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Volumn 92, Issue 5, 2004, Pages 929-939

Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Comparison with heparin and low-molecular-weight heparin

Author keywords

Antithrombin; Coagulation proteinases; Heparin; Hexadecasaccharide; Pentasaccharide

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 10A INHIBITOR; BLOOD CLOTTING FACTOR 11A; BLOOD CLOTTING FACTOR 12A; BLOOD CLOTTING FACTOR 7A; BLOOD CLOTTING FACTOR 9A; FONDAPARINUX; HEPARIN; IDRAPARINUX; LOW MOLECULAR WEIGHT HEPARIN; OLIGOSACCHARIDE; PROTEINASE; SR 123781A; THROMBIN; TISSUE PLASMINOGEN ACTIVATOR; UNCLASSIFIED DRUG;

EID: 9144269020     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH04-06-0384     Document Type: Article
Times cited : (119)

References (58)
  • 1
    • 0028061369 scopus 로고
    • Regulation of thrombin activity by antithrombin and heparin
    • Olson ST, Björk I. Regulation of thrombin activity by antithrombin and heparin. Semin Thromb Hemost 1994; 20: 373-409.
    • (1994) Semin. Thromb. Hemost. , vol.20 , pp. 373-409
    • Olson, S.T.1    Björk, I.2
  • 2
    • 0031455114 scopus 로고    scopus 로고
    • Antithrombin. A bloody important serpin
    • Church FC, Cunningham DD, Ginsburg D, Hoffman M, Stone SR, Tollefsen DM, eds. New York, Plenum Press
    • Björk I, Olson ST. Antithrombin. A bloody important serpin. In: Church FC, Cunningham DD, Ginsburg D, Hoffman M, Stone SR, Tollefsen DM, eds. Chemistry and Biology of Serpins. New York, Plenum Press 1997; 17-33.
    • (1997) Chemistry and Biology of Serpins , pp. 17-33
    • Björk, I.1    Olson, S.T.2
  • 3
    • 0037837506 scopus 로고    scopus 로고
    • 1976-83, a critical period in the history of heparin: The discovery of the antithrombin binding site
    • Petitou M, Casu B, Lindahl U. 1976-83, a critical period in the history of heparin: the discovery of the antithrombin binding site. Biochimie 2003; 85: 83-9.
    • (2003) Biochimie , vol.85 , pp. 83-89
    • Petitou, M.1    Casu, B.2    Lindahl, U.3
  • 4
    • 0026690347 scopus 로고
    • Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement
    • Olson ST, Björk I, Sheffer R, et al. Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement. J Biol Chem 1992; 267: 12528-38.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12528-12538
    • Olson, S.T.1    Björk, I.2    Sheffer, R.3
  • 5
    • 0029897204 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding
    • Huntington JA, Olson ST, Fan BQ et al. Mechanism of heparin activation of antithrombin. Evidence for reactive center loop preinsertion with expulsion upon heparin binding. Biochemistry 1996; 35: 8495-503.
    • (1996) Biochemistry , vol.35 , pp. 8495-8503
    • Huntington, J.A.1    Olson, S.T.2    Fan, B.Q.3
  • 7
    • 0034685780 scopus 로고    scopus 로고
    • The conformational activation of antithrombin - A 2.85-Å structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions
    • Huntington JA, McCoy A, Belzar KJ, et al. The conformational activation of antithrombin - A 2.85-Å structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regions. J Biol Chem 2000; 275: 15377-83.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15377-15383
    • Huntington, J.A.1    McCoy, A.2    Belzar, K.J.3
  • 8
    • 0035805579 scopus 로고    scopus 로고
    • Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence - Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin
    • Chuang YJ, Swanson R, Raja SM, et al. Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence - Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin. J Biol Chem 2001; 276: 14961-71.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14961-14971
    • Chuang, Y.J.1    Swanson, R.2    Raja, S.M.3
  • 9
    • 0035810925 scopus 로고    scopus 로고
    • The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation
    • Chuang YJ, Swanson R, Raja SM, et al. The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation. Biochemistry 2001; 40: 6670-9.
    • (2001) Biochemistry , vol.40 , pp. 6670-6679
    • Chuang, Y.J.1    Swanson, R.2    Raja, S.M.3
  • 10
    • 0022977122 scopus 로고
    • Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa
    • Danielsson A, Raub E, Lindahl U, et al. Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. J Biol Chem 1986; 261: 15467-73.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15467-15473
    • Danielsson, A.1    Raub, E.2    Lindahl, U.3
  • 11
    • 0025831251 scopus 로고
    • Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects
    • Olson ST, Björk I. Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects. J Biol Chem 1991; 266: 6353-64.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6353-6364
    • Olson, S.T.1    Björk, I.2
  • 12
    • 0038164797 scopus 로고    scopus 로고
    • Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites
    • Bedsted T, Swanson R, Chuang Y-J, et al. Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites. Biochemistry 2003; 42: 8143-52.
    • (2003) Biochemistry , vol.42 , pp. 8143-8152
    • Bedsted, T.1    Swanson, R.2    Chuang, Y.-J.3
  • 13
    • 0041315481 scopus 로고    scopus 로고
    • Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide
    • Wiebe EM, Stafford AR, Fredenburgh JC, et al. Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide. J Biol Chem 2003; 278: 35767-74.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35767-35774
    • Wiebe, E.M.1    Stafford, A.R.2    Fredenburgh, J.C.3
  • 14
    • 0004123216 scopus 로고    scopus 로고
    • Heparin-binding proteins
    • San Diego, CA, Academic Press
    • Conrad HE. Heparin-binding proteins. San Diego, CA, Academic Press; 1998.
    • (1998)
    • Conrad, H.E.1
  • 16
    • 0023716024 scopus 로고
    • Total hip arthroplasty after renal transplantadon. Long-term follow-up study and assessment of metabolic bone status
    • Devlin VJ, Einhorn TA, Gordon SL, et al. Total hip arthroplasty after renal transplantadon. Long-term follow-up study and assessment of metabolic bone status. J Arthroplasty 1988; 3: 205-13.
    • (1988) J. Arthroplasty , vol.3 , pp. 205-213
    • Devlin, V.J.1    Einhorn, T.A.2    Gordon, S.L.3
  • 17
    • 0029049674 scopus 로고
    • Low molecular weight heparin(s)
    • Barrowcliffe TW. Low molecular weight heparin(s). Br J Haematol 1995; 90: 1-7.
    • (1995) Br. J. Haematol. , vol.90 , pp. 1-7
    • Barrowcliffe, T.W.1
  • 18
    • 33748233635 scopus 로고
    • The unique antithrombin III binding domain of heparin: A lead to new synthetic antithrombotics
    • van Boeckel CAA, Petitou M. The unique antithrombin III binding domain of heparin: A lead to new synthetic antithrombotics. Angew Chem 1993; 32: 1671-90.
    • (1993) Angew Chem. , vol.32 , pp. 1671-1690
    • van Boeckel, C.A.A.1    Petitou, M.2
  • 19
    • 0344938369 scopus 로고    scopus 로고
    • Synthesis of thrombin-inhibiting heparin mimetics without side effects
    • Petitou M, Hérault JP, Bernat A, et al. Synthesis of thrombin-inhibiting heparin mimetics without side effects. Nature 1999; 398: 417-22.
    • (1999) Nature , vol.398 , pp. 417-422
    • Petitou, M.1    Hérault, J.P.2    Bernat, A.3
  • 20
    • 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 JC, et al. Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity. Biochem Biophys Res Commun 1983; 116: 492-9.
    • (1983) Biochem. Biophys. Res. Commun. , vol.116 , pp. 492-499
    • Choay, J.1    Petitou, M.2    Lormeau, J.C.3
  • 21
    • 0035283092 scopus 로고    scopus 로고
    • A synthetic pentasaccharide for the prevention of deep-vein thrombosis after total hip replacement
    • Turpie AGG, Gallus AS, Hoek JA. A synthetic pentasaccharide for the prevention of deep-vein thrombosis after total hip replacement. N Engl J Med 2001; 344: 619-25.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 619-625
    • Turpie, A.G.G.1    Gallus, A.S.2    Hoek, J.A.3
  • 22
    • 0035522302 scopus 로고    scopus 로고
    • Fondaparinux compared with enoxaparin for the prevention of venous thromboembolism after hip-fracture surgery
    • Eriksson BI, Bauer KA, Lassen MR, et al. Fondaparinux compared with enoxaparin for the prevention of venous thromboembolism after hip-fracture surgery. N Engl J Med 2001; 345: 1298-304.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1298-1304
    • Eriksson, B.I.1    Bauer, K.A.2    Lassen, M.R.3
  • 23
    • 0035522304 scopus 로고    scopus 로고
    • Fondaparinux compared with enoxaparin for the prevention of venous thromboembolism after elective major knee surgery
    • Bauer KA, Eriksson BI, Lassen MR, et al. Fondaparinux compared with enoxaparin for the prevention of venous thromboembolism after elective major knee surgery. N Engl J Med 2001; 345: 1305-10.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1305-1310
    • Bauer, K.A.1    Eriksson, B.I.2    Lassen, M.R.3
  • 24
    • 0037048227 scopus 로고    scopus 로고
    • Fondaparinux versus enoxaparin for the prevention of venous thromboembolism in major orthopedic surgery. A meta-analysis of 4 randomized double-blind studies
    • Turpie AGG, Bauer KA, Eriksson BI, et al. Fondaparinux versus enoxaparin for the prevention of venous thromboembolism in major orthopedic surgery. A meta-analysis of 4 randomized double-blind studies. Arch Intern Med 2002; 162: 1833-40.
    • (2002) Arch. Intern. Med. , vol.162 , pp. 1833-1840
    • Turpie, A.G.G.1    Bauer, K.A.2    Eriksson, B.I.3
  • 25
    • 0141450381 scopus 로고    scopus 로고
    • Influence of the duration of fondaparinux (Arixtra®) prophylaxis in preventing venous thromboembolism following major orthopedic surgery
    • Eriksson BI, Bauer KA, Lassen MR, et al. Influence of the duration of fondaparinux (Arixtra®) prophylaxis in preventing venous thromboembolism following major orthopedic surgery. J Thromb Haemost 2003; 1: 383-4.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 383-384
    • Eriksson, B.I.1    Bauer, K.A.2    Lassen, M.R.3
  • 26
    • 2642617786 scopus 로고    scopus 로고
    • Biochemical and pharmacological properties of SANORG 34006, a potent and long-acting synthetic pentasaccharide
    • Herbert JM, Hérault JP, Bernat A, et al. Biochemical and pharmacological properties of SANORG 34006, a potent and long-acting synthetic pentasaccharide. Blood 1998; 91: 4197-205.
    • (1998) Blood , vol.91 , pp. 4197-4205
    • Herbert, J.M.1    Hérault, J.P.2    Bernat, A.3
  • 28
    • 0019429980 scopus 로고
    • Binding to antithrombin of heparin fractions with different molecular weights
    • Danielsson A, Björk I. Binding to antithrombin of heparin fractions with different molecular weights. Biochem J 1981; 193: 427-33.
    • (1981) Biochem. J. , vol.193 , pp. 427-433
    • Danielsson, A.1    Björk, I.2
  • 29
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Olson ST, Björk I, Shore JD. Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol 1993; 222: 525-60.
    • (1993) Methods Enzymol. , vol.222 , pp. 525-560
    • Olson, S.T.1    Björk, I.2    Shore, J.D.3
  • 30
    • 0017386261 scopus 로고
    • The size and shape of human and bovine antithrombin III
    • Nordenman B, Nyström C, Björk I. The size and shape of human and bovine antithrombin III. Eur J Biochem 1977; 78: 195-203.
    • (1977) Eur. J. Biochem. , vol.78 , pp. 195-203
    • Nordenman, B.1    Nyström, C.2    Björk, I.3
  • 31
    • 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 PE, Day DE, Verhamme IM, et al. 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 1996; 271: 1072-80.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1072-1080
    • Bock, P.E.1    Day, D.E.2    Verhamme, I.M.3
  • 32
    • 33845554295 scopus 로고
    • p-Guanidinobenzoic acid esters of fluorescein as active-site titrants of serine proteases
    • Melhado LL, Peltz SW, Leytus SP, et al. p Guanidinobenzoic acid esters of fluorescein as active-site titrants of serine proteases. J Am Chem Soc 1982; 104: 7299-306.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7299-7306
    • Melhado, L.L.1    Peltz, S.W.2    Leytus, S.P.3
  • 33
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1987; 166: 368-79.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0033520102 scopus 로고    scopus 로고
    • The role of Arg46 and Arg47 of antithrombin in heparin binding
    • Arocas V, Bock SC, Olson ST, et al. The role of Arg46 and Arg47 of antithrombin in heparin binding. Biochemistry 1999; 38: 10196-204.
    • (1999) Biochemistry , vol.38 , pp. 10196-10204
    • Arocas, V.1    Bock, S.C.2    Olson, S.T.3
  • 36
    • 0020320723 scopus 로고
    • The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin
    • Björk I, Jackson CM, Jörnvall H, et al. The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin. J Biol Chem 1982; 257: 2406-11.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2406-2411
    • Björk, I.1    Jackson, C.M.2    Jörnvall, H.3
  • 37
    • 0020359205 scopus 로고
    • Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin
    • Björk I, Fish WW. Production in vitro and properties of a modified form of bovine antithrombin, cleaved at the active site by thrombin. J Biol Chem 1982; 257: 9487-93.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9487-9493
    • Björk, I.1    Fish, W.W.2
  • 38
    • 0022389299 scopus 로고
    • Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin
    • Olson ST. Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of alpha-thrombin. J Biol Chem 1985; 260: 10153-60.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10153-10160
    • Olson, S.T.1
  • 39
    • 0037729208 scopus 로고    scopus 로고
    • Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols
    • Stürzebecher J, Kopetzki E, Bode W, et al. Dramatic enhancement of the catalytic activity of coagulation factor IXa by alcohols. FEBS Lett 1997; 412: 295-300.
    • (1997) FEBS Lett. , vol.412 , pp. 295-300
    • Stürzebecher, J.1    Kopetzki, E.2    Bode, W.3
  • 40
    • 0035797920 scopus 로고    scopus 로고
    • Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsin
    • Olson ST, Swanson R, Day D, et al. Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsin. Biochemistry 2001; 40: 11742-56.
    • (2001) Biochemistry , vol.40 , pp. 11742-11756
    • Olson, S.T.1    Swanson, R.2    Day, D.3
  • 41
    • 0026687039 scopus 로고
    • Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation
    • Björk I, Ylinenjärvi K, Olson ST, et al. Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation. Biochein J 1992; 286: 793-800.
    • (1992) Biochein. J. , vol.286 , pp. 793-800
    • Björk, I.1    Ylinenjärvi, K.2    Olson, S.T.3
  • 42
    • 0030917184 scopus 로고    scopus 로고
    • The oligosaccharide side chain on Asn-135 of α-antithrombin, absent in β-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change
    • Turk B, Brieditis I, Bock SC, et al. The oligosaccharide side chain on Asn-135 of α-antithrombin, absent in β-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Biochemistry 1997; 36: 6682-91.
    • (1997) Biochemistry , vol.36 , pp. 6682-6691
    • Turk, B.1    Brieditis, I.2    Bock, S.C.3
  • 43
    • 0034705489 scopus 로고    scopus 로고
    • Role of arginine 129 in heparin binding and activation of antithrombin
    • Desai U, Swanson R, Bock SC, et al. Role of arginine 129 in heparin binding and activation of antithrombin. J Biol Chem 2000; 275: 18976-84.
    • (2000) J. Biol. Chem. , vol.275 , pp. 18976-18984
    • Desai, U.1    Swanson, R.2    Bock, S.C.3
  • 44
    • 0027514873 scopus 로고
    • High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: Role for antithrombin in the regulation of kallikrein
    • Olson ST, Sheffer R, Francis AM. High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: Role for antithrombin in the regulation of kallikrein. Biochemistry 1993; 32: 12136-47.
    • (1993) Biochemistry , vol.32 , pp. 12136-12147
    • Olson, S.T.1    Sheffer, R.2    Francis, A.M.3
  • 45
    • 0021843169 scopus 로고
    • Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III
    • Pixley RA, Schapira M, Colman RW. Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III. Blood 1985; 66: 198-203.
    • (1985) Blood , vol.66 , pp. 198-203
    • Pixley, R.A.1    Schapira, M.2    Colman, R.W.3
  • 46
    • 0032479424 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin factor Xa reaction by a template mechanism - Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa
    • Rezaie AR. Calcium enhances heparin catalysis of the antithrombin factor Xa reaction by a template mechanism - Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa. J Biol Chem 1998; 273: 16824-7.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16824-16827
    • Rezaie, A.R.1
  • 47
    • 0034601781 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies
    • Rezaie AR, Olson ST. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies. Biochemistry 2000; 39: 12083-90.
    • (2000) Biochemistry , vol.39 , pp. 12083-12090
    • Rezaie, A.R.1    Olson, S.T.2
  • 48
    • 0025925360 scopus 로고
    • Characterization of factor VII association with tissue factor in solution. High and low affinity calcium binding sites in factor VII contribute to functionally distinct interactions
    • Ruf W, Kalnik MW, Lund-Hansen T, et al. Characterization of factor VII association with tissue factor in solution. High and low affinity calcium binding sites in factor VII contribute to functionally distinct interactions. J Biol Chem 1991; 266: 15719-25.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15719-15725
    • Ruf, W.1    Kalnik, M.W.2    Lund-Hansen, T.3
  • 49
    • 0030035480 scopus 로고    scopus 로고
    • Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin
    • Lormeau JC, Herault JP, Herbert JM. Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin. Thromb Haemost 1996; 76: 5-8.
    • (1996) Thromb. Haemost. , vol.76 , pp. 5-8
    • Lormeau, J.C.1    Herault, J.P.2    Herbert, J.M.3
  • 50
    • 0032571333 scopus 로고    scopus 로고
    • Mechanism of heparin activation of antithrombin - Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin
    • Desai UR, Petitou M, Björk I, et al. Mechanism of heparin activation of antithrombin - Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin. J Biol Chem 1998; 273: 7478-87.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7478-7487
    • Desai, U.R.1    Petitou, M.2    Björk, I.3
  • 51
    • 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, Söderstrom 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 1981; 193: 395-400.
    • (1981) Biochem. J. , vol.193 , pp. 395-400
    • Holmer, E.1    Kurachi, K.2    Söderstrom, G.3
  • 52
    • 0032553436 scopus 로고    scopus 로고
    • Characterization of a heparin binding site on the heavy chain of factor XI
    • Zhao MM, Abdel-Razek T, Sun MF, et al. Characterization of a heparin binding site on the heavy chain of factor XI. J Biol Chem 1998; 273: 31153-9.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31153-31159
    • Zhao, M.M.1    Abdel-Razek, T.2    Sun, M.F.3
  • 53
    • 0035954370 scopus 로고    scopus 로고
    • Localization of a heparin binding site in the catalytic domain of factor XIa
    • Badellino KO, Walsh PN. Localization of a heparin binding site in the catalytic domain of factor XIa. Biochemistry 2001; 40: 7569-80.
    • (2001) Biochemistry , vol.40 , pp. 7569-7580
    • Badellino, K.O.1    Walsh, P.N.2
  • 54
    • 0024370972 scopus 로고
    • Factors influencing the acceleration of human factor XIa inactivation by antithrombin III
    • Scott CF, Colman RW. Factors influencing the acceleration of human factor XIa inactivation by antithrombin III. Blood 1989; 73: 1873-9.
    • (1989) Blood , vol.73 , pp. 1873-1879
    • Scott, C.F.1    Colman, R.W.2
  • 55
    • 15844367087 scopus 로고    scopus 로고
    • Modulation of contact system proteases by glycosaminoglycans - Selective enhancement of the inhibition of factor XIa
    • Wuillemin WA, Eldering E, Citarella F, et al. Modulation of contact system proteases by glycosaminoglycans - Selective enhancement of the inhibition of factor XIa. J Biol Chem 1996; 271: 12913-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12913-12918
    • Wuillemin, W.A.1    Eldering, E.2    Citarella, F.3
  • 56
    • 0347695991 scopus 로고    scopus 로고
    • Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin
    • Izaguirre G, Zhang W, Swanson R, et al. Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin. J Biol Chem 2003; 278: 51433-40.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51433-51440
    • Izaguirre, G.1    Zhang, W.2    Swanson, R.3
  • 57
    • 0026691354 scopus 로고
    • Ratios of anti-factor Xa to antithrombin activities of heparins as determined in recalcified human plasma
    • Schoen P, Lindhout T, Hemker HC. Ratios of anti-factor Xa to antithrombin activities of heparins as determined in recalcified human plasma. Br J Haematol 1992; 81: 255-62.
    • (1992) Br. J. Haematol. , vol.81 , pp. 255-262
    • Schoen, P.1    Lindhout, T.2    Hemker, H.C.3
  • 58
    • 0028898786 scopus 로고
    • Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement
    • Streusand VJ, Björk I, Gettins PGW, et al. Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement. J Biol Chem 1995; 270: 9043-51.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9043-9051
    • Streusand, V.J.1    Björk, I.2    Gettins, P.G.W.3


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