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Volumn 144, Issue 4, 1999, Pages 777-787

Matrix valency regulates integrin-mediated lymphoid adhesion via Syk kinase

Author keywords

Cell adhesion; Extracellular matrix; Integrin; Lymphocyte; Protein tyrosine kinase

Indexed keywords

INTEGRIN;

EID: 0033593790     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.144.4.777     Document Type: Article
Times cited : (42)

References (57)
  • 1
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules and selectins
    • Aplin, A.E., A. Howe, S.K. Alahari, and R.L. Juliano. 1998. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules and selectins. Pharmacol. Rev. 50:197-263.
    • (1998) Pharmacol. Rev. , vol.50 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 2
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni, G., and M.E. Hemler. 1998. Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci. 23:30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 3
    • 0028090058 scopus 로고
    • Interactions of Lyn with the antigen receptor during B cell activation
    • Burg, D.L., M.T. Furlong, M.L. Harrison, and R.L. Geahlen. 1994. Interactions of Lyn with the antigen receptor during B cell activation. J. Biol. Chem. 269: 28136-28142.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28136-28142
    • Burg, D.L.1    Furlong, M.T.2    Harrison, M.L.3    Geahlen, R.L.4
  • 4
    • 0030001675 scopus 로고    scopus 로고
    • Lymphocyte homing and homeostasis
    • Butcher, E.G., and L.J. Picker. Lymphocyte homing and homeostasis. 1996. Science. 272:60-66.
    • (1996) Science , vol.272 , pp. 60-66
    • Butcher, E.G.1    Picker, L.J.2
  • 5
    • 0029976419 scopus 로고    scopus 로고
    • The C-C chemokine MCP-1 differentially modulates the avidity of ß1 and ß2 integrins on T lymphocytes
    • Carr, M.W., R. Alon, and T.A. Springer. 1996. The C-C chemokine MCP-1 differentially modulates the avidity of ß1 and ß2 integrins on T lymphocytes. Immunity. 4:179-187.
    • (1996) Immunity , vol.4 , pp. 179-187
    • Carr, M.W.1    Alon, R.2    Springer, T.A.3
  • 6
    • 0030175744 scopus 로고    scopus 로고
    • Regulation of antigen receptor signal transduction by protein tyrosine kinases
    • Chan, A.C., and A.S. Shaw. 1996. Regulation of antigen receptor signal transduction by protein tyrosine kinases. Curr. Opin. Immunol. 8:394-401.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 394-401
    • Chan, A.C.1    Shaw, A.S.2
  • 7
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng, A.M., B. Rowley, W. Pao, A. Hayday, J.B. Bolen, and T. Pawson. 1995. Syk tyrosine kinase required for mouse viability and B-cell development. Nature. 378:303-306.
    • (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
  • 8
    • 0005306564 scopus 로고
    • Human endothelial cells synthesize and express an Arg-gly-asp-directed adhesion receptor involved in attachment to fibrinogen and von willebrand factor
    • Cheresh, D.A. 1987. Human endothelial cells synthesize and express an Arg-Gly-Asp-directed adhesion receptor involved in attachment to fibrinogen and von Willebrand factor. Proc. Natl. Acad. Sci. USA. 84:6471-6475.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6471-6475
    • Cheresh, D.A.1
  • 9
    • 0030018913 scopus 로고    scopus 로고
    • Cell adhesion and migration are regulated at distinct stages of thymic T cell development: The roles of fibronectin. VLA-4, and VLA-5
    • Crisa, L., V. Cirulli, M.H. Ellisman, J.K. Ishii, M.J. Elices, and D.R. Salomon. 1996. Cell adhesion and migration are regulated at distinct stages of thymic T cell development: the roles of fibronectin. VLA-4, and VLA-5, J. Exp. Med. 184:215-228.
    • (1996) J. Exp. Med. , vol.184 , pp. 215-228
    • Crisa, L.1    Cirulli, V.2    Ellisman, M.H.3    Ishii, J.K.4    Elices, M.J.5    Salomon, D.R.6
  • 10
    • 0024506757 scopus 로고
    • Phorhol ester modulation of integrin-mediated cell adhesion: A postreceptor event
    • Danilov, Y.N., and R.L. Juliano. 1989. Phorhol ester modulation of integrin-mediated cell adhesion: a postreceptor event. J. Cell Biol. 108:1925-1933.
    • (1989) J. Cell Biol. , vol.108 , pp. 1925-1933
    • Danilov, Y.N.1    Juliano, R.L.2
  • 11
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogcne product
    • Deckert, M., S. Tartare-Deckert, C. Couture, T. Mustelin, and A. Altman. 1996. Functional and physical interactions of Syk family kinases with the Vav proto-oncogcne product. Immunity. 5:591-604.
    • (1996) Immunity , vol.5 , pp. 591-604
    • Deckert, M.1    Tartare-Deckert, S.2    Couture, C.3    Mustelin, T.4    Altman, A.5
  • 12
    • 0029004025 scopus 로고
    • Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability, and angiogenesis
    • Dvorak, H.F., L.F. Brown, M. Detmar, and A.M. Dvorak. 1995. Vascular permeability factor/vascular endothelial growth factor, microvascular hyperpermeability, and angiogenesis. Am. J. Pathol. 146:1029-1039.
    • (1995) Am. J. Pathol. , vol.146 , pp. 1029-1039
    • Dvorak, H.F.1    Brown, L.F.2    Detmar, M.3    Dvorak, A.M.4
  • 13
    • 0021984584 scopus 로고
    • A linkage between the hematostatic and immune systems embodies in the fibripolytic release of lymphocyte suppressive peptides
    • Edgington, T.S., L.K. Curtiss, and E.F. Plow. 1985. A linkage between the hematostatic and immune systems embodies in the fibripolytic release of lymphocyte suppressive peptides. J. Immunol. 134:471-477.
    • (1985) J. Immunol. , vol.134 , pp. 471-477
    • Edgington, T.S.1    Curtiss, L.K.2    Plow, E.F.3
  • 15
    • 0026775143 scopus 로고
    • Distinct biological consequences of integrin αvβ3-mediated melanoma cell adhesion to fibrinogen and its plasmic fragments
    • Felding-Habermann, B., Z.M. Ruggeri, and D.A. Cheresh. 1992. Distinct biological consequences of integrin αvβ3-mediated melanoma cell adhesion to fibrinogen and its plasmic fragments. J. Biol. Chem. 267:5070-5077.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5070-5077
    • Felding-Habermann, B.1    Ruggeri, Z.M.2    Cheresh, D.A.3
  • 16
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin β3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo, E.J., P.C. Brooks, S.L. Deming, C. Damsky, and D.A. Cheresh. 1995. Requirement of the NPXY motif in the integrin β3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo. J. Cell Biol. 130:441-450.
    • (1995) J. Cell Biol. , vol.130 , pp. 441-450
    • Filardo, E.J.1    Brooks, P.C.2    Deming, S.L.3    Damsky, C.4    Cheresh, D.A.5
  • 17
    • 0025241904 scopus 로고
    • Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers
    • Frelinger, A.L., III, I. Cohen, E.F. Plow, M.A. Smith, J. Roberts, S.C. Lam, and M.H. Ginsberg. 1990. Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers. J. Biol. Chem. 265:6346-6352.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6346-6352
    • Frelinger A.L. III1    Cohen, I.2    Plow, E.F.3    Smith, M.A.4    Roberts, J.5    Lam, S.C.6    Ginsberg, M.H.7
  • 18
    • 0031010040 scopus 로고    scopus 로고
    • Cross-linking of integrins induces tyrosine phosphorylation of the proto-oncogene product Vav and the protein tyrosine kinase Syk in human factor-dependent myeloid cells
    • Gotoh, A., H. Takahira, R.L. Geahlen, and H.E. Broxmeyer. 1997. Cross-linking of integrins induces tyrosine phosphorylation of the proto-oncogene product Vav and the protein tyrosine kinase Syk in human factor-dependent myeloid cells. Cell Growth Differ. 8:721-729.
    • (1997) Cell Growth Differ. , vol.8 , pp. 721-729
    • Gotoh, A.1    Takahira, H.2    Geahlen, R.L.3    Broxmeyer, H.E.4
  • 20
    • 0029940091 scopus 로고    scopus 로고
    • The vitronectin receptor (αvβ3) as an example for the role of integrins in T lymphocyte stimulation
    • Halvorson, M.J., J.E. Coligan, and K. Sturmhofel. 1996. The vitronectin receptor (αvβ3) as an example for the role of integrins in T lymphocyte stimulation. Immunol. Res. 15:16-29.
    • (1996) Immunol. Res. , vol.15 , pp. 16-29
    • Halvorson, M.J.1    Coligan, J.E.2    Sturmhofel, K.3
  • 21
    • 0026555594 scopus 로고
    • Lymphocyte adhesion can be regulated by cytoskeleton-associated. PMA-induced capping of surface receptors
    • Haverstack, D.M., H. Sakai, and L.S. Gray. 1992. Lymphocyte adhesion can be regulated by cytoskeleton-associated. PMA-induced capping of surface receptors. Am. J. Physiol. 262:C916-C926.
    • (1992) Am. J. Physiol. , vol.262
    • Haverstack, D.M.1    Sakai, H.2    Gray, L.S.3
  • 22
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions and their role on leukocytes
    • Hemler, M.E. 1990. VLA proteins in the integrin family: structures, functions and their role on leukocytes. Annu. Rev. Immunol. 8:365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 23
    • 0028263876 scopus 로고
    • Inhibition of CD41 T lymphocyte binding to fibronectin and immune-cell accumulation in inflammatory sites by non-peptidic mimetics of Arg-Gly-Asp
    • Hershkoviz, R., N. Greenspoon, Y.A. Mekori, R. Hadari, R. Alon, G. Kapustina, and O. Lider. 1994. Inhibition of CD41 T lymphocyte binding to fibronectin and immune-cell accumulation in inflammatory sites by non-peptidic mimetics of Arg-Gly-Asp. Clin. Exp. Immunol. 95:270-276.
    • (1994) Clin. Exp. Immunol. , vol.95 , pp. 270-276
    • Hershkoviz, R.1    Greenspoon, N.2    Mekori, Y.A.3    Hadari, R.4    Alon, R.5    Kapustina, G.6    Lider, O.7
  • 24
    • 0030759829 scopus 로고    scopus 로고
    • Growth arrest of Epstein-Barr virus immortalized B lymphocytes by adenovirus-delivered ribozymes
    • Huang, S., D. Stupack, P. Mathias, Y. Wang, and G. Nemerow. 1997. Growth arrest of Epstein-Barr virus immortalized B lymphocytes by adenovirus-delivered ribozymes. Proc. Nat. Acad. Sci. USA. 94:8156-8161.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 8156-8161
    • Huang, S.1    Stupack, D.2    Mathias, P.3    Wang, Y.4    Nemerow, G.5
  • 25
    • 0031573216 scopus 로고    scopus 로고
    • α4β integrin-mediated tyrosine phosphorylation in human T cells: Characterization of Crk-and Fyn-associated substrates (pp105. Pp115, and human enhancer of filamentation-1) and integrin-dependent activation of p59fyn1
    • Hunter, A.J., and Y. Shimizu. 1997. α4β integrin-mediated tyrosine phosphorylation in human T cells: characterization of Crk-and Fyn-associated substrates (pp105. pp115, and human enhancer of filamentation-1) and integrin-dependent activation of p59fyn1. J. Immunol. 159:4806-4814.
    • (1997) J. Immunol. , vol.159 , pp. 4806-4814
    • Hunter, A.J.1    Shimizu, Y.2
  • 26
    • 0027771387 scopus 로고
    • Dual inhibition of VLA-4 and LFA-1 maximally inhibits cutaneous delayed-type hypersensitivity-induced inflammation
    • Issekutz, T.B. 1993. Dual inhibition of VLA-4 and LFA-1 maximally inhibits cutaneous delayed-type hypersensitivity-induced inflammation. Am. J. Pathol. 143:1286-1293.
    • (1993) Am. J. Pathol. , vol.143 , pp. 1286-1293
    • Issekutz, T.B.1
  • 27
    • 0031909355 scopus 로고    scopus 로고
    • Cooperation between Syk and Rac1 leads to synergistic JNK activation in T lymphocytes
    • Jacinto, E., G. Werlen, and M. Karin. 1998. Cooperation between Syk and Rac1 leads to synergistic JNK activation in T lymphocytes. Immunity. 8:31-41.
    • (1998) Immunity , vol.8 , pp. 31-41
    • Jacinto, E.1    Werlen, G.2    Karin, M.3
  • 28
    • 0030968306 scopus 로고    scopus 로고
    • Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130
    • Keshvara, L.M., C. Isaacson, M.L. Harrison, and R.L. Geahlen. 1997. Syk activation and dissociation from the B-cell antigen receptor is mediated by phosphorylation of tyrosine 130. J. Biol. Chem. 272:10377-10381.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10377-10381
    • Keshvara, L.M.1    Isaacson, C.2    Harrison, M.L.3    Geahlen, R.L.4
  • 29
    • 0024327897 scopus 로고
    • Cell biology of cytotoxic and helper T cell functions: Immunofluorescence microscopic studies of single cells and cell couples
    • Kupfer, A., and S.J. Singer. 1989. Cell biology of cytotoxic and helper T cell functions: immunofluorescence microscopic studies of single cells and cell couples. Annu. Rev. Immunol. 7:309-337.
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 309-337
    • Kupfer, A.1    Singer, S.J.2
  • 30
    • 0028783396 scopus 로고
    • Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling
    • Kurosaki, T., S.A. Johnson, L. Pao, K. Sada, H. Yamamura, and J.C. Cambier. 1995. Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. J. Exp. Med. 182:1815-1823.
    • (1995) J. Exp. Med. , vol.182 , pp. 1815-1823
    • Kurosaki, T.1    Johnson, S.A.2    Pao, L.3    Sada, K.4    Yamamura, H.5    Cambier, J.C.6
  • 31
    • 0030059222 scopus 로고    scopus 로고
    • Role of rho in chemoattractant-activated leukocyte through integrins
    • Laudanna, C., J.J. Campbell, and E.C. Butcher. 1996. Role of rho in chemoattractant-activated leukocyte through integrins. Science. 271:981-983.
    • (1996) Science , vol.271 , pp. 981-983
    • Laudanna, C.1    Campbell, J.J.2    Butcher, E.C.3
  • 32
    • 0031912083 scopus 로고    scopus 로고
    • Adenovirus endocytosis via alpha(v) integrins requires phosphoinositide-3-OH kinase
    • Li, E., D. Stupack, R. Klemke, D.A. Cheresh, and G.R. Nemerow. 1998. Adenovirus endocytosis via alpha(v) integrins requires phosphoinositide-3-OH kinase. J. Virol. 72:2055-2061.
    • (1998) J. Virol. , vol.72 , pp. 2055-2061
    • Li, E.1    Stupack, D.2    Klemke, R.3    Cheresh, D.A.4    Nemerow, G.R.5
  • 33
    • 0029005762 scopus 로고
    • Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells. A possible signaling role for the syk tyrosine kinase
    • Lin, T.H., C. Rosales, K. Mondai, J.B. Bolen, S. Haskill, and R.L. Juliano. 1995. Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells. A possible signaling role for the Syk tyrosine kinase. J. Biol. Chem. 270:16189-16197.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16189-16197
    • Lin, T.H.1    Rosales, C.2    Mondai, K.3    Bolen, J.B.4    Haskill, S.5    Juliano, R.L.6
  • 34
    • 0031032421 scopus 로고    scopus 로고
    • Cytotoxic T lymphocytes express a β3 integrin which can induce the phosphorylation of focal adhesion kinase and the related PYK-2
    • Ma, E.A., O, Lou, N.N. Berg, and H.L. Ostergaard. 1997. Cytotoxic T lymphocytes express a β3 integrin which can induce the phosphorylation of focal adhesion kinase and the related PYK-2. Ear. J. Immunol. 27:329-335.
    • (1997) Ear. J. Immunol. , vol.27 , pp. 329-335
    • Ma, E.A.1    Lou, O.2    Berg, N.N.3    Ostergaard, H.L.4
  • 35
    • 0028086074 scopus 로고
    • Multiple adenovirus serotypes use αv integrins for infection
    • Mathias, P., T. Wickham, M. Moore, and G. Nemerow. 1994. Multiple adenovirus serotypes use αv integrins for infection. J. Virol. 68:6811-6814.
    • (1994) J. Virol. , vol.68 , pp. 6811-6814
    • Mathias, P.1    Wickham, T.2    Moore, M.3    Nemerow, G.4
  • 36
    • 0032032228 scopus 로고    scopus 로고
    • Transmembrane-truncated αvβ3 retains high affinity for ligand binding: Evidence for an "inside-out" suppressor?
    • Mehta, R.J., B. Diefenbach, A. Brown, E. Cullen, A. Jonczyk, D. Gussow, G.A. Lukenbach, and S.L. Goodman. 1998. Transmembrane-truncated αvβ3 retains high affinity for ligand binding: evidence for an "inside-out" suppressor? Biochem. J. 330:861-869.
    • (1998) Biochem. J. , vol.330 , pp. 861-869
    • Mehta, R.J.1    Diefenbach, B.2    Brown, A.3    Cullen, E.4    Jonczyk, A.5    Gussow, D.6    Lukenbach, G.A.7    Goodman, S.L.8
  • 37
    • 0028809739 scopus 로고
    • The covalent structure of factor XIIIa crosslinked fibrinogen fibrils
    • Mosesson, M.W., K.R. Siebenlist, J.F. Hainfeld, and J.S. Wall. 1995. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. J. Struct. Biol. 115:88-101.
    • (1995) J. Struct. Biol. , vol.115 , pp. 88-101
    • Mosesson, M.W.1    Siebenlist, K.R.2    Hainfeld, J.F.3    Wall, J.S.4
  • 38
    • 0031437888 scopus 로고    scopus 로고
    • Activation of protein-tyrosine kinase Pyk2 is downstream of Syk in FceRI signaling
    • Okazaki, H., J. Zhang, M.M. Hamawy, and R.P. Siniganian. 1997. Activation of protein-tyrosine kinase Pyk2 is downstream of Syk in FceRI signaling. J. Biol. Chem. 272:32443-32447.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32443-32447
    • Okazaki, H.1    Zhang, J.2    Hamawy, M.M.3    Siniganian, R.P.4
  • 39
    • 0029867911 scopus 로고    scopus 로고
    • Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates alpha-tubulin on tyrosine
    • Peters, J.D., M.T. Furlong, D.J. Asai, M.L. Harrison, and R.L. Geanlen. 1996. Syk, activated by cross-linking the B-cell antigen receptor, localizes to the cytosol where it interacts with and phosphorylates alpha-tubulin on tyrosine. J. Biol. Chem. 271:4755-1762.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4755-11762
    • Peters, J.D.1    Furlong, M.T.2    Asai, D.J.3    Harrison, M.L.4    Geanlen, R.L.5
  • 40
    • 0025840355 scopus 로고
    • Regulated expression and function of CDIIc/CD18 integrin on human B lymphocytes. Relationship between attachment to fibrinogen and triggering of proliferation through CDIIc/CD18
    • Postigo, A.A., A.L. Corbi, F. Sanchez-Madrid, and M.O. de Landazuri. 1991. Regulated expression and function of CDIIc/CD18 integrin on human B lymphocytes. Relationship between attachment to fibrinogen and triggering of proliferation through CDIIc/CD18. J Exp. Med. 174:1313-1322.
    • (1991) J Exp. Med. , vol.174 , pp. 1313-1322
    • Postigo, A.A.1    Corbi, A.L.2    Sanchez-Madrid, F.3    De Landazuri, M.O.4
  • 41
    • 0027769921 scopus 로고
    • The role of adheison molecules in the pathogenesis of rheumatoid arthritis
    • Postigo, A.A., R. Garcia-Vicuna, A. Laffon, and F. Sanchez-Madrid. 1993. The role of adheison molecules in the pathogenesis of rheumatoid arthritis. Autoimmunity. 16:69-76.
    • (1993) Autoimmunity. , vol.16 , pp. 69-76
    • Postigo, A.A.1    Garcia-Vicuna, R.2    Laffon, A.3    Sanchez-Madrid, F.4
  • 42
    • 0030294361 scopus 로고    scopus 로고
    • β1 integrin-mediated activation of focal adhesion kinase and its association with Fyn and Zap-70 in human NK cells
    • Rabinowich, H., M. Manciulea, R.B. Herberman, and T.L. Whiteside. β1 integrin-mediated activation of focal adhesion kinase and its association with Fyn and Zap-70 in human NK cells. J. Immunol. 157:3860-3868.
    • J. Immunol. , vol.157 , pp. 3860-3868
    • Rabinowich, H.1    Manciulea, M.2    Herberman, R.B.3    Whiteside, T.L.4
  • 43
    • 0026701517 scopus 로고
    • Lymphocyte migration through extracellular matrix
    • Ratner, S. 1992. Lymphocyte migration through extracellular matrix. Invasion Metastasis. 12:82-100.
    • (1992) Invasion Metastasis , vol.12 , pp. 82-100
    • Ratner, S.1
  • 44
    • 0027289639 scopus 로고
    • Fibrin and fibrinogen degradation products with an inteact D domain C-terminal γ chain inhibit an early step in accessory cell-dependent lymphocyte mitogenesis
    • Robson, S.C., R. Saunders, L.R. Purves, C. de Jager, A. Corrigall, and R.E. Kirsch. 1993. Fibrin and fibrinogen degradation products with an inteact D domain C-terminal γ chain inhibit an early step in accessory cell-dependent lymphocyte mitogenesis. Blood. 81:3006-3014.
    • (1993) Blood , vol.81 , pp. 3006-3014
    • Robson, S.C.1    Saunders, R.2    Purves, L.R.3    De Jager, C.4    Corrigall, A.5    Kirsch, R.E.6
  • 45
    • 0030055076 scopus 로고    scopus 로고
    • Extracellular matrix and lung inflammation
    • Roman, J. 1996. Extracellular matrix and lung inflammation. Immunol. Res. 15: 163-178.
    • (1996) Immunol. Res. , vol.15 , pp. 163-178
    • Roman, J.1
  • 47
    • 0344996900 scopus 로고
    • Lymphocyte interactions with extracellular matrix
    • Shimizu, Y., and S. Shaw. 1991. Lymphocyte interactions with extracellular matrix. FASEB (Fed Am. Soc. Exp. Biol.) J. 135:105-117.
    • (1991) FASEB (Fed Am. Soc. Exp. Biol.) J. , vol.135 , pp. 105-117
    • Shimizu, Y.1    Shaw, S.2
  • 48
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer, T.A. 1994. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell. 76:301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 49
    • 0017088029 scopus 로고
    • Lymphocyte homing into lymph nodes: In vitro demonstration of the selective affinity of recirculating lymphocytes for high-endothelial venules
    • Stamper, H.B., Jr., and J.J. Woodruff. 1976. Lymphocyte homing into lymph nodes: in vitro demonstration of the selective affinity of recirculating lymphocytes for high-endothelial venules. J. Exp. Med. 144:828-833.
    • (1976) J. Exp. Med. , vol.144 , pp. 828-833
    • Stamper H.B., Jr.1    Woodruff, J.J.2
  • 50
    • 0029946652 scopus 로고    scopus 로고
    • Regulation of leukocyte integrin function: Affinity vs. Avidity
    • Stewart, M., and N. Hogg. 1996. Regulation of leukocyte integrin function: affinity vs. avidity. J. Cell. Biochem. 61:554-561.
    • (1996) J. Cell. Biochem. , vol.61 , pp. 554-561
    • Stewart, M.1    Hogg, N.2
  • 52
    • 0027053032 scopus 로고
    • Inducible b cell adherence to extracellular matrix mediated by a β3 integrin
    • Stupack, D.G., C. Shen, and J.A. Wilkins. 1992. Inducible B cell adherence to extracellular matrix mediated by a β3 integrin. Exp. Cell Res. 203:443-448.
    • (1992) Exp. Cell Res. , vol.203 , pp. 443-448
    • Stupack, D.G.1    Shen, C.2    Wilkins, J.A.3
  • 53
    • 0030888167 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the vav proto-oncogene product links FceR1 to the Rac1-JNK pathway
    • Teramoto, H., P. Salem, K.C. Robbins, X.R. Bustelo, and J.S. Gulkind. 1997. Tyrosine phosphorylation of the vav proto-oncogene product links FceR1 to the Rac1-JNK pathway. J. Biol. Chem. 272:10751-10755.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10751-10755
    • Teramoto, H.1    Salem, P.2    Robbins, K.C.3    Bustelo, X.R.4    Gulkind, J.S.5
  • 55
    • 0028176149 scopus 로고
    • 2+ modulates leukocyte function-associated antigen-1 cell surface distribution of T lymphocytes and consequently affects cell adhesion
    • 2+ modulates leukocyte function-associated antigen-1 cell surface distribution of T lymphocytes and consequently affects cell adhesion. J. Cell Biol. 124: 1061-1070.
    • (1994) J. Cell Biol. , vol.124 , pp. 1061-1070
    • Van Kooyk, Y.1    Weder, P.2    Heje, K.3    Figdor, G.G.4
  • 56
    • 0029892373 scopus 로고    scopus 로고
    • Tytosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors
    • Wan, Y., T. Kurosaki, and X.Y. Huang. 1996. Tytosine kinases in activation of the MAP kinase cascade by G-protein-coupled receptors, Nature. 380:541-544.
    • (1996) Nature , vol.380 , pp. 541-544
    • Wan, Y.1    Kurosaki, T.2    Huang, X.Y.3
  • 57
    • 0027166647 scopus 로고
    • Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
    • Wickham, T.J., P. Mathias, D.A. Cheresh, and G.R. Nemerow. 1993. Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment. Cell. 73:309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.