메뉴 건너뛰기




Volumn 12, Issue 1, 2000, Pages 23-34

The role of lipid rafts in T cell antigen receptor (TCR) signalling

Author keywords

Lipid rafts; Protein tyrosine kinase (PTK); Signal transduction; T cell antigen receptor (TCR)

Indexed keywords

CD45 ANTIGEN; CHOLESTEROL; LIPID; MEMBRANE LIPID; MEMBRANE PROTEIN; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 0033998793     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1006/smim.2000.0204     Document Type: Article
Times cited : (376)

References (72)
  • 1
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol. 14:1998;111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 2
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature. 394:1998;798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 3
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson RGW. The caveolae membrane system. Annu Rev Biochem. 67:1998;199-225.
    • (1998) Annu Rev Biochem , vol.67 , pp. 199-225
    • Anderson, R.G.W.1
  • 5
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra AM, Williamson E, Simons K, Parton RG. De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc Natl Acad Sci USA. 92:1995;8655-8659.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 8
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers W, Crise B, Rose JK. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol Cell Biol. 14:1994;5384-5391.
    • (1994) Mol Cell Biol , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 9
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang W, Trible RP, Samelson LE. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity. 9:1998;239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 10
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 92:1998;83-92.
    • (1998) Cell , vol.92 , pp. 83-92
    • Zhang, W.1    Sloan-Lancaster, J.2    Kitchen, J.3    Trible, R.P.4    Samelson, L.E.5
  • 11
    • 0032576969 scopus 로고    scopus 로고
    • Compartmentalization of phosphatidylinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin
    • Liu Y, Casey L, Pike LJ. Compartmentalization of phosphatidylinositol 4,5-bisphosphate in low-density membrane domains in the absence of caveolin. Biochem Biophys Res Comm. 245:1998;684-690.
    • (1998) Biochem Biophys Res Comm , vol.245 , pp. 684-690
    • Liu, Y.1    Casey, L.2    Pike, L.J.3
  • 12
    • 0032878516 scopus 로고    scopus 로고
    • Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment
    • Shan X, Wange RL. Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment. J Biol Chem. 274:1999;29323-29330.
    • (1999) J Biol Chem , vol.274 , pp. 29323-29330
    • Shan, X.1    Wange, R.L.2
  • 13
  • 15
    • 0031570462 scopus 로고    scopus 로고
    • Phosphatidylinositol-based glycolipid-anchored proteins enhance proximal TCR signaling events
    • Romagnoli P, Bron C. Phosphatidylinositol-based glycolipid-anchored proteins enhance proximal TCR signaling events. J Immunol. 158:1997;5757-5764.
    • (1997) J Immunol , vol.158 , pp. 5757-5764
    • Romagnoli, P.1    Bron, C.2
  • 17
    • 0027986678 scopus 로고
    • Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif
    • Koegl M, Zlatkine P, Ley SC, Courtneidge SA, Magee AI. Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif. Biochem J. 303:1994;749-753.
    • (1994) Biochem J , vol.303 , pp. 749-753
    • Koegl, M.1    Zlatkine, P.2    Ley, S.C.3    Courtneidge, S.A.4    Magee, A.I.5
  • 18
    • 0030746106 scopus 로고    scopus 로고
    • S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes
    • Kabouridis PS, Magee AI, Ley SC. S-acylation of LCK protein tyrosine kinase is essential for its signalling function in T lymphocytes. EMBO J. 16:1997;4983-4998.
    • (1997) EMBO J , vol.16 , pp. 4983-4998
    • Kabouridis, P.S.1    Magee, A.I.2    Ley, S.C.3
  • 20
    • 0033538474 scopus 로고    scopus 로고
    • New insights into the interaction of Ras with the plasma membrane
    • Magee T, Marshall C. New insights into the interaction of Ras with the plasma membrane. Cell. 98:1999;9-12.
    • (1999) Cell , vol.98 , pp. 9-12
    • Magee, T.1    Marshall, C.2
  • 21
    • 0033147405 scopus 로고    scopus 로고
    • Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis el egans
    • Scheel J, Srinivasan J, Honnert U, Henske A, Kurzchalia TV. Involvement of caveolin-1 in meiotic cell-cycle progression in Caenorhabditis el egans. Nature Cell Biol. 1:1999;127-129.
    • (1999) Nature Cell Biol , vol.1 , pp. 127-129
    • Scheel, J.1    Srinivasan, J.2    Honnert, U.3    Henske, A.4    Kurzchalia, T.V.5
  • 24
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compart mentation is required for efficient T cell activation
    • Xavier R, Brennan T, Li Q, McCormack C, Seed B. Membrane compart mentation is required for efficient T cell activation. Immunity. 8:1998;723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 25
    • 0342713043 scopus 로고    scopus 로고
    • T cell receptor signalling results in rapid tyrosine phosphorylation of the linker protein LAT present in detergent-resistant membrane microdomains
    • Brdicka T, Cerny J, Horejsi V. T cell receptor signalling results in rapid tyrosine phosphorylation of the linker protein LAT present in detergent-resistant membrane microdomains. Biochem Biophys Res Commun. 248:1998;356-360.
    • (1998) Biochem Biophys Res Commun , vol.248 , pp. 356-360
    • Brdicka, T.1    Cerny, J.2    Horejsi, V.3
  • 26
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown DA, London E. Structure and origin of ordered lipid domains in biological membranes. J Membr Biol. 164:1998;103-114.
    • (1998) J Membr Biol , vol.164 , pp. 103-114
    • Brown, D.A.1    London, E.2
  • 28
    • 0032938740 scopus 로고    scopus 로고
    • Microdomain-dependent regulation of Lck and Fyn protein tyrosine kinases in T lymphocyte plasma membranes
    • Ilangumaran S, Arni S, van Echten-Deckert G, Hoessli DC. Microdomain-dependent regulation of Lck and Fyn protein tyrosine kinases in T lymphocyte plasma membranes. Mol Biol Cell. 10:1999;891-905.
    • (1999) Mol Biol Cell , vol.10 , pp. 891-905
    • Ilangumaran, S.1    Arni, S.2    Van, E.-D.G.3    Hoessli, D.C.4
  • 29
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • Rodgers W, Rose JK. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. J Cell Biol. 135:1996;1515-1523.
    • (1996) J Cell Biol , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 30
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra AM, Williamson E, Simons K, Parton RG. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J Biol Chem. 269:1994;30745-30748.
    • (1994) J Biol Chem , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 31
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder T, Scheiffele P, Verkade P, Simons K. Lipid domain structure of the plasma membrane revealed by patching of membrane components. J Cell Biol. 141:1998;929-942.
    • (1998) J Cell Biol , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 32
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signalling via the T cell antigen receptor
    • Janes P, Ley SC, Magee AI. Aggregation of lipid rafts accompanies signalling via the T cell antigen receptor. J Cell Biol. 147:1999;447-461.
    • (1999) J Cell Biol , vol.147 , pp. 447-461
    • Janes, P.1    Ley, S.C.2    Magee, A.I.3
  • 33
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the l ck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus DB, Weiss A. Genetic evidence for the involvement of the l ck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell. 70:1992;585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 34
    • 0028352175 scopus 로고
    • Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins
    • Thomas JL, Holowka D, Baird B, Webb WW. Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J Cell Biol. 125:1994;795-802.
    • (1994) J Cell Biol , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 35
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer TP, Meyer T. Compartmentalized IgE receptor-mediated signal transduction in living cells. J Cell Biol. 139:1997;1447-1454.
    • (1997) J Cell Biol , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 36
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field KA, Holowka D, Baird B. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J Biol Chem. 272:1997;4276-4280.
    • (1997) J Biol Chem , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 37
    • 0031962079 scopus 로고    scopus 로고
    • Rapid redistribution of CD20 to a low density detergent-insoluble membrane compartment
    • Deans JP, Robbins SM, Polyak MJ, Savage JA. Rapid redistribution of CD20 to a low density detergent-insoluble membrane compartment. J Biol Chem. 273:1998;344-348.
    • (1998) J Biol Chem , vol.273 , pp. 344-348
    • Deans, J.P.1    Robbins, S.M.2    Polyak, M.J.3    Savage, J.A.4
  • 38
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder T, Simons K. Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur J Immunol. 29:1999;556-562.
    • (1999) Eur J Immunol , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 39
    • 85031639054 scopus 로고    scopus 로고
    • Kabouridis, PS, Janzen, J, Magee, AI, Ley, SC, 1999
    • Kabouridis, PS, Janzen, J, Magee, AI, Ley, SC, 1999.
  • 40
    • 0030814765 scopus 로고    scopus 로고
    • Signal transduction via glycosyl phosphatidylinositol-anchored proteins in T cells is inhibited by lowering cholesterol
    • Stulnig TM, Berger M, Sigmund T, Stockinger H, Horejsi V, Waldhausl W. Signal transduction via glycosyl phosphatidylinositol-anchored proteins in T cells is inhibited by lowering cholesterol. J Biol Chem. 272:1997;19242-19247.
    • (1997) J Biol Chem , vol.272 , pp. 19242-19247
    • Stulnig, T.M.1    Berger, M.2    Sigmund, T.3    Stockinger, H.4    Horejsi, V.5    Waldhausl, W.6
  • 41
    • 0032476714 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids inhibit T cell signal transduction by modification of detergent-insoluble membrane domains
    • Stulnig TM, Berger M, Sigmund T, Raederstorff D, Stockinger H, Waldhausl W. Polyunsaturated fatty acids inhibit T cell signal transduction by modification of detergent-insoluble membrane domains. J Cell Biol. 143:1998;637-644.
    • (1998) J Cell Biol , vol.143 , pp. 637-644
    • Stulnig, T.M.1    Berger, M.2    Sigmund, T.3    Raederstorff, D.4    Stockinger, H.5    Waldhausl, W.6
  • 42
    • 0033577805 scopus 로고    scopus 로고
    • Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcRI and their association with detergent-resistant membranes
    • Sheets ED, Holowka D, Baird B. Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcRI and their association with detergent-resistant membranes. J Cell Biol. 145:1999;877-887.
    • (1999) J Cell Biol , vol.145 , pp. 877-887
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 43
    • 0027248384 scopus 로고
    • 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibition in a rat mast cell line
    • Shakarjian MP, Eiseman E, Penhallow RC, Bolen JB. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase inhibition in a rat mast cell line. J Biol Chem. 268:1993;15252-15259.
    • (1993) J Biol Chem , vol.268 , pp. 15252-15259
    • Shakarjian, M.P.1    Eiseman, E.2    Penhallow, R.C.3    Bolen, J.B.4
  • 44
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi T, Anderson RGW. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J Biol Chem. 273:1998;21099-21104.
    • (1998) J Biol Chem , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.W.2
  • 46
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • Pingel J, Thomas ML. Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell. 58:1989;1055-1065.
    • (1989) Cell , vol.58 , pp. 1055-1065
    • Pingel, J.1    Thomas, M.L.2
  • 47
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyinositol pathway
    • Koretzky GA, Picus J, Thomas ML, Weiss A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyinositol pathway. Nature. 346:1990;66-68.
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 48
    • 0033558102 scopus 로고    scopus 로고
    • The CD45 tyrosine phosphatase is an inhibit or of Lck activity in thymocytes
    • D'Oro U, Ashwell JD. The CD45 tyrosine phosphatase is an inhibit or of Lck activity in thymocytes. J Immunol. 162:1999;1879-1883.
    • (1999) J Immunol , vol.162 , pp. 1879-1883
    • D'Oro, U.1    Ashwell, J.D.2
  • 49
    • 0033178727 scopus 로고    scopus 로고
    • CD45 negatively regulates Lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells
    • Katagiri T, Ogimoto M, Hasegawa K, Arimura Y, Mitomo K, Okada M, Clark MR, Mizuno K, Yakura H. CD45 negatively regulates Lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells. J Immunol. 163:1999;1321-1326.
    • (1999) J Immunol , vol.163 , pp. 1321-1326
    • Katagiri, T.1    Ogimoto, M.2    Hasegawa, K.3    Arimura, Y.4    Mitomo, K.5    Okada, M.6    Clark, M.R.7    Mizuno, K.8    Yakura, H.9
  • 52
    • 0028278702 scopus 로고
    • Cell calcium signaling via GM1 cell surface gangliosides in the human jurkat T cell line
    • Gouy H, Deterre P, Debre P, Bismuth G. Cell calcium signaling via GM1 cell surface gangliosides in the human jurkat T cell line. J Immunol. 152:1994;3271-3281.
    • (1994) J Immunol , vol.152 , pp. 3271-3281
    • Gouy, H.1    Deterre, P.2    Debre, P.3    Bismuth, G.4
  • 53
    • 0032986606 scopus 로고    scopus 로고
    • The regulation of antigen-receptor signaling by protein tyrosine phosphatases: A hole in the story
    • Thomas ML. The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story. Curr Opin Immun. 11:1999;270-276.
    • (1999) Curr Opin Immun , vol.11 , pp. 270-276
    • Thomas, M.L.1
  • 54
    • 0030946259 scopus 로고    scopus 로고
    • Reconstitution of interactions between protein tyrosine phosphatase CD45 and tyrosine protein kinase p56lck in nonlymphoid cells
    • Gervais FG, Veillette A. Reconstitution of interactions between protein tyrosine phosphatase CD45 and tyrosine protein kinase p56lck in nonlymphoid cells. J Biol Chem. 272:1997;12754-12761.
    • (1997) J Biol Chem , vol.272 , pp. 12754-12761
    • Gervais, F.G.1    Veillette, A.2
  • 55
    • 0027997103 scopus 로고
    • Specific interaction of the CD45 protein tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain
    • Furukawa T, Itoh M, Krueger NX, Streuli M, Saito H. Specific interaction of the CD45 protein tyrosine phosphatase with tyrosine phosphorylated CD3 ζ chain. Proc Natl Acad Sci USA. 91:1994;10928-10932.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10928-10932
    • Furukawa, T.1    Itoh, M.2    Krueger, N.X.3    Streuli, M.4    Saito, H.5
  • 57
    • 0009013817 scopus 로고
    • CD45 regulates signal transduction and lymphocyte activation by specific association with receptor molecules on T or B cells
    • Ledbetter JA, Tonks NK, Fischer EH, Clark EA. CD45 regulates signal transduction and lymphocyte activation by specific association with receptor molecules on T or B cells. Proc Natl Acad Sci USA. 85:1988;8628-8632.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8628-8632
    • Ledbetter, J.A.1    Tonks, N.K.2    Fischer, E.H.3    Clark, E.A.4
  • 58
    • 0026536632 scopus 로고
    • CD45 modulates T cell receptor/CD3-induced activation of human thymocytes via regulation of tyrosine phosphorylation
    • Turka LA, Kanner SB, Schieven GL, Thompson CB, Ledbetter JA. CD45 modulates T cell receptor/CD3-induced activation of human thymocytes via regulation of tyrosine phosphorylation. Eur J Immunol. 22:1992;551-557.
    • (1992) Eur J Immunol , vol.22 , pp. 551-557
    • Turka, L.A.1    Kanner, S.B.2    Schieven, G.L.3    Thompson, C.B.4    Ledbetter, J.A.5
  • 60
    • 0023905133 scopus 로고
    • Thy-1 a nd Ly-6-mediated lymphokine production and growth inhibition of a T cell hybridoma require co-expression of the T cell antigen receptor complex
    • Sussman JJ, Saito T, Shevach EM, Germain RN, Ashwell JD. Thy-1 a nd Ly-6-mediated lymphokine production and growth inhibition of a T cell hybridoma require co-expression of the T cell antigen receptor complex. J Immunol. 140:1988;2520-2526.
    • (1988) J Immunol , vol.140 , pp. 2520-2526
    • Sussman, J.J.1    Saito, T.2    Shevach, E.M.3    Germain, R.N.4    Ashwell, J.D.5
  • 61
    • 0026079656 scopus 로고
    • CD59 functions as a signal-transducing molecule for human T cell activation
    • Korty PE, Brando C, Shevach EM. CD59 functions as a signal-transducing molecule for human T cell activation. J Immunol. 146:1991;4092-4098.
    • (1991) J Immunol , vol.146 , pp. 4092-4098
    • Korty, P.E.1    Brando, C.2    Shevach, E.M.3
  • 62
    • 0029060404 scopus 로고
    • The glycosylphosphatidylinositol-anchored CD59 protein stimulates both T cell receptor-ζ / ZAP-70-dependent and -independent signaling pathways in T cells
    • Deckert M, Ticchioni M, Mari B, Mary D, Bernard A. The glycosylphosphatidylinositol-anchored CD59 protein stimulates both T cell receptor-ζ / ZAP-70-dependent and -independent signaling pathways in T cells. Eur J Immunol. 25:1995;1815-1822.
    • (1995) Eur J Immunol , vol.25 , pp. 1815-1822
    • Deckert, M.1    Ticchioni, M.2    Mari, B.3    Mary, D.4    Bernard, A.5
  • 63
    • 0028889177 scopus 로고
    • An alternative way of CD4 and CD8 association with protein kinases of the Src family
    • Cinek T, Hilgert I, Horejsi V. An alternative way of CD4 and CD8 association with protein kinases of the Src family. Immunogen. 41:1995;110-116.
    • (1995) Immunogen , vol.41 , pp. 110-116
    • Cinek, T.1    Hilgert, I.2    Horejsi, V.3
  • 65
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganisation of membrane microdomains
    • Viola A, Schroeder S, Sakakibara Y, Lanzavecchia A. T lymphocyte costimulation mediated by reorganisation of membrane microdomains. Science. 283:1999;680-682.
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 66
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks CRF, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature. 395:1998;82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.F.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 68
    • 0030927323 scopus 로고    scopus 로고
    • Making the T cell receptor go the distance: A topological view of T cell activation
    • Shaw AS, Dustin ML. Making the T cell receptor go the distance: a topological view of T cell activation. Immunity. 6:1997;361-369.
    • (1997) Immunity , vol.6 , pp. 361-369
    • Shaw, A.S.1    Dustin, M.L.2
  • 69
    • 0029930984 scopus 로고    scopus 로고
    • The structure and ligand interactions of CD2: Implications for T cell function
    • Davis SJ, van der Merwe PA. The structure and ligand interactions of CD2: implications for T cell function. Immunol Today. 17:1996;177-187.
    • (1996) Immunol Today , vol.17 , pp. 177-187
    • Davis, S.J.1    Van, D.M.P.2
  • 70
    • 0032534304 scopus 로고    scopus 로고
    • TCR signalling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site
    • Sperling AI, Sedy JR, Manjunath N, Kupfer A, Ardman B, Burkhardt JK. TCR signalling induces selective exclusion of CD43 from the T cell-antigen-presenting cell contact site. J Immunol. 161:1998;6459-6462.
    • (1998) J Immunol , vol.161 , pp. 6459-6462
    • Sperling, A.I.1    Sedy, J.R.2    Manjunath, N.3    Kupfer, A.4    Ardman, B.5    Burkhardt, J.K.6
  • 71
    • 0032545218 scopus 로고    scopus 로고
    • A receptor/cytoskeletal movement triggered by costimulation during T cell activation
    • Wulfing C, Davis MM. A receptor/cytoskeletal movement triggered by costimulation during T cell activation. Science. 282:1998;2266-2269.
    • (1998) Science , vol.282 , pp. 2266-2269
    • Wulfing, C.1    Davis, M.M.2
  • 72
    • 0033010661 scopus 로고    scopus 로고
    • Genetic analysis of B cell antigen receptor signalling
    • Kurosaki T. Genetic analysis of B cell antigen receptor signalling. Annu Rev Immunol. 17:1999;555-592.
    • (1999) Annu Rev Immunol , vol.17 , pp. 555-592
    • Kurosaki, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.