메뉴 건너뛰기




Volumn 92, Issue , 2015, Pages 619-636

Small molecules inhibitors of plasminogen activator inhibitor-1-An overview

Author keywords

Cardiovascular diseases; Fibrinolysis; Inhibitors; Plasminogen activator inhibitor (PAI 1); Tissue type plasminogen activator (tPA); Urokinase plasminogen activator (uPA)

Indexed keywords

AZETIDINE DERIVATIVE; BENZOFURAN DERIVATIVE; BENZOTHIOPHENE DERIVATIVE; EMBELIN; FLUFENAMIC ACID; INDOLE DERIVATIVE; MENTHOL; OXADIAZOLE DERIVATIVE; OXADIAZOLIDINEDIONE; OXALAMIDE DERIVATIVE; OXAZOLIDINE DERIVATIVE; PIPERAZINE DERIVATIVE; PIPERAZINEDIONE; PLASMINOGEN ACTIVATOR INHIBITOR 1; POLYPHENOL DERIVATIVE; PROTEIN INHIBITOR; PSEUDO PEPTIDE INHIBITOR; PYRROLIN 2 ONE DERIVATIVE; PYRROLINE DERIVATIVE; UNCLASSIFIED DRUG; MOLECULAR LIBRARY; SERPINE1 PROTEIN, HUMAN;

EID: 84922309247     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2015.01.010     Document Type: Review
Times cited : (47)

References (104)
  • 2
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • C.M. Hekman, D.J. Loskutoff, Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants, J. Biol. Chem. 260 (1985) 11581e11587 doi:10/1985; 260(21):11581e7.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 3
    • 0026471040 scopus 로고
    • A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate
    • T. Urano, L. Strandberg, L.B. Johansson, T. Ny, A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate, Eur. J. Biochem. 209 (1992) 985e992, http://dx.doi.org/10.1111/j.1432-1033.1992.tb17372.x.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 985-992
    • Urano, T.1    Strandberg, L.2    Johansson, L.B.3    Ny, T.4
  • 4
    • 0026664170 scopus 로고
    • Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator
    • P.J. Declerck, M. De Mol, D.E. Vaughansq, D. Collen, Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator, J. Biol. Chem. 267 (1992) 11693e11696.
    • (1992) J Biol. Chem. , vol.267 , pp. 11693-11696
    • Declerck, P.J.1    De Mol, M.2    Vaughansq, D.E.3    Collen, D.4
  • 5
    • 58349083298 scopus 로고    scopus 로고
    • High quality structure of cleaved PAI-1-stab
    • M. Dewilde, S.V. Strelkov, A. Rabijns, P.J. Declerck, High quality structure of cleaved PAI-1-stab, J. Struct. Biol. 165 (2009) 126e132, http://dx.doi.org/10.1016/j.jsb.2008.11.001.
    • (2009) J. Struct. Biol. , vol.165 , pp. 126-132
    • Dewilde, M.1    Strelkov, S.V.2    Rabijns, A.3    Declerck, P.J.4
  • 6
    • 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, M.A. Francis-Chmura, J.D. Shore, D. Ginsburg, 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) 7676e7680, http://dx.doi.org/10.1074/jbc.272.12.7676.
    • (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, M.A.5    Shore, J.D.6    Ginsburg, D.7
  • 7
    • 0025774971 scopus 로고
    • Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin
    • D. Seiffert, D.J. Loskutoff, Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin, J. Biol. Chem. 266 (1991) 2824e2830.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2824-2830
    • Seiffert, D.1    Loskutoff, D.J.2
  • 8
    • 0037743532 scopus 로고    scopus 로고
    • How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration
    • A. Zhou, J.A. Huntington, N.S. Pannu, R.W. Carrell, R.J. Read, How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration, Nat. Struct. Biol. 10 (2003) 541e544, http://dx.doi.org/10.1038/nsb943.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 541-544
    • Zhou, A.1    Huntington, J.A.2    Pannu, N.S.3    Carrell, R.W.4    Read, R.J.5
  • 9
    • 44849086179 scopus 로고    scopus 로고
    • A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activity
    • C.R. Schar, G.E. Blouse, K.H. Minor, C.B. Peterson, A deletion mutant of vitronectin lacking the somatomedin B domain exhibits residual plasminogen activator inhibitor-1-binding activity, J. Biol. Chem. 283 (2008) 10297e10309, http://dx.doi.org/10.1074/jbc.M708017200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 10297-10309
    • Schar, C.R.1    Blouse, G.E.2    Minor, K.H.3    Peterson, C.B.4
  • 10
    • 0028339118 scopus 로고
    • Localization of vitronectin binding domain in plasminogen activator inhibitor-1
    • D.A. Lawrence, M.B. Berkenpas, S. Palaniappan, D. Ginsburg, Localization of vitronectin binding domain in plasminogen activator inhibitor-1, J. Biol. Chem. 269 (1994) 15223e15228.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15223-15228
    • Lawrence, D.A.1    Berkenpas, M.B.2    Palaniappan, S.3    Ginsburg, D.4
  • 11
    • 0036156207 scopus 로고    scopus 로고
    • Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin. Characterization of different PAI-1 mutants
    • N.A. De Prada, F. Schroeck, E. Sinner, B. Muehlenweg, Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin. Characterization of different PAI-1 mutants, Eur. J. Biochem. 269 (2002) 184e192, http://dx.doi.org/10.1046/j.0014-2956.2002.02639.x.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 184-192
    • De Prada, N.A.1    Schroeck, F.2    Sinner, E.3    Muehlenweg, B.4
  • 12
    • 0028786263 scopus 로고
    • Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis: An update
    • M. Vanmeijer, H. Pannekoek, Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis: an update, Fibrinolysis 9 (1995) 263e276, http://dx.doi.org/10.1016/S0268-9499(95)80015-8.
    • (1995) Fibrinolysis , vol.9 , pp. 263-276
    • Vanmeijer, M.1    Pannekoek, H.2
  • 13
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis
    • M.S. Pepper, Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis, Arterioscler. Thromb. Vasc. Biol. 21 (2001) 1104e1117, http://dx.doi.org/10.1161/hq0701.093685.
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 1104-1117
    • Pepper, M.S.1
  • 14
    • 0032531051 scopus 로고    scopus 로고
    • Development and disease in proteinase-deficient mice: Role of the plasminogen, matrix metalloproteinase and coagulation system
    • P. Carmeliet, D. Collen, Development and disease in proteinase-deficient mice: role of the plasminogen, matrix metalloproteinase and coagulation system, Thromb. Res. 91 (1998) 255e285, http://dx.doi.org/10.1016/S0049-3848(98)00122-4.
    • (1998) Thromb Res. , vol.91 , pp. 255-285
    • Carmeliet, P.1    Collen, D.2
  • 15
    • 0036289761 scopus 로고    scopus 로고
    • PAI-1 promotes extracellular matrix deposition in the airways of a murine asthma model
    • C. Oh, B. Ariue, R. Alban, B. Shaw, S. Cho, PAI-1 promotes extracellular matrix deposition in the airways of a murine asthma model, Biochem. Biophys. Res. Commun. 294 (2002) 1155e1160, http://dx.doi.org/10.1016/S0006-291X(02)00577-6.
    • (2002) Biochem. Biophys. Res. Commun. , vol.294 , pp. 1155-1160
    • Oh, C.1    Ariue, B.2    Alban, R.3    Shaw, B.4    Cho, S.5
  • 16
    • 0029745109 scopus 로고    scopus 로고
    • The serpin PAI-1 inhibits cell migration by blocking integrin avb3 binding to vitronectin
    • S. Stefansson, D.A. Lawrence, The serpin PAI-1 inhibits cell migration by blocking integrin avb3 binding to vitronectin, Nature 383 (1996) 441e443, http://dx.doi.org/10.1038/383441a0.
    • (1996) Nature , vol.383 , pp. 441-443
    • Stefansson, S.1    Lawrence, D.A.2
  • 17
    • 56049085765 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1: The expression, biological functions, and effects on tumorigenesis and tumor cell adhesion and migration, J
    • C. Lee, T. Huang, Plasminogen activator inhibitor-1: the expression, biological functions, and effects on tumorigenesis and tumor cell adhesion and migration, J. Cancer Mol. 1 (2005) 25e36.
    • (2005) Cancer Mol. , vol.1 , pp. 25-36
    • Lee, C.1    Huang, T.2
  • 18
    • 0036790506 scopus 로고    scopus 로고
    • PAI-1 and cellular migration: Dabbling in paradox
    • D.E. Vaughan, PAI-1 and cellular migration: dabbling in paradox, Arterioscler. Thromb. Vasc. Biol. 22 (2002) 1522e1523, http://dx.doi.org/10.1161/01.ATV.0000037901.89736.0A.
    • (2002) Arterioscler. Thromb. Vasc. Biol. , vol.22 , pp. 1522-1523
    • Vaughan, D.E.1
  • 19
    • 84878308272 scopus 로고    scopus 로고
    • The apparent uPA/PAI-1 paradox in cancer: More than meets the eye
    • H.C. Kwaan, A.P. Mazar, B.J. McMahon, The apparent uPA/PAI-1 paradox in cancer: more than meets the eye, Semin. Thromb. Haemost. 39 (2013) 382e391, http://dx.doi.org/10.1055/s-0033-1338127.
    • (2013) Semin. Thromb. Haemost. , vol.39 , pp. 382-391
    • Kwaan, H.C.1    Mazar, A.P.2    McMahon, B.J.3
  • 22
    • 0038823700 scopus 로고    scopus 로고
    • Dose-dependent modulation of choroidal neovascularization by plasminogen activator inhibitor type I: Implications for clinical trials
    • V. Lambert, C. Munaut, P. Carmeliet, Dose-dependent modulation of choroidal neovascularization by plasminogen activator inhibitor type I: implications for clinical trials, Investig. Ophthalmol. Vis. Sci. 44 (2003) 2791e2797.
    • (2003) Investig. Ophthalmol. Vis. Sci. , vol.44 , pp. 2791-2797
    • Lambert, V.1    Munaut, C.2    Carmeliet, P.3
  • 23
    • 0036834573 scopus 로고    scopus 로고
    • Regulation of plasminogen activator inhibitor (PAI)-1 expression in a human trophoblast cell line by glucocorticoid (GC) and transforming growth factor (TGF)-b
    • Y. Ma, J.S. Ryu, A. Dulay, M. Segal, S. Guller, Regulation of plasminogen activator inhibitor (PAI)-1 expression in a human trophoblast cell line by glucocorticoid (GC) and transforming growth factor (TGF)-b, Placenta 23 (2002) 727e734, http://dx.doi.org/10.1053/plac.2002.0863.
    • (2002) Placenta , vol.23 , pp. 727-734
    • Ma, Y.1    Ryu, J.S.2    Dulay, A.3    Segal, M.4    Guller, S.5
  • 24
    • 0034747099 scopus 로고    scopus 로고
    • TGF-b 1-induced PAI-1 gene expression requires MEK activity and cell-to-substrate adhesion
    • S.M. Kutz, J. Hordines, P.J. Mckeown-Longo, P.J. Higgins, TGF-b 1-induced PAI-1 gene expression requires MEK activity and cell-to-substrate adhesion, J. Cell Sci. 21 (2001) 3905e3914.
    • (2001) J. Cell Sci. , vol.21 , pp. 3905-3914
    • Kutz, S.M.1    Hordines, J.2    McKeown-Longo, P.J.3    Higgins, P.J.4
  • 25
    • 35348837775 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 in vascular thrombosis
    • R. Westrick, D. Eitzman, Plasminogen activator inhibitor-1 in vascular thrombosis, Curr. Drug Targets 8 (2007) 966e1002.
    • (2007) Curr. Drug Targets , vol.8 , pp. 966-1002
    • Westrick, R.1    Eitzman, D.2
  • 26
    • 0036299591 scopus 로고    scopus 로고
    • Inhibition of PAI-1: A new anti-thrombotic approach
    • Q. Wu, Z. Zhao, Inhibition of PAI-1: a new anti-thrombotic approach, Curr. Drug Targets. Cardiovasc. Haematol. Disord. 2 (2002) 27e42, http://dx.doi.org/10.2174/1568006023337727.
    • (2002) Curr. Drug Targets. Cardiovasc. Haematol. Disord. , vol.2 , pp. 27-42
    • Wu, Q.1    Zhao, Z.2
  • 27
    • 80051547446 scopus 로고    scopus 로고
    • Multifaceted role of plasminogen activator inhibitor-1 in regulating early remodeling of vein bypass grafts
    • Y. Ji, T.L. Strawn, E.A. Grunz, M.J. Stevenson, A.W. Lohman, D.A. Lawrence, W.P. Fay, Multifaceted role of plasminogen activator inhibitor-1 in regulating early remodeling of vein bypass grafts, Arterioscler. Thromb. Vasc. Biol. 31 (2011) 1781e1787, http://dx.doi.org/10.1161/ATVBAHA.111.228767.
    • (2011) Arterioscler. Thromb. Vasc. Biol. , vol.31 , pp. 1781-1787
    • Ji, Y.1    Strawn, T.L.2    Grunz, E.A.3    Stevenson, M.J.4    Lohman, A.W.5    Lawrence, D.A.6    Fay, W.P.7
  • 28
    • 70349574151 scopus 로고    scopus 로고
    • Recombinant plasminogen activator inhibitor-1 inhibits intimal hyperplasia
    • J. Wu, L. Peng, G.A. McMahon, D.A. Lawrence, W.P. Fay, Recombinant plasminogen activator inhibitor-1 inhibits intimal hyperplasia, Arterioscler. Thromb. Vasc. Biol. 29 (2009) 1565e1570, http://dx.doi.org/10.1161/ATVBAHA.109.189514.
    • (2009) Arterioscler. Thromb. Vasc. Biol. , vol.29 , pp. 1565-1570
    • Wu, J.1    Peng, L.2    McMahon, G.A.3    Lawrence, D.A.4    Fay, W.P.5
  • 29
    • 0034672348 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 deficiency protects against atherosclerosis progression in the mouse carotid artery
    • D. Eitzman, R. Westrick, Z. Xu, Plasminogen activator inhibitor-1 deficiency protects against atherosclerosis progression in the mouse carotid artery, Blood 96 (2000) 4212e4215.
    • (2000) Blood , vol.96 , pp. 4212-4215
    • Eitzman, D.1    Westrick, R.2    Xu, Z.3
  • 31
    • 84924810915 scopus 로고    scopus 로고
    • Novel combinatorial therapeutic targeting of PAI-1 (SERPINE1) gene expression in alzheimer's disease
    • S. Kutz, C. Higgins, P. Higgins, Novel combinatorial therapeutic targeting of PAI-1 (SERPINE1) gene expression in alzheimer's disease, Mol. Med. Ther. 1 (2012) 1e6, http://dx.doi.org/10.4172/2324-8769.1000106.Novel.
    • (2012) Mol. Med. Ther. , vol.1 , pp. 1-6
    • Kutz, S.1    Higgins, C.2    Higgins, P.3
  • 32
    • 15044365690 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1: A common denominator in obesity, diabetes and cardiovascular disease
    • B. De Taeye, L.H. Smith, D.E. Vaughan, Plasminogen activator inhibitor-1: a common denominator in obesity, diabetes and cardiovascular disease, Curr. Opin. Pharmacol. 5 (2005) 149e154, http://dx.doi.org/10.1016/j.coph.2005.01.007.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 149-154
    • De Taeye, B.1    Smith, L.H.2    Vaughan, D.E.3
  • 33
    • 33749063994 scopus 로고    scopus 로고
    • A role for plasminogen activator inhibitor-1 in obesity: From pie to PAI? Arterioscler
    • M.L.G. Correia, W.G. Haynes, A role for plasminogen activator inhibitor-1 in obesity: from pie to PAI? Arterioscler. Thromb. Vasc. Biol. 26 (2006) 2183e2185, http://dx.doi.org/10.1161/01.ATV.0000244018.24120.70.
    • (2006) Thromb. Vasc. Biol. , vol.26 , pp. 2183-2185
    • Correia, M.L.G.1    Haynes, W.G.2
  • 34
    • 84866647405 scopus 로고    scopus 로고
    • PAI-1 and diabetes: A journey from the bench to the bedside
    • D.J. Schneider, B.E. Sobel, PAI-1 and diabetes: a journey from the bench to the bedside, Diabetes Care 35 (2012) 1961e1967, http://dx.doi.org/10.2337/dc12-0638.
    • (2012) Diabetes Care , vol.35 , pp. 1961-1967
    • Schneider, D.J.1    Sobel, B.E.2
  • 35
    • 0347480398 scopus 로고    scopus 로고
    • Effect of plasminogen activator inhibitor-1 in diabetes mellitus and cardiovascular disease
    • C.J. Lyon, W.A. Hsueh, Effect of plasminogen activator inhibitor-1 in diabetes mellitus and cardiovascular disease, Am. J. Med. 115 (2003) 62e68, http://dx.doi.org/10.1016/j.amjmed.2003.08.014.
    • (2003) Am. J. Med. , vol.115 , pp. 62-68
    • Lyon, C.J.1    Hsueh, W.A.2
  • 36
    • 0034518414 scopus 로고    scopus 로고
    • PAI-1, fibrosis, and the elusive provisional fibrin matrix
    • D.J. Loskutoff, J.P. Quigley, PAI-1, fibrosis, and the elusive provisional fibrin matrix, J. Clin. Investig. 106 (2000) 1441e1443.
    • (2000) J Clin. Investig. , vol.106 , pp. 1441-1443
    • Loskutoff, D.J.1    Quigley, J.P.2
  • 37
    • 82155192325 scopus 로고    scopus 로고
    • PAI-1 in tissue fibrosis
    • A. Ghosh, D. Vaughan, PAI-1 in tissue fibrosis, J. Cell. Physiol. 227 (2012) 493e507, http://dx.doi.org/10.1002/jcp.22783.PAI-1.
    • (2012) J. Cell. Physiol. , vol.227 , pp. 493-507
    • Ghosh, A.1    Vaughan, D.2
  • 38
    • 77957797829 scopus 로고    scopus 로고
    • Therapeutic potential of plasminogen activator inhibitor-1 inhibitors
    • N. Brown, Therapeutic potential of plasminogen activator inhibitor-1 inhibitors, Ther. Adv. Cardiovasc. Dis. 4 (2010) 315e324, http://dx.doi.org/10.1177/1753944710379126.
    • (2010) Ther. Adv. Cardiovasc. Dis. , vol.4 , pp. 315-324
    • Brown, N.1
  • 39
    • 84879333770 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 inhibitors: A patent review 2006-present
    • Y.M. Fortenberry, Plasminogen activator inhibitor-1 inhibitors: a patent review (2006-present), Expert Opin. Ther. Pat. 23 (2013) 801e815, http://dx.doi.org/10.1517/13543776.2013.782393.
    • (2013) Expert Opin. Ther. Pat. , vol.23 , pp. 801-815
    • Fortenberry, Y.M.1
  • 40
    • 1642318429 scopus 로고    scopus 로고
    • The structural basis for the pathophysiological relevance of PAI-I in cardiovascular diseases and the development of potential PAI-I inhibitors
    • A. Gils, P.J. Declerck, The structural basis for the pathophysiological relevance of PAI-I in cardiovascular diseases and the development of potential PAI-I inhibitors, Thromb. Haemost. 91 (2004) 425e437, http://dx.doi.org/10.1160/TH03-12-0764.
    • (2004) Thromb. Haemost. , vol.91 , pp. 425-437
    • Gils, A.1    Declerck, P.J.2
  • 41
    • 84904859019 scopus 로고    scopus 로고
    • Inhibition of PAI-1 antiproteolytic activity against tPA by RNA aptamers
    • J. Damare, S. Brandal, Y.M. Fortenberry, Inhibition of PAI-1 antiproteolytic activity against tPA by RNA aptamers, Nucleic Acid Ther. 24 (2014), http://dx.doi.org/10.1089/nat.2013.0475.
    • (2014) Nucleic Acid Ther. , vol.24
    • Damare, J.1    Brandal, S.2    Fortenberry, Y.M.3
  • 42
    • 0026573859 scopus 로고
    • Inhibiting the inhibitor
    • V.J. Marder, Inhibiting the inhibitor, Circulation 85 (1992) 386e387, http://dx.doi.org/10.1161/01.CIR.85.1.386.
    • (1992) Circulation , vol.85 , pp. 386-387
    • Marder, V.J.1
  • 43
    • 84866235383 scopus 로고    scopus 로고
    • The biochemistry, physiology and pathological roles of PAI-1 and the requirements for PAI-1 inhibition in vivo
    • B. Van De Craen, P.J. Declerck, A. Gils, The biochemistry, physiology and pathological roles of PAI-1 and the requirements for PAI-1 inhibition in vivo, Thromb. Res. 130 (2012) 576e585, http://dx.doi.org/10.1016/j.thromres.2012.06.023.
    • (2012) Thromb Res. , vol.130 , pp. 576-585
    • Craen De B.Van1    Declerck, P.J.2    Gils, A.3
  • 45
    • 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, L. Sjolin, J. Deinum, 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) 627e636, http://dx.doi.org/10.1016/S0969-2126(98)00064-1.
    • (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    Deinum, J.7
  • 46
    • 84858706063 scopus 로고    scopus 로고
    • A peptide mimicking the C-terminal part of the reactive center loop induces the transition to the latent form of plasminogen activator inhibitor type-1
    • S. D'Amico, J.A. Martial, I. Struman, A peptide mimicking the C-terminal part of the reactive center loop induces the transition to the latent form of plasminogen activator inhibitor type-1, FEBS Lett. 586 (2012) 686e692, http://dx.doi.org/10.1016/j.febslet.2012.02.013.
    • (2012) FEBS Lett. , vol.586 , pp. 686-692
    • D'Amico, S.1    Martial, J.A.2    Struman, I.3
  • 48
    • 42249111398 scopus 로고    scopus 로고
    • Inhibition of plasminogen activator inhibitor-1: Its mechanism and effectiveness on coagulation and fibrosis
    • Y. Izuhara, S. Takahashi, M. Nangaku, S. Takizawa, H. Ishida, K. Kurokawa, C. van Ypersele de Strihou, N. Hirayama, T. Miyata, Inhibition of plasminogen activator inhibitor-1: its mechanism and effectiveness on coagulation and fibrosis, Arterioscler. Thromb. Vasc. Biol. 28 (2008) 672e677, http://dx.doi.org/10.1161/ATVBAHA.107.157479.
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 672-677
    • Izuhara, Y.1    Takahashi, S.2    Nangaku, M.3    Takizawa, S.4    Ishida, H.5    Kurokawa, K.6    Hirayama, N.7    Miyata, T.8
  • 49
    • 77951730692 scopus 로고    scopus 로고
    • Structureeactivity relationships of new 2-acylamino-3-thiophenecarboxylic acid dimers as plasminogen activator inhibitor-1 inhibitors
    • N. Yamaoka, Y. Kawano, Y. Izuhara, T. Miyata, K. Meguro, Structureeactivity relationships of new 2-acylamino-3-thiophenecarboxylic acid dimers as plasminogen activator inhibitor-1 inhibitors, Chem. Pharm. Bull. (Tokyo) 58 (2010) 615e619, http://dx.doi.org/10.1248/cpb.58.615.
    • (2010) Chem. Pharm. Bull. (Tokyo) , vol.58 , pp. 615-619
    • Yamaoka, N.1    Kawano, Y.2    Izuhara, Y.3    Miyata, T.4    Meguro, K.5
  • 50
    • 79551489999 scopus 로고    scopus 로고
    • Structureeactivity relationships of new N-acylanthranilic acid derivatives as plasminogen activator inhibitor-1 inhibitors
    • N. Yamaoka, H. Kodama, Y. Izuhara, T. Miyata, K. Meguro, Structureeactivity relationships of new N-acylanthranilic acid derivatives as plasminogen activator inhibitor-1 inhibitors, Chem. Pharm. Bull. (Tokyo) 59 (2011) 215e224, http://dx.doi.org/10.1248/cpb.59.215.
    • (2011) Chem. Pharm. Bull. (Tokyo) , vol.59 , pp. 215-224
    • Yamaoka, N.1    Kodama, H.2    Izuhara, Y.3    Miyata, T.4    Meguro, K.5
  • 51
    • 77952011905 scopus 로고    scopus 로고
    • A novel inhibitor of plasminogen activator inhibitor-1 provides antithrombotic benefits devoid of bleeding effect in nonhuman primates
    • Y. Izuhara, N. Yamaoka, H. Kodama, T. Dan, S. Takizawa, N. Hirayama, K. Meguro, C. van Ypersele de Strihou, T. Miyata, A novel inhibitor of plasminogen activator inhibitor-1 provides antithrombotic benefits devoid of bleeding effect in nonhuman primates, J. Cereb. Blood Flow Metab. 30 (2010) 904e912, http://dx.doi.org/10.1038/jcbfm.2009.272.
    • (2010) J. Cereb. Blood Flow Metab. , vol.30 , pp. 904-912
    • Izuhara, Y.1    Yamaoka, N.2    Kodama, H.3    Dan, T.4    Takizawa, S.5    Hirayama, N.6    Meguro, K.7    Miyata, T.8
  • 52
    • 0029801041 scopus 로고    scopus 로고
    • Inhibition of plasminogen activator inhibitor-1 activity by two diketopiperazines, XR330 and XR334 produced by streptomyces sp
    • J. Bryans, P. Charlton, I. Chicarelli-Robinson, M. Collins, R. Faint, C. Latham, I. Shaw, S. Trew, Inhibition of plasminogen activator inhibitor-1 activity by two diketopiperazines, XR330 and XR334 produced by streptomyces sp, J. Antibiot. (Tokyo) 49 (1996) 1014e1021.
    • (1996) J Antibiot. (Tokyo) , vol.49 , pp. 1014-1021
    • Bryans, J.1    Charlton, P.2    Chicarelli-Robinson, I.3    Collins, M.4    Faint, R.5    Latham, C.6    Shaw, I.7    Trew, S.8
  • 54
    • 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, D. Templeton, I. Mackie, S. Machin, P. Bevan, XR5118, a novel modulator of plasminogen activator inhibitor-1 (PAI-1), increases endogenous tPA activity in the rat, Fibrinolysis Proteolysis 11 (1997) 51e56, http://dx.doi.org/10.1016/S0268-9499(97) 80009-4.
    • (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    MacKie, I.7    MacHin, S.8    Bevan, P.9
  • 56
    • 0035829167 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of a series of diketopiperazine inhibitors of plasminogen activator inhibitor-1
    • A. Folkes, M.B. Roe, S. Sohal, J. Golec, R. Faint, T. Brooks, P. Charlton, Synthesis and in vitro evaluation of a series of diketopiperazine inhibitors of plasminogen activator inhibitor-1, Bioorg. Med. Chem. Lett. 11 (2001) 2589e2592, http://dx.doi.org/10.1016/S0960-894X(01)00508-X.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 2589-2592
    • Folkes, A.1    Roe, M.B.2    Sohal, S.3    Golec, J.4    Faint, R.5    Brooks, T.6    Charlton, P.7
  • 59
    • 4344692277 scopus 로고    scopus 로고
    • XR5967, a novel modulator of plasminogen activator inhibitor-1 activity, suppresses tumor cell invasion and angiogenesis in vitro
    • T. Brooks, S. Wang, N. Brünner, P. Charlton, XR5967, a novel modulator of plasminogen activator inhibitor-1 activity, suppresses tumor cell invasion and angiogenesis in vitro, Anticancer Drugs 15 (2004) 37e44, http://dx.doi.org/10.1097/00001813-200401000-00007.
    • (2004) Anticancer Drugs , vol.15 , pp. 37-44
    • Brooks, T.1    Wang, S.2    Brünner, N.3    Charlton, P.4
  • 60
    • 0039518548 scopus 로고    scopus 로고
    • Identification of the binding site for a lowmolecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis
    • P. Bj?orquist, J. Ehnebom, T. Inghardt, L. Hansson, M. Lindberg, M. Linschoten, M. Str?omqvist, J. Deinum, Identification of the binding site for a lowmolecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis, Biochemistry 37 (1998) 1227e1234, http://dx.doi.org/10.1021/bi971554q.
    • (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    Stromqvist, M.7    Deinum, J.8
  • 61
    • 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, J
    • R. Egelund, A.P. Einholm, K.E. Pedersen, R.W. Nielsen, A. Christensen, J. Deinum, P.A. Andreasen, 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. 276 (2001) 13077e13086, http://dx.doi.org/10.1074/jbc.M009024200.
    • (2001) Biol. Chem. , vol.276 , pp. 13077-13086
    • Egelund, R.1    Einholm, A.P.2    Pedersen, K.E.3    Nielsen, R.W.4    Christensen, A.5    Deinum, J.6    Andreasen, P.A.7
  • 63
    • 12544250776 scopus 로고    scopus 로고
    • Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy
    • D. Crandall, H. Elokdah, L. Di, J.K. Hennan, N.V. Gorlatova, D.A. Lawrence, Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy, J. Thromb. Haemost. 2 (2004) 1422e1428, http://dx.doi.org/10.1111/j.1538-7836.2004.00829.x.
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 1422-1428
    • Crandall, D.1    Elokdah, H.2    Di, L.3    Hennan, J.K.4    Gorlatova, N.V.5    Lawrence, D.A.6
  • 64
    • 0036301837 scopus 로고    scopus 로고
    • Characterization and comparative evaluation of a novel PAI-1 inhibitor
    • A. Gils, J.-M. Stassen, H. Nar, J.T. Kley, W. Wienen, U.J. Ries, P.J. Declerck, Characterization and comparative evaluation of a novel PAI-1 inhibitor, Thromb. Haemost. 88 (2002) 137e143, http://dx.doi.org/10.1111/j.1538-7836.2004.00829.x.
    • (2002) Thromb. Haemost. , vol.88 , pp. 137-143
    • Gils, A.1    Stassen, J.-M.2    Nar, H.3    Kley, J.T.4    Wienen, W.5    Ries, U.J.6    Declerck, P.J.7
  • 65
    • 0018100595 scopus 로고
    • Fendosal (HP 129): A potent anti-inflammatory and analgesic compound
    • H. Lassman, J. Wilker, V. Anderson, M. Agnew, R. Allen, W. Novick, Fendosal (HP 129): a potent anti-inflammatory and analgesic compound, Agents Actions 8 (1978) 209e217, http://dx.doi.org/10.1007/BF01966606.
    • (1978) Agents Actions , vol.8 , pp. 209-217
    • Lassman, H.1    Wilker, J.2    Anderson, V.3    Agnew, M.4    Allen, R.5    Novick, W.6
  • 68
    • 0017256270 scopus 로고
    • Carboxyarylindoles as nonsteroidal antiinflammatory agents
    • V.B. Anderson, M.N. Agnew, R.C. Allen, Carboxyarylindoles as nonsteroidal antiinflammatory agents, J. Med. Chem. 19 (1976) 318e325, http://dx.doi.org/10.1021/jm00224a023.
    • (1976) J. Med. Chem. , vol.19 , pp. 318-325
    • Anderson, V.B.1    Agnew, M.N.2    Allen, R.C.3
  • 69
    • 3042687515 scopus 로고    scopus 로고
    • Crandall 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, G. Krishnamurthy, D.L. Crandall, Tiplaxtinin, a novel, orally efficacious inhibitor of plasminogen activator inhibitor-1: design, synthesis, and preclinical characterization, J. Med. Chem. 47 (2004) 3491e3494, http://dx.doi.org/10.1021/jm049766q.
    • (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
  • 70
    • 84922324612 scopus 로고    scopus 로고
    • Heart disease and stroke, more than 300 medicines in testing for two leading causes of death in americans
    • Heart disease and stroke, more than 300 medicines in testing for two leading causes of death in americans, Med. Dev. Hear. Dis. Stroke 1 (2009) 1e31. http://www.phrma.org/sites/default/files/pdf/heart-2009.pdf.
    • (2009) Med. Dev. Hear. Dis. Stroke , vol.1 , pp. 1-31
  • 71
    • 34247871548 scopus 로고    scopus 로고
    • Mechanism of inactivation of plasminogen activator inhibitor-1 by a small molecule inhibitor
    • N.V. Gorlatova, J.M. Cale, H. Elokdah, D. Li, K. Fan, M. Warnock, D.L. Crandall, D.A. Lawrence, Mechanism of inactivation of plasminogen activator inhibitor-1 by a small molecule inhibitor, J. Biol. Chem. 282 (2007) 9288e9296, http://dx.doi.org/10.1074/jbc.M611642200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 9288-9296
    • Gorlatova, N.V.1    Cale, J.M.2    Elokdah, H.3    Li, D.4    Fan, K.5    Warnock, M.6    Crandall, D.L.7    Lawrence, D.A.8
  • 73
    • 34748834611 scopus 로고    scopus 로고
    • Neutralization of plasminogen activator inhibitor i (PAI-1) by the synthetic antagonist PAI-749 via a dual mechanism of action
    • S.J. Gardell, J.A. Krueger, T.A. Antrilli, H. Elokdah, S. Mayer, S.J. Orcutt, D.L. Crandall, G.P. Vlasuk, Neutralization of plasminogen activator inhibitor I (PAI-1) by the synthetic antagonist PAI-749 via a dual mechanism of action, Mol. Pharmacol. 72 (2007) 897e906, http://dx.doi.org/10.1124/mol.107.037010.protease.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 897-906
    • Gardell, S.J.1    Krueger, J.A.2    Antrilli, T.A.3    Elokdah, H.4    Mayer, S.5    Orcutt, S.J.6    Crandall, D.L.7    Vlasuk, G.P.8
  • 77
    • 84922304088 scopus 로고    scopus 로고
    • http://clinicaltrials.gov/show/NCT00366288No, (n.d.).
  • 78
    • 0037687834 scopus 로고    scopus 로고
    • New fibrinolytic agents: Benzothiophene derivatives as inhibitors of the t-PA-PAI-1 complex formation
    • G. De Nanteuil, C. Lila-Ambroise, A. Rupin, M.-O. Vallez, T.J. Verbeuren, New fibrinolytic agents: benzothiophene derivatives as inhibitors of the t-PA-PAI-1 complex formation, Bioorg. Med. Chem. Lett. 13 (2003) 1705e1708, http://dx.doi.org/10.1016/S0960-894X(03)00233-6.
    • (2003) Bioorg. Med. Chem. Lett. 13 , pp. 1705-1708
    • De Nanteuil, G.1    Lila-Ambroise, C.2    Rupin, A.3    Vallez, M.-O.4    Verbeuren, T.J.5
  • 79
    • 44549084070 scopus 로고    scopus 로고
    • S35225 is a direct inhibitor of plasminogen activator inhibitor type-1 activity in the blood
    • A. Rupin, R. Gaertner, P. Mennecier, I. Richard, A. Benoist, G. De Nanteuil, T.J. Verbeuren, S35225 is a direct inhibitor of plasminogen activator inhibitor type-1 activity in the blood, Thromb. Res. 122 (2008) 265e270, http://dx.doi.org/10.1016/j.thromres.2007.11.006.
    • (2008) Thromb. Res. , vol.122 , pp. 265-270
    • Rupin, A.1    Gaertner, R.2    Mennecier, P.3    Richard, I.4    Benoist, A.5    De Nanteuil, G.6    Verbeuren, T.J.7
  • 86
    • 70349165391 scopus 로고    scopus 로고
    • Synthesis and evaluation of pyrrolin-2-one compounds, a series of plasminogen activator inhibitor-1 inhibitors
    • H. Miyazaki, T. Ogiku, H. Sai, Y. Moritani, A. Ohtani, H. Ohmizu, Synthesis and evaluation of pyrrolin-2-one compounds, a series of plasminogen activator inhibitor-1 inhibitors, Chem. Pharm. Bull. (Tokyo) 57 (2009) 979e985, http://dx.doi.org/10.1248/cpb.57.979.
    • (2009) Chem. Pharm. Bull. (Tokyo) , vol.57 , pp. 979-985
    • Miyazaki, H.1    Ogiku, T.2    Sai, H.3    Moritani, Y.4    Ohtani, A.5    Ohmizu, H.6
  • 87
    • 72249087741 scopus 로고    scopus 로고
    • Evaluation of pyrrolin-2-one derivatives synthesized by a new practical method as inhibitors of plasminogen activator inhibitor-1 (PAI-1)
    • H. Miyazaki, T. Miyake, Y. Terakawa, H. Ohmizu, T. Ogiku, A. Ohtani, Evaluation of pyrrolin-2-one derivatives synthesized by a new practical method as inhibitors of plasminogen activator inhibitor-1 (PAI-1), Bioorg. Med. Chem. Lett. 20 (2010) 546e548, http://dx.doi.org/10.1016/j.bmcl.2009.11.102.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 546-548
    • Miyazaki, H.1    Miyake, T.2    Terakawa, Y.3    Ohmizu, H.4    Ogiku, T.5    Ohtani, A.6
  • 91
    • 13244259179 scopus 로고    scopus 로고
    • Tannic acid stimulates glucose transport and inhibits adipocyte differentiation in 3T3-L1 cells 1
    • X. Liu, J. Kim, Y. Li, J. Li, F. Liu, X. Chen, Tannic acid stimulates glucose transport and inhibits adipocyte differentiation in 3T3-L1 cells 1, J. Nutr. 135 (2005) 165e171.
    • (2005) J. Nutr. , vol.135 , pp. 165-171
    • Liu, X.1    Kim, J.2    Li, Y.3    Li, J.4    Liu, F.5    Chen, X.6
  • 93
    • 84890850269 scopus 로고    scopus 로고
    • Mechanistic characterization and crystal structure of a small molecule inactivator bound to plasminogen activator inhibitor-1
    • S.-H. Lia, A.A. Reinke, K.L. Sanders, C.D. Emal, J.C. Whisstock, J.A. Stuckey, D.A. Lawrence, Mechanistic characterization and crystal structure of a small molecule inactivator bound to plasminogen activator inhibitor-1, Proc. Natl. Acad. Sci. U. S. A. 110 (2013) 4941e4949, http://dx.doi.org/10.1073/pnas.1216499110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 4941-4949
    • Lia, S.-H.1    Reinke, A.A.2    Sanders, K.L.3    Emal, C.D.4    Whisstock, J.C.5    Stuckey, J.A.6    Lawrence, D.A.7
  • 94
    • 74049135491 scopus 로고    scopus 로고
    • Novel bisarylsulfonamides and aryl sulfonimides as inactivators of plasminogen activator inhibitor-1 (PAI-1)
    • N.C. El-Ayache, S.-H. Li, M. Warnock, D.A. Lawrence, C.D. Emal, Novel bisarylsulfonamides and aryl sulfonimides as inactivators of plasminogen activator inhibitor-1 (PAI-1), Bioorg. Med. Chem. Lett. 20 (2010) 966e970, http://dx.doi.org/10.1016/j.bmcl.2009.12.051.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 966-970
    • El-Ayache, N.C.1    Li, S.-H.2    Warnock, M.3    Lawrence, D.A.4    Emal, C.D.5
  • 96
    • 79951918138 scopus 로고    scopus 로고
    • Effects of specific chemical suppressors of plasminogen activator inhibitor-1 in cardiovascular diseases
    • J.-I. Suzuki, M. Ogawa, S. Muto, A. Itai, Y. Hirata, Mitsuaki Isobe, R. Nagai, Effects of specific chemical suppressors of plasminogen activator inhibitor-1 in cardiovascular diseases, Expert Opin. Investig. Drugs 20 (2011) 255e264, http://dx.doi.org/10.1517/13543784.2011.546784.
    • (2011) Expert Opin. Investig. Drugs , vol.20 , pp. 255-264
    • Suzuki, J.-I.1    Ogawa, M.2    Muto, S.3    Itai, A.4    Hirata, Y.5    Isobe, M.6    Nagai, R.7
  • 98
    • 84874340538 scopus 로고    scopus 로고
    • Structural insight into inactivation of plasminogen activator inhibitor-1 by a smallmolecule antagonist
    • Z. Lin, J. Jensen, Z. Hong, X. Shi, L. Hu, P.A. Andreasen, M. Huang, Structural insight into inactivation of plasminogen activator inhibitor-1 by a smallmolecule antagonist, Chem. Biol. 20 (2013) 253e261, http://dx.doi.org/10.1016/j.chembiol.2013.01.002.
    • (2013) Chem. Biol. , vol.20 , pp. 253-261
    • Lin, Z.1    Jensen, J.2    Hong, Z.3    Shi, X.4    Hu, L.5    Andreasen, P.A.6    Huang, M.7
  • 99
    • 0017326573 scopus 로고
    • Some pharmacological investigations of embelin and its semisynthetic derivatives
    • O. Gupta, M. Ali, G. Ray, C. Atal, Some pharmacological investigations of embelin and its semisynthetic derivatives, Indian J. Physiol. Pharmacol. 21 (1976) 31e39.
    • (1976) Indian J. Physiol. Pharmacol. , vol.21 , pp. 31-39
    • Gupta, O.1    Ali, M.2    Ray, G.3    Atal, C.4
  • 101
    • 2642603246 scopus 로고
    • Synthesis of embelin, rapanone and related quinones
    • L.F. Fieser, E.M. Chambrel, Synthesis of embelin, rapanone and related quinones, J. Am. Chem. Soc. 70 (1948) 71e75.
    • (1948) J. Am. Chem. Soc. , vol.70 , pp. 71-75
    • Fieser, L.F.1    Chambrel, E.M.2
  • 102
    • 84899650270 scopus 로고    scopus 로고
    • Design, synthesis, and SAR of embelin analogues as the inhibitors of PAI-1 (plasminogen activator inhibitor-1)
    • F. Chen, G. Zhang, Z. Hong, Z. Lin, M. Lei, M. Huang, L. Hu, Design, synthesis, and SAR of embelin analogues as the inhibitors of PAI-1 (plasminogen activator inhibitor-1), Bioorg. Med. Chem. Lett. 24 (2014) 2379e2382, http://dx.doi.org/10.1016/j.bmcl.2014.03.045.
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 2379-2382
    • Chen, F.1    Zhang, G.2    Hong, Z.3    Lin, Z.4    Lei, M.5    Huang, M.6    Hu, L.7
  • 104
    • 0025371467 scopus 로고
    • Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene
    • L. Erickson, G. Fici, J. Lund, T. Boyle, H.G. Polites, K.R. Marotti, Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene, Nature 346 (1990) 74e76, http://dx.doi.org/10.1038/346074a0.
    • (1990) Nature , vol.346 , pp. 74-76
    • Erickson, L.1    Fici, G.2    Lund, J.3    Boyle, T.4    Polites, H.G.5    Marotti, K.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.