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Volumn 10, Issue 1, 2004, Pages 33-39

The GPIbα-thrombin interaction: Far from crystal clear

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN IB; GLYCOPROTEIN IB ALPHA; GLYCOPROTEIN V; PROTEIN SUBUNIT; THROMBIN; THROMBIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 0742287058     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2003.11.009     Document Type: Review
Times cited : (32)

References (63)
  • 1
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal-structure of human α-thrombin- interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W., et al. The refined 1.9 Å crystal-structure of human α-thrombin-interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 8:1989;3467-3475.
    • (1989) EMBO J. , vol.8 , pp. 3467-3475
    • Bode, W.1
  • 2
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal-structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin - Structure-analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function-relationships
    • Bode W., et al. The refined 1.9-Å X-ray crystal-structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin - structure-analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function-relationships. Protein Sci. 1:1992;426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1
  • 3
    • 0034925134 scopus 로고    scopus 로고
    • Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation
    • Esmon C.T. Protein C anticoagulant pathway and its role in controlling microvascular thrombosis and inflammation. Crit. Care Med. 29:2001;S48-S51.
    • (2001) Crit. Care Med. , vol.29
    • Esmon, C.T.1
  • 4
    • 0033559805 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin
    • Kahn M.L., et al. Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin. J. Clin. Invest. 103:1999;879-887.
    • (1999) J. Clin. Invest. , vol.103 , pp. 879-887
    • Kahn, M.L.1
  • 5
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu T.K., et al. Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell. 64:1991;1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1
  • 6
    • 0017156040 scopus 로고
    • Platelet glycocalicin - Single receptor for platelet-aggregation induced by thrombin or ristocetin
    • Okumura T., et al. Platelet glycocalicin - single receptor for platelet-aggregation induced by thrombin or ristocetin. Thromb. Res. 8:1976;701-706.
    • (1976) Thromb. Res. , vol.8 , pp. 701-706
    • Okumura, T.1
  • 7
    • 0018190052 scopus 로고
    • Platelet glycocalicin - Interaction with thrombin and role as thrombin receptor of platelet surface
    • Okumura T., et al. Platelet glycocalicin - interaction with thrombin and role as thrombin receptor of platelet surface. J. Biol. Chem. 253:1978;3435-3443.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3435-3443
    • Okumura, T.1
  • 8
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin S.R. Thrombin signalling and protease-activated receptors. Nature. 407:2000;258-264.
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 9
    • 0032499696 scopus 로고    scopus 로고
    • Cloning and characterization of human protease-activated receptor 4
    • Xu W.F., et al. Cloning and characterization of human protease-activated receptor 4. Proc. Natl. Acad. Sci. U. S. A. 95:1998;6642-6646.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6642-6646
    • Xu, W.F.1
  • 10
    • 0034923236 scopus 로고    scopus 로고
    • The vascular biology of the glycoprotein Ib-IX-V complex
    • Berndt M.C., et al. The vascular biology of the glycoprotein Ib-IX-V complex. Thromb. Haemost. 86:2001;178-188.
    • (2001) Thromb. Haemost. , vol.86 , pp. 178-188
    • Berndt, M.C.1
  • 11
    • 0022376248 scopus 로고
    • Purification and preliminary characterization of the glycoprotein Ib complex in the human-platelet membrane
    • Berndt M.C., et al. Purification and preliminary characterization of the glycoprotein Ib complex in the human-platelet membrane. Eur. J. Biochem. 151:1985;637-649.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 637-649
    • Berndt, M.C.1
  • 12
    • 0026580102 scopus 로고
    • Glycoprotein-V and glycoprotein-Ib-IX form a noncovalent complex in the platelet membrane
    • Modderman P.W., et al. Glycoprotein-V and glycoprotein-Ib-IX form a noncovalent complex in the platelet membrane. J. Biol. Chem. 267:1992;364-369.
    • (1992) J. Biol. Chem. , vol.267 , pp. 364-369
    • Modderman, P.W.1
  • 13
    • 0037127251 scopus 로고    scopus 로고
    • Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin
    • Baglia F.A., et al. Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin. J. Biol. Chem. 277:2002;1662-1668.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1662-1668
    • Baglia, F.A.1
  • 14
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibα as a binding site for von Willebrand factor and α-thrombin
    • Ward C.M., et al. Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibα as a binding site for von Willebrand factor and α-thrombin. Biochemistry. 35:1996;4929-4938.
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1
  • 15
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Ibα and its complex with von Willebrand factor A1 domain
    • Huizinga E.G., et al. Structures of glycoprotein Ibα and its complex with von Willebrand factor A1 domain. Science. 297:2002;1176-1179.
    • (2002) Science , vol.297 , pp. 1176-1179
    • Huizinga, E.G.1
  • 16
    • 0037144544 scopus 로고    scopus 로고
    • Crystal structure of the platelet glycoprotein Ibα N-terminal domain reveals an unmasking mechanism for receptor activation
    • Uff S., et al. Crystal structure of the platelet glycoprotein Ibα N-terminal domain reveals an unmasking mechanism for receptor activation. J. Biol. Chem. 277:2002;35657-35663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35657-35663
    • Uff, S.1
  • 17
    • 0037119606 scopus 로고    scopus 로고
    • Biomedicine. Contact - How platelets touch von willebrand factor
    • Sadler J.E. Biomedicine. Contact - how platelets touch von willebrand factor. Science. 297:2002;1128-1129.
    • (2002) Science , vol.297 , pp. 1128-1129
    • Sadler, J.E.1
  • 18
    • 0019729478 scopus 로고
    • Interaction of thrombin with platelets: Purification of the thrombin substrate
    • Berndt M.C., et al. Interaction of thrombin with platelets: purification of the thrombin substrate. Ann. New York Acad. Sci. 370:1981;87-95.
    • (1981) Ann. New York Acad. Sci. , vol.370 , pp. 87-95
    • Berndt, M.C.1
  • 19
    • 0030960071 scopus 로고    scopus 로고
    • Role of glycoprotein V in the formation of the platelet high-affinity thrombin binding site
    • Dong J.F., et al. Role of glycoprotein V in the formation of the platelet high-affinity thrombin binding site. Blood. 89:1997;4355-4363.
    • (1997) Blood , vol.89 , pp. 4355-4363
    • Dong, J.F.1
  • 20
    • 0020516779 scopus 로고
    • Correlation of thrombin-induced glycoprotein-V hydrolysis and platelet activation
    • McGowan E.B., et al. Correlation of thrombin-induced glycoprotein-V hydrolysis and platelet activation. J. Biol. Chem. 258:1983;11243-11248.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11243-11248
    • McGowan, E.B.1
  • 21
    • 0035852682 scopus 로고    scopus 로고
    • A thrombin receptor function for platelet glycoprotein-Ib-IX unmasked by cleavage of glycoprotein V
    • Ramakrishnan V., et al. A thrombin receptor function for platelet glycoprotein-Ib-IX unmasked by cleavage of glycoprotein V. Proc. Natl. Acad. Sci. U. S. A. 98:2001;1823-1828.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 1823-1828
    • Ramakrishnan, V.1
  • 22
    • 0033539692 scopus 로고    scopus 로고
    • Increased thrombin responsiveness in platelets from mice lacking glycoprotein V
    • Ramakrishnan V., et al. Increased thrombin responsiveness in platelets from mice lacking glycoprotein V. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13336-13341.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13336-13341
    • Ramakrishnan, V.1
  • 23
    • 0017176530 scopus 로고
    • Equilibrium binding of thrombin to platelets
    • Martin B.M., et al. Equilibrium binding of thrombin to platelets. Biochemistry. 15:1976;4886-4893.
    • (1976) Biochemistry , vol.15 , pp. 4886-4893
    • Martin, B.M.1
  • 24
    • 0017643578 scopus 로고
    • Structure-function-relationships in interaction of α thrombin with blood-platelets
    • Workman E.F., et al. Structure-function-relationships in interaction of α thrombin with blood-platelets. J. Biol. Chem. 252:1977;7118-7123.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7118-7123
    • Workman, E.F.1
  • 25
    • 0028181751 scopus 로고
    • Localization and characterization of an α-thrombin-binding site on platelet glycoprotein Ibα
    • De Marco L., et al. Localization and characterization of an α-thrombin-binding site on platelet glycoprotein Ibα J. Biol. Chem. 269:1994;6478-6484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6478-6484
    • De Marco, L.1
  • 26
    • 0022870417 scopus 로고
    • The glycocalicin portion of platelet glycoprotein Ib expresses both high and moderate affinity receptor sites for thrombin. A soluble radioreceptor assay for the interaction of thrombin with platelets
    • Harmon J.T., et al. The glycocalicin portion of platelet glycoprotein Ib expresses both high and moderate affinity receptor sites for thrombin. A soluble radioreceptor assay for the interaction of thrombin with platelets. J. Biol. Chem. 261:1986;13224-13229.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13224-13229
    • Harmon, J.T.1
  • 27
    • 0030960071 scopus 로고    scopus 로고
    • Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site
    • Dong J.F., et al. Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site. Blood. 89:1997;4355-4363.
    • (1997) Blood , vol.89 , pp. 4355-4363
    • Dong, J.F.1
  • 28
    • 0035895962 scopus 로고    scopus 로고
    • Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets
    • De Candia E., et al. Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets. J. Biol. Chem. 276:2001;4692-4698.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4692-4698
    • De Candia, E.1
  • 29
    • 0022924102 scopus 로고
    • Thrombin interactions with platelet membrane-proteins
    • Berndt M.C., et al. Thrombin interactions with platelet membrane-proteins. Ann. New York Acad. Sci. 485:1986;374-386.
    • (1986) Ann. New York Acad. Sci. , vol.485 , pp. 374-386
    • Berndt, M.C.1
  • 30
    • 0017944584 scopus 로고
    • Reduced thrombin binding and aggregation in Bernard-Soulier platelets
    • Jamieson G.A., et al. Reduced thrombin binding and aggregation in Bernard-Soulier platelets. J. Clin. Invest. 61:1978;861-864.
    • (1978) J. Clin. Invest. , vol.61 , pp. 861-864
    • Jamieson, G.A.1
  • 31
    • 0022573085 scopus 로고
    • Modified platelet responses to thrombin - Evidence for two types of receptors or coupling mechanisms
    • McGowan E.B., et al. Modified platelet responses to thrombin - evidence for two types of receptors or coupling mechanisms. J. Biol. Chem. 261:1986;739-746.
    • (1986) J. Biol. Chem. , vol.261 , pp. 739-746
    • McGowan, E.B.1
  • 32
    • 0035877749 scopus 로고    scopus 로고
    • Unique pathway of thrombin-induced platelet aggregation mediated by glycoprotein Ib
    • Soslau G., et al. Unique pathway of thrombin-induced platelet aggregation mediated by glycoprotein Ib. J. Biol. Chem. 276:2001;21173-21183.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21173-21183
    • Soslau, G.1
  • 33
    • 0037294478 scopus 로고    scopus 로고
    • Thrombin-induced conversion of fibrinogen to fibrin results in rapid platelet trapping which is not dependent on platelet activation or GPIb
    • Jarvis G.E., et al. Thrombin-induced conversion of fibrinogen to fibrin results in rapid platelet trapping which is not dependent on platelet activation or GPIb. Br. J. Pharmacol. 138:2003;574-583.
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 574-583
    • Jarvis, G.E.1
  • 34
    • 0037616282 scopus 로고    scopus 로고
    • Thrombin binding to GPIbα induces platelet aggregation and fibrin clot retraction supported by resting αiIbβ3 interaction with polymerized fibrin
    • Dubois C., et al. Thrombin binding to GPIbα induces platelet aggregation and fibrin clot retraction supported by resting αIIbβ3 interaction with polymerized fibrin. Thromb. Haemost. 89:2003;853-865.
    • (2003) Thromb. Haemost. , vol.89 , pp. 853-865
    • Dubois, C.1
  • 35
    • 0038037101 scopus 로고    scopus 로고
    • Glycoprotein Ib-mediated platelet activation - A signalling pathway triggered by thrombin
    • Adam F., et al. Glycoprotein Ib-mediated platelet activation - a signalling pathway triggered by thrombin. Eur. J. Biochem. 270:2003;2959-2970.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2959-2970
    • Adam, F.1
  • 36
    • 0037152190 scopus 로고    scopus 로고
    • Localization of the adhesion receptor glycoprotein Ib-IX-V complex to lipid rafts is required for platelet adhesion and activation
    • Shrimpton C.N., et al. Localization of the adhesion receptor glycoprotein Ib-IX-V complex to lipid rafts is required for platelet adhesion and activation. J. Exp. Med. 196:2002;1057-1066.
    • (2002) J. Exp. Med. , vol.196 , pp. 1057-1066
    • Shrimpton, C.N.1
  • 37
    • 0020634274 scopus 로고
    • Thrombin receptors define responsiveness of cholesterol-modified platelets
    • Tandon N., et al. Thrombin receptors define responsiveness of cholesterol-modified platelets. J. Biol. Chem. 258:1983;11840-11845.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11840-11845
    • Tandon, N.1
  • 38
    • 0035907373 scopus 로고    scopus 로고
    • Regulation of von Willebrand factor finding to the platelet glycoprotein Ib-IX by a membrane skeleton-dependent inside-out signal
    • Englund G.D., et al. Regulation of von Willebrand factor finding to the platelet glycoprotein Ib-IX by a membrane skeleton-dependent inside-out signal. J. Biol. Chem. 276:2001;16952-16959.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16952-16959
    • Englund, G.D.1
  • 39
    • 0028181314 scopus 로고
    • High-affinity α-thrombin binding to platelet glycoprotein-Ib- α - Identification of two binding domains
    • Gralnick H.R., et al. High-affinity α-thrombin binding to platelet glycoprotein-Ib-α - identification of two binding domains. Proc. Natl. Acad. Sci. U. S. A. 91:1994;6334-6338.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 6334-6338
    • Gralnick, H.R.1
  • 40
    • 0028940892 scopus 로고
    • Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in von Willebrand factor and α-thrombin binding
    • Marchese P., et al. Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in von Willebrand factor and α-thrombin binding. J. Biol. Chem. 270:1995;9571-9578.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9571-9578
    • Marchese, P.1
  • 41
    • 0028029520 scopus 로고
    • Tyrosine sulfation of the glycoprotein Ib-IX complex - Identification of sulfated residues and effect on ligand-binding
    • Dong J.F., et al. Tyrosine sulfation of the glycoprotein Ib-IX complex - identification of sulfated residues and effect on ligand-binding. Biochemistry. 33:1994;13946-13953.
    • (1994) Biochemistry , vol.33 , pp. 13946-13953
    • Dong, J.F.1
  • 42
    • 0025329390 scopus 로고
    • The structure of a complex of recombinant hirudin and human α-thrombin
    • Rydel T.J., et al. The structure of a complex of recombinant hirudin and human α-thrombin. Science. 249:1990;277-280.
    • (1990) Science , vol.249 , pp. 277-280
    • Rydel, T.J.1
  • 43
    • 0027137420 scopus 로고
    • Understanding thrombin and hemostasis
    • Fenton J.W., et al. Understanding thrombin and hemostasis. Hematol. Oncol. Clin. North Am. 7:1993;1107-1119.
    • (1993) Hematol. Oncol. Clin. North Am. , vol.7 , pp. 1107-1119
    • Fenton, J.W.1
  • 44
    • 0035077402 scopus 로고    scopus 로고
    • The amino acid sequence in fibrin responsible for high affinity thrombin binding
    • Meh D.A., et al. The amino acid sequence in fibrin responsible for high affinity thrombin binding. Thromb. Haemost. 85:2001;470-474.
    • (2001) Thromb. Haemost. , vol.85 , pp. 470-474
    • Meh, D.A.1
  • 45
    • 0041344493 scopus 로고    scopus 로고
    • The interaction of the 268-282 region of GPIb-α with the heparin binding site of thrombin inhibits the enzyme activation of factor VIII
    • De Cristofaro R., et al. The interaction of the 268-282 region of GPIb-α with the heparin binding site of thrombin inhibits the enzyme activation of factor VIII. Biochem. J. 373:2003;593-601.
    • (2003) Biochem. J. , vol.373 , pp. 593-601
    • De Cristofaro, R.1
  • 46
    • 0025314996 scopus 로고
    • Conversion of recombinant hirudin to the natural form by in vitro tyrosine sulfation - Differential substrate specificities of leech and bovine tyrosylprotein sulfotransferases
    • Niehrs C., et al. Conversion of recombinant hirudin to the natural form by in vitro tyrosine sulfation - differential substrate specificities of leech and bovine tyrosylprotein sulfotransferases. J. Biol. Chem. 265:1990;9314-9318.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9314-9318
    • Niehrs, C.1
  • 47
    • 0028231924 scopus 로고
    • Posttranslational sulfation of factor-V is required for efficient thrombin cleavage and activation and for full procoagulant activity
    • Pittman D.D., et al. Posttranslational sulfation of factor-V is required for efficient thrombin cleavage and activation and for full procoagulant activity. Biochemistry. 33:1994;6952-6959.
    • (1994) Biochemistry , vol.33 , pp. 6952-6959
    • Pittman, D.D.1
  • 48
    • 0025181730 scopus 로고
    • Localization of von Willebrand factor and thrombin-interactive domains on human platelet glycoprotein Ib
    • Katagiri Y., et al. Localization of von Willebrand factor and thrombin-interactive domains on human platelet glycoprotein Ib. Thromb. Haemost. 63:1990;122-126.
    • (1990) Thromb. Haemost. , vol.63 , pp. 122-126
    • Katagiri, Y.1
  • 49
    • 0021320067 scopus 로고
    • Inhibition of the thrombin-platelet reaction by hirudin
    • Hoffmann A., et al. Inhibition of the thrombin-platelet reaction by hirudin. Haemostasis. 14:1984;164-169.
    • (1984) Haemostasis , vol.14 , pp. 164-169
    • Hoffmann, A.1
  • 50
    • 0025859659 scopus 로고
    • Effect of the hirudin carboxy-terminal peptide-54-65 on the interaction of thrombin with platelets
    • Jandrot-Perrus M., et al. Effect of the hirudin carboxy-terminal peptide-54-65 on the interaction of thrombin with platelets. Thromb. Haemost. 66:1991;300-305.
    • (1991) Thromb. Haemost. , vol.66 , pp. 300-305
    • Jandrot-Perrus, M.1
  • 51
    • 0023949896 scopus 로고
    • Cross-linking of α-thrombin and γ-thrombin to distinct binding-sites on human-platelets
    • Jandrot-Perrus M., et al. Cross-linking of α-thrombin and γ-thrombin to distinct binding-sites on human-platelets. Eur. J. Biochem. 174:1988;359-367.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 359-367
    • Jandrot-Perrus, M.1
  • 52
    • 0031825436 scopus 로고    scopus 로고
    • Bouton, M.C. et al. (1998) Characteristics of the interaction between thrombin exosite 1 and the sequence 269-287 [correction of 269-297] of platelet glycoprotein Ibα. Thromb. Haemost. 80, 310-315.
    • Bouton, M.C. et al. (1998) Characteristics of the interaction between thrombin exosite 1 and the sequence 269-287 [correction of 269-297] of platelet glycoprotein Ibα. Thromb. Haemost. 80, 310-315.
  • 53
    • 0026458485 scopus 로고
    • Thrombin interaction with platelet glycoprotein-Ib - Effect of glycocalicin on thrombin specificity
    • Jandrot-Perrus M., et al. Thrombin interaction with platelet glycoprotein-Ib - effect of glycocalicin on thrombin specificity. Blood. 80:1992;2781-2786.
    • (1992) Blood , vol.80 , pp. 2781-2786
    • Jandrot-Perrus, M.1
  • 54
    • 0035818425 scopus 로고    scopus 로고
    • Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib
    • De Cristofaro R., et al. Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib. Biochemistry. 40:2001;13268-13273.
    • (2001) Biochemistry , vol.40 , pp. 13268-13273
    • De Cristofaro, R.1
  • 55
    • 0035794133 scopus 로고    scopus 로고
    • Platelet glycoprotein Ibα binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin
    • Li C.Q., et al. Platelet glycoprotein Ibα binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin. J. Biol. Chem. 276:2001;6161-6168.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6161-6168
    • Li, C.Q.1
  • 56
    • 0346850827 scopus 로고    scopus 로고
    • in activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ibα with thrombin anion binding exosites I and II, respectively. J. Biol. Chem. 10.1074/jbc.M306925200 (
    • Yun, T.H. et al. (2003) Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ibα with thrombin anion binding exosites I and II, respectively. J. Biol. Chem. 10.1074/jbc.M306925200 ( www.jbc.org/ ).
  • 57
    • 0030934108 scopus 로고    scopus 로고
    • Thrombin interaction with platelet GPIb: Role of the heparin binding domain
    • De Candia E., et al. Thrombin interaction with platelet GPIb: role of the heparin binding domain. Thromb. Haemost. 77:1997;735-740.
    • (1997) Thromb. Haemost. , vol.77 , pp. 735-740
    • De Candia, E.1
  • 58
    • 0032526259 scopus 로고    scopus 로고
    • Binding of human α-thrombin to platelet GPIb: Energetics and functional effects
    • De Cristofaro R., et al. Binding of human α-thrombin to platelet GPIb: energetics and functional effects. Biochem. J. 332:1998;643-650.
    • (1998) Biochem. J. , vol.332 , pp. 643-650
    • De Cristofaro, R.1
  • 59
    • 0037815126 scopus 로고    scopus 로고
    • Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα
    • Celikel R., et al. Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα Science. 301:2003;218-221.
    • (2003) Science , vol.301 , pp. 218-221
    • Celikel, R.1
  • 60
    • 0038157329 scopus 로고    scopus 로고
    • Crystal structure of the GPIbα-thrombin complex essential for platelet aggregation
    • Dumas J.J., et al. Crystal structure of the GPIbα-thrombin complex essential for platelet aggregation. Science. 301:2003;222-226.
    • (2003) Science , vol.301 , pp. 222-226
    • Dumas, J.J.1
  • 61
    • 0037477607 scopus 로고    scopus 로고
    • A ménage à trois in two configurations
    • Sadler J.E. A ménage à trois in two configurations. Science. 301:2003;177-179.
    • (2003) Science , vol.301 , pp. 177-179
    • Sadler, J.E.1
  • 62
    • 0026244229 scopus 로고
    • Molscript - A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. Molscript - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 63
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E.A., et al. Raster3D: photorealistic molecular graphics. Macromol. Crystallog. 277:1997;505-524.
    • (1997) Macromol. Crystallog. , vol.277 , pp. 505-524
    • Merritt, E.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.