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Volumn 86, Issue 1, 1997, Pages 1-36

Biochemical and pharmacologic rationale for the development of a synthetic heparin pentasaccharide

Author keywords

Antithrombin; Antithrombotic; Factor Xa; Heparin; Pentasaccharide

Indexed keywords

HEPARIN; PENTASACCHARIDE;

EID: 0030952743     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(97)00042-X     Document Type: Article
Times cited : (105)

References (141)
  • 2
    • 0014242234 scopus 로고
    • Highly purified antithrombin III with heparin cofactor activity prepared by disc electrophoresis
    • ABILDGAARD U. Highly purified antithrombin III with heparin cofactor activity prepared by disc electrophoresis. Scand J Clin Lab Invest. 21:1968;89-91.
    • (1968) Scand J Clin Lab Invest , vol.21 , pp. 89-91
    • Abildgaard, U.1
  • 3
    • 0017044123 scopus 로고
    • Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin III and by gel filtration
    • ANDERSSON L.O., BARROWCLIFFE T.W., HOLMER E., JOHNSON E.A., SIMS G.E.C. Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin III and by gel filtration. Thromb Res. 9:1976;575-583.
    • (1976) Thromb Res , vol.9 , pp. 575-583
    • Andersson, L.O.1    Barrowcliffe, T.W.2    Holmer, E.3    Johnson, E.A.4    Sims, G.E.C.5
  • 4
    • 0017074450 scopus 로고
    • Anticoagulant activity of heparin: Separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin
    • HÖÖK M., BJÖRK I., HOPWOOD J., LINDAHL U. Anticoagulant activity of heparin: Separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin. FEBS Lett. 66:1976;90-93.
    • (1976) FEBS Lett , vol.66 , pp. 90-93
    • Höök, M.1    Björk, I.2    Hopwood, J.3    Lindahl, U.4
  • 6
    • 0019499060 scopus 로고
    • The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin
    • HOLMER E., KURACHI K., SÖDERSTRÖM G. The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin. Biochem J. 193:1981;395-400.
    • (1981) Biochem J , vol.193 , pp. 395-400
    • Holmer, E.1    Kurachi, K.2    Söderström, G.3
  • 7
    • 0018076716 scopus 로고
    • The molecular weight dependence of the anticoagulant activity of heparin
    • LAURENT T.C., TENGBLAD A., THUNBERG L., HÖÖ M., LINDAHL U. The molecular weight dependence of the anticoagulant activity of heparin. Biochem J. 175:1978;691-701.
    • (1978) Biochem J , vol.175 , pp. 691-701
    • Laurent, T.C.1    Tengblad, A.2    Thunberg, L.3    Höö, M.4    Lindahl, U.5
  • 11
    • 0019794201 scopus 로고
    • Relationship between the anti-thrombotic and anticoagulant effects of low molecular weight heparin
    • CARTER C.J., KELTON J.G., HIRSH J., GENT M. Relationship between the anti-thrombotic and anticoagulant effects of low molecular weight heparin. Thromb Res. 21:1981;169-174.
    • (1981) Thromb Res , vol.21 , pp. 169-174
    • Carter, C.J.1    Kelton, J.G.2    Hirsh, J.3    Gent, M.4
  • 12
    • 0019982471 scopus 로고
    • Anticoagulant and antithrombotic effects of heparin and low molecular weight heparin fragments in rabbits
    • HOLMER E., MATTSSON C., NILSSON S. Anticoagulant and antithrombotic effects of heparin and low molecular weight heparin fragments in rabbits. Thromb Res. 25:1982;475-485.
    • (1982) Thromb Res , vol.25 , pp. 475-485
    • Holmer, E.1    Mattsson, C.2    Nilsson, S.3
  • 13
    • 0020416889 scopus 로고
    • Discordance between the anti-Xa activity and the antithrombotic activity in an ultra-low molecular weight heparin fraction
    • OCKELFORD P.A., CARTER C.J., MITCHELL L., HIRSH J. Discordance between the anti-Xa activity and the antithrombotic activity in an ultra-low molecular weight heparin fraction. Thromb Res. 28:1982;401-409.
    • (1982) Thromb Res , vol.28 , pp. 401-409
    • Ockelford, P.A.1    Carter, C.J.2    Mitchell, L.3    Hirsh, J.4
  • 14
    • 0019512082 scopus 로고
    • Studies in man and experimental animals of a low molecular weight heparin fraction
    • THOMAS D.P., MERTON R.E., LEWIS W.E., BARROWCLIFFE T.W. Studies in man and experimental animals of a low molecular weight heparin fraction. Thromb Haemost. 45:1981;214-218.
    • (1981) Thromb Haemost , vol.45 , pp. 214-218
    • Thomas, D.P.1    Merton, R.E.2    Lewis, W.E.3    Barrowcliffe, T.W.4
  • 15
    • 0019953801 scopus 로고
    • Effects of heparin oligosaccharides with high affinity for antithrombin III in experimental venous thrombosis
    • THOMAS D.P., MERTON R.E., BARROWCLIFFE T.W., THUNBERG L., LINDAHL U. Effects of heparin oligosaccharides with high affinity for antithrombin III in experimental venous thrombosis. Thromb Haemost. 47:1982;244-248.
    • (1982) Thromb Haemost , vol.47 , pp. 244-248
    • Thomas, D.P.1    Merton, R.E.2    Barrowcliffe, T.W.3    Thunberg, L.4    Lindahl, U.5
  • 16
    • 0019391466 scopus 로고
    • Structural studies on a biologically active hexasaccharide obtained from heparin
    • CHOAY J., LORMEAU J.C., PETITOU M., SINÄY P., FAREED J. Structural studies on a biologically active hexasaccharide obtained from heparin. Ann NY Acad Sci. 370:1981;644-649.
    • (1981) Ann NY Acad Sci , vol.370 , pp. 644-649
    • Choay, J.1    Lormeau, J.C.2    Petitou, M.3    Sinäy, P.4    Fareed, J.5
  • 17
    • 0020108082 scopus 로고
    • Further characterization of the antithrombin-binding sequence in heparin
    • THUNBERG L., BÄCKSTRÖM G., LINDAHL U. Further characterization of the antithrombin-binding sequence in heparin. Carbohydr Res. 100:1982;393-410.
    • (1982) Carbohydr Res , vol.100 , pp. 393-410
    • Thunberg, L.1    Bäckström, G.2    Lindahl, U.3
  • 19
    • 0021061174 scopus 로고
    • Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
    • CHOAY J., PETITOU M., LORMEAU J.C., SINÄY P., CASU B., GATTI G. Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem Biophys Acta. 116:1983;492-499.
    • (1983) Biochem Biophys Acta , vol.116 , pp. 492-499
    • Choay, J.1    Petitou, M.2    Lormeau, J.C.3    Sinäy, P.4    Casu, B.5    Gatti, G.6
  • 20
    • 0000391007 scopus 로고
    • Correlation between structure and function of heparin
    • ROSENBERG R.D., LAM L. Correlation between structure and function of heparin. Proc Natl Acad Sci USA. 76:1979;1218-1222.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 1218-1222
    • Rosenberg, R.D.1    Lam, L.2
  • 22
    • 0023049220 scopus 로고
    • Synthesis of heparin fragments. A chemical synthesis of the pentasaccharide 0-(2-deoxy-2-sulfamido-6-O-sulfo-alpha-D-glucopyranosyl)-1->4)-0-(beta-D- glucopyranosyluronic acid)-(1->4)-0-(2-deoxy-2-sulfamido-3, 6-di-0-sulfo-alpha-D-glucopyranosyl)-(1->4)-0-(2-O-sulfo-alpha-L-idopyranosyluronic acid)-(1->4)-2-deoxy-2-sulfamido-6-O-sulfo-D-glucopyranose decasodium salt, a heparin
    • fragment having high affinity for antithrombin III
    • PETITOU M., DUCHAUSSOY P., LEDERMAN I., CHOAY J., SINÄY P., JACQUINET J.C., TORRI G. Synthesis of heparin fragments. A chemical synthesis of the pentasaccharide 0-(2-deoxy-2-sulfamido-6-O-sulfo-alpha-D-glucopyranosyl)-1->4)-0-(beta-D- glucopyranosyluronic acid)-(1->4)-0-(2-deoxy-2-sulfamido-3, 6-di-0-sulfo-alpha-D-glucopyranosyl)-(1->4)-0-(2-O-sulfo-alpha- L-idopyranosyluronic acid)-(1->4)-2-deoxy-2-sulfamido-6-O-sulfo-D-glucopyranose decasodium salt, a heparin fragment having high affinity for antithrombin III. Carbohydr Res. 147:1986;221-236.
    • (1986) Carbohydr Res , vol.147 , pp. 221-236
    • Petitou, M.1    Duchaussoy, P.2    Lederman, I.3    Choay, J.4    Sinäy, P.5    Jacquinet, J.C.6    Torri, G.7
  • 23
    • 0022368634 scopus 로고
    • Contribution of monosaccharide residues in heparin binding to antithrombin III
    • ATHA D.H., LORMEAU J.C., PETITOU M., ROSENBERG R.D., CHOAY J. Contribution of monosaccharide residues in heparin binding to antithrombin III. Biochemistry. 24:1985;6723-6729.
    • (1985) Biochemistry , vol.24 , pp. 6723-6729
    • Atha, D.H.1    Lormeau, J.C.2    Petitou, M.3    Rosenberg, R.D.4    Choay, J.5
  • 24
    • 0022394350 scopus 로고
    • Mono- And bidimensional 500 MHZ proton NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: Evidence for conformational peculiarity of the sulfated iduronate residue
    • TORRI G., CASU B., GATTI G., PETITOU M., CHOAY J., JACQUINET J.C. Mono- and bidimensional 500 MHZ proton NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: Evidence for conformational peculiarity of the sulfated iduronate residue. Biochem Biophys Res Commun. 128:1985;134-140.
    • (1985) Biochem Biophys Res Commun , vol.128 , pp. 134-140
    • Torri, G.1    Casu, B.2    Gatti, G.3    Petitou, M.4    Choay, J.5    Jacquinet, J.C.6
  • 25
    • 0020544564 scopus 로고
    • The antithrombin-binding sequence in heparin. Identification of an essential 6-0 sulfate group
    • LINDAHL U., BÄCKSTRÖM G., THUNBERG L. The antithrombin-binding sequence in heparin. Identification of an essential 6-0 sulfate group. J Biol Chem. 258:1983;9826-9830.
    • (1983) J Biol Chem , vol.258 , pp. 9826-9830
    • Lindahl, U.1    Bäckström, G.2    Thunberg, L.3
  • 26
    • 0019862158 scopus 로고
    • The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups
    • RIESENFELD J., THUNBERG L., HÖÖK M., LINDAHL U. The antithrombin-binding sequence of heparin. Location of essential N-sulfate groups. J Biol Chem. 256:1981;2389-2394.
    • (1981) J Biol Chem , vol.256 , pp. 2389-2394
    • Riesenfeld, J.1    Thunberg, L.2    Höök, M.3    Lindahl, U.4
  • 28
    • 0025743779 scopus 로고
    • A new synthetic pentasaccharide with increased anti-factor Xa activity: Possible role for anionic clusters in the interaction of heparin and antithrombin III
    • PETITOU M., LORMEAU J.C., CHOAY J. A new synthetic pentasaccharide with increased anti-factor Xa activity: Possible role for anionic clusters in the interaction of heparin and antithrombin III. Semin Thromb Hemost. 17(2):1991;143-146.
    • (1991) Semin Thromb Hemost , vol.17 , Issue.2 , pp. 143-146
    • Petitou, M.1    Lormeau, J.C.2    Choay, J.3
  • 29
    • 0027028822 scopus 로고
    • Chemical synthesis of heparin fragments and analogues
    • PETITOU M., VAN BOECKEL C.A.A. Chemical synthesis of heparin fragments and analogues. Prog Chem Org Nat Prod. 60:1992;143-210.
    • (1992) Prog Chem Org Nat Prod , vol.60 , pp. 143-210
    • Petitou, M.1    Van Boeckel, C.A.A.2
  • 30
    • 0023655635 scopus 로고
    • Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III
    • RAGAZZI M., FERRO D.R. Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III. Carbohyr Res. 165:1987;C1-C5.
    • (1987) Carbohyr Res , vol.165
    • Ragazzi, M.1    Ferro, D.R.2
  • 31
    • 0025707188 scopus 로고
    • Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III
    • RAGAZZI M., FERRO D.R. Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III. Carbohydr Res. 195:1990;169-185.
    • (1990) Carbohydr Res , vol.195 , pp. 169-185
    • Ragazzi, M.1    Ferro, D.R.2
  • 32
    • 0019801543 scopus 로고
    • The structure of heparin oligosaccharide fragments with anti-factor Xa activity containing the minimal antithrombin III-binding sequence
    • CASU B., ORESTE P., TORRI G., ZOPPETTI G., CHOAY J., LORMEAU J.C., PETITOU M., SINÄY P. The structure of heparin oligosaccharide fragments with anti-factor Xa activity containing the minimal antithrombin III-binding sequence. Biochem J. 197:1981;599-609.
    • (1981) Biochem J , vol.197 , pp. 599-609
    • Casu, B.1    Oreste, P.2    Torri, G.3    Zoppetti, G.4    Choay, J.5    Lormeau, J.C.6    Petitou, M.7    Sinäy, P.8
  • 33
    • 0024969298 scopus 로고
    • 1H-n.m.r. spectroscopy of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III
    • 1H-n.m.r. spectroscopy of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III. Carbohydr Res. 185:1989;69-76.
    • (1989) Carbohydr Res , vol.185 , pp. 69-76
    • Gettins, P.1
  • 34
    • 0021226263 scopus 로고
    • Synthetic heparin fragments: New and efficient tools for the study of heparin and its interactions
    • PETITOU M. Synthetic heparin fragments: new and efficient tools for the study of heparin and its interactions. Nouv Rev Fr Hematol. 26:1984;221-226.
    • (1984) Nouv Rev Fr Hematol , vol.26 , pp. 221-226
    • Petitou, M.1
  • 35
    • 0024288551 scopus 로고
    • Binding of heparin to antithrombin III: A chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue
    • PETITOU M., DUCHAUSSOY P., LEDERMAN I., CHOAY J. Binding of heparin to antithrombin III: A chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue. Carbohydr Res. 179:1988;163-172.
    • (1988) Carbohydr Res , vol.179 , pp. 163-172
    • Petitou, M.1    Duchaussoy, P.2    Lederman, I.3    Choay, J.4
  • 37
    • 0024166295 scopus 로고
    • Importance of a 3-O-sulfate group in a heparin pentasaccharide for antithrombotic activity
    • WALENGA J.M., PETITOU M., SAMAMA M., FAREED J., CHOAY J. Importance of a 3-O-sulfate group in a heparin pentasaccharide for antithrombotic activity. Thromb Res. 52:1988;553-563.
    • (1988) Thromb Res , vol.52 , pp. 553-563
    • Walenga, J.M.1    Petitou, M.2    Samama, M.3    Fareed, J.4    Choay, J.5
  • 39
    • 0038823170 scopus 로고
    • A new synthetic pentasaccharide with increased anti-factor Xa activity: Possible role for anionic clusters in the interaction of heparin and antithrombin III
    • PETITOU M., LORMEAU J.C., CHOAY J. A new synthetic pentasaccharide with increased anti-factor Xa activity: Possible role for anionic clusters in the interaction of heparin and antithrombin III. Semin Thromb Res. 19(2):1993;143-146.
    • (1993) Semin Thromb Res , vol.19 , Issue.2 , pp. 143-146
    • Petitou, M.1    Lormeau, J.C.2    Choay, J.3
  • 41
    • 0025770037 scopus 로고
    • Antifactor Xa activity and antithrombotic activity in rats of structural analogues of the minimum antithrombin III binding sequence: Discovery of compounds with a longer duration of action than of the natural pentasaccharide
    • MEULEMAN D.G., HOBBELEN P.M.J., VAN DINTHER T.G., VOGEL G.M.T., VAN BOECKEL C.A.A., MOELKER H.C.T. Antifactor Xa activity and antithrombotic activity in rats of structural analogues of the minimum antithrombin III binding sequence: Discovery of compounds with a longer duration of action than of the natural pentasaccharide. Semin Thromb Hemost. 17(1):1991;112-117.
    • (1991) Semin Thromb Hemost , vol.17 , Issue.1 , pp. 112-117
    • Meuleman, D.G.1    Hobbelen, P.M.J.2    Van Dinther, T.G.3    Vogel, G.M.T.4    Van Boeckel, C.A.A.5    Moelker, H.C.T.6
  • 42
  • 43
    • 0343902282 scopus 로고
    • Biochemical and pharmacological properties of O-sulfated, O-methylated analogues of the natural pentasaccharide
    • HERAULT J.P., BARZU T., CREPON B., BERNAT A., LORMEAU J.C., HERBERT J.M., PETITOU M. Biochemical and pharmacological properties of O-sulfated, O-methylated analogues of the natural pentasaccharide. Thromb Haemost. 73:1995;1321.
    • (1995) Thromb Haemost , vol.73 , pp. 1321
    • Herault, J.P.1    Barzu, T.2    Crepon, B.3    Bernat, A.4    Lormeau, J.C.5    Herbert, J.M.6    Petitou, M.7
  • 44
    • 0343902282 scopus 로고
    • Biochemical and pharmacological properties of SANORG 32701, a potent analogue of the 'natural pentasaccharide.'
    • HERBERT J.M., HERAULT J.P., BARZU T., BERNAT A., LORMEAU J.C., PETITOU M. Biochemical and pharmacological properties of SANORG 32701, a potent analogue of the 'natural pentasaccharide.'. Thromb Haemost. 73:1995;1321.
    • (1995) Thromb Haemost , vol.73 , pp. 1321
    • Herbert, J.M.1    Herault, J.P.2    Barzu, T.3    Bernat, A.4    Lormeau, J.C.5    Petitou, M.6
  • 45
    • 0020620229 scopus 로고
    • Isolation and sequence characterization of a cDNA clone of human antithrombin III
    • CHANDRA T., STACKHOUSE R., KIDD V.J., WOO S.L.C. Isolation and sequence characterization of a cDNA clone of human antithrombin III. Proc Natl Acad Sci USA. 80:1983;1845-1848.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1845-1848
    • Chandra, T.1    Stackhouse, R.2    Kidd, V.J.3    Woo, S.L.C.4
  • 47
    • 0015821564 scopus 로고
    • The purification and mechanism of action of human antithrombin-heparin cofactor
    • ROSENBERG R.D., DAMUS P.S. The purification and mechanism of action of human antithrombin-heparin cofactor. J Biol Chem. 248:1973;6490-6505.
    • (1973) J Biol Chem , vol.248 , pp. 6490-6505
    • Rosenberg, R.D.1    Damus, P.S.2
  • 48
    • 0015853889 scopus 로고
    • Anticoagulant action of heparin
    • DAMUS P.S., HICKS M., ROSENBERG R.D. Anticoagulant action of heparin. Nature. 246:1973;355-357.
    • (1973) Nature , vol.246 , pp. 355-357
    • Damus, P.S.1    Hicks, M.2    Rosenberg, R.D.3
  • 49
    • 0019163952 scopus 로고
    • The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin
    • JORDAN R.E., OOSTA G.M., GARDNER W.T., ROSENBERG R.D. The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. J Biol Chem. 255:1980;10081-10090.
    • (1980) J Biol Chem , vol.255 , pp. 10081-10090
    • Jordan, R.E.1    Oosta, G.M.2    Gardner, W.T.3    Rosenberg, R.D.4
  • 50
    • 0023742709 scopus 로고
    • New carbohydrate site in mutant antithrombin (7ILE-ASN) with decreased heparin affinity
    • BRENNAN S.O., BORG J.Y., GEORGE P.M., SORIA C., SORIA J., CAEN J., CARRELL R.W. New carbohydrate site in mutant antithrombin (7ILE-ASN) with decreased heparin affinity. FEBS Lett. 237:1988;118-122.
    • (1988) FEBS Lett , vol.237 , pp. 118-122
    • Brennan, S.O.1    Borg, J.Y.2    George, P.M.3    Soria, C.4    Soria, J.5    Caen, J.6    Carrell, R.W.7
  • 51
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions
    • OLSON S.T., BJÖRK I., SHEFFER R., CRAIG P.A., SHORE J.D., CHOAY J. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. J Biol Chem. 267:1992;12528-12538.
    • (1992) J Biol Chem , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Björk, I.2    Sheffer, R.3    Craig, P.A.4    Shore, J.D.5    Choay, J.6
  • 52
    • 0002061080 scopus 로고
    • Antithrombin and related inhibitors of coagulation proteinases
    • A.J. Barrett and G.S. Salvesen (eds.), Elsevier, Amsterdam, The Netherlands
    • BJÖRK, I. and DANIELSSON, A. Antithrombin and related inhibitors of coagulation proteinases. In: Proteinase Inhibitors. A.J. Barrett and G.S. Salvesen (eds.), pp. 489-513, Elsevier, Amsterdam, The Netherlands (1986).
    • (1986) In: Proteinase Inhibitors , pp. 489-513
    • Björk, I.1    Danielsson, A.2
  • 53
    • 0023277522 scopus 로고
    • Antithrombin conformation and the catalytic role of heparin II. Is the heparin-induced conformational change in antithrombin required for rapid inactivation of thrombin
    • PETERSON C.B., BLACKBURN M.N. Antithrombin conformation and the catalytic role of heparin II. Is the heparin-induced conformational change in antithrombin required for rapid inactivation of thrombin. J Biol Chem. 262:1987;7559-7566.
    • (1987) J Biol Chem , vol.262 , pp. 7559-7566
    • Peterson, C.B.1    Blackburn, M.N.2
  • 54
    • 0023037887 scopus 로고
    • Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity purified heparin
    • NESHEIM M., BLACKBURN M.H., LAWLER C.M., MANN K.G. Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity purified heparin. J Biol Chem. 261:1986;3214-3221.
    • (1986) J Biol Chem , vol.261 , pp. 3214-3221
    • Nesheim, M.1    Blackburn, M.H.2    Lawler, C.M.3    Mann, K.G.4
  • 55
    • 0021363605 scopus 로고
    • Involvement of heparin chain length in the heparin catalyzed inhibition of thrombin by antithrombin III
    • HOYLAERTS M., OWEN W.G., COLLEN D. Involvement of heparin chain length in the heparin catalyzed inhibition of thrombin by antithrombin III. J Biol Chem. 259:1984;5670-5677.
    • (1984) J Biol Chem , vol.259 , pp. 5670-5677
    • Hoylaerts, M.1    Owen, W.G.2    Collen, D.3
  • 56
    • 0020412932 scopus 로고
    • The heparin-enhanced antithrombin III/thrombin reaction is saturable with respect to both thrombin and antithrombin III
    • GRIFFITH M.J. The heparin-enhanced antithrombin III/thrombin reaction is saturable with respect to both thrombin and antithrombin III. J Biol Chem. 257:1982;13899-13902.
    • (1982) J Biol Chem , vol.257 , pp. 13899-13902
    • Griffith, M.J.1
  • 57
    • 0022003799 scopus 로고
    • Reactive site peptides structural similarity between heparin cofactor II and antithrombin III
    • GRIFFITH M.J., NOYES L.M., CHURCH F.C. Reactive site peptides structural similarity between heparin cofactor II and antithrombin III. J Biol Chem. 260:1985;2218-2225.
    • (1985) J Biol Chem , vol.260 , pp. 2218-2225
    • Griffith, M.J.1    Noyes, L.M.2    Church, F.C.3
  • 58
    • 0029563321 scopus 로고
    • The effect of the synthetic pentasaccharide SR 90107/ORG 31540 on thrombin generation ex vivo is uniquely due to AT-mediated neutralization of factor Xa.
    • LORMEAU J.C., HERAULT J.P. The effect of the synthetic pentasaccharide SR 90107/ORG 31540 on thrombin generation ex vivo is uniquely due to AT-mediated neutralization of factor Xa. Thromb Haemost. 74:1995;1474-1477.
    • (1995) Thromb Haemost , vol.74 , pp. 1474-1477
    • Lormeau, J.C.1    Herault, J.P.2
  • 59
    • 0343466436 scopus 로고
    • Heparin cofactor II interactions with heparin pentasaccharide are minimal to mediate its antithrombotic actions
    • KAISER B., HOPPENSTEADT D., JESKE W., WALENGA J.M., FAREED J., SAMAMA M. Heparin cofactor II interactions with heparin pentasaccharide are minimal to mediate its antithrombotic actions. Thromb Haemost. 69:1993;1111.
    • (1993) Thromb Haemost , vol.69 , pp. 1111
    • Kaiser, B.1    Hoppensteadt, D.2    Jeske, W.3    Walenga, J.M.4    Fareed, J.5    Samama, M.6
  • 60
    • 0021864389 scopus 로고
    • Preliminary biochemical and pharmacological studies on a chemically synthesized pentasaccharide
    • WALENGA J.M., FAREED J. Preliminary biochemical and pharmacological studies on a chemically synthesized pentasaccharide. Semin Thromb Hemost. 11:1985;89-99.
    • (1985) Semin Thromb Hemost , vol.11 , pp. 89-99
    • Walenga, J.M.1    Fareed, J.2
  • 61
    • 0028296628 scopus 로고
    • Dermatan sulfate is a more potent inhibitor of clot-bound thrombin than unfractionated and low molecular weight heparins
    • BENDAYAN P., BOCCALON H., DUPOUY D., BONEU B. Dermatan sulfate is a more potent inhibitor of clot-bound thrombin than unfractionated and low molecular weight heparins. Thromb Haemost. 71:1994;576-580.
    • (1994) Thromb Haemost , vol.71 , pp. 576-580
    • Bendayan, P.1    Boccalon, H.2    Dupouy, D.3    Boneu, B.4
  • 62
    • 0025324338 scopus 로고
    • The inhibition of intrinsic prothrombinase and its generation by heparin and four derivatives in prothrombin poor plasma
    • BENDETOWICZ A.V., BARA L., SAMAMA M.M. The inhibition of intrinsic prothrombinase and its generation by heparin and four derivatives in prothrombin poor plasma. Thromb Res. 58:1990;445-454.
    • (1990) Thromb Res , vol.58 , pp. 445-454
    • Bendetowicz, A.V.1    Bara, L.2    Samama, M.M.3
  • 63
    • 0024436366 scopus 로고
    • Free factor Xa is on the main pathway of thrombin generation in clotting plasma
    • HEMKER H.C., CHOAY J., BÉGUIN S. Free factor Xa is on the main pathway of thrombin generation in clotting plasma. Biochem Biophys Acta. 992:1989;409-411.
    • (1989) Biochem Biophys Acta , vol.992 , pp. 409-411
    • Hemker, H.C.1    Choay, J.2    Béguin, S.3
  • 64
    • 0027199974 scopus 로고
    • Importance of factor Xa in determining the procoagulant activity of whole-blood clots
    • EISENBERG P.R., SIEGEL J.E., ABENDSCHEIN D.R., MILETICH J.P. Importance of factor Xa in determining the procoagulant activity of whole-blood clots. J Clin Invest. 91:1993;1877-1883.
    • (1993) J Clin Invest , vol.91 , pp. 1877-1883
    • Eisenberg, P.R.1    Siegel, J.E.2    Abendschein, D.R.3    Miletich, J.P.4
  • 65
    • 0027501426 scopus 로고
    • Antithrombotic effects of synthetic pentasaccharide with high affinity for plasma antithrombin III in nonhuman primates
    • CADROY Y., HANSON S.R., HARKER L.A. Antithrombotic effects of synthetic pentasaccharide with high affinity for plasma antithrombin III in nonhuman primates. Thromb Haemost. 70:1993;631-635.
    • (1993) Thromb Haemost , vol.70 , pp. 631-635
    • Cadroy, Y.1    Hanson, S.R.2    Harker, L.A.3
  • 67
    • 0023214250 scopus 로고
    • Antithrombotic activity of a synthetic heparin pentasaccharide in a rabbit stasis thrombosis model using different thrombogenic challenges
    • WALENGA J.M., PETITOU M., LORMEAU J.C., SAMAMA M., FAREED J., CHOAY J. Antithrombotic activity of a synthetic heparin pentasaccharide in a rabbit stasis thrombosis model using different thrombogenic challenges. Thromb Res. 46:1987;187-198.
    • (1987) Thromb Res , vol.46 , pp. 187-198
    • Walenga, J.M.1    Petitou, M.2    Lormeau, J.C.3    Samama, M.4    Fareed, J.5    Choay, J.6
  • 68
    • 0037808805 scopus 로고
    • AT III as a rate limiting factor for the measurement of pentasaccharide in laboratory assays
    • WALENGA J.M., BARA L., HOPPENSTEADT D., CHOAY J., FAREED J., SAMAMA M. AT III as a rate limiting factor for the measurement of pentasaccharide in laboratory assays. Thromb Haemost. 65:1991;1314.
    • (1991) Thromb Haemost , vol.65 , pp. 1314
    • Walenga, J.M.1    Bara, L.2    Hoppensteadt, D.3    Choay, J.4    Fareed, J.5    Samama, M.6
  • 70
    • 0023923422 scopus 로고
    • The inhibition of the generation of thrombin and the antithrombotic effect of a pentasaccharide with sole anti-factor Xa activity
    • WALENGA J.M., BARA L., PETITOU M., SAMAMA M., FAREED J., CHOAY J. The inhibition of the generation of thrombin and the antithrombotic effect of a pentasaccharide with sole anti-factor Xa activity. Thromb Res. 51:1988;23-33.
    • (1988) Thromb Res , vol.51 , pp. 23-33
    • Walenga, J.M.1    Bara, L.2    Petitou, M.3    Samama, M.4    Fareed, J.5    Choay, J.6
  • 71
    • 0038485155 scopus 로고
    • The antithrombotic activity of synthetic pentasaccharides and fraxiparine is closely correlated with their respective ability to alter thromboplastin-triggered thrombin generation ex vivo
    • DOL F., GAICH C., PETITOU M., BONEU B., CARANOBE C., BERNAT A., SAINTE MARIE M., HERBERT J.M. The antithrombotic activity of synthetic pentasaccharides and fraxiparine is closely correlated with their respective ability to alter thromboplastin-triggered thrombin generation ex vivo. Thromb Haemost. 69:1993;655.
    • (1993) Thromb Haemost , vol.69 , pp. 655
    • Dol, F.1    Gaich, C.2    Petitou, M.3    Boneu, B.4    Caranobe, C.5    Bernat, A.6    Sainte Marie, M.7    Herbert, J.M.8
  • 72
    • 0002970153 scopus 로고
    • Relative contribution of factor Xa and factor IIa inhibition in the mediation of the antithrombotic actions of LMWHs and synthetic heparin pentasaccharides
    • WALENGA J.M., FAREED J. Relative contribution of factor Xa and factor IIa inhibition in the mediation of the antithrombotic actions of LMWHs and synthetic heparin pentasaccharides. Thromb Haemorr Dis. 3:1991;53-59.
    • (1991) Thromb Haemorr Dis , vol.3 , pp. 53-59
    • Walenga, J.M.1    Fareed, J.2
  • 73
    • 0025131983 scopus 로고
    • Inhibition of factor X and factor V activation by dermatan sulfate and a pentasaccharide with high affinity for antithrombin III in human plasma
    • OFOSU F.A., CHOAY J., ANVARI N., SMITH L.M., BLAJCHMAN M.A. Inhibition of factor X and factor V activation by dermatan sulfate and a pentasaccharide with high affinity for antithrombin III in human plasma. Eur J Biochem. 193:1990;485-493.
    • (1990) Eur J Biochem , vol.193 , pp. 485-493
    • Ofosu, F.A.1    Choay, J.2    Anvari, N.3    Smith, L.M.4    Blajchman, M.A.5
  • 74
    • 0024339952 scopus 로고
    • The action of a synthetic pentasaccharide on thrombin generation in whole plasma
    • BÉGUIN S., CHOAY J., HEMKER H.C. The action of a synthetic pentasaccharide on thrombin generation in whole plasma. Thromb Haemost. 61:1989;397-401.
    • (1989) Thromb Haemost , vol.61 , pp. 397-401
    • Béguin, S.1    Choay, J.2    Hemker, H.C.3
  • 75
    • 0027476096 scopus 로고
    • Comparative inhibition of extrinsic and intrinsic thrombin generation by standard heparin, a low molecular weight heparin, and a synthetic AT-III binding pentasaccharide
    • LORMEAU J.C., HERAULT J.P. Comparative inhibition of extrinsic and intrinsic thrombin generation by standard heparin, a low molecular weight heparin, and a synthetic AT-III binding pentasaccharide. Thromb Haemost. 69:1993;152-156.
    • (1993) Thromb Haemost , vol.69 , pp. 152-156
    • Lormeau, J.C.1    Herault, J.P.2
  • 76
    • 0025888910 scopus 로고
    • Modulation of the enzymatic activity of α-thrombin by polyanions: Consequences on intrinsic activation of factor V and factor VIII
    • OFOSU F.A. Modulation of the enzymatic activity of α-thrombin by polyanions: Consequences on intrinsic activation of factor V and factor VIII. Haemostasis. 21:1991;240-247.
    • (1991) Haemostasis , vol.21 , pp. 240-247
    • Ofosu, F.A.1
  • 77
    • 0026500854 scopus 로고
    • Lipoprotein-associated coagulation inhibitor (LACI) is a cofactor for heparin: Synergistic anticoagulant action between LACI and sulfated polysaccharides
    • WUN T.-C. Lipoprotein-associated coagulation inhibitor (LACI) is a cofactor for heparin: Synergistic anticoagulant action between LACI and sulfated polysaccharides. Blood. 79:1992;430-438.
    • (1992) Blood , vol.79 , pp. 430-438
    • Wun, T.-C.1
  • 79
    • 0027263354 scopus 로고
    • Binding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa
    • RAO L.V.M., RAPAPORT S.I., HOANG A.D. Binding of factor VIIa to tissue factor permits rapid antithrombin III/heparin inhibition of factor VIIa. Blood. 81:1993;2600-2607.
    • (1993) Blood , vol.81 , pp. 2600-2607
    • Rao, L.V.M.1    Rapaport, S.I.2    Hoang, A.D.3
  • 80
    • 0026702636 scopus 로고
    • The low molecular weight heparin enoxaparin inhibits the consumption of factor VII and prothrombin activation in vivo associated with elective knee replacement surgery
    • OFOSU F.A., LECLERC J., DELORME F., CRAVEN S., SHAFAI S., FREWIN L., BLAJCHMAN M.A. The low molecular weight heparin enoxaparin inhibits the consumption of factor VII and prothrombin activation in vivo associated with elective knee replacement surgery. Br J Haematol. 83:1992;391-399.
    • (1992) Br J Haematol , vol.83 , pp. 391-399
    • Ofosu, F.A.1    Leclerc, J.2    Delorme, F.3    Craven, S.4    Shafai, S.5    Frewin, L.6    Blajchman, M.A.7
  • 81
    • 0029873917 scopus 로고    scopus 로고
    • Treatment with LMWHs inhibits factor VIIa generation during in vitro coagulation of whole blood
    • GEROTZIAFAS G.T., BARA L., BLOCH M.F., MAKRIS P.E., SAMAMA M.M. Treatment with LMWHs inhibits factor VIIa generation during in vitro coagulation of whole blood. Thromb Res. 81:1996;491-496.
    • (1996) Thromb Res , vol.81 , pp. 491-496
    • Gerotziafas, G.T.1    Bara, L.2    Bloch, M.F.3    Makris, P.E.4    Samama, M.M.5
  • 82
    • 0030035480 scopus 로고    scopus 로고
    • Antithrombin mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to AT
    • LORMEAU J.C., HERAULT J.P., HERBERT J.M. Antithrombin mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to AT. Thromb Haemost. 76:1996;5-8.
    • (1996) Thromb Haemost , vol.76 , pp. 5-8
    • Lormeau, J.C.1    Herault, J.P.2    Herbert, J.M.3
  • 83
    • 0023851665 scopus 로고
    • Lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: Insight into its possible mechanism of action
    • BROZE G.J., WARREN L.P., NOVOTNY W.F., HIGUCHI D.A., GIRARD J.J., MILETICH J.P. Lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: Insight into its possible mechanism of action. Blood. 71:1988;335-343.
    • (1988) Blood , vol.71 , pp. 335-343
    • Broze, G.J.1    Warren, L.P.2    Novotny, W.F.3    Higuchi, D.A.4    Girard, J.J.5    Miletich, J.P.6
  • 84
    • 0029939395 scopus 로고    scopus 로고
    • Initiation of the tissue factor pathway of coagulation in the presence of heparin: Control by antithrombin III and tissue factor pathway inhibitor
    • JESTY J., LORENZ A., RODRIGUEZ J., WUN T-C. Initiation of the tissue factor pathway of coagulation in the presence of heparin: Control by antithrombin III and tissue factor pathway inhibitor. Blood. 87:1996;2301-2307.
    • (1996) Blood , vol.87 , pp. 2301-2307
    • Jesty, J.1    Lorenz, A.2    Rodriguez, J.3    Wun, T-C.4
  • 85
    • 0028796872 scopus 로고
    • TFPI antigen levels in normal human volunteers after IV and SC administration of heparin and a low molecular weight heparin
    • HOPPENSTEADT D., WALENGA J.M., FASANELLA A., JESKE W., FAREED J. TFPI antigen levels in normal human volunteers after IV and SC administration of heparin and a low molecular weight heparin. Thromb Res. 77:1994;175-185.
    • (1994) Thromb Res , vol.77 , pp. 175-185
    • Hoppensteadt, D.1    Walenga, J.M.2    Fasanella, A.3    Jeske, W.4    Fareed, J.5
  • 86
    • 0027420108 scopus 로고
    • Comparative effects of enoxaparin and unfractionated heparin in healthy volunteers on prothrombin consumption in whole blood during coagulation, and release of tissue factor pathway inhibitor
    • BARA L., BLOCH M.F., ZITOUN D., SAMAMA M., COLLIGNON F., FRYDMAN A., UZAN A., BOUTHIER J. Comparative effects of enoxaparin and unfractionated heparin in healthy volunteers on prothrombin consumption in whole blood during coagulation, and release of tissue factor pathway inhibitor. Thromb Res. 69:1993;443-452.
    • (1993) Thromb Res , vol.69 , pp. 443-452
    • Bara, L.1    Bloch, M.F.2    Zitoun, D.3    Samama, M.4    Collignon, F.5    Frydman, A.6    Uzan, A.7    Bouthier, J.8
  • 88
    • 0026500854 scopus 로고
    • Lipoprotein associated coagulation inhibitor (LACI) is a cofactor for heparin: Synergistic anticoagulant action between LACI and sulfated polysaccharides
    • WUN T.C. Lipoprotein associated coagulation inhibitor (LACI) is a cofactor for heparin: Synergistic anticoagulant action between LACI and sulfated polysaccharides. Blood. 79:1992;430-438.
    • (1992) Blood , vol.79 , pp. 430-438
    • Wun, T.C.1
  • 89
    • 0028124139 scopus 로고
    • Plasma TFPI activity after intravenous injection of pentasaccharide (PS) and unfractionated heparin in rabbits
    • ZITOUN D., BARA L., BLOCH M.F., SAMAMA M.M. Plasma TFPI activity after intravenous injection of pentasaccharide (PS) and unfractionated heparin in rabbits. Thromb Res. 75:1994;577-580.
    • (1994) Thromb Res , vol.75 , pp. 577-580
    • Zitoun, D.1    Bara, L.2    Bloch, M.F.3    Samama, M.M.4
  • 90
    • 0343902273 scopus 로고
    • Molecular weight dependence on the release of tissue factor pathway inhibitor after subcutaneous and intravenous actions of heparins
    • LOJEWSKI B., BACHER P., JESKE W., FAREED J. Molecular weight dependence on the release of tissue factor pathway inhibitor after subcutaneous and intravenous actions of heparins. Thromb Haemost. 69:1993;1174.
    • (1993) Thromb Haemost , vol.69 , pp. 1174
    • Lojewski, B.1    Bacher, P.2    Jeske, W.3    Fareed, J.4
  • 91
    • 0028141562 scopus 로고
    • Inhibitory effects of TFPI on thrombin and factor Xa generation in vitro-modulatory action of glycosaminoglycans
    • KAISER B., HOPPENSTEADT D.A., JESKE W., WUN T.C., FAREED J. Inhibitory effects of TFPI on thrombin and factor Xa generation in vitro-modulatory action of glycosaminoglycans. Thromb Res. 75:1994;609-616.
    • (1994) Thromb Res , vol.75 , pp. 609-616
    • Kaiser, B.1    Hoppensteadt, D.A.2    Jeske, W.3    Wun, T.C.4    Fareed, J.5
  • 92
    • 0029900257 scopus 로고    scopus 로고
    • The synthetic pentasaccharide SR 90107A/Org 31540 enhances tissue-type plasminogen activator-induced thrombolysis in rabbits
    • BERNAT A., HOFFMANN P., SAINTE-MARIE M., HERBERT J.M. The synthetic pentasaccharide SR 90107A/Org 31540 enhances tissue-type plasminogen activator-induced thrombolysis in rabbits. Fibrinolysis. 10:1996;151-157.
    • (1996) Fibrinolysis , vol.10 , pp. 151-157
    • Bernat, A.1    Hoffmann, P.2    Sainte-Marie, M.3    Herbert, J.M.4
  • 93
    • 0000400184 scopus 로고    scopus 로고
    • Effect of unfractionated heparin and a heparin pentasaccharide on the thrombolytic process in an experimental model in rabbits
    • KAISER B., FAREED J. Effect of unfractionated heparin and a heparin pentasaccharide on the thrombolytic process in an experimental model in rabbits. Fibrinolysis. 10(Suppl 3):1996;127.
    • (1996) Fibrinolysis , vol.10 , Issue.SUPPL. 3 , pp. 127
    • Kaiser, B.1    Fareed, J.2
  • 94
    • 0343902272 scopus 로고
    • An overview of nonheparin glycosaminoglycans as antithrombotic agents
    • L. Poller (ed.), Churchill Livingstone, London
    • FAREED, J., HOPPENSTEADT, D., JESKE, W. and WALENGA, J.M. An overview of nonheparin glycosaminoglycans as antithrombotic agents. In: Recent Advances in Blood Coagulation. L. Poller (ed.), pp. 169-187, Churchill Livingstone, London (1993).
    • (1993) In: Recent Advances in Blood Coagulation , pp. 169-187
    • Fareed, J.1    Hoppensteadt, D.2    Jeske, W.3    Walenga, J.M.4
  • 96
    • 0026446350 scopus 로고
    • Influence of selected heparins on human neutrophil functions in vitro
    • LABROUCHE S., FREYBURGER G., BELLOC F., BOISSEAU M.R. Influence of selected heparins on human neutrophil functions in vitro. Thromb Haemost. 68:1992;556-562.
    • (1992) Thromb Haemost , vol.68 , pp. 556-562
    • Labrouche, S.1    Freyburger, G.2    Belloc, F.3    Boisseau, M.R.4
  • 97
    • 0037739442 scopus 로고
    • Active surveillance for heparin-induced thrombocytopenia or thromboembolism
    • WALLIS D.E., LEWIS B.E., PIFARRÉ R., SCANLON P.J. Active surveillance for heparin-induced thrombocytopenia or thromboembolism. Chest. 106:1994;120S.
    • (1994) Chest , vol.106
    • Wallis, D.E.1    Lewis, B.E.2    Pifarré, R.3    Scanlon, P.J.4
  • 98
    • 0022504141 scopus 로고
    • Heparin-induced platelet aggregation: Dose/response relationships for a low molecular weight heparin derivative (PK 10169) and its subfractions
    • BRACE L.D., FAREED J. Heparin-induced platelet aggregation: Dose/response relationships for a low molecular weight heparin derivative (PK 10169) and its subfractions. Thromb Res. 42:1986;769-782.
    • (1986) Thromb Res , vol.42 , pp. 769-782
    • Brace, L.D.1    Fareed, J.2
  • 99
    • 0024360749 scopus 로고
    • In vitro studies of the interaction of heparin, low molecular weight heparin and heparinoids with platelets
    • MESSMORE H.L., GRIFFIN B., FAREED J., COYNE E., SEGHATCHIAN J. In vitro studies of the interaction of heparin, low molecular weight heparin and heparinoids with platelets. Ann NY Acad Sci. 556:1989;217-231.
    • (1989) Ann NY Acad Sci , vol.556 , pp. 217-231
    • Messmore, H.L.1    Griffin, B.2    Fareed, J.3    Coyne, E.4    Seghatchian, J.5
  • 100
    • 0002787983 scopus 로고    scopus 로고
    • Relative heparin-induced thrombocytopenic potential of low molecular weight heparins and new antithrombotic agents
    • WALENGA J.M., KOZA M.J., LEWIS B.E., PIFARRÉ R. Relative heparin-induced thrombocytopenic potential of low molecular weight heparins and new antithrombotic agents. Clin Appl Thromb/Hemostasis. 2(Suppl 1):1996;S21-S27.
    • (1996) Clin Appl Thromb/Hemostasis , vol.2 , Issue.SUPPL. 1
    • Walenga, J.M.1    Koza, M.J.2    Lewis, B.E.3    Pifarré, R.4
  • 101
    • 0028798995 scopus 로고
    • Absence of in vitro cross-reaction of pentasaccharide with the plasma heparin dependent factor of twenty-five patients with heparin associated thrombocytopenia
    • ELALAMY I., LECRUBIER C., POTEVIN F., ABDELOUAHED M., BARA L., MARIE J.P., SAMAMA M. Absence of in vitro cross-reaction of pentasaccharide with the plasma heparin dependent factor of twenty-five patients with heparin associated thrombocytopenia. Thromb Haemost. 74:1995;1384-1385.
    • (1995) Thromb Haemost , vol.74 , pp. 1384-1385
    • Elalamy, I.1    Lecrubier, C.2    Potevin, F.3    Abdelouahed, M.4    Bara, L.5    Marie, J.P.6    Samama, M.7
  • 102
    • 0029086769 scopus 로고
    • Characterization of the structural requirements for a carbohydrate based anticoagulant with a reduced risk of inducing the immunological type of heparin-associated thrombocytopenia
    • GREINACHER A., ALBAN S., DUMMEL V., FRANZ G., MUELLER-ECKHARDT C. Characterization of the structural requirements for a carbohydrate based anticoagulant with a reduced risk of inducing the immunological type of heparin-associated thrombocytopenia. Thromb Haemost. 74:1995;886-892.
    • (1995) Thromb Haemost , vol.74 , pp. 886-892
    • Greinacher, A.1    Alban, S.2    Dummel, V.3    Franz, G.4    Mueller-Eckhardt, C.5
  • 103
    • 0343030712 scopus 로고
    • Comparative heparin induced thrombocytopenic response with low molecular weight heparin and a synthetic pentasaccharide
    • PIFARRÉ R., WALENGA J.M., KOZA M.J., KHENKINA Y., FAREED J. Comparative heparin induced thrombocytopenic response with low molecular weight heparin and a synthetic pentasaccharide. Thromb Haemost. 69:1993;1319.
    • (1993) Thromb Haemost , vol.69 , pp. 1319
    • Pifarré, R.1    Walenga, J.M.2    Koza, M.J.3    Khenkina, Y.4    Fareed, J.5
  • 104
    • 0004931268 scopus 로고    scopus 로고
    • Development of a flow cytometric assay for the detection of heparin induced thrombocytopenia
    • JESKE W., SZATKOWSKI E., HOPPENSTEADT D., WALENGA J.M. Development of a flow cytometric assay for the detection of heparin induced thrombocytopenia. Blood. 88(Suppl 1):1996;317a.
    • (1996) Blood , vol.88 , Issue.SUPPL. 1
    • Jeske, W.1    Szatkowski, E.2    Hoppensteadt, D.3    Walenga, J.M.4
  • 105
    • 84940137996 scopus 로고
    • Biologic assay of a thrombosis-inducing activity in human serum
    • WESSLER S., REIMER S.M., SHEPS M.C. Biologic assay of a thrombosis-inducing activity in human serum. J Appl Physiol. 14:1959;943-946.
    • (1959) J Appl Physiol , vol.14 , pp. 943-946
    • Wessler, S.1    Reimer, S.M.2    Sheps, M.C.3
  • 106
    • 0022571055 scopus 로고
    • Intravenous antithrombotic activity of a synthetic heparin pentasaccharide in a human serum induced stasis thrombosis model
    • WALENGA J.M., FAREED J., PETITOU M., SAMAMA M., LORMEAU J.C., CHOAY J. Intravenous antithrombotic activity of a synthetic heparin pentasaccharide in a human serum induced stasis thrombosis model. Thromb Res. 43:1986;243-248.
    • (1986) Thromb Res , vol.43 , pp. 243-248
    • Walenga, J.M.1    Fareed, J.2    Petitou, M.3    Samama, M.4    Lormeau, J.C.5    Choay, J.6
  • 107
    • 0024582005 scopus 로고
    • The relative antithrombotic effectiveness of heparin, a low molecular weight heparin, and a pentasaccharide fragment in an animal model
    • THOMAS D.P., MERTON R.E., GRAY E., BARROWCLIFFE T.W. The relative antithrombotic effectiveness of heparin, a low molecular weight heparin, and a pentasaccharide fragment in an animal model. Thromb Haemost. 61:1989;204-207.
    • (1989) Thromb Haemost , vol.61 , pp. 204-207
    • Thomas, D.P.1    Merton, R.E.2    Gray, E.3    Barrowcliffe, T.W.4
  • 108
    • 0025145086 scopus 로고
    • Antithrombotic potencies of heparins in relation to their antifactor Xa and antithrombin activities: An experimental study in two models of thrombosis in the rabbit
    • AMAR J., CARANOBE P., SIE P., BONEU B. Antithrombotic potencies of heparins in relation to their antifactor Xa and antithrombin activities: An experimental study in two models of thrombosis in the rabbit. Br J Haematol. 76:1990;94-100.
    • (1990) Br J Haematol , vol.76 , pp. 94-100
    • Amar, J.1    Caranobe, P.2    Sie, P.3    Boneu, B.4
  • 109
  • 110
    • 0021930129 scopus 로고
    • The relative importance of thrombin inhibition and factor Xa inhibition to the antithrombotic effects of heparin
    • BUCHANAN M.R., BONEU B., OFOSU F., HIRSH J. The relative importance of thrombin inhibition and factor Xa inhibition to the antithrombotic effects of heparin. Blood. 65:1985;198-201.
    • (1985) Blood , vol.65 , pp. 198-201
    • Buchanan, M.R.1    Boneu, B.2    Ofosu, F.3    Hirsh, J.4
  • 111
    • 0021162806 scopus 로고
    • A comparison of the antithrombotic and haemorrhagic effects of low molecular weight heparin fractions: The influence of the method of preparation
    • CADE J.F., BUCHANAN M.R., BONEU B., OCKELFORD P., CARTER C.J., CERSKUS A.L., HIRSH J. A comparison of the antithrombotic and haemorrhagic effects of low molecular weight heparin fractions: The influence of the method of preparation. Thromb Res. 35:1985;613-625.
    • (1985) Thromb Res , vol.35 , pp. 613-625
    • Cade, J.F.1    Buchanan, M.R.2    Boneu, B.3    Ockelford, P.4    Carter, C.J.5    Cerskus, A.L.6    Hirsh, J.7
  • 112
    • 0022254370 scopus 로고
    • The effect of heparin fragments of different molecular weights on experimental thrombosis and haemostasis
    • BERGQVIST D., NILSSON B., HEDNER U., PEDERSEN P.C., OSTERGAARD P.B. The effect of heparin fragments of different molecular weights on experimental thrombosis and haemostasis. Thromb Res. 38:1985;589-601.
    • (1985) Thromb Res , vol.38 , pp. 589-601
    • Bergqvist, D.1    Nilsson, B.2    Hedner, U.3    Pedersen, P.C.4    Ostergaard, P.B.5
  • 113
    • 0024530951 scopus 로고
    • Rat jugular vein hemostasis - A new model for testing antithrombotic agents
    • RAAKE W., ELLING H. Rat jugular vein hemostasis - A new model for testing antithrombotic agents. Thromb Res. 53:1989;73-77.
    • (1989) Thromb Res , vol.53 , pp. 73-77
    • Raake, W.1    Elling, H.2
  • 114
    • 0024371047 scopus 로고
    • Comparison of two experimental thrombosis models in rats, effects of four glycosaminoglycans
    • VOGEL G.M.T., MEULEMAN D.G., BOURGONDIEN F.G.M., HOBBELEN P.M.J. Comparison of two experimental thrombosis models in rats, effects of four glycosaminoglycans. Thromb Res. 54:1989;399-410.
    • (1989) Thromb Res , vol.54 , pp. 399-410
    • Vogel, G.M.T.1    Meuleman, D.G.2    Bourgondien, F.G.M.3    Hobbelen, P.M.J.4
  • 115
    • 0027340349 scopus 로고
    • Pentasaccharide and Orgaran arrest, whereas heparin delays thrombus formation in a rat arteriovenous shunt
    • VOGEL G.M.T., VAN AMSTERDAM R.G.M., KOP W.J., MEULEMAN D.G. Pentasaccharide and Orgaran arrest, whereas heparin delays thrombus formation in a rat arteriovenous shunt. Thromb Haemost. 69:1993;29-34.
    • (1993) Thromb Haemost , vol.69 , pp. 29-34
    • Vogel, G.M.T.1    Van Amsterdam, R.G.M.2    Kop, W.J.3    Meuleman, D.G.4
  • 116
    • 0023944770 scopus 로고
    • Effect of low molecular weight heparins on laser-induced thrombus formation in rat mesenteric vessels
    • WEICHERT W., BREDDIN H.K. Effect of low molecular weight heparins on laser-induced thrombus formation in rat mesenteric vessels. Haemostasis. 18(Suppl 3):1988;55-63.
    • (1988) Haemostasis , vol.18 , Issue.SUPPL. 3 , pp. 55-63
    • Weichert, W.1    Breddin, H.K.2
  • 117
    • 0029793638 scopus 로고    scopus 로고
    • Protamine sulfate inhibits pentasaccharide (SR 80027)-induced bleeding without affecting its antithrombotic and anti-factor Xa activity in the rat
    • BERNAT A., HERBERT J.M. Protamine sulfate inhibits pentasaccharide (SR 80027)-induced bleeding without affecting its antithrombotic and anti-factor Xa activity in the rat. Haemostasis. 26:1996;195-202.
    • (1996) Haemostasis , vol.26 , pp. 195-202
    • Bernat, A.1    Herbert, J.M.2
  • 119
    • 0028211342 scopus 로고
    • Ex-vivo and in vitro evidence that low molecular weight heparins exhibit less binding to plasma proteins than unfractionated heparin
    • YOUNG E., WELLS P., HOLLOWAY S., WEITZ J., HIRSH J. Ex-vivo and in vitro evidence that low molecular weight heparins exhibit less binding to plasma proteins than unfractionated heparin. Thromb Haemost. 71:1994;300-304.
    • (1994) Thromb Haemost , vol.71 , pp. 300-304
    • Young, E.1    Wells, P.2    Holloway, S.3    Weitz, J.4    Hirsh, J.5
  • 120
    • 0001416176 scopus 로고
    • Endogenous AT III as a limiting factor in the mediation of antiprotease actions of heparins and related oligosaccharides. Impact on the pharmacodynamic parameters as calculated by using functional methods
    • BACHER P., FAREED J., HOPPENSTEADT D., WALENGA J.M., IQBAL O. Endogenous AT III as a limiting factor in the mediation of antiprotease actions of heparins and related oligosaccharides. Impact on the pharmacodynamic parameters as calculated by using functional methods. Thromb Haemost. 65:1991;932.
    • (1991) Thromb Haemost , vol.65 , pp. 932
    • Bacher, P.1    Fareed, J.2    Hoppensteadt, D.3    Walenga, J.M.4    Iqbal, O.5
  • 121
    • 0000417730 scopus 로고
    • Pharmacokinetic (PK) parameters of AT binding pentasaccharides in three animal species: Predictive value for humans
    • CRÉPON B., DONAT F., BARZU T., HÉRAULT J.P. Pharmacokinetic (PK) parameters of AT binding pentasaccharides in three animal species: Predictive value for humans. Thromb Haemost. 69:1993;654.
    • (1993) Thromb Haemost , vol.69 , pp. 654
    • Crépon, B.1    Donat, F.2    Barzu, T.3    Hérault, J.P.4
  • 122
  • 124
    • 0024543984 scopus 로고
    • Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor
    • GIRARD T.J., WARREN L.A., NOVOTNY W.F., LIKERT K.M., BROWN S.G., MILETICH J.P., BROZE G.J. Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. Nature. 338:1989;518-520.
    • (1989) Nature , vol.338 , pp. 518-520
    • Girard, T.J.1    Warren, L.A.2    Novotny, W.F.3    Likert, K.M.4    Brown, S.G.5    Miletich, J.P.6    Broze, G.J.7
  • 125
    • 0027724106 scopus 로고
    • Kinetics of factor Xa inhibition by tissue factor pathway inhibitor
    • HUANG Z.F., WUN T.C., BROZE G.J. Kinetics of factor Xa inhibition by tissue factor pathway inhibitor. J Biol Chem. 268:1993;26950-26955.
    • (1993) J Biol Chem , vol.268 , pp. 26950-26955
    • Huang, Z.F.1    Wun, T.C.2    Broze, G.J.3
  • 127
    • 0023189460 scopus 로고
    • Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation
    • TUSZYNSKI G.P., GASIC T.B., GASIC G.J. Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation. J Biol Chem. 262:1987;9718-9723.
    • (1987) J Biol Chem , vol.262 , pp. 9718-9723
    • Tuszynski, G.P.1    Gasic, T.B.2    Gasic, G.J.3
  • 128
    • 0025891319 scopus 로고
    • Comparison of the in vivo anticoagulant properties of standard heparin and the highly selective factor Xa inhibitors antistasin and tick anticoagulant peptide (TAP) in a rabbit model of venous thrombosis
    • VLASUK G.P., RAMJIT D., FUJITA T., DUNWIDDIE C.T., NUTT E.M., SMITH D.E., SHEBUSKI R.J. Comparison of the in vivo anticoagulant properties of standard heparin and the highly selective factor Xa inhibitors antistasin and tick anticoagulant peptide (TAP) in a rabbit model of venous thrombosis. Thromb Haemost. 65:1991;257-262.
    • (1991) Thromb Haemost , vol.65 , pp. 257-262
    • Vlasuk, G.P.1    Ramjit, D.2    Fujita, T.3    Dunwiddie, C.T.4    Nutt, E.M.5    Smith, D.E.6    Shebuski, R.J.7
  • 130
    • 0028260914 scopus 로고
    • Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa from the Mexican leech Haementeria officinalis
    • THEUNISSEN H.J., DIJKEMA R., SWINKELS J.C., DE POORTER T.L., VINK P.M., VAN DINTHER T.G. Mutational analysis of antistasin, an inhibitor of blood coagulation factor Xa from the Mexican leech Haementeria officinalis. Thromb Res. 75:1994;41-50.
    • (1994) Thromb Res , vol.75 , pp. 41-50
    • Theunissen, H.J.1    Dijkema, R.2    Swinkels, J.C.3    De Poorter, T.L.4    Vink, P.M.5    Van Dinther, T.G.6
  • 131
    • 0029079611 scopus 로고
    • Basic and applied pharmacology of low molecular weight heparins
    • FAREED, J. Basic and applied pharmacology of low molecular weight heparins. Pharmacy Therapeut June, 16s-24s, 1995.
    • (1995) Pharmacy Therapeut June
    • Fareed, J.1
  • 133
    • 0028006821 scopus 로고
    • Pharmacokinetic and pharmacodynamic properties of two pentasaccharides with high affinity to antithrombin III in the rabbit: Comparison with CY216
    • CARRIE D., CARANOBE C., SALVIN S., HOUIN G., PETITOU M., LORMEAU J.C., VAN BOECKEL C., MEULEMAN D., BONEU B. Pharmacokinetic and pharmacodynamic properties of two pentasaccharides with high affinity to antithrombin III in the rabbit: Comparison with CY216. Blood. 84:1994;2571-2577.
    • (1994) Blood , vol.84 , pp. 2571-2577
    • Carrie, D.1    Caranobe, C.2    Salvin, S.3    Houin, G.4    Petitou, M.5    Lormeau, J.C.6    Van Boeckel, C.7    Meuleman, D.8    Boneu, B.9
  • 135
    • 0023886488 scopus 로고
    • Proposed heparin binding site in antithrombin based on arginine 47
    • BORG J.Y., OWEN M.C., SORIA C., CAEN J., CARRELL R.W. Proposed heparin binding site in antithrombin based on arginine 47. J Clin Invest. 81:1988;1292-1296.
    • (1988) J Clin Invest , vol.81 , pp. 1292-1296
    • Borg, J.Y.1    Owen, M.C.2    Soria, C.3    Caen, J.4    Carrell, R.W.5
  • 136
    • 0022622201 scopus 로고
    • Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity
    • CHANG J.Y., TRAN T.H. Antithrombin III Basel. Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. J Biol Chem. 261:1986;1174-1176.
    • (1986) J Biol Chem , vol.261 , pp. 1174-1176
    • Chang, J.Y.1    Tran, T.H.2
  • 137
    • 0023881380 scopus 로고
    • Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow
    • ERDJUMENT H., LANE D.A., PANICO M., DIMARZO V., MORRIS H.R. Single amino acid substitutions in the reactive site of antithrombin leading to thrombosis. Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. J Biol Chem. 263:1988;5589-5593.
    • (1988) J Biol Chem , vol.263 , pp. 5589-5593
    • Erdjument, H.1    Lane, D.A.2    Panico, M.3    Dimarzo, V.4    Morris, H.R.5
  • 138
    • 0027945752 scopus 로고
    • Role of N- And C-terminal aminoacids in antithrombin binding to pentasaccharide
    • MILLE B., WATTON J., BARROWCLIFFE T., MANI J.C., LANE D. Role of N- and C-terminal aminoacids in antithrombin binding to pentasaccharide. J Biol Chem. 269:1994;29435-29443.
    • (1994) J Biol Chem , vol.269 , pp. 29435-29443
    • Mille, B.1    Watton, J.2    Barrowcliffe, T.3    Mani, J.C.4    Lane, D.5
  • 139
    • 0027367815 scopus 로고
    • Parallel mechanisms of high molecular weight kininogen action as a cofactor in kallikrein inactivation and prekallikrein activation reactions
    • OLSON S.T., FRANCIS A.M., SHEFFER R., CHOAY J. Parallel mechanisms of high molecular weight kininogen action as a cofactor in kallikrein inactivation and prekallikrein activation reactions. Biochemistry. 32:1993;12148-12159.
    • (1993) Biochemistry , vol.32 , pp. 12148-12159
    • Olson, S.T.1    Francis, A.M.2    Sheffer, R.3    Choay, J.4
  • 141
    • 0025282218 scopus 로고
    • Inhibition of the early stages of the thrombin generation reaction by various glycosaminoglycans
    • VISSER A., MEULEMAN D.G. Inhibition of the early stages of the thrombin generation reaction by various glycosaminoglycans. Thromb Res. 58:1990;469-474.
    • (1990) Thromb Res , vol.58 , pp. 469-474
    • Visser, A.1    Meuleman, D.G.2


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