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  • 1
    Bode W. The structure of thrombin, a chameleon-like proteinase. J Thromb Haemost 2005; 3: 237988.
  • 2
    Bode W, Turk D, Karshikov A. The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci 1992; 1: 42671.
  • 3
    Di Cera E. Thrombin as a procoagulant and an anticoagulant. J Thromb Haemost 2007 (this issue).
  • 4
    Huntington JA. Molecular recognition mechanisms of thrombin. J Thromb Haemost 2005; 3: 186172.
  • 5
    Krishnaswamy S. Exosite-driven substrate specificity and function in coagulation. J Thromb Haemost 2005; 3: 5467.
  • 6
    Bock P. Exosites in the substrate specificity of blood coagulation reactions. J Thromb Haemost 2007; 5 (Suppl. 1): 8194.
  • 7
    Page MJ, Macgillivray RTA, Di Cera E. Determinants of specificity in coagulation proteases. J Thromb Haemost 2005; 3: 24018.
  • 8
    Pineda AO, Carrell CJ, Bush LA, Prasad S, Caccia S, Chen ZW, Mathews FS, Di Cera E. Molecular dissection of Na+ binding to thrombin. J Biol Chem 2004; 279: 3184253.
  • 9
    Gruber A, Cantwell AM, Di Cera E, Hanson SR. The thrombin mutant W215A/E217A shows safe and potent anticoagulant and antithrombotic effects in vivo. J Biol Chem 2002; 277: 275814.
  • 10
    Gruber A, Fernandez JA, Bush L, Marzec U, Griffin JH, Hanson SR, E DIC. Limited generation of activated protein C during infusion of the protein C activator thrombin analog W215A/E217A in primates. J Thromb Haemost 2006; 4: 3927.
  • 11
    Carter WJ, Myles T, Gibbs CS, Leung LL, Huntington JA. Crystal structure of anticoagulant thrombin variant E217 K provides insights into thrombin allostery. J Biol Chem 2004; 279: 2638794.
  • 12
    Huntington JA, Esmon CT. The molecular basis of thrombin allostery revealed by a 1.8 A structure of the “slow” form. Structure (Camb) 2003; 11: 46979.
  • 13
    Pineda AO, Savvides SN, Waksman G, Di Cera E. Crystal structure of the anticoagulant slow form of thrombin. J Biol Chem 2002; 277: 4017780.
  • 14
    Pineda AO, Zhang E, Guinto ER, Savvides SN, Tulinsky A, Di Cera E. Crystal structure of the thrombin mutant D221A/D222 K: the Asp222:Arg187 ion-pair stabilizes the fast form. Biophys Chem 2004; 112: 2536.
  • 15
    Pineda AO, Chen ZW, Bah A, Garvey LC, Mathews FS, Di Cera E. Crystal structure of thrombin in a self-inhibited conformation. J Biol Chem 2006; 281: 329228.
  • 16
    Mann KG, Brummel K, Butenas S. What is all that thrombin for? J Thromb Haemost 2003; 1: 150414.
  • 17
    Monroe DM, Hoffman M. What does it take to make the perfect clot? Arterioscler Thromb Vasc Biol 2006; 26: 418.
  • 18
    Orcutt SJ, Krishnaswamy S. Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin. J Biol Chem 2004; 279: 5492736.
  • 19
    Wu Q, Picard V, Aiach M, Sadler JE. Activation-induced exposure of the thrombin anion-binding exosite. Interactions of recombinant mutant prothrombins with thrombomodulin and a thrombin exosite-specific antibody. J Biol Chem 1994; 269: 372530.
  • 20
    Mollica L, Preston RJ, Chion AC, Lees SJ, Collins P, Lewis S, Lane DA. Autoantibodies to thrombin directed against both of its cryptic exosites. Br J Haematol 2006; 132: 48793.
  • 21
    Mosesson MW. Fibrinogen and fibrin structure and functions. J Thromb Haemost 2005; 3: 1894904.
  • 22
    Coughlin SR. Protease-activated receptors in hemostasis, thrombosis and vascular biology. J Thromb Haemost 2005; 3: 180014.
  • 23
    Ramakrishnan V, DeGuzman F, Bao M, Hall SW, Leung LL, Phillips DR. A thrombin receptor function for platelet glycoprotein Ib-IX unmasked by cleavage of glycoprotein V. Proc Natl Acad Sci U S A 2001; 98: 18238.
  • 24
    Baglia FA, Badellino KO, Li CQ, Lopez JA, Walsh PN. Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin. J Biol Chem 2002; 277: 16628.
  • 25
    Esmon CT. Molecular events that control the protein C anticoagulant pathway. Thromb Haemost 1993; 70: 2935.
  • 26
    Ruf W. Is APC activation of endothelial cell PAR1 important in severe sepsis? Yes. J Thromb Haemost 2005; 3: 19124.
  • 27
    Riewald M, Petrovan RJ, Donner A, Mueller BM, Ruf W. Activation of endothelial cell protease activated receptor 1 by the protein C pathway. Science 2002; 296: 18802.
  • 28
    Nesheim M. Thrombin and fibrinolysis. Chest 2003; 124: 33S9S.
  • 29
    Bouma BN, Meijers JC. Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U). J Thromb Haemost 2003; 1: 156674.
  • 30
    Nagashima M, Yin ZF, Zhao L, White K, Zhu Y, Lasky N, Halks-Miller M, Broze GJ Jr, Fay WP, Morser J. Thrombin-activatable fibrinolysis inhibitor (TAFI) deficiency is compatible with murine life. J Clin Invest 2002; 109: 10110.
  • 31
    Nishimura T, Myles T, Piloponsky A, Kao PN, Berry GJ, Leung LL. Thrombin-activatable procarboxypeptidase B regulates activated complement C5a in vivo. Blood 2007; 109: 19927.
  • 32
    Li W, Johnson DJ, Esmon CT, Huntington JA. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Nat Struct Mol Biol 2004; 11: 85762.
  • 33
    Tollefsen DM. Heparin cofactor II. Adv Exp Med Biol 1997; 425: 3544.
  • 34
    Lane DA, Philippou H, Huntington JA. Directing thrombin. Blood 2005; 106: 260512.
  • 35
    Philippou H, Rance J, Myles T, Hall SW, Ariens RA, Grant PJ, Leung L, Lane DA. Roles of low specificity and cofactor interaction sites on thrombin during factor XIII activation. Competition for cofactor sites on thrombin determines its fate. J Biol Chem 2003; 278: 320206.
  • 36
    Tsiang M, Jain AK, Dunn KE, Rojas ME, Leung LL, Gibbs CS. Functional mapping of the surface residues of human thrombin. J Biol Chem 1995; 270: 1685463.
  • 37
    Pechik I, Madrazo J, Mosesson MW, Hernandez I, Gilliland GL, Medved L. Crystal structure of the complex between thrombin and the central “E” region of fibrin. Proc Natl Acad Sci U S A 2004; 101: 271823.
  • 38
    Myles T, Yun TH, Leung LL. Structural requirements for the activation of human factor VIII by thrombin. Blood 2002; 100: 28206.
  • 39
    Myles T, Yun TH, Hall SW, Leung LL. An extensive interaction interface between thrombin and factor V is required for factor V activation. J Biol Chem 2001; 276: 251439.
  • 40
    Hall SW, Nagashima M, Zhao L, Morser J, Leung LL. Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains. J Biol Chem 1999; 274: 255106.
  • 41
    Hall SW, Gibbs CS, Leung LL. Identification of critical residues on thrombin mediating its interaction with fibrin. Thromb Haemost 2001; 86: 146674.
  • 42
    Esmon CT. Structure and functions of the endothelial cell protein C receptor. Crit Care Med 2004; 32: S298301.
  • 43
    Bourin MC, Ohlin AK, Lane DA, Stenflo J, Lindahl U. Relationship between anticoagulant activities and polyanionic properties of rabbit thrombomodulin. J Biol Chem 1988; 263: 804452.
  • 44
    Rezaie AR, Yang L. Thrombomodulin allosterically modulates the activity of the anticoagulant thrombin. Proc Natl Acad Sci U S A 2003; 100: 120516.
  • 45
    Rezaie AR, Olson ST. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies. Biochemistry 2000; 39: 1208390.
  • 46
    Ayala YM, Cantwell AM, Rose T, Bush LA, Arosio D, Di Cera E. Molecular mapping of thrombin-receptor interactions. Proteins 2001; 45: 10716.
  • 47
    Myles T, Le Bonniec BF, Stone SR. The dual role of thrombin’s anion-binding exosite-I in the recognition and cleavage of the protease-activated receptor 1. Eur J Biochem 2001; 268: 707.
  • 48
    Li CQ, Vindigni A, Sadler JE, Wardell MR. Platelet glycoprotein Ib alpha binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin. J Biol Chem 2001; 276: 61618.
  • 49
    Streusand VJ, Bjork I, Gettins PG, Petitou M, Olson ST. Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement. J Biol Chem 1995; 270: 904351.
  • 50
    Crawley JT, Lam JK, Rance JB, Mollica LR, O’Donnell JS, Lane DA. Proteolytic inactivation of ADAMTS13 by thrombin and plasmin. Blood 2005; 105: 108593.
  • 51
    Lam JK, Chion CKNK, Zanardelli S, Lane DA, Crawley JTB. Further characterisation of ADAMTS13 inactivation by thrombin. J Thromb Haemost 2007 (in press).
  • 52
    Higgins DL, Lewis SD, Shafer JA. Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin. J Biol Chem 1983; 258: 927682.
  • 53
    Esmon CT, Lollar P. Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII. J Biol Chem 1996; 271: 138827.
  • 54
    Meh DA, Siebenlist KR, Mosesson MW. Identification and characterization of the thrombin binding sites on fibrin. J Biol Chem 1996; 271: 231215.
  • 55
    Yun TH, Baglia FA, Myles T, Navaneetham D, Lopez JA, Walsh PN, Leung LL. Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively. J Biol Chem 2003; 278: 481129.