메뉴 건너뛰기




Volumn 111, Issue 12, 1998, Pages 1759-1766

The 'ligand-induced conformational change' of α5β1 integrin. Relocation of α5 subunit to uncover the β1 stalk region

Author keywords

Cell adhesion; Conformational change; Integrin; Ligand binding

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; INTEGRIN; PROTEIN SUBUNIT;

EID: 0031854334     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni, G., Shih, D. T., Buck, C. A. and Hemler, M. E. (1995). Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270, 25570-25577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 2
    • 0022390602 scopus 로고
    • Effect of Calcium on the platelet membrane glycoprotein IIb-IIIa complex
    • Brass, L. F., Shattil, S. J., Kunicki, T. J. and Bennett, J. S. (1985). Effect of Calcium on the platelet membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 260, 7875-7881.
    • (1985) J. Biol. Chem. , vol.260 , pp. 7875-7881
    • Brass, L.F.1    Shattil, S.J.2    Kunicki, T.J.3    Bennett, J.S.4
  • 3
    • 0029157259 scopus 로고
    • Assembly and function of integrin receptors is dependent on opposing alpha and beta cytoplasmic domains
    • Briesewitz, R., Kern, A. and Marcantonio, E. E. (1995). Assembly and function of integrin receptors is dependent on opposing alpha and beta cytoplasmic domains. Mol. Biol. Cell 6, 997-1010.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 997-1010
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 4
    • 0027255758 scopus 로고
    • Ligand intercellular adhesion molecule I has a necessary role in activation of integrin lymphocyte function-associated molecule I
    • Cabanas, C. and Hogg, N. (1993). Ligand intercellular adhesion molecule I has a necessary role in activation of integrin lymphocyte function-associated molecule I. Proc. Nat. Acad. Sci. USA 90, 5838-5842.
    • (1993) Proc. Nat. Acad. Sci. USA , vol.90 , pp. 5838-5842
    • Cabanas, C.1    Hogg, N.2
  • 5
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen, Q., Kinch, M. S., Lin, T. H., Burridge, K. and Juliano, R. L. (1994). Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269, 26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.L.5
  • 8
    • 0024443411 scopus 로고
    • T-cell receptor crosslinking transiently stimulates adhesiveness through LFA-1
    • Dustin, M. L. and Springer, T. A. (1989). T-cell receptor crosslinking transiently stimulates adhesiveness through LFA-1. Nature 341, 619-624.
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 9
    • 0024208260 scopus 로고
    • Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion
    • Frelinger, A. L., Lam, S. C.-T., Plow, K. F., Smith, M. A., Loftus, J. C. and Ginsberg, M. H. (1988). Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. J. Biol. Chem. 263 12397-12402.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12397-12402
    • Frelinger, A.L.1    Lam, S.C.-T.2    Plow, K.F.3    Smith, M.A.4    Loftus, J.C.5    Ginsberg, M.H.6
  • 10
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger, A. L., Du, X. P., Plow, K. F. and Ginsberg, M. H. (1991). Monoclonal antibodies to ligand-occupied conformers of integrin αIIbβ3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266, 17106-17111.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17106-17111
    • Frelinger, A.L.1    Du, X.P.2    Plow, K.F.3    Ginsberg, M.H.4
  • 11
    • 0026061621 scopus 로고
    • Monoclonal antibodies that inhibit binding of propolypeptide of von Willebrand factor to collagen. Localization of epitopes
    • Fujisawa, T., Takagi, J., Sekiya, F., Goto, A., Miake, F. and Saito, Y. (1991). Monoclonal antibodies that inhibit binding of propolypeptide of von Willebrand factor to collagen. Localization of epitopes. Eur. J. Biochem. 196, 673-677.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 673-677
    • Fujisawa, T.1    Takagi, J.2    Sekiya, F.3    Goto, A.4    Miake, F.5    Saito, Y.6
  • 12
    • 0021267104 scopus 로고
    • Glycoproteins of 210.000 and 130.000 m. w. on activated T cells: Cell distribution and antigenic relation to components on resting cells and T cell lines
    • Hemler, M. E., Sanchez-Madrid, F., Flotte, T. J., Krensky, A. M., Burakoff, S. J., Bhan, A. K., Springer, T. A. and Strominger, J. L. (1984). Glycoproteins of 210.000 and 130.000 m. w. on activated T cells: cell distribution and antigenic relation to components on resting cells and T cell lines. J. Immunol. 132, 3011-3018.
    • (1984) J. Immunol. , vol.132 , pp. 3011-3018
    • Hemler, M.E.1    Sanchez-Madrid, F.2    Flotte, T.J.3    Krensky, A.M.4    Burakoff, S.J.5    Bhan, A.K.6    Springer, T.A.7    Strominger, J.L.8
  • 13
    • 0025218924 scopus 로고
    • VLA proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler, M. K. (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.K.1
  • 14
    • 0028324995 scopus 로고
    • Ligand-induced adhesion to activated endothelium and to vascular cell adhesion molecule-I in lymphocytes transfected with the N-formyl peptide receptor
    • Honda, S., Campbell, J. J., Andrew, D. P., Engelhardt, B., Butcher, B. A., Warnock, R. A., Ye, R. D. and Butcher, K. C. (1994). Ligand-induced adhesion to activated endothelium and to vascular cell adhesion molecule-I in lymphocytes transfected with the N-formyl peptide receptor. J. Immunol. 152, 4026-4035.
    • (1994) J. Immunol. , vol.152 , pp. 4026-4035
    • Honda, S.1    Campbell, J.J.2    Andrew, D.P.3    Engelhardt, B.4    Butcher, B.A.5    Warnock, R.A.6    Ye, R.D.7    Butcher, K.C.8
  • 15
    • 0029039630 scopus 로고
    • Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit
    • Honda, S., Tomiyama, Y., Pelletier, A. J., Annis, D., Honda, Y., Orchekowski, R., Ruggeri, Z. and Kunicki, T. J. (1995). Topography of ligand-induced binding sites, including a novel cation-sensitive epitope (AP5) at the amino terminus, of the human integrin β3 subunit. J. Biol. Chem. 270, 11947-11954.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11947-11954
    • Honda, S.1    Tomiyama, Y.2    Pelletier, A.J.3    Annis, D.4    Honda, Y.5    Orchekowski, R.6    Ruggeri, Z.7    Kunicki, T.J.8
  • 16
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin, N. A. and Hall, A. (1995). The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131, 1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 17
    • 0030990436 scopus 로고    scopus 로고
    • Folding of the conserved domain but not of flanking regions in the integrin β2 subunit requires association with the α subunit
    • Huang, C., Lu, C. and Springer, T. A. (1997). Folding of the conserved domain but not of flanking regions in the integrin β2 subunit requires association with the α subunit. Proc. Nat. Acad. Sci. USA 94, 3156-3161.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 3156-3161
    • Huang, C.1    Lu, C.2    Springer, T.A.3
  • 19
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 20
    • 0030788570 scopus 로고    scopus 로고
    • Multiple loop structures critical for ligand binding of the integrin α4 subunit in the upper face of the β-propeller mode I
    • Irie, A., Kamata, T. and Takada, Y. (1997). Multiple loop structures critical for ligand binding of the integrin α4 subunit in the upper face of the β-propeller mode I. Proc. Nat. Acad. Sci. USA 94, 7198-7203.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 7198-7203
    • Irie, A.1    Kamata, T.2    Takada, Y.3
  • 22
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18)
    • Lee, J. O., Rieu, P., Arnaout, M. A. and Liddington, R. (1995). Crystal structure of the A domain from the alpha subunit of integrin CR3 (CD11b/CD18). Cell 80, 631-638.
    • (1995) Cell , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 23
    • 0030611706 scopus 로고    scopus 로고
    • Evidence that the integrin β3 and β5 subunits contain a metal ion-dependent adhesion site-like motif but lack an I domain
    • Lin, E. C. K., Ratnikov, B. I., Tsai, P. M., Gonzalez, E. R., McDonald, S., Pelletier, A. J. and Smith, J. W. (1997). Evidence that the integrin β3 and β5 subunits contain a metal ion-dependent adhesion site-like motif but lack an I domain. J. Biol. Chem. 272, 14236-14243.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14236-14243
    • Lin, E.C.K.1    Ratnikov, B.I.2    Tsai, P.M.3    Gonzalez, E.R.4    McDonald, S.5    Pelletier, A.J.6    Smith, J.W.7
  • 24
    • 0031569914 scopus 로고    scopus 로고
    • New insights into integrin-ligand interaction
    • Loftus, J. C. and Liddington, R. C. (1997). New insights into integrin-ligand interaction. J. Clin. Invest. 99, 2302-2306.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2302-2306
    • Loftus, J.C.1    Liddington, R.C.2
  • 25
    • 0027364840 scopus 로고
    • Direct evidence for two affinity states for lymphocyte function-associated antigen I on activated T cells
    • Lollo, B. A., Chan, K. W., Hanson, E. M., Moy, V. T. and Brian, A. A. (1993). Direct evidence for two affinity states for lymphocyte function-associated antigen I on activated T cells. J. Biol. Chem. 268, 21693-21700.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21693-21700
    • Lollo, B.A.1    Chan, K.W.2    Hanson, E.M.3    Moy, V.T.4    Brian, A.A.5
  • 26
    • 0028803769 scopus 로고
    • Distinct ligand binding sites in the I domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation
    • McGuire, S. L. and Bajt, M. L. (1995). Distinct ligand binding sites in the I domain of integrin αMβ2 that differentially affect a divalent cation-dependent conformation. J. Biol. Chem. 270, 25866-25871.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25866-25871
    • McGuire, S.L.1    Bajt, M.L.2
  • 27
    • 0029807068 scopus 로고    scopus 로고
    • Molecular requirements for assembly and function of a minimized human integrin αIIbβ3
    • McKay, B. S., Annis, D. S., Honda, S., Christie, D. and Kunicki, T. J. (1996). Molecular requirements for assembly and function of a minimized human integrin αIIbβ3. J. Biol. Chem. 271, 30544-30547.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30544-30547
    • McKay, B.S.1    Annis, D.S.2    Honda, S.3    Christie, D.4    Kunicki, T.J.5
  • 28
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto, S., Akiyama, S. K. and Yamada, K. M. (1995). Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267, 883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 29
    • 0019061918 scopus 로고
    • LIGAND: A versatile computerized approach for characterization of ligand-binding systems
    • Munson, P. J. and Rodbard, D. (1980). LIGAND: A versatile computerized approach for characterization of ligand-binding systems. Anal. Biochem. 107, 220-239.
    • (1980) Anal. Biochem. , vol.107 , pp. 220-239
    • Munson, P.J.1    Rodbard, D.2
  • 30
    • 0024293497 scopus 로고
    • Electron microscopy and structural model of human fibronectin receptor
    • Nermut, M. V., Green, N. M., Eason, P., Yamada, S. S. and Yamada, K. M. (1988). Electron microscopy and structural model of human fibronectin receptor. EMBO J. 7, 4093-4099.
    • (1988) EMBO J. , vol.7 , pp. 4093-4099
    • Nermut, M.V.1    Green, N.M.2    Eason, P.3    Yamada, S.S.4    Yamada, K.M.5
  • 32
    • 0029670835 scopus 로고    scopus 로고
    • Activation of the integrin αvβ3 involves a discrete cation-binding site that regulates conformation
    • Pelletier, A. J., Kunicki, T. and Quaranta, V. (1996). Activation of the integrin αvβ3 involves a discrete cation-binding site that regulates conformation. J. Biol. Chem. 271, 1364-1370.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1364-1370
    • Pelletier, A.J.1    Kunicki, T.2    Quaranta, V.3
  • 33
    • 0025904579 scopus 로고
    • GPIIb-IIIa: The responsive integrin
    • Phillips, D. R., Charo, I. F. and Scarborough, R. M. (1991). GPIIb-IIIa: the responsive integrin. Cell 65, 359-362.
    • (1991) Cell , vol.65 , pp. 359-362
    • Phillips, D.R.1    Charo, I.F.2    Scarborough, R.M.3
  • 34
    • 0022575551 scopus 로고
    • Temperature-dependent effects of Calcium on the membrane glycoprotein IIb-IIIa complex and platelet aggregability
    • Pidard, D., Didry, D., Kunicki, T. J. and Nurden, A. T. (1986). Temperature-dependent effects of Calcium on the membrane glycoprotein IIb-IIIa complex and platelet aggregability. Blood 67, 604-611.
    • (1986) Blood , vol.67 , pp. 604-611
    • Pidard, D.1    Didry, D.2    Kunicki, T.J.3    Nurden, A.T.4
  • 35
    • 0029953173 scopus 로고    scopus 로고
    • Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain
    • Puzon-McLaughlin, W., Yednock, T. A. and Takada, Y. (1996). Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain. J. Biol. Chem. 271, 16580-16585.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16580-16585
    • Puzon-McLaughlin, W.1    Yednock, T.A.2    Takada, Y.3
  • 36
    • 0029786408 scopus 로고    scopus 로고
    • Critical residues for ligand binding in an I domain-like structure of the integrin β subunit
    • Puzon-McLaughlin, W. and Takada, Y. (1996). Critical residues for ligand binding in an I domain-like structure of the integrin β subunit. J. Biol. Chem. 271, 20438-20443.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20438-20443
    • Puzon-McLaughlin, W.1    Takada, Y.2
  • 37
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin
    • Qu, A. and Leahy, D. J. (1995). Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, αLβ2) integrin. Proc. Nat. Acad. Sci. USA 92, 10277-10281.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 39
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., Hanks, S. K., Hunter, T. and van-der-Geer, P. (1994). Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372, 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van-der-Geer, P.4
  • 40
    • 0025745212 scopus 로고
    • Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α5β1, independent of cell shape
    • Schwartz, M. A., Lechene, C. and Ingber, D. E. (1991). Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α5β1, independent of cell shape. Proc. Nat. Acad. Sci. USA 88, 7849-7853.
    • (1991) Proc. Nat. Acad. Sci. USA , vol.88 , pp. 7849-7853
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 41
    • 0022180156 scopus 로고
    • Changes in the platelet membrane glycoprotein IIb-IIIa complex during platelel activation
    • Shattil, S. J., Hoxie, J. A., Cunningham, M. and Brass, L. F. (1985). Changes in the platelet membrane glycoprotein IIb-IIIa complex during platelel activation. J. Biol. Chem. 260, 11107-11114.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11107-11114
    • Shattil, S.J.1    Hoxie, J.A.2    Cunningham, M.3    Brass, L.F.4
  • 42
    • 0030878409 scopus 로고    scopus 로고
    • Integrin signaling in vascular biology
    • Shattil, S. J. and Ginsberg, M. H. (1997). Integrin signaling in vascular biology. J. Clin. Invest. 100, 1-5.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1-5
    • Shattil, S.J.1    Ginsberg, M.H.2
  • 43
    • 0025363922 scopus 로고
    • Regulated expression and binding of three VLA (β1) integrin receptors on T cells
    • Shimizu, Y., Van-Seventer, G. A., Horgan, K. J. and Shaw, S. (1990). Regulated expression and binding of three VLA (β1) integrin receptors on T cells. Nature 345, 250-253.
    • (1990) Nature , vol.345 , pp. 250-253
    • Shimizu, Y.1    Van-Seventer, G.A.2    Horgan, K.J.3    Shaw, S.4
  • 44
    • 0025781381 scopus 로고
    • Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex
    • Sims, P. J., Ginsberg, M. H., Plow, E. F. and Shattil, S. J. (1991). Effect of platelet activation on the conformation of the plasma membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 266, 7345-7352.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7345-7352
    • Sims, P.J.1    Ginsberg, M.H.2    Plow, E.F.3    Shattil, S.J.4
  • 45
    • 0031013031 scopus 로고    scopus 로고
    • Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain
    • Springer, T. A. (1997). Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain. Proc. Nat. Acad. Sci. USA 94, 65-72.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 65-72
    • Springer, T.A.1
  • 46
    • 0026460174 scopus 로고
    • A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques
    • Takada, Y., Ylanne, J., Mandelman, D., Puzon, W. and Ginsberg, M. H. (1992). A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques. J. Cell Biol. 119, 913-921.
    • (1992) J. Cell Biol. , vol.119 , pp. 913-921
    • Takada, Y.1    Ylanne, J.2    Mandelman, D.3    Puzon, W.4    Ginsberg, M.H.5
  • 47
    • 0030913268 scopus 로고    scopus 로고
    • Structural interlock between ligand binding site and stalk like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope
    • Takagi, J., Isobe, T., Takada, Y. and Saito, Y. (1997). Structural interlock between ligand binding site and stalk like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope. J. Biochem. 121, 914-921.
    • (1997) J. Biochem. , vol.121 , pp. 914-921
    • Takagi, J.1    Isobe, T.2    Takada, Y.3    Saito, Y.4
  • 48
    • 0029786892 scopus 로고    scopus 로고
    • Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit
    • Tozer, E. C., Liddington, R. C., Sutcliffe, M. J., Smeeton, A. H. and Loftus, J. C. (1996). Ligand binding to integrin αIIbβ3 is dependent on a MIDAS-like domain in the β3 subunit. J. Biol. Chem. 271, 21978-21984.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21978-21984
    • Tozer, E.C.1    Liddington, R.C.2    Sutcliffe, M.J.3    Smeeton, A.H.4    Loftus, J.C.5
  • 49
    • 0031029272 scopus 로고    scopus 로고
    • A structure prediction for the ligand-binding region of the integrin β subunit: Evidence for the presence of a von Willebrand factor A domain
    • Tuckwell, D. S. and Humphries, M. J. (1997). A structure prediction for the ligand-binding region of the integrin β subunit: evidence for the presence of a von Willebrand factor A domain. FEBS Lett. 400, 297-303.
    • (1997) FEBS Lett. , vol.400 , pp. 297-303
    • Tuckwell, D.S.1    Humphries, M.J.2
  • 50
    • 0026728176 scopus 로고
    • Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy
    • Weisel, J. W., Nagaswami, C., Vilaire, G. and Bennett, J. S. (1992). Examination of the platelet membrane glycoprotein IIb-IIIa complex and its interaction with fibrinogen and other ligands by electron microscopy. J. Biol. Chem. 267, 16637-16643.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16637-16643
    • Weisel, J.W.1    Nagaswami, C.2    Vilaire, G.3    Bennett, J.S.4
  • 51
    • 0028973093 scopus 로고
    • α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand
    • Yednock, T. A., Cannon, C., Vandevert, C., Goldbach, E. G., Shaw, G., Ellis, D. K., Liaw, C., Fritz, L. C. and Tanner, L. I. (1995). α4β1 integrin-dependent cell adhesion is regulated by a low affinity receptor pool that is conformationally responsive to ligand. J. Biol. Chem. 270, 28740-28750.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28740-28750
    • Yednock, T.A.1    Cannon, C.2    Vandevert, C.3    Goldbach, E.G.4    Shaw, G.5    Ellis, D.K.6    Liaw, C.7    Fritz, L.C.8    Tanner, L.I.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.