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Volumn 115, Issue 4, 2005, Pages 341-350

Characterization of a small molecule PAI-1 inhibitor, ZK4044

Author keywords

Antithrombotics; Fibrinolysis; PAI 1; PAI 1 inhibitor; Thrombolysis

Indexed keywords

ANTICOAGULANT AGENT; PLASMINOGEN ACTIVATOR INHIBITOR; UNCLASSIFIED DRUG; ZK 4044;

EID: 19944434102     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.thromres.2004.09.021     Document Type: Article
Times cited : (33)

References (51)
  • 1
    • 0023130521 scopus 로고
    • Plasminogen activator inhibitors
    • E.D. Sprengers, and C. Kluft Plasminogen activator inhibitors Blood 69 1987 381 387
    • (1987) Blood , vol.69 , pp. 381-387
    • Sprengers, E.D.1    Kluft, C.2
  • 3
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • D. Collen, and H.R. Lijnen Basic and clinical aspects of fibrinolysis and thrombolysis Blood 78 1991 3114 3124
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 4
    • 0029160127 scopus 로고
    • The fibrinolytic system: From Petri dishes to genetic engineering
    • M. Verstraete The fibrinolytic system: from Petri dishes to genetic engineering Thromb. Haemost. 74 1995 25 35
    • (1995) Thromb. Haemost. , vol.74 , pp. 25-35
    • Verstraete, M.1
  • 5
    • 0029153839 scopus 로고
    • Plasminogen activator inhibitor 1 (PAI-1) in plasma: Its role in thrombotic disease
    • B. Wiman Plasminogen activator inhibitor 1 (PAI-1) in plasma: its role in thrombotic disease Thromb. Haemost. 74 1995 71 76
    • (1995) Thromb. Haemost. , vol.74 , pp. 71-76
    • Wiman, B.1
  • 6
    • 0026607397 scopus 로고
    • Hypofibrinolysis in patients with a history of idiopathic deep vein thrombosis and/or pulmonary embolism
    • V. Grimaudo, F. Bachmann, J. Hauert, M.A. Christe, and E.K. Kruithof Hypofibrinolysis in patients with a history of idiopathic deep vein thrombosis and/or pulmonary embolism Thromb. Haemost. 67 1992 397 401
    • (1992) Thromb. Haemost. , vol.67 , pp. 397-401
    • Grimaudo, V.1    Bachmann, F.2    Hauert, J.3    Christe, M.A.4    Kruithof, E.K.5
  • 7
    • 0028006127 scopus 로고
    • Inhibition of endotoxin-induced activation of coagulation and fibrinolysis by pentoxifylline or by a monoclonal anti-tissue factor antibody in chimpanzees
    • M. Levi, H. ten Cate, K.A. Bauer, T. van der Poll, T.S. Edgington, and H.R. Buller Inhibition of endotoxin-induced activation of coagulation and fibrinolysis by pentoxifylline or by a monoclonal anti-tissue factor antibody in chimpanzees J. Clin. Invest. 93 1994 114 120
    • (1994) J. Clin. Invest. , vol.93 , pp. 114-120
    • Levi, M.1    Ten Cate, H.2    Bauer, K.A.3    Van Der Poll, T.4    Edgington, T.S.5    Buller, H.R.6
  • 8
    • 0024562002 scopus 로고
    • Promotion and subsequent inhibition of plasminogen activation after administration of intravenous endotoxin to normal subjects [see comments]
    • A.F. Suffredini, P.C. Harpel, and J.E. Parrillo Promotion and subsequent inhibition of plasminogen activation after administration of intravenous endotoxin to normal subjects [see comments] N. Engl. J. Med. 320 1989 1165 1172
    • (1989) N. Engl. J. Med. , vol.320 , pp. 1165-1172
    • Suffredini, A.F.1    Harpel, P.C.2    Parrillo, J.E.3
  • 9
    • 0031929812 scopus 로고    scopus 로고
    • Derangements of coagulation and fibrinolysis in critically ill patients with sepsis and septic shock
    • M.G. Vervloet, L.G. Thijs, and C.E. Hack Derangements of coagulation and fibrinolysis in critically ill patients with sepsis and septic shock Semin. Thromb. Hemost. 24 1998 33 44
    • (1998) Semin. Thromb. Hemost. , vol.24 , pp. 33-44
    • Vervloet, M.G.1    Thijs, L.G.2    Hack, C.E.3
  • 10
    • 0027438822 scopus 로고
    • Involvement of the hemostatic system in the insulin resistance syndrome. a study of 1500 patients with angina pectoris. the ECAT Angina Pectoris Study Group
    • I. Juhan-Vague, S.G. Thompson, and J. Jespersen Involvement of the hemostatic system in the insulin resistance syndrome. A study of 1500 patients with angina pectoris. The ECAT Angina Pectoris Study Group Arterioscler. Thromb. 13 1993 1865 1873
    • (1993) Arterioscler. Thromb. , vol.13 , pp. 1865-1873
    • Juhan-Vague, I.1    Thompson, S.G.2    Jespersen, J.3
  • 11
    • 0027303073 scopus 로고
    • Plasminogen activator inhibitor 1 and atherothrombosis
    • I. Juhan-Vague, and M.C. Alessi Plasminogen activator inhibitor 1 and atherothrombosis Thromb. Haemost. 70 1993 138 143
    • (1993) Thromb. Haemost. , vol.70 , pp. 138-143
    • Juhan-Vague, I.1    Alessi, M.C.2
  • 12
    • 0032974449 scopus 로고    scopus 로고
    • Correlation between coronary morphology and molecular markers of fibrinolysis in unstable angina pectoris
    • H.M. Hoffmeister, M. Jur, U. Helber, M. Fischer, W. Heller, and L. Seipel Correlation between coronary morphology and molecular markers of fibrinolysis in unstable angina pectoris Atherosclerosis 144 1999 151 157
    • (1999) Atherosclerosis , vol.144 , pp. 151-157
    • Hoffmeister, H.M.1    Jur, M.2    Helber, U.3    Fischer, M.4    Heller, W.5    Seipel, L.6
  • 13
    • 0023185776 scopus 로고
    • Plasminogen activator inhibitor in plasma: Risk factor for recurrent myocardial infarction
    • A. Hamsten, U. de Faire, G. Walldius, G. Dahlen, A. Szamosi, and C. Landou Plasminogen activator inhibitor in plasma: risk factor for recurrent myocardial infarction Lancet 2 1987 3 9
    • (1987) Lancet , vol.2 , pp. 3-9
    • Hamsten, A.1    De Faire, U.2    Walldius, G.3    Dahlen, G.4    Szamosi, A.5    Landou, C.6
  • 14
    • 0025371467 scopus 로고
    • Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene
    • L.A. Erickson, G.J. Fici, J.E. Lund, T.P. Boyle, H.G. Polites, and K.R. Marotti Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene Nature 346 1990 74 76
    • (1990) Nature , vol.346 , pp. 74-76
    • Erickson, L.A.1    Fici, G.J.2    Lund, J.E.3    Boyle, T.P.4    Polites, H.G.5    Marotti, K.R.6
  • 15
    • 0037162388 scopus 로고    scopus 로고
    • Age-dependent spontaneous coronary arterial thrombosis in transgenic mice that express a stable form of human plasminogen activator inhibitor-1
    • M. Eren, C.A. Painter, J.B. Atkinson, P.J. Declerck, and D.E. Vaughan Age-dependent spontaneous coronary arterial thrombosis in transgenic mice that express a stable form of human plasminogen activator inhibitor-1 Circulation 106 2002 491 496
    • (2002) Circulation , vol.106 , pp. 491-496
    • Eren, M.1    Painter, C.A.2    Atkinson, J.B.3    Declerck, P.J.4    Vaughan, D.E.5
  • 16
    • 0345725987 scopus 로고    scopus 로고
    • Regulation of arterial thrombolysis by plasminogen activator inhibitor-1 in mice
    • P.M. Farrehi, C.K. Ozaki, P. Carmeliet, and W.P. Fay Regulation of arterial thrombolysis by plasminogen activator inhibitor-1 in mice Circulation 97 1998 1002 1008
    • (1998) Circulation , vol.97 , pp. 1002-1008
    • Farrehi, P.M.1    Ozaki, C.K.2    Carmeliet, P.3    Fay, W.P.4
  • 17
    • 0034650976 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 and vitronectin promote vascular thrombosis in mice
    • D.T. Eitzman, R.J. Westrick, E.G. Nabel, and D. Ginsburg Plasminogen activator inhibitor-1 and vitronectin promote vascular thrombosis in mice Blood 95 2000 577 580
    • (2000) Blood , vol.95 , pp. 577-580
    • Eitzman, D.T.1    Westrick, R.J.2    Nabel, E.G.3    Ginsburg, D.4
  • 18
    • 0033564748 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 is a major determinant of arterial thrombolysis resistance
    • Y. Zhu, P. Carmeliet, and W.P. Fay Plasminogen activator inhibitor-1 is a major determinant of arterial thrombolysis resistance Circulation 99 1999 3050 3055
    • (1999) Circulation , vol.99 , pp. 3050-3055
    • Zhu, Y.1    Carmeliet, P.2    Fay, W.P.3
  • 19
    • 0027135792 scopus 로고
    • Plasminogen activator inhibitor-1 gene-deficient mice: II. Effects on hemostasis, thrombosis, and thrombolysis
    • P. Carmeliet, J.M. Stassen, L. Schoonjans, B. Ream, J.J. van den Oord, and M. De Mol Plasminogen activator inhibitor-1 gene-deficient mice: II. Effects on hemostasis, thrombosis, and thrombolysis J. Clin. Invest. 92 1993 2756 2760
    • (1993) J. Clin. Invest. , vol.92 , pp. 2756-2760
    • Carmeliet, P.1    Stassen, J.M.2    Schoonjans, L.3    Ream, B.4    Van Den Oord, J.J.5    De Mol, M.6
  • 21
    • 0030610091 scopus 로고    scopus 로고
    • The Fab-fragment of a PAI-1 inhibiting antibody reduces thrombus size and restores blood flow in a rat model of arterial thrombosis
    • J.J. van Giezen, G. Wahlund, V. Nerme, and T. Abrahamsson The Fab-fragment of a PAI-1 inhibiting antibody reduces thrombus size and restores blood flow in a rat model of arterial thrombosis Thromb. Haemost. 77 1997 964 969
    • (1997) Thromb. Haemost. , vol.77 , pp. 964-969
    • Van Giezen, J.J.1    Wahlund, G.2    Nerme, V.3    Abrahamsson, T.4
  • 22
    • 0026597817 scopus 로고
    • Inhibition of plasminogen activator inhibitor-1 activity results in promotion of endogenous thrombolysis and inhibition of thrombus extension in models of experimental thrombosis [see comments]
    • M. Levi, B.J. Biemond, A.J. van Zonneveld, J.W. ten Cate, and H. Pannekoek Inhibition of plasminogen activator inhibitor-1 activity results in promotion of endogenous thrombolysis and inhibition of thrombus extension in models of experimental thrombosis [see comments] Circulation 85 1992 305 312
    • (1992) Circulation , vol.85 , pp. 305-312
    • Levi, M.1    Biemond, B.J.2    Van Zonneveld, A.J.3    Ten Cate, J.W.4    Pannekoek, H.5
  • 23
    • 0028909718 scopus 로고
    • Thrombolysis and reocclusion in experimental jugular vein and coronary artery thrombosis. Effects of a plasminogen activator inhibitor type 1-neutralizing monoclonal antibody
    • B.J. Biemond, M. Levi, R. Coronel, M.J. Janse, J.W. ten Cate, and H. Pannekoek Thrombolysis and reocclusion in experimental jugular vein and coronary artery thrombosis. Effects of a plasminogen activator inhibitor type 1-neutralizing monoclonal antibody Circulation 91 1995 1175 1181
    • (1995) Circulation , vol.91 , pp. 1175-1181
    • Biemond, B.J.1    Levi, M.2    Coronel, R.3    Janse, M.J.4    Ten Cate, J.W.5    Pannekoek, H.6
  • 24
    • 0028851871 scopus 로고
    • Biological effects of combined inactivation of plasminogen activator and plasminogen activator inhibitor-1 gene function in mice
    • H.R. Lijnen, L. Moons, V. Beelen, P. Carmelie, and D. Collen Biological effects of combined inactivation of plasminogen activator and plasminogen activator inhibitor-1 gene function in mice Thromb. Haemost. 74 1995 1126 1131
    • (1995) Thromb. Haemost. , vol.74 , pp. 1126-1131
    • Lijnen, H.R.1    Moons, L.2    Beelen, V.3    Carmelie, P.4    Collen, D.5
  • 26
    • 10744228127 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of menthol-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1)
    • B. Ye, S. Bauer, B.O. Buckman, A. Ghannam, B.D. Griedel, and S.K. Khim Synthesis and biological evaluation of menthol-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1) Bioorg. Med. Chem. Lett. 13 2003 3361 3365
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 3361-3365
    • Ye, B.1    Bauer, S.2    Buckman, B.O.3    Ghannam, A.4    Griedel, B.D.5    Khim, S.K.6
  • 27
    • 0023268018 scopus 로고
    • An automated fibrinolytic assay performed in microtiter plates
    • D.P. Beebe, and D.L. Aronson An automated fibrinolytic assay performed in microtiter plates Thromb. Res. 47 1987 123 128
    • (1987) Thromb. Res. , vol.47 , pp. 123-128
    • Beebe, D.P.1    Aronson, D.L.2
  • 28
    • 0041355222 scopus 로고    scopus 로고
    • Mutations in the substrate binding site of thrombin-activatable fibrinolysis inhibitor (TAFI) alter its substrate specificity
    • L. Zhao, B. Buckman, M. Seto, J. Morser, and M. Nagashima Mutations in the substrate binding site of thrombin-activatable fibrinolysis inhibitor (TAFI) alter its substrate specificity J. Biol. Chem. 278 2003 32359 32366
    • (2003) J. Biol. Chem. , vol.278 , pp. 32359-32366
    • Zhao, L.1    Buckman, B.2    Seto, M.3    Morser, J.4    Nagashima, M.5
  • 29
    • 0028596532 scopus 로고
    • Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator
    • P. Bjorquist, M. Brohlin, J. Ehnebom, M. Ericsson, C. Kristiansen, and G. Pohl Plasminogen activator inhibitor type-1 interacts exclusively with the proteinase domain of tissue plasminogen activator Biochim. Biophys. Acta 1209 1994 191 202
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 191-202
    • Bjorquist, P.1    Brohlin, M.2    Ehnebom, J.3    Ericsson, M.4    Kristiansen, C.5    Pohl, G.6
  • 30
    • 0030898213 scopus 로고    scopus 로고
    • Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin. Implications for the regulation of pericellular proteolysis
    • D.A. Lawrence, S. Palaniappan, S. Stefansson, S.T. Olson, A.M. Francis-Chmura, and J.D. Shore Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin. Implications for the regulation of pericellular proteolysis J. Biol. Chem. 272 1997 7676 7680
    • (1997) J. Biol. Chem. , vol.272 , pp. 7676-7680
    • Lawrence, D.A.1    Palaniappan, S.2    Stefansson, S.3    Olson, S.T.4    Francis-Chmura, A.M.5    Shore, J.D.6
  • 31
    • 0036336458 scopus 로고    scopus 로고
    • Importance of N-terminal residues in plasminogen activator inhibitor 1 on its antibody induced latency transition
    • T.H. Ngo, Y. Zhou, J.M. Stassen, and P.J. Declerck Importance of N-terminal residues in plasminogen activator inhibitor 1 on its antibody induced latency transition Thromb. Haemost. 88 2002 288 293
    • (2002) Thromb. Haemost. , vol.88 , pp. 288-293
    • Ngo, T.H.1    Zhou, Y.2    Stassen, J.M.3    Declerck, P.J.4
  • 32
    • 0027945176 scopus 로고
    • Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition
    • D.A. Lawrence, S.T. Olson, S. Palaniappan, and D. Ginsburg Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition J. Biol. Chem. 269 1994 27657 27662
    • (1994) J. Biol. Chem. , vol.269 , pp. 27657-27662
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 33
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • M.B. Berkenpas, D.A. Lawrence, and D. Ginsburg Molecular evolution of plasminogen activator inhibitor-1 functional stability EMBO J. 14 1995 2969 2977
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 34
    • 0027445304 scopus 로고
    • Inhibition of endothelial cell expression of plasminogen activator inhibitor type-1 by gemfibrozil
    • S. Fujii, H. Sawa, and B.E. Sobel Inhibition of endothelial cell expression of plasminogen activator inhibitor type-1 by gemfibrozil Thromb. Haemost. 70 1993 642 647
    • (1993) Thromb. Haemost. , vol.70 , pp. 642-647
    • Fujii, S.1    Sawa, H.2    Sobel, B.E.3
  • 35
    • 0031733038 scopus 로고    scopus 로고
    • Fibrate-modulated expression of fibrinogen, plasminogen activator inhibitor-1 and apolipoprotein A-I in cultured cynomolgus monkey hepatocytes-role of the peroxisome proliferator-activated receptor-alpha
    • M. Kockx, H.M. Princen, and T. Kooistra Fibrate-modulated expression of fibrinogen, plasminogen activator inhibitor-1 and apolipoprotein A-I in cultured cynomolgus monkey hepatocytes-role of the peroxisome proliferator-activated receptor-alpha Thromb. Haemost. 80 1998 942 948
    • (1998) Thromb. Haemost. , vol.80 , pp. 942-948
    • Kockx, M.1    Princen, H.M.2    Kooistra, T.3
  • 36
    • 0031568825 scopus 로고    scopus 로고
    • A new butadiene derivative, T-686, inhibits plasminogen activator inhibitor type-1 production in vitro by cultured human vascular endothelial cells and development of atherosclerotic lesions in vivo in rabbits
    • B. Vinogradsky, S.P. Bell, J. Woodcock-Mitchell, A. Ohtani, and S. Fujii A new butadiene derivative, T-686, inhibits plasminogen activator inhibitor type-1 production in vitro by cultured human vascular endothelial cells and development of atherosclerotic lesions in vivo in rabbits Thromb. Res. 85 1997 305 314
    • (1997) Thromb. Res. , vol.85 , pp. 305-314
    • Vinogradsky, B.1    Bell, S.P.2    Woodcock-Mitchell, J.3    Ohtani, A.4    Fujii, S.5
  • 37
    • 0028302011 scopus 로고
    • Effect of notoginsenoside R1 on the synthesis of tissue-type plasminogen activator and plasminogen activator inhibitor-1 in cultured human umbilical vein endothelial cells
    • W. Zhang, J. Wojta, and B.R. Binder Effect of notoginsenoside R1 on the synthesis of tissue-type plasminogen activator and plasminogen activator inhibitor-1 in cultured human umbilical vein endothelial cells Arterioscler. Thromb. 14 1994 1040 1046
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 1040-1046
    • Zhang, W.1    Wojta, J.2    Binder, B.R.3
  • 38
    • 0030978115 scopus 로고    scopus 로고
    • Notoginsenoside R1 counteracts endotoxininduced activation of endothelial cells in vitro and endotoxin-induced lethality in mice in vivo
    • W.J. Zhang, J. Wojta, and B.R. Binder Notoginsenoside R1 counteracts endotoxininduced activation of endothelial cells in vitro and endotoxin-induced lethality in mice in vivo Arterioscler. Thromb. Vasc. Biol. 17 1997 465 474
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 465-474
    • Zhang, W.J.1    Wojta, J.2    Binder, B.R.3
  • 40
    • 0039518548 scopus 로고    scopus 로고
    • Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis
    • P. Bjorquist, J. Ehnebom, T. Inghardt, L. Hansson, M. Lindberg, and M. Linschoten Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis Biochemistry 37 1998 1227 1234
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Bjorquist, P.1    Ehnebom, J.2    Inghardt, T.3    Hansson, L.4    Lindberg, M.5    Linschoten, M.6
  • 41
    • 3042687515 scopus 로고    scopus 로고
    • Tiplaxtinin, a novel, orally efficacious inhibitor of plasminogen activator inhibitor-1: Design, synthesis, and preclinical characterization
    • H. Elokdah, M. Abou-Gharbia, J.K. Hennan, G. McFarlane, C.P. Mugford, and G. Krishnamurthy Tiplaxtinin, a novel, orally efficacious inhibitor of plasminogen activator inhibitor-1: design, synthesis, and preclinical characterization J. Med. Chem. 47 2004 3491 3494
    • (2004) J. Med. Chem. , vol.47 , pp. 3491-3494
    • Elokdah, H.1    Abou-Gharbia, M.2    Hennan, J.K.3    McFarlane, G.4    Mugford, C.P.5    Krishnamurthy, G.6
  • 42
    • 1642452634 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of piperazine-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1)
    • B. Ye, Y.L. Chou, R. Karanjawala, W. Lee, S.F. Lu, and K.J. Shaw Synthesis and biological evaluation of piperazine-based derivatives as inhibitors of plasminogen activator inhibitor-1 (PAI-1) Bioorg. Med. Chem. Lett. 14 2004 761 765
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 761-765
    • Ye, B.1    Chou, Y.L.2    Karanjawala, R.3    Lee, W.4    Lu, S.F.5    Shaw, K.J.6
  • 43
    • 0030904328 scopus 로고    scopus 로고
    • XR5118, a novel modulator of plasminogen activator inhibitor-1 (PAI-1), increases endogenous tPA activity in the rat
    • P. Charlton, R. Faint, C. Barnes, F. Bent, A. Folkes, and D. Templeton XR5118, a novel modulator of plasminogen activator inhibitor-1 (PAI-1), increases endogenous tPA activity in the rat Fibrinolysis Proteolysis 11 1997 51 56
    • (1997) Fibrinolysis Proteolysis , vol.11 , pp. 51-56
    • Charlton, P.1    Faint, R.2    Barnes, C.3    Bent, F.4    Folkes, A.5    Templeton, D.6
  • 44
    • 0030857519 scopus 로고    scopus 로고
    • Novel low-molecular-weight inhibitor of PAI-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits
    • P.W. Friederich, M. Levi, B.J. Biemond, P. Charlton, D. Templeton, and A.J. van Zonneveld Novel low-molecular-weight inhibitor of PAI-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits Circulation 96 1997 916 921
    • (1997) Circulation , vol.96 , pp. 916-921
    • Friederich, P.W.1    Levi, M.2    Biemond, B.J.3    Charlton, P.4    Templeton, D.5    Van Zonneveld, A.J.6
  • 45
    • 12544250776 scopus 로고    scopus 로고
    • Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy
    • D.L. Crandall, H. Elokdah, L. Di, J.K. Hennan, N.V. Gorlatova, and D.A. Lawrence Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy J. Thromb. Haemost. 2 2004 1422 1428
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 1422-1428
    • Crandall, D.L.1    Elokdah, H.2    Di, L.3    Hennan, J.K.4    Gorlatova, N.V.5    Lawrence, D.A.6
  • 47
    • 0029161540 scopus 로고
    • Crystallization and X-ray diffraction data of the cleaved form of plasminogen activator inhibitor-1
    • K. Aertgeerts, H.L. De Bondt, C. De Ranter, and P.J. Declerck Crystallization and X-ray diffraction data of the cleaved form of plasminogen activator inhibitor-1 Proteins 23 1995 118 121
    • (1995) Proteins , vol.23 , pp. 118-121
    • Aertgeerts, K.1    De Bondt, H.L.2    De Ranter, C.3    Declerck, P.J.4
  • 48
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • A.M. Sharp, P.E. Stein, N.S. Pannu, R.W. Carrell, M.B. Berkenpas, and D. Ginsburg The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion Struct. Fold Des. 7 1999 111 118
    • (1999) Struct. Fold Des. , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3    Carrell, R.W.4    Berkenpas, M.B.5    Ginsburg, D.6
  • 49
    • 0038606342 scopus 로고    scopus 로고
    • Immobilization of the distal hinge in the labile serpin plasminogen activator inhibitor 1: Identification of a transition state with distinct conformational and functional properties
    • B. De Taeye, G. Compernolle, M. Dewilde, W. Biesemans, and P.J. Declerck Immobilization of the distal hinge in the labile serpin plasminogen activator inhibitor 1: identification of a transition state with distinct conformational and functional properties J. Biol. Chem. 278 2003 23899 23905
    • (2003) J. Biol. Chem. , vol.278 , pp. 23899-23905
    • De Taeye, B.1    Compernolle, G.2    Dewilde, M.3    Biesemans, W.4    Declerck, P.J.5
  • 50
    • 0034737309 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation
    • H. Nar, M. Bauer, J.M. Stassen, D. Lang, A. Gils, and P.J. Declerck Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation J. Mol. Biol. 297 2000 683 695
    • (2000) J. Mol. Biol. , vol.297 , pp. 683-695
    • Nar, H.1    Bauer, M.2    Stassen, J.M.3    Lang, D.4    Gils, A.5    Declerck, P.J.6
  • 51
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory mechanism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • Y. Xue, P. Bjorquist, T. Inghardt, M. Linschoten, D. Musil, and L. Sjolin Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide Structure 6 1998 627 636
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Bjorquist, P.2    Inghardt, T.3    Linschoten, M.4    Musil, D.5    Sjolin, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.