메뉴 건너뛰기




Volumn 165, Issue 2, 2009, Pages 126-132

High quality structure of cleaved PAI-1-stab

Author keywords

Crystal structure; PAI 1; Plasminogen activator inhibitor 1; Rational drug design; Serpin

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1;

EID: 58349083298     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2008.11.001     Document Type: Article
Times cited : (15)

References (56)
  • 1
    • 0029157233 scopus 로고
    • Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1
    • Aertgeerts K., De Bondt H.L., De Ranter C.J., and Declerck P.J. Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat. Struct. Biol. 2 (1995) 891-897
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 891-897
    • Aertgeerts, K.1    De Bondt, H.L.2    De Ranter, C.J.3    Declerck, P.J.4
  • 2
    • 0033018464 scopus 로고    scopus 로고
    • Solvent effects on activity and conformation of plasminogen activator inhibitor-1
    • Andreasen P.A., Egelund R., Jensen S., and Rodenburg K.W. Solvent effects on activity and conformation of plasminogen activator inhibitor-1. Thromb. Haemost. 81 (1999) 407-414
    • (1999) Thromb. Haemost. , vol.81 , pp. 407-414
    • Andreasen, P.A.1    Egelund, R.2    Jensen, S.3    Rodenburg, K.W.4
  • 3
    • 0028064911 scopus 로고
    • Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop
    • Audenaert A.M., Knockaert I., Collen D., and Declerck P.J. Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop. J. Biol. Chem. 269 (1994) 19559-19564
    • (1994) J. Biol. Chem. , vol.269 , pp. 19559-19564
    • Audenaert, A.M.1    Knockaert, I.2    Collen, D.3    Declerck, P.J.4
  • 5
    • 0025892608 scopus 로고
    • Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins
    • Baumann U., Huber R., Bode W., Grosse D., Lesjak M., and Laurell C.B. Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins. J. Mol. Biol. 218 (1991) 595-606
    • (1991) J. Mol. Biol. , vol.218 , pp. 595-606
    • Baumann, U.1    Huber, R.2    Bode, W.3    Grosse, D.4    Lesjak, M.5    Laurell, C.B.6
  • 6
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas M.B., Lawrence D.A., and Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 14 (1995) 2969-2977
    • (1995) EMBO J. , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 7
    • 0034089869 scopus 로고    scopus 로고
    • Importance of the hinge region between a-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neutralizing antibodies
    • Bijnens A.P., Gils A., Knockaert I., Stassen J.M., and Declerck P.J. Importance of the hinge region between a-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. 275 (2000) 6375-6380
    • (2000) J. Biol. Chem. , vol.275 , pp. 6375-6380
    • Bijnens, A.P.1    Gils, A.2    Knockaert, I.3    Stassen, J.M.4    Declerck, P.J.5
  • 8
    • 0035002340 scopus 로고    scopus 로고
    • Elucidation of the binding regions of PAI-1 neutralizing antibodies using chimeric variants of human and rat PAI-1
    • Bijnens A.P., Ngo T.H., Gils A., Dewaele J., Knockaert I., Stassen J.M., and Declerck P.J. Elucidation of the binding regions of PAI-1 neutralizing antibodies using chimeric variants of human and rat PAI-1. Thromb. Haemost. 85 (2001) 866-874
    • (2001) Thromb. Haemost. , vol.85 , pp. 866-874
    • Bijnens, A.P.1    Ngo, T.H.2    Gils, A.3    Dewaele, J.4    Knockaert, I.5    Stassen, J.M.6    Declerck, P.J.7
  • 9
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: the free R value. Methods and applications
    • Brünger A.T. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr. D Biol. Crystallogr. 49 (1993) 24-36
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 24-36
    • Brünger, A.T.1
  • 12
    • 9144257322 scopus 로고    scopus 로고
    • The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant ?
    • De Taeye B., Gils A., and Declerck P.J. The story of the serpin plasminogen activator inhibitor 1: is there any need for another mutant ?. Thromb. Haemost. 92 (2004) 898-924
    • (2004) Thromb. Haemost. , vol.92 , pp. 898-924
    • De Taeye, B.1    Gils, A.2    Declerck, P.J.3
  • 13
    • 0031031869 scopus 로고    scopus 로고
    • Neutralization of plasminogen activator inhibitor-1 inhibitory properties: identification of two different mechanisms
    • Debrock S., and Declerck P.J. Neutralization of plasminogen activator inhibitor-1 inhibitory properties: identification of two different mechanisms. Biochim. Biophys. Acta 1337 (1997) 257-266
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 257-266
    • Debrock, S.1    Declerck, P.J.2
  • 14
    • 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 P.J., De Mol M., Alessi M.C., Baudner S., Paques E.P., Preissner K.T., Muller Berghaus G., and Collen D. 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. 263 (1988) 15454-15461
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3    Baudner, S.4    Paques, E.P.5    Preissner, K.T.6    Muller Berghaus, G.7    Collen, D.8
  • 15
    • 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 P.J., De Mol M., Vaughan D.E., and Collen D. Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a noninhibitory substrate for tissue-type plasminogen activator. J. Biol. Chem. 267 (1992) 11693-11696
    • (1992) J. Biol. Chem. , vol.267 , pp. 11693-11696
    • Declerck, P.J.1    De Mol, M.2    Vaughan, D.E.3    Collen, D.4
  • 18
    • 0025371467 scopus 로고
    • Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene
    • Erickson L.A., Fici G.J., Lund J.E., Boyle T.P., Polites H.G., and Marotti K.R. Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene. Nature 346 (1990) 74-76
    • (1990) Nature , vol.346 , pp. 74-76
    • Erickson, L.A.1    Fici, G.J.2    Lund, J.E.3    Boyle, T.P.4    Polites, H.G.5    Marotti, K.R.6
  • 19
    • 0031755765 scopus 로고    scopus 로고
    • Structure-function relationship in serpins: current concepts and controversies
    • Gils A., and Declerck P.J. Structure-function relationship in serpins: current concepts and controversies. Thromb. Haemost. 80 (1998) 531-541
    • (1998) Thromb. Haemost. , vol.80 , pp. 531-541
    • Gils, A.1    Declerck, P.J.2
  • 20
    • 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., and Declerck P.J. Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 35 (1996) 7474-7481
    • (1996) Biochemistry , vol.35 , pp. 7474-7481
    • Gils, A.1    Knockaert, I.2    Declerck, P.J.3
  • 21
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • Hekman C.M., and Loskutoff D.J. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J. Biol. Chem. 260 (1985) 11581-11587
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 22
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 (2000) 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 23
    • 52949152789 scopus 로고    scopus 로고
    • High resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: a new tool for detailed interaction studies and modeling
    • Jensen J.K., and Gettins P.G.W. High resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: a new tool for detailed interaction studies and modeling. Protein Sci. 17 (2008) 184-1849
    • (2008) Protein Sci. , vol.17 , pp. 184-1849
    • Jensen, J.K.1    Gettins, P.G.W.2
  • 25
    • 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 P.M., Sottrup Jensen L., Justesen J., Rodenburg K.W., and Andreasen P.A. 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. 241 (1996) 38-46
    • (1996) Eur. J. Biochem. , vol.241 , pp. 38-46
    • Kjoller, L.1    Martensen, P.M.2    Sottrup Jensen, L.3    Justesen, J.4    Rodenburg, K.W.5    Andreasen, P.A.6
  • 26
    • 0021225478 scopus 로고
    • Demonstration of a fast-acting inhibitor of plasminogen activators in human plasma
    • Kruithof E.K., Tran Thang C., Ransijn A., and Bachmann F. Demonstration of a fast-acting inhibitor of plasminogen activators in human plasma. Blood 64 (1984) 907-913
    • (1984) Blood , vol.64 , pp. 907-913
    • Kruithof, E.K.1    Tran Thang, C.2    Ransijn, A.3    Bachmann, F.4
  • 27
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 28
    • 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., and Ny T. Purification of active human plasminogen activator inhibitor 1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells. Eur. J. Biochem. 186 (1989) 523-533
    • (1989) Eur. J. Biochem. , vol.186 , pp. 523-533
    • Lawrence, D.1    Strandberg, L.2    Grundstrom, T.3    Ny, T.4
  • 29
    • 0027945176 scopus 로고
    • Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition
    • Lawrence D.A., Olson S.T., Palaniappan S., and Ginsburg D. Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition. J. Biol. Chem. 269 (1994) 27657-27662
    • (1994) J. Biol. Chem. , vol.269 , pp. 27657-27662
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 30
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H., Tokuoka R., Deisenhofer J., and Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177 (1984) 531-557
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 31
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 0027290655 scopus 로고
    • Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor
    • Munch M., Heegaard C.W., and Andreasen P.A. Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim. Biophys. Acta 1202 (1993) 29-37
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 29-37
    • Munch, M.1    Heegaard, C.W.2    Andreasen, P.A.3
  • 36
    • 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 J.M., Lang D., Gils A., and Declerck P.J. Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. J. Mol. Biol. 297 (2000) 683-695
    • (2000) J. Mol. Biol. , vol.297 , pp. 683-695
    • Nar, H.1    Bauer, M.2    Stassen, J.M.3    Lang, D.4    Gils, A.5    Declerck, P.J.6
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter Jr. C.W., and Sweet R.M. (Eds), Academic Press, New York
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter Jr. C.W., and Sweet R.M. (Eds). Methods in Enzymology (1997), Academic Press, New York 307-326
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0026075399 scopus 로고
    • A critical review of the evidence supporting a relationship between impaired fibrinolytic activity and venous thromboembolism
    • Prins M.H., and Hirsh J. A critical review of the evidence supporting a relationship between impaired fibrinolytic activity and venous thromboembolism. Arch. Intern. Med. 151 (1991) 1721-1731
    • (1991) Arch. Intern. Med. , vol.151 , pp. 1721-1731
    • Prins, M.H.1    Hirsh, J.2
  • 40
    • 0027965876 scopus 로고
    • Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Escherichia coli
    • Sancho E., Tonge D.W., Hockney R.C., and Booth N.A. Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Escherichia coli. Eur. J. Biochem. 224 (1994) 125-134
    • (1994) Eur. J. Biochem. , vol.224 , pp. 125-134
    • Sancho, E.1    Tonge, D.W.2    Hockney, R.C.3    Booth, N.A.4
  • 41
    • 0009448606 scopus 로고    scopus 로고
    • Vitronectin and substitution of a b-strand 5A lysine residue potentiate activity-neutralization of PA inhibitor-1 by monoclonal antibodies against a-helix F
    • Schousboe S.L., Egelund R., Kirkegaard T., Preissner K.T., Rodenburg K.W., and Andreasen P.A. Vitronectin and substitution of a b-strand 5A lysine residue potentiate activity-neutralization of PA inhibitor-1 by monoclonal antibodies against a-helix F. Thromb. Haemost. 83 (2000) 742-751
    • (2000) Thromb. Haemost. , vol.83 , pp. 742-751
    • Schousboe, S.L.1    Egelund, R.2    Kirkegaard, T.3    Preissner, K.T.4    Rodenburg, K.W.5    Andreasen, P.A.6
  • 42
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B., Ginsburg D., Lawrence D.A., and Read R.J. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure 7 (1999) 111-118
    • (1999) Structure , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3    Carrell, R.W.4    Berkenpas, M.B.5    Ginsburg, D.6    Lawrence, D.A.7    Read, R.J.8
  • 43
    • 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 J.D., Day D.E., Francis Chmura A.M., Verhamme I., Kvassman J., Lawrence D.A., and Ginsburg D. 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 (1995) 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
  • 44
    • 0033841662 scopus 로고    scopus 로고
    • Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition
    • Simonovic M., Gettins P.G.W., and Volz K. Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition. Protein Sci. 9 (2000) 1423-1427
    • (2000) Protein Sci. , vol.9 , pp. 1423-1427
    • Simonovic, M.1    Gettins, P.G.W.2    Volz, K.3
  • 45
    • 58349097139 scopus 로고    scopus 로고
    • Stein, P.E., Baek, K., 2002. 1.8 Å resolution structure of latent plasminogen activator inhibitor-1. Protein data bank code 11j5.
    • Stein, P.E., Baek, K., 2002. 1.8 Å resolution structure of latent plasminogen activator inhibitor-1. Protein data bank code 11j5.
  • 46
    • 0035951303 scopus 로고    scopus 로고
    • Different structural requirements for plasminogen activator inhibitor 1 (PAI-1) during latency transition and proteinase inhibition as evidenced by phage-displayed hypermutated PAI-1 libraries
    • Stoop A.A., Eldering E., Dafforn T.R., Read R.J., and Pannekoek H. Different structural requirements for plasminogen activator inhibitor 1 (PAI-1) during latency transition and proteinase inhibition as evidenced by phage-displayed hypermutated PAI-1 libraries. J. Mol. Biol. 305 (2001) 773-783
    • (2001) J. Mol. Biol. , vol.305 , pp. 773-783
    • Stoop, A.A.1    Eldering, E.2    Dafforn, T.R.3    Read, R.J.4    Pannekoek, H.5
  • 47
    • 0034713878 scopus 로고    scopus 로고
    • Structures of active and latent PAI-1: a possible stabilizing role for chloride ions
    • Stout T.J., Graham H., Buckley D.I., and Matthews D.J. Structures of active and latent PAI-1: a possible stabilizing role for chloride ions. Biochemistry 39 (2000) 8460-8469
    • (2000) Biochemistry , vol.39 , pp. 8460-8469
    • Stout, T.J.1    Graham, H.2    Buckley, D.I.3    Matthews, D.J.4
  • 48
    • 0029317438 scopus 로고
    • Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition [letter]
    • Tucker H.M., Mottonen J., Goldsmith E.J., and Gerard R.D. Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition [letter]. Nat. Struct. Biol. 2 (1995) 442-445
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 442-445
    • Tucker, H.M.1    Mottonen, J.2    Goldsmith, E.J.3    Gerard, R.D.4
  • 49
    • 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 L.B., and Ny T. A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate. Eur. J. Biochem. 209 (1992) 985-992
    • (1992) Eur. J. Biochem. , vol.209 , pp. 985-992
    • Urano, T.1    Strandberg, L.2    Johansson, L.B.3    Ny, T.4
  • 50
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 51
    • 0028786263 scopus 로고
    • Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis: an update
    • van Meijer M., and Pannekoek H. Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis: an update. Fibrinolysis 9 (1995) 261-276
    • (1995) Fibrinolysis , vol.9 , pp. 261-276
    • van Meijer, M.1    Pannekoek, H.2
  • 52
    • 33846704118 scopus 로고    scopus 로고
    • Evaluation of the mechanism of inactivation of plasminogen activator inhibitor-1 by monoclonal antibodies using a stable variant
    • Vleugels N., Gils A., Mannaerts S., Knockaert I., and Declerck P.J. Evaluation of the mechanism of inactivation of plasminogen activator inhibitor-1 by monoclonal antibodies using a stable variant. Fibrinolysis Proteol. 12 (1998) 277-282
    • (1998) Fibrinolysis Proteol. , vol.12 , pp. 277-282
    • Vleugels, N.1    Gils, A.2    Mannaerts, S.3    Knockaert, I.4    Declerck, P.J.5
  • 53
    • 0032615858 scopus 로고    scopus 로고
    • Predictive value of fibrinolytic factors in coronary heart disease
    • Wiman B. Predictive value of fibrinolytic factors in coronary heart disease. Scand. J. Clin. Lab. Invest. 59 (1999) 23-31
    • (1999) Scand. J. Clin. Lab. Invest. , vol.59 , pp. 23-31
    • Wiman, B.1
  • 54
    • 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 M.A., and Andreasen P.A. 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 (2001) 1095-1106
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1095-1106
    • Wind, T.1    Jensen, M.A.2    Andreasen, P.A.3
  • 55
    • 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., Linschoten M., Musil D., Sjölin L., and Deinum J. 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 6 (1998) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.