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Volumn 76, Issue 5, 1996, Pages 640-650

Non-receptor protein tyrosine kinases and phosphatases in human platelets

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CELL SURFACE RECEPTOR; ENZYME; PHOSPHATASE; PROTEIN TYROSINE KINASE;

EID: 0029911291     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1650637     Document Type: Review
Times cited : (66)

References (151)
  • 1
  • 3
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990; 61: 203-12.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 5
    • 0026727212 scopus 로고
    • c-src family of protein-tyrosine kinases: Structure, regulation and function
    • c-src family of protein-tyrosine kinases: Structure, regulation and function. Crit Rev Oncogen 1992; 3: 401-46.
    • (1992) Crit Rev Oncogen , vol.3 , pp. 401-446
    • Brickell, P.M.1
  • 7
    • 0028221289 scopus 로고
    • Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor
    • Vassbotn FS, Havnen OK, Heldin CH, Holmsen H. Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor. J Biol Chem 1994; 269: 13874-9.
    • (1994) J Biol Chem , vol.269 , pp. 13874-13879
    • Vassbotn, F.S.1    Havnen, O.K.2    Heldin, C.H.3    Holmsen, H.4
  • 8
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes
    • Fischer EH, Charbonneau H, Tonks NK. Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes. Science 1991; 253: 401-6.
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charbonneau, H.2    Tonks, N.K.3
  • 9
    • 0028047349 scopus 로고
    • Phosphotyrosine phosphatases with SH2 domains: Regulators of signal transduction
    • Feng G, Pawson T. Phosphotyrosine phosphatases with SH2 domains: regulators of signal transduction. Trends Genet 1994; 10: 54-8.
    • (1994) Trends Genet , vol.10 , pp. 54-58
    • Feng, G.1    Pawson, T.2
  • 10
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • Sun H, Tonks NK. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. TIBS 1994; 19: 480-5.
    • (1994) TIBS , vol.19 , pp. 480-485
    • Sun, H.1    Tonks, N.K.2
  • 12
    • 0344297230 scopus 로고
    • Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets
    • Golden A, Brugge JS. Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets. Proc Natl Acad Sci USA 1989; 86: 901-5.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 901-905
    • Golden, A.1    Brugge, J.S.2
  • 13
    • 3142588838 scopus 로고
    • Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets
    • Ferrell JE, Martin GS. Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets. Proc Natl Acad Sci USA 1989; 86: 2234-38.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2234-2238
    • Ferrell, J.E.1    Martin, G.S.2
  • 15
    • 0024511998 scopus 로고
    • Thrombin and collagen induce rapid phosphorylation of a common set of cellular proteins on tyrosine in human platelets
    • Nakamura S, Yamamura H. Thrombin and collagen induce rapid phosphorylation of a common set of cellular proteins on tyrosine in human platelets. J Biol Chem 1989; 264: 7089-91.
    • (1989) J Biol Chem , vol.264 , pp. 7089-7091
    • Nakamura, S.1    Yamamura, H.2
  • 17
    • 0028060528 scopus 로고
    • Shear-stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s)
    • Razdan K, Hellums JD, Kroll MH. Shear-stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s). Biochem J 1994; 302: 681-6.
    • (1994) Biochem J , vol.302 , pp. 681-686
    • Razdan, K.1    Hellums, J.D.2    Kroll, M.H.3
  • 18
    • 0025925359 scopus 로고
    • c-src, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
    • c-src, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J Biol Chem 1991; 266: 15705-9.
    • (1991) J Biol Chem , vol.266 , pp. 15705-15709
    • Grondin, P.1    Plantavid, M.2    Sultan, C.3    Breton, M.4    Mauco, G.5    Chap, H.6
  • 19
    • 0028951464 scopus 로고
    • Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase
    • Guinebault C, Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H. Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase. J Cell Biol 1995; 129: 831-42.
    • (1995) J Cell Biol , vol.129 , pp. 831-842
    • Guinebault, C.1    Payrastre, B.2    Racaud-Sultan, C.3    Mazarguil, H.4    Breton, M.5    Mauco, G.6    Plantavid, M.7    Chap, H.8
  • 21
    • 0029035974 scopus 로고
    • 3 through cytoskeletal reorganisation and tyrosine phosphorylation in human platelets
    • 3 through cytoskeletal reorganisation and tyrosine phosphorylation in human platelets. J Biol Chem 1995; 270: 11927-34.
    • (1995) J Biol Chem , vol.270 , pp. 11927-11934
    • Ezumi, Y.1    Takayama, H.2    Okuma, M.3
  • 23
    • 0027368466 scopus 로고
    • Vinculin is a major platelet protein that undergoes calcium-dependent tyrosine phosphorylation
    • Vostal JG, Shulman NR. Vinculin is a major platelet protein that undergoes calcium-dependent tyrosine phosphorylation. Biochem J 1993; 294: 675-80.
    • (1993) Biochem J , vol.294 , pp. 675-680
    • Vostal, J.G.1    Shulman, N.R.2
  • 24
    • 0028043160 scopus 로고
    • Evidence for a role for tyrosine phosphorylation of phospolipase Cγ2 in collagen-induced platelet cytosolic calcium mobilisation
    • Daniel JL, Dangelmaier C, Smith JB. Evidence for a role for tyrosine phosphorylation of phospolipase Cγ2 in collagen-induced platelet cytosolic calcium mobilisation. Biochem J 1994; 302: 617-22.
    • (1994) Biochem J , vol.302 , pp. 617-622
    • Daniel, J.L.1    Dangelmaier, C.2    Smith, J.B.3
  • 27
    • 0025214662 scopus 로고
    • Erbstatin blocks platelet activating factor-induced protein-tyrosine phosphorylation, phosphoinositide hydrolysis, protein kinase C activation, serotonin secretion and aggregation of rabbit platelets
    • Salari H, Duronio V, Howard SL, Demos M, Jones K, Reany A, Hudson AT, Pelech SL. Erbstatin blocks platelet activating factor-induced protein-tyrosine phosphorylation, phosphoinositide hydrolysis, protein kinase C activation, serotonin secretion and aggregation of rabbit platelets. FEBS Letts 1990; 263: 104-8.
    • (1990) FEBS Letts , vol.263 , pp. 104-108
    • Salari, H.1    Duronio, V.2    Howard, S.L.3    Demos, M.4    Jones, K.5    Reany, A.6    Hudson, A.T.7    Pelech, S.L.8
  • 28
    • 0024988230 scopus 로고
    • Effect of genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets
    • Gaudette DC, Holub BJ. Effect of genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets. Biochem Biophys Res Commun 1990; 170: 238-42.
    • (1990) Biochem Biophys Res Commun , vol.170 , pp. 238-242
    • Gaudette, D.C.1    Holub, B.J.2
  • 30
    • 0026765030 scopus 로고
    • Thrombin-induced human platelet aggregation is inhibited by protein-tyrosine kinase inhibitors, ST638 and genistein
    • Asahi M, Yanagi S, Ohta S, Inazu T, Sakai K, Takeuchi F, Taniguchi T, Yamamura H. Thrombin-induced human platelet aggregation is inhibited by protein-tyrosine kinase inhibitors, ST638 and genistein. FEBS Letts 1992; 309: 10-4.
    • (1992) FEBS Letts , vol.309 , pp. 10-14
    • Asahi, M.1    Yanagi, S.2    Ohta, S.3    Inazu, T.4    Sakai, K.5    Takeuchi, F.6    Taniguchi, T.7    Yamamura, H.8
  • 32
    • 0024350371 scopus 로고
    • Vanadate and molybdate increase tyrosine phosphorylation in a 50-kilodalton protein and stimulate secretion in electropermeabilised platelets
    • Lerea KM, Tonks NK, Krebs EG, Fischer EH, Glomset JA. Vanadate and molybdate increase tyrosine phosphorylation in a 50-kilodalton protein and stimulate secretion in electropermeabilised platelets. Biochem 1989; 28: 9286-92.
    • (1989) Biochem , vol.28 , pp. 9286-9292
    • Lerea, K.M.1    Tonks, N.K.2    Krebs, E.G.3    Fischer, E.H.4    Glomset, J.A.5
  • 34
  • 35
    • 0027380501 scopus 로고
    • Tyrosine phosphorylation in platelets. Potential roles in intracellular signal transduction
    • Clark EA, Brugge JS. Tyrosine phosphorylation in platelets. Potential roles in intracellular signal transduction. Trends Cardiovasc Med 1993; 3: 218-27.
    • (1993) Trends Cardiovasc Med , vol.3 , pp. 218-227
    • Clark, E.A.1    Brugge, J.S.2
  • 36
    • 0026023289 scopus 로고
    • Targeted disruption of c-src proto-oncogene leads to osteopetrosis mice
    • Soriano P, Montgomery C, Geske R, Bradley A. Targeted disruption of c-src proto-oncogene leads to osteopetrosis mice. Cell 1991; 64: 693-702.
    • (1991) Cell , vol.64 , pp. 693-702
    • Soriano, P.1    Montgomery, C.2    Geske, R.3    Bradley, A.4
  • 38
    • 0026612411 scopus 로고
    • fyn mutant mice display differential signalling in thymocytes and peripheral T cells
    • fyn mutant mice display differential signalling in thymocytes and peripheral T cells. Cell 1992; 70: 741-50.
    • (1992) Cell , vol.70 , pp. 741-750
    • Stein, P.L.1    Lee, H.M.2    Rich, S.3    Soriano, P.4
  • 40
    • 0029278886 scopus 로고
    • Structure-function relationships in src family and related protein tyrosine kinases
    • Superti-Furga G, Courtneidge SA. Structure-function relationships in src family and related protein tyrosine kinases. Bioessays 1995; 17: 321-30.
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 42
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan KB, Bibbins KB, Swedlow JR, Arnaud M, Morgan DO, Varmus HE. Association of the amino-terminal half of c-src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J 1994; 13: 4745-56.
    • (1994) EMBO J , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 46
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper JA, Howell B. The when and how of Src regulation. Cell 1993; 73: 1051-4.
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 47
    • 0027340192 scopus 로고
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets
    • c-src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol Cell Biol 1993; 13: 1863-71.
    • (1993) Mol Cell Biol , vol.13 , pp. 1863-1871
    • Clark, E.A.1    Brugge, J.S.2
  • 48
    • 0023317189 scopus 로고
    • src with Triton X-100-resistant cellular structure correlates with morphological transformation
    • src with Triton X-100-resistant cellular structure correlates with morphological transformation. Proc Natl Acad Sci USA 1987; 84: 2312-6.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2312-2316
    • Hamaguchi, M.1    Hanafusa, H.2
  • 49
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to the extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to the extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 1992; 119: 893-903.
    • (1992) J Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.2    Romer, L.H.3
  • 51
    • 0026739248 scopus 로고
    • src with Triton X-100-insoluble residue in human blood platelets requires platelet aggregation and actin polymerisation
    • src with Triton X-100-insoluble residue in human blood platelets requires platelet aggregation and actin polymerisation. J Biol Chem 1992; 267: 20075-81.
    • (1992) J Biol Chem , vol.267 , pp. 20075-20081
    • Oda, A.1    Druker, B.J.2    Smith, M.3    Salzman, E.W.4
  • 52
    • 0026597050 scopus 로고
    • c-src to the cytoskeleton during platelet aggregation
    • c-src to the cytoskeleton during platelet aggregation. EMBO J 1992; 11: 855-61.
    • (1992) EMBO J , vol.11 , pp. 855-861
    • Horvath, A.R.1    Muszbek, L.2    Kellie, S.3
  • 53
    • 0029034939 scopus 로고
    • c-Src enhances the spreading of src -/- fibroblasts on fibronectin by a kinase-independent mechanism
    • Kaplan KB, Swedlow JR, Morgan DO, Varmus HE. c-Src enhances the spreading of src -/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes and Development 1995; 9: 1505-17.
    • (1995) Genes and Development , vol.9 , pp. 1505-1517
    • Kaplan, K.B.1    Swedlow, J.R.2    Morgan, D.O.3    Varmus, H.E.4
  • 55
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller MD, Juliano RL. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 1992; 267: 23439-42.
    • (1992) J Biol Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.D.4    Juliano, R.L.5
  • 56
    • 0026759309 scopus 로고
    • Regulation of focal adhesion associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan J, Shalloway D. Regulation of focal adhesion associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992; 358: 690-2.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.1    Shalloway, D.2
  • 58
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller MD, Parsons JT. Focal adhesion kinase and associated proteins. Curr Opin Cell Biol 1994; 6: 705-10.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 59
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller MD, Otey CA, Hildebrand Jd, Parsons JT. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J Cell Biol 1995; 130: 1181-7.
    • (1995) J Cell Biol , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, Jd.3    Parsons, J.T.4
  • 60
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand JD, Schaller MD, Parsons JT. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol Biol Cell 1995; 6: 637-47.
    • (1995) Mol Biol Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 63
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for src family kinases
    • Calalb MB, Polte TR, Hanks SK. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for src family kinases. Mol Cell Biol 1995; 15: 954-63.
    • (1995) Mol Cell Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 67
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994; 372: 786-91.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 68
    • 0028986116 scopus 로고
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 1995; 15: 2635-45.
    • (1995) Mol Cell Biol , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 69
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen H, Guan J. Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1994; 91: 10148-52.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10148-10152
    • Chen, H.1    Guan, J.2
  • 70
    • 0029873045 scopus 로고    scopus 로고
    • Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle T-transformed fibroblasts
    • Bachelot C, Rameh L, Parsons JT, Cantley LC. Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle T-transformed fibroblasts. Biochim Biophys Acta 1996; 1311: 45-52.
    • (1996) Biochim Biophys Acta , vol.1311 , pp. 45-52
    • Bachelot, C.1    Rameh, L.2    Parsons, J.T.3    Cantley, L.C.4
  • 71
    • 0029965695 scopus 로고    scopus 로고
    • Integrin-mediated signalling: Regulation by protein tyrosine kinases and small GTP-binding proteins
    • Parson JT. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr Opin Cell Biol 1996; 8: 146-52.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 146-152
    • Parson, J.T.1
  • 74
  • 77
    • 0029096541 scopus 로고
    • Cloning and characterisation of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T. Cloning and characterisation of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem 1995; 270: 21206-19.
    • (1995) J Biol Chem , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 83
    • 0027185152 scopus 로고
    • T cell activation by clustered tyrosine kinases
    • Kolanus W, Romeo C, Seed B. T cell activation by clustered tyrosine kinases. Cell 1993; 74: 171-83.
    • (1993) Cell , vol.74 , pp. 171-183
    • Kolanus, W.1    Romeo, C.2    Seed, B.3
  • 86
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng AM, Rowley B, Pao W, Hayday A, Bolen JB, Pawson T. Syk tyrosine kinase required for mouse viability and B-cell development. Nature 1995; 378: 303-6.
    • (1995) Nature , vol.378 , pp. 303-306
    • Cheng, A.M.1    Rowley, B.2    Pao, W.3    Hayday, A.4    Bolen, J.B.5    Pawson, T.6
  • 87
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
    • Shiue L, Zoller MJ, Brugge JS. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J Biol Chem 1995; 270: 10498-502.
    • (1995) J Biol Chem , vol.270 , pp. 10498-10502
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 88
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan AC, Desai DM, Weiss A. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol 1994; 12: 555-92.
    • (1994) Annu Rev Immunol , vol.12 , pp. 555-592
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 90
    • 0026757299 scopus 로고
    • Activation of FcgRII induces tyrosine phosphorylation of multiple proteins including FcgRII
    • Huang MM, Indik Z, Brass LF, Hoxie JA, Schreiber AD, Brugge JS. Activation of FcgRII induces tyrosine phosphorylation of multiple proteins including FcgRII. J Biol Chem 1992; 267: 5467-73.
    • (1992) J Biol Chem , vol.267 , pp. 5467-5473
    • Huang, M.M.1    Indik, Z.2    Brass, L.F.3    Hoxie, J.A.4    Schreiber, A.D.5    Brugge, J.S.6
  • 92
    • 0029883665 scopus 로고    scopus 로고
    • syk noncovalently associate with the low affinity Fcg receptor on human platelets through an immunoreceptor tyrosine-based activation motif
    • syk noncovalently associate with the low affinity Fcg receptor on human platelets through an immunoreceptor tyrosine-based activation motif. J Biol Chem 1996; 271: 10775-81.
    • (1996) J Biol Chem , vol.271 , pp. 10775-10781
    • Chacko, G.W.1    Brandt, J.T.2    Coggeshall, K.M.3    Anderson, C.L.4
  • 93
    • 0028856876 scopus 로고
    • Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the FcgIIa receptor
    • Yanaga F, Poole A, Asselin J, Blake R, Schieven GL, Clark EA, Watson SP. Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the FcgIIa receptor. Biochem J 1995; 311: 471-8.
    • (1995) Biochem J , vol.311 , pp. 471-478
    • Yanaga, F.1    Poole, A.2    Asselin, J.3    Blake, R.4    Schieven, G.L.5    Clark, E.A.6    Watson, S.P.7
  • 96
    • 0028037889 scopus 로고
    • Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation
    • Clark EA, Trikha M, Markland FS, Brugge JS. Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation. J Biol Chem 1994; 269: 21940-3.
    • (1994) J Biol Chem , vol.269 , pp. 21940-21943
    • Clark, E.A.1    Trikha, M.2    Markland, F.S.3    Brugge, J.S.4
  • 97
    • 12044249985 scopus 로고
    • Cytokine signal transduction and the JAK family of protein tyrosine kinases
    • Wilks AF, Harpur AG. Cytokine signal transduction and the JAK family of protein tyrosine kinases. Bioessays 1994; 16: 313-20.
    • (1994) Bioessays , vol.16 , pp. 313-320
    • Wilks, A.F.1    Harpur, A.G.2
  • 98
    • 0026081302 scopus 로고
    • Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase
    • Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, Ziemiecki A. Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol Cell Biol 1991; 11: 2057-65.
    • (1991) Mol Cell Biol , vol.11 , pp. 2057-2065
    • Wilks, A.F.1    Harpur, A.G.2    Kurban, R.R.3    Ralph, S.J.4    Zurcher, G.5    Ziemiecki, A.6
  • 99
    • 0028026923 scopus 로고
    • Phosphorylation of JAK2 in thrombin-stimulated human platelets
    • Rodriguez-Linares B, Watson SP. Phosphorylation of JAK2 in thrombin-stimulated human platelets. FEBS Letts 1994; 352: 335-8.
    • (1994) FEBS Letts , vol.352 , pp. 335-338
    • Rodriguez-Linares, B.1    Watson, S.P.2
  • 100
    • 0023766362 scopus 로고
    • Platelet tyrosine-specific protein phosphorylation is regulated by thrombin
    • Ferrel JE, Martin GS. Platelet tyrosine-specific protein phosphorylation is regulated by thrombin. Mol Cell Biol 1988; 8: 3603-10.
    • (1988) Mol Cell Biol , vol.8 , pp. 3603-3610
    • Ferrel, J.E.1    Martin, G.S.2
  • 101
    • 0027328791 scopus 로고
    • Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton
    • Pumiglia KM, Feinstein MB. Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton. Biochem J 1993; 294: 253-60.
    • (1993) Biochem J , vol.294 , pp. 253-260
    • Pumiglia, K.M.1    Feinstein, M.B.2
  • 102
    • 0025676023 scopus 로고
    • Role of platelet membrane glycoprotein IIb-IIIa in agonist-induced tyrosine phosphorylation of platelet proteins
    • Golden A, Brugge JS, Shattil SJ. Role of platelet membrane glycoprotein IIb-IIIa in agonist-induced tyrosine phosphorylation of platelet proteins. J Cell Biol 1990; 111: 3117-27.
    • (1990) J Cell Biol , vol.111 , pp. 3117-3127
    • Golden, A.1    Brugge, J.S.2    Shattil, S.J.3
  • 104
    • 0027419589 scopus 로고
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex
    • src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J Cell Biol 1993; 120: 1417-26.
    • (1993) J Cell Biol , vol.120 , pp. 1417-1426
    • Wu, H.1    Parsons, J.T.2
  • 105
    • 0029069226 scopus 로고
    • Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertusis toxin-sensitive heterodimeric G-protein
    • Li RY, Gaits F, Ragab A, Ragab-Thomas JMF, Chap H. Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertusis toxin-sensitive heterodimeric G-protein. EMBO J 1995; 14: 2519-26.
    • (1995) EMBO J , vol.14 , pp. 2519-2526
    • Li, R.Y.1    Gaits, F.2    Ragab, A.3    Ragab-Thomas, J.M.F.4    Chap, H.5
  • 107
    • 0027748236 scopus 로고
    • The platelet cytoskeleton
    • Fox JEB. The platelet cytoskeleton. Thromb Haemost 1993; 70: 884-93.
    • (1993) Thromb Haemost , vol.70 , pp. 884-893
    • Fox, J.E.B.1
  • 108
    • 0028817908 scopus 로고
    • Convergence on integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper GE, McNamee HP, Dike LE, Bojanowski K, Ingber DE. Convergence on integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol Biol Cell 1995; 6: 1349-65
    • (1995) Mol Biol Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 109
    • 0027242121 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal reorganisation in platelets are triggered by interaction of integrin receptors with their immobilised ligands
    • Haimovich B, Lipfert L, Brugge JS, Shattil SJ. Tyrosine phosphorylation and cytoskeletal reorganisation in platelets are triggered by interaction of integrin receptors with their immobilised ligands. J Biol Chem 1993; 268: 15868-77.
    • (1993) J Biol Chem , vol.268 , pp. 15868-15877
    • Haimovich, B.1    Lipfert, L.2    Brugge, J.S.3    Shattil, S.J.4
  • 110
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S, Akiyama SK, Yamada KM. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 1995; 267: 883-5.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 111
    • 0028205463 scopus 로고
    • Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets
    • Li RY, Gaits F, Ragab A, Ragad-Thomas JMF, Chap H. Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets. FEBS Letts 1994; 343: 89-93.
    • (1994) FEBS Letts , vol.343 , pp. 89-93
    • Li, R.Y.1    Gaits, F.2    Ragab, A.3    Ragad-Thomas, J.M.F.4    Chap, H.5
  • 112
    • 0027494395 scopus 로고
    • Calpain-catalysed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets
    • Frangioni JV, Oda A, Smith M, Salzman EW, Neel BG. Calpain-catalysed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets. EMBO J 1993; 12: 4843-56.
    • (1993) EMBO J , vol.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3    Salzman, E.W.4    Neel, B.G.5
  • 113
    • 0011185737 scopus 로고
    • The leukocyte common antigen (CD45): A putative receptor-linked protein tyrosine phosphatase
    • Charbonneau H, Tonks NK, Walsh KA, Fischer EH. The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. Proc Natl Acad Sci USA 1988; 85: 7182-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7182-7186
    • Charbonneau, H.1    Tonks, N.K.2    Walsh, K.A.3    Fischer, E.H.4
  • 114
    • 0026584285 scopus 로고
    • The non-transmembrane tyrosine phosphatase PTP-1B localises to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni JV, Beahm PH, Shifrin V, Jost CA, Neel BG. The non-transmembrane tyrosine phosphatase PTP-1B localises to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 1992; 68: 545-60.
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 115
    • 0027223005 scopus 로고
    • Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: Identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation
    • Flint AJ, Gebbink FGB, Franza BR, Hill DE, Tonks NK. Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation. EMBO J 1993; 12: 1937-46.
    • (1993) EMBO J , vol.12 , pp. 1937-1946
    • Flint, A.J.1    Gebbink, F.G.B.2    Franza, B.R.3    Hill, D.E.4    Tonks, N.K.5
  • 117
    • 0025816584 scopus 로고
    • A protein tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases
    • Shen S, Bastien L, Posner BI, Chretien P. A protein tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases. Nature 1991; 352: 736-9.
    • (1991) Nature , vol.352 , pp. 736-739
    • Shen, S.1    Bastien, L.2    Posner, B.I.3    Chretien, P.4
  • 118
    • 0026516065 scopus 로고
    • Isolation of a src homology 2-containing tyrosine phosphatase
    • Plutzky J, Neel BG, Rosenberg RD. Isolation of a src homology 2-containing tyrosine phosphatase. Proc Natl Acad Sci USA 1992; 89: 1123-7.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1123-1127
    • Plutzky, J.1    Neel, B.G.2    Rosenberg, R.D.3
  • 119
    • 0026547356 scopus 로고
    • Protein tyrosine phosphatase containing SH2 domains: Characterisation, preferential expression in haematopoietic cells, and localisation to human chromosome 12 p12-p13
    • Yi T, Cleveland JL, Ihle JN. Protein tyrosine phosphatase containing SH2 domains: characterisation, preferential expression in haematopoietic cells, and localisation to human chromosome 12 p12-p13. Mol Cell Biol 1992; 12: 836-46.
    • (1992) Mol Cell Biol , vol.12 , pp. 836-846
    • Yi, T.1    Cleveland, J.L.2    Ihle, J.N.3
  • 120
    • 0026742211 scopus 로고
    • Characterisation of haematopoietic intracellular protein tyrosine phosphatases: Description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
    • Matthews RJ, Bowne DB, Flores E, Thomas ML. Characterisation of haematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol Cell Biol 1992; 12: 2396-405.
    • (1992) Mol Cell Biol , vol.12 , pp. 2396-2405
    • Matthews, R.J.1    Bowne, D.B.2    Flores, E.3    Thomas, M.L.4
  • 122
    • 0027195626 scopus 로고
    • Motheaten and viable motheaten mice have viable mutations in the haematopoietic cell phosphatase gene
    • Tsui HW, Siminovitch KA, Souza L, Tsui FWL. Motheaten and viable motheaten mice have viable mutations in the haematopoietic cell phosphatase gene. Nature Genetics 1993; 4: 124-9.
    • (1993) Nature Genetics , vol.4 , pp. 124-129
    • Tsui, H.W.1    Siminovitch, K.A.2    Souza, L.3    Tsui, F.W.L.4
  • 123
    • 0027197067 scopus 로고
    • Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
    • Schultz LD, Schweitzer PA, Rajan TV, Yi T, Ihle JN, Matthews RJ, Thomas ML, Beier DR. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 1993; 73: 1445-54.
    • (1993) Cell , vol.73 , pp. 1445-1454
    • Schultz, L.D.1    Schweitzer, P.A.2    Rajan, T.V.3    Yi, T.4    Ihle, J.N.5    Matthews, R.J.6    Thomas, M.L.7    Beier, D.R.8
  • 124
    • 0027359495 scopus 로고
    • Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice
    • Kozlowski M, Mlinaric-Rascan I, Feng GS, Shen R, Pawson T, Siminovitch KA. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J Exp Med 1993; 178: 2157-63.
    • (1993) J Exp Med , vol.178 , pp. 2157-2163
    • Kozlowski, M.1    Mlinaric-Rascan, I.2    Feng, G.S.3    Shen, R.4    Pawson, T.5    Siminovitch, K.A.6
  • 125
    • 0027488637 scopus 로고
    • Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis
    • Yi T, Mui A L, Krystal G, Ihle JN. Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol Cell Biol 1993; 13: 7577-86.
    • (1993) Mol Cell Biol , vol.13 , pp. 7577-7586
    • Yi, T.1    Mui, A.L.2    Krystal, G.3    Ihle, J.N.4
  • 126
    • 0029914934 scopus 로고    scopus 로고
    • Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-src in human platelets
    • Falet H, Ramos-Morales F, Bachelot C, Fischer S, Rendu F. Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-src in human platelets. FEBS Letts 1996; 383: 165-9.
    • (1996) FEBS Letts , vol.383 , pp. 165-169
    • Falet, H.1    Ramos-Morales, F.2    Bachelot, C.3    Fischer, S.4    Rendu, F.5
  • 127
    • 0027262361 scopus 로고
    • Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains
    • Zhao Z, Shen SH, Fischer EH. Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains. Proc Natl Acad Sci USA 1993; 90: 4251-5.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4251-4255
    • Zhao, Z.1    Shen, S.H.2    Fischer, E.H.3
  • 128
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase: A putative homolog of Drosophila corkscrew
    • Freeman RM, Plutzky J, Neel BG. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc Natl Acad Sci USA 1992; 89: 11239-43.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11239-11243
    • Freeman, R.M.1    Plutzky, J.2    Neel, B.G.3
  • 129
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as target of protein-tyrosine kinases
    • Feng GS, Hui CC, Pawson T. SH2-containing phosphotyrosine phosphatase as target of protein-tyrosine kinases. Science 1993; 259: 1607-11.
    • (1993) Science , vol.259 , pp. 1607-1611
    • Feng, G.S.1    Hui, C.C.2    Pawson, T.3
  • 130
    • 0027399168 scopus 로고
    • Activation of phosphotyrosine phosphatase by tyrosine phosphorylation
    • Vogel W, Lammers R, Huang J, Ullrich A. Activation of phosphotyrosine phosphatase by tyrosine phosphorylation. Science 1993; 259: 1611-4.
    • (1993) Science , vol.259 , pp. 1611-1614
    • Vogel, W.1    Lammers, R.2    Huang, J.3    Ullrich, A.4
  • 131
    • 0026749442 scopus 로고
    • Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3 with sequence similarity to the src-homology region 2
    • Adachi M, Sekiya M, Miyachi T, Matsuno K, Hinoda Y, Imai K, Yachi A. Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3 with sequence similarity to the src-homology region 2. FEBS Letts 1992; 314: 335-9.
    • (1992) FEBS Letts , vol.314 , pp. 335-339
    • Adachi, M.1    Sekiya, M.2    Miyachi, T.3    Matsuno, K.4    Hinoda, Y.5    Imai, K.6    Yachi, A.7
  • 132
    • 0027531954 scopus 로고
    • A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains
    • Ahmad S, Banville D, Zhao Z, Fischer EH, Shen SH. A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains. Proc Natl Acad Sci USA 1993; 90: 2197-201.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2197-2201
    • Ahmad, S.1    Banville, D.2    Zhao, Z.3    Fischer, E.H.4    Shen, S.H.5
  • 133
    • 0027490590 scopus 로고
    • Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2
    • Lechleider RJ, Freeman RM Jr, Neel BG. Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2. J Biol Chem 1993; 268: 13434-8.
    • (1993) J Biol Chem , vol.268 , pp. 13434-13438
    • Lechleider, R.J.1    Freeman Jr., R.M.2    Neel, B.G.3
  • 134
    • 0027432407 scopus 로고
    • Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine-1009, on the human platelet-derived growth factor receptor
    • Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, Shoelson SE, Walsh CT, Neel BG. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine-1009, on the human platelet-derived growth factor receptor. J Biol Chem 1993; 268: 21478-81.
    • (1993) J Biol Chem , vol.268 , pp. 21478-21481
    • Lechleider, R.J.1    Sugimoto, S.2    Bennett, A.M.3    Kashishian, A.S.4    Cooper, J.A.5    Shoelson, S.E.6    Walsh, C.T.7    Neel, B.G.8
  • 135
    • 0028021665 scopus 로고
    • Characterisation of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains
    • Dechert U, Adam M, Harder KW, Clark-Lewis I, Jirik F. Characterisation of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. J Biol Chem 1994; 269: 5602-11.
    • (1994) J Biol Chem , vol.269 , pp. 5602-5611
    • Dechert, U.1    Adam, M.2    Harder, K.W.3    Clark-Lewis, I.4    Jirik, F.5
  • 138
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological-pathological involvement
    • Saido TC, Sorimachi H, Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J 1994; 8: 814-22.
    • (1994) FASEB J , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 139
    • 0027535351 scopus 로고
    • Evidence that activation of platelet calpain is induced as a consequence of binding of adhesive ligand to the integrin, glycoprotein IIb-IIIa
    • Fox JEB, Taylor RG, Taffarel M, Boyles JK, Goll DE. Evidence that activation of platelet calpain is induced as a consequence of binding of adhesive ligand to the integrin, glycoprotein IIb-IIIa. J Cell Biol 1993; 120: 1501-7.
    • (1993) J Cell Biol , vol.120 , pp. 1501-1507
    • Fox, J.E.B.1    Taylor, R.G.2    Taffarel, M.3    Boyles, J.K.4    Goll, D.E.5
  • 140
    • 0039825543 scopus 로고
    • Role of the cytoskeleton in regulating integrin-induced transmembrane signalling
    • Abstr
    • Fox JEB, Santos G, Zuerbig S, Saido TC. Role of the cytoskeleton in regulating integrin-induced transmembrane signalling. Thromb Haemost 1995; 73: 987 (Abstr).
    • (1995) Thromb Haemost , vol.73 , pp. 987
    • Fox, J.E.B.1    Santos, G.2    Zuerbig, S.3    Saido, T.C.4
  • 141
    • 0025820405 scopus 로고
    • Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets
    • Fox JEB, Austin CD, Reynolds CC, Steffen PK. Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets. J Biol Chem 1991; 266, 13289-95.
    • (1991) J Biol Chem , vol.266 , pp. 13289-13295
    • Fox, J.E.B.1    Austin, C.D.2    Reynolds, C.C.3    Steffen, P.K.4
  • 142
    • 0025362663 scopus 로고
    • Role of membrane skeleton in preventing the shedding of procoagulant-rich microvesicles from the platelet plasma membrane
    • Fox JEB, Austin CD, Boyles JK, Steffen PK. Role of membrane skeleton in preventing the shedding of procoagulant-rich microvesicles from the platelet plasma membrane. J Cell Biol 1990; 111: 483-93.
    • (1990) J Cell Biol , vol.111 , pp. 483-493
    • Fox, J.E.B.1    Austin, C.D.2    Boyles, J.K.3    Steffen, P.K.4
  • 143
    • 0025694929 scopus 로고
    • The role of calpain in stimulus-response coupling: Evidence that calpain mediates agonist-induced expression of procoagulant activity in platelets
    • Fox JEB, Reynolds CC, Austin CD. The role of calpain in stimulus-response coupling: evidence that calpain mediates agonist-induced expression of procoagulant activity in platelets. Blood 1990; 76: 2510-9.
    • (1990) Blood , vol.76 , pp. 2510-2519
    • Fox, J.E.B.1    Reynolds, C.C.2    Austin, C.D.3
  • 144
    • 0027301820 scopus 로고
    • Platelet-derived microparticle formation involves glycoprotein IIb-IIIa
    • Gemmell CH, Sefton MV, Yeo EL. Platelet-derived microparticle formation involves glycoprotein IIb-IIIa. J Biol Chem 1993; 268: 14586-9.
    • (1993) J Biol Chem , vol.268 , pp. 14586-14589
    • Gemmell, C.H.1    Sefton, M.V.2    Yeo, E.L.3
  • 145
    • 0028220773 scopus 로고
    • Correlation between inhibition of cytoskeleton proteins and anti-vesiculation effect of calpeptin during A23187-induced activation of human platelets: Are vesicles shed by filopod fragmentation?
    • Basse F, Gaffet P, Bienvenue A. Correlation between inhibition of cytoskeleton proteins and anti-vesiculation effect of calpeptin during A23187-induced activation of human platelets: are vesicles shed by filopod fragmentation? Biochim Biophys Acta 1994; 1190: 217-24.
    • (1994) Biochim Biophys Acta , vol.1190 , pp. 217-224
    • Basse, F.1    Gaffet, P.2    Bienvenue, A.3
  • 146
    • 0027181304 scopus 로고
    • The effect of calpeptin (a calpain specific inhibitor) on agonist induced microparticle formation from the platelet plasma membrane
    • Yano Y, Shiba E, Kambayashi J, Sakon M, Kawasaki T, Fujitani K, Kang J, Mori T. The effect of calpeptin (a calpain specific inhibitor) on agonist induced microparticle formation from the platelet plasma membrane. Thromb Res 1993; 71: 385-96.
    • (1993) Thromb Res , vol.71 , pp. 385-396
    • Yano, Y.1    Shiba, E.2    Kambayashi, J.3    Sakon, M.4    Kawasaki, T.5    Fujitani, K.6    Kang, J.7    Mori, T.8
  • 147
    • 0026688548 scopus 로고
    • Platelet procoagulant activity and microvesicle formation. Its putative role in hemostasis and thrombosis
    • Zwaal RF, Comfurius P, Bevers EM. Platelet procoagulant activity and microvesicle formation. Its putative role in hemostasis and thrombosis. Biochim Biophys Acta 1992; 1180: 1-8.
    • (1992) Biochim Biophys Acta , vol.1180 , pp. 1-8
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 148
    • 0023661249 scopus 로고
    • Colocalisation of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle MC, Burridge K, DeMartino GN, Croall DE. Colocalisation of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 1987; 51: 569-77.
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.E.4
  • 149
    • 0028920431 scopus 로고
    • Participation of calpain in protein-tyrosine phosphorylation and dephosphorylation in human blood platelets
    • Ariyoshi H, Oda A, Salzman EW. Participation of calpain in protein-tyrosine phosphorylation and dephosphorylation in human blood platelets. Arterioscl Thromb Vasc Biol 1995; 15: 511-4.
    • (1995) Arterioscl Thromb Vasc Biol , vol.15 , pp. 511-514
    • Ariyoshi, H.1    Oda, A.2    Salzman, E.W.3
  • 150
    • 0024988230 scopus 로고
    • Effect of Genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets
    • Douglas CG, Holub B. Effect of Genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets. Biochem Biophys Res Comm 1990; 238-42.
    • (1990) Biochem Biophys Res Comm , pp. 238-242
    • Douglas, C.G.1    Holub, B.2


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