메뉴 건너뛰기




Volumn 40, Issue 1, 1998, Pages 92-103

Contact activation of the plasma coagulation cascade. III. Biophysical aspects of thrombin-binding anticoagulants

Author keywords

Anticoagulation; Aptamers; Blood; Coagulation; DNA ligands; Mathematical model; Plasma; Thrombin; Thrombin ligand

Indexed keywords

BLOOD; COAGULATION; DISSOCIATION; DNA; LEAST SQUARES APPROXIMATIONS; MATHEMATICAL MODELS; POLYMERIZATION; PROTEINS; REACTION KINETICS;

EID: 0032053413     PISSN: 00219304     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4636(199804)40:1<92::AID-JBM11>3.0.CO;2-M     Document Type: Article
Times cited : (25)

References (30)
  • 2
    • 0029347516 scopus 로고
    • Contact activation of the plasma coagulation cascade. I. Procoagulant surface energy and chemistry
    • E. A. Vogler, J. C. Graper, G. R. Harper, L. M. Lander, and W. J. Brittain, "Contact activation of the plasma coagulation cascade. I. Procoagulant surface energy and chemistry," J. Biomed. Mater. Res., 29, 1005-1016 (1995).
    • (1995) J. Biomed. Mater. Res. , vol.29 , pp. 1005-1016
    • Vogler, E.A.1    Graper, J.C.2    Harper, G.R.3    Lander, L.M.4    Brittain, W.J.5
  • 3
    • 6844253651 scopus 로고
    • Antithrombotic therapy
    • W. J. Williams, E. Bestler, A. J. Ersler, and M. A. Lichtman (eds.), McGraw-Hill, Inc., New York
    • L. A. Harker, "Antithrombotic therapy," in Hematology W. J. Williams, E. Bestler, A. J. Ersler, and M. A. Lichtman (eds.), McGraw-Hill, Inc., New York, 1990, pp. 1569-1581.
    • (1990) Hematology , pp. 1569-1581
    • Harker, L.A.1
  • 5
    • 0027571734 scopus 로고
    • Interaction of heparin with pollalyamine-immobilized surfaces
    • X. Ma, S. F. Mohammad, and S. W. Kim, "Interaction of heparin with pollalyamine-immobilized surfaces," J. Biomed. Mater. Res., 27, 357-365 (1993).
    • (1993) J. Biomed. Mater. Res. , vol.27 , pp. 357-365
    • Ma, X.1    Mohammad, S.F.2    Kim, S.W.3
  • 8
    • 0027427161 scopus 로고
    • Synthetic low-molecular weight thrombin inhibitors - Molecular design and pharmacological profile
    • C. Tapparelli, R. Metternich, C. Ehrhardt, and N. S. Cook, "Synthetic low-molecular weight thrombin inhibitors - Molecular design and pharmacological profile," Trends in Pharmacol. Sci, 14, 366-376 (1993).
    • (1993) Trends in Pharmacol. Sci , vol.14 , pp. 366-376
    • Tapparelli, C.1    Metternich, R.2    Ehrhardt, C.3    Cook, N.S.4
  • 9
    • 0026575221 scopus 로고
    • Selection of single-stranded DNA molecules that bind and inhibit human thrombin
    • L. C. Bock, L. C. Griffin, J. A. Latham, W. H. Vermass, and J. Toole, "Selection of single-stranded DNA molecules that bind and inhibit human thrombin," Nature, 355, 564-566 (1992).
    • (1992) Nature , vol.355 , pp. 564-566
    • Bock, L.C.1    Griffin, L.C.2    Latham, J.A.3    Vermass, W.H.4    Toole, J.5
  • 12
    • 0019262612 scopus 로고
    • Kinetic study on the effects of acidic polysaccharides on the interaction of fibrinogen and thrombin
    • E. Nakanishi, H. Sato, and A. Nakajima, "Kinetic study on the effects of acidic polysaccharides on the interaction of fibrinogen and thrombin," Polym. Bull, 3, 655-664 (1980).
    • (1980) Polym. Bull , vol.3 , pp. 655-664
    • Nakanishi, E.1    Sato, H.2    Nakajima, A.3
  • 13
    • 0021964109 scopus 로고
    • Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin III. Effects of competitive inhibitors
    • H. Sato and A. Nakajima, "Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin III. Effects of competitive inhibitors," Thromb. Res., 37, 327-335 (1985).
    • (1985) Thromb. Res. , vol.37 , pp. 327-335
    • Sato, H.1    Nakajima, A.2
  • 14
    • 0021243970 scopus 로고
    • Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin (I): Application of mathematical treatment of turbidimetrical method
    • H. Sato and A. Nakima, "Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin (I): Application of mathematical treatment of turbidimetrical method," Thromb. Res., 33, 645-651 (1984).
    • (1984) Thromb. Res. , vol.33 , pp. 645-651
    • Sato, H.1    Nakima, A.2
  • 15
    • 0021248461 scopus 로고
    • Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin (II): Application of enzyme kinetics to turbidimetrical method
    • H. Sato and A. Nakima, "Kinetic study on the initial stage of the fibrinogen-fibrin conversion by thrombin (II): Application of enzyme kinetics to turbidimetrical method," Thromb. Res., 35, 133-139 (1984).
    • (1984) Thromb. Res. , vol.35 , pp. 133-139
    • Sato, H.1    Nakima, A.2
  • 16
    • 0022354752 scopus 로고
    • Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin
    • S. D. Lewis, P. P. Shields, and J. A. Shafer, "Characterization of the kinetic pathway for liberation of fibrinopeptides during assembly of fibrin," J. Biol. Chem., 260, 10192-10199 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 10192-10199
    • Lewis, S.D.1    Shields, P.P.2    Shafer, J.A.3
  • 18
    • 0020524008 scopus 로고
    • Formation of soluble fibrin oligomers in purified systems and in plasma
    • N. Alkjaersig and A. P. Fletcher, "Formation of soluble fibrin oligomers in purified systems and in plasma," Biochem. J., 213, 75-83 (1983).
    • (1983) Biochem. J. , vol.213 , pp. 75-83
    • Alkjaersig, N.1    Fletcher, A.P.2
  • 19
    • 6844239315 scopus 로고
    • A kinetic model for the thrombin-catalyzed conversion of plasma levels of fibrinogen to fibrin in the presence of antithrombin
    • M. C. Naski and J. A. Shafer, "A kinetic model for the thrombin-catalyzed conversion of plasma levels of fibrinogen to fibrin in the presence of antithrombin," J. Biol. Chem., 266, 1303-1310 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 1303-1310
    • Naski, M.C.1    Shafer, J.A.2
  • 20
    • 0023684568 scopus 로고
    • An automated approach to characterize in simple kinetic terms the generation and inactivation of thrombin and the interaction of fibrinogen with thrombin
    • D. R. Hoak, S. K. Banerjee, and G. Kaldor, "An automated approach to characterize in simple kinetic terms the generation and inactivation of thrombin and the interaction of fibrinogen with thrombin,Clin. Chem., 34, 1971-1975 (1988).
    • (1988) Clin. Chem. , vol.34 , pp. 1971-1975
    • Hoak, D.R.1    Banerjee, S.K.2    Kaldor, G.3
  • 21
    • 0020964886 scopus 로고
    • Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin
    • D. L. Higgins, S. D. Lewis, and J. A. Shafer, "Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin," J. Biol. Chem., 258, 9276-9282 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 9276-9282
    • Higgins, D.L.1    Lewis, S.D.2    Shafer, J.A.3
  • 22
    • 0000832942 scopus 로고
    • Interfacial chemistry in biomaterials science
    • J. Berg (ed.), Marcel Dekker, Inc., New York
    • E. A. Vogler, "Interfacial chemistry in biomaterials science," in Wettability (Surfactant Science Series 49), J. Berg (ed.), Marcel Dekker, Inc., New York, 1993, pp. 184-250.
    • (1993) Wettability (Surfactant Science Series 49) , pp. 184-250
    • Vogler, E.A.1
  • 23
    • 0025152505 scopus 로고
    • Hematological and clinicochemical profiles of healthy swine and swine with inflammatory processes
    • J. Odink, J. F. M. Smeets, I. J. R. Visser, H. Sandman, and J. M. A. Snijders, "Hematological and clinicochemical profiles of healthy swine and swine with inflammatory processes," J. Animal Sci., 68, 163-170 (1990).
    • (1990) J. Animal Sci. , vol.68 , pp. 163-170
    • Odink, J.1    Smeets, J.F.M.2    Visser, I.J.R.3    Sandman, H.4    Snijders, J.M.A.5
  • 24
    • 0027323560 scopus 로고
    • Effect of temperature on the association step in thrombin-fibrinogen interaction
    • M. Picozzi and R. De Cristofaro, "Effect of temperature on the association step in thrombin-fibrinogen interaction," Biochem. J., 294, 563-567 (1993).
    • (1993) Biochem. J. , vol.294 , pp. 563-567
    • Picozzi, M.1    De Cristofaro, R.2
  • 25
    • 0027399667 scopus 로고
    • Hirudin as a molecular probe for thrombin in vitro and during systemic coagulation in the pig
    • P. Zoldhelyi, J. H. Cheesbro, and G. O. Whyte, "Hirudin as a molecular probe for thrombin in vitro and during systemic coagulation in the pig," Proc. Natl. Acad. Sci. USA, 90, 1819-1823 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1819-1823
    • Zoldhelyi, P.1    Cheesbro, J.H.2    Whyte, G.O.3
  • 26
    • 0021272142 scopus 로고
    • Normal haemostasis parameters: A study in a well-defined inborn population of preterm infants
    • D. Beverly, M. Inwood, G. Chance, M. Schaus, and B. O'Keefe, "Normal haemostasis parameters: A study in a well-defined inborn population of preterm infants," Early Human Dev., 9, 249-257 (1984).
    • (1984) Early Human Dev. , vol.9 , pp. 249-257
    • Beverly, D.1    Inwood, M.2    Chance, G.3    Schaus, M.4    O'Keefe, B.5
  • 29
    • 0016704277 scopus 로고
    • Characterization and Quantitation of the five major plasma protein fractions in seven-day-old piglets
    • Y. M. Le Gal, "Characterization and Quantitation of the five major plasma protein fractions in seven-day-old piglets," Biol. Neonate, 26, 174-181 (1975).
    • (1975) Biol. Neonate , vol.26 , pp. 174-181
    • Le Gal, Y.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.