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Volumn 91, Issue 3, 2004, Pages 425-437

The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitors

Author keywords

Fibrinolysis; PAI 1; Serpin; Thrombosis

Indexed keywords

3 BENZYLIDENE 4 (3,4,5 TRIMETHOXYBENZYLIDENE)SUCCINIMIDE; ALTEPLASE; ANTISENSE OLIGONUCLEOTIDE; FENDOSAL; FLUFENAMIC ACID; MONOCLONAL ANTIBODY; PEPTIDE DERIVATIVE; PIPERAZINEDIONE; PLASMIN; PLASMINOGEN; PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE INHIBITOR; TENECTEPLASE; TISSUE PLASMINOGEN ACTIVATOR; TRITON X 100; UROKINASE; VITRONECTIN;

EID: 1642318429     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (91)

References (180)
  • 1
    • 0001724344 scopus 로고
    • Serpins: The superfamily of plasma serine proteinase inhibitors
    • Barrett, Salvesen, eds. Elsevier Science
    • Carrell RW, Boswell DR. Serpins: The superfamily of plasma serine proteinase inhibitors. In: Barrett, Salvesen, eds. Proteinase inhibitors. Elsevier Science, 1986; 403-20.
    • (1986) Proteinase Inhibitors , pp. 403-420
    • Carrell, R.W.1    Boswell, D.R.2
  • 2
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1- anti-trypsin for structure and function of serpins
    • Huber R, Carrell RW. Implications of the three-dimensional structure of alpha 1- anti-trypsin for structure and function of serpins. Biochemistry 1989; 28: 8951-66.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 3
    • 0032578355 scopus 로고    scopus 로고
    • The 0.78 angstrom structure of a serine protease: Bacillus lentus subtilisin
    • Kuhn P, Knapp M, Soltis SM, et al. The 0.78 angstrom structure of a serine protease: Bacillus lentus subtilisin. Biochemistry 1998; 37: 13446-52.
    • (1998) Biochemistry , vol.37 , pp. 13446-13452
    • Kuhn, P.1    Knapp, M.2    Soltis, S.M.3
  • 4
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • Irving JA, Pike RN, Lesk AM, et al. Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function. Genome Res 2000; 10: 1845-64.
    • (2000) Genome Res. , vol.10 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3
  • 5
    • 0035060052 scopus 로고    scopus 로고
    • Vertebrate serpins: Construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses
    • Ragg H, Lokot T, Kamp PB, et al. Vertebrate serpins: construction of a conflict-free phylogeny by combining exon-intron and diagnostic site analyses. Mol Biol Evol 2001; 18: 577-84.
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 577-584
    • Ragg, H.1    Lokot, T.2    Kamp, P.B.3
  • 7
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationship in serpins: Current concepts and controversies
    • Gils A, Declerck PJ. Structure-function relationship in serpins: Current concepts and controversies. Thromb Haemost 1998; 80: 531-41.
    • (1998) Thromb. Haemost. , vol.80 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 9
    • 0032485864 scopus 로고    scopus 로고
    • An ester bond linking a fragment of a serine proteinase to its serpin inhibitor
    • Egelund R, Rodenburg KW, Andreasen PA, et al. An ester bond linking a fragment of a serine proteinase to its serpin inhibitor. Biochemistry 1998; 37: 6375-9.
    • (1998) Biochemistry , vol.37 , pp. 6375-6379
    • Egelund, R.1    Rodenburg, K.W.2    Andreasen, P.A.3
  • 10
    • 0028824030 scopus 로고
    • Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
    • Lawrence DA, Ginsburg D, Day DE, et al. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates. J Biol Chem 1995; 270: 25309-12.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25309-25312
    • Lawrence, D.A.1    Ginsburg, D.2    Day, D.E.3
  • 11
    • 0029591826 scopus 로고
    • The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex
    • Wilczynska M, Fa M, Ohlsson PI, et al. The inhibition mechanism of serpins. Evidence that the mobile reactive center loop is cleaved in the native protease-inhibitor complex. J Biol Chem 1995; 270: 29652-5.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29652-29655
    • Wilczynska, M.1    Fa, M.2    Ohlsson, P.I.3
  • 12
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature 2000; 407: 923-6.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 13
    • 0022976041 scopus 로고
    • Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme
    • Andreasen PA, Nielsen LS, Kristensen P, et al. Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme. J Biol Chem 1986; 261: 7644-51.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7644-7651
    • Andreasen, P.A.1    Nielsen, L.S.2    Kristensen, P.3
  • 14
    • 0022852285 scopus 로고
    • cDNA cloning of human plasminogen activator-inhibitor from endothelial cells
    • Ginsburg D, Zeheb R, Yang AY, et al. cDNA cloning of human plasminogen activator-inhibitor from endothelial cells. J Clin Invest 1986; 78: 1673-80.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1673-1680
    • Ginsburg, D.1    Zeheb, R.2    Yang, A.Y.3
  • 15
    • 0345693050 scopus 로고
    • Cloning and sequence of a cDNA coding for the human beta- migrating endothelial-cell-type plasminogen activator inhibitor
    • Ny T, Sawdey M, Lawrence D, et al. Cloning and sequence of a cDNA coding for the human beta- migrating endothelial-cell-type plasminogen activator inhibitor. Proc Natl Acad Sci U S A 1986; 83: 6776-80.
    • (1986) Proc. Natl. Acad. Sci. U S A , vol.83 , pp. 6776-6780
    • Ny, T.1    Sawdey, M.2    Lawrence, D.3
  • 16
    • 0022800441 scopus 로고
    • Endothelial plasminogen activator inhibitor (PAI): A new member of the Serpin gene family
    • Pannekoek H, Veerman H, Lambers H, et al. Endothelial plasminogen activator inhibitor (PAI): A new member of the Serpin gene family. EMBO J 1986; 5: 2539-44.
    • (1986) EMBO J. , vol.5 , pp. 2539-2544
    • Pannekoek, H.1    Veerman, H.2    Lambers, H.3
  • 17
    • 0021687079 scopus 로고
    • Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells
    • van Mourik JA, Lawrence DA, Loskutoff DJ. Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells. J Biol Chem 1984; 259: 14914-21.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14914-14921
    • van Mourik, J.A.1    Lawrence, D.A.2    Loskutoff, D.J.3
  • 18
    • 0042466527 scopus 로고    scopus 로고
    • Biochemical importance of glycosylation of plasminogen activator inhibitor-1
    • Gils A, Pedersen KE, Skottrup P, et al. Biochemical importance of glycosylation of plasminogen activator inhibitor-1. Thromb Haemost 2003; 90: 206-17.
    • (2003) Thromb. Haemost. , vol.90 , pp. 206-217
    • Gils, A.1    Pedersen, K.E.2    Skottrup, P.3
  • 19
    • 0019876904 scopus 로고
    • An inhibitor of plasminogen activator in rabbit endothelial cells
    • Loskutoff DJ, Edgington TS. An inhibitor of plasminogen activator in rabbit endothelial cells. J Biol Chem 1981; 256: 4142-5.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4142-4145
    • Loskutoff, D.J.1    Edgington, T.S.2
  • 20
    • 0020625088 scopus 로고
    • Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells
    • Loskutoff DJ, van Mourik JA, Erickson LA, et al. Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells. Proc Natl Acad Sci U S A 1983; 80: 2956-60.
    • (1983) Proc. Natl. Acad. Sci. U S A , vol.80 , pp. 2956-2960
    • Loskutoff, D.J.1    van Mourik, J.A.2    Erickson, L.A.3
  • 21
    • 0020328292 scopus 로고
    • The dexamethasone-induced inhibitor of fibrinolytic activity in hepatoma cells. A cellular product which specifically inhibits plasminogen activation
    • Coleman PL, Barouski PA, Gelehrter TD. The dexamethasone-induced inhibitor of fibrinolytic activity in hepatoma cells. A cellular product which specifically inhibits plasminogen activation. J Biol Chem 1982; 257: 4260-4.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4260-4264
    • Coleman, P.L.1    Barouski, P.A.2    Gelehrter, T.D.3
  • 22
    • 0023201909 scopus 로고
    • Plasminogen activator inhibitor from human endothelial cells. Purification and partial characterization
    • Booth NA, MacGregor IR, Hunter NR, et al. Plasminogen activator inhibitor from human endothelial cells. Purification and partial characterization. Eur J Biochem 1987; 165: 595-600.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 595-600
    • Booth, N.A.1    MacGregor, I.R.2    Hunter, N.R.3
  • 23
    • 0022829320 scopus 로고
    • Purification of an active plasminogen activator inhibitor immunologically related to the endothelial type plasminogen activator inhibitor from the conditioned media of a human melanoma cell line
    • [published erratum appears in J Biol Chem 1988 Jan 25;263(3):1593]
    • Wagner OF, Vetterlein M, Binder BR. Purification of an active plasminogen activator inhibitor immunologically related to the endothelial type plasminogen activator inhibitor from the conditioned media of a human melanoma cell line [published erratum appears in J Biol Chem 1988 Jan 25;263(3):1593]. J Biol Chem 1986; 261: 14474-81.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14474-14481
    • Wagner, O.F.1    Vetterlein, M.2    Binder, B.R.3
  • 24
    • 0642308772 scopus 로고
    • On the relationship between different molecular forms of the fast inhibitor of tissue plasminogen activator
    • Chmielewska J, Carlsson T, Urden G, et al. On the relationship between different molecular forms of the fast inhibitor of tissue plasminogen activator. Fibrinolysis 1987; 1: 67-73.
    • (1987) Fibrinolysis , vol.1 , pp. 67-73
    • Chmielewska, J.1    Carlsson, T.2    Urden, G.3
  • 25
    • 0021353283 scopus 로고
    • Plasma levels of a specific inhibitor of tissue-type plasminogen activator (and urokinase) in normal and pathological conditions
    • Juhan Vague I, Moerman B, De Cock F, et al. Plasma levels of a specific inhibitor of tissue-type plasminogen activator (and urokinase) in normal and pathological conditions. Thromb Res 1984; 33: 523-30.
    • (1984) Thromb. Res. , vol.33 , pp. 523-530
    • Juhan Vague, I.1    Moerman, B.2    De Cock, F.3
  • 26
    • 0023574958 scopus 로고
    • Plasminogen activator inhibitor 1: Development of a radioimmunoassay and observations on its plasma concentration during venous occlusion and after platelet aggregation
    • Kruithof EK, Nicolosa G, Bachmann F. Plasminogen activator inhibitor 1: Development of a radioimmunoassay and observations on its plasma concentration during venous occlusion and after platelet aggregation. Blood 1987; 70: 1645-53.
    • (1987) Blood , vol.70 , pp. 1645-1653
    • Kruithof, E.K.1    Nicolosa, G.2    Bachmann, F.3
  • 27
    • 0030975615 scopus 로고    scopus 로고
    • Production of plasminogen activator inhibitor 1 by human adipose tissue: Possible link between visceral fat accumulation and vascular disease
    • Alessi MC, Peiretti F, Morange P, et al. Production of plasminogen activator inhibitor 1 by human adipose tissue: Possible link between visceral fat accumulation and vascular disease. Diabetes 1997; 46: 860-7.
    • (1997) Diabetes , vol.46 , pp. 860-867
    • Alessi, M.C.1    Peiretti, F.2    Morange, P.3
  • 28
    • 0026350498 scopus 로고
    • Systematic mutational analyses of protein-protein interfaces
    • Wells JA. Systematic mutational analyses of protein-protein interfaces. Methods Enzymol 1991; 202: 390-411.
    • (1991) Methods Enzymol. , vol.202 , pp. 390-411
    • Wells, J.A.1
  • 29
    • 0023181782 scopus 로고
    • Structure of the human plasminogen activator inhibitor 1 gene: Nonrandom distribution of introns
    • Loskutoff DJ, Linders M, Keijer J, et al. Structure of the human plasminogen activator inhibitor 1 gene: Nonrandom distribution of introns. Biochemistry 1987; 26: 3763-8.
    • (1987) Biochemistry , vol.26 , pp. 3763-3768
    • Loskutoff, D.J.1    Linders, M.2    Keijer, J.3
  • 30
    • 0023937182 scopus 로고
    • Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences
    • Bosma PJ, van den Berg EA, Kooistra T, et al. Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. J Biol Chem 1988; 263: 9129-41.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9129-9141
    • Bosma, P.J.1    van den Berg, E.A.2    Kooistra, T.3
  • 31
    • 0023812882 scopus 로고
    • The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family
    • Strandberg L, Lawrence D, Ny T. The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur J Biochem 1988; 176: 609-16.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 609-616
    • Strandberg, L.1    Lawrence, D.2    Ny, T.3
  • 32
    • 0023888941 scopus 로고
    • The regulatory region of the human plasminogen activator inhibitor type-1 (PAI-1) gene
    • Riccio A, Lund LR, Sartorio R, et al. The regulatory region of the human plasminogen activator inhibitor type-1 (PAI-1) gene. Nucleic Acids Res 1988; 16: 2805-24.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2805-2824
    • Riccio, A.1    Lund, L.R.2    Sartorio, R.3
  • 33
    • 0024234809 scopus 로고
    • Cloning and sequencing of cDNA for the rat plasminogen activator inhibitor-1
    • Zeheb R, Gelehrter TD. Cloning and sequencing of cDNA for the rat plasminogen activator inhibitor-1. Gene 1988; 73: 459-68.
    • (1988) Gene , vol.73 , pp. 459-468
    • Zeheb, R.1    Gelehrter, T.D.2
  • 34
    • 0024446121 scopus 로고
    • cDNA for bovine type 1 plasminogen activator inhibitor (PAI-1)
    • Mimuro J, Sawdey M, Hattori M, et al. cDNA for bovine type 1 plasminogen activator inhibitor (PAI-1). Nucleic Acids Res 1989; 17: 8872.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8872
    • Mimuro, J.1    Sawdey, M.2    Hattori, M.3
  • 35
    • 0025122368 scopus 로고
    • The c-myc-regulated gene mrl encodes plasminogen activator inhibitor 1
    • Prendergast GC, Diamond LE, Dahl D, et al. The c-myc-regulated gene mrl encodes plasminogen activator inhibitor 1. Mol Cell Biol 1990; 10: 1265-9.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1265-1269
    • Prendergast, G.C.1    Diamond, L.E.2    Dahl, D.3
  • 36
    • 0026785349 scopus 로고
    • Purification and characterisation of recombinant rabbit plasminogen activator inhibitor-1 expressed in Saccharomyces cerevisiae
    • Hofmann KJ, Mayer EJ, Schultz LD, et al. Purification and characterisation of recombinant rabbit plasminogen activator inhibitor-1 expressed in Saccharomyces cerevisiae. Fibrinolysis 1992; 6: 263-72.
    • (1992) Fibrinolysis , vol.6 , pp. 263-272
    • Hofmann, K.J.1    Mayer, E.J.2    Schultz, L.D.3
  • 37
    • 0031050028 scopus 로고    scopus 로고
    • Expression and characterization of recombinant porcine plasminogen activator inhibitor-1
    • Bijnens AP, Knockaert I, Cousin E, et al. Expression and characterization of recombinant porcine plasminogen activator inhibitor-1. Thromb Haemost 1997; 77: 350-6.
    • (1997) Thromb. Haemost. , vol.77 , pp. 350-356
    • Bijnens, A.P.1    Knockaert, I.2    Cousin, E.3
  • 38
    • 0029860677 scopus 로고    scopus 로고
    • Identification of a cis-acting sequence in the human plasminogen activator inhibitor type-1 gene that mediates transforming growth factor-beta1 responsiveness in endothelium in vivo
    • Dong G, Schulick AH, DeYoung MB, et al. Identification of a cis-acting sequence in the human plasminogen activator inhibitor type-1 gene that mediates transforming growth factor-beta1 responsiveness in endothelium in vivo. J Biol Chem 1996; 271: 29969-77.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29969-29977
    • Dong, G.1    Schulick, A.H.2    DeYoung, M.B.3
  • 40
    • 0034704076 scopus 로고    scopus 로고
    • Regulation of plasminogen activator inhibitor-1 expression by transforming growth factor-beta -induced physical and functional interactions between smads and Sp1
    • Datta PK, Blake MC, Moses HL. Regulation of plasminogen activator inhibitor-1 expression by transforming growth factor-beta -induced physical and functional interactions between smads and Sp1. J Biol Chem 2000; 275: 40014-9.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40014-40019
    • Datta, P.K.1    Blake, M.C.2    Moses, H.L.3
  • 41
    • 0034661835 scopus 로고    scopus 로고
    • Sp1-like activity mediates angiotensin-II-induced plasminogen-activator inhibitor type-1 (PAI-1) gene expression in mesangial cells
    • Motojima M, Ando T, Yoshioka T. Sp1-like activity mediates angiotensin-II-induced plasminogen-activator inhibitor type-1 (PAI-1) gene expression in mesangial cells. Biochem J 2000; 349: 435-41.
    • (2000) Biochem. J. , vol.349 , pp. 435-441
    • Motojima, M.1    Ando, T.2    Yoshioka, T.3
  • 42
    • 1642387335 scopus 로고    scopus 로고
    • Tissue- and agonist-specific regulation of human and murine plasminogen activator inhibitor-1 promoters in transgenic mice
    • Eren M, Painter CA, Gleaves LA, et al. Tissue- and agonist-specific regulation of human and murine plasminogen activator inhibitor-1 promoters in transgenic mice. J Thromb Haemost 2003; 1: 2389-96.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2389-2396
    • Eren, M.1    Painter, C.A.2    Gleaves, L.A.3
  • 43
    • 0038281353 scopus 로고    scopus 로고
    • Direct binding of Nur77/NAK-1 to the plasminogen activator inhibitor 1 (PAI-1) promoter regulates TNF alpha -induced PAI-1 expression
    • Gruber F, Hufnagl P, Hofer-Warbinek R, et al. Direct binding of Nur77/NAK-1 to the plasminogen activator inhibitor 1 (PAI-1) promoter regulates TNF alpha -induced PAI-1 expression. Blood 2003; 101: 3042-8.
    • (2003) Blood , vol.101 , pp. 3042-3048
    • Gruber, F.1    Hufnagl, P.2    Hofer-Warbinek, R.3
  • 44
    • 0024791659 scopus 로고
    • Purification of active human plasminogen activator inhibitor 1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells
    • Lawrence D, Strandberg L, Grundstrom T, et al. Purification of active human plasminogen activator inhibitor 1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells. Eur J Biochem 1989; 186: 523-33.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 523-533
    • Lawrence, D.1    Strandberg, L.2    Grundstrom, T.3
  • 45
    • 0028064911 scopus 로고
    • Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop
    • Audenaert AM, Knockaert I, Collen D, et al. Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J Biol Chem 1994; 269: 19559-64.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19559-19564
    • Audenaert, A.M.1    Knockaert, I.2    Collen, D.3
  • 46
    • 0029943026 scopus 로고    scopus 로고
    • Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop
    • Gils A, Knockaert I, Declerck PJ. Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 1996; 35: 7474-81.
    • (1996) Biochemistry , vol.35 , pp. 7474-7481
    • Gils, A.1    Knockaert, I.2    Declerck, P.J.3
  • 47
    • 0029828508 scopus 로고    scopus 로고
    • Conformational changes of the reactive centre loop and beta strand 5a accompany temperature dependent inhibitor substrate transition of plasminogen activator inhibitor 1
    • Kjoller L, Martensen PM, Sottrupjensen L, et al. Conformational changes of the reactive centre loop and beta strand 5a accompany temperature dependent inhibitor substrate transition of plasminogen activator inhibitor 1. Eur J Biochem 1996; 241: 38-46.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 38-46
    • Kjoller, L.1    Martensen, P.M.2    Sottrupjensen, L.3
  • 48
    • 0031962017 scopus 로고    scopus 로고
    • Binding of urokinase-type plasminogen activator plasminogen activator inhibitor-1 complex to the endocytosis receptors alpha(2)-macroglobulin receptor low-density lipoprotein receptor- related protein and very-low-density lipoprotein receptor involves basic residues in the inhibitor
    • Rodenburg KW, Kjoller L, Petersen HH, et al. Binding of urokinase-type plasminogen activator plasminogen activator inhibitor-1 complex to the endocytosis receptors alpha(2)-macroglobulin receptor low-density lipoprotein receptor- related protein and very-low-density lipoprotein receptor involves basic residues in the inhibitor. Biochem J 1998; 329 Part 1: 55-63.
    • (1998) Biochem. J. , vol.329 , Issue.PART 1 , pp. 55-63
    • Rodenburg, K.W.1    Kjoller, L.2    Petersen, H.H.3
  • 49
    • 0035210951 scopus 로고    scopus 로고
    • Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms
    • Hansen M, Busse MN, Andreasen PA. Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms. Eur J Biochem 2001; 268: 6274-83.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6274-6283
    • Hansen, M.1    Busse, M.N.2    Andreasen, P.A.3
  • 50
    • 0034040240 scopus 로고    scopus 로고
    • Glycosylation dependent conformational transitions in plasminogen activator inhibitor-1: Evidence for the presence of two active conformations
    • Gils A, Knockaert I, Brouwers E, et al. Glycosylation dependent conformational transitions in plasminogen activator inhibitor-1: Evidence for the presence of two active conformations. Fibrinolysis Proteolysis 2000; 14: 58-64.
    • (2000) Fibrinolysis Proteolysis , vol.14 , pp. 58-64
    • Gils, A.1    Knockaert, I.2    Brouwers, E.3
  • 51
    • 0033018464 scopus 로고    scopus 로고
    • Solvent effects on activity and conformation of plasminogen activator inhibitor-1
    • Andreasen PA, Egelund R, Jensen S, et al. Solvent effects on activity and conformation of plasminogen activator inhibitor-1. Thromb Haemost 1999; 81: 407-14.
    • (1999) Thromb. Haemost. , vol.81 , pp. 407-414
    • Andreasen, P.A.1    Egelund, R.2    Jensen, S.3
  • 52
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman CM, Loskutoff DJ. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J Biol Chem 1985; 260: 11581-7.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 53
    • 0026664170 scopus 로고
    • Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a noninhibitory substrate for tissue-type plasminogen activator
    • Declerck PJ, De Mol M, Vaughan DE, et al. Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a noninhibitory substrate for tissue-type plasminogen activator. J Biol Chem 1992; 267: 11693-6.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11693-11696
    • Declerck, P.J.1    De Mol, M.2    Vaughan, D.E.3
  • 54
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • Aertgeerts K, De Bondt HL, De Ranter C, et al. Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat Struct Biol 1995: 2(10): 891-7.
    • (1995) Nat. Struct. Biol. , vol.2 , Issue.10 , pp. 891-897
    • Aertgeerts, K.1    De Bondt, H.L.2    De Ranter, C.3
  • 55
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • Sharp AM, Stein PE, Pannu NS, et al. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure Fold Des 1999; 7: 111-8.
    • (1999) Structure Fold Des. , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3
  • 56
    • 0034737309 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation
    • Nar H, Bauer M, Stassen JM, et al. Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. J Mol Biol 2000; 297: 683-95.
    • (2000) J. Mol. Biol. , vol.297 , pp. 683-695
    • Nar, H.1    Bauer, M.2    Stassen, J.M.3
  • 57
    • 0034713878 scopus 로고    scopus 로고
    • Structures of active and latent PAI-1: A possible stabilizing role for chloride ions
    • Stout TJ, Graham H, Buckley DI, et al. Structures of active and latent PAI-1: A possible stabilizing role for chloride ions. Biochemistry 2000; 39: 8460-9.
    • (2000) Biochemistry , vol.39 , pp. 8460-8469
    • Stout, T.J.1    Graham, H.2    Buckley, D.I.3
  • 58
    • 0026546881 scopus 로고
    • Structural basis of latency in plasminogen activator inhibitor-1
    • Mottonen J, Strand A, Symersky J, et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature 1992; 355: 270-3.
    • (1992) Nature , vol.355 , pp. 270-273
    • Mottonen, J.1    Strand, A.2    Symersky, J.3
  • 59
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas MB, Lawrence DA, Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J 1995; 14: 2969-77.
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 60
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin)
    • Declerck PJ, De Mol M, Alessi MC,et al. Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J Biol Chem 1988; 263: 15454-61.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3
  • 61
    • 0024321164 scopus 로고
    • Affinity purification of active plasminogen activator inhibitor-1 (PAI-1) using immobilized anhydrourokinase. Demonstration of the binding, stabilization, and activation of PAI-1 by vitronectin
    • Wun TC, Palmier MO, Siegel NR, et al. Affinity purification of active plasminogen activator inhibitor-1 (PAI-1) using immobilized anhydrourokinase. Demonstration of the binding, stabilization, and activation of PAI-1 by vitronectin. J Biol Chem 1989; 264: 7862-8.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7862-7868
    • Wun, T.C.1    Palmier, M.O.2    Siegel, N.R.3
  • 62
    • 0025347305 scopus 로고
    • Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties
    • Ehrlich AJ, Gebbink RK, Keijer J, et al. Alteration of serpin specificity by a protein cofactor. Vitronectin endows plasminogen activator inhibitor 1 with thrombin inhibitory properties. J Biol Chem 1990; 265: 13029-35.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13029-13035
    • Ehrlich, A.J.1    Gebbink, R.K.2    Keijer, J.3
  • 63
    • 0027272044 scopus 로고
    • Kinetics of inactivation of alpha-thrombin by plasminogen activator inhibitor-1. Comparison of the effects of native and urea-treated forms of vitronectin
    • Naski MC, Lawrence DA, Mosher DF, et al. Kinetics of inactivation of alpha-thrombin by plasminogen activator inhibitor-1. Comparison of the effects of native and urea-treated forms of vitronectin. J Biol Chem 1993; 268: 12367-72.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12367-12372
    • Naski, M.C.1    Lawrence, D.A.2    Mosher, D.F.3
  • 64
    • 0035844272 scopus 로고    scopus 로고
    • Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1 - Implications for the mechanism of profibrinolytic action of activated protein C
    • Rezaie AR. Vitronectin functions as a cofactor for rapid inhibition of activated protein C by plasminogen activator inhibitor-1 - Implications for the mechanism of profibrinolytic action of activated protein C. J Biol Chem 2001; 276: 15567-70.
    • (2001) J. Biol. Chem. , vol.276 , pp. 15567-15570
    • Rezaie, A.R.1
  • 65
    • 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
    • Lawrence DA, Palaniappan S, Stefansson S, et al. 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 1997; 272: 7676-80.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7676-7680
    • Lawrence, D.A.1    Palaniappan, S.2    Stefansson, S.3
  • 66
    • 0028339118 scopus 로고
    • Localization of vitronectin binding domain in plasminogen activator inhibitor-1
    • Lawrence DA, Berkenpas MB, Palaniappan S, et al. Localization of vitronectin binding domain in plasminogen activator inhibitor-1. J Biol Chem 1994; 269: 15223-8.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15223-15228
    • Lawrence, D.A.1    Berkenpas, M.B.2    Palaniappan, S.3
  • 67
    • 0027963421 scopus 로고
    • Determination of the vitronectin binding site on plasminogen activator inhibitor 1 (PAI-1)
    • van Meijer M, Gebbink RK, Preissner KT, et al. Determination of the vitronectin binding site on plasminogen activator inhibitor 1 (PAI-1). FEBS Lett 1994; 352: 342-6.
    • (1994) FEBS Lett. , vol.352 , pp. 342-346
    • van Meijer, M.1    Gebbink, R.K.2    Preissner, K.T.3
  • 68
    • 0029026675 scopus 로고
    • Localization of a vitronectin binding region of plasminogen activator inhibitor-1
    • Padmanabhan J, Sane DC. Localization of a vitronectin binding region of plasminogen activator inhibitor-1. Thromb Haemost 1995; 73: 829-34.
    • (1995) Thromb. Haemost. , vol.73 , pp. 829-834
    • Padmanabhan, J.1    Sane, D.C.2
  • 69
    • 0036156207 scopus 로고    scopus 로고
    • Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin
    • Arroyo DP, Schroeck F, Sinner EK, et al. Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin. Eur J Biochem 2002; 269: 184-92.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 184-192
    • Arroyo, D.P.1    Schroeck, F.2    Sinner, E.K.3
  • 70
    • 0037134909 scopus 로고    scopus 로고
    • The vitronectin binding area of plasminogen activator inhibitor-1, mapped by mutagenesis and protection against an inactivating organochemical ligand
    • Jensen JK, Wind T, Andreasen PA. The vitronectin binding area of plasminogen activator inhibitor-1, mapped by mutagenesis and protection against an inactivating organochemical ligand. FEBS Lett 2002; 521: 91-4.
    • (2002) FEBS Lett. , vol.521 , pp. 91-94
    • Jensen, J.K.1    Wind, T.2    Andreasen, P.A.3
  • 71
    • 0037743532 scopus 로고    scopus 로고
    • How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration
    • Zhou A, Huntington JA, Pannu NS, et al. How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration. Nat Struct Biol 2003; 10: 541-4.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 541-544
    • Zhou, A.1    Huntington, J.A.2    Pannu, N.S.3
  • 72
    • 0347355503 scopus 로고    scopus 로고
    • Construction of a plasminogen activator inhibitor-1 variant without measurable affinity to vitronectin but otherwise normal
    • Jensen JK, Durand KV, Skeldal S, et al. Construction of a plasminogen activator inhibitor-1 variant without measurable affinity to vitronectin but otherwise normal. FEBS Lett 2004; 556: 175-9.
    • (2004) FEBS Lett. , vol.556 , pp. 175-179
    • Jensen, J.K.1    Durand, K.V.2    Skeldal, S.3
  • 73
    • 0025788321 scopus 로고
    • Mechanism of serpin action: Evidence that C1 inhibitor functions as a suicide substrate
    • Patston PA, Gettins P, Beechem J, et al. Mechanism of serpin action: Evidence that C1 inhibitor functions as a suicide substrate. Biochemistry 1991; 30: 8876-82.
    • (1991) Biochemistry , vol.30 , pp. 8876-8882
    • Patston, P.A.1    Gettins, P.2    Beechem, J.3
  • 74
    • 0030973123 scopus 로고    scopus 로고
    • Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1
    • Gils A, Declerck PJ. Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor 1. J Biol Chem 1997; 272: 12662-6.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12662-12666
    • Gils, A.1    Declerck, P.J.2
  • 75
    • 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
    • De Taeye B, Compernolle G, Dewilde M, et al. 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 2003; 278: 23899-905.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23899-23905
    • De Taeye, B.1    Compernolle, G.2    Dewilde, M.3
  • 76
    • 0025990175 scopus 로고
    • On the target specificity of plasminogen activator inhibitor 1: The role of heparin, vitronectin, and the reactive site
    • Keijer J, Linders M, Wegman JJ, et al. On the target specificity of plasminogen activator inhibitor 1: The role of heparin, vitronectin, and the reactive site. Blood 1991; 78: 1254-61.
    • (1991) Blood , vol.78 , pp. 1254-1261
    • Keijer, J.1    Linders, M.2    Wegman, J.J.3
  • 77
    • 0021985069 scopus 로고
    • 1-Antitrypsin and the serpins: Variation and countervariation
    • 1-Antitrypsin and the serpins: variation and countervariation. TIBS 1985; 20-4.
    • (1985) TIBS , pp. 20-24
    • Carrell, R.1    Travis, J.2
  • 78
    • 0026783247 scopus 로고
    • Saturation mutagenesis of the plasminogen activator inhibitor-1 reactive center
    • Sherman PM, Lawrence DA, Yang AY, et al. Saturation mutagenesis of the plasminogen activator inhibitor-1 reactive center. J Biol Chem 1992; 267: 7588-95.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7588-7595
    • Sherman, P.M.1    Lawrence, D.A.2    Yang, A.Y.3
  • 79
    • 0028918245 scopus 로고
    • Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity
    • Sherman PM, Lawrence DA, Verhamme IM, et al. Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity. J Biol Chem 1995; 270: 9301-6.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9301-9306
    • Sherman, P.M.1    Lawrence, D.A.2    Verhamme, I.M.3
  • 80
    • 0025917199 scopus 로고
    • Combinatorial mutagenesis of the reactive site region in plasminogen activator inhibitor 1
    • York JD, Li P, Gardell SJ. Combinatorial mutagenesis of the reactive site region in plasminogen activator inhibitor 1. J Biol Chem 1991; 266: 8495-500.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8495-8500
    • York, J.D.1    Li, P.2    Gardell, S.J.3
  • 81
    • 0028829502 scopus 로고
    • Time-resolved polarized fluorescence spectroscopy studies of plasminogen activator inhibitor type 1: Conformational changes of the reactive center upon interactions with target proteases, vitronectin and heparin
    • Fa M, Karolin J, Aleshkov S, et al. Time-resolved polarized fluorescence spectroscopy studies of plasminogen activator inhibitor type 1: Conformational changes of the reactive center upon interactions with target proteases, vitronectin and heparin. Biochemistry 1995; 34: 13833-40.
    • (1995) Biochemistry , vol.34 , pp. 13833-13840
    • Fa, M.1    Karolin, J.2    Aleshkov, S.3
  • 82
    • 0023923568 scopus 로고
    • Kinetics of the inhibition of plasminogen activators by the plasminogen-activator inhibitor. Evidence for 'second-site' interactions
    • Chmielewska J, Ranby M, Wiman B. Kinetics of the inhibition of plasminogen activators by the plasminogen-activator inhibitor. Evidence for 'second-site' interactions. Biochem J 1988; 251: 327-32.
    • (1988) Biochem. J. , vol.251 , pp. 327-332
    • Chmielewska, J.1    Ranby, M.2    Wiman, B.3
  • 83
    • 0023883856 scopus 로고
    • Bovine plasminogen activator inhibitor 1: Specificity determinations and comparison of the active, latent, and guanidine-activated forms
    • Hekman CM, Loskutoff DJ. Bovine plasminogen activator inhibitor 1: Specificity determinations and comparison of the active, latent, and guanidine-activated forms. Biochemistry 1988; 27: 2911-8.
    • (1988) Biochemistry , vol.27 , pp. 2911-2918
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 84
    • 0025227854 scopus 로고
    • Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants
    • Lawrence DA, Strandberg L, Ericson J, et al. Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants. J Biol Chem 1990; 265: 20293-301.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20293-20301
    • Lawrence, D.A.1    Strandberg, L.2    Ericson, J.3
  • 85
    • 0024381603 scopus 로고
    • Serpin-resistant mutants of human tissue-type plasminogen activator
    • Madison EL, Goldsmith EJ, Gerard RD, et al. Serpin-resistant mutants of human tissue-type plasminogen activator. Nature 1989; 339: 721-4.
    • (1989) Nature , vol.339 , pp. 721-724
    • Madison, E.L.1    Goldsmith, E.J.2    Gerard, R.D.3
  • 86
    • 0025597970 scopus 로고
    • Restoration of serine protease-inhibitor interaction by protein engineering
    • Madison EL, Goldsmith EJ, Gething MJ, et al. Restoration of serine protease-inhibitor interaction by protein engineering. J Biol Chem 1990; 265: 21423-6.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21423-21426
    • Madison, E.L.1    Goldsmith, E.J.2    Gething, M.J.3
  • 87
    • 0029875848 scopus 로고    scopus 로고
    • Sequence requirements in the reactive-center loop of plasminogen- activator inhibitor-1 for recognition of plasminogen activators
    • Tucker HM, Gerard RD. Sequence requirements in the reactive-center loop of plasminogen- activator inhibitor-1 for recognition of plasminogen activators. Eur J Biochem 1996; 237: 180-7.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 180-187
    • Tucker, H.M.1    Gerard, R.D.2
  • 88
    • 0035911151 scopus 로고    scopus 로고
    • The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin: Implications for antiangiogenic strategies
    • Bajou K, Masson V, Gerard RD, et al. The plasminogen activator inhibitor PAI-1 controls in vivo tumor vascularization by interaction with proteases, not vitronectin: Implications for antiangiogenic strategies. J Cell Biol 2001; 152: 777-84.
    • (2001) J. Cell Biol. , vol.152 , pp. 777-784
    • Bajou, K.1    Masson, V.2    Gerard, R.D.3
  • 89
    • 18244389007 scopus 로고    scopus 로고
    • The pro-or antiangiogenic effect of plasminogen activator inhibitor 1 is dose dependent
    • Devy L, Blacher S, Grignet-Debrus C, et al. The pro-or antiangiogenic effect of plasminogen activator inhibitor 1 is dose dependent. FASEB J 2002; 16: 147-54.
    • (2002) FASEB J. , vol.16 , pp. 147-154
    • Devy, L.1    Blacher, S.2    Grignet-Debrus, C.3
  • 90
    • 0034014726 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor 1 may promote tumour growth through inhibition of apoptosis
    • Kwaan HC, Wang J, Svoboda K, et al. Plasminogen activator inhibitor 1 may promote tumour growth through inhibition of apoptosis. Br J Cancer 2000; 82: 1702-8.
    • (2000) Br. J. Cancer , vol.82 , pp. 1702-1708
    • Kwaan, H.C.1    Wang, J.2    Svoboda, K.3
  • 91
    • 0034667385 scopus 로고    scopus 로고
    • Tumor development is retarded in mice lacking the gene for urokinase-type plasminogen activator or its inhibitor, plasminogen activator inhibitor-1
    • Gutierrez LS, Schulman A, Brito RT, et al. Tumor development is retarded in mice lacking the gene for urokinase-type plasminogen activator or its inhibitor, plasminogen activator inhibitor-1. Cancer Res 2000; 60: 5839-47.
    • (2000) Cancer Res. , vol.60 , pp. 5839-5847
    • Gutierrez, L.S.1    Schulman, A.2    Brito, R.T.3
  • 92
    • 0031902286 scopus 로고    scopus 로고
    • Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization
    • Bajou K, Noel A, Gerard RD, et al, Absence of host plasminogen activator inhibitor 1 prevents cancer invasion and vascularization. Nat Med 1998; 4: 923-8.
    • (1998) Nat. Med. , vol.4 , pp. 923-928
    • Bajou, K.1    Noel, A.2    Gerard, R.D.3
  • 93
    • 0034791672 scopus 로고    scopus 로고
    • Plasmin-dependent and -independent effects of plasminogen activators and inhibitor-1 on ex vivo angiogenesis
    • Brodsky S, Chen J, Lee A, et al. Plasmin-dependent and -independent effects of plasminogen activators and inhibitor-1 on ex vivo angiogenesis. Am J Physiol Heart Circ Physiol 2001; 281: H1784-H1792.
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Brodsky, S.1    Chen, J.2    Lee, A.3
  • 94
    • 12144289397 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 and tumour growth, invasion, and metastasis
    • Durand MKV, Bødker JS, Christensen A, et al. Plasminogen activator inhibitor-1 and tumour growth, invasion, and metastasis. Thromb Haemost 2004; 91: 438-49.
    • (2004) Thromb. Haemost. , vol.91 , pp. 438-449
    • Durand, M.K.V.1    Bødker, J.S.2    Christensen, A.3
  • 95
    • 1642375334 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1: Novel tumor-derived factors with a high prognostic and predictive impact in breast cancer
    • Harbeck N, Kates RE, Gauger K, et al. Urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1: Novel tumor-derived factors with a high prognostic and predictive impact in breast cancer. Thromb Haemost 2004; 91: 450-6.
    • (2004) Thromb. Haemost. , vol.91 , pp. 450-456
    • Harbeck, N.1    Kates, R.E.2    Gauger, K.3
  • 96
    • 0021677450 scopus 로고
    • Detection and partial characterization of an inhibitor of plasminogen activator in human platelets
    • Erickson LA, Ginsberg MH, Loskutoff DJ. Detection and partial characterization of an inhibitor of plasminogen activator in human platelets. J Clin Invest 1984; 74: 1465-72.
    • (1984) J. Clin. Invest. , vol.74 , pp. 1465-1472
    • Erickson, L.A.1    Ginsberg, M.H.2    Loskutoff, D.J.3
  • 97
    • 0024558517 scopus 로고
    • Bleeding diathesis due to decreased functional activity of type 1 plasminogen activator inhibitor
    • Schleef RR, Higgins DL, Pillemer E, et al. Bleeding diathesis due to decreased functional activity of type 1 plasminogen activator inhibitor. J Clin Invest 1989; 83: 1747-52.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1747-1752
    • Schleef, R.R.1    Higgins, D.L.2    Pillemer, E.3
  • 98
    • 0025971596 scopus 로고
    • A lifelong bleeding disorder associated with a deficiency of plasminogen activator inhibitor type 1
    • Dieval J, Nguyen G, Gross S, et al. A lifelong bleeding disorder associated with a deficiency of plasminogen activator inhibitor type 1. Blood 1991; 77: 528-32.
    • (1991) Blood , vol.77 , pp. 528-532
    • Dieval, J.1    Nguyen, G.2    Gross, S.3
  • 99
    • 0027274012 scopus 로고
    • Deficiency of plasma plasminogen activator inhibitor 1 results in hyperfibrinolytic bleeding
    • Lee MH, Vosburgh E, Anderson K, et al. Deficiency of plasma plasminogen activator inhibitor 1 results in hyperfibrinolytic bleeding. Blood 1993; 81: 2357-62.
    • (1993) Blood , vol.81 , pp. 2357-2362
    • Lee, M.H.1    Vosburgh, E.2    Anderson, K.3
  • 100
    • 0030997665 scopus 로고    scopus 로고
    • Human plasminogen activator inhibitor 1 (pai 1) deficiency: Characterization of a large kindred with a null mutation in the pai 1 gene
    • Fay WP, Parker AC, Condrey LR, et al. Human plasminogen activator inhibitor 1 (pai 1) deficiency: Characterization of a large kindred with a null mutation in the pai 1 gene. Blood 1997; 90: 204-8.
    • (1997) Blood , vol.90 , pp. 204-208
    • Fay, W.P.1    Parker, A.C.2    Condrey, L.R.3
  • 101
    • 0343239034 scopus 로고    scopus 로고
    • Four cases of bleeding diathesis in children due to congenital plasminogen activator inhibitor-1 deficiency
    • Minowa H, Takahashi Y, Tanaka T, et al. Four cases of bleeding diathesis in children due to congenital plasminogen activator inhibitor-1 deficiency. Haemostasis 1999; 29: 286-91.
    • (1999) Haemostasis , vol.29 , pp. 286-291
    • Minowa, H.1    Takahashi, Y.2    Tanaka, T.3
  • 102
    • 0023185776 scopus 로고
    • Plasminogen activator inhibitor in plasma: Risk factor for recurrent myocardial infarction
    • Hamsten A, de Faire U, Walldius G, et al. Plasminogen activator inhibitor in plasma: Risk factor for recurrent myocardial infarction. Lancet 1987; 2: 3-9.
    • (1987) Lancet , vol.2 , pp. 3-9
    • Hamsten, A.1    de Faire, U.2    Walldius, G.3
  • 103
    • 0027441963 scopus 로고
    • Fibrinolytic activity, clotting factors, and long-term incidence of ischaemic heart disease in the Northwick Park Heart Study
    • [see comments]
    • Meade TW, Ruddock V, Stirling Y, et al. Fibrinolytic activity, clotting factors, and long-term incidence of ischaemic heart disease in the Northwick Park Heart Study [see comments]. Lancet 1993; 342: 1076-9.
    • (1993) Lancet , vol.342 , pp. 1076-1079
    • Meade, T.W.1    Ruddock, V.2    Stirling, Y.3
  • 104
    • 0028909230 scopus 로고
    • Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris
    • European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group
    • Thompson SG, Kienast J, Pyke SD, et al. Hemostatic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. European Concerted Action on Thrombosis and Disabilities Angina Pectoris Study Group. N Engl J Med 1995; 332: 635-41.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 635-641
    • Thompson, S.G.1    Kienast, J.2    Pyke, S.D.3
  • 105
    • 0029805074 scopus 로고    scopus 로고
    • Fibrinolytic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris
    • Julian Vague I, Pyke SDM, Alessi MC, et al. Fibrinolytic factors and the risk of myocardial infarction or sudden death in patients with angina pectoris. Circulation 1996; 94: 2057-63.
    • (1996) Circulation , vol.94 , pp. 2057-2063
    • Julian Vague, I.1    Pyke, S.D.M.2    Alessi, M.C.3
  • 106
    • 0035051534 scopus 로고    scopus 로고
    • Prospective study of fibrinolytic factors and incident coronary heart disease - The Atherosclerosis Risk in Communities (ARIC) Study
    • Folsom AR, Aleksik N, Park E, et al. Prospective study of fibrinolytic factors and incident coronary heart disease - The Atherosclerosis Risk in Communities (ARIC) Study. Arterioscler Thromb Vasc Biol 2001; 21: 611-7.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 611-617
    • Folsom, A.R.1    Aleksik, N.2    Park, E.3
  • 107
    • 0035432902 scopus 로고    scopus 로고
    • Disruption of the plasminogen activator inhibitor-1 gene reduces the adiposity and improves the metabolic profile of genetically obese and diabetic ob/ob mice
    • Schafer K, Fujisawa K, Konstantinides S, et al. Disruption of the plasminogen activator inhibitor-1 gene reduces the adiposity and improves the metabolic profile of genetically obese and diabetic ob/ob mice. FASEB Journal 2001; 15: 1840-2.
    • (2001) FASEB Journal , vol.15 , pp. 1840-1842
    • Schafer, K.1    Fujisawa, K.2    Konstantinides, S.3
  • 108
    • 0026650622 scopus 로고
    • Increased type 1 plasminogen activator inhibitor gene expression in atherosclerotic human arteries
    • Schneiderman J, Sawdey MS, Keeton MR, et al. Increased type 1 plasminogen activator inhibitor gene expression in atherosclerotic human arteries. Proc Natl Acad Sci U S A 1992; 89: 6998-7002.
    • (1992) Proc. Natl. Acad. Sci. U S A , vol.89 , pp. 6998-7002
    • Schneiderman, J.1    Sawdey, M.S.2    Keeton, M.R.3
  • 109
    • 0029112387 scopus 로고
    • Plasminogen activator expression in human atherosclerotic lesions
    • Lupu F, Heim DA, Bachmann F, et al. Plasminogen activator expression in human atherosclerotic lesions. Arterioscler Thromb Vasc Biol 1995; 15: 1444-55.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1444-1455
    • Lupu, F.1    Heim, D.A.2    Bachmann, F.3
  • 111
    • 0028901713 scopus 로고
    • Allele-specific increase in basal transcription of the plasminogen-activator inhibitor 1 gene is associated with myocardial infarction
    • Eriksson P, Kallin B, van 't Hooft FM, et al. Allele-specific increase in basal transcription of the plasminogen-activator inhibitor 1 gene is associated with myocardial infarction. Proc Natl Acad Sci U S A 1995; 92: 1851-5.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 1851-1855
    • Eriksson, P.1    Kallin, B.2    van't Hooft, F.M.3
  • 112
    • 0031016432 scopus 로고    scopus 로고
    • Arterial and venous thrombosis is not associated with the 4g/5g polymorphism in the promoter of the plasminogen activator inhibitor gene in a large cohort of us men
    • Ridker PM, Hennekens CH, Lindpaintner K, et al. Arterial and venous thrombosis is not associated with the 4g/5g polymorphism in the promoter of the plasminogen activator inhibitor gene in a large cohort of us men. Circulation 1997; 95: 59-62.
    • (1997) Circulation , vol.95 , pp. 59-62
    • Ridker, P.M.1    Hennekens, C.H.2    Lindpaintner, K.3
  • 113
    • 2642692693 scopus 로고    scopus 로고
    • A common 4G allele in the promoter of the plasminogen activator inhibitor-1 (PAI-1) gene as a risk factor for pulmonary embolism and arterial thrombosis in hereditary protein S deficiency
    • Zoller B, Garcia-de-Frutos P, Dahlback B. A common 4G allele in the promoter of the plasminogen activator inhibitor-1 (PAI-1) gene as a risk factor for pulmonary embolism and arterial thrombosis in hereditary protein S deficiency. Thromb Haemost 1998; 79: 802-7.
    • (1998) Thromb. Haemost. , vol.79 , pp. 802-807
    • Zoller, B.1    Garcia-de-Frutos, P.2    Dahlback, B.3
  • 114
    • 0031984392 scopus 로고    scopus 로고
    • Metabolic determinants are much more important than genetic polymorphisms in determining the PAI-1 activity and antigen plasma concentrations: A family study with part of the Stanislas Cohort
    • Henry M, Tregouet DA, Alessi MC, et al. Metabolic determinants are much more important than genetic polymorphisms in determining the PAI-1 activity and antigen plasma concentrations: A family study with part of the Stanislas Cohort. Arterioscler Thromb Vasc Biol 1998; 18: 84-91.
    • (1998) Arterioscler. Thromb. Vasc. Biol. , vol.18 , pp. 84-91
    • Henry, M.1    Tregouet, D.A.2    Alessi, M.C.3
  • 115
    • 1642382493 scopus 로고    scopus 로고
    • The plasminogen activator inhibitor-1 -675 4G/5G genotype influences the risk of myocardial infarction associated with elevated plasma proinsulin and insulin concentrations in men from Europe: The HIFMECH Study
    • Juhan-Vague I, Morange PE, Frere C, et al. The plasminogen activator inhibitor-1 -675 4G/5G genotype influences the risk of myocardial infarction associated with elevated plasma proinsulin and insulin concentrations in men from Europe: The HIFMECH Study. J Thromb Haemost 2003; 1: 2322-9.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2322-2329
    • Juhan-Vague, I.1    Morange, P.E.2    Frere, C.3
  • 116
    • 0027311245 scopus 로고
    • The two allele sequences of a common polymorphism in the promoter of the plasminogen activator inhibitor-1 (PAI-1) gene respond differently to interleukin-1 in HepG2 cells
    • Dawson SJ, Wiman B, Hamsten A, et al. The two allele sequences of a common polymorphism in the promoter of the plasminogen activator inhibitor-1 (PAI-1) gene respond differently to interleukin-1 in HepG2 cells. J Biol Chem 1993; 268: 10739-45.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10739-10745
    • Dawson, S.J.1    Wiman, B.2    Hamsten, A.3
  • 117
    • 0027267328 scopus 로고
    • Stimulation of plasminogen activator inhibitor in vivo by infusion of angiotensin II. Evidence of a potential interaction between the renin-angiotensin system and fibrinolytic function
    • Ridker PM, Gaboury CL, Conlin PR, et al. Stimulation of plasminogen activator inhibitor in vivo by infusion of angiotensin II. Evidence of a potential interaction between the renin-angiotensin system and fibrinolytic function. Circulation 1993; 87: 1969-73.
    • (1993) Circulation , vol.87 , pp. 1969-1973
    • Ridker, P.M.1    Gaboury, C.L.2    Conlin, P.R.3
  • 119
    • 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, 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
  • 120
    • 0025731989 scopus 로고
    • High resolution analysis of functional determinants on human tissue-type plasminogen activator
    • Bennett WF, Paoni NF, Keyt BA, 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
  • 121
    • 0034616216 scopus 로고    scopus 로고
    • Identification of the mechanism responsible for the increased fibrin specificity of TNK-tissue plasminogen activator relative to tissue plasminogen activator
    • Stewart RJ, Fredenburgh JC, Leslie BA, et al. Identification of the mechanism responsible for the increased fibrin specificity of TNK-tissue plasminogen activator relative to tissue plasminogen activator, J Biol Chem 2000; 275: 10112-20.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10112-10120
    • Stewart, R.J.1    Fredenburgh, J.C.2    Leslie, B.A.3
  • 122
    • 0035578092 scopus 로고    scopus 로고
    • Safety of the weight-adjusted dosing regimen of tenecteplase in the ASSENT-Trial
    • Angeja BG, Alexander JH, Chin R, et al. Safety of the weight-adjusted dosing regimen of tenecteplase in the ASSENT-Trial. Am J Cardiol 2001; 88: 1240-5.
    • (2001) Am. J. Cardiol. , vol.88 , pp. 1240-1245
    • Angeja, B.G.1    Alexander, J.H.2    Chin, R.3
  • 123
    • 18244376408 scopus 로고    scopus 로고
    • Incidence and predictors of bleeding events after fibrinolytic therapy with fibrin-specific agents: A comparison of TNK-tPA and rt-PA
    • Van de Werf F, Barron HV, Armstrong PW, et al. Incidence and predictors of bleeding events after fibrinolytic therapy with fibrin-specific agents: A comparison of TNK-tPA and rt-PA. Eur Heart J 2001; 22: 2253-61.
    • (2001) Eur. Heart J. , vol.22 , pp. 2253-2261
    • Van de Werf, F.1    Barron, H.V.2    Armstrong, P.W.3
  • 124
    • 0035169698 scopus 로고    scopus 로고
    • Determination of a weight-adjusted dose of TNK-tissue plasminogen activator
    • Wang-Clow F, Fox NL, Cannon CP, et al. Determination of a weight-adjusted dose of TNK-tissue plasminogen activator. Am Heart J 2001; 141: 33-40.
    • (2001) Am. Heart J. , vol.141 , pp. 33-40
    • Wang-Clow, F.1    Fox, N.L.2    Cannon, C.P.3
  • 125
    • 0037329323 scopus 로고    scopus 로고
    • Comparative fibrinolytic activity of front-loaded alteplase and the single-bolus mutants tenecteplase and lanoteplase during treatment of acute myocardial infarction
    • Al Shwafi KA, de Meester A, Pirenne B, et al. Comparative fibrinolytic activity of front-loaded alteplase and the single-bolus mutants tenecteplase and lanoteplase during treatment of acute myocardial infarction. Am Heart J 2003; 145: 217-25.
    • (2003) Am. Heart J. , vol.145 , pp. 217-225
    • Al Shwafi, K.A.1    de Meester, A.2    Pirenne, B.3
  • 126
    • 0037385538 scopus 로고    scopus 로고
    • Effect of tenecteplase versus alteplase on platelets during the first 3 hours of treatment for acute myocardial infarction: The Assessment of the Safety and Efficacy of a New Thrombolytic Agent (ASSENT-2) platelet substudy
    • Serebruany VL, Malinin AI, Callahan KP, et al. Effect of tenecteplase versus alteplase on platelets during the first 3 hours of treatment for acute myocardial infarction: The Assessment of the Safety and Efficacy of a New Thrombolytic Agent (ASSENT-2) platelet substudy. Am Heart J 2003; 145: 636-42.
    • (2003) Am. Heart J. , vol.145 , pp. 636-642
    • Serebruany, V.L.1    Malinin, A.I.2    Callahan, K.P.3
  • 127
    • 0025371467 scopus 로고
    • Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene
    • Erickson LA, Fici GJ, Lund JE, et al. Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene. Nature 1990; 346: 74-6.
    • (1990) Nature , vol.346 , pp. 74-76
    • Erickson, L.A.1    Fici, G.J.2    Lund, J.E.3
  • 128
    • 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
    • Eren M, Painter CA, Atkinson JB, et al. Age-dependent spontaneous coronary arterial thrombosis in transgenic mice that express a stable form of human plasminogen activator inhibitor-1. Circulation 2002; 106: 491-6.
    • (2002) Circulation , vol.106 , pp. 491-496
    • Eren, M.1    Painter, C.A.2    Atkinson, J.B.3
  • 129
    • 0027144754 scopus 로고
    • Plasminogen activator inhibitor-1 gene-deficient mice. I. Generation by homologous recombination and characterization
    • Carmeliet P, Kieckens L, Schoonjans L, et al. Plasminogen activator inhibitor-1 gene-deficient mice. I. Generation by homologous recombination and characterization. J Clin Invest 1993; 92: 2746-55.
    • (1993) J. Clin. Invest. , vol.92 , pp. 2746-2755
    • Carmeliet, P.1    Kieckens, L.2    Schoonjans, L.3
  • 130
    • 0029583657 scopus 로고
    • Vitronectin is not essential for normal mammalian development and fertility
    • Zheng X, Saunders TL, Camper SA, et al. Vitronectin is not essential for normal mammalian development and fertility. Proc Natl Acad Sci U S A 1995; 92: 12426-30.
    • (1995) Proc. Natl. Acad. Sci. U S A , vol.92 , pp. 12426-12430
    • Zheng, X.1    Saunders, T.L.2    Camper, S.A.3
  • 131
    • 0034650976 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 and vitronectin promote vascular thrombosis in mice
    • Eitzman DT, Westrick RJ, Nabel EG, et al. Plasminogen activator inhibitor-1 and vitronectin promote vascular thrombosis in mice. Blood 2000; 95: 577-80.
    • (2000) Blood , vol.95 , pp. 577-580
    • Eitzman, D.T.1    Westrick, R.J.2    Nabel, E.G.3
  • 132
    • 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]
    • Levi M, Biemond BJ, van Zonneveld AJ, et al. 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 1992; 85: 305-12.
    • (1992) Circulation , vol.85 , pp. 305-312
    • Levi, M.1    Biemond, B.J.2    van Zonneveld, A.J.3
  • 133
    • 0027213980 scopus 로고
    • Definition of epitopes within plasminogen activator inhibitor type-1 (PAI-1) using multiple peptide synthesis
    • Perrie AM, MacGregor IR, Booth NA. Definition of epitopes within plasminogen activator inhibitor type-1 (PAI-1) using multiple peptide synthesis. Fibrinolysis 1993; 7: 257-63.
    • (1993) Fibrinolysis , vol.7 , pp. 257-263
    • Perrie, A.M.1    MacGregor, I.R.2    Booth, N.A.3
  • 134
    • 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
    • Biemond BJ, Levi M, Coronel R, et al. Thrombolysis and reocclusion in experimental jugular vein and coronary artery thrombosis, Effects of a plasminogen activator inhibitor type 1-neutralizing monoclonal antibody. Circulation 1995; 91: 1175-81.
    • (1995) Circulation , vol.91 , pp. 1175-1181
    • Biemond, B.J.1    Levi, M.2    Coronel, R.3
  • 135
    • 0031031869 scopus 로고    scopus 로고
    • Neutralization of plasminogen activator inhibitor-1 inhibitory properties: Identification of two different mechanisms
    • Debrock S, Declerck PJ. Neutralization of plasminogen activator inhibitor-1 inhibitory properties: Identification of two different mechanisms. Biochim Biophys Acta 1997; 1337: 257-66.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 257-266
    • Debrock, S.1    Declerck, P.J.2
  • 136
    • 0031708331 scopus 로고    scopus 로고
    • Antithrombotic activity of a monoclonal antibody inducing the substrate form of plasminogen activator inhibitor type 1 in rat models of venous and arterial thrombosis
    • Berry CN, Lunven C, Lechaire I, et al. Antithrombotic activity of a monoclonal antibody inducing the substrate form of plasminogen activator inhibitor type 1 in rat models of venous and arterial thrombosis. Br J Pharmacol 1998; 125: 29-34.
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 29-34
    • Berry, C.N.1    Lunven, C.2    Lechaire, I.3
  • 137
    • 0032418252 scopus 로고    scopus 로고
    • Suppression of plasminogen activator inhibitor 1 (PAI-1) activity levels in rats by monoclonal antibodies
    • Ngo TH, Declerck PJ. Suppression of plasminogen activator inhibitor 1 (PAI-1) activity levels in rats by monoclonal antibodies. Fibrinolysis Proteolysis 1998; 12: 335-9.
    • (1998) Fibrinolysis Proteolysis , vol.12 , pp. 335-339
    • Ngo, T.H.1    Declerck, P.J.2
  • 138
    • 0035977012 scopus 로고    scopus 로고
    • The distal hinge of the reactive site loop and its proximity: A target to modulate plasminogen activator inhibitor-1 activity
    • Bijnens AP, Gils A, Stassen JM, et al. The distal hinge of the reactive site loop and its proximity: A target to modulate plasminogen activator inhibitor-1 activity. J Biol Chem 2001; 276: 44912-8.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44912-44918
    • Bijnens, A.P.1    Gils, A.2    Stassen, J.M.3
  • 139
    • 0028832866 scopus 로고
    • The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A
    • Kvassman JO, Lawrence DA, Shore JD. The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A. J Biol Chem 1995; 270: 27942-7.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27942-27947
    • Kvassman, J.O.1    Lawrence, D.A.2    Shore, J.D.3
  • 140
    • 0028958184 scopus 로고
    • Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro
    • Eitzman DT, Fay WP, Lawrence DA, et al. Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro. J Clin Invest 1995; 95: 2416-20.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2416-2420
    • Eitzman, D.T.1    Fay, W.P.2    Lawrence, D.A.3
  • 141
    • 0032524769 scopus 로고    scopus 로고
    • Interfering with the inhibitory meachnism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide
    • Xue Y, Björquist P, Inghardt T, et al. Interfering with the inhibitory meachnism of serpins: Crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 1998; 6: 627-36.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Björquist, P.2    Inghardt, T.3
  • 142
    • 0242643928 scopus 로고    scopus 로고
    • Selection of peptides that bind to plasminogen activator inhibitor 1 (PAI-1) using random peptide phage-display libraries
    • Gardsvoll H, van-Zonneveld AJ, Holm A, et al. Selection of peptides that bind to plasminogen activator inhibitor 1 (PAI-1) using random peptide phage-display libraries. FEBS Lett 1998; 431: 170-4.
    • (1998) FEBS Lett. , vol.431 , pp. 170-174
    • Gardsvoll, H.1    van-Zonneveld, A.J.2    Holm, A.3
  • 143
    • 0029801041 scopus 로고    scopus 로고
    • Inhibition of plasminogen activator inhibitor 1 activity by two diketopiperazines, XR330 and XR334 produced by streptomyces sp
    • Bryans J, Charlton PR, Collins M, et al. Inhibition of plasminogen activator inhibitor 1 activity by two diketopiperazines, XR330 and XR334 produced by streptomyces sp. J Antibiot 1996; 49: 1014-21.
    • (1996) J. Antibiot. , vol.49 , pp. 1014-1021
    • Bryans, J.1    Charlton, P.R.2    Collins, M.3
  • 144
    • 0029894647 scopus 로고    scopus 로고
    • Evaluation of a low molecular weight modulator of human plasminogen activator inhibitor-1 activity
    • Charlton PA, Faint RW, Bent F, et al. Evaluation of a low molecular weight modulator of human plasminogen activator inhibitor-1 activity. Thromb Haemost 1996; 75: 808-15.
    • (1996) Thromb. Haemost. , vol.75 , pp. 808-815
    • Charlton, P.A.1    Faint, R.W.2    Bent, F.3
  • 145
    • 0030904328 scopus 로고    scopus 로고
    • XR5118, a novel modulator of plasminogen activator inhibitor 1 (PAI 1), increases endogenous tpa activity in the rat
    • Charlton P, Faint R, Barnes C, et al. XR5118, a novel modulator of plasminogen activator inhibitor 1 (PAI 1), increases endogenous tpa activity in the rat. Fibrinolysis & Proteolysis 1997; 11: 51-6.
    • (1997) Fibrinolysis & Proteolysis , vol.11 , pp. 51-56
    • Charlton, P.1    Faint, R.2    Barnes, C.3
  • 146
    • 0030857519 scopus 로고    scopus 로고
    • Novel low molecular weight inhibitor of pai-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits
    • Friederich PW, Levi MR, Biemond BJ, et al. Novel low molecular weight inhibitor of pai-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits. Circulation 1997; 96: 916-21.
    • (1997) Circulation , vol.96 , pp. 916-921
    • Friederich, P.W.1    Levi, M.R.2    Biemond, B.J.3
  • 147
    • 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
    • Bjorquist P, Ehnebom J, Inghardt T, et al. Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis. Biochemistry 1998; 37: 1227-34.
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Bjorquist, P.1    Ehnebom, J.2    Inghardt, T.3
  • 148
    • 0035829167 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of a series of diketopiperazine inhibitors of plasminogen activator inhibitor-1
    • Folkes A, Roe MB, Sohal S, et al. Synthesis and in vitro evaluation of a series of diketopiperazine inhibitors of plasminogen activator inhibitor-1. Bioorg Med Chem Lett 2001; 11: 2589-92.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 2589-2592
    • Folkes, A.1    Roe, M.B.2    Sohal, S.3
  • 149
    • 0035918137 scopus 로고    scopus 로고
    • A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands - Ligand-induced serpin polymerization
    • Egelund R, Einholm AP, Pedersen KE, et al. A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands - Ligand-induced serpin polymerization. J Biol Chem 2001; 276: 13077-86.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13077-13086
    • Egelund, R.1    Einholm, A.P.2    Pedersen, K.E.3
  • 150
    • 0036301837 scopus 로고    scopus 로고
    • Characterization and comparative evaluation of a novel PAI-1 inhibitor
    • Gils A, Stassen JM, Nar H, et al. Characterization and comparative evaluation of a novel PAI-1 inhibitor. Thromb Haemost 2002; 88: 137-43.
    • (2002) Thromb. Haemost. , vol.88 , pp. 137-143
    • Gils, A.1    Stassen, J.M.2    Nar, H.3
  • 152
    • 0031850760 scopus 로고    scopus 로고
    • Modulation of plasminogen activator inhibitor 1 by Triton X-100 - Identification of two consecutive conformational transitions
    • Gils A, Declerck PJ. Modulation of plasminogen activator inhibitor 1 by Triton X-100 - Identification of two consecutive conformational transitions. Thromb Haemost 1998; 80: 286-91.
    • (1998) Thromb. Haemost. , vol.80 , pp. 286-291
    • Gils, A.1    Declerck, P.J.2
  • 153
    • 0031457916 scopus 로고    scopus 로고
    • Stereodependent inhibition of plasminogen activator inhibitor type 1 by phosphorothioate oligonucleotides: Proof of sequence specificity in cell culture and in vivo rat experiments
    • Stec WJ, Cierniewski CS, Okruszek A, et al. Stereodependent inhibition of plasminogen activator inhibitor type 1 by phosphorothioate oligonucleotides: Proof of sequence specificity in cell culture and in vivo rat experiments. Antisense Nucleic Acid Drug Dev 1997; 7: 567-73.
    • (1997) Antisense Nucleic Acid Drug Dev. , vol.7 , pp. 567-573
    • Stec, W.J.1    Cierniewski, C.S.2    Okruszek, A.3
  • 154
    • 0022495806 scopus 로고
    • Monoclonal antibodies to human 54,000 molecular weight plasminogen activator inhibitor from fibrosarcoma cells- inhibitor neutralization and one-step affinity purification
    • Nielsen LS, Andreasen PA, Grondahl Hansen J, et al. Monoclonal antibodies to human 54,000 molecular weight plasminogen activator inhibitor from fibrosarcoma cells- inhibitor neutralization and one-step affinity purification. Thromb Haemost 1986; 55: 206-12.
    • (1986) Thromb. Haemost. , vol.55 , pp. 206-212
    • Nielsen, L.S.1    Andreasen, P.A.2    Grondahl Hansen, J.3
  • 155
    • 0025171921 scopus 로고
    • Murine monoclonal antibodies against active site epitopes on human endothelial plasminogen activator inhibibitor (PAI-1)
    • MacGregor IR, Tonner AM, Micklem LR, et al. Murine monoclonal antibodies against active site epitopes on human endothelial plasminogen activator inhibibitor (PAI-1). Fibrinolysis 1990; 4: 27-34.
    • (1990) Fibrinolysis , vol.4 , pp. 27-34
    • MacGregor, I.R.1    Tonner, A.M.2    Micklem, L.R.3
  • 156
    • 0028865093 scopus 로고
    • Immunoassay of murine t-PA, u-PA and PAI-1 using monoclonal antibodies raised in gene-inactivated mice
    • Declerck PJ, Verstreken M, Collen D. Immunoassay of murine t-PA, u-PA and PAI-1 using monoclonal antibodies raised in gene-inactivated mice. Thromb Haemost 1995; 74: 1305-9.
    • (1995) Thromb. Haemost. , vol.74 , pp. 1305-1309
    • Declerck, P.J.1    Verstreken, M.2    Collen, D.3
  • 157
    • 0031969215 scopus 로고    scopus 로고
    • Monoclonal antibody-based immunoassays for the specific quantitation of rat PAI-1 antigen and activity in biological samples
    • Ngo TH, Verheyen S, Knockaert I, et al. Monoclonal antibody-based immunoassays for the specific quantitation of rat PAI-1 antigen and activity in biological samples. Thromb Haemost 1998; 79: 808-12.
    • (1998) Thromb. Haemost. , vol.79 , pp. 808-812
    • Ngo, T.H.1    Verheyen, S.2    Knockaert, I.3
  • 158
    • 0034533897 scopus 로고    scopus 로고
    • Immunoassays for the quantitation of porcine PAI-1 antigen and activity in biological fluid samples
    • Leng HM, Brouwers E, Knockaert I, et al. Immunoassays for the quantitation of porcine PAI-1 antigen and activity in biological fluid samples. Thromb Haemost 2000; 84: 1082-6.
    • (2000) Thromb. Haemost. , vol.84 , pp. 1082-1086
    • Leng, H.M.1    Brouwers, E.2    Knockaert, I.3
  • 159
    • 0034089869 scopus 로고    scopus 로고
    • Importance of the hinge region between α-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neutralizing antibodies
    • Bijnens AP, Gils A, Knockaert I, et al. Importance of the hinge region between α-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neutralizing antibodies. J Biol Chem 2000; 275: 6375-80.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6375-6380
    • Bijnens, A.P.1    Gils, A.2    Knockaert, I.3
  • 160
    • 0033580955 scopus 로고    scopus 로고
    • Accelerated conversion of human plasminogen activator inhibitor-1 to its latent form by antibody binding
    • Verhamme I, Kvassman JO, Day DE, et al. Accelerated conversion of human plasminogen activator inhibitor-1 to its latent form by antibody binding. J Biol Chem 1999; 274: 17511-7.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17511-17517
    • Verhamme, I.1    Kvassman, J.O.2    Day, D.E.3
  • 161
    • 0036336458 scopus 로고    scopus 로고
    • Importance of N-terminal residues in plasminogen activator inhibitor 1 on its antibody induced latency transition
    • Ngo TH, Zhou Y, Stassen JM, et al. Importance of N-terminal residues in plasminogen activator inhibitor 1 on its antibody induced latency transition. Thromb Haemost 2002; 88: 288-93.
    • (2002) Thromb. Haemost. , vol.88 , pp. 288-293
    • Ngo, T.H.1    Zhou, Y.2    Stassen, J.M.3
  • 162
    • 0025319933 scopus 로고
    • Measurement of plasminogen activator inhibitor 1 (PAI-1) in plasma with various monoclonal antibody-based enzyme-linked immunosorbent assays
    • Declerck PJ, Collen D. Measurement of plasminogen activator inhibitor 1 (PAI-1) in plasma with various monoclonal antibody-based enzyme-linked immunosorbent assays. Thromb Res Suppl 1990; 10: 3-9.
    • (1990) Thromb. Res. Suppl. , vol.10 , pp. 3-9
    • Declerck, P.J.1    Collen, D.2
  • 163
    • 0025744035 scopus 로고
    • The interaction of plasminogen activator inhibitor 1 with plasminogen activators (tissue-type and urokinase-type) and fibrin: Localization of interaction sites and physiologic relevance
    • Keijer J, Linders M, van Zonneveld AJ, et al. The interaction of plasminogen activator inhibitor 1 with plasminogen activators (tissue-type and urokinase-type) and fibrin: Localization of interaction sites and physiologic relevance. Blood 1991; 78: 401-9.
    • (1991) Blood , vol.78 , pp. 401-409
    • Keijer, J.1    Linders, M.2    van Zonneveld, A.J.3
  • 164
    • 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
    • van Giezen JJ, Wahlund G, Nerme, et al. 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 1997; 77: 964-9.
    • (1997) Thromb. Haemost. , vol.77 , pp. 964-969
    • van Giezen, J.J.1    Wahlund, G.2    Nerme, A.3
  • 165
    • 0035657712 scopus 로고    scopus 로고
    • Inactivation of plasminogen activator inhibitor-1 accelerates thrombolysis of a platelet-rich thrombus in rat mesenteric arterioles
    • Rupin A, Martin F, Vallez MO, et al. Inactivation of plasminogen activator inhibitor-1 accelerates thrombolysis of a platelet-rich thrombus in rat mesenteric arterioles. Thromb Haemost 2001; 86: 1528-31.
    • (2001) Thromb. Haemost. , vol.86 , pp. 1528-1531
    • Rupin, A.1    Martin, F.2    Vallez, M.O.3
  • 166
    • 0033916564 scopus 로고    scopus 로고
    • Prevention of renal fibrin deposition in endotoxin-induced DIC through inhibition of PAI-1
    • Montes R, Declerck PJ, Calvo A, et al. Prevention of renal fibrin deposition in endotoxin-induced DIC through inhibition of PAI-1. Thromb Haemost 2000; 84: 65-70.
    • (2000) Thromb. Haemost. , vol.84 , pp. 65-70
    • Montes, R.1    Declerck, P.J.2    Calvo, A.3
  • 167
    • 0034283566 scopus 로고    scopus 로고
    • High-density mutagenesis by combined DMA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: Application to study structure-function of plasminogen activation inhibitor 1 (PAI-1)
    • Stoop AA, Jespers; L, Lasters I, et al. High-density mutagenesis by combined DMA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: Application to study structure-function of plasminogen activation inhibitor 1 (PAI-1). J Mol Biol 2000; 301: 1135-47.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1135-1147
    • Stoop, A.A.1    Jespers, L.2    Lasters, I.3
  • 168
    • 0035059744 scopus 로고    scopus 로고
    • Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1 - Implications for antibody-mediated PAI-1-neutralization and vitronectin-binding
    • Wind T, Jensen MA, Andreasen PA. Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1 - Implications for antibody-mediated PAI-1-neutralization and vitronectin-binding. Eur J Biochem 2001; 268: 1095-106.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1095-1106
    • Wind, T.1    Jensen, M.A.2    Andreasen, P.A.3
  • 169
    • 0346461093 scopus 로고    scopus 로고
    • Mechanisms of conversion of plasminogen activator inhibitor 1 from a suicide inhibitor to a substrate by monoclonal antibodies
    • Komissarov AA, Declerck PJ, Shore JD. Mechanisms of conversion of plasminogen activator inhibitor 1 from a suicide inhibitor to a substrate by monoclonal antibodies. J Biol Chem 2002; 277: 43858-65.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43858-43865
    • Komissarov, A.A.1    Declerck, P.J.2    Shore, J.D.3
  • 170
    • 0042191343 scopus 로고    scopus 로고
    • Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1
    • Naessens D, Gils A, Compernolle G, et al. Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1. J Thromb Haemost 2003; 1: 1028-33.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1028-1033
    • Naessens, D.1    Gils, A.2    Compernolle, G.3
  • 171
    • 0037623683 scopus 로고    scopus 로고
    • Elucidation of the epitope of a latency-inducing antibody: Identification of a new molecular target for PAI-1 inhibition
    • Naessens D, Gils A, Compernolle G, et al. Elucidation of the epitope of a latency-inducing antibody: Identification of a new molecular target for PAI-1 inhibition. Thromb Haemost 2003; 90: 52-8.
    • (2003) Thromb. Haemost. , vol.90 , pp. 52-58
    • Naessens, D.1    Gils, A.2    Compernolle, G.3
  • 172
    • 0038276073 scopus 로고    scopus 로고
    • Mapping of a conformational epitope on plasminogen activator inhibitor-1 by random mutagenesis. Implications for serpin function
    • Gorlatova NV, Elokdah H, Fan K, et al. Mapping of a conformational epitope on plasminogen activator inhibitor-1 by random mutagenesis. Implications for serpin function. J Biol Chem 2003; 278: 16329-35.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16329-16335
    • Gorlatova, N.V.1    Elokdah, H.2    Fan, K.3
  • 173
    • 0035854722 scopus 로고    scopus 로고
    • Identification of a target site in plasminogen activator inhibitor-1 that allows neutralization of its inhibitory properties concomitant with an allosteric up-regulation of its antiadhesive properties
    • Ngo TH, Hoylaerts MF, Knockaert I, et al. Identification of a target site in plasminogen activator inhibitor-1 that allows neutralization of its inhibitory properties concomitant with an allosteric up-regulation of its antiadhesive properties. J Biol Chem 2001; 276: 26243-8.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26243-26248
    • Ngo, T.H.1    Hoylaerts, M.F.2    Knockaert, I.3
  • 174
    • 0037031812 scopus 로고    scopus 로고
    • A novel antithrombotic role for high molecular weight kininogen as inhibitor of plasminogen activator inhibitor-1 function
    • Chavakis T, Pixley RA, Isordia-Salas I, et al. A novel antithrombotic role for high molecular weight kininogen as inhibitor of plasminogen activator inhibitor-1 function. J Biol Chem 2002; 277: 32677-82.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32677-32682
    • Chavakis, T.1    Pixley, R.A.2    Isordia-Salas, I.3
  • 175
    • 0042697195 scopus 로고    scopus 로고
    • Biochemical mechanism of action of a dike-topiperazine inactivator of plasminogen activator inhibitor-1
    • Einholm AP, Pedersen KE, Wind T, et al. Biochemical mechanism of action of a dike-topiperazine inactivator of plasminogen activator inhibitor-1. Biochem J 2003; 373: 723-32.
    • (2003) Biochem. J. , vol.373 , pp. 723-732
    • Einholm, A.P.1    Pedersen, K.E.2    Wind, T.3
  • 176
    • 18544368620 scopus 로고    scopus 로고
    • Novel inhibitors of plasminogen activator inhibitor-1: Development of new templates from diketopiperazines
    • Wang S, Golec J, Miller W, et al. Novel inhibitors of plasminogen activator inhibitor-1: Development of new templates from diketopiperazines. Bioorg Med Chem Lett 2002; 12: 2367-70.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2367-2370
    • Wang, S.1    Golec, J.2    Miller, W.3
  • 177
    • 0038266897 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 polymers, induced by inactivating amphipathic organochemical ligands
    • Pedersen KE, Einholm AP, Christensen A, et al. Plasminogen activator inhibitor-1 polymers, induced by inactivating amphipathic organochemical ligands. Biochem J 2003; 372: 747-55.
    • (2003) Biochem. J. , vol.372 , pp. 747-755
    • Pedersen, K.E.1    Einholm, A.P.2    Christensen, A.3
  • 178
    • 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
    • Vinogradsky B, Bell SP, Woodcock-Mitchell J, et al. 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 1997; 85: 305-14.
    • (1997) Thromb. Res. , vol.85 , pp. 305-314
    • Vinogradsky, B.1    Bell, S.P.2    Woodcock-Mitchell, J.3
  • 179
    • 0034971351 scopus 로고    scopus 로고
    • Regulation of PAI-1 concentration in platelets by systemic administration of antisense oligonucleotides to rats
    • Pawlowska Z, Chabielska E, Kobylanska A, et al. Regulation of PAI-1 concentration in platelets by systemic administration of antisense oligonucleotides to rats. Thromb Haemost 2001; 85: 1086-9.
    • (2001) Thromb. Haemost. , vol.85 , pp. 1086-1089
    • Pawlowska, Z.1    Chabielska, E.2    Kobylanska, A.3
  • 180
    • 0031934204 scopus 로고    scopus 로고
    • Phosphorothioate oligodeoxyribonucleotides antisense to PAI-1 mRNA increase fibrinolysis and modify experimental thrombosis in rats
    • Pawlowska Z, Pluskota E, Chabielska E, et al. Phosphorothioate oligodeoxyribonucleotides antisense to PAI-1 mRNA increase fibrinolysis and modify experimental thrombosis in rats. Thromb Haemost 1998; 79: 348-53.
    • (1998) Thromb. Haemost. , vol.79 , pp. 348-353
    • Pawlowska, Z.1    Pluskota, E.2    Chabielska, E.3


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