메뉴 건너뛰기




Volumn 157, Issue 9, 1996, Pages 3860-3868

β1 Integrin-Mediated Activation of Focal Adhesion Kinase and Its Association with Fyn and Zap-70 in Human NK Cells

Author keywords

[No Author keywords available]

Indexed keywords

BETA1 INTEGRIN; CELL ADHESION MOLECULE; FIBRONECTIN RECEPTOR; FOCAL ADHESION KINASE; FOCAL ADHESION KINASE 1; FYN PROTEIN, HUMAN; HOMING RECEPTOR; INTEGRIN; LYN PROTEIN-TYROSINE KINASE; ONCOPROTEIN; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN KINASE ZAP 70; PROTEIN TYROSINE KINASE; PTK2 PROTEIN, HUMAN; VERY LATE ACTIVATION ANTIGEN 4; ZAP70 PROTEIN, HUMAN;

EID: 0030294361     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (35)

References (71)
  • 1
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11.
    • (1992) Cell , vol.69 , pp. 11
    • Hynes, R.1
  • 2
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams, J., and F. Watts. 1993. Regulation of development and differentiation by the extracellular matrix. Development 117:1183.
    • (1993) Development , vol.117 , pp. 1183
    • Adams, J.1    Watts, F.2
  • 3
    • 0026512073 scopus 로고
    • Signal transduction from the extracellular matrix: The integrin-tyrosine kinase connection
    • Kornberg, L., and R. L. Juliano. 1992. Signal transduction from the extracellular matrix: the integrin-tyrosine kinase connection. Trends Pharmacol. Sci. 13:93.
    • (1992) Trends Pharmacol. Sci. , vol.13 , pp. 93
    • Kornberg, L.1    Juliano, R.L.2
  • 4
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano, R. L., and S. Haskill. 1993. Signal transduction from the extracellular matrix. J. Cell Biol. 120:577.
    • (1993) J. Cell Biol. , vol.120 , pp. 577
    • Juliano, R.L.1    Haskill, S.2
  • 5
    • 0027413896 scopus 로고
    • Signaling by integrins: Implication for tumorigenesis
    • Schwartz, M. A. 1993. Signaling by integrins: implication for tumorigenesis. Cancer Res. 53:1503.
    • (1993) Cancer Res. , vol.53 , pp. 1503
    • Schwartz, M.A.1
  • 6
    • 0025745212 scopus 로고
    • Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape
    • Schwartz, M. A., C. Lechene, and D. E. Ingber. 1991. Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape. Proc. Natl. Acad. Sci. USA 88:7849.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7849
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 7
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium
    • Schwartz, M. A. 1993. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. J. Cell Biol. 120:1003.
    • (1993) J. Cell Biol. , vol.120 , pp. 1003
    • Schwartz, M.A.1
  • 8
    • 0026756730 scopus 로고
    • Integrin as a primary signal transduction molecule regulating monocyte immediate-early gene induction
    • Yurochko, A., D. Liu, S. Eirman, and S. Haskill. 1992. Integrin as a primary signal transduction molecule regulating monocyte immediate-early gene induction. Proc. Natl. Acad. Sci. USA 89:9034.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9034
    • Yurochko, A.1    Liu, D.2    Eirman, S.3    Haskill, S.4
  • 12
    • 0026535397 scopus 로고
    • Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein
    • Nojima, Y., D. Rothstein, K. Sugita, S. Schlossman, and C. Morimoto. 1992. Ligation of VLA-4 on T cells stimulates tyrosine phosphorylation of a 105-kD protein. J. Exp. Med. 175:1045.
    • (1992) J. Exp. Med. , vol.175 , pp. 1045
    • Nojima, Y.1    Rothstein, D.2    Sugita, K.3    Schlossman, S.4    Morimoto, C.5
  • 14
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins
    • Kornberg, L. J., H. S. Earp, C. E. Turner, C. Prockop, and R. L. Juliano. 1991. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of beta 1 integrins. Proc. Natl. Acad. Sci. USA 88:8392.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8392
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 15
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 16
    • 0026476697 scopus 로고
    • FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell 71: 891.
    • (1992) Cell , vol.71 , pp. 891
    • Zachary, I.1    Rozengurt, E.2
  • 17
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233.
    • (1995) Science , vol.268 , pp. 233
    • Clark, E.A.1    Brugge, J.S.2
  • 21
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper, J. A., and B. Howel. 1993. The when and how of Src regulation. Cell 73:1051.
    • (1993) Cell , vol.73 , pp. 1051
    • Cooper, J.A.1    Howel, B.2
  • 22
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • Schlessinger, J., and A. Ullrich. 1992. Growth factor signaling by receptor tyrosine kinases. Neuron 9:383.
    • (1992) Neuron , vol.9 , pp. 383
    • Schlessinger, J.1    Ullrich, A.2
  • 24
    • 0027938974 scopus 로고
    • Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase
    • Chen, H. C., and J. L. Guan. 1994. Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA 91: 10148.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10148
    • Chen, H.C.1    Guan, J.L.2
  • 25
    • 0028260229 scopus 로고
    • Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src
    • Sabe, H., A. Hata, M. Okada, H. Nakagawa, and H. Hanafusa. 1994. Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc. Natl. Acad. Sci. USA 91:3984.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3984
    • Sabe, H.1    Hata, A.2    Okada, M.3    Nakagawa, H.4    Hanafusa, H.5
  • 26
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. 1994. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786.
    • (1994) Nature , vol.372 , pp. 786
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 27
    • 0025195765 scopus 로고
    • Roles of adhesion molecules in T-cell recognition: Fundamental similarities between four integrins on resting human T cells (LFA-1, VLA-4, VLA-5, VLA-6) in expression, binding and costimulation
    • Shimizu, Y., G. A. van Seventer, K. J. Horgan, and S. Shaw. 1990. Roles of adhesion molecules in T-cell recognition: fundamental similarities between four integrins on resting human T cells (LFA-1, VLA-4, VLA-5, VLA-6) in expression, binding and costimulation. Immunol. Rev. 114:109.
    • (1990) Immunol. Rev. , vol.114 , pp. 109
    • Shimizu, Y.1    Van Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 28
    • 0028967288 scopus 로고
    • Fibronectin induces phosphorylation of a 120-kDa protein and synergizes with the T cell receptor to activate cytotoxic T cell clones
    • Ostergaard, H. L., and E. A. Ma. 1995. Fibronectin induces phosphorylation of a 120-kDa protein and synergizes with the T cell receptor to activate cytotoxic T cell clones. Eur. J. Immunol. 25:252.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 252
    • Ostergaard, H.L.1    Ma, E.A.2
  • 29
    • 0027431097 scopus 로고
    • Post-receptor occupancy events in leukocytes during beta 1 integrin-ligand interactions
    • Sanchez-Mateos, P., A. G. Arroyo, M. A. Balboa, and F. Sanchez-Madrid. 1993. Post-receptor occupancy events in leukocytes during beta 1 integrin-ligand interactions. Eur. J. Immunol. 23:2642.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2642
    • Sanchez-Mateos, P.1    Arroyo, A.G.2    Balboa, M.A.3    Sanchez-Madrid, F.4
  • 33
    • 0025964248 scopus 로고
    • Human natural killer cells express VLA-4 and VLA-5, which mediate their adhesion to fibronectin
    • Gismondi, A., S. Morrone, M. J. Humphries, M. Piccoli, L. Frati, and A. Santoni. 1991. Human natural killer cells express VLA-4 and VLA-5, which mediate their adhesion to fibronectin. J. Immunol. 146:384.
    • (1991) J. Immunol. , vol.146 , pp. 384
    • Gismondi, A.1    Morrone, S.2    Humphries, M.J.3    Piccoli, M.4    Frati, L.5    Santoni, A.6
  • 34
    • 0026756152 scopus 로고
    • Triggering through CD16 or phorbol esters enhances adhesion of NK cells to laminin via very late antigen 6
    • Gismondi, A., F. Mainiero, S. Morrone, G. Palmieri, M. Piccoli, L. Frati, and A. Santoni. 1992. Triggering through CD16 or phorbol esters enhances adhesion of NK cells to laminin via very late antigen 6. J. Exp. Med. 176:1251.
    • (1992) J. Exp. Med. , vol.176 , pp. 1251
    • Gismondi, A.1    Mainiero, F.2    Morrone, S.3    Palmieri, G.4    Piccoli, M.5    Frati, L.6    Santoni, A.7
  • 36
    • 0027195865 scopus 로고
    • Response of human NK cells to IL-6: Alteration of the cell surface phenotype, adhesion to fibronectin and laminin, and TNF-αβ secretion
    • Rabinowich, H., R. B. Herberman, and T. L. Whiteside. 1993. Response of human NK cells to IL-6: alteration of the cell surface phenotype, adhesion to fibronectin and laminin, and TNF-αβ secretion. J. Immunol. 150:4844.
    • (1993) J. Immunol. , vol.150 , pp. 4844
    • Rabinowich, H.1    Herberman, R.B.2    Whiteside, T.L.3
  • 37
    • 0024792513 scopus 로고
    • Biology of natural killer cells
    • Trinchieri, G. 1989. Biology of natural killer cells. Adv. Immunol. 47:187.
    • (1989) Adv. Immunol. , vol.47 , pp. 187
    • Trinchieri, G.1
  • 39
    • 0015821893 scopus 로고
    • A rapid method for the isolation of functional thymus derived murine lymphocytes
    • Julius, M. H., E. Simpson, and L. A. Herzenberg. 1973. A rapid method for the isolation of functional thymus derived murine lymphocytes. Eur. J. Immunol. 3:645.
    • (1973) Eur. J. Immunol. , vol.3 , pp. 645
    • Julius, M.H.1    Simpson, E.2    Herzenberg, L.A.3
  • 40
    • 0026680671 scopus 로고
    • The role of cytokines in the adoptive immunotherapy of an experimental model of human head and neck cancer by human IL-2-activated NK cells
    • Rabinowich, H., D. Vitolo, S. Altarac, R. B. Herberman, and T. L. Whiteside. 1992. The role of cytokines in the adoptive immunotherapy of an experimental model of human head and neck cancer by human IL-2-activated NK cells. J. Immunol. 149:340.
    • (1992) J. Immunol. , vol.149 , pp. 340
    • Rabinowich, H.1    Vitolo, D.2    Altarac, S.3    Herberman, R.B.4    Whiteside, T.L.5
  • 41
    • 0028208977 scopus 로고
    • Expression and function of CD7 molecule on human natural killer (NK) cells
    • Rabinowich, H., L. Pricop, R. B. Herberman, and T. L. Whiteside. 1994. Expression and function of CD7 molecule on human natural killer (NK) cells. J. Immunol. 152:517.
    • (1994) J. Immunol. , vol.152 , pp. 517
    • Rabinowich, H.1    Pricop, L.2    Herberman, R.B.3    Whiteside, T.L.4
  • 42
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to Immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins
    • Kamps, M. P., and B. M. Sefton. 1989. Acid and base hydrolysis of phosphoproteins bound to Immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins. Anal. Biochem. 176:22.
    • (1989) Anal. Biochem. , vol.176 , pp. 22
    • Kamps, M.P.1    Sefton, B.M.2
  • 43
    • 0029031806 scopus 로고
    • Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins
    • Neumeister, E. N., Y. Zhu, S. Richard, C. Terhorst, A. C. Chan, and A. S. Shaw. 1995. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. Mol. Cell. Biol. 15:3171.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3171
    • Neumeister, E.N.1    Zhu, Y.2    Richard, S.3    Terhorst, C.4    Chan, A.C.5    Shaw, A.S.6
  • 44
    • 0029071585 scopus 로고
    • Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function
    • Chan, A. C., M. Dalton, R. Johnson, G. H. Kong, T. Wang, R. Thoma, and T. Kurosaki. 1995. Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function. EMBO J. 14:2499.
    • (1995) EMBO J. , vol.14 , pp. 2499
    • Chan, A.C.1    Dalton, M.2    Johnson, R.3    Kong, G.H.4    Wang, T.5    Thoma, R.6    Kurosaki, T.7
  • 45
    • 0029563574 scopus 로고
    • Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk
    • Koegl, M., S. A. Courtneidge, and G. Superti-Furga. 1995. Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk. Oncogene 11:2317.
    • (1995) Oncogene , vol.11 , pp. 2317
    • Koegl, M.1    Courtneidge, S.A.2    Superti-Furga, G.3
  • 46
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263.
    • (1994) Cell , vol.76 , pp. 263
    • Weiss, A.1    Littman, D.R.2
  • 51
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen, B. G., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction proteins. Cell 80:237.
    • (1995) Cell , vol.80 , pp. 237
    • Cohen, B.G.1    Ren, R.2    Baltimore, D.3
  • 52
    • 0027293670 scopus 로고
    • Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells
    • Weng, Z., J. A. Taylor, C. E. Turner, J. S. Brugge, and C. Seidel-Dugan 1993. Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells. J. Biol. Chem. 268:14956.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14956
    • Weng, Z.1    Taylor, J.A.2    Turner, C.E.3    Brugge, J.S.4    Seidel-Dugan, C.5
  • 53
    • 0029133702 scopus 로고
    • Requirement of MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins
    • David, M., E. Petricoin III, C. Benjamin, R. Pine, M. J. Weber, and A. C. Larner. 1995. Requirement of MAP kinase (ERK2) activity in interferon α- and interferon β-stimulated gene expression through STAT proteins. Science 269:1721.
    • (1995) Science , vol.269 , pp. 1721
    • David, M.1    Petricoin III, E.2    Benjamin, C.3    Pine, R.4    Weber, M.J.5    Larner, A.C.6
  • 54
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller, M. D., C. A. Otey, J. D. Hildebrand, and J. T. Parsons. 1995. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J. Cell Biol. 130:1181.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 55
    • 0028533592 scopus 로고
    • Tensin: A potenlial link between the cytoskeleton and signal transduction
    • Lo, S. H., E. Weisberg, and L. B. Chen. 1994. Tensin: a potenlial link between the cytoskeleton and signal transduction. Bioessays 16:817.
    • (1994) Bioessays , vol.16 , pp. 817
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.3
  • 56
  • 57
    • 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, K. B., K. B. Bibbins, J. R. Swedlow, M. Arnaud, D. O. Morgan, and H. E. Varmus. 1994. 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. 13:4745.
    • (1994) EMBO J. , vol.13 , pp. 4745
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 58
    • 0027219262 scopus 로고
    • Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts
    • Birge, R. B., J. E. Fajardo, C. Reichman, S. E. Shoelson, Z. Songyang, L. C. Cantley, and H. Hanafusa. 1993. Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell. Biol. 13:4648.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4648
    • Birge, R.B.1    Fajardo, J.E.2    Reichman, C.3    Shoelson, S.E.4    Songyang, Z.5    Cantley, L.C.6    Hanafusa, H.7
  • 60
    • 0028960755 scopus 로고
    • Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes
    • Zaffran, Y., J. C. Escallier, S. Ruta, C. Capo, and J. L. Mege. 1995. Zymosan-triggered association of tyrosine phosphoproteins and lyn kinase with cytoskeleton in human monocytes. J. Immunol. 154:3488.
    • (1995) J. Immunol. , vol.154 , pp. 3488
    • Zaffran, Y.1    Escallier, J.C.2    Ruta, S.3    Capo, C.4    Mege, J.L.5
  • 61
    • 0026483786 scopus 로고
    • ZAP-70: A 70-kD protein-tyrosine kinase that associates with the TCR zeta chain
    • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992. ZAP-70: a 70-kD protein-tyrosine kinase that associates with the TCR zeta chain. Cell 71:649.
    • (1992) Cell , vol.71 , pp. 649
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 62
    • 0027255212 scopus 로고
    • Association of a 70-kDa tyrosine phosphoprotein with the CD16:zeta: Gamma complex expressed in human natural killer cells
    • Vivier, E., A. da Silva, M. Ackerly, H. Levine, C. E. Rudd, and P. Anderson. 1993. Association of a 70-kDa tyrosine phosphoprotein with the CD16:zeta: gamma complex expressed in human natural killer cells. Eur. J. Immunol. 23: 1872.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 1872
    • Vivier, E.1    Da Silva, A.2    Ackerly, M.3    Levine, H.4    Rudd, C.E.5    Anderson, P.6
  • 63
    • 0028130057 scopus 로고
    • Fc receptors: Rubor redux
    • Ravetch, J. V. 1994. Fc receptors: rubor redux. Cell 78:553.
    • (1994) Cell , vol.78 , pp. 553
    • Ravetch, J.V.1
  • 65
    • 0027996890 scopus 로고
    • Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase substrate
    • Kanner, S. B., A. Aruffo, and P. Y. Chan. 1994. Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase substrate. Proc. Natl. Acad. Sci. USA 91:10484.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10484
    • Kanner, S.B.1    Aruffo, A.2    Chan, P.Y.3
  • 66
    • 0029076191 scopus 로고
    • Role of VLA-4 molecule in T cell costimulation: Identification of tyrosine phosphorylation pattern induced by ligation of VLA-4
    • Sato, T., K. Tachibana, Y. Nojima, N. D'Avirro, and C. Morimoto. 1995. Role of VLA-4 molecule in T cell costimulation: identification of tyrosine phosphorylation pattern induced by ligation of VLA-4. J. Immunol. 155:2938.
    • (1995) J. Immunol. , vol.155 , pp. 2938
    • Sato, T.1    Tachibana, K.2    Nojima, Y.3    D'Avirro, N.4    Morimoto, C.5
  • 70
    • 0028037889 scopus 로고
    • Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation
    • Clark, E. A., M. Trikha, F. S. Markland, and J. S. Brugge. 1994. Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation. J. Biol. Chem. 269:21940.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21940
    • Clark, E.A.1    Trikha, M.2    Markland, F.S.3    Brugge, J.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.