메뉴 건너뛰기




Volumn 12, Issue 7, 2006, Pages 849-857

Development of new fibrinolytic agents

Author keywords

bat PA; Endothelial cells; Fibrinolysis; Mutant t PA; scu PA; Staphylokinase; t PA; u PA

Indexed keywords

ALTEPLASE; BUTYLOXYCARBONYLSERYLPROLINE HYDROXIDE; DESMOPRESSIN; DESMOTEPLASE; DIPEPTIDE DERIVATIVE; FIBRIN; FIBRINOLYTIC AGENT; LANOTEPLASE; MONOSODIUM [2 (6 HYDROXYNAPHTHALEN 2 YL) 6 METHYLPYRIMIDIN 4 YLOXY]ACETATE DEHYDRATE; MONTEPLASE; N PALMITOYLSERYLPROLINE HYDROXIDE; N STEAROYL DEXTRO SERYLPROLINE HYDROXIDE; N STEAROYLSERYLPROLINE HYDROXIDE; PAMITEPLASE; PLASMINOGEN ACTIVATOR; PROUROKINASE; PYRIMIDINE DERIVATIVE; RETEPLASE; SARUPLASE; SERYLPROLINE; STAPHYLOKINASE; STREPTOKINASE; TENECTEPLASE; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG; UROKINASE; VASOPRESSIN DERIVATIVE;

EID: 33645287745     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161206776056065     Document Type: Review
Times cited : (29)

References (86)
  • 1
    • 0142107201 scopus 로고
    • Yamaguchi T, Mori K, Minematsu K, del Zoppo GJ Eds, Springer-Verlag Tokyo
    • Matsuo O. In: Yamaguchi T, Mori K, Minematsu K, del Zoppo GJ Eds, New thrombolytic agents: Basic development. Springer-Verlag Tokyo 1995; 182-7.
    • (1995) New Thrombolytic Agents: Basic Development , pp. 182-187
    • Matsuo, O.1
  • 2
    • 0018893682 scopus 로고
    • On the regulation and control of fibrinolysis
    • Collen D. On the regulation and control of fibrinolysis. Thromb Haemost 1980; 43: 77-89.
    • (1980) Thromb Haemost , vol.43 , pp. 77-89
    • Collen, D.1
  • 3
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • Collen D, Lijnen HR. Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 1991; 78: 3114-24.
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 4
    • 0017710297 scopus 로고    scopus 로고
    • Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma
    • Wiman B, Collen, D. Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur J Biochem 1997; 78: 19-26.
    • (1997) Eur J Biochem , vol.78 , pp. 19-26
    • Wiman, B.1    Collen, D.2
  • 5
    • 0017102105 scopus 로고
    • Isolation and characterization of α2-plasmin inhibitor from human plasma
    • Moroi M, Aoki N. Isolation and characterization of α2-plasmin inhibitor from human plasma. J Biol Chem 1976; 251: 5956-65.
    • (1976) J Biol Chem , vol.251 , pp. 5956-5965
    • Moroi, M.1    Aoki, N.2
  • 6
    • 0017847923 scopus 로고
    • Molecular mechanism of physiological fibrinolysis
    • Wiman B, Collen D. Molecular mechanism of physiological fibrinolysis. Nature 1987; 272: 549-50.
    • (1987) Nature , vol.272 , pp. 549-550
    • Wiman, B.1    Collen, D.2
  • 7
    • 0020655457 scopus 로고
    • Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli
    • Pennica D, Holmes WE, Kohr WJ, Harkins RN, Vehar GA, Ward CA, et al. Cloning and expression of human tissue-type plasminogen activator cDNA in E. coli. Nature 1984; 301: 214-21.
    • (1984) Nature , vol.301 , pp. 214-221
    • Pennica, D.1    Holmes, W.E.2    Kohr, W.J.3    Harkins, R.N.4    Vehar, G.A.5    Ward, C.A.6
  • 8
    • 0020471109 scopus 로고
    • Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator
    • Rijken DC, Hoylaerts M, Collen D. Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator. J Biol Chem 1982; 257: 2920-5.
    • (1982) J Biol Chem , vol.257 , pp. 2920-2925
    • Rijken, D.C.1    Hoylaerts, M.2    Collen, D.3
  • 9
    • 0019862683 scopus 로고
    • Thrombolysis by human tissue plasminogen activator and urokinase in rabbits with experimental pulmonary embolus
    • Matsuo O, Rijken DC, Cullen D. Thrombolysis by human tissue plasminogen activator and urokinase in rabbits with experimental pulmonary embolus. Nature 1981; 291: 590-1.
    • (1981) Nature , vol.291 , pp. 590-591
    • Matsuo, O.1    Rijken, D.C.2    Cullen, D.3
  • 10
    • 0022974681 scopus 로고
    • On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid
    • van Zonneveld AJ, Veerman H, Pannekoek H. On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Inhibition of kringle-2 binding to fibrin by epsilon-amino caproic acid. J Biol Chem 1986; 261: 14214-8.
    • (1986) J Biol Chem , vol.261 , pp. 14214-14218
    • van Zonneveld, A.J.1    Veerman, H.2    Pannekoek, H.3
  • 11
    • 0019987224 scopus 로고
    • Studies on the kinetics of plasminogen activation by tissue plasminogen activator
    • Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochim Biophys Acts. 1982; 704: 461-9.
    • (1982) Biochim Biophys Acts , vol.704 , pp. 461-469
    • Ranby, M.1
  • 12
    • 0025605398 scopus 로고
    • Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis
    • Weening-Verhoeff EJ, Quax PH, van Leeuwen RT, Rehberg EF, Marotti KR, Verheijen JH. Involvement of aspartic and glutamic residues in kringle-2 of tissue-type plasminogen activator in lysine binding, fibrin binding and stimulation of activity as revealed by chemical modification and oligonucleotide-directed mutagenesis. Protein Eng 1990; 4: 191-8.
    • (1990) Protein Eng , vol.4 , pp. 191-198
    • Weening-Verhoeff, E.J.1    Quax, P.H.2    van Leeuwen, R.T.3    Rehberg, E.F.4    Marotti, K.R.5    Verheijen, J.H.6
  • 13
    • 0023866371 scopus 로고
    • Isolation and characterization of three different carbohydrate chains from melanoma tissue plasminogen activator
    • Pohl G, Kenne L, Nilsson B, Einarsson M. Isolation and characterization of three different carbohydrate chains from melanoma tissue plasminogen activator. Eur J Biochem 1987; 170: 69-75.
    • (1987) Eur J Biochem , vol.170 , pp. 69-75
    • Pohl, G.1    Kenne, L.2    Nilsson, B.3    Einarsson, M.4
  • 14
    • 0034725801 scopus 로고    scopus 로고
    • Third-generation thrombolytic drugs
    • Verstraete M. Third-generation thrombolytic drugs. Am J Med 2000; 109: 52-8.
    • (2000) Am J Med , vol.109 , pp. 52-58
    • Verstraete, M.1
  • 15
    • 0027095723 scopus 로고
    • Reversible interactions between plasminogen activators and plasminogen activator inhibitor-1
    • Mimuro J, Kaneko M, Murakami T, Matsuda M, Sakata Y. Reversible interactions between plasminogen activators and plasminogen activator inhibitor-1. Biochim Biophys Acta 1992; 1160: 325-34.
    • (1992) Biochim Biophys Acta , vol.1160 , pp. 325-334
    • Mimuro, J.1    Kaneko, M.2    Murakami, T.3    Matsuda, M.4    Sakata, Y.5
  • 16
    • 0025731989 scopus 로고
    • High resolution analysis of functional determinants on human tissue-type plasminogen activator
    • Bennett WF, Paoni NF, Keyt BA, Botstein D, Jones AJ, Presta L, et al. High resolution analysis of functional determinants on human tissue-type plasminogen activator. J Biol Chem 1991; 266: 5191-201.
    • (1991) J Biol Chem , vol.266 , pp. 5191-5201
    • Bennett, W.F.1    Paoni, N.F.2    Keyt, B.A.3    Botstein, D.4    Jones, A.J.5    Presta, L.6
  • 17
    • 0027223892 scopus 로고
    • A slow clearing, fibrin-specific, PAI-1 resistant variant of t-PA (T103N, KHRR 296-299 AAAA)
    • Paoni NF, Keyt BA, Refino CJ, Chow AM, Nguyen HV, Berleau LT, et al. A slow clearing, fibrin-specific, PAI-1 resistant variant of t-PA (T103N, KHRR 296-299 AAAA). Thromb Haemost 1993; 70: 307-12.
    • (1993) Thromb Haemost , vol.70 , pp. 307-312
    • Paoni, N.F.1    Keyt, B.A.2    Refino, C.J.3    Chow, A.M.4    Nguyen, H.V.5    Berleau, L.T.6
  • 18
    • 0027240597 scopus 로고
    • An international randomized trial comparing four thrombolytic strategies for acute myocardial infarction
    • The GUSTO investigators
    • The GUSTO investigators. An international randomized trial comparing four thrombolytic strategies for acute myocardial infarction. N Engl J Med 1993; 329: 673-82.
    • (1993) N Engl J Med , vol.329 , pp. 673-682
  • 19
    • 0022578098 scopus 로고
    • Activation of plasminogen by pro-urokinase. II. Kinetics
    • Collen D, Zamarron C, Lijnen HR, Hoylaerts M. Activation of plasminogen by pro-urokinase. II. Kinetics. J Biol Chem 1986; 261: 1259-66.
    • (1986) J Biol Chem , vol.261 , pp. 1259-1266
    • Collen, D.1    Zamarron, C.2    Lijnen, H.R.3    Hoylaerts, M.4
  • 20
    • 0022387786 scopus 로고
    • Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin
    • Kasai S, Arimura H, Nishida M, Suyama T. Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin. J Biol Chem 1985; 260: 12377-81.
    • (1985) J Biol Chem , vol.260 , pp. 12377-12381
    • Kasai, S.1    Arimura, H.2    Nishida, M.3    Suyama, T.4
  • 21
    • 0025810460 scopus 로고
    • Half-life of single-chain urokinase-type plasminogen activator (scu-PA) and two-chain urokinase-type plasminogen activator (teu-PA) in patients with acute myocardial infarction
    • Kohler M, Sen S, Miyashita C, Hermes R, Pindur G, Heiden M, et al. Half-life of single-chain urokinase-type plasminogen activator (scu-PA) and two-chain urokinase-type plasminogen activator (teu-PA) in patients with acute myocardial infarction. Thromb Res 1991; 62: 75-81.
    • (1991) Thromb Res , vol.62 , pp. 75-81
    • Kohler, M.1    Sen, S.2    Miyashita, C.3    Hermes, R.4    Pindur, G.5    Heiden, M.6
  • 22
    • 84919587044 scopus 로고
    • Randomised double-blind trial of recombinant pro-urokinase against streptokinase in acute myocardial infarction
    • PRIMI Trial Study Group
    • PRIMI Trial Study Group. Randomised double-blind trial of recombinant pro-urokinase against streptokinase in acute myocardial infarction. Lancet 1989; 1: 863-8.
    • (1989) Lancet , vol.1 , pp. 863-868
  • 23
    • 0032032528 scopus 로고    scopus 로고
    • Randomized, double-blind study comparing saruplase with streptokinase therapy in acute myocardial infarction: The COMPASS Equivalence Trial. Comparison Trial of Saruplase and Streptokinase (COMASS) Investigators
    • Tebbe U, Michels R, Adgey J, Boland J, Caspi A, Charbonnier B, et al. Randomized, double-blind study comparing saruplase with streptokinase therapy in acute myocardial infarction: the COMPASS Equivalence Trial. Comparison Trial of Saruplase and Streptokinase (COMASS) Investigators. J Am Coll Cardiol 1998; 31: 487-93.
    • (1998) J Am Coll Cardiol , vol.31 , pp. 487-493
    • Tebbe, U.1    Michels, R.2    Adgey, J.3    Boland, J.4    Caspi, A.5    Charbonnier, B.6
  • 24
    • 0030980996 scopus 로고    scopus 로고
    • Comparison of saruplase and alteplase in acute myocardial infarction. SESAM Study Group. The Study in Europe with Saruplase and Alteplase in Myocardial Infarction
    • Bar FW, Meyer J, Vermeer F, Michels R, Charbonnier B, Haerten K, et al. Comparison of saruplase and alteplase in acute myocardial infarction. SESAM Study Group. The Study in Europe with Saruplase and Alteplase in Myocardial Infarction. Am J Cardiol 1997; 79: 727-32.
    • (1997) Am J Cardiol , vol.79 , pp. 727-732
    • Bar, F.W.1    Meyer, J.2    Vermeer, F.3    Michels, R.4    Charbonnier, B.5    Haerten, K.6
  • 25
    • 0344069499 scopus 로고    scopus 로고
    • Saruplase is a safe and effective thrombolytic agent; observations in 1, 698 patients: Results of the PASS study. Practical Applications of Saruplase Study
    • Vermeer F, Bosl I, Meyer J, Bar F, Charbonnier B, Windeler J, et al. Saruplase is a safe and effective thrombolytic agent; observations in 1, 698 patients: results of the PASS study. Practical Applications of Saruplase Study. J Thromb Thrombolysis 1999; 8: 143-50.
    • (1999) J Thromb Thrombolysis , vol.8 , pp. 143-150
    • Vermeer, F.1    Bosl, I.2    Meyer, J.3    Bar, F.4    Charbonnier, B.5    Windeler, J.6
  • 26
    • 0025735319 scopus 로고
    • Thrombolytic properties of a novel modified human tissue-type plasminogen activator (E6010): A bolus injection of E6010 has equivalent potency of lysing young and aged canine coronary thrombi
    • Suzuki S, Saito M, Suzuki N, Kato H, Nagaoka N, Yoshitake S, et al. Thrombolytic properties of a novel modified human tissue-type plasminogen activator (E6010): a bolus injection of E6010 has equivalent potency of lysing young and aged canine coronary thrombi. J Cardiovasc Pharmacol 1991; 17: 738-46.
    • (1991) J Cardiovasc Pharmacol , vol.17 , pp. 738-746
    • Suzuki, S.1    Saito, M.2    Suzuki, N.3    Kato, H.4    Nagaoka, N.5    Yoshitake, S.6
  • 27
    • 0342989036 scopus 로고
    • Coronary thrombolysis in acute myocardial infarction of E6010 (Novel modified t-PA): A multicenter, doubleblind, does-finding study
    • Kawai C, Hosoda S, Kimata S, Kanmatsuse K, Suzuki S, Motomiya T, et al. Coronary thrombolysis in acute myocardial infarction of E6010 (Novel modified t-PA): a multicenter, doubleblind, does-finding study. Jpn Pharmacol Ther 1994; 22: 3925-50.
    • (1994) Jpn Pharmacol Ther , vol.22 , pp. 3925-3950
    • Kawai, C.1    Hosoda, S.2    Kimata, S.3    Kanmatsuse, K.4    Suzuki, S.5    Motomiya, T.6
  • 28
    • 0030970592 scopus 로고    scopus 로고
    • A prospective, randomized, double-blind multicenter trial ofa single bolus injection of the novel modified t-PA E6010 in the treatment of acute myocardial infarction: Comparison with native t-PA. E6010 Study Group
    • Kawai C, Yui Y, Hosoda S, Nobuyoshi M, Suzuki S, Sato H, Takatsu F, et al. A prospective, randomized, double-blind multicenter trial ofa single bolus injection of the novel modified t-PA E6010 in the treatment of acute myocardial infarction: comparison with native t-PA. E6010 Study Group. J Am Coll Cardiol 1997; 29: 1447-53.
    • (1997) J Am Coll Cardiol , vol.29 , pp. 1447-1453
    • Kawai, C.1    Yui, Y.2    Hosoda, S.3    Nobuyoshi, M.4    Suzuki, S.5    Sato, H.6    Takatsu, F.7
  • 29
    • 0036782275 scopus 로고    scopus 로고
    • A new thrombolytic agent, monteplase, is independent of the plasminogen activator inhibitor in patients with acute myocardial infarction: Initial results of the Combining Monteplase with Angioplasty (COMA) trial
    • Inoue T, Yaguchi I, Takayanagi K, Hayashi T, Morooka S, Eguchi Y. A new thrombolytic agent, monteplase, is independent of the plasminogen activator inhibitor in patients with acute myocardial infarction: initial results of the Combining Monteplase with Angioplasty (COMA) trial. Am Heart J 2002; 144: 673 (135).
    • (2002) Am Heart J , vol.144 , Issue.E5 , pp. 673
    • Inoue, T.1    Yaguchi, I.2    Takayanagi, K.3    Hayashi, T.4    Morooka, S.5    Eguchi, Y.6
  • 30
    • 0030913788 scopus 로고    scopus 로고
    • Single and repeated intravenous toxicity studies of pamite-plase (genetical recombination) in rats and monkeys
    • Ishikawa A, Ohata T, Imamura K, Iwasaki M, Sakai T, Matsuzawa T, et al. Single and repeated intravenous toxicity studies of pamite-plase (genetical recombination) in rats and monkeys. J Toxicol Sci 1997; 22: 117-33.
    • (1997) J Toxicol Sci , vol.22 , pp. 117-133
    • Ishikawa, A.1    Ohata, T.2    Imamura, K.3    Iwasaki, M.4    Sakai, T.5    Matsuzawa, T.6
  • 31
    • 0027427576 scopus 로고
    • Thrombolytic activity of a novel modified tissue-type plasminogen activator, YM866, in a canine model of coronary artery thrombosis
    • Kawasaki T, Katoh M, Kaku S, Gushima H, Takenaka T, Yui Y, et al. Thrombolytic activity of a novel modified tissue-type plasminogen activator, YM866, in a canine model of coronary artery thrombosis. Jpn J Pharmacol 1993; 63: 9-16.
    • (1993) Jpn J Pharmacol , vol.63 , pp. 9-16
    • Kawasaki, T.1    Katoh, M.2    Kaku, S.3    Gushima, H.4    Takenaka, T.5    Yui, Y.6
  • 33
    • 0006074366 scopus 로고    scopus 로고
    • Randomized, double-blind multicenter trial of YM866 (modified t-PA) by intravenous bolus injection in patients with acute myocardial infarction in comparison with tisokinase (native t-PA)
    • Yui Y, Kawai C, Hosoda S, Aoki N, Takano T, Kimmatsuse Y, et al. Randomized, double-blind multicenter trial of YM866 (modified t-PA) by intravenous bolus injection in patients with acute myocardial infarction in comparison with tisokinase (native t-PA). J New Remedies Clin 1996; 45: 2175-2210.
    • (1996) J New Remedies Clin , vol.45 , pp. 2175-2210
    • Yui, Y.1    Kawai, C.2    Hosoda, S.3    Aoki, N.4    Takano, T.5    Kimmatsuse, Y.6
  • 34
    • 0026575312 scopus 로고
    • Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022
    • Kohnert U, Rudolph R, Verheijen JH, Weening-Verhoeff EJ, Stern A, et al. Biochemical properties of the kringle 2 and protease domains are maintained in the refolded t-PA deletion variant BM 06.022. Protein Eng 1992; 5: 93-100.
    • (1992) Protein Eng , vol.5 , pp. 93-100
    • Kohnert, U.1    Rudolph, R.2    Verheijen, J.H.3    Weening-Verhoeff, E.J.4    Stern, A.5
  • 36
    • 0026012337 scopus 로고
    • Pharmacokinetic and hemostatic properties of the recombinant plasminogen activator but 06.022 in healthy volunteers
    • Martin U, von Mollendorff E, Akpan W, Kientsch-Engel R, Kaufmann B, Neugebauer G. Pharmacokinetic and hemostatic properties of the recombinant plasminogen activator but 06.022 in healthy volunteers. Thromb Haemost 1991; 66: 569-74.
    • (1991) Thromb Haemost , vol.66 , pp. 569-574
    • Martin, U.1    von Mollendorff, E.2    Akpan, W.3    Kientsch-Engel, R.4    Kaufmann, B.5    Neugebauer, G.6
  • 37
    • 0029066701 scopus 로고
    • More rapid, complete, and stable coronary thrombolysis with bolus administration of reteplase compared with alteplase infusion in acute myocardial infarction. RAPID Investigators
    • Smalling RW, Bode C, Kalbfleisch J, Sen S, Limbourg P, Forycki F, et al. More rapid, complete, and stable coronary thrombolysis with bolus administration of reteplase compared with alteplase infusion in acute myocardial infarction. RAPID Investigators. Circulation 1995; 91: 2725-32.
    • (1995) Circulation , vol.91 , pp. 2725-2732
    • Smalling, R.W.1    Bode, C.2    Kalbfleisch, J.3    Sen, S.4    Limbourg, P.5    Forycki, F.6
  • 38
    • 0343849937 scopus 로고    scopus 로고
    • Randomized comparison of coronary thrombolysis achieved with double-bolus reteplase (recombinant plasminogen activator) and front-loaded, accelerated alteplase (recombinant tissue plasminogen activator) in patients with acute myocardial infarction. The RAPID II Investigators
    • Bode C, Smalling RW, Berg G, Burnett C, Lorch G, Kalbfleisch JM, et al. Randomized comparison of coronary thrombolysis achieved with double-bolus reteplase (recombinant plasminogen activator) and front-loaded, accelerated alteplase (recombinant tissue plasminogen activator) in patients with acute myocardial infarction. The RAPID II Investigators. Circulation 1996; 94: 891-8.
    • (1996) Circulation , vol.94 , pp. 891-898
    • Bode, C.1    Smalling, R.W.2    Berg, G.3    Burnett, C.4    Lorch, G.5    Kalbfleisch, J.M.6
  • 39
    • 0029142436 scopus 로고
    • Randomised, double-blind comparison of reteplase double-bolus administration with streptokinase in acute myocardial infarction (INJECT): Trial to investigate equivalence
    • International Joint Efficacy Comparison of Thrombolytics
    • International Joint Efficacy Comparison of Thrombolytics. Randomised, double-blind comparison of reteplase double-bolus administration with streptokinase in acute myocardial infarction (INJECT): trial to investigate equivalence. Lancet 1995; 346: 329-36.
    • (1995) Lancet , vol.346 , pp. 329-336
  • 40
    • 0030879325 scopus 로고    scopus 로고
    • A comparison of reteplase with alteplase for acute myocardial infarction
    • The Global Use of Strategies to Open Occluded Coronary Arteries (GUSTO III) Investigators
    • The Global Use of Strategies to Open Occluded Coronary Arteries (GUSTO III) Investigators. A comparison of reteplase with alteplase for acute myocardial infarction. N Engl J Med 1997; 337: 1118-23.
    • (1997) N Engl J Med , vol.337 , pp. 1118-1123
  • 42
    • 0032910324 scopus 로고    scopus 로고
    • Safety assessment of single-bolus administration of TNK tissue-plasminogen activator in acute myocardial infarction: The ASSENT-1 trial. The ASSENT-1 Investigators
    • Van de Werf F, Cannon CP, Luyten A, Houbracken K, McCabe CH, Berioli S, et al. Safety assessment of single-bolus administration of TNK tissue-plasminogen activator in acute myocardial infarction: the ASSENT-1 trial. The ASSENT-1 Investigators. Am Heart J 1999; 137: 786-91.
    • (1999) Am Heart J , vol.137 , pp. 786-791
    • Van de Werf, F.1    Cannon, C.P.2    Luyten, A.3    Houbracken, K.4    McCabe, C.H.5    Berioli, S.6
  • 43
    • 0032578970 scopus 로고    scopus 로고
    • TNK-tissue plasminogen activator compared with front-loaded alteplase in acute myocardial infarction: Results of the TIMI 1OB trial. Thrombolysis in Myocardial Infarction (TIMI) 1OB Investigators
    • Cannon CP, Gibson CM, McCabe CH, Adgey AA, Schweiger MJ, Sequeira RF, et al. TNK-tissue plasminogen activator compared with front-loaded alteplase in acute myocardial infarction: results of the TIMI 1OB trial. Thrombolysis in Myocardial Infarction (TIMI) 1OB Investigators. Circulation 1998; 98: 2805-14.
    • (1998) Circulation , vol.98 , pp. 2805-2814
    • Cannon, C.P.1    Gibson, C.M.2    McCabe, C.H.3    Adgey, A.A.4    Schweiger, M.J.5    Sequeira, R.F.6
  • 44
    • 0033612881 scopus 로고    scopus 로고
    • Single-bolus tenecteplase compared with front-loaded alteplase in acute myocardial infarction: The ASSENT-2 double-blind randomised trial
    • Assessment of the Safety and Efficacy of a New Thrombolytic Investigators
    • Assessment of the Safety and Efficacy of a New Thrombolytic Investigators. Single-bolus tenecteplase compared with front-loaded alteplase in acute myocardial infarction: the ASSENT-2 double-blind randomised trial. Lancet 1999; 354: 716-22.
    • (1999) Lancet , vol.354 , pp. 716-722
  • 45
    • 0024391283 scopus 로고
    • Pharmacokinetic and distribution analysis of variant forms of tissue-type plasminogen activator with prolonged clearance in rat
    • Larsen GR, Metzger M, Henson K, Blue Y, Horgan P. Pharmacokinetic and distribution analysis of variant forms of tissue-type plasminogen activator with prolonged clearance in rat. Blood 1989; 73: 1842-50.
    • (1989) Blood , vol.73 , pp. 1842-1850
    • Larsen, G.R.1    Metzger, M.2    Henson, K.3    Blue, Y.4    Horgan, P.5
  • 46
    • 0032542048 scopus 로고    scopus 로고
    • Evaluation of a weight-adjusted single-bolus plasminogen activator in patients with myocardial infarction: A double-blind, randomized angiographic trial of lanoteplase versus alteplase
    • den Heijer P, Vermeer F, Ambrosioni E, Sadowski Z, Lopez-Sendon JL, von Essen R, et al. Evaluation of a weight-adjusted single-bolus plasminogen activator in patients with myocardial infarction: a double-blind, randomized angiographic trial of lanoteplase versus alteplase. Circulation 1998; 98: 2117-25.
    • (1998) Circulation , vol.98 , pp. 2117-2125
    • den Heijer, P.1    Vermeer, F.2    Ambrosioni, E.3    Sadowski, Z.4    Lopez-Sendon, J.L.5    von Essen, R.6
  • 47
    • 0034543078 scopus 로고    scopus 로고
    • Intravenous NPA for the treatment of infarcting myocardium early; InTIME-II, a double-blind comparison of single-bolus lanoteplase vs accelerated alteplase for the treatment of patients with acute myocardial infarction
    • InTIME-II Investigators
    • InTIME-II Investigators. Intravenous NPA for the treatment of infarcting myocardium early; InTIME-II, a double-blind comparison of single-bolus lanoteplase vs accelerated alteplase for the treatment of patients with acute myocardial infarction. Eur Heart J 2000; 21: 2005-13.
    • (2000) Eur Heart J , vol.21 , pp. 2005-2013
  • 48
    • 0026808895 scopus 로고
    • Isolation and characterization of natural and recombinant staphylokinase
    • Collen D, Silence K, Demarsin E, De Mo M, Lijnen HR., Isolation and characterization of natural and recombinant staphylokinase. Fibrinolysis 1992; 6: 203-13.
    • (1992) Fibrinolysis , vol.6 , pp. 203-213
    • Collen, D.1    Silence, K.2    Demarsin, E.3    De Mo, M.4    Lijnen, H.R.5
  • 49
    • 0021856403 scopus 로고
    • Overproduction of staphylokinase in Escherichia coli and its characterization
    • Sako, T. Overproduction of staphylokinase in Escherichia coli and its characterization. Eur J Biochem 1985; 149: 557-563.
    • (1985) Eur J Biochem , vol.149 , pp. 557-563
    • Sako, T.1
  • 50
    • 0023806696 scopus 로고
    • Purification and characterization of the bacterial plasminogen activator staphylokinase, secreted by a recombinant bacillus subtilis
    • Gerlach D, Kraft R, Behnke D. Purification and characterization of the bacterial plasminogen activator staphylokinase, secreted by a recombinant bacillus subtilis. Zbl Bakt Mikr Hyg 1988; 269: 314-22.
    • (1988) Zbl Bakt Mikr Hyg , vol.269 , pp. 314-322
    • Gerlach, D.1    Kraft, R.2    Behnke, D.3
  • 51
    • 0027325808 scopus 로고
    • Molecular conversions of recombinant staphylokinase during plasminogen activation in purified systems and in human plasma
    • Ueshima S, Silence K, Collen D, Lijnen HR. Molecular conversions of recombinant staphylokinase during plasminogen activation in purified systems and in human plasma. Thromb Haemost 1993; 70: 495-9.
    • (1993) Thromb Haemost , vol.70 , pp. 495-499
    • Ueshima, S.1    Silence, K.2    Collen, D.3    Lijnen, H.R.4
  • 52
  • 53
    • 0015213796 scopus 로고
    • The mechanism of activation of human plasminogen by streptokinase
    • McClintock DK, Bell PH. The mechanism of activation of human plasminogen by streptokinase. Biochem Biophys Res Commun 1971; 43: 694-702.
    • (1971) Biochem Biophys Res Commun , vol.43 , pp. 694-702
    • McClintock, D.K.1    Bell, P.H.2
  • 54
    • 0024382950 scopus 로고
    • Mechanism of fibrin-specific fibrinolysis by staphylokinase: Participation of α2-plasmin inhibitor
    • Sakai M, Watanuki M Matsuo O. Mechanism of fibrin-specific fibrinolysis by staphylokinase: participation of α2-plasmin inhibitor. Biochem Biophys Res Commun 1989; 162: 830-7.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 830-837
    • Sakai, M.1    Watanuki, M.2    Matsuo, O.3
  • 55
    • 0026585355 scopus 로고
    • On the molecular interactions between plasminogen-staphylokinase, α2-antiplasmin and fibrin
    • Lijnen HR, Van Hoef B, Matsuo O, Collen D. On the molecular interactions between plasminogen-staphylokinase, α2-antiplasmin and fibrin. Biochim Biophys Acta 1992; 1118: 144-8.
    • (1992) Biochim Biophys Acta , vol.1118 , pp. 144-148
    • Lijnen, H.R.1    Van Hoef, B.2    Matsuo, O.3    Collen, D.4
  • 56
    • 0027945294 scopus 로고
    • Kinetic analysis of plasminogen activation by staphylokinase/plasminogen complex in the presence of fibrin
    • Okada K, Yuasa H, Hagiya Y, Fukao H, Ueshima S, Matsuo O. Kinetic analysis of plasminogen activation by staphylokinase/plasminogen complex in the presence of fibrin. Thromb Res 1994; 76: 181-91.
    • (1994) Thromb Res , vol.76 , pp. 181-191
    • Okada, K.1    Yuasa, H.2    Hagiya, Y.3    Fukao, H.4    Ueshima, S.5    Matsuo, O.6
  • 57
    • 0028151219 scopus 로고
    • Effects of α2-plasmin inhibitor on plasminogen activation by staphylokinase/plasminogen complex
    • Okada K, Nonaka T, Matsumoto H, Fukao H, Ueshima S, Matsuo O. Effects of α2-plasmin inhibitor on plasminogen activation by staphylokinase/ plasminogen complex. Thromb Res 1994; 76: 211-20.
    • (1994) Thromb Res , vol.76 , pp. 211-220
    • Okada, K.1    Nonaka, T.2    Matsumoto, H.3    Fukao, H.4    Ueshima, S.5    Matsuo, O.6
  • 58
    • 0025949188 scopus 로고
    • On the mechanism of fibrin-specific plasminogen activation by staphylokinase
    • Lijnen HR, Van Hoef B, De Cock F, Okada K, Ueshima S, Matsuo O, et al. On the mechanism of fibrin-specific plasminogen activation by staphylokinase. J Biol Chem 1991; 266: 11826-32.
    • (1991) J Biol Chem , vol.266 , pp. 11826-11832
    • Lijnen, H.R.1    Van Hoef, B.2    De Cock, F.3    Okada, K.4    Ueshima, S.5    Matsuo, O.6
  • 59
    • 0029661824 scopus 로고    scopus 로고
    • Effects of fibrin and α2-antiplasmin an plasminogen activation by staphylokinase
    • Okada K, Ueshima S, Takaishi T, Yuasa H, Fukao H, Matauo O. Effects of fibrin and α2-antiplasmin an plasminogen activation by staphylokinase. Am J Hemat 1996; 53: 151-7.
    • (1996) Am J Hemat , vol.53 , pp. 151-157
    • Okada, K.1    Ueshima, S.2    Takaishi, T.3    Yuasa, H.4    Fukao, H.5    Matauo, O.6
  • 62
    • 0029583136 scopus 로고
    • Identification of urokinase-type plasminogen activator receptor in human endothelial cells and its modulation by phorbol myristate acetate
    • Matsumoto H, Ueshima S, Fukao H, Mitsui Y, Matsuo O. Identification of urokinase-type plasminogen activator receptor in human endothelial cells and its modulation by phorbol myristate acetate. Cell Struct Func 1995; 20: 429-37.
    • (1995) Cell Struct Func , vol.20 , pp. 429-437
    • Matsumoto, H.1    Ueshima, S.2    Fukao, H.3    Mitsui, Y.4    Matsuo, O.5
  • 63
    • 0025741431 scopus 로고
    • Comparative fibrinolytic properties of staphylokinase and streptokinase in animal models of venous thrombosis
    • Lijnen HR, Stassen JM, Vanlinthout I, Fukao H, Okada K, Matsuo O, et al. Comparative fibrinolytic properties of staphylokinase and streptokinase in animal models of venous thrombosis. Thromb Haemost 1991; 66: 468-73.
    • (1991) Thromb Haemost , vol.66 , pp. 468-473
    • Lijnen, H.R.1    Stassen, J.M.2    Vanlinthout, I.3    Fukao, H.4    Okada, K.5    Matsuo, O.6
  • 65
    • 0027502707 scopus 로고
    • Comparative immunogenicity and thrombolytic properties toward arterial and venous thrombi of staphylokinase and streptokinase in baboons
    • Collen D, De Cock F, Stassen JM. Comparative immunogenicity and thrombolytic properties toward arterial and venous thrombi of staphylokinase and streptokinase in baboons. Circulation 1993; 87: 996-1006.
    • (1993) Circulation , vol.87 , pp. 996-1006
    • Collen, D.1    De Cock, F.2    Stassen, J.M.3
  • 67
    • 0028829271 scopus 로고
    • For the STAR Trial Group. A randomized trial of recombinant staphylokinase versus alteplase for coronary artery patency in acute myocardial infarction
    • Vanderschueren S, Barrions L, Kerinchai P, Van den Heuvel P, Hermans L, Vrolix M, et al. for the STAR Trial Group. A randomized trial of recombinant staphylokinase versus alteplase for coronary artery patency in acute myocardial infarction. Circulation 1995; 92: 2044-9.
    • (1995) Circulation , vol.92 , pp. 2044-2049
    • Vanderschueren, S.1    Barrions, L.2    Kerinchai, P.3    Van den Heuvel, P.4    Hermans, L.5    Vrolix, M.6
  • 69
    • 0034633820 scopus 로고    scopus 로고
    • Polyethylene glycol-derivatized cysteine-substitution variants of recombinant staphylokinase for single-bolus treatment of acute myocardial infarction
    • Collen D, Sinnaeve P, Demarsin E, Moreau H, De Maeyer M, Jespers L, et al. Polyethylene glycol-derivatized cysteine-substitution variants of recombinant staphylokinase for single-bolus treatment of acute myocardial infarction. Circulation 2000; 102: 1766-72.
    • (2000) Circulation , vol.102 , pp. 1766-1772
    • Collen, D.1    Sinnaeve, P.2    Demarsin, E.3    Moreau, H.4    De Maeyer, M.5    Jespers, L.6
  • 70
    • 0345283158 scopus 로고    scopus 로고
    • Clinical development of PEGylated recombinant staphylokinase (PEG-Sak) for bolus thrombolytic treatment of patients with acute myocardial infarction
    • Moreadith RW, Collen D. Clinical development of PEGylated recombinant staphylokinase (PEG-Sak) for bolus thrombolytic treatment of patients with acute myocardial infarction. Adv Drug Deliv Rev 2003; 55: 1337-45.
    • (2003) Adv Drug Deliv Rev , vol.55 , pp. 1337-1345
    • Moreadith, R.W.1    Collen, D.2
  • 71
    • 0026077159 scopus 로고
    • The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: Cloning and expression
    • Kratzschmar J, Haendler B, Langer G, Boidol W, Bringmann P, Alagon A, et al. The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: cloning and expression. Gene 1991; 105: 229-37.
    • (1991) Gene , vol.105 , pp. 229-237
    • Kratzschmar, J.1    Haendler, B.2    Langer, G.3    Boidol, W.4    Bringmann, P.5    Alagon, A.6
  • 72
    • 0028791659 scopus 로고
    • Structural features mediating fibrin selectivity of vampire bat plasminogen activators
    • Bringmann P, Gruber D, Liese A, Toschi L, Kratzchmar J, Schleuning WD, et al. Structural features mediating fibrin selectivity of vampire bat plasminogen activators. J Biol Chem 1995; 270: 25596-603.
    • (1995) J Biol Chem , vol.270 , pp. 25596-25603
    • Bringmann, P.1    Gruber, D.2    Liese, A.3    Toschi, L.4    Kratzchmar, J.5    Schleuning, W.D.6
  • 73
    • 0032519630 scopus 로고    scopus 로고
    • Fibrin selectivity of the isolated protease domains of tissue-type and vampire bat salivary gland plasminogen activators
    • Toschi L, Bringmann P, Petri T, Donner P, Schleuning WD. Fibrin selectivity of the isolated protease domains of tissue-type and vampire bat salivary gland plasminogen activators. Eur J Biochem 1998; 252: 108-12.
    • (1998) Eur J Biochem , vol.252 , pp. 108-112
    • Toschi, L.1    Bringmann, P.2    Petri, T.3    Donner, P.4    Schleuning, W.D.5
  • 74
    • 0026576384 scopus 로고
    • Vampire bat salivary plasminogen activator promotes rapid and sustained reperfusion without concomitant systemic plasminogen activation in a canine model of arterial thrombosis
    • Mellott MJ, Stabilito H, Holahan MA, Cuca GC, Wang S, Li P, et al. Vampire bat salivary plasminogen activator promotes rapid and sustained reperfusion without concomitant systemic plasminogen activation in a canine model of arterial thrombosis. Arterioscler Thromb 1992; 12: 212-21.
    • (1992) Arterioscler Thromb , vol.12 , pp. 212-221
    • Mellott, M.J.1    Stabilito, H.2    Holahan, M.A.3    Cuca, G.C.4    Wang, S.5    Li, P.6
  • 75
    • 0037321482 scopus 로고    scopus 로고
    • Vampire bat salivary plasminogen activator (desmoteplase): A unique fibrinolytic enzyme that does not promote neurodegeneration
    • Liberatore GT, Samson A, Bladin C, Schleuning WD, Medcalf RL. Vampire bat salivary plasminogen activator (desmoteplase): a unique fibrinolytic enzyme that does not promote neurodegeneration. Stroke 2003; 34: 537-43.
    • (2003) Stroke , vol.34 , pp. 537-543
    • Liberatore, G.T.1    Samson, A.2    Bladin, C.3    Schleuning, W.D.4    Medcalf, R.L.5
  • 76
    • 0015745534 scopus 로고
    • A new vasopressin analogue and fibrinolysis
    • Grader AMA, da Costa J, Cash JD. A new vasopressin analogue and fibrinolysis. Lancet 1973; 2: 1417-8.
    • (1973) Lancet , vol.2 , pp. 1417-1418
    • Grader, A.M.A.1    da Costa, J.2    Cash, J.D.3
  • 78
    • 0037093220 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator (t-PA) is stored in Weibel-Palade bodies in human endothelial cells both in vitro and in vivo
    • Huber D, Cramer EM, Kaufmann JE, Meda P, Masse J-M, Kruithof EKO, et al. Tissue-type plasminogen activator (t-PA) is stored in Weibel-Palade bodies in human endothelial cells both in vitro and in vivo. Blood 2002; 99: 3637-45.
    • (2002) Blood , vol.99 , pp. 3637-3645
    • Huber, D.1    Cramer, E.M.2    Kaufmann, J.E.3    Meda, P.4    Masse, J.-M.5    Kruithof, E.K.O.6
  • 79
    • 0029061442 scopus 로고
    • Plasminogen activator inhibitor type-1 determines plasmin formation in patients with ischaemic heart disease
    • Pedersen OD, Gram J, Jespersen J. Plasminogen activator inhibitor type-1 determines plasmin formation in patients with ischaemic heart disease. Thromb Haemost 1995; 73: 835-40.
    • (1995) Thromb Haemost , vol.73 , pp. 835-840
    • Pedersen, O.D.1    Gram, J.2    Jespersen, J.3
  • 81
    • 0023757497 scopus 로고
    • Desmopressin: A nontransfusional form of treatment for congenital and acquired bleeding disorders
    • Mannucci PM. Desmopressin: a nontransfusional form of treatment for congenital and acquired bleeding disorders. Blood 1988; 72: 1449-55.
    • (1988) Blood , vol.72 , pp. 1449-1455
    • Mannucci, P.M.1
  • 82
    • 0028004596 scopus 로고
    • Synthetic dipeptide, N-Stearoyl-D-Ser-L-Pro-OEt, induces release of tissue-type plasminogen activator in cultured cells and in experimental animals
    • Okayama T, Nakano M, Odake S, Hagiwara M, Morikawa T, Ueshima S, et al. Synthetic dipeptide, N-Stearoyl-D-Ser-L-Pro-OEt, induces release of tissue-type plasminogen activator in cultured cells and in experimental animals. Chem Pharm Bull 1994; 42: 1854-8.
    • (1994) Chem Pharm Bull , vol.42 , pp. 1854-1858
    • Okayama, T.1    Nakano, M.2    Odake, S.3    Hagiwara, M.4    Morikawa, T.5    Ueshima, S.6
  • 83
    • 0036282649 scopus 로고    scopus 로고
    • Function of tissue-type plasminogen activator releaser on vascular endothelial cells and thrombosis in vivo
    • Ueshima S, Matsuno H, Hayashi M, Horibuchi K, Okada K, Fukao H, et al. Function of tissue-type plasminogen activator releaser on vascular endothelial cells and thrombosis in vivo. Thromb Haemost 2002; 87: 1069-74.
    • (2002) Thromb Haemost , vol.87 , pp. 1069-1074
    • Ueshima, S.1    Matsuno, H.2    Hayashi, M.3    Horibuchi, K.4    Okada, K.5    Fukao, H.6
  • 84
    • 0347917028 scopus 로고    scopus 로고
    • The urokinase plasminogen activator system: Role in malignancy
    • Duffy MJ. The urokinase plasminogen activator system: role in malignancy. Curr Pharm Des 2004; 10(1): 39-49.
    • (2004) Curr Pharm Des , vol.10 , Issue.1 , pp. 39-49
    • Duffy, M.J.1
  • 85
    • 21044455501 scopus 로고    scopus 로고
    • Targeting of antioxidant and antithrombotic drugs to endothelial cell adhesion molecules
    • Muro S, Muzykantov VR. Targeting of antioxidant and antithrombotic drugs to endothelial cell adhesion molecules. Curr Pharm Des 2005; 11(18): 2383-401.
    • (2005) Curr Pharm Des , vol.11 , Issue.18 , pp. 2383-2401
    • Muro, S.1    Muzykantov, V.R.2
  • 86
    • 1642373288 scopus 로고    scopus 로고
    • Heparins and heparinoids: Occurrence, structure and mechanism of antithrombotic and hemorrhagic activities
    • Nader HB, Lopes CC, Rocha HA, Santos EA, Dietrich CP. Heparins and heparinoids: occurrence, structure and mechanism of antithrombotic and hemorrhagic activities. Curr Pharm Des 2004; 10(9): 951-66.
    • (2004) Curr Pharm Des , vol.10 , Issue.9 , pp. 951-966
    • Nader, H.B.1    Lopes, C.C.2    Rocha, H.A.3    Santos, E.A.4    Dietrich, C.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.