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Volumn 29, Issue 1, 1999, Pages 58-71

The haemostatic balance - Astrup revisited

Author keywords

Fibrinolysis; Haemostatic balance; Thrombosis

Indexed keywords

BLOOD CLOTTING FACTOR 12; FIBRIN; KALLIKREIN; PROTEIN C; THROMBIN; THROMBOMODULIN; UROKINASE;

EID: 0032829303     PISSN: 03010147     EISSN: None     Source Type: Journal    
DOI: 10.1159/000022461     Document Type: Conference Paper
Times cited : (33)

References (69)
  • 1
    • 0000826288 scopus 로고
    • The haemostatic balance
    • Astrup T: The haemostatic balance. Thromb Diath Haemorrh 1958;2: 347-356.
    • (1958) Thromb Diath Haemorrh , vol.2 , pp. 347-356
    • Astrup, T.1
  • 2
    • 49749164627 scopus 로고
    • The biological significance of fibrinolysis
    • Astrup T: The biological significance of fibrinolysis. Lancet 1956;ii: 565-568.
    • (1956) Lancet , vol.2 , pp. 565-568
    • Astrup, T.1
  • 3
    • 0344793022 scopus 로고
    • Fibrin formation: The influence of plasminogen, thrombin and calcium
    • Valencia
    • Gaffney PJ, Templeman J, Mahmoud M, Joe F: Fibrin formation: The influence of plasminogen, thrombin and calcium, (abstract). 7th Int Congr Thromb, Valencia, 1982.
    • (1982) 7th Int Congr Thromb
    • Gaffney, P.J.1    Templeman, J.2    Mahmoud, M.3    Joe, F.4
  • 4
    • 33846662754 scopus 로고    scopus 로고
    • Modulation of fibrin thickness and its relevance to the composition and lysis of fibrin
    • Edgell TA, Gaffney PJ: Modulation of fibrin thickness and its relevance to the composition and lysis of fibrin. Fibrinolysis 1999;10(suppl 4): 11.
    • (1999) Fibrinolysis , vol.10 , Issue.SUPPL. 4 , pp. 11
    • Edgell, T.A.1    Gaffney, P.J.2
  • 5
    • 0027327939 scopus 로고
    • Fibrinogen binds to heparin: The relationship of the binding of other adhesive proteins to heparin
    • Mouri H, Ohkubo T: Fibrinogen binds to heparin: The relationship of the binding of other adhesive proteins to heparin. Arch Biochem Biophys 1993;303:27-31.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 27-31
    • Mouri, H.1    Ohkubo, T.2
  • 8
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • Collen D, Lijnen HR: Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 1991;78:3114-3124.
    • (1991) Blood , vol.78 , pp. 3114-3124
    • Collen, D.1    Lijnen, H.R.2
  • 9
    • 0016742118 scopus 로고
    • Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-amino-carboxylic acids
    • Thorsen S: Differences in the binding to fibrin of native plasminogen and plasminogen modified by proteolytic degradation. Influence of omega-amino-carboxylic acids. Biochim Biophys Acta 1975;393:55-65.
    • (1975) Biochim Biophys Acta , vol.393 , pp. 55-65
    • Thorsen, S.1
  • 10
    • 0021701868 scopus 로고
    • Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots
    • Tran-Thang C, Kruithof EKO, Bachmann FJ: Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots. Clin Invest 1984;74:2009-2016.
    • (1984) Clin Invest , vol.74 , pp. 2009-2016
    • Tran-Thang, C.1    Kruithof, E.K.O.2    Bachmann, F.J.3
  • 11
    • 0345223873 scopus 로고    scopus 로고
    • Fibrinolysis and the hypercoagulable state
    • Seghatchian MJ, Samama MM, Hecker SP (eds): New York, CRC Press
    • Gaffney PJ: Fibrinolysis and the hypercoagulable state; in Seghatchian MJ, Samama MM, Hecker SP (eds): Hypercoagulable States. New York, CRC Press, 1996, p 117.
    • (1996) Hypercoagulable States , pp. 117
    • Gaffney, P.J.1
  • 12
    • 0020575314 scopus 로고
    • Factor XII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin
    • Ichinose A, Tamaki T, Aoki N: Factor XII-mediated cross-linking of NH2-terminal peptide of alpha 2-plasmin inhibitor to fibrin. FEBS Lett 1983;153:369-371.
    • (1983) FEBS Lett , vol.153 , pp. 369-371
    • Ichinose, A.1    Tamaki, T.2    Aoki, N.3
  • 13
    • 0025853337 scopus 로고
    • The regulation of the activation of the fibrinolysis system
    • Takada A, Urano T, Takada Y: The regulation of the activation of the fibrinolysis system. Adv Exp Mcd Biol 1990;281:209-222.
    • (1990) Adv Exp Mcd Biol , vol.281 , pp. 209-222
    • Takada, A.1    Urano, T.2    Takada, Y.3
  • 14
    • 0017847923 scopus 로고
    • Molecular mechanisms of physiological fibrinolysis
    • Wiman B, Collen D: Molecular mechanisms of physiological fibrinolysis. Nature 1987;272:549.
    • (1987) Nature , vol.272 , pp. 549
    • Wiman, B.1    Collen, D.2
  • 16
    • 0014690463 scopus 로고
    • High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity
    • Marder VJ, Shulman NR: High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanism of their anticoagulant activity. J Biol Chem 1969;244: 2120-2124.
    • (1969) J Biol Chem , vol.244 , pp. 2120-2124
    • Marder, V.J.1    Shulman, N.R.2
  • 17
    • 0018583629 scopus 로고
    • The ability of fibrinogen fragments to support ADP-induced platelet aggregation
    • Holt JC, Mahmoud M, Gaffney PJ: The ability of fibrinogen fragments to support ADP-induced platelet aggregation. Thromb Res 1979;16: 427-435.
    • (1979) Thromb Res , vol.16 , pp. 427-435
    • Holt, J.C.1    Mahmoud, M.2    Gaffney, P.J.3
  • 18
    • 0020063793 scopus 로고
    • Isolation of a membrane-bound co-factor for thrombin-catalyzed activation of protein C
    • Esmon NL, Owen WG, Esmon CT: Isolation of a membrane-bound co-factor for thrombin-catalyzed activation of protein C. J Biol Chem 1982;257:859-864.
    • (1982) J Biol Chem , vol.257 , pp. 859-864
    • Esmon, N.L.1    Owen, W.G.2    Esmon, C.T.3
  • 19
    • 0026704809 scopus 로고
    • Regulation of blood coagulation by the protein C system
    • Walker FJ, Fay PJ: Regulation of blood coagulation by the protein C system. FASEB J 1992;6:2561-2567.
    • (1992) FASEB J , vol.6 , pp. 2561-2567
    • Walker, F.J.1    Fay, P.J.2
  • 20
    • 0001907582 scopus 로고
    • An overview of fibrinolysis
    • Bloom AL, Forbes CD, Tuddenham EGD, Thomas DP (eds): Edinburgh, Churchill Livingstone
    • Gaffney PJ, Longstaff C: An overview of fibrinolysis; in Bloom AL, Forbes CD, Tuddenham EGD, Thomas DP (eds): Thrombosis and Haemostasis. Edinburgh, Churchill Livingstone, 1994, pp 549-573.
    • (1994) Thrombosis and Haemostasis , pp. 549-573
    • Gaffney, P.J.1    Longstaff, C.2
  • 21
    • 0345655702 scopus 로고
    • Fibrinolysis. A delicate balance between enzymes and inhibitors
    • Neri Sereri GG, Gensini GF, Abbate R, Prisco D (eds): Florence, Scientific Press
    • Gaffney PJ, Willmott NJ, Longstaff C: Fibrinolysis. A delicate balance between enzymes and inhibitors; in Neri Sereri GG, Gensini GF, Abbate R, Prisco D (eds): Fibrinolysis. An Update. Florence, Scientific Press, 1992, pp 519-548.
    • (1992) Fibrinolysis. An Update , pp. 519-548
    • Gaffney, P.J.1    Willmott, N.J.2    Longstaff, C.3
  • 22
    • 0000060135 scopus 로고
    • Molecular aspects of plasminogen, plasminogen activators and plasmin
    • Bloom AL, Forbes CD, Tuddenham EGD, Thomas DP (eds): Edinburgh, Churchill Livingstone
    • Backmann F: Molecular aspects of plasminogen, plasminogen activators and plasmin; in Bloom AL, Forbes CD, Tuddenham EGD, Thomas DP (eds): Thrombosis and Haemostasis. Edinburgh, Churchill Livingstone, 1994, pp 575-613.
    • (1994) Thrombosis and Haemostasis , pp. 575-613
    • Backmann, F.1
  • 23
    • 0006573997 scopus 로고
    • Plasminogen activator inhibitors
    • Castellino FT, Gaffney PJ, Samama MM, Takada A (eds): Amsterdam, Elsevier
    • Thorsen S, Phillips M: Plasminogen activator inhibitors; in Castellino FT, Gaffney PJ, Samama MM, Takada A (eds): Fundamental and Clinical Fibrinolysis. Amsterdam, Elsevier, 1987, pp 83-98.
    • (1987) Fundamental and Clinical Fibrinolysis , pp. 83-98
    • Thorsen, S.1    Phillips, M.2
  • 24
    • 0017656247 scopus 로고
    • Structure of fibrinogen and degradation products of fibrinogen and fibrin
    • Gaffney PJ: Structure of fibrinogen and degradation products of fibrinogen and fibrin. Br Med Bull 1977; 33:245-251.
    • (1977) Br Med Bull , vol.33 , pp. 245-251
    • Gaffney, P.J.1
  • 25
    • 0020025365 scopus 로고
    • A molecular model of plasmic degradation of crosslinked fibrin
    • Francis CW, Marder VJ: A molecular model of plasmic degradation of crosslinked fibrin. Semin Thromb Haemost 1982;8:25-35.
    • (1982) Semin Thromb Haemost , vol.8 , pp. 25-35
    • Francis, C.W.1    Marder, V.J.2
  • 26
    • 0020972656 scopus 로고
    • The occurence and clinical relevance of fibrin fragments in blood
    • Gaffney PJ: The occurence and clinical relevance of fibrin fragments in blood. Ann NY Acad Sci 1983;408: 407-423.
    • (1983) Ann NY Acad Sci , vol.408 , pp. 407-423
    • Gaffney, P.J.1
  • 27
    • 0027436193 scopus 로고
    • D dimer. History of the discovery, characterisation and utility of this and other fibrin fragments
    • Gaffney PJ: D dimer. History of the discovery, characterisation and utility of this and other fibrin fragments. Fibrinolysis 1993;7(suppl 2): 2-8.
    • (1993) Fibrinolysis , vol.7 , Issue.SUPPL. 2 , pp. 2-8
    • Gaffney, P.J.1
  • 28
    • 0020045862 scopus 로고
    • Detection and relevance of crosslinked fibrin derivatives in blood
    • Graeff H, Hafter R: Detection and relevance of crosslinked fibrin derivatives in blood. Semin Thromb Haemost 1982;8:57-68.
    • (1982) Semin Thromb Haemost , vol.8 , pp. 57-68
    • Graeff, H.1    Hafter, R.2
  • 29
    • 0016719982 scopus 로고
    • Distinction between fibrinogen and fibrin degradation products in plasma
    • Gaffney PJ: Distinction between fibrinogen and fibrin degradation products in plasma. Clin Chim Acta 1975;65:109-115.
    • (1975) Clin Chim Acta , vol.65 , pp. 109-115
    • Gaffney, P.J.1
  • 30
    • 0029064442 scopus 로고
    • Fibrin degradation products (FnDP) assays. Analysis of standardisation issues and target antigens in plasma
    • Gaffney PJ, Edgell TA, Creighton-Kempsford LJ: Fibrin degradation products (FnDP) assays. Analysis of standardisation issues and target antigens in plasma. Br J Haematol 1995;90:187-194.
    • (1995) Br J Haematol , vol.90 , pp. 187-194
    • Gaffney, P.J.1    Edgell, T.A.2    Creighton-Kempsford, L.J.3
  • 31
    • 0000852842 scopus 로고
    • On the significance of the release of two different peptides from fibrinogen during clotting
    • Laurent TC, Blombäck B: On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chem Scand 1958; 12:1875-1877.
    • (1958) Acta Chem Scand , vol.12 , pp. 1875-1877
    • Laurent, T.C.1    Blombäck, B.2
  • 32
    • 0016172029 scopus 로고
    • Evidence of localization of polymerization sites in fibrinogen
    • Kudryk BJ, Collen D, Woods KR, Blombäck B: Evidence of localization of polymerization sites in fibrinogen. J Biol Chem 1974;249: 3322-3325.
    • (1974) J Biol Chem , vol.249 , pp. 3322-3325
    • Kudryk, B.J.1    Collen, D.2    Woods, K.R.3    Blombäck, B.4
  • 34
    • 0025157058 scopus 로고
    • Normal and fibrinaemic patient plasma contain high-molecular weight crosslinked fibrin-(ogen) derivatives with intact fibrinopeptide A
    • Gron B, Bennick A, Nieuwenhuisen W, Brosstad F: Normal and fibrinaemic patient plasma contain high-molecular weight crosslinked fibrin-(ogen) derivatives with intact fibrinopeptide A. Thromb Res 1990;57: 259-270.
    • (1990) Thromb Res , vol.57 , pp. 259-270
    • Gron, B.1    Bennick, A.2    Nieuwenhuisen, W.3    Brosstad, F.4
  • 35
    • 0025551185 scopus 로고
    • Validity of enzyme-linked immunosorbent assays of crosslinked fibrin degradation products as a measure of clot lysis
    • Eisenberg PR, Jaffe AS, Stump DC, Collen D, Bovill EG: Validity of enzyme-linked immunosorbent assays of crosslinked fibrin degradation products as a measure of clot lysis. Circulation 1990;82:1159-1168.
    • (1990) Circulation , vol.82 , pp. 1159-1168
    • Eisenberg, P.R.1    Jaffe, A.S.2    Stump, D.C.3    Collen, D.4    Bovill, E.G.5
  • 37
    • 0021162619 scopus 로고
    • Clinical studies of protein C
    • Griffin JH: Clinical studies of protein C. Semin Thromb Haemost 1984;10:162-166.
    • (1984) Semin Thromb Haemost , vol.10 , pp. 162-166
    • Griffin, J.H.1
  • 38
    • 0025833619 scopus 로고
    • Protein S and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system
    • Dahlback B: Protein S and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system. Thromb Haemost 1991;66:49-61.
    • (1991) Thromb Haemost , vol.66 , pp. 49-61
    • Dahlback, B.1
  • 39
    • 0344361112 scopus 로고
    • Some structure-function relationships in protein C pathway
    • Aznour J, España F (eds): Springer-Verlag Iberica
    • Ohlin A-K, Stenflo J: Some structure-function relationships in protein C pathway: in Aznour J, España F (eds): Barcelona, Springer-Verlag Iberica, 1990, pp 11-24.
    • (1990) Barcelona , pp. 11-24
    • Ohlin, A.-K.1    Stenflo, J.2
  • 40
    • 0018715761 scopus 로고
    • The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V
    • Walker FJ, Sexton PW, Esmon CT: The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V. Biochim Biophys Acta 1979;571:333-342.
    • (1979) Biochim Biophys Acta , vol.571 , pp. 333-342
    • Walker, F.J.1    Sexton, P.W.2    Esmon, C.T.3
  • 41
    • 0020590426 scopus 로고
    • Regulation of activated protein C by thrombin-modified protein S
    • Suzuki K, Nishioka J, Hashimoto S: Regulation of activated protein C by thrombin-modified protein S. J Biochem 1983;94:699-705.
    • (1983) J Biochem , vol.94 , pp. 699-705
    • Suzuki, K.1    Nishioka, J.2    Hashimoto, S.3
  • 42
    • 0019332589 scopus 로고
    • Regulation of activated protein C by a new protein. A possible function for bovine protein S
    • Walker FJ: Regulation of activated protein C by a new protein. A possible function for bovine protein S. J Biol Chem 1980;255:5521-5524.
    • (1980) J Biol Chem , vol.255 , pp. 5521-5524
    • Walker, F.J.1
  • 43
    • 0015896821 scopus 로고
    • Autoprothrombin II-A: Thrombin removal and mechanism of induction of fibrinolysis
    • Zoltan RP, Seegers WH: Autoprothrombin II-A: Thrombin removal and mechanism of induction of fibrinolysis. Thromb Res 1973;3:23-33.
    • (1973) Thromb Res , vol.3 , pp. 23-33
    • Zoltan, R.P.1    Seegers, W.H.2
  • 44
    • 0017283234 scopus 로고
    • A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterisation
    • Stenflo J: A new vitamin K-dependent protein. Purification from bovine plasma and preliminary characterisation. J Biol Chem 1976;251: 355-363.
    • (1976) J Biol Chem , vol.251 , pp. 355-363
    • Stenflo, J.1
  • 45
    • 0022910521 scopus 로고
    • Mechanism of protein C-dependent clot lysis: Role of plasminogen activator inhibitor
    • Sakata Y, Loskutoff DJ, Gladson CL, Hekman CM, Griffin JH: Mechanism of protein C-dependent clot lysis: Role of plasminogen activator inhibitor. Blood 1986;68: 1218-1223.
    • (1986) Blood , vol.68 , pp. 1218-1223
    • Sakata, Y.1    Loskutoff, D.J.2    Gladson, C.L.3    Hekman, C.M.4    Griffin, J.H.5
  • 46
    • 0025184934 scopus 로고
    • The activated protein C-mediated enhancement of tissue-type plasminogen activator-induced fibrinolysis in a cell-free system
    • Bajzar L, Fredenburgh JC, Nesheim M: The activated protein C-mediated enhancement of tissue-type plasminogen activator-induced fibrinolysis in a cell-free system. J Biol Chem 1990;265:16948-16954.
    • (1990) J Biol Chem , vol.265 , pp. 16948-16954
    • Bajzar, L.1    Fredenburgh, J.C.2    Nesheim, M.3
  • 47
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar L, Manuel R, Nesheim ME: Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J Biol Chem 1995; 270:14477-14484.
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 48
    • 0030742896 scopus 로고    scopus 로고
    • Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
    • Nesheim M, Wang W, Boffa M, Nagashima M, Morser J, Bajzar L: Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb Haemost 1997;78:386-391.
    • (1997) Thromb Haemost , vol.78 , pp. 386-391
    • Nesheim, M.1    Wang, W.2    Boffa, M.3    Nagashima, M.4    Morser, J.5    Bajzar, L.6
  • 49
    • 0027161205 scopus 로고
    • Molecular events that control the protein C anticoagulant pathway
    • Esmon CT: Molecular events that control the protein C anticoagulant pathway. Thromb Haemost 1993; 70:29-35.
    • (1993) Thromb Haemost , vol.70 , pp. 29-35
    • Esmon, C.T.1
  • 50
    • 0028232356 scopus 로고
    • The significant enhancement of fibrinolysis by calcium ion in a cell free system: The shortening of euglobulin clot lysis time by calcium ion
    • Kojima Y, Urano T, Kojima K, Serizawa K, Takada Y, Takada A: The significant enhancement of fibrinolysis by calcium ion in a cell free system: The shortening of euglobulin clot lysis time by calcium ion. Thromb Haemost 1994;72:113-118.
    • (1994) Thromb Haemost , vol.72 , pp. 113-118
    • Kojima, Y.1    Urano, T.2    Kojima, K.3    Serizawa, K.4    Takada, Y.5    Takada, A.6
  • 51
    • 0021351386 scopus 로고
    • Intrinsic plasma fibrinolysis: Involvement or urokinase-related activity in the factor XII-independent plasminogen proactivator pathway
    • Kluft C, Wijngaards G, Jie AFH: Intrinsic plasma fibrinolysis: Involvement or urokinase-related activity in the factor XII-independent plasminogen proactivator pathway. J Lab Clin Med 1984;103:408-419.
    • (1984) J Lab Clin Med , vol.103 , pp. 408-419
    • Kluft, C.1    Wijngaards, G.2    Jie, A.F.H.3
  • 52
    • 0345223863 scopus 로고
    • The role of molecules immunologically related to urokinase in contact system-dependent fibrinolysis
    • Castellino FJ, Gaffney PJ, Samama MM, Takada A (eds): Amsterdam, Elsevier
    • Miles LA, Griffin JH: The role of molecules immunologically related to urokinase in contact system-dependent fibrinolysis; in Castellino FJ, Gaffney PJ, Samama MM, Takada A (eds): Fundamental and Clinical Fibrinolysis. Amsterdam, Elsevier, 1987, pp 45-55.
    • (1987) Fundamental and Clinical Fibrinolysis , pp. 45-55
    • Miles, L.A.1    Griffin, J.H.2
  • 53
    • 0020672163 scopus 로고
    • Dextran-sulphate dependent fibrinolysis in whole human plasma: Dependence on factor XII and prekallikrein
    • Miles LA, Rothschild Z, Griffin JH: Dextran-sulphate dependent fibrinolysis in whole human plasma: Dependence on factor XII and prekallikrein. J Lab Clin Med 1983;101: 214-225.
    • (1983) J Lab Clin Med , vol.101 , pp. 214-225
    • Miles, L.A.1    Rothschild, Z.2    Griffin, J.H.3
  • 55
    • 0345655691 scopus 로고
    • Interaction between the extrinsic and intrinsic systems of fibrinolysis
    • Davidson JF, Cepelak V, Samama MM, Desmoyers PC (eds): Edinburgh, Churchill Livingstone
    • Kluft C, Jie AFH: Interaction between the extrinsic and intrinsic systems of fibrinolysis; in Davidson JF, Cepelak V, Samama MM, Desmoyers PC (eds): Progress in Chemical Fibrinolysis and Thrombolysis. Edinburgh, Churchill Livingstone, 1979, pp 25-31.
    • (1979) Progress in Chemical Fibrinolysis and Thrombolysis , pp. 25-31
    • Kluft, C.1    Jie, A.F.H.2
  • 56
    • 0023900930 scopus 로고
    • Effects of plasma kallikrein and bradykinin infusions into pigs on plasma fibrinolytic variables and urinary excretion of thromboxane and prostacyclin metabolites
    • Egberg N, Gallimore MJ, Green K, Jacobsson J, Vesterqvist D, Wiman B: Effects of plasma kallikrein and bradykinin infusions into pigs on plasma fibrinolytic variables and urinary excretion of thromboxane and prostacyclin metabolites. Fibrinolysis 1988;2:101-106.
    • (1988) Fibrinolysis , vol.2 , pp. 101-106
    • Egberg, N.1    Gallimore, M.J.2    Green, K.3    Jacobsson, J.4    Vesterqvist, D.5    Wiman, B.6
  • 58
    • 0009501764 scopus 로고
    • Prourokinase activation in the euglobulin fractions
    • Hauert J, Bachmann F: Prourokinase activation in the euglobulin fractions (abstract). Thromb Haemost 1985;54:122.
    • (1985) Thromb Haemost , vol.54 , pp. 122
    • Hauert, J.1    Bachmann, F.2
  • 59
    • 0023942788 scopus 로고
    • Surface receptors for urokinase plasminogen activator
    • Blasi F: Surface receptors for urokinase plasminogen activator. Fibrinolysis 1988;2:73-84.
    • (1988) Fibrinolysis , vol.2 , pp. 73-84
    • Blasi, F.1
  • 60
    • 0027385945 scopus 로고
    • Urokinase-type plasminogen activator and malignancy - Review
    • Duffy MJ: Urokinase-type plasminogen activator and malignancy - Review. Fibrinolysis 1993;7:295-302.
    • (1993) Fibrinolysis , vol.7 , pp. 295-302
    • Duffy, M.J.1
  • 62
    • 85005186443 scopus 로고
    • Fibrinolysis and cell surfaces
    • Castellino FJ, Gaffney PJ, Samama MM, Takada A (eds): Amsterdam, Elsevier
    • Miles LA, Plow EF: Fibrinolysis and cell surfaces; in Castellino FJ, Gaffney PJ, Samama MM, Takada A (eds): Fundamental and Clinical Fibrinolysis. Amsterdam, Elsevier, 1987, pp 111-123.
    • (1987) Fundamental and Clinical Fibrinolysis , pp. 111-123
    • Miles, L.A.1    Plow, E.F.2
  • 64
    • 0023941054 scopus 로고
    • Plasminogen receptors: Ubiquitous sites for cellular regulation of fibrinolysis
    • Miles LA, Plow EF: Plasminogen receptors: Ubiquitous sites for cellular regulation of fibrinolysis. Fibrinolysis 1988;2:61-71.
    • (1988) Fibrinolysis , vol.2 , pp. 61-71
    • Miles, L.A.1    Plow, E.F.2
  • 65
    • 0023515489 scopus 로고
    • Binding of tissue plasminogen activator to cultured human endothelial cells
    • Hajjar KA, Hamel NM, Harpel PC, Nachmann NL: Binding of tissue plasminogen activator to cultured human endothelial cells. J Clin Invest 1987;870:1712-1719.
    • (1987) J Clin Invest , vol.870 , pp. 1712-1719
    • Hajjar, K.A.1    Hamel, N.M.2    Harpel, P.C.3    Nachmann, N.L.4
  • 66
    • 0001149917 scopus 로고
    • Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes
    • Stopelli MP, Corti A, Soffientini A, Cassani G, Blasi F, Assoian RK: Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proc Natl Acad Sci USA 1985;82:4939-4943.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4939-4943
    • Stopelli, M.P.1    Corti, A.2    Soffientini, A.3    Cassani, G.4    Blasi, F.5    Assoian, R.K.6
  • 67
    • 0004729574 scopus 로고
    • Detection of fibrin and its fragments using monoclonal antibodies. Clinical implications
    • Nagy I, Losanczy H, Vinazzer H (eds): Würzburg, Schmitt & Meyer
    • Gaffney PJ, Creighton-Kempsford LJ, Tymkewycz PM: Detection of fibrin and its fragments using monoclonal antibodies. Clinical implications; in Nagy I, Losanczy H, Vinazzer H (eds): Thrombosis and Haemorrhagic Disorders. Würzburg, Schmitt & Meyer, 1990. pp 121-134.
    • (1990) Thrombosis and Haemorrhagic Disorders , pp. 121-134
    • Gaffney, P.J.1    Creighton-Kempsford, L.J.2    Tymkewycz, P.M.3
  • 68
    • 0003268476 scopus 로고    scopus 로고
    • Fibrinolysis and the haemostatic balance: Harmonisation of some old and new concepts
    • Takada T, Collen D, Gaffney PJ (eds): Amsterdam, Elsevier
    • Gaffney PJ, Edgell TA: Fibrinolysis and the haemostatic balance: Harmonisation of some old and new concepts; in Takada T, Collen D, Gaffney PJ (eds): Recent Progress in Blood Coagulation and Fibrinolysis. Amsterdam, Elsevier, 1997, pp 127-141.
    • (1997) Recent Progress in Blood Coagulation and Fibrinolysis , pp. 127-141
    • Gaffney, P.J.1    Edgell, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.