem 281, 1305-1308.
    PubMed PMID: 16267046, PDF

  • Krem MM & Di Cera E. Evolution of enzyme cascades from embryonic development to blood coagulation. (2002) Trends Biochem Sci 26, 67-74.
    PubMed PMID: 11852243, PDF

  • Di Cera E. Site-specific analysis of mutational effects in proteins. (1998) Adv Protein Chem 51, 59-119.
    PubMed PMID: 961516, PDF