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Volumn 74, Issue 3, 2008, Pages 641-653

A peptide accelerating the conversion of plasminogen activator inhibitor-1 to an inactive latent state

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; CYSTEINE; HEPARIN; HYBRID PROTEIN; LIGAND; MONOCLONAL ANTIBODY; PAIONIN 4 PROTEIN; PEPTIDE LIBRARY; PLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR INHIBITOR 1; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 50449087284     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.108.046417     Document Type: Article
Times cited : (23)

References (60)
  • 1
    • 45349091918 scopus 로고    scopus 로고
    • A cyclic peptidylic inhibitor of murine urokinase-type plasminogen activator: Changing species specificity by substitution of a single residue
    • Andersen LM, Wind T, Hansen HD, and Andreasen PA (2008) A cyclic peptidylic inhibitor of murine urokinase-type plasminogen activator: Changing species specificity by substitution of a single residue. Biochem J 412:447-457.
    • (2008) Biochem J , vol.412 , pp. 447-457
    • Andersen, L.M.1    Wind, T.2    Hansen, H.D.3    Andreasen, P.A.4
  • 2
    • 35348834104 scopus 로고    scopus 로고
    • PAI-1 - a potential therapeutic target in cancer
    • Andreasen PA (2007) PAI-1 - a potential therapeutic target in cancer. Curr Drug Targets 8:1030-1041.
    • (2007) Curr Drug Targets , vol.8 , pp. 1030-1041
    • Andreasen, P.A.1
  • 3
    • 0033018464 scopus 로고    scopus 로고
    • Solvent effects on activity and conformation of plasminogen activator inhibitor-1
    • Andreasen PA, Egelund R, Jensen S, and Rodenburg KW (1999) Solvent effects on activity and conformation of plasminogen activator inhibitor-1. Thromb Haemost 81:407-414.
    • (1999) Thromb Haemost , vol.81 , pp. 407-414
    • Andreasen, P.A.1    Egelund, R.2    Jensen, S.3    Rodenburg, K.W.4
  • 4
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen PA, Egelund R, and Petersen HH (2000) The plasminogen activation system in tumor growth, invasion, and metastasis. Cell Mol Life Sci 57:25-40.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 5
    • 0030788411 scopus 로고    scopus 로고
    • The urokinase-type plasminogen activator system in cancer metastasis: A review
    • Andreasen PA, Kjøller L, Christensen L, and Duffy MJ (1997) The urokinase-type plasminogen activator system in cancer metastasis: a review. Int J Cancer 72:1-22.
    • (1997) Int J Cancer , vol.72 , pp. 1-22
    • Andreasen, P.A.1    Kjøller, L.2    Christensen, L.3    Duffy, M.J.4
  • 6
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas MB, Lawrence DA, and Ginsburg D (1995) Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J 14:2969-2977.
    • (1995) EMBO J , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 7
    • 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
    • Björquist P, Ehnebom J, Inghardt T, Hansson L, Lindberg M, Linschoten M, Strömqvist M, and Deinum J (1998) Identification of the binding site for a lowmolecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis. Biochemistry 37:1227-1234.
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Björquist, P.1    Ehnebom, J.2    Inghardt, T.3    Hansson, L.4    Lindberg, M.5    Linschoten, M.6    Strömqvist, M.7    Deinum, J.8
  • 8
    • 0142095053 scopus 로고    scopus 로고
    • Mutation of the highly conserved tryptophan in the serpin breach region alters the inhibitory mechanism of plasminogen activator inhibitor-1
    • Blouse GE, Perron MJ, Kvassman JO, Yunus S, Thompson JH, Betts RL, Lutter LC, and Shore JD (2003) Mutation of the highly conserved tryptophan in the serpin breach region alters the inhibitory mechanism of plasminogen activator inhibitor-1. Biochemistry 42:12260-12272.
    • (2003) Biochemistry , vol.42 , pp. 12260-12272
    • Blouse, G.E.1    Perron, M.J.2    Kvassman, J.O.3    Yunus, S.4    Thompson, J.H.5    Betts, R.L.6    Lutter, L.C.7    Shore, J.D.8
  • 9
    • 0038071502 scopus 로고    scopus 로고
    • Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents
    • Bødker JS, Wind T, Jensen JK, Hansen M, Pedersen KE, and Andreasen PA (2003) Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents. Eur J Biochem 270:1672-1679.
    • (2003) Eur J Biochem , vol.270 , pp. 1672-1679
    • Bødker, J.S.1    Wind, T.2    Jensen, J.K.3    Hansen, M.4    Pedersen, K.E.5    Andreasen, P.A.6
  • 10
    • 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 P, Chicarelli-Robinson I, Collins M, Faint R, Latham C, Shaw I, and Trew S (1996) Inhibition of plasminogen activator inhibitor-1 activity by two diketopiperazines, XR330 and XR334 produced by Streptomyces sp. J Antibiot (Tokyo) 49:1014-1021.
    • (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
  • 13
    • 0032827853 scopus 로고    scopus 로고
    • Inhibition of plasminogen activator inhibitor-1 by 11-keto-9(E),12(E)-octadecadienoic acid, a novel fatty acid produced by Trichoderma sp
    • Chikanishi T, Shinohara C, Kikuchi T, Endo A, and Hasumi K (1999) Inhibition of plasminogen activator inhibitor-1 by 11-keto-9(E),12(E)-octadecadienoic acid, a novel fatty acid produced by Trichoderma sp. J Antibiot (Tokyo) 52:797-802.
    • (1999) J Antibiot (Tokyo) , vol.52 , pp. 797-802
    • Chikanishi, T.1    Shinohara, C.2    Kikuchi, T.3    Endo, A.4    Hasumi, K.5
  • 14
    • 12544250776 scopus 로고    scopus 로고
    • Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy
    • Crandall DL, Elokdah H, Di L, Hennan JK, Gorlatova NV, and Lawrence DA (2004) Characterization and comparative evaluation of a structurally unique PAI-1 inhibitor exhibiting oral in-vivo efficacy. J Thromb Haemost 2:1422-1428.
    • (2004) J Thromb Haemost , vol.2 , pp. 1422-1428
    • Crandall, D.L.1    Elokdah, H.2    Di, L.3    Hennan, J.K.4    Gorlatova, N.V.5    Lawrence, D.A.6
  • 15
    • 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, and Collen D (1995) Immunoassay of murine t-PA, u-PA and PAI-1 using monoclonal antibodies raised in gene-inactivated mice. Thromb Haemost 74:1305-1309.
    • (1995) Thromb Haemost , vol.74 , pp. 1305-1309
    • Declerck, P.J.1    Verstreken, M.2    Collen, D.3
  • 16
    • 0037687834 scopus 로고    scopus 로고
    • New fibrinolytic agents: Benzothiophene derivatives as inhibitors of the t-PA-PAI-1 complex formation
    • De Nanteuil G, Lila-Ambroise C, Rupin A, Vallez MO, and Verbeuren TJ (2003) New fibrinolytic agents: benzothiophene derivatives as inhibitors of the t-PA-PAI-1 complex formation. Bioorg Med Chem Lett 13:1705-1708.
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 1705-1708
    • De Nanteuil, G.1    Lila-Ambroise, C.2    Rupin, A.3    Vallez, M.O.4    Verbeuren, T.J.5
  • 19
    • 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, Nielsen RW, Christensen A, Deinum J, and Andreasen PA (2001a) 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 276:13077-13086.
    • (2001) J 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
  • 20
    • 0034832458 scopus 로고    scopus 로고
    • A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism
    • Egelund R, Petersen TE, and Andreasen PA (2001b) A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism. Eur J Biochem 268:673-685.
    • (2001) Eur J Biochem , vol.268 , pp. 673-685
    • Egelund, R.1    Petersen, T.E.2    Andreasen, P.A.3
  • 22
    • 0026755995 scopus 로고
    • Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin
    • Ehrlich HJ, Gebbink RK, Keijer J, and Pannekoek H (1992) Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin. J Biol Chem 267:11606-11611.
    • (1992) J Biol Chem , vol.267 , pp. 11606-11611
    • Ehrlich, H.J.1    Gebbink, R.K.2    Keijer, J.3    Pannekoek, H.4
  • 25
    • 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, Golec J, Faint R, Brooks T, and Charlton P (2001) Synthesis and in vitro evaluation of a series of diketopiperazine inhibitors of plasminogen activator inhibitor-1. Bioorg Med Chem Lett 11:2589-2592.
    • (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
  • 27
    • 0242643928 scopus 로고    scopus 로고
    • Selection of peptides that bind to plasminogen activator inhibitor 1 (PAI-1) using random peptide phage-display libraries
    • Gårdsvoll H, van Zonneveld AJ, Holm A, Eldering E, van Meijer M, Danø K, and Pannekoek H (1998) Selection of peptides that bind to plasminogen activator inhibitor 1 (PAI-1) using random peptide phage-display libraries. FEBS Lett 431:170-174.
    • (1998) FEBS Lett , vol.431 , pp. 170-174
    • Gårdsvoll, H.1    van Zonneveld, A.J.2    Holm, A.3    Eldering, E.4    van Meijer, M.5    Danø, K.6    Pannekoek, H.7
  • 28
    • 0031850760 scopus 로고    scopus 로고
    • Modulation of plasminogen activator inhibitor 1 by Triton X-100- identification of two consecutive conformational transitions
    • Gils A and Declerck PJ (1998) Modulation of plasminogen activator inhibitor 1 by Triton X-100- identification of two consecutive conformational transitions. Thromb Haemost 80:286-291.
    • (1998) Thromb Haemost , vol.80 , pp. 286-291
    • Gils, A.1    Declerck, P.J.2
  • 29
    • 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
    • Gils A and Declerck PJ (2004) The structural basis for the pathophysiological relevance of PAI-I in cardiovascular diseases and the development of potential PAI-I inhibitors. Thromb Haemost 91:425-437.
    • (2004) Thromb Haemost , vol.91 , pp. 425-437
    • Gils, A.1    Declerck, P.J.2
  • 30
    • 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, and Declerck PJ (2000) Glycosylation dependent conformational transitions in plasminogen activator inhibitor-1: evidence for the presence of two active conformations. Fibrinolysis Proteolysis 14:58-64.
    • (2000) Fibrinolysis Proteolysis , vol.14 , pp. 58-64
    • Gils, A.1    Knockaert, I.2    Brouwers, E.3    Declerck, P.J.4
  • 34
    • 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, Crandall DL, and Lawrence DA (2003) Mapping of a conformational epitope on plasminogen activator inhibitor-1 by random mutagenesis. Implications for serpin function. J Biol Chem 278:16329-16335.
    • (2003) J Biol Chem , vol.278 , pp. 16329-16335
    • Gorlatova, N.V.1    Elokdah, H.2    Fan, K.3    Crandall, D.L.4    Lawrence, D.A.5
  • 35
    • 33644669437 scopus 로고    scopus 로고
    • A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition
    • Hansen M, Wind T, Blouse GE, Christensen A, Petersen HH, Kjelgaard S, Mathiasen L, Holtet TL, and Andreasen PA (2005) A urokinase-type plasminogen activator-inhibiting cyclic peptide with an unusual P2 residue and an extended protease binding surface demonstrates new modalities for enzyme inhibition. J Biol Chem 280:38424-38437.
    • (2005) J Biol Chem , vol.280 , pp. 38424-38437
    • Hansen, M.1    Wind, T.2    Blouse, G.E.3    Christensen, A.4    Petersen, H.H.5    Kjelgaard, S.6    Mathiasen, L.7    Holtet, T.L.8    Andreasen, P.A.9
  • 36
    • 33746503823 scopus 로고    scopus 로고
    • Shape-shifting serpins-advantages of a mobile mechanism
    • Huntington JA (2006) Shape-shifting serpins-advantages of a mobile mechanism. Trends Biochem Sci 31:427-435.
    • (2006) Trends Biochem Sci , vol.31 , pp. 427-435
    • Huntington, J.A.1
  • 37
    • 33750559320 scopus 로고    scopus 로고
    • Inhibition of plasminogen activator inhibitor-1 binding to endocytosis receptors of the low-density-lipoprotein receptor family by a peptide isolated from a phage display library
    • Jensen JK, Malmendal A, Schiøtt B, Skeldal S, Pedersen KE, Celik L, Nielsen NC, Andreasen PA, and Wind T (2006) Inhibition of plasminogen activator inhibitor-1 binding to endocytosis receptors of the low-density-lipoprotein receptor family by a peptide isolated from a phage display library. Biochem J 399:387-396.
    • (2006) Biochem J , vol.399 , pp. 387-396
    • Jensen, J.K.1    Malmendal, A.2    Schiøtt, B.3    Skeldal, S.4    Pedersen, K.E.5    Celik, L.6    Nielsen, N.C.7    Andreasen, P.A.8    Wind, T.9
  • 38
    • 0027976103 scopus 로고
    • Isolation of a highly specific ligand for the α5β1 integrin from a phage display library
    • Koivunen E, Wang B, and Ruoslahti E (1994) Isolation of a highly specific ligand for the α5β1 integrin from a phage display library. J Cell Biol 124:373-380.
    • (1994) J Cell Biol , vol.124 , pp. 373-380
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 40
    • 0026333459 scopus 로고
    • Type-1 inhibitor of plasminogen activators. Distinction between latent, activated and reactive centre-cleaved forms with thermal stability and monoclonal antibodies
    • Munch M, Heegaard C, Jensen PH, and Andreasen PA (1991) Type-1 inhibitor of plasminogen activators. Distinction between latent, activated and reactive centre-cleaved forms with thermal stability and monoclonal antibodies. FEBS Lett 295:102-106.
    • (1991) FEBS Lett , vol.295 , pp. 102-106
    • Munch, M.1    Heegaard, C.2    Jensen, P.H.3    Andreasen, P.A.4
  • 41
    • 0027290655 scopus 로고
    • Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor
    • Munch M, Heegaard CW, and Andreasen PA (1993) Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim Biophys Acta 1202:29-37.
    • (1993) Biochim Biophys Acta , vol.1202 , pp. 29-37
    • Munch, M.1    Heegaard, C.W.2    Andreasen, P.A.3
  • 42
    • 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, and Declerck PJ (2003) Elucidation of the epitope of a latency-inducing antibody: identification of a new molecular target for PAI-1 inhibition. Thromb Haemost 90:52-58.
    • (2003) Thromb Haemost , vol.90 , pp. 52-58
    • Naessens, D.1    Gils, A.2    Compernolle, G.3    Declerck, P.J.4
  • 44
    • 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, Grøndahl-Hansen J, Huang JY, Kristensen P, and Danø K (1986) Monoclonal antibodies to human 54,000 molecular weight plasminogen activator inhibitor from fibrosarcoma cells-inhibitor neutralization and one-step affinity purification. Thromb Haemost 55:206-212.
    • (1986) Thromb Haemost , vol.55 , pp. 206-212
    • Nielsen, L.S.1    Andreasen, P.A.2    Grøndahl-Hansen, J.3    Huang, J.Y.4    Kristensen, P.5    Danø, K.6
  • 47
    • 0025226070 scopus 로고
    • Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A
    • Schulze AJ, Baumann U, Knof S, Jaeger E, Huber R, and Laurell CB (1990) Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur J Biochem 194:51-56.
    • (1990) Eur J Biochem , vol.194 , pp. 51-56
    • Schulze, A.J.1    Baumann, U.2    Knof, S.3    Jaeger, E.4    Huber, R.5    Laurell, C.B.6
  • 48
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott JK and Smith GP (1990) Searching for peptide ligands with an epitope library. Science 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 49
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore JD, Day DE, Francis-Chmura AM, Verhamme I, Kvassman J, Lawrence DA, and Ginsburg D (1995) A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism. J Biol Chem 270:5395-5398.
    • (1995) J Biol Chem , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 50
    • 50449092585 scopus 로고    scopus 로고
    • Engineered antagonists of uPA and PAI-1. Springer, New York
    • in press
    • Stoppelli MP, Andersen LM, Votta G, and Andreasen PA (2008). Engineered antagonists of uPA and PAI-1. Springer, New York, in press.
    • (2008)
    • Stoppelli, M.P.1    Andersen, L.M.2    Votta, G.3    Andreasen, P.A.4
  • 51
    • 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, and Matthews DJ (2000) Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Biochemistry 39:8460-8469.
    • (2000) Biochemistry , vol.39 , pp. 8460-8469
    • Stout, T.J.1    Graham, H.2    Buckley, D.I.3    Matthews, D.J.4
  • 52
    • 11844294719 scopus 로고    scopus 로고
    • A novel pesticide-induced conformational state of the oestrogen receptor ligand-binding domain, detected by conformation-specific peptide binding
    • Sumbayev VV, Bonefeld-Jørgensen EC, Wind T, and Andreasen PA (2005) A novel pesticide-induced conformational state of the oestrogen receptor ligand-binding domain, detected by conformation-specific peptide binding. FEBS Lett 579:541-548.
    • (2005) FEBS Lett , vol.579 , pp. 541-548
    • Sumbayev, V.V.1    Bonefeld-Jørgensen, E.C.2    Wind, T.3    Andreasen, P.A.4
  • 53
    • 0026471040 scopus 로고
    • A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate
    • Urano T, Strandberg L, Johansson LB, and Ny T (1992) A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate. Eur J Biochem 209:985-992.
    • (1992) Eur J Biochem , vol.209 , pp. 985-992
    • Urano, T.1    Strandberg, L.2    Johansson, L.B.3    Ny, T.4
  • 54
    • 0032185396 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1: A common denominator in cardiovascular disease
    • Vaughan DE (1998) Plasminogen activator inhibitor-1: a common denominator in cardiovascular disease. J Investig Med 46:370-376.
    • (1998) J Investig Med , vol.46 , pp. 370-376
    • Vaughan, D.E.1
  • 55
    • 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 D, Debrock S, Vleugels N, Declerck PJ, and Shore JD (1999) Accelerated conversion of human plasminogen activator inhibitor-1 to its latent form by antibody binding. J Biol Chem 274:17511-17517.
    • (1999) J Biol Chem , vol.274 , pp. 17511-17517
    • Verhamme, I.1    Kvassman, J.O.2    Day, D.3    Debrock, S.4    Vleugels, N.5    Declerck, P.J.6    Shore, J.D.7
  • 57
    • 0036005954 scopus 로고    scopus 로고
    • The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1. Roles of the reactive centre loop, the shutter region, the flexible joint-region and the small serpin fragment
    • Wind T, Hansen M, Jensen JK, and Andreasen PA (2002) The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1. Roles of the reactive centre loop, the shutter region, the flexible joint-region and the small serpin fragment. Biol Chem 383:21-36.
    • (2002) Biol Chem , vol.383 , pp. 21-36
    • Wind, T.1    Hansen, M.2    Jensen, J.K.3    Andreasen, P.A.4
  • 59
    • 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, and Andreasen PA (2001) 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 268:1095-1106.
    • (2001) Eur J Biochem , vol.268 , pp. 1095-1106
    • Wind, T.1    Jensen, M.A.2    Andreasen, P.A.3
  • 60
    • 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
    • Xue Y, Björquist P, Inghardt T, Linschoten M, Musil D, Sjölin L, and Deinum J (1998) 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 6:627-636.
    • (1998) Structure , vol.6 , pp. 627-636
    • Xue, Y.1    Björquist, P.2    Inghardt, T.3    Linschoten, M.4    Musil, D.5    Sjölin, L.6    Deinum, J.7


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