A study of the activation of fibrin-bound plasminogen by tissue-type plasminogen activator, single chain urokinase and sequential combinations of the activators
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[1] V. Gurewich,et al. A comparison of the rates of clot lysis in a plasma milieu induced by tissue plasminogen activator (t-PA) and rec-pro-urokinase: Evidence that t-PA has a more restricted mode of action , 1992 .
[2] E. Topol,et al. Clot-selective coronary thrombolysis with lowdose synergistic combinations of single-chain urokinase-type plasminogen activator and recombinant tissue-type plasminogen activator☆ , 1991 .
[3] Jian-ning Liu,et al. A comparative study of the promotion of tissue plasminogen activator and pro-urokinase-induced plasminogen activation by fragments D and E-2 of fibrin. , 1991, The Journal of clinical investigation.
[4] E. Angles-cano,et al. Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. , 1991, Biochemistry.
[5] S. Husain,et al. Single-chain urokinase-type plasminogen activator does not possess measurable intrinsic amidolytic or plasminogen activator activities. , 1991, Biochemistry.
[6] P. Declerck,et al. Role of α2-Antiplasmin in Fibrin-Specific Clot Lysis with Single-Chain Urokinase-Type Plasminogen Activator in Human Plasma , 1991, Thrombosis and Haemostasis.
[7] D. Rouy,et al. The mechanism of activation of plasminogen at the fibrin surface by tissue-type plasminogen activator in a plasma milieu in vitro. Role of alpha 2-antiplasmin. , 1990, The Biochemical journal.
[8] B. Sobel,et al. The Nature of Synergy between Tissue-Type and Single Chain Urokinase-Type Plasminogen Activators , 1989, Thrombosis and Haemostasis.
[9] D. Collen,et al. The mechanism of plasminogen activation and fibrin dissolution by single chain urokinase-type plasminogen activator in a plasma milieu in vitro. , 1989, Blood.
[10] D. Collen,et al. Thrombolytic properties of human tissue-type plasminogen activator, single-chain urokinase-type plasminogen activator, and synergistic combinations in venous thrombosis models in dogs and rabbits , 1989 .
[11] H. Gold,et al. Synergistic combinations of recombinant human tissue-type plasminogen activator and human single-chain urokinase-type plasminogen activator. Effect on thrombolysis and reocclusion in a canine coronary artery thrombosis model with high-grade stenosis. , 1989, Circulation.
[12] M. Samama,et al. Thrombolytic properties of tissue plasminogen activator (t-PA) and single chain urokinase plasminogen activator (scu-PA) in vitro: Absence of synergy as demonstrated by two quantitative analytical methods , 1989 .
[13] L. Lund,et al. One-chain urokinase-type plasminogen activator from human sarcoma cells is a proenzyme with little or no intrinsic activity. , 1988, The Journal of biological chemistry.
[14] F. Castellino,et al. The activation of human [Glu1]plasminogen by human single-chain urokinase , 1988 .
[15] V. Gurewich,et al. Complementary modes of action of tissue-type plasminogen activator and pro-urokinase by which their synergistic effect on clot lysis may be explained. , 1988, The Journal of clinical investigation.
[16] M. Scully,et al. Plasminogen activation by single-chain urokinase in functional isolation. A kinetic study. , 1987, The Journal of biological chemistry.
[17] D. Collen,et al. Coronary arterial thrombolysis with low-dose synergistic combinations of recombinant tissue-type plasminogen activator (rt-PA) and recombinant single-chain urokinase-type plasminogen activator (rscu-PA) for acute myocardial infarction. , 1987, The American journal of cardiology.
[18] V. Gurewich,et al. Activation of plasminogen by single-chain urokinase or by two-chain urokinase--a demonstration that single-chain urokinase has a low catalytic activity (pro-urokinase). , 1987, Blood.
[19] V. Gurewich,et al. A comparative study of the efficacy and specificity of tissue plasminogen activator and pro-urokinase: demonstration of synergism and of different thresholds of non-selectivity. , 1986, Thrombosis research.
[20] M. Verstraete,et al. Synergism of thrombolytic agents in vivo. , 1986, Circulation.
[21] D. Collen,et al. Absence of Synergism Between Tissue-Type Plasminogen Activator (t-PA), Single-Chain UrokinaseType Plasminogen Activator (scu-PA) and Urokinase on Clot Lysis in a Plasma Milieu In Vitro , 1986, Thrombosis and Haemostasis.
[22] V. Gurewich,et al. Pro-urokinase: a study of its stability in plasma and of a mechanism for its selective fibrinolytic effect. , 1986, Blood.
[23] E. Angles-cano,et al. A spectrophotometric solid-phase fibrin-tissue plasminogen activator activity assay (SOFIA-tPA) for high-fibrin-affinity tissue plasminogen activators. , 1986, Analytical biochemistry.
[24] M. Hoylaerts,et al. Activation of plasminogen by pro-urokinase. II. Kinetics. , 1986, The Journal of biological chemistry.
[25] M. Blaber,et al. Activation of plasminogen by pro-urokinase. I. Mechanism. , 1986, The Journal of biological chemistry.
[26] D. Collen,et al. Activation of Plasminogen by Pro-urokinase , 1986 .
[27] D. Collen,et al. A monoclonal antibody specific for Lys-plasminogen. Application to the study of the activation pathways of plasminogen in vivo. , 1985, The Journal of biological chemistry.
[28] W. Nieuwenhuizen,et al. A monoclonal antibody, specific for human fibrinogen, fibrinopeptide A-containing fragments and not reacting with free fibrinopeptide A. , 1985, Blood.
[29] D. Collen,et al. Biological and Thrombolytic Properties of Proenzyme and Active Forms of Human Urokinase – I. Fibrinolytic and Fibrinogenolytic Properties in Human Plasma In Vitro of Urokinases Obtained from Human Urine or by Recombinant DNA Technology , 1984, Thrombosis and Haemostasis.
[30] M. Blaber,et al. Biological and Thrombolytic Properties of Proenzyme and Active Forms of Human Urokinase – III. Thrombolytic Properties of Natural and Recombinant Urokinase in Rabbits with Experimental Jugular Vein Thrombosis , 1984, Thrombosis and Haemostasis.
[31] V. Gurewich,et al. Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase). A study in vitro and in two animal species. , 1984, The Journal of clinical investigation.
[32] S. Thorsen,et al. Initial plasmin-degradation of fibrin as the basis of a positive feed-back mechanism in fibrinolysis. , 1984, European journal of biochemistry.
[33] S. Husain,et al. Purification and partial characterization of a single-chain high-molecular-weight form of urokinase from human urine. , 1983, Archives of biochemistry and biophysics.
[34] W. Schleuning,et al. Isolation and characterization of urokinase from human plasma. , 1982, The Journal of biological chemistry.
[35] K. Robbins,et al. [30] Human plasmin , 1981 .
[36] B. Wiman,et al. Molecular mechanism of physiological fibrinolysis , 1978, Nature.
[37] P. Fraker,et al. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril. , 1978, Biochemical and biophysical research communications.
[38] B. Wiman,et al. Characterization of human plasminogen. II. Separation and partial characterization of different molecular forms of human plasminogen. , 1972, Biochimica et biophysica acta.
[39] D. Deutsch,et al. Plasminogen: Purification from Human Plasma by Affinity Chromatography , 1970, Science.
[40] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.