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Volumn 4, Issue , 2003, Pages 1-15

Distal hinge of plasminogen activator inhibitor-1 involves its latency transition and specificities toward serine proteases

Author keywords

[No Author keywords available]

Indexed keywords

GUANIDINE; MUTANT PROTEIN; PLASMIN; PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE; ALANINE; ARGININE; GLUTAMIC ACID; SERINE PROTEINASE INHIBITOR;

EID: 0942295654     PISSN: 14712091     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2091-4-5     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0345693050 scopus 로고
    • Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor
    • Ny T, Sawdey M, Lawrence D, Millan JL and Loskutoff DJ: Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor Proc Natl Acad Sci USA 1986, 83:6776-80.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6776-6780
    • Ny, T.1    Sawdey, M.2    Lawrence, D.3    Millan, J.L.4    Loskutoff, D.J.5
  • 4
    • 0024272445 scopus 로고
    • Plasminogen activators and their inhibitors
    • Loskutoff DJ and Schleef RR: Plasminogen activators and their inhibitors Methods Enzymol 1988, 163:293-302.
    • (1988) Methods Enzymol , vol.163 , pp. 293-302
    • Loskutoff, D.J.1    Schleef, R.R.2
  • 5
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen PA Egelund R, Petersen HH: The plasminogen activation system in tumor growth, invasion, and metastasis Cell Mol Life Sci 2000, 57:25-40.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 6
    • 0034660437 scopus 로고    scopus 로고
    • Plasminogen-activator inhibitor type 1 and coronary artery disease
    • Kohler HP Grant PJ: Plasminogen-activator inhibitor type 1 and coronary artery disease N Engl J Med 2000, 342:1792-1801.
    • (2000) N Engl J Med , vol.342 , pp. 1792-1801
    • Kohler, H.P.1    Grant, P.J.2
  • 7
    • 0025371467 scopus 로고
    • Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene
    • issn: 0028-0836
    • Erickson LA, Fici GJ, Lund JE, Boyle TP, Polites HG and Marotti KR: Development of venous occlusions in mice transgenic for the plasminogen activator inhibitor-1 gene Nature 1990, 346:74-6 issn: 0028-0836.
    • (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
  • 8
    • 0033376209 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type-1 (PAI-1) and its role in cardiovascular disease
    • Nordt TK Peter K, Ruef J, Kubler W, Bode C: Plasminogen activator inhibitor type-1 (PAI-1) and its role in cardiovascular disease Thromb Haemost 1999, 82 Suppl 1:14-18.
    • (1999) Thromb Haemost , vol.82 , Issue.SUPPL. 1 , pp. 14-18
    • Nordt, T.K.1    Peter, K.2    Ruef, J.3    Kubler, W.4    Bode, C.5
  • 10
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
    • Huber R and Carrell RW: Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins Biochemistry 1989, 28:8951-8966.
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 12
    • 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: Structures of active and latent PAI-1: a possible stabilizing role for chloride ions Biochemistry 2000, 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
  • 15
    • 0028918245 scopus 로고
    • Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity
    • Sherman PM, Lawrence DA, Verhamme IM, Paielli D, Shore JD and Ginsburg D: Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity. J Biol Chem 1995, 270:9301-9306.
    • (1995) J Biol Chem , vol.270 , pp. 9301-9306
    • Sherman, P.M.1    Lawrence, D.A.2    Verhamme, I.M.3    Paielli, D.4    Shore, J.D.5    Ginsburg, D.6
  • 16
    • 0025744035 scopus 로고
    • The interaction of plasminogen activator inhibitor 1 with plasminogen activators (tissue-type and urokinase-type) and fibrin: Localization of interaction sites and physiologic relevance
    • Keijer J, Linders M, van Zonneveld AJ, Ehrlich HJ, de Boer JP 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 1991, 78:401-409.
    • (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
  • 20
    • 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 DL, 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 1989, 186:523-533.
    • (1989) Eur J Biochem , vol.186 , pp. 523-533
    • Lawrence, D.L.1    Strandberg, L.2    Grundstrom, T.3    Ny, T.4
  • 21
    • 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: 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 1995, 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
  • 22
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas MB Lawrence DA, Ginsburg D: Molecular evolution of plasminogen activator inhibitor-1 functional stability EMBO J 1995, 14:2969-2977.
    • (1995) EMBO J , vol.14 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 23
    • 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
    • A. Allart Stoopa Eric Elderinga, Timothy R. Daffornb, Randy J. Readb and Hans Pannekoek: 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 2001, 305:773-783.
    • (2001) J Mol Biol , vol.305 , pp. 773-783
    • Stoopa, A.A.1    Elderinga, E.2    Daffornb, T.R.3    Readb, R.J.4    Pannekoek, H.5
  • 24
    • 0023741058 scopus 로고
    • Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3
    • Matsumura M, Becktel WJ and Matthews BW: Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3 Nature 1988, 334:406-410.
    • (1988) Nature , vol.334 , pp. 406-410
    • Matsumura, M.1    Becktel, W.J.2    Matthews, B.W.3
  • 25
    • 0030716390 scopus 로고    scopus 로고
    • Role of the P6-P3′ region of the serpin reactive loop in the formation and breakdown of the inhibitory complex
    • Plotnick MI, Schechter NM, Wang ZM, Liu X and Rubin H: Role of the P6-P3′ region of the serpin reactive loop in the formation and breakdown of the inhibitory complex Biochemistry 1997, 36:14601-14608.
    • (1997) Biochemistry , vol.36 , pp. 14601-14608
    • Plotnick, M.I.1    Schechter, N.M.2    Wang, Z.M.3    Liu, X.4    Rubin, H.5
  • 26
    • 0032558382 scopus 로고    scopus 로고
    • Elucidation of the structural basis for the slow reactivity of thrombin with plasminogen activator inhibitor-1
    • Rezaie AR: Elucidation of the structural basis for the slow reactivity of thrombin with plasminogen activator inhibitor-1. Biochemistry 1998, 37:13138-13142.
    • (1998) Biochemistry , vol.37 , pp. 13138-13142
    • Rezaie, A.R.1
  • 27
    • 0025227854 scopus 로고
    • Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants
    • Lawrence DA, Strandberg L, Ericson J and Ny T: Structure-function studies of the SERPIN plasminogen activator inhibitor type 1. Analysis of chimeric strained loop mutants J Biol Chem 1990, 265:20293-20301.
    • (1990) J Biol Chem , vol.265 , pp. 20293-20301
    • Lawrence, D.A.1    Strandberg, L.2    Ericson, J.3    Ny, T.4
  • 30
    • 0029828508 scopus 로고    scopus 로고
    • Conformational changes of the reactive-centre loop and beta-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1
    • Kjoller L, Martensen PM, Sottrup Jensen L, Justesen J, Rodenburg KW and Andreasen PA: Conformational changes of the reactive-centre loop and beta-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1. Eur J Biochem 1996, 241:38-46.
    • (1996) Eur J Biochem , vol.241 , pp. 38-46
    • Kjoller, L.1    Martensen, P.M.2    Sottrup Jensen, L.3    Justesen, J.4    Rodenburg, K.W.5    Andreasen, P.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.