1) Meltzer ME, Doggen CJ, de Groot PG, et al. The impact of the fibrinolytic system on the risk of venous and arterial thrombosis. Semin Thromb Hemost. 2009; 35: 468-77
|
|
|
2) Longstaff C, Thelwell C, Williams SC, et al. The interplay between tissue plasminogen activator domains and fibrin structures in the regulation of fibrinolysis: kinetic and microscopic studies. Blood. 2011; 117: 661-8
|
|
|
3) Campbell RA, Overmyer KA, Selzman CH, et al. Contributions of extravascular and intravascular cells to fibrin network formation, structure, and stability. Blood. 2009; 114: 4886-96
|
|
|
4) Suzuki Y, Mogami H, Ihara H, et al. Unique secretory dynamics of tissue plasminogen activator and its modulation by plasminogen activator inhibitor-1 in vascular endothelial cells. Blood. 2009; 113: 470-8
|
|
|
5) Suzuki Y, Yasui H, Brozska T, et al. Surface-retained tPA is essential for effective fibrinolysis on vascular endothelial cells. Blood. in press
|
|
|
6) Dan T, Miyata T. Translational research of novel PAI-1 inhibitors. Nippon Yakurigaku Zasshi. 2010; 136: 340-3
|
|
|
7) Willemse JL, Heylen E, Nesheim ME, et al. Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy? J Thromb Haemost. 2009; 7: 1962-71
|
|
|
8) Alessi MC, Juhan-Vague I. PAI-1 and the metabolic syndrome: links, causes, and consequences. Arterioscler Thromb Vasc Biol. 2006; 26: 2200-7
|
|
|
9) Oliver JJ, Webb DJ, Newby DE. Stimulated tissue plasminogen activator release as a marker of endothelial function in humans. Arterioscler Thromb Vasc Biol. 2005; 25: 2470-9
|
|
|
10) Robinson SD, Ludlam CA, Boon NA, et al. Endothelial fibrinolytic capacity predicts future adverse cardiovascular events in patients with coronary heart disease. Arterioscler Thromb Vasc Biol. 2007; 27: 1651-6
|
|
|
11) Mutch NJ, Koikkalainen JS, Fraser SR, et al. Model thrombi formed under flow reveal the role of factor XIII-mediated cross-linking in resistance to fibrinolysis. J Thromb Haemost. 2010; 8: 2017-24
|
|
|
12) Fraser SR, Booth NA, Mutch NJ. The anti-fibrinolytic function of factor XIII is exclusively expressed through {alpha}2-antiplasmin cross-linking. Blood. 2011; 117: 6371-4
|
|
|
13) Sakata Y, Aoki N. Significance of cross-linking of alpha 2-plasmin inhibitor to fibrin in inhibition of fibrinolysis and in hemostasis. J Clin Invest. 1982; 69: 536-42
|
|
|
14) Lowenberg EC, Meijers JC, Monia BP, et al. Coagulation factor XI as a novel target for antithrombotic treatment. J Thromb Haemost. 2010; 8: 2349-57
|
|
|
15) Salomon O, Steinberg DM, Zucker M, et al. Patients with severe factor XI deficiency have a reduced incidence of deep-vein thrombosis. Thromb Haemost. 2011; 105: 269-73
|
|
|
16) Brouns R, Heylen E, Willemse JL, et al. The decrease in procarboxypeptidase U (TAFI) concentration in acute ischemic stroke correlates with stroke severity, evolution and outcome. J Thromb Haemost. 2010; 8: 75-80
|
|
|
17) Izuhara Y, Takahashi S, Nangaku M, et al. Inhibition of plasminogen activator inhibitor-1: its mechanism and effectiveness on coagulation and fibrosis. Arterioscler Thromb Vasc Biol. 2008; 28: 672-7
|
|
|
18) Izuhara Y, Yamaoka N, Kodama H, et al. A novel inhibitor of plasminogen activator inhibitor-1 provides antithrombotic benefits devoid of bleeding effect in nonhuman primates. J Cereb Blood Flow Metab. 2010; 30: 904-12
|
|
|
19) Vercauteren E, Emmerechts J, Peeters M, et al. Evaluation of the profibrinolytic properties of an anti-TAFI monoclonal antibody in a mouse thromboembolism model. Blood. 2011; 117: 4615-22
|
|
|