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Volumn 15, Issue 9, 2007, Pages 1105-1116

Study of Recombinant Antibody Fragments and PAI-1 Complexes Combining Protein-Protein Docking and Results from Site-Directed Mutagenesis (DOI:10.1016/j.str.2007.07.009);Study of Recombinant Antibody Fragments and PAI-1 Complexes Combining Protein-Protein Docking and Results from Site-Directed Mutagenesis

Author keywords

PROTEINS

Indexed keywords

MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MA 56A7C10; MONOCLONAL ANTIBODY MA 8H9D4; NEUTRALIZING ANTIBODY; PLASMINOGEN ACTIVATOR INHIBITOR 1; RECOMBINANT ANTIBODY; UNCLASSIFIED DRUG;

EID: 34548410760     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2007.09.002     Document Type: Erratum
Times cited : (7)

References (86)
  • 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
    • 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 M.C., Peiretti F., Morange P., Henry M., Nalbone G., and Juhan-Vague I. Production of plasminogen activator inhibitor 1 by human adipose tissue: possible link between visceral fat accumulation and vascular disease. Diabetes 46 (1997) 860-867
    • (1997) Diabetes , vol.46 , pp. 860-867
    • Alessi, M.C.1    Peiretti, F.2    Morange, P.3    Henry, M.4    Nalbone, G.5    Juhan-Vague, I.6
  • 3
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B., Lesk A.M., and Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273 (1997) 927-948
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 4
    • 2642518000 scopus 로고    scopus 로고
    • Hydrophobic complementarity in protein-protein docking
    • Berchanski A., Shapira B., and Eisenstein M. Hydrophobic complementarity in protein-protein docking. Proteins 56 (2004) 130-142
    • (2004) Proteins , vol.56 , pp. 130-142
    • Berchanski, A.1    Shapira, B.2    Eisenstein, M.3
  • 6
    • 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 C.N., Lunven C., Lechaire I., Girardot C., and O'Connor S.E. 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. 25 (1998) 29-34
    • (1998) Br. J. Pharmacol. , vol.25 , pp. 29-34
    • Berry, C.N.1    Lunven, C.2    Lechaire, I.3    Girardot, C.4    O'Connor, S.E.5
  • 7
    • 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 A.P., Gils A., Stassen J.M., Komissarov A.A., Knockaert I., Brouwers E., Shore J.D., and Declerck P.J. The distal hinge of the reactive site loop and its proximity: a target to modulate plasminogen activator inhibitor-1 activity. J. Biol. Chem. 276 (2001) 44912-44918
    • (2001) J. Biol. Chem. , vol.276 , pp. 44912-44918
    • Bijnens, A.P.1    Gils, A.2    Stassen, J.M.3    Komissarov, A.A.4    Knockaert, I.5    Brouwers, E.6    Shore, J.D.7    Declerck, P.J.8
  • 8
    • 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., Hansson L., Lindberg M., Linschoten M., Stromqvist M., and Deinum J. Identification of the binding site for a low-molecular-weight inhibitor of plasminogen activator inhibitor type 1 by site-directed mutagenesis. Biochemistry 37 (1998) 1227-1234
    • (1998) Biochemistry , vol.37 , pp. 1227-1234
    • Bjorquist, P.1    Ehnebom, J.2    Inghardt, T.3    Hansson, L.4    Lindberg, M.5    Linschoten, M.6    Stromqvist, M.7    Deinum, J.8
  • 10
    • 0023173201 scopus 로고
    • Prediction of the folding of short polypeptide segments by uniform conformational sampling
    • Bruccoleri R.E., and Karplus M. Prediction of the folding of short polypeptide segments by uniform conformational sampling. Biopolymers 26 (1987) 137-168
    • (1987) Biopolymers , vol.26 , pp. 137-168
    • Bruccoleri, R.E.1    Karplus, M.2
  • 12
    • 0038359596 scopus 로고    scopus 로고
    • Successful discrimination of protein interactions
    • Camacho C.J., and Gatchell D.W. Successful discrimination of protein interactions. Proteins 52 (2003) 92-97
    • (2003) Proteins , vol.52 , pp. 92-97
    • Camacho, C.J.1    Gatchell, D.W.2
  • 13
    • 0034663658 scopus 로고    scopus 로고
    • Scoring docked conformations generated by rigid-body protein-protein docking
    • Camacho C.J., Gatchell D.W., Kimura S.R., and Vajda S. Scoring docked conformations generated by rigid-body protein-protein docking. Proteins 40 (2000) 525-537
    • (2000) Proteins , vol.40 , pp. 525-537
    • Camacho, C.J.1    Gatchell, D.W.2    Kimura, S.R.3    Vajda, S.4
  • 16
    • 0038526303 scopus 로고    scopus 로고
    • ZDOCK: an initial-stage protein docking algorithm
    • Chen R., Li L., and Weng Z. ZDOCK: an initial-stage protein docking algorithm. Proteins 52 (2003) 80-87
    • (2003) Proteins , vol.52 , pp. 80-87
    • Chen, R.1    Li, L.2    Weng, Z.3
  • 17
  • 19
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: an automated docking and discrimination method for the prediction of protein complexes
    • Comeau S.R., Gatchell D.W., Vajda S., and Camacho C.J. ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20 (2004) 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 20
    • 21644472422 scopus 로고    scopus 로고
    • Performance of the first docking server ClusPro in CAPRI runds 3-5
    • Comeau S.R., Vajda S., and Camacho C.J. Performance of the first docking server ClusPro in CAPRI runds 3-5. Proteins 60 (2005) 239-244
    • (2005) Proteins , vol.60 , pp. 239-244
    • Comeau, S.R.1    Vajda, S.2    Camacho, C.J.3
  • 22
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D.R., and Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 93 (1996) 7-12
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 23
    • 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
  • 24
    • 0030896006 scopus 로고    scopus 로고
    • Cloning of a single-chain variable fragment (scFv) switching active plasminogen activator inhibitor-1 to substrate
    • Debrock S., Sironi L., and Declerck P.J. Cloning of a single-chain variable fragment (scFv) switching active plasminogen activator inhibitor-1 to substrate. Gene 189 (1997) 83-88
    • (1997) Gene , vol.189 , pp. 83-88
    • Debrock, S.1    Sironi, L.2    Declerck, P.J.3
  • 25
    • 0025319933 scopus 로고
    • Measurement of plasminogen activator inhibitor 1 (PAI-1) in plasma with various monoclonal antibody-based enzyme-linked immunosorbent assays
    • Declerck P.J., and Collen D. Measurement of plasminogen activator inhibitor 1 (PAI-1) in plasma with various monoclonal antibody-based enzyme-linked immunosorbent assays. Throm. Res. Suppl. 10 (1990) 3-9
    • (1990) Throm. Res. Suppl. , vol.10 , pp. 3-9
    • Declerck, P.J.1    Collen, D.2
  • 26
    • 0026664170 scopus 로고
    • Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as noninhibitory substrate for tissue-type plasminigen 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 noninhibitory substrate for tissue-type plasminigen 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
  • 28
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet J., De Maeyer M., Haze B., and Lasters I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature 356 (1992) 539-542
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Haze, B.3    Lasters, I.4
  • 30
    • 4344586901 scopus 로고    scopus 로고
    • Comparative analysis of the proteinase specificity in wild-type and stabilized plasminogen activator inhibitor-1: evidence for contribution of intramolecular flexibility
    • De Taeye B., Gils A., Vleugels N., Rabijns A., and Declerck P.J. Comparative analysis of the proteinase specificity in wild-type and stabilized plasminogen activator inhibitor-1: evidence for contribution of intramolecular flexibility. Biochem. Biophys. Res. Commun. 321 (2004) 746-751
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 746-751
    • De Taeye, B.1    Gils, A.2    Vleugels, N.3    Rabijns, A.4    Declerck, P.J.5
  • 31
    • 2442423093 scopus 로고    scopus 로고
    • Site-directed targeting of Plasminogen Activator Inhibitor-1 as an example for a novel approach in rational drug design
    • De Taeye B., Compernolle G., and Declerck P.J. Site-directed targeting of Plasminogen Activator Inhibitor-1 as an example for a novel approach in rational drug design. J. Biol. Chem. 279 (2004) 20447-20450
    • (2004) J. Biol. Chem. , vol.279 , pp. 20447-20450
    • De Taeye, B.1    Compernolle, G.2    Declerck, P.J.3
  • 32
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C., Boelens R., and Bonvin A.M. HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J. Am. Chem. Soc. 125 (2003) 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 34
    • 3042687515 scopus 로고    scopus 로고
    • Tiplaxtinin, a novel, orally efficacious inhibitor of plasminogen activator inhibitor-1: design, synthesis, and preclinical characterization
    • Elokdah H., Abou-Gharbia M., Hennan J.K., McFarlane G., Mugford C.P., Krishnamurthy G., and Crandall D.L. Tiplaxtinin, a novel, orally efficacious inhibitor of plasminogen activator inhibitor-1: design, synthesis, and preclinical characterization. J. Med. Chem. 47 (2004) 3491-3494
    • (2004) J. Med. Chem. , vol.47 , pp. 3491-3494
    • Elokdah, H.1    Abou-Gharbia, M.2    Hennan, J.K.3    McFarlane, G.4    Mugford, C.P.5    Krishnamurthy, G.6    Crandall, D.L.7
  • 35
    • 17344380633 scopus 로고    scopus 로고
    • ICM-DISCO docking by global energy optimization with fully flexible side-chains
    • Fernandez-Recio J., Totrov M., and Abagyan R. ICM-DISCO docking by global energy optimization with fully flexible side-chains. Proteins 52 (2003) 113-117
    • (2003) Proteins , vol.52 , pp. 113-117
    • Fernandez-Recio, J.1    Totrov, M.2    Abagyan, R.3
  • 36
    • 0035829167 scopus 로고    scopus 로고
    • Synthesis and in vitro evaluation of diketopiperazine inhibitors of plasminogen activator inhibitor-1
    • Folkes A., Roe M.B., Sohal S., Golec J., Faint R., Brooks T., and Charlton P. Synthesis and in vitro evaluation of diketopiperazine inhibitors of plasminogen activator inhibitor-1. Bioorg. Med. Chem. Lett. 11 (2001) 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
  • 37
    • 1642318429 scopus 로고    scopus 로고
    • The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitors
    • Gils A., and Declerck P.J. The structural basis for the pathophysiological relevance of PAI-1 in cardiovascular diseases and the development of potential PAI-1 inhibitors. Thromb. Haemost. 91 (2004) 425-437
    • (2004) Thromb. Haemost. , vol.91 , pp. 425-437
    • Gils, A.1    Declerck, P.J.2
  • 39
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid body displacement and side-chain conformations
    • Gray J.J., Moughon S.E., Wang C., Schueler-Furman O., Misura K.M., Morozov A.V., and Baker D. Protein-protein docking with simultaneous optimization of rigid body displacement and side-chain conformations. J. Mol. Biol. 331 (2003) 281-299
    • (2003) J. Mol. Biol. , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.E.2    Wang, C.3    Schueler-Furman, O.4    Misura, K.M.5    Morozov, A.V.6    Baker, D.7
  • 40
    • 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
  • 41
    • 0023883856 scopus 로고
    • Bovine plasminogen activator inhibitor 1: specificity determinations and comparison of the active, latent, and guanidine-activated forms
    • Hekman C.M., and Loskutoff D.J. Bovine plasminogen activator inhibitor 1: specificity determinations and comparison of the active, latent, and guanidine-activated forms. Biochemistry 19 (1988) 2911-2918
    • (1988) Biochemistry , vol.19 , pp. 2911-2918
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 42
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of α1-antitrypsin for the structure and functions of serpins
    • Huber R., and Carrel R.W. Implications of the three-dimensional structure of α1-antitrypsin for the structure and functions of serpins. Biochemistry 28 (1989) 8951-8966
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrel, R.W.2
  • 43
    • 0024246956 scopus 로고
    • Surface, subunit interfaces and interior of oligomeric proteins
    • Janin J., Miller S., and Chothia C. Surface, subunit interfaces and interior of oligomeric proteins. J. Mol. Biol. 204 (1988) 155-164
    • (1988) J. Mol. Biol. , vol.204 , pp. 155-164
    • Janin, J.1    Miller, S.2    Chothia, C.3
  • 46
    • 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 A.J., Ehrlich H.J., de Boer J.P., and Pannekoek H. 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 78 (1991) 401-409
    • (1991) Blood , vol.78 , pp. 401-409
    • Keijer, J.1    Linders, M.2    van Zonneveld, A.J.3    Ehrlich, H.J.4    de Boer, J.P.5    Pannekoek, H.6
  • 47
    • 0028881975 scopus 로고
    • SURFNET: a program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski R.A. SURFNET: a program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13 (1995) 323-330
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 48
    • 0000243829 scopus 로고
    • PROCHECK - a program to check the stereochemical quality of protein structures
    • Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26 (1993) 283-291
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 49
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B.K., and Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 50
    • 0242299200 scopus 로고    scopus 로고
    • RDOCK: refinement of rigid body protein docking predictions
    • Li L., Chen R., and Weng Z.P. RDOCK: refinement of rigid body protein docking predictions. Proteins 53 (2003) 693-707
    • (2003) Proteins , vol.53 , pp. 693-707
    • Li, L.1    Chen, R.2    Weng, Z.P.3
  • 51
    • 24944474033 scopus 로고    scopus 로고
    • On the role of plasminogen activator inhibitor-1 in adipose tissue development and insulin resistance in mice
    • Lijnen H.R., Alessi M.C., Van H.B., Collen D., and Juhan-Vague I. On the role of plasminogen activator inhibitor-1 in adipose tissue development and insulin resistance in mice. J. Thromb. Haemost. 3 (2005) 1174-1179
    • (2005) J. Thromb. Haemost. , vol.3 , pp. 1174-1179
    • Lijnen, H.R.1    Alessi, M.C.2    Van, H.B.3    Collen, D.4    Juhan-Vague, I.5
  • 52
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chotia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chotia, C.2    Janin, J.3
  • 53
    • 0025171921 scopus 로고
    • Murine monoclonal antibodies against active site epitopes on human endothelial plasminogen activator inhibitor (PAI-1)
    • MacGregor I.R., Tonner A.M., Mickelm L.R., James K., and Booth N.A. Murine monoclonal antibodies against active site epitopes on human endothelial plasminogen activator inhibitor (PAI-1). Fibrinolysis 4 (1990) 27-34
    • (1990) Fibrinolysis , vol.4 , pp. 27-34
    • MacGregor, I.R.1    Tonner, A.M.2    Mickelm, L.R.3    James, K.4    Booth, N.A.5
  • 55
  • 56
    • 0026356869 scopus 로고
    • Molecular modelling of antibody combining sites
    • Martin A.C.R., Cheetham J.C., and Rees A.R. Molecular modelling of antibody combining sites. Methods Enzymol. 203 (1991) 121-153
    • (1991) Methods Enzymol. , vol.203 , pp. 121-153
    • Martin, A.C.R.1    Cheetham, J.C.2    Rees, A.R.3
  • 60
    • 0027290655 scopus 로고
    • Interconversions between active, inert and substrate forms of denaturated/refolded type-1 plasminogen activator inhibitor
    • Munch M., Heegaard C.W., and Andreasen P.A. Interconversions between active, inert and substrate forms of denaturated/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
  • 61
    • 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., and Declerck P.J. Elucidation of a novel epitope of a substrate-inducing monoclonal antibody against the serpin PAI-1. J. Thromb. Haemost. 1 (2003) 1028-1033
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1028-1033
    • Naessens, D.1    Gils, A.2    Compernolle, G.3    Declerck, P.J.4
  • 62
    • 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
  • 63
    • 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 L.S., Andreasen P.A., Grondahl H.J., Huang J.Y., Kristensen P., and Dano K. Monoclonal antibodies to human 54,000 molecular weight plasminogen activator inhibitor from fibrosarcoma cells-inhibitor neutralization and one-step affinity purification. Thromb. Haemost. 55 (1986) 206-212
    • (1986) Thromb. Haemost. , vol.55 , pp. 206-212
    • Nielsen, L.S.1    Andreasen, P.A.2    Grondahl, H.J.3    Huang, J.Y.4    Kristensen, P.5    Dano, K.6
  • 64
    • 0032143386 scopus 로고    scopus 로고
    • Augmentation of arterial endothelial cell expression of the plasminogen activator inhibitor type-1 (PAI-1) gene by proinsulin and insulin vivo
    • Nordt T.K., Sawa H., Fujii S., Bode C., and Sobel B.E. Augmentation of arterial endothelial cell expression of the plasminogen activator inhibitor type-1 (PAI-1) gene by proinsulin and insulin vivo. J. Mol. Cell. Cardiol. 30 (1998) 1535-1543
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 1535-1543
    • Nordt, T.K.1    Sawa, H.2    Fujii, S.3    Bode, C.4    Sobel, B.E.5
  • 69
    • 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 M.O., Bonhomme E., and Verbeuren T.J. Inactivation of plasminogen activator inhibitor-1 accelerates thrombolysis of a platelet-rich thrombus in rat mesenteric arterioles. Thromb. Haemost. 86 (2001) 1528-1531
    • (2001) Thromb. Haemost. , vol.86 , pp. 1528-1531
    • Rupin, A.1    Martin, F.2    Vallez, M.O.3    Bonhomme, E.4    Verbeuren, T.J.5
  • 70
    • 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., and Loskutoff D.J. 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 J. 15 (2001) 1840-1842
    • (2001) FASEB J. , vol.15 , pp. 1840-1842
    • Schafer, K.1    Fujisawa, K.2    Konstantinides, S.3    Loskutoff, D.J.4
  • 71
    • 0029880730 scopus 로고    scopus 로고
    • The significance of hypofibrinolysis for the risk of recurrence of venous thromboembolism. Duration of Anticoagulation (DURAC) Trial Study Group
    • Schulman S., and Wiman B. The significance of hypofibrinolysis for the risk of recurrence of venous thromboembolism. Duration of Anticoagulation (DURAC) Trial Study Group. Thromb. Haemost. 75 (1996) 607-611
    • (1996) Thromb. Haemost. , vol.75 , pp. 607-611
    • Schulman, S.1    Wiman, B.2
  • 72
    • 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., Carrel R.W., Bekenpas M.B., Ginsburg D., Lawrence D.A., and Read R. 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    Carrel, R.W.4    Bekenpas, M.B.5    Ginsburg, D.6    Lawrence, D.A.7    Read, R.8
  • 73
    • 0030577371 scopus 로고    scopus 로고
    • Structural classification of CDR-H3 in antibodies
    • Shirai H., Kidera A., and Nakamura H. Structural classification of CDR-H3 in antibodies. FEBS Lett. 399 (1996) 1-8
    • (1996) FEBS Lett. , vol.399 , pp. 1-8
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 74
    • 0033058759 scopus 로고    scopus 로고
    • H3-rules: identification of CDR-H3 structures in antibodies
    • Shirai H., Kidera A., and Nakamura H. H3-rules: identification of CDR-H3 structures in antibodies. FEBS Lett. 455 (1999) 188-197
    • (1999) FEBS Lett. , vol.455 , pp. 188-197
    • Shirai, H.1    Kidera, A.2    Nakamura, H.3
  • 76
    • 30344474589 scopus 로고    scopus 로고
    • Humanization by variable domain resurfacing and grafting on a human IgG4, using a new approach for determination of non-human like surface accessible framework residues based on homology modelling of variable domains
    • Staelens S., Desmet J., Ngo T.H., Vauterin S., Pareyn I., Barbeaux P., Van Rompaey I., Stassen J.M., Deckmyn H., and Vanhoorelbeke K. Humanization by variable domain resurfacing and grafting on a human IgG4, using a new approach for determination of non-human like surface accessible framework residues based on homology modelling of variable domains. Mol. Immunol. 43 (2006) 1243-1257
    • (2006) Mol. Immunol. , vol.43 , pp. 1243-1257
    • Staelens, S.1    Desmet, J.2    Ngo, T.H.3    Vauterin, S.4    Pareyn, I.5    Barbeaux, P.6    Van Rompaey, I.7    Stassen, J.M.8    Deckmyn, H.9    Vanhoorelbeke, K.10
  • 77
    • 33644869406 scopus 로고    scopus 로고
    • Paratope determination of the antithrombotic antibody 82D6A3 based on the crystal structure of its complex with the von Willebrand factor A3-domain
    • Staelens S., Hadders M.A., Vauterin S., Platteau C., De Maeyer M., Vanhoorelbeke K., Huizinga E.G., and Deckmyn H. Paratope determination of the antithrombotic antibody 82D6A3 based on the crystal structure of its complex with the von Willebrand factor A3-domain. J. Biol. Chem. 281 (2006) 2225-2231
    • (2006) J. Biol. Chem. , vol.281 , pp. 2225-2231
    • Staelens, S.1    Hadders, M.A.2    Vauterin, S.3    Platteau, C.4    De Maeyer, M.5    Vanhoorelbeke, K.6    Huizinga, E.G.7    Deckmyn, H.8
  • 78
    • 0029430865 scopus 로고    scopus 로고
    • Ten Eyck, L.F., Mandell, J., Roberts, V.A., and Pique, M.E. (1995). Surveying molecular interactions with DOT. Proceedings of the 1995 ACM/IEEE Supercomputing Conference, A. Hayes, and M. Simmons, eds. (New York: ACM Press).
  • 79
    • 12544256528 scopus 로고    scopus 로고
    • Data-driven docking for the study of biomolecular complexes
    • van Dijk A.D.J., Boelens R., and Bonvin A.M.J.J. Data-driven docking for the study of biomolecular complexes. FEBS J. 272 (2005) 293-312
    • (2005) FEBS J. , vol.272 , pp. 293-312
    • van Dijk, A.D.J.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 80
    • 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 J.J., Wahlund G., Nerme, and Abrahamson T. The Fab-fragment of a PAI-1 inhibiting antibody reduces thrombus size and restores blood flow in a rat model of arterial thrombosis. Thromb. Haemost. 77 (1997) 964-969
    • (1997) Thromb. Haemost. , vol.77 , pp. 964-969
    • van Giezen, J.J.1    Wahlund, G.2    Nerme3    Abrahamson, T.4
  • 81
    • 0037251696 scopus 로고    scopus 로고
    • Elucidation of the paratope of scFv-8H9D4, a PAI-1 neutralizing antibody derivative
    • Verbeke K., Gils A., Stassen J.M., and Declerck P.J. Elucidation of the paratope of scFv-8H9D4, a PAI-1 neutralizing antibody derivative. Thromb. Haemost. 89 (2003) 74-82
    • (2003) Thromb. Haemost. , vol.89 , pp. 74-82
    • Verbeke, K.1    Gils, A.2    Stassen, J.M.3    Declerck, P.J.4
  • 82
    • 4644371458 scopus 로고    scopus 로고
    • Cloning and paratope analysis of an antibody fragment, a rational approach for the design of a PAI-1 inhibitor
    • Verbeke K., Gils A., and Declerck P.J. Cloning and paratope analysis of an antibody fragment, a rational approach for the design of a PAI-1 inhibitor. J. Thromb. Haemost. 2 (2004) 289-297
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 289-297
    • Verbeke, K.1    Gils, A.2    Declerck, P.J.3
  • 83
    • 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 S.P., Woodcock-Mitchell J., Ohtani A., and Fujii S. A new butadiene derivative, T-686, inhibits plasminogen activator inhibitor type-1 production in vitro by cultured human vascular endothelial cells and development of atherosclerotic lesions in vivo in rabbits. Thromb. Res. 85 (1997) 305-314
    • (1997) Thromb. Res. , vol.85 , pp. 305-314
    • Vinogradsky, B.1    Bell, S.P.2    Woodcock-Mitchell, J.3    Ohtani, A.4    Fujii, S.5
  • 84
    • 17744364070 scopus 로고    scopus 로고
    • Improved side-chain modeling for protein-protein docking
    • Wang C., Schueler-Furman O., and Baker D. Improved side-chain modeling for protein-protein docking. Protein Sci. 14 (2005) 1328-1339
    • (2005) Protein Sci. , vol.14 , pp. 1328-1339
    • Wang, C.1    Schueler-Furman, O.2    Baker, D.3
  • 86
    • 0034458999 scopus 로고    scopus 로고
    • WAM: an improved algorithm for modeling antibodies on the WEB
    • Whitelegg N.R., and Rees A.R. WAM: an improved algorithm for modeling antibodies on the WEB. Protein Eng. 13 (2000) 819-824
    • (2000) Protein Eng. , vol.13 , pp. 819-824
    • Whitelegg, N.R.1    Rees, A.R.2


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