메뉴 건너뛰기




Volumn 288, Issue 41, 2013, Pages 29482-29493

Full time course kinetics of the streptokinase-plasminogen activation pathway

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC COMPLEXES; CHROMOGENIC SUBSTRATE; CONTINUOUS MEASUREMENTS; DISSOCIATION CONSTANT; EQUILIBRIUM BINDING; FIBRINOGEN COMPLEXES; FREE CONCENTRATION; TRANSIENT FORMATION;

EID: 84885645095     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.477935     Document Type: Article
Times cited : (11)

References (62)
  • 2
    • 4444338258 scopus 로고    scopus 로고
    • The pathogenic equine streptococci
    • Timoney, J. F. (2004) The pathogenic equine streptococci. Vet. Res. 35, 397-409
    • (2004) Vet. Res , vol.35 , pp. 397-409
    • Timoney, J.F.1
  • 3
    • 84870250295 scopus 로고    scopus 로고
    • Streptokinase variants from Streptococcus pyogenes isolates display altered plasminogen activation characteristics. Implications for pathogenesis
    • Cook, S. M., Skora, A., Gillen, C. M., Walker, M. J., and McArthur, J. D. (2012) Streptokinase variants from Streptococcus pyogenes isolates display altered plasminogen activation characteristics. Implications for pathogenesis. Mol. Microbiol. 86, 1052-1062
    • (2012) Mol. Microbiol , vol.86 , pp. 1052-1062
    • Cook, S.M.1    Skora, A.2    Gillen, C.M.3    Walker, M.J.4    McArthur, J.D.5
  • 4
    • 0347622756 scopus 로고    scopus 로고
    • Natural selection and evolution of streptococcal virulence genes involved in tissue-specific adaptations
    • Kalia, A., and Bessen, D. E. (2004) Natural selection and evolution of streptococcal virulence genes involved in tissue-specific adaptations. J. Bacteriol. 186, 110-121
    • (2004) J. Bacteriol , vol.186 , pp. 110-121
    • Kalia, A.1    Bessen, D.E.2
  • 5
    • 0032508547 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human plasmin complexed with streptokinase
    • Wang, X., Lin, X., Loy, J. A., Tang, J., and Zhang, X. C. (1998) Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science 281, 1662-1665
    • (1998) Science , vol.281 , pp. 1662-1665
    • Wang, X.1    Lin, X.2    Loy, J.A.3    Tang, J.4    Zhang, X.C.5
  • 6
    • 0017107996 scopus 로고
    • Induction of the bovine trypsinogentrypsin transition by peptides sequentially similar to the N-terminus of trypsin
    • Bode, W., and Huber, R. (1976) Induction of the bovine trypsinogentrypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett. 68, 231-236
    • (1976) FEBS Lett , vol.68 , pp. 231-236
    • Bode, W.1    Huber, R.2
  • 7
    • 0033586797 scopus 로고    scopus 로고
    • Deletion of Ile1 changes the mechanism of streptokinase. Evidence for the molecular sexuality hypothesis
    • Wang, S., Reed, G. L., and Hedstrom, L. (1999) Deletion of Ile1 changes the mechanism of streptokinase. Evidence for the molecular sexuality hypothesis. Biochemistry 38, 5232-5240
    • (1999) Biochemistry , vol.38 , pp. 5232-5240
    • Wang, S.1    Reed, G.L.2    Hedstrom, L.3
  • 8
    • 0033937010 scopus 로고    scopus 로고
    • Zymogen activation in the streptokinase-plasminogen complex. Ile1 is required for the formation of a functional active site
    • Wang, S., Reed, G. L., and Hedstrom, L. (2000) Zymogen activation in the streptokinase-plasminogen complex. Ile1 is required for the formation of a functional active site. Eur. J. Biochem. 267, 3994-4001
    • (2000) Eur. J. Biochem , vol.267 , pp. 3994-4001
    • Wang, S.1    Reed, G.L.2    Hedstrom, L.3
  • 9
    • 0035854772 scopus 로고    scopus 로고
    • Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation
    • Boxrud, P. D., Verhamme, I. M., Fay, W. P., and Bock, P. E. (2001) Streptokinase triggers conformational activation of plasminogen through specific interactions of the amino-terminal sequence and stabilizes the active zymogen conformation. J. Biol. Chem. 276, 26084-26089
    • (2001) J. Biol. Chem , vol.276 , pp. 26084-26089
    • Boxrud, P.D.1    Verhamme, I.M.2    Fay, W.P.3    Bock, P.E.4
  • 11
    • 0034640546 scopus 로고    scopus 로고
    • Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen
    • Boxrud, P. D., Fay, W. P., and Bock, P. E. (2000) Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen. J. Biol. Chem. 275, 14579-14589
    • (2000) J. Biol. Chem , vol.275 , pp. 14579-14589
    • Boxrud, P.D.1    Fay, W.P.2    Bock, P.E.3
  • 12
    • 0034649426 scopus 로고    scopus 로고
    • Streptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactions
    • Boxrud, P. D., and Bock, P. E. (2000) Streptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactions. Biochemistry 39, 13974-13981
    • (2000) Biochemistry , vol.39 , pp. 13974-13981
    • Boxrud, P.D.1    Bock, P.E.2
  • 13
    • 33748741069 scopus 로고    scopus 로고
    • Binding of the COOH-terminal lysine residue of streptokinase to plasmin(ogen) kringles enhances formation of the streptokinase· plasmin(ogen) catalytic complexes
    • Panizzi, P., Boxrud, P. D., Verhamme, I. M., and Bock, P. E. (2006) Binding of the COOH-terminal lysine residue of streptokinase to plasmin(ogen) kringles enhances formation of the streptokinase·plasmin(ogen) catalytic complexes. J. Biol. Chem. 281, 26774-26778
    • (2006) J. Biol. Chem , vol.281 , pp. 26774-26778
    • Panizzi, P.1    Boxrud, P.D.2    Verhamme, I.M.3    Bock, P.E.4
  • 14
    • 0018191312 scopus 로고
    • Steady state kinetics of activation of human and bovine plasminogens by streptokinase and its equimolar complexes with various activated forms of human plasminogen
    • Wohl, R. C., Summaria, L., Arzadon, L., and Robbins, K. C. (1978) Steady state kinetics of activation of human and bovine plasminogens by streptokinase and its equimolar complexes with various activated forms of human plasminogen. J. Biol. Chem. 253, 1402-1407
    • (1978) J. Biol. Chem , vol.253 , pp. 1402-1407
    • Wohl, R.C.1    Summaria, L.2    Arzadon, L.3    Robbins, K.C.4
  • 15
    • 0018898952 scopus 로고
    • Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 °c
    • Wohl, R. C., Summaria, L., and Robbins, K. C. (1980) Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 °C. J. Biol. Chem. 255, 2005-2013
    • (1980) J. Biol. Chem , vol.255 , pp. 2005-2013
    • Wohl, R.C.1    Summaria, L.2    Robbins, K.C.3
  • 17
    • 4344601358 scopus 로고    scopus 로고
    • Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase
    • Boxrud, P. D., Verhamme, I. M., and Bock, P. E. (2004) Resolution of conformational activation in the kinetic mechanism of plasminogen activation by streptokinase. J. Biol. Chem. 279, 36633-36641
    • (2004) J. Biol. Chem , vol.279 , pp. 36633-36641
    • Boxrud, P.D.1    Verhamme, I.M.2    Bock, P.E.3
  • 18
    • 4344608139 scopus 로고    scopus 로고
    • Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase
    • Boxrud, P. D., and Bock, P. E. (2004) Coupling of conformational and proteolytic activation in the kinetic mechanism of plasminogen activation by streptokinase. J. Biol. Chem. 279, 36642-36649
    • (2004) J. Biol. Chem , vol.279 , pp. 36642-36649
    • Boxrud, P.D.1    Bock, P.E.2
  • 19
    • 83455178215 scopus 로고    scopus 로고
    • Substrate kringlemediated catalysis by the streptokinase-plasmin activator complex. Critical contribution of kringle-4 revealed by the mutagenesis approaches
    • Joshi, K. K., Nanda, J. S., Kumar, P., and Sahni, G. (2012) Substrate kringlemediated catalysis by the streptokinase-plasmin activator complex. Critical contribution of kringle-4 revealed by the mutagenesis approaches. Biochim. Biophys. Acta 1824, 326-333
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 326-333
    • Joshi, K.K.1    Nanda, J.S.2    Kumar, P.3    Sahni, G.4
  • 20
    • 67749114693 scopus 로고    scopus 로고
    • Plasminogen substrate recognition by the streptokinase- plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase β-domain and kringle 5 of the substrate
    • Tharp, A. C., Laha, M., Panizzi, P., Thompson, M. W., Fuentes-Prior, P., and Bock, P. E. (2009) Plasminogen substrate recognition by the streptokinase- plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase β-domain and kringle 5 of the substrate. J. Biol. Chem. 284, 19511-19521
    • (2009) J. Biol. Chem , vol.284 , pp. 19511-19521
    • Tharp, A.C.1    Laha, M.2    Panizzi, P.3    Thompson, M.W.4    Fuentes-Prior, P.5    Bock, P.E.6
  • 21
    • 0033406645 scopus 로고    scopus 로고
    • Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis
    • Chaudhary, A., Vasudha, S., Rajagopal, K., Komath, S. S., Garg, N., Yadav, M., Mande, S. C., and Sahni, G. (1999) Function of the central domain of streptokinase in substrate plasminogen docking and processing revealed by site-directed mutagenesis. Protein Sci. 8, 2791-2805
    • (1999) Protein Sci , vol.8 , pp. 2791-2805
    • Chaudhary, A.1    Vasudha, S.2    Rajagopal, K.3    Komath, S.S.4    Garg, N.5    Yadav, M.6    Mande, S.C.7    Sahni, G.8
  • 22
    • 0037066763 scopus 로고    scopus 로고
    • Involvement of a nine-residue loop of streptokinase in the generation of macromolecular substrate specificity by the activator complex through interaction with substrate kringle domains
    • Dhar, J., Pande, A. H., Sundram, V., Nanda, J. S., Mande, S. C., and Sahni, G. (2002) Involvement of a nine-residue loop of streptokinase in the generation of macromolecular substrate specificity by the activator complex through interaction with substrate kringle domains. J. Biol. Chem. 277, 13257-13267
    • (2002) J. Biol. Chem , vol.277 , pp. 13257-13267
    • Dhar, J.1    Pande, A.H.2    Sundram, V.3    Nanda, J.S.4    Mande, S.C.5    Sahni, G.6
  • 23
    • 0030025146 scopus 로고    scopus 로고
    • Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinase
    • Bock, P. E., Day, D. E., Verhamme, I. M., Bernardo, M. M., Olson, S. T., and Shore, J. D. (1996) Analogs of human plasminogen that are labeled with fluorescence probes at the catalytic site of the zymogen. Preparation, characterization, and interaction with streptokinase. J. Biol. Chem. 271, 1072-1080
    • (1996) J. Biol. Chem , vol.271 , pp. 1072-1080
    • Bock, P.E.1    Day, D.E.2    Verhamme, I.M.3    Bernardo, M.M.4    Olson, S.T.5    Shore, J.D.6
  • 24
    • 0014932863 scopus 로고
    • Plasminogen. Purification from human plasma by affinity chromatography
    • Deutsch, D. G., and Mertz, E. T. (1970) Plasminogen. Purification from human plasma by affinity chromatography. Science 170, 1095-1096
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 25
    • 0032558433 scopus 로고    scopus 로고
    • Demonstration of exosite I-dependent interactions of thrombin with human factor v and factor Va involving the factor Va heavy chain. Analysis by affinity chromatography employing a novel method for active-site-selective immobilization of serine proteinases
    • Dharmawardana, K. R., and Bock, P. E. (1998) Demonstration of exosite I-dependent interactions of thrombin with human factor V and factor Va involving the factor Va heavy chain. Analysis by affinity chromatography employing a novel method for active-site-selective immobilization of serine proteinases. Biochemistry 37, 13143-13152
    • (1998) Biochemistry , vol.37 , pp. 13143-13152
    • Dharmawardana, K.R.1    Bock, P.E.2
  • 26
    • 0024500253 scopus 로고
    • A rapid and simple method for the separation of four molecular forms of human plasminogen
    • Nieuwenhuizen, W., and Traas, D. W. (1989) A rapid and simple method for the separation of four molecular forms of human plasminogen. Thromb. Haemost. 61, 208-210
    • (1989) Thromb. Haemost , vol.61 , pp. 208-210
    • Nieuwenhuizen, W.1    Traas, D.W.2
  • 28
    • 0015866290 scopus 로고
    • Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid
    • Sjöholm, I. (1973) Studies on the conformational changes of plasminogen induced during activation to plasmin and by 6-aminohexanoic acid. Eur. J. Biochem. 39, 471-479
    • (1973) Eur. J. Biochem , vol.39 , pp. 471-479
    • Sjöholm, I.1
  • 29
    • 0017126764 scopus 로고
    • Mechanism of the urokinasecatalyzed activation of human plasminogen
    • Violand, B. N., and Castellino, F. J. (1976) Mechanism of the urokinasecatalyzed activation of human plasminogen. J. Biol. Chem. 251, 3906-3912
    • (1976) J. Biol. Chem , vol.251 , pp. 3906-3912
    • Violand, B.N.1    Castellino, F.J.2
  • 30
    • 0020306559 scopus 로고
    • Complete amino acid sequence of streptokinase and its homology with serine proteases
    • Jackson, K. W., and Tang, J. (1982) Complete amino acid sequence of streptokinase and its homology with serine proteases. Biochemistry 21, 6620-6625
    • (1982) Biochemistry , vol.21 , pp. 6620-6625
    • Jackson, K.W.1    Tang, J.2
  • 31
    • 0017710297 scopus 로고
    • Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma
    • Wiman, B., and Collen, D. (1977) Purification and characterization of human antiplasmin, the fast-acting plasmin inhibitor in plasma. Eur. J. Biochem. 78, 19-26
    • (1977) Eur. J. Biochem , vol.78 , pp. 19-26
    • Wiman, B.1    Collen, D.2
  • 32
    • 0017102105 scopus 로고
    • Isolation and characterization of α2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis
    • Moroi, M., and Aoki, N. (1976) Isolation and characterization of α2-plasmin inhibitor from human plasma. A novel proteinase inhibitor which inhibits activator-induced clot lysis. J. Biol. Chem. 251, 5956-5965
    • (1976) J. Biol. Chem , vol.251 , pp. 5956-5965
    • Moroi, M.1    Aoki, N.2
  • 33
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall, E., and Ruoslahti, E. (1977) Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer 20, 1-5
    • (1977) Int. J. Cancer , vol.20 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 34
    • 0025886248 scopus 로고
    • A kinetic model for the α-thrombincatalyzed conversion of plasma levels of fibrinogen to fibrin in the presence of antithrombin III
    • Naski, M. C., and Shafer, J. A. (1991) A kinetic model for the α-thrombincatalyzed conversion of plasma levels of fibrinogen to fibrin in the presence of antithrombin III. J. Biol. Chem. 266, 13003-13010
    • (1991) J. Biol. Chem , vol.266 , pp. 13003-13010
    • Naski, M.C.1    Shafer, J.A.2
  • 35
    • 0025096662 scopus 로고
    • Heparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombinfibrin polymer-heparin ternary complex
    • Hogg, P. J., and Jackson, C. M. (1990) Heparin promotes the binding of thrombin to fibrin polymer. Quantitative characterization of a thrombinfibrin polymer-heparin ternary complex. J. Biol. Chem. 265, 241-247
    • (1990) J. Biol. Chem , vol.265 , pp. 241-247
    • Hogg, P.J.1    Jackson, C.M.2
  • 36
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • (David, A. D. P., and John, M. S., eds), Academic Press, Inc., New York
    • Weisel, J. W. (2005) Fibrinogen and fibrin. in Advances in Protein Chemistry (David, A. D. P., and John, M. S., eds) pp. 247-299, Academic Press, Inc., New York
    • (2005) Advances in Protein Chemistry , pp. 247-299
    • Weisel, J.W.1
  • 37
    • 0020655601 scopus 로고
    • The action of thrombin on peptide p-nitroanilide substrates. Substrate selectivity and examination of hydrolysis under different reaction conditions
    • Lottenberg, R., Hall, J. A., Blinder, M., Binder, E. P., and Jackson, C. M. (1983) The action of thrombin on peptide p-nitroanilide substrates. Substrate selectivity and examination of hydrolysis under different reaction conditions. Biochim. Biophys. Acta 742, 539-557
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 539-557
    • Lottenberg, R.1    Hall, J.A.2    Blinder, M.3    Binder, E.P.4    Jackson, C.M.5
  • 38
    • 0021103421 scopus 로고
    • Solution composition dependent variation in extinction coefficients for p-nitroaniline
    • Lottenberg, R., and Jackson, C. M. (1983) Solution composition dependent variation in extinction coefficients for p-nitroaniline. Biochim. Biophys. Acta 742, 558-564
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 558-564
    • Lottenberg, R.1    Jackson, C.M.2
  • 39
    • 84965092734 scopus 로고
    • ε-Aminocaproic acid. An inhibitor of plasminogen activation
    • Alkjaersig, N., Fletcher, A. P., and Sherry, S. (1959) ε-Aminocaproic acid. An inhibitor of plasminogen activation. J. Biol. Chem. 234, 832-837
    • (1959) J. Biol. Chem , vol.234 , pp. 832-837
    • Alkjaersig, N.1    Fletcher, A.P.2    Sherry, S.3
  • 40
    • 0034712699 scopus 로고    scopus 로고
    • ε amino caproic acid inhibits streptokinase-plasminogen activator complex formation and substrate binding through kringle-dependent mechanisms
    • Lin, L. F., Houng, A., and Reed, G. L. (2000) ε amino caproic acid inhibits streptokinase-plasminogen activator complex formation and substrate binding through kringle-dependent mechanisms. Biochemistry 39, 4740-4745
    • (2000) Biochemistry , vol.39 , pp. 4740-4745
    • Lin, L.F.1    Houng, A.2    Reed, G.L.3
  • 41
    • 0018709725 scopus 로고
    • Kinetics of the reactions between streptokinase, plasmin and α2- antiplasmin
    • Cederholm-Williams, S. A., De Cock, F., Lijnen, H. R., and Collen, D. (1979) Kinetics of the reactions between streptokinase, plasmin and α2- antiplasmin. Eur. J. Biochem. 100, 125-132
    • (1979) Eur. J. Biochem , vol.100 , pp. 125-132
    • Cederholm-Williams, S.A.1    De Cock, F.2    Lijnen, H.R.3    Collen, D.4
  • 43
    • 60549105802 scopus 로고    scopus 로고
    • Global Kinetic Explorer. A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) Global Kinetic Explorer. A new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387, 20-29
    • (2009) Anal. Biochem , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 44
    • 60549112465 scopus 로고    scopus 로고
    • FitSpace Explorer. An algorithm to evaluate multidimensional parameter space in fitting kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) FitSpace Explorer. An algorithm to evaluate multidimensional parameter space in fitting kinetic data. Anal. Biochem. 387, 30-41
    • (2009) Anal. Biochem , vol.387 , pp. 30-41
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 45
    • 54449095662 scopus 로고    scopus 로고
    • Rapid-reaction kinetic characterization of the pathway of streptokinase·plasmin catalytic complex formation
    • Verhamme, I. M., and Bock, P. E. (2008) Rapid-reaction kinetic characterization of the pathway of streptokinase·plasmin catalytic complex formation. J. Biol. Chem. 283, 26137-26147
    • (2008) J. Biol. Chem , vol.283 , pp. 26137-26147
    • Verhamme, I.M.1    Bock, P.E.2
  • 46
    • 0022254808 scopus 로고
    • Effects of human fibrinogen and its cleavage products on activation of human plasminogen by streptokinase
    • Chibber, B. A., Morris, J. P., and Castellino, F. J. (1985) Effects of human fibrinogen and its cleavage products on activation of human plasminogen by streptokinase. Biochemistry 24, 3429-3434
    • (1985) Biochemistry , vol.24 , pp. 3429-3434
    • Chibber, B.A.1    Morris, J.P.2    Castellino, F.J.3
  • 47
    • 0019981975 scopus 로고
    • Enhancement of the streptokinase-catalyzed activation of human plasminogen by human fibrinogen and its plasminolysis products
    • Strickland, D. K., Morris, J. P., and Castellino, F. J. (1982) Enhancement of the streptokinase-catalyzed activation of human plasminogen by human fibrinogen and its plasminolysis products. Biochemistry 21, 721-728
    • (1982) Biochemistry , vol.21 , pp. 721-728
    • Strickland, D.K.1    Morris, J.P.2    Castellino, F.J.3
  • 48
    • 0029039458 scopus 로고
    • Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen
    • Wang, H., Lottenberg, R., and Boyle, M. D. (1995) Analysis of the interaction of group A streptococci with fibrinogen, streptokinase and plasminogen. Microb. Pathog. 18, 153-166
    • (1995) Microb. Pathog , vol.18 , pp. 153-166
    • Wang, H.1    Lottenberg, R.2    Boyle, M.D.3
  • 49
    • 0021998211 scopus 로고
    • The activation of Glu- and Lys-plasminogens by streptokinase. Effects of fibrin, fibrinogen and their degradation products
    • Takada, A., Takada, Y., and Sugawara, Y. (1985) The activation of Glu- and Lys-plasminogens by streptokinase. Effects of fibrin, fibrinogen and their degradation products. Thromb. Res. 37, 465-475
    • (1985) Thromb. Res , vol.37 , pp. 465-475
    • Takada, A.1    Takada, Y.2    Sugawara, Y.3
  • 50
    • 0024562550 scopus 로고
    • Evidence for the formation of a trimolecular complex between streptokinase, plasminogen and fibrinogen
    • Takada, Y., and Takada, A. (1989) Evidence for the formation of a trimolecular complex between streptokinase, plasminogen and fibrinogen. Thromb. Res. 53, 409-415
    • (1989) Thromb. Res , vol.53 , pp. 409-415
    • Takada, Y.1    Takada, A.2
  • 51
    • 31344462457 scopus 로고    scopus 로고
    • Fibrinogen fragmentDis necessary and sufficient to anchor a surface plasminogen-activating complex in Streptococcus pyogenes
    • Hess, J. L., and Boyle, M. D. (2006) Fibrinogen fragmentDis necessary and sufficient to anchor a surface plasminogen-activating complex in Streptococcus pyogenes. Proteomics 6, 375-378
    • (2006) Proteomics , vol.6 , pp. 375-378
    • Hess, J.L.1    Boyle, M.D.2
  • 52
    • 33746619204 scopus 로고    scopus 로고
    • The interaction between pathogens and the host coagulation system
    • Sun, H. (2006) The interaction between pathogens and the host coagulation system. Physiology 21, 281-288
    • (2006) Physiology , vol.21 , pp. 281-288
    • Sun, H.1
  • 53
    • 48749114201 scopus 로고    scopus 로고
    • M proteinmediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate
    • Sanderson-Smith, M. L., Dinkla, K., Cole, J. N., Cork, A. J., Maamary, P. G., McArthur, J. D., Chhatwal, G. S., and Walker, M. J. (2008) M proteinmediated plasminogen binding is essential for the virulence of an invasive Streptococcus pyogenes isolate. FASEB J. 22, 2715-2722
    • (2008) FASEB J , vol.22 , pp. 2715-2722
    • Sanderson-Smith, M.L.1    Dinkla, K.2    Cole, J.N.3    Cork, A.J.4    Maamary, P.G.5    McArthur, J.D.6    Chhatwal, G.S.7    Walker, M.J.8
  • 54
    • 21244444520 scopus 로고    scopus 로고
    • Is plasminogen deployed as a Streptococcus pyogenes virulence factor?
    • Walker, M. J., McArthur, J. D., McKay, F., and Ranson, M. (2005) Is plasminogen deployed as a Streptococcus pyogenes virulence factor? Trends Microbiol. 13, 308-313
    • (2005) Trends Microbiol , vol.13 , pp. 308-313
    • Walker, M.J.1    McArthur, J.D.2    McKay, F.3    Ranson, M.4
  • 56
    • 0027451350 scopus 로고
    • PAM, a novel plasminogen-binding protein from Streptococcus pyogenes
    • Berge, A., and Sjöbring, U. (1993) PAM, a novel plasminogen-binding protein from Streptococcus pyogenes. J. Biol. Chem. 268, 25417-25424
    • (1993) J. Biol. Chem , vol.268 , pp. 25417-25424
    • Berge, A.1    Sjöbring, U.2
  • 58
    • 40449131624 scopus 로고    scopus 로고
    • Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence
    • McNamara, C., Zinkernagel, A. S., Macheboeuf, P., Cunningham, M. W., Nizet, V., and Ghosh, P. (2008) Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence. Science 319, 1405-1408
    • (2008) Science , vol.319 , pp. 1405-1408
    • McNamara, C.1    Zinkernagel, A.S.2    Macheboeuf, P.3    Cunningham, M.W.4    Nizet, V.5    Ghosh, P.6
  • 60
    • 33748744172 scopus 로고    scopus 로고
    • The maintenance of high affinity plasminogen binding by group A streptococcal plasminogen-binding M-like protein is mediated by arginine and histidine residues within the a1 and a2 repeat domains
    • Sanderson-Smith, M. L., Walker, M. J., and Ranson, M. (2006) The maintenance of high affinity plasminogen binding by group A streptococcal plasminogen-binding M-like protein is mediated by arginine and histidine residues within the a1 and a2 repeat domains. J. Biol. Chem. 281, 25965-25971
    • (2006) J. Biol. Chem , vol.281 , pp. 25965-25971
    • Sanderson-Smith, M.L.1    Walker, M.J.2    Ranson, M.3
  • 61
    • 0031042682 scopus 로고    scopus 로고
    • Plasminogen activation by invasive human pathogens
    • Boyle, M. D., and Lottenberg, R. (1997) Plasminogen activation by invasive human pathogens. Thromb. Haemost. 77, 1-10
    • (1997) Thromb. Haemost , vol.77 , pp. 1-10
    • Boyle, M.D.1    Lottenberg, R.2
  • 62
    • 84871325888 scopus 로고    scopus 로고
    • Characterization of streptokinases from group A streptococci reveals a strong functional relationship that supports the coinheritance of plasminogen- binding M protein and cluster 2b streptokinase
    • Zhang, Y., Liang, Z., Hsueh, H.-T., Ploplis, V. A., and Castellino, F. J. (2012) Characterization of streptokinases from group A streptococci reveals a strong functional relationship that supports the coinheritance of plasminogen- binding M protein and cluster 2b streptokinase. J. Biol. Chem. 287, 42093-42103
    • (2012) J. Biol. Chem , vol.287 , pp. 42093-42103
    • Zhang, Y.1    Liang, Z.2    Hsueh, H.-T.3    Ploplis, V.A.4    Castellino, F.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.