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Volumn 35, Issue 12, 2014, Pages 597-603

Force and affinity in ligand discrimination by the TCR

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR;

EID: 84915752670     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2014.10.007     Document Type: Review
Times cited : (31)

References (61)
  • 1
    • 84862628815 scopus 로고    scopus 로고
    • Photocrosslinkable pMHC monomers stain T cells specifically and cause ligand-bound TCRs to be 'preferentially' transported to the cSMAC
    • Xie J., et al. Photocrosslinkable pMHC monomers stain T cells specifically and cause ligand-bound TCRs to be 'preferentially' transported to the cSMAC. Nat. Immunol. 2012, 13:674-680.
    • (2012) Nat. Immunol. , vol.13 , pp. 674-680
    • Xie, J.1
  • 2
    • 84893837202 scopus 로고    scopus 로고
    • CD28 and CD3 have complementary roles in T-cell traction forces
    • Bashour K.T., et al. CD28 and CD3 have complementary roles in T-cell traction forces. Proc. Natl. Acad. Sci. U.S.A. 2014, 111:2241-2246.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 2241-2246
    • Bashour, K.T.1
  • 3
    • 84898644308 scopus 로고    scopus 로고
    • Accumulation of dynamic catch bonds between TCR and agonist peptide-MHC triggers T cell signaling
    • Liu B., et al. Accumulation of dynamic catch bonds between TCR and agonist peptide-MHC triggers T cell signaling. Cell 2014, 157:357-368.
    • (2014) Cell , vol.157 , pp. 357-368
    • Liu, B.1
  • 4
    • 0023917132 scopus 로고
    • The reaction-limited kinetics of membrane-to-surface adhesion and detachment
    • Dembo M., et al. The reaction-limited kinetics of membrane-to-surface adhesion and detachment. Proc. R. Soc. Lond. B: Biol. Sci. 1988, 234:55-83.
    • (1988) Proc. R. Soc. Lond. B: Biol. Sci. , vol.234 , pp. 55-83
    • Dembo, M.1
  • 5
    • 33646088314 scopus 로고    scopus 로고
    • Catch-bond model derived from allostery explains force-activated bacterial adhesion
    • Thomas W., et al. Catch-bond model derived from allostery explains force-activated bacterial adhesion. Biophys. J. 2006, 90:753-764.
    • (2006) Biophys. J. , vol.90 , pp. 753-764
    • Thomas, W.1
  • 6
    • 0028589333 scopus 로고
    • Kinetics of T-cell receptor binding to peptide/I-Ek complexes: correlation of the dissociation rate with T-cell responsiveness
    • Matsui K., et al. Kinetics of T-cell receptor binding to peptide/I-Ek complexes: correlation of the dissociation rate with T-cell responsiveness. Proc. Natl. Acad. Sci. U.S.A. 1994, 91:12862-12866.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12862-12866
    • Matsui, K.1
  • 7
    • 0032438551 scopus 로고    scopus 로고
    • High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling
    • Kersh G.J., et al. High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling. Immunity 1998, 9:817-826.
    • (1998) Immunity , vol.9 , pp. 817-826
    • Kersh, G.J.1
  • 8
    • 33845607123 scopus 로고    scopus 로고
    • Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling
    • Daniels M.A., et al. Thymic selection threshold defined by compartmentalization of Ras/MAPK signalling. Nature 2006, 444:724-729.
    • (2006) Nature , vol.444 , pp. 724-729
    • Daniels, M.A.1
  • 9
    • 0033082989 scopus 로고    scopus 로고
    • Qualitative and quantitative differences in T cell receptor binding of agonist and antagonist ligands
    • Alam S.M., et al. Qualitative and quantitative differences in T cell receptor binding of agonist and antagonist ligands. Immunity 1999, 10:227-237.
    • (1999) Immunity , vol.10 , pp. 227-237
    • Alam, S.M.1
  • 10
    • 0031283279 scopus 로고    scopus 로고
    • Alphabeta T cell receptor interactions with syngeneic and allogeneic ligands: affinity measurements and crystallization
    • Garcia K.C., et al. Alphabeta T cell receptor interactions with syngeneic and allogeneic ligands: affinity measurements and crystallization. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:13838-13843.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13838-13843
    • Garcia, K.C.1
  • 11
    • 77952712883 scopus 로고    scopus 로고
    • Fast on-rates allow short dwell time ligands to activate T cells
    • Govern C.C., et al. Fast on-rates allow short dwell time ligands to activate T cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:8724-8729.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 8724-8729
    • Govern, C.C.1
  • 12
    • 33645239805 scopus 로고    scopus 로고
    • Molecular flexibility can influence the stimulatory ability of receptor-ligand interactions at cell-cell junctions
    • Qi S., et al. Molecular flexibility can influence the stimulatory ability of receptor-ligand interactions at cell-cell junctions. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:4416-4421.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4416-4421
    • Qi, S.1
  • 13
    • 76949085272 scopus 로고    scopus 로고
    • Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time
    • Aleksic M., et al. Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time. Immunity 2010, 32:163-174.
    • (2010) Immunity , vol.32 , pp. 163-174
    • Aleksic, M.1
  • 14
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell G.I. Models for the specific adhesion of cells to cells. Science 1978, 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 15
    • 0035182368 scopus 로고    scopus 로고
    • Identification of self through two-dimensional chemistry and synapses
    • Dustin M.L., et al. Identification of self through two-dimensional chemistry and synapses. Annu. Rev. Cell Dev. Biol. 2001, 17:133-157.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 133-157
    • Dustin, M.L.1
  • 16
    • 0030927323 scopus 로고    scopus 로고
    • Making the T cell receptor go the distance: a topological view of T cell activation
    • Shaw A.S., Dustin M.L. Making the T cell receptor go the distance: a topological view of T cell activation. Immunity 1997, 6:361-369.
    • (1997) Immunity , vol.6 , pp. 361-369
    • Shaw, A.S.1    Dustin, M.L.2
  • 17
    • 0026641188 scopus 로고
    • Surface contact requirements for activation of cytotoxic T lymphocytes
    • Mescher M.F. Surface contact requirements for activation of cytotoxic T lymphocytes. J. Immunol. 1992, 149:2402-2405.
    • (1992) J. Immunol. , vol.149 , pp. 2402-2405
    • Mescher, M.F.1
  • 18
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith C.G., et al. The relationship between force and focal complex development. J. Cell Biol. 2002, 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1
  • 19
    • 67349114397 scopus 로고    scopus 로고
    • T cell antigen receptor signaling and immunological synapse stability require myosin IIA
    • Ilani T., et al. T cell antigen receptor signaling and immunological synapse stability require myosin IIA. Nat. Immunol. 2009, 10:531-539.
    • (2009) Nat. Immunol. , vol.10 , pp. 531-539
    • Ilani, T.1
  • 20
    • 0005448458 scopus 로고    scopus 로고
    • Polarity of T cell shape, motility, and sensitivity to antigen
    • Negulescu P.A., et al. Polarity of T cell shape, motility, and sensitivity to antigen. Immunity 1996, 4:421-430.
    • (1996) Immunity , vol.4 , pp. 421-430
    • Negulescu, P.A.1
  • 21
    • 71449090489 scopus 로고    scopus 로고
    • The alphabeta T cell receptor is an anisotropic mechanosensor
    • Kim S.T., et al. The alphabeta T cell receptor is an anisotropic mechanosensor. J. Biol. Chem. 2009, 284:31028-31037.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31028-31037
    • Kim, S.T.1
  • 22
    • 77953473256 scopus 로고    scopus 로고
    • Cutting edge: mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling
    • Li Y.C., et al. Cutting edge: mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling. J. Immunol. 2010, 184:5959-5963.
    • (2010) J. Immunol. , vol.184 , pp. 5959-5963
    • Li, Y.C.1
  • 23
    • 84856004728 scopus 로고    scopus 로고
    • Mechanosensing in T lymphocyte activation
    • Judokusumo E., et al. Mechanosensing in T lymphocyte activation. Biophys. J. 2012, 102:L5-L7.
    • (2012) Biophys. J. , vol.102 , pp. L5-L7
    • Judokusumo, E.1
  • 24
    • 84864131658 scopus 로고    scopus 로고
    • Substrate rigidity regulates human T cell activation and proliferation
    • O'Connor R.S., et al. Substrate rigidity regulates human T cell activation and proliferation. J. Immunol. 2012, 189:1330-1339.
    • (2012) J. Immunol. , vol.189 , pp. 1330-1339
    • O'Connor, R.S.1
  • 25
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: a molecular machine controlling T cell activation
    • Grakoui A., et al. The immunological synapse: a molecular machine controlling T cell activation. Science 1999, 285:221-227.
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1
  • 26
    • 84862998686 scopus 로고    scopus 로고
    • Hydrodynamic trapping of molecules in lipid bilayers
    • Jonsson P., et al. Hydrodynamic trapping of molecules in lipid bilayers. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:10328-10333.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 10328-10333
    • Jonsson, P.1
  • 27
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • Dustin M.L., et al. Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. J. Cell Biol. 1996, 132:465-474.
    • (1996) J. Cell Biol. , vol.132 , pp. 465-474
    • Dustin, M.L.1
  • 28
    • 36849016784 scopus 로고    scopus 로고
    • Quantification and modeling of tripartite CD2-, CD58FC chimera (Alefacept)-, and CD16-mediated cell adhesion
    • Dustin M.L., et al. Quantification and modeling of tripartite CD2-, CD58FC chimera (Alefacept)-, and CD16-mediated cell adhesion. J. Biol. Chem. 2007, 282:34748-34757.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34748-34757
    • Dustin, M.L.1
  • 29
    • 47749135219 scopus 로고    scopus 로고
    • Measuring diffusion and binding kinetics by contact area FRAP
    • Tolentino T.P., et al. Measuring diffusion and binding kinetics by contact area FRAP. Biophys. J. 2008, 95:920-930.
    • (2008) Biophys. J. , vol.95 , pp. 920-930
    • Tolentino, T.P.1
  • 30
    • 0027932728 scopus 로고
    • Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59
    • van der Merwe P.A., et al. Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59. Biochemistry 1994, 33:10149-10160.
    • (1994) Biochemistry , vol.33 , pp. 10149-10160
    • van der Merwe, P.A.1
  • 31
    • 84877071090 scopus 로고    scopus 로고
    • Theory and simulations of adhesion receptor dimerization on membrane surfaces
    • Wu Y., et al. Theory and simulations of adhesion receptor dimerization on membrane surfaces. Biophys. J. 2013, 104:1221-1229.
    • (2013) Biophys. J. , vol.104 , pp. 1221-1229
    • Wu, Y.1
  • 32
    • 79960897879 scopus 로고    scopus 로고
    • Transforming binding affinities from three dimensions to two with application to cadherin clustering
    • Wu Y., et al. Transforming binding affinities from three dimensions to two with application to cadherin clustering. Nature 2011, 475:510-513.
    • (2011) Nature , vol.475 , pp. 510-513
    • Wu, Y.1
  • 33
    • 84895891752 scopus 로고    scopus 로고
    • Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse
    • Choudhuri K., et al. Polarized release of T-cell-receptor-enriched microvesicles at the immunological synapse. Nature 2014, 507:118-123.
    • (2014) Nature , vol.507 , pp. 118-123
    • Choudhuri, K.1
  • 34
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • Huppa J.B., et al. TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity. Nature 2010, 463:963-967.
    • (2010) Nature , vol.463 , pp. 963-967
    • Huppa, J.B.1
  • 35
    • 84880089372 scopus 로고    scopus 로고
    • Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells
    • O'Donoghue G.P., et al. Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells. Elife 2013, 2:e00778.
    • (2013) Elife , vol.2 , pp. e00778
    • O'Donoghue, G.P.1
  • 36
    • 0031682733 scopus 로고    scopus 로고
    • Measuring two-dimensional receptor-ligand binding kinetics by micropipette
    • Chesla S.E., et al. Measuring two-dimensional receptor-ligand binding kinetics by micropipette. Biophys. J. 1998, 75:1553-1572.
    • (1998) Biophys. J. , vol.75 , pp. 1553-1572
    • Chesla, S.E.1
  • 37
    • 36749092326 scopus 로고    scopus 로고
    • Memory in receptor-ligand-mediated cell adhesion
    • Zarnitsyna V.I., et al. Memory in receptor-ligand-mediated cell adhesion. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:18037-18042.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 18037-18042
    • Zarnitsyna, V.I.1
  • 38
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • Huang J., et al. The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature 2010, 464:932-936.
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1
  • 39
    • 0023150401 scopus 로고
    • The T lymphocyte glycoprotein CD2 (LFA-2/T11/E-Rosette receptor) binds the cell surface ligand LFA-3
    • Selvaraj P., et al. The T lymphocyte glycoprotein CD2 (LFA-2/T11/E-Rosette receptor) binds the cell surface ligand LFA-3. Nature 1987, 326:400-403.
    • (1987) Nature , vol.326 , pp. 400-403
    • Selvaraj, P.1
  • 40
    • 0034714287 scopus 로고    scopus 로고
    • Binding sites of leukocyte beta 2 integrins (LFA-1, Mac-1) on the human ICAM-4/LW blood group protein
    • Hermand P., et al. Binding sites of leukocyte beta 2 integrins (LFA-1, Mac-1) on the human ICAM-4/LW blood group protein. J. Biol. Chem. 2000, 275:26002-26010.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26002-26010
    • Hermand, P.1
  • 41
    • 0035880255 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-4 binds alpha(4)beta(1) and alpha(V)-family integrins through novel integrin-binding mechanisms
    • Spring F.A., et al. Intercellular adhesion molecule-4 binds alpha(4)beta(1) and alpha(V)-family integrins through novel integrin-binding mechanisms. Blood 2001, 98:458-466.
    • (2001) Blood , vol.98 , pp. 458-466
    • Spring, F.A.1
  • 42
    • 34347210360 scopus 로고    scopus 로고
    • Using force to probe single-molecule receptor-cytoskeletal anchoring beneath the surface of a living cell
    • Evans E., Kinoshita K. Using force to probe single-molecule receptor-cytoskeletal anchoring beneath the surface of a living cell. Methods Cell Biol. 2007, 83:373-396.
    • (2007) Methods Cell Biol. , vol.83 , pp. 373-396
    • Evans, E.1    Kinoshita, K.2
  • 43
    • 84915754505 scopus 로고    scopus 로고
    • Coreceptor scanning by the T cell receptor provides a mechanism for T cell tolerance
    • Stepanek O., et al. Coreceptor scanning by the T cell receptor provides a mechanism for T cell tolerance. Cell 2014, 159:333-345.
    • (2014) Cell , vol.159 , pp. 333-345
    • Stepanek, O.1
  • 44
    • 84856020544 scopus 로고    scopus 로고
    • Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands
    • Robert P., et al. Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands. Biophys. J. 2012, 102:248-257.
    • (2012) Biophys. J. , vol.102 , pp. 248-257
    • Robert, P.1
  • 45
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • 2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 1985, 260:3440-3450.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1
  • 46
    • 34447647655 scopus 로고    scopus 로고
    • Spatial and temporal dynamics of T cell receptor signaling with a photoactivatable agonist
    • Huse M., et al. Spatial and temporal dynamics of T cell receptor signaling with a photoactivatable agonist. Immunity 2007, 27:76-88.
    • (2007) Immunity , vol.27 , pp. 76-88
    • Huse, M.1
  • 47
    • 0000810666 scopus 로고
    • Role of T3 surface molecules in human T-cell activation: T3-dependent activation results in an increase in cytoplasmic free calcium
    • Weiss A., et al. Role of T3 surface molecules in human T-cell activation: T3-dependent activation results in an increase in cytoplasmic free calcium. Proc. Natl. Acad. Sci. U.S.A. 1984, 81:4169-4173.
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4169-4173
    • Weiss, A.1
  • 48
    • 0028961573 scopus 로고
    • Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton
    • Valitutti S., et al. Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton. J. Exp. Med. 1995, 181:577-584.
    • (1995) J. Exp. Med. , vol.181 , pp. 577-584
    • Valitutti, S.1
  • 49
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • Varma R., et al. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 2006, 25:117-127.
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1
  • 50
    • 0037167816 scopus 로고    scopus 로고
    • Direct observation of ligand recognition by T cells
    • Irvine D.J., et al. Direct observation of ligand recognition by T cells. Nature 2002, 419:845-849.
    • (2002) Nature , vol.419 , pp. 845-849
    • Irvine, D.J.1
  • 51
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S., et al. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 2006, 441:179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1
  • 52
    • 0022607871 scopus 로고
    • Quantification of cell surface roughness; a method for studying cell mechanical and adhesive properties
    • Mege J.L., et al. Quantification of cell surface roughness; a method for studying cell mechanical and adhesive properties. J. Theor. Biol. 1986, 119:147-160.
    • (1986) J. Theor. Biol. , vol.119 , pp. 147-160
    • Mege, J.L.1
  • 53
    • 77950398569 scopus 로고    scopus 로고
    • Membrane nanotubes facilitate long-distance interactions between natural killer cells and target cells
    • Chauveau A., et al. Membrane nanotubes facilitate long-distance interactions between natural killer cells and target cells. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:5545-5550.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5545-5550
    • Chauveau, A.1
  • 54
    • 84903641324 scopus 로고    scopus 로고
    • Accumulation of serial forces on TCR and CD8 frequently applied by agonist antigenic peptides embedded in MHC molecules triggers calcium in T cells
    • Pryshchep S., et al. Accumulation of serial forces on TCR and CD8 frequently applied by agonist antigenic peptides embedded in MHC molecules triggers calcium in T cells. J. Immunol. 2014, 193:68-76.
    • (2014) J. Immunol. , vol.193 , pp. 68-76
    • Pryshchep, S.1
  • 55
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • McKeithan T.W. Kinetic proofreading in T-cell receptor signal transduction. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:5042-5046.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1
  • 56
    • 0037144842 scopus 로고    scopus 로고
    • T cell receptor ligation induces the formation of dynamically regulated signaling assemblies
    • Bunnell S.C., et al. T cell receptor ligation induces the formation of dynamically regulated signaling assemblies. J. Cell Biol. 2002, 158:1263-1275.
    • (2002) J. Cell Biol. , vol.158 , pp. 1263-1275
    • Bunnell, S.C.1
  • 57
    • 27544441784 scopus 로고    scopus 로고
    • Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling
    • Campi G., et al. Actin and agonist MHC-peptide complex-dependent T cell receptor microclusters as scaffolds for signaling. J. Exp. Med. 2005, 202:1031-1036.
    • (2005) J. Exp. Med. , vol.202 , pp. 1031-1036
    • Campi, G.1
  • 58
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature 1990, 346:425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 59
    • 0029140842 scopus 로고
    • Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells
    • van der Merwe P.A., et al. Topology of the CD2-CD48 cell-adhesion molecule complex: implications for antigen recognition by T cells. Curr. Biol. 1995, 5:74-84.
    • (1995) Curr. Biol. , vol.5 , pp. 74-84
    • van der Merwe, P.A.1
  • 60
    • 42049101786 scopus 로고    scopus 로고
    • The receptor deformation model of TCR triggering
    • Ma Z., et al. The receptor deformation model of TCR triggering. FASEB J. 2008, 22:1002-1008.
    • (2008) FASEB J. , vol.22 , pp. 1002-1008
    • Ma, Z.1
  • 61
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • Lillemeier B.F., et al. TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat. Immunol. 2010, 11:90-96.
    • (2010) Nat. Immunol. , vol.11 , pp. 90-96
    • Lillemeier, B.F.1


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