메뉴 건너뛰기




Volumn 5, Issue 10, 1998, Pages 917-923

The ternary microplasmin-staphylokinasemicroplasmin complex is a proteinasecofactor-substrate complex in action

Author keywords

[No Author keywords available]

Indexed keywords

MICROPLASMIN; PLASMIN; STAPHYLOKINASE; UNCLASSIFIED DRUG; AUR PROTEIN, STAPHYLOCOCCUS AUREUS; METALLOPROTEINASE; PEPTIDE FRAGMENT;

EID: 0031596034     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/2359     Document Type: Review
Times cited : (137)

References (30)
  • 1
    • 0000060135 scopus 로고
    • eds Bloom, A. L., Forbes, C. D., Thomas, D. P. & Tuddenham E. G. D. Churchill Livingstone, London;
    • Bachman, F. In Haemostasis and thombosis (eds Bloom, A. L., Forbes, C. D., Thomas, D. P. & Tuddenham E. G. D.) 575-614 (Churchill Livingstone, London; 1994).
    • (1994) Haemostasis and Thombosis , pp. 575-614
    • Bachman, F.1
  • 2
    • 0030842795 scopus 로고    scopus 로고
    • Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration
    • Chapman, H. A. Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration. Curr. Opin. Cell Biol. 9, 714-724 (1997).
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 714-724
    • Chapman, H.A.1
  • 3
    • 0029944122 scopus 로고    scopus 로고
    • Angiostatin induces and sustains dormancy of human primary tumors in mice
    • O' Reilly, M. S., Holmgren, L., Chen, C. & Folkman, J. Angiostatin induces and sustains dormancy of human primary tumors in mice. Nature Med. 2, 689-692 (1996).
    • (1996) Nature Med. , vol.2 , pp. 689-692
    • O' Reilly, M.S.1    Holmgren, L.2    Chen, C.3    Folkman, J.4
  • 4
    • 0032502267 scopus 로고    scopus 로고
    • Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen
    • Chang, Y. et al. Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen. Biochemistry 37, 3258-3271 (1998).
    • (1998) Biochemistry , vol.37 , pp. 3258-3271
    • Chang, Y.1
  • 5
    • 0027933043 scopus 로고
    • Probing structure function relationships of tissue-type plasminogen activator by site specific mutagenesis
    • Madison, E. L. Probing structure function relationships of tissue-type plasminogen activator by site specific mutagenesis. Fibrinolysis 8, 221-236 (1994).
    • (1994) Fibrinolysis , vol.8 , pp. 221-236
    • Madison, E.L.1
  • 7
    • 0031941584 scopus 로고    scopus 로고
    • Staphylokinase: A potent, uniquely fibrin selective thrombolytic agent
    • Collen, D. Staphylokinase: a potent, uniquely fibrin selective thrombolytic agent. Nature Med. 4, 279-284 (1998).
    • (1998) Nature Med. , vol.4 , pp. 279-284
    • Collen, D.1
  • 8
    • 0030888405 scopus 로고    scopus 로고
    • Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential
    • Rabijns, A., De Bondt H. L. & De Ranter C. Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential. Nature Struct. Biol. 4, 357-360 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 357-360
    • Rabijns, A.1    De Bondt, H.L.2    De Ranter, C.3
  • 9
    • 0027982294 scopus 로고
    • Characterization of the interaction between plasminogen and staphylokinase
    • Lijnen, H, R., De Cock, F., Van Hoef, B., Schlott, B. & Collen, D. Characterization of the interaction between plasminogen and staphylokinase. Eur. J. Biochem. 224, 143-149 (1994).
    • (1994) Eur. J. Biochem. , vol.224 , pp. 143-149
    • Lijnen, H.R.1    De Cock, F.2    Van Hoef, B.3    Schlott, B.4    Collen, D.5
  • 10
    • 0028785331 scopus 로고
    • Structure-function relationships in staphylokinase as revealed by "clustered charge to alanine" mutagenesis
    • Silence, K. et al. Structure-function relationships in staphylokinase as revealed by "clustered charge to alanine" mutagenesis. J. Biol. Chem. 270, 27192-27198 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27192-27198
    • Silence, K.1
  • 12
    • 0032485885 scopus 로고    scopus 로고
    • Arginine 719 in human plasminogen mediates format ion of the staphylokinase:plasmin activator complex
    • Jespers, L. et al. Arginine 719 in human plasminogen mediates format ion of the staphylokinase:plasmin activator complex. Biochemistry 37, 6380-6386 (1998).
    • (1998) Biochemistry , vol.37 , pp. 6380-6386
    • Jespers, L.1
  • 13
    • 0028075741 scopus 로고
    • Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase
    • Dawson, K. M., Marshall, J. M., Raper, R. H., Gilbert, R. J. & Ponting C. P. Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase. Biochemistry 33, 12042-12047 (1994).
    • (1994) Biochemistry , vol.33 , pp. 12042-12047
    • Dawson, K.M.1    Marshall, J.M.2    Raper, R.H.3    Gilbert, R.J.4    Ponting, C.P.5
  • 14
    • 0029645121 scopus 로고
    • The crystal structure of the catalytic domain of human urokinase-type plasminogen activator
    • Spraggon, G. et al. The crystal structure of the catalytic domain of human urokinase-type plasminogen activator. Structure 3, 681-691 (1995).
    • (1995) Structure , vol.3 , pp. 681-691
    • Spraggon, G.1
  • 15
    • 0029665065 scopus 로고    scopus 로고
    • The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator
    • Lamba, D. et al. The 2.3 Å crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J. Mol. Biol. 258, 117-135 (1996).
    • (1996) J. Mol. Biol. , vol.258 , pp. 117-135
    • Lamba, D.1
  • 16
    • 0028801352 scopus 로고
    • X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B
    • Brandstetter, H., Bauer, M., Huber, R., Lollar, P. and Bode, W. X-ray structure of clotting factor IXa: Active site and module structure related to Xase activity and hemophilia B. J. Cell. Biol. 92, 9796-9800 (1995).
    • (1995) J. Cell. Biol. , vol.92 , pp. 9796-9800
    • Brandstetter, H.1    Bauer, M.2    Huber, R.3    Lollar, P.4    Bode, W.5
  • 17
    • 0028109290 scopus 로고
    • Membrane-dependent reactions in blood coagulation: Role of the vitamin K-dependent enzyme complexes
    • Kalafatis, M., Swords, N. A., Rand, M. D. and Mann, K. G. Membrane-dependent reactions in blood coagulation: role of the vitamin K-dependent enzyme complexes. Biochem. Biophys. Acta 1227, 113-129 (1994).
    • (1994) Biochem. Biophys. Acta , vol.1227 , pp. 113-129
    • Kalafatis, M.1    Swords, N.A.2    Rand, M.D.3    Mann, K.G.4
  • 18
    • 0029926396 scopus 로고    scopus 로고
    • The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
    • Banner, D. et al. The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor. Nature 380, 41-46 (1996).
    • (1996) Nature , vol.380 , pp. 41-46
    • Banner, D.1
  • 19
    • 0030742394 scopus 로고    scopus 로고
    • Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray structure of single-chain human tPA
    • Renatus, M. et al. Lysine 156 promotes the anomalous proenzyme activity of tPA: X-ray structure of single-chain human tPA. EMBO J. 16, 4797-4805, 1997.
    • (1997) EMBO J. , vol.16 , pp. 4797-4805
    • Renatus, M.1
  • 20
    • 0030729772 scopus 로고    scopus 로고
    • Converting blood coagulation factor IX into factor Xa: Dramatic increase in amidolytic activity identifies important active site determinants
    • Hopfner, K. P. et al. Converting blood coagulation factor IX into factor Xa: dramatic increase in amidolytic activity identifies important active site determinants. EMBO J. 16, 6626-6635 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6626-6635
    • Hopfner, K.P.1
  • 21
    • 0027957844 scopus 로고
    • High yield production and purification of recombinant staphylokinase for thrombolytic therapy
    • Schlott, B. et al. High yield production and purification of recombinant staphylokinase for thrombolytic therapy. Biotechnology 12, 185-189 (1993).
    • (1993) Biotechnology , vol.12 , pp. 185-189
    • Schlott, B.1
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No. 4
    • Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 28
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representation of macromolecules
    • Evans, S. V. SETOR: hardware lighted three-dimensional solid model representation of macromolecules. J. Mol. Graph. 11, 134-138 (1990).
    • (1990) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 29
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G. J. ALSCRIPT: a tool to format multiple sequence alignments. Prof. Engng. 6, 37-40 (1993).
    • (1993) Prof. Engng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 30
    • 0000732609 scopus 로고
    • Grasp - Graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. Grasp - graphical representation and analysis of surface properties. Biophys. J. 64, A166 (1993).
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.