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Volumn 82, Issue 2, 1999, Pages 357-364

The glycoprotein Ib-IX-V complex in platelet adhesion and signaling

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; GLYCOPROTEIN; MEMBRANE PROTEIN; PADGEM PROTEIN; THROMBIN; THROMBOCYTE RECEPTOR; VON WILLEBRAND FACTOR;

EID: 0032722464     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615854     Document Type: Conference Paper
Times cited : (117)

References (66)
  • 2
    • 0028274014 scopus 로고
    • The platelet glycoprotein Ib-IX complex
    • López JA. The platelet glycoprotein Ib-IX complex. Blood Coagul Fibrinolysis. 1994;5:97-119.
    • (1994) Blood Coagul Fibrinolysis , vol.5 , pp. 97-119
    • López, J.A.1
  • 4
    • 0029086650 scopus 로고
    • Flow-related platelet deposition on subendothelium
    • Weiss HJ. Flow-related platelet deposition on subendothelium. Thromb Haemostas. 1995;74:117-122.
    • (1995) Thromb Haemostas , vol.74 , pp. 117-122
    • Weiss, H.J.1
  • 6
    • 0032102098 scopus 로고    scopus 로고
    • Collagen receptor signaling in platelets: Extending the role of the ITAM
    • Watson SP, Gibbins J. Collagen receptor signaling in platelets: extending the role of the ITAM. Immunol Today. 1998;19:260-264.
    • (1998) Immunol Today , vol.19 , pp. 260-264
    • Watson, S.P.1    Gibbins, J.2
  • 7
    • 0029862473 scopus 로고    scopus 로고
    • Snake venom proteins modulating the interaction between Von Willebrand factor and platelet glycoprotein Ib
    • Fujimura Y, Kawasaki T, Titani K. Snake venom proteins modulating the interaction between von Willebrand factor and platelet glycoprotein Ib. Thromb Haemostas. 1997;76:633-639.
    • (1997) Thromb Haemostas , vol.76 , pp. 633-639
    • Fujimura, Y.1    Kawasaki, T.2    Titani, K.3
  • 8
    • 0030748125 scopus 로고    scopus 로고
    • Mechanisms initiating platelet thrombus formation
    • Ruggeri ZM. Mechanisms initiating platelet thrombus formation. Thromb Haemostas. 1997;78:611-616.
    • (1997) Thromb Haemostas , vol.78 , pp. 611-616
    • Ruggeri, Z.M.1
  • 9
    • 0031819681 scopus 로고    scopus 로고
    • Adhesion-dependent signaling and the initiation of haemostasis and thrombosis
    • Andrews RK, Berndt MC. Adhesion-dependent signaling and the initiation of haemostasis and thrombosis. Histol Histopath. 1998;13:837-844.
    • (1998) Histol Histopath , vol.13 , pp. 837-844
    • Andrews, R.K.1    Berndt, M.C.2
  • 10
    • 0009467123 scopus 로고    scopus 로고
    • Berndt MC, ed. Berndt MC (ed). Reading, PA: Harwood Academic Publishers. Reading In press
    • Fox JEB, Meyer SC. In: Berndt MC, ed. Platelets, Thrombosis and the Vessel Wall. Berndt MC (ed). Reading, PA: Harwood Academic Publishers. Reading In press.
    • Platelets, Thrombosis and the Vessel Wall
    • Fox, J.E.B.1    Meyer, S.C.2
  • 12
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on Von Willebrand factor
    • Savage B, Salvidar E, Ruggeri ZM. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell 1996;84:289-297.
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Salvidar, E.2    Ruggeri, Z.M.3
  • 13
    • 0032483550 scopus 로고    scopus 로고
    • Synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow
    • Savage B, Almus-Jacobs F, Ruggeri ZM. Synergy of multiple substrate-receptor interactions in platelet thrombus formation under flow. Cell. 1998;94:657-666.
    • (1998) Cell , vol.94 , pp. 657-666
    • Savage, B.1    Almus-Jacobs, F.2    Ruggeri, Z.M.3
  • 14
    • 0032518555 scopus 로고    scopus 로고
    • Distinct mechanisms of platelet aggregation as a consequence of different shearing flow conditions
    • Goto S, Ikeda Y, Salvidar E, Ruggeri ZM. Distinct mechanisms of platelet aggregation as a consequence of different shearing flow conditions. J Clin Invest. 1998;101:479-486.
    • (1998) J Clin Invest , vol.101 , pp. 479-486
    • Goto, S.1    Ikeda, Y.2    Salvidar, E.3    Ruggeri, Z.M.4
  • 15
    • 0032533592 scopus 로고    scopus 로고
    • Shear-dependent rolling on Von Willebrand factor of mammalian cells expressing the platelet glycoprotein Ib-IX-V complex
    • Fredrickson BJ, Dong J-F, McIntire LV, López JA. Shear-dependent rolling on von Willebrand factor of mammalian cells expressing the platelet glycoprotein Ib-IX-V complex. Blood. 1998;92:3684-3693.
    • (1998) Blood , vol.92 , pp. 3684-3693
    • Fredrickson, B.J.1    Dong, J.-F.2    McIntire, L.V.3    López, J.A.4
  • 16
    • 0029963871 scopus 로고    scopus 로고
    • Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet Von Willebrand factor receptor glycoprotein Ibα. Binding site for Von Willebrand factor and α-thrombin
    • Ward CM, Andrews RK, Smith AI, Berndt MC. Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibα. Binding site for von Willebrand factor and α-thrombin. Biochemistry. 1996;35:4929-4938.
    • (1996) Biochemistry , vol.35 , pp. 4929-4938
    • Ward, C.M.1    Andrews, R.K.2    Smith, A.I.3    Berndt, M.C.4
  • 17
    • 0028029520 scopus 로고
    • Tyrosine sulfation of the glycoprotein Ib-IX complex: Identification of sulfated residues and effect on ligand binding
    • Dong J-F, Li CQ, López JA. Tyrosine sulfation of the glycoprotein Ib-IX complex: Identification of sulfated residues and effect on ligand binding. Biochemistry. 1994;33:13946-13953.
    • (1994) Biochemistry , vol.33 , pp. 13946-13953
    • Dong, J.-F.1    Li, C.Q.2    López, J.A.3
  • 18
    • 0028940892 scopus 로고
    • Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in Von Willebrand factor and α-thrombin binding
    • Marchese P, Murata M, Mazzucato M, Pradella P, De Marco L, Ware J, Ruggeri ZM. Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in von Willebrand factor and α-thrombin binding. J Biol Chem. 1995;270:9571-9578.
    • (1995) J Biol Chem , vol.270 , pp. 9571-9578
    • Marchese, P.1    Murata, M.2    Mazzucato, M.3    Pradella, P.4    De Marco, L.5    Ware, J.6    Ruggeri, Z.M.7
  • 20
    • 0032553548 scopus 로고    scopus 로고
    • Synthesis, assembly, and intracellular transport of the platelet glycoprotein Ib-IX-V complex
    • Dong J-F, Gao S, López JA. Synthesis, assembly, and intracellular transport of the platelet glycoprotein Ib-IX-V complex. J Biol Chem. 1998;273,31449-31454.
    • (1998) J Biol Chem , vol.273 , pp. 31449-31454
    • Dong, J.-F.1    Gao, S.2    López, J.A.3
  • 21
    • 0032579407 scopus 로고    scopus 로고
    • Role of actin-binding protein in insertion of adhesion receptors into the membrane
    • Meyer SC, Sanan DA, Fox JEB. Role of actin-binding protein in insertion of adhesion receptors into the membrane. J Biol Chem. 1998;273:3013-3020.
    • (1998) J Biol Chem , vol.273 , pp. 3013-3020
    • Meyer, S.C.1    Sanan, D.A.2    Fox, J.E.B.3
  • 23
    • 0030901560 scopus 로고    scopus 로고
    • Missense mutations of the glycoprotein (GP) Ibβ gene impairing the GPIb α/β disulfide linkage in a family with giant platelet disorder
    • 1997
    • Kunishima S, López JA, Kobayashi S, Imai N, Kamiya T, Saito H, Naoe T. Missense mutations of the glycoprotein (GP) Ibβ gene impairing the GPIb α/β disulfide linkage in a family with giant platelet disorder. Blood. 1997;89:2404-2412,1997.
    • (1997) Blood , vol.89 , pp. 2404-2412
    • Kunishima, S.1    López, J.A.2    Kobayashi, S.3    Imai, N.4    Kamiya, T.5    Saito, H.6    Naoe, T.7
  • 24
    • 0029951698 scopus 로고    scopus 로고
    • Platelet-type Von Willebrand disease
    • Miller JL. Platelet-type von Willebrand disease. Thromb Haemostas. 1996;75:865-869.
    • (1996) Thromb Haemostas , vol.75 , pp. 865-869
    • Miller, J.L.1
  • 25
    • 0025777192 scopus 로고
    • Site-directed mutagenesis of a soluble recombinant fragment of platelet glycoprotein Ibα demonstrating negatively charged residues involved in Von Willebrand factor binding
    • Murata M, Ware J, Ruggeri ZM. Site-directed mutagenesis of a soluble recombinant fragment of platelet glycoprotein Ibα demonstrating negatively charged residues involved in von Willebrand factor binding. J Biol Chem. 1990;266:15474-15480.
    • (1990) J Biol Chem , vol.266 , pp. 15474-15480
    • Murata, M.1    Ware, J.2    Ruggeri, Z.M.3
  • 26
    • 4243963717 scopus 로고    scopus 로고
    • Identification of monoclonal antibody epitopes and the ristocetin-dependent binding site on the α-chain of the platelet GP Ib-IX-V complex using canine-human chimaeras
    • Berndt MC, Shen Y, Romo G, Kenny DA, López JA, Andrews RK. Identification of monoclonal antibody epitopes and the ristocetin-dependent binding site on the α-chain of the platelet GP Ib-IX-V complex using canine-human chimaeras. Blood. 1998;92:703a.
    • (1998) Blood , vol.92
    • Berndt, M.C.1    Shen, Y.2    Romo, G.3    Kenny, D.A.4    López, J.A.5    Andrews, R.K.6
  • 27
    • 0031893823 scopus 로고    scopus 로고
    • Characterization of the initial α-thrombin interaction with glycoprotein Ibα in relation to platelet activation
    • Mazzucato M, De Marco L, Masotti A, Pradella P, Bahou WF, Ruggeri ZM. Characterization of the initial α-thrombin interaction with glycoprotein Ibα in relation to platelet activation. J Biol Chem. 1998;273:1880-1887.
    • (1998) J Biol Chem , vol.273 , pp. 1880-1887
    • Mazzucato, M.1    De Marco, L.2    Masotti, A.3    Pradella, P.4    Bahou, W.F.5    Ruggeri, Z.M.6
  • 28
    • 0030960071 scopus 로고    scopus 로고
    • Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site
    • Dong J-F, Sae-Tung G, López JA. Role of glycoprotein V in the formation of the platelet high-affinity thrombin-binding site. Blood. 1997;89:4355-4363.
    • (1997) Blood , vol.89 , pp. 4355-4363
    • Dong, J.-F.1    Sae-Tung, G.2    López, J.A.3
  • 31
    • 0026723481 scopus 로고
    • Characterization of three alboaggregins purified from Trimeresurus albolabris venom
    • Peng M, Lu W, Kirby EP. Characterization of three alboaggregins purified from Trimeresurus albolabris venom. Thromb Haemostas. 1992;67:702-707.
    • (1992) Thromb Haemostas , vol.67 , pp. 702-707
    • Peng, M.1    Lu, W.2    Kirby, E.P.3
  • 32
    • 0029816492 scopus 로고    scopus 로고
    • Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet activation
    • Andrews RK, Kroll MH, Ward CM, Rose JW, Scarborough RM, Smith AI, López JA, Berndt MC. Binding of a novel 50-kilodalton alboaggregin from Trimeresurus albolabris and related viper venom proteins to the platelet membrane glycoprotein Ib-IX-V complex. Effect on platelet aggregation and glycoprotein Ib-mediated platelet activation. Biochemistry. 1996;35:12629-12639.
    • (1996) Biochemistry , vol.35 , pp. 12629-12639
    • Andrews, R.K.1    Kroll, M.H.2    Ward, C.M.3    Rose, J.W.4    Scarborough, R.M.5    Smith, A.I.6    López, J.A.7    Berndt, M.C.8
  • 34
    • 0031787654 scopus 로고    scopus 로고
    • Purification and characterization of kaouthiagin, a Von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom
    • Hamako J, Matsui T, Nishida S, Nomura S, Fujimura Y, Ito M, Ozeki Y, Titani K. Purification and characterization of kaouthiagin, a von Willebrand factor-binding and -cleaving metalloproteinase from Naja kaouthia cobra venom. Thromb Haemostas. 1998;80:499-505.
    • (1998) Thromb Haemostas , vol.80 , pp. 499-505
    • Hamako, J.1    Matsui, T.2    Nishida, S.3    Nomura, S.4    Fujimura, Y.5    Ito, M.6    Ozeki, Y.7    Titani, K.8
  • 35
    • 0029119149 scopus 로고
    • Platelets roll on stimulated endothelium in vivo: An interaction mediated by endothelial P-selectin
    • Frenette PS, Johnson RC, Hynes RO, Wagner DD. Platelets roll on stimulated endothelium in vivo: an interaction mediated by endothelial P-selectin. Proc Natl Acad Sci USA. 1995;92:7450-7454.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7450-7454
    • Frenette, P.S.1    Johnson, R.C.2    Hynes, R.O.3    Wagner, D.D.4
  • 38
    • 0028970042 scopus 로고
    • Cell biology of atherosclerosis
    • Ross R. Cell biology of atherosclerosis. Ann Rev Physiol. 1995;57:791-804.
    • (1995) Ann Rev Physiol , vol.57 , pp. 791-804
    • Ross, R.1
  • 39
    • 0029926254 scopus 로고    scopus 로고
    • Platelet-dependent primary haemostasis promotes selectin- and integrin-mediated neutrophil adhesion to damaged endothelium under flow conditions
    • Kuijper PHM, Torres G, van der Linden JAM, Lammers J-WJ, Sixma JJ, Koenderman L, Zwaginga JJ. Platelet-dependent primary haemostasis promotes selectin- and integrin-mediated neutrophil adhesion to damaged endothelium under flow conditions. Blood. 1996;87:3271-3281.
    • (1996) Blood , vol.87 , pp. 3271-3281
    • Kuijper, P.H.M.1    Torres, G.2    Van Der Linden, J.A.M.3    Lammers, J.-W.J.4    Sixma, J.J.5    Koenderman, L.6    Zwaginga, J.J.7
  • 40
    • 0028935791 scopus 로고
    • Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration
    • Springer TA. Traffic signals on endothelium for lymphocyte recirculation and leukocyte emigration. Ann Rev Physiol. 1995;57:827-872.
    • (1995) Ann Rev Physiol , vol.57 , pp. 827-872
    • Springer, T.A.1
  • 42
    • 0028885684 scopus 로고
    • A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding
    • Sako D, Comess KM, Barone KM, Camphausen RT, Cumming DA, Shaw GD. A sulfated peptide segment at the amino terminus of PSGL-1 is critical for P-selectin binding. Cell. 1995;83:323-331.
    • (1995) Cell , vol.83 , pp. 323-331
    • Sako, D.1    Comess, K.M.2    Barone, K.M.3    Camphausen, R.T.4    Cumming, D.A.5    Shaw, G.D.6
  • 43
    • 0028807440 scopus 로고
    • A novel cobra venom metalloproteinase, mocarhagin, cleaves a ten amino acid peptide from the mature N-terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding
    • De Luca M, Dunlop LC, Andrews RK, Flannery JV, Ettling R, Cumming DA, Veldman GM, Berndt MC. A novel cobra venom metalloproteinase, mocarhagin, cleaves a ten amino acid peptide from the mature N-terminus of P-selectin glycoprotein ligand receptor, PSGL-1, and abolishes P-selectin binding. J Biol Chem. 1995;270:26734-26737.
    • (1995) J Biol Chem , vol.270 , pp. 26734-26737
    • De Luca, M.1    Dunlop, L.C.2    Andrews, R.K.3    Flannery, J.V.4    Ettling, R.5    Cumming, D.A.6    Veldman, G.M.7    Berndt, M.C.8
  • 44
    • 0030294239 scopus 로고    scopus 로고
    • L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: Interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity
    • Tu L, Chen A, Delahunty MD, Moore KL, Watson SR, McEver RP, Tedder TF. L-selectin binds to P-selectin glycoprotein ligand-1 on leukocytes: interactions between the lectin, epidermal growth factor, and consensus repeat domains of the selectins determine ligand binding specificity. J Immunol. 1996;157:3995-4004.
    • (1996) J Immunol , vol.157 , pp. 3995-4004
    • Tu, L.1    Chen, A.2    Delahunty, M.D.3    Moore, K.L.4    Watson, S.R.5    McEver, R.P.6    Tedder, T.F.7
  • 45
    • 0029987391 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ haematopoietic progenitor cells
    • Spertini O, Cordey AS, Monai N, Giuffre L, Schapira M. P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ haematopoietic progenitor cells. J Cell Biol. 1996;135:523-531.
    • (1996) J Cell Biol , vol.135 , pp. 523-531
    • Spertini, O.1    Cordey, A.S.2    Monai, N.3    Giuffre, L.4    Schapira, M.5
  • 46
    • 0029793468 scopus 로고    scopus 로고
    • P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation
    • Guyer DA, Moore KL, Lynam EB, Schammel CM, Rogelj S, McEver RP, Sklar LA. P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation. Blood. 1996;88:2415-2421.
    • (1996) Blood , vol.88 , pp. 2415-2421
    • Guyer, D.A.1    Moore, K.L.2    Lynam, E.B.3    Schammel, C.M.4    Rogelj, S.5    McEver, R.P.6    Sklar, L.A.7
  • 47
    • 0029758146 scopus 로고    scopus 로고
    • Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro
    • Walcheck B, Moore KL, McEver RP, Kishimoto TK. Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro. J Clin Invest. 1996;98:1081-1087.
    • (1996) J Clin Invest , vol.98 , pp. 1081-1087
    • Walcheck, B.1    Moore, K.L.2    McEver, R.P.3    Kishimoto, T.K.4
  • 49
    • 0027291531 scopus 로고
    • Downregulation of human platelet reactivity by neutrophils. Participation of lipoxygenase derivatives and adhesive proteins
    • Valles J, Santos MT, Marcus AJ, Safier LB, Broekman MJ, Islam N, Ullman HL, Aznar J. Downregulation of human platelet reactivity by neutrophils. Participation of lipoxygenase derivatives and adhesive proteins. J Clin Invest. 1993;92:1357-1365.
    • (1993) J Clin Invest , vol.92 , pp. 1357-1365
    • Valles, J.1    Santos, M.T.2    Marcus, A.J.3    Safier, L.B.4    Broekman, M.J.5    Islam, N.6    Ullman, H.L.7    Aznar, J.8
  • 50
    • 0031982997 scopus 로고    scopus 로고
    • Platelet/endothelial cell adhesion molecule-1 serves as a costimulatory agonist receptor that modulates integrin-dependent adhesion and aggregation of human platelets
    • Varon D, Jackson DE, Shenkman B, Dardik R, Tamarin I, Savion N, Newman PJ. Platelet/endothelial cell adhesion molecule-1 serves as a costimulatory agonist receptor that modulates integrin-dependent adhesion and aggregation of human platelets. Blood. 1998;91:500-507.
    • (1998) Blood , vol.91 , pp. 500-507
    • Varon, D.1    Jackson, D.E.2    Shenkman, B.3    Dardik, R.4    Tamarin, I.5    Savion, N.6    Newman, P.J.7
  • 51
    • 0027982055 scopus 로고
    • A functional integrin ligand on the surface of platelets: Intercellular adhesion molecule-2
    • Diacovo TG, deFougerolles AR, Bainton DF, Springer TA. A functional integrin ligand on the surface of platelets: intercellular adhesion molecule-2. J Clin Invest. 1994;94:1243-1251.
    • (1994) J Clin Invest , vol.94 , pp. 1243-1251
    • Diacovo, T.G.1    DeFougerolles, A.R.2    Bainton, D.F.3    Springer, T.A.4
  • 52
    • 0029950954 scopus 로고    scopus 로고
    • The cytoplasmic domain of the α-subunit of glycoprotein (GP) Ib mediates attachment of the entire GP Ib-IX complex to the cytoskeleton and regulates Von Willebrand factor-induced changes in cell morphology
    • Cunningham JG, Meyer SC, Fox JEB. The cytoplasmic domain of the α-subunit of glycoprotein (GP) Ib mediates attachment of the entire GP Ib-IX complex to the cytoskeleton and regulates von Willebrand Factor-induced changes in cell morphology. J Biol Chem. 1996;271:11581-11587.
    • (1996) J Biol Chem , vol.271 , pp. 11581-11587
    • Cunningham, J.G.1    Meyer, S.C.2    Fox, J.E.B.3
  • 53
    • 0026687701 scopus 로고
    • Identification of a region from the cytoplasmic domain of the platelet membrane GP Ib-IX complex that binds to purified actin-binding protein
    • Andrews RK, Fox JEB. Identification of a region from the cytoplasmic domain of the platelet membrane GP Ib-IX complex that binds to purified actin-binding protein. J Biol Chem. 1992;267:18605-18611.
    • (1992) J Biol Chem , vol.267 , pp. 18605-18611
    • Andrews, R.K.1    Fox, J.E.B.2
  • 55
    • 0029922841 scopus 로고    scopus 로고
    • Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα
    • Du X, Fox JE, Pei S. Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ibα. J Biol Chem. 1996;271:7362-7367.
    • (1996) J Biol Chem , vol.271 , pp. 7362-7367
    • Du, X.1    Fox, J.E.2    Pei, S.3
  • 56
    • 0032512413 scopus 로고    scopus 로고
    • Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    • Andrews RK, Harris SJ, McNally T, Berndt MC. Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex. Biochemistry. 1998;37:638-647.
    • (1998) Biochemistry , vol.37 , pp. 638-647
    • Andrews, R.K.1    Harris, S.J.2    McNally, T.3    Berndt, M.C.4
  • 57
    • 0032519507 scopus 로고    scopus 로고
    • Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits GP Ibα and Ibβ
    • Calverly DC, Kavanagh TJ, Roth GJ. Human signaling protein 14-3-3ζ interacts with platelet glycoprotein Ib subunits GP Ibα and Ibβ. Blood. 1998;91:1295-1303.
    • (1998) Blood , vol.91 , pp. 1295-1303
    • Calverly, D.C.1    Kavanagh, T.J.2    Roth, G.J.3
  • 58
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 and its possible role in coordinating multiple signaling pathways
    • Aitken A. 14-3-3 and its possible role in coordinating multiple signaling pathways. Trends Cell Biol. 1996;6:341-347.
    • (1996) Trends Cell Biol , vol.6 , pp. 341-347
    • Aitken, A.1
  • 59
    • 0029871708 scopus 로고    scopus 로고
    • Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
    • Muslin AJ, Tanner JW, Allen PM, Shaw AS. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell. 1996;84:889-897.
    • (1996) Cell , vol.84 , pp. 889-897
    • Muslin, A.J.1    Tanner, J.W.2    Allen, P.M.3    Shaw, A.S.4
  • 61
    • 0030948462 scopus 로고    scopus 로고
    • Serine phosphorylation of cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motif
    • Liu Y-C, Liu Y, Elly C, Yoshida H, Lipkowitz S, Altman A. Serine phosphorylation of cbl induced by phorbol ester enhances its association with 14-3-3 proteins in T cells via a novel serine-rich 14-3-3-binding motif. J Biol Chem. 1997;272:9979-9985.
    • (1997) J Biol Chem , vol.272 , pp. 9979-9985
    • Liu, Y.-C.1    Liu, Y.2    Elly, C.3    Yoshida, H.4    Lipkowitz, S.5    Altman, A.6
  • 62
    • 0030995955 scopus 로고    scopus 로고
    • 14-3-3 (ε) interacts with the insulin-like growth factor 1 receptor substrate 1 in a phosphoserine-dependent manner
    • Craparo A, Freund R, Gustafson TA. 14-3-3 (ε) interacts with the insulin-like growth factor 1 receptor substrate 1 in a phosphoserine-dependent manner. J Biol Chem. 1997;272:11663-11669.
    • (1997) J Biol Chem , vol.272 , pp. 11663-11669
    • Craparo, A.1    Freund, R.2    Gustafson, T.A.3
  • 64
    • 0032509336 scopus 로고    scopus 로고
    • A novel ligand-binding site in the ζ-form 14-3-3 protein recognizing the platelet glycoprotein Ibα and distinct from the c-raf-binding site
    • Gu M, Du X. A novel ligand-binding site in the ζ-form 14-3-3 protein recognizing the platelet glycoprotein Ibα and distinct from the c-raf-binding site. J Biol Chem. 1998;273:33465-33471.
    • (1998) J Biol Chem , vol.273 , pp. 33465-33471
    • Gu, M.1    Du, X.2
  • 65
    • 0027985446 scopus 로고
    • Adhesion receptor activation of phosphatidylinositol 3-kinase: Von Willebrand factor stimulates the cytoskeletal association and activation of phosphatidylinositol 3-kinase and pp60src in human platelets
    • Jackson SP, Schoenwaelder SM, Yan Y, Rabinowitz I, Salem HH, Mitchell CA. Adhesion receptor activation of phosphatidylinositol 3-kinase: von Willebrand factor stimulates the cytoskeletal association and activation of phosphatidylinositol 3-kinase and pp60src in human platelets. J Biol Chem. 1994;269:27093-27099.
    • (1994) J Biol Chem , vol.269 , pp. 27093-27099
    • Jackson, S.P.1    Schoenwaelder, S.M.2    Yan, Y.3    Rabinowitz, I.4    Salem, H.H.5    Mitchell, C.A.6
  • 66
    • 0031454108 scopus 로고    scopus 로고
    • Glycoprotein Ib-Von Willebrand factor interactions activate tyrosine kinases in human platelets
    • Asazuma N, Ozaki Y, Satoh K, Handa M, Fujimura Y, Miura S, Kume S. Glycoprotein Ib-von Willebrand factor interactions activate tyrosine kinases in human platelets. Blood. 1997;90:4789-4798.
    • (1997) Blood , vol.90 , pp. 4789-4798
    • Asazuma, N.1    Ozaki, Y.2    Satoh, K.3    Handa, M.4    Fujimura, Y.5    Miura, S.6    Kume, S.7


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