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Volumn 19, Issue 1, 1999, Pages 1-24

CD28/CTLA-4 and CD80/CD86 families

Author keywords

Cell surface molecules; Costimulatory molecules; Signal transduction; T lymphocytes

Indexed keywords

B7 ANTIGEN; CD28 ANTIGEN; CD86 ANTIGEN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; MEMBRANE ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; RAS PROTEIN; T LYMPHOCYTE RECEPTOR;

EID: 0033062691     PISSN: 0257277X     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02786473     Document Type: Review
Times cited : (160)

References (198)
  • 1
    • 0026541544 scopus 로고
    • The two-signal model of lymphocyte activation twenty-one years later
    • Bretscher P: The two-signal model of lymphocyte activation twenty-one years later. Immunol Today 1992;13:74-76.
    • (1992) Immunol Today , vol.13 , pp. 74-76
    • Bretscher, P.1
  • 2
    • 0027087331 scopus 로고
    • Costimulation of T lymphocytes: The role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy
    • Schwartz RH: Costimulation of T lymphocytes: The role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy. Cell 1992;71:1065-1068.
    • (1992) Cell , vol.71 , pp. 1065-1068
    • Schwartz, R.H.1
  • 3
    • 0025339511 scopus 로고
    • A cell culture model for T lymphocyte clonal anergy
    • Schwartz RH: A cell culture model for T lymphocyte clonal anergy. Science 1990;248:1349-1356.
    • (1990) Science , vol.248 , pp. 1349-1356
    • Schwartz, R.H.1
  • 5
    • 0027403299 scopus 로고
    • The role of the CD28 receptor during T cell responses to antigen
    • Linsley PS, Ledbetter JA. The role of the CD28 receptor during T cell responses to antigen. Ann Rev Immunol 1993;11:191-212.
    • (1993) Ann Rev Immunol , vol.11 , pp. 191-212
    • Linsley, P.S.1    Ledbetter, J.A.2
  • 7
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y: Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 1992;258:607-614.
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 9
    • 0030884739 scopus 로고    scopus 로고
    • Evidence that a kinase distinct from protein kinase C and phosphatidylinositol 3-kinase mediates ligation-dependent serine/threonine phosphorylation of the T-lymphocyte co-stimulatory receptor CD28
    • Parry RV, Olive D, Westwick J, Sansom DM, Ward SG: Evidence that a kinase distinct from protein kinase C and phosphatidylinositol 3-kinase mediates ligation-dependent serine/threonine phosphorylation of the T-lymphocyte co-stimulatory receptor CD28. Biochem J 1997;326:249-257.
    • (1997) Biochem J , vol.326 , pp. 249-257
    • Parry, R.V.1    Olive, D.2    Westwick, J.3    Sansom, D.M.4    Ward, S.G.5
  • 10
    • 0028675006 scopus 로고
    • Human B7-1 (CD80) and B7-2 (CD86) bind with similar avidities but distinct kinetics to CD28 and CTLA-4 receptors
    • Linsley PS, Greene JL, Brady W, Bajorath J, Ledbetter JA, Peach R: Human B7-1 (CD80) and B7-2 (CD86) bind with similar avidities but distinct kinetics to CD28 and CTLA-4 receptors. Immunity 1994;793-801.
    • (1994) Immunity , pp. 793-801
    • Linsley, P.S.1    Greene, J.L.2    Brady, W.3    Bajorath, J.4    Ledbetter, J.A.5    Peach, R.6
  • 11
    • 0027057908 scopus 로고
    • CTLA-4 and CD28 mRNA are coexpressed in most T cells after activation. Expression of CTLA-4 and CD28 mRNA does not correlate with the pattern of lymphokine production
    • Freeman GJ, Lombard DB, Gimmi CD, Brod SA, Lee K, Laning JC, et al.: CTLA-4 and CD28 mRNA are coexpressed in most T cells after activation. Expression of CTLA-4 and CD28 mRNA does not correlate with the pattern of lymphokine production. J Immunol 1992;149(12):3795-3801.
    • (1992) J Immunol , vol.149 , Issue.12 , pp. 3795-3801
    • Freeman, G.J.1    Lombard, D.B.2    Gimmi, C.D.3    Brod, S.A.4    Lee, K.5    Laning, J.C.6
  • 12
    • 0026486220 scopus 로고
    • Coexpression and functional cooperativity of CTLA-4 and CD28 mRNA on activated T lymphocytes
    • Linsley PS, Greene JL, Tan P, Bradshaw J, Ledbetter JA, Anasetti C, et al.: Coexpression and functional cooperativity of CTLA-4 and CD28 mRNA on activated T lymphocytes. J Exp Med 1992;176:1595-1604.
    • (1992) J Exp Med , vol.176 , pp. 1595-1604
    • Linsley, P.S.1    Greene, J.L.2    Tan, P.3    Bradshaw, J.4    Ledbetter, J.A.5    Anasetti, C.6
  • 15
    • 0028910221 scopus 로고
    • CTLA-4 binding to the lipid kinase phosphatidylinositol 3-Kinase in T cells
    • Schneider H, Prasad KVS, Shoelson SE, Rudd CE: CTLA-4 binding to the lipid kinase phosphatidylinositol 3-Kinase in T cells. J Exp Med 1995;181:351-355.
    • (1995) J Exp Med , vol.181 , pp. 351-355
    • Schneider, H.1    Prasad, K.V.S.2    Shoelson, S.E.3    Rudd, C.E.4
  • 16
    • 0028852073 scopus 로고
    • Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail
    • Leung HT, Bradshaw J, Cleaveland JS, Linsley PS: Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail. J Biol Chem 1995;270:25,107-25,114.
    • (1995) J Biol Chem , vol.270 , pp. 25107-25114
    • Leung, H.T.1    Bradshaw, J.2    Cleaveland, J.S.3    Linsley, P.S.4
  • 17
    • 0030443168 scopus 로고    scopus 로고
    • Regulation of surface and intracellular expression of CTLA4 on mouse T cells
    • Alegre M, Noel PJ, Eisfelder BJ, Chuang E, Clark M, Reiner SL, et al.: Regulation of surface and intracellular expression of CTLA4 on mouse T cells. J Immunol 1996;157:4762-4770.
    • (1996) J Immunol , vol.157 , pp. 4762-4770
    • Alegre, M.1    Noel, P.J.2    Eisfelder, B.J.3    Chuang, E.4    Clark, M.5    Reiner, S.L.6
  • 18
    • 0030917081 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls internaliztion of CTLA-4 by regulating its interaction with clathrin-associated adapter complex AP-2
    • Shiratori T, Miyatake S, Ohno H, Nakadeko C, Isono K, Bonifacino JS, et al.: Tyrosine phosphorylation controls internaliztion of CTLA-4 by regulating its interaction with clathrin-associated adapter complex AP-2. Immunity 1997;6:583-589.
    • (1997) Immunity , vol.6 , pp. 583-589
    • Shiratori, T.1    Miyatake, S.2    Ohno, H.3    Nakadeko, C.4    Isono, K.5    Bonifacino, J.S.6
  • 19
    • 0030611358 scopus 로고    scopus 로고
    • Interaction of CTLA-4 with AP50, a clathrin-coated pit adapter protein
    • Zhang Y, Allison JP: Interaction of CTLA-4 with AP50, a clathrin-coated pit adapter protein. Proc Natl Acad Sci USA 1997;94:9273-9278.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9273-9278
    • Zhang, Y.1    Allison, J.P.2
  • 20
  • 21
    • 0020069605 scopus 로고
    • B lymphoblast antigen (BB-1) expressed on Epstein-Barr virus-activated B cell blasts, B lymphoblstoid cell lines, and Burkitt's lymphomas
    • Yokochi T, Holly RD, Clark EA: B lymphoblast antigen (BB-1) expressed on Epstein-Barr virus-activated B cell blasts, B lymphoblstoid cell lines, and Burkitt's lymphomas. J Immunol 1982;128(2):823-828.
    • (1982) J Immunol , vol.128 , Issue.2 , pp. 823-828
    • Yokochi, T.1    Holly, R.D.2    Clark, E.A.3
  • 22
    • 0025322552 scopus 로고
    • T-cell antigen CD28 mediates adhesion with B cells by interacting with activation antigen B7/BB-1
    • Linsley PS, Clark EA, Ledbetter JA. T-cell antigen CD28 mediates adhesion with B cells by interacting with activation antigen B7/BB-1. Proc Natl Acad Sci USA 1990;87:5031-5035.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5031-5035
    • Linsley, P.S.1    Clark, E.A.2    Ledbetter, J.A.3
  • 23
    • 0024444165 scopus 로고
    • B7, a new member of the 1g superfamily with unique expression on activated and neoplastic B cells
    • Freeman GJ, Freedman AS, Segil JM, Lee G, Whitman JF, Nadler L: B7, a new member of the 1g superfamily with unique expression on activated and neoplastic B cells. J Immunol 1989;143:2714-2722.
    • (1989) J Immunol , vol.143 , pp. 2714-2722
    • Freeman, G.J.1    Freedman, A.S.2    Segil, J.M.3    Lee, G.4    Whitman, J.F.5    Nadler, L.6
  • 24
    • 0025873393 scopus 로고
    • Structure, expression, and T cell costimulatory activity of the murine homologue of the human B lymphocyte activation antigen B7
    • Freeman GJ, Gray GS, Gimmi CD, Lombard DB, Zhou, L-J, Whiite M, et al.: Structure, expression, and T cell costimulatory activity of the murine homologue of the human B lymphocyte activation antigen B7. J Exp Med 1991;174(3):625-631.
    • (1991) J Exp Med , vol.174 , Issue.3 , pp. 625-631
    • Freeman, G.J.1    Gray, G.S.2    Gimmi, C.D.3    Lombard, D.B.4    Zhou, L.-J.5    Whiite, M.6
  • 25
    • 0032530373 scopus 로고    scopus 로고
    • Two regions in the CD80 cytoplasmic tail regulate CD80 redistribution and T cell costimulation
    • Doty RT, Clark EA: Two regions in the CD80 cytoplasmic tail regulate CD80 redistribution and T cell costimulation. J Immunol 1998;161:2700-2707.
    • (1998) J Immunol , vol.161 , pp. 2700-2707
    • Doty, R.T.1    Clark, E.A.2
  • 26
    • 0029914089 scopus 로고    scopus 로고
    • Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions
    • Greene JL, Leytze GM, Emswiler J, Peach R, Bajorath J, Cosand W, et al.: Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions. J Biol Chem 1996;271(43):26,762-26,771.
    • (1996) J Biol Chem , vol.271 , Issue.43 , pp. 26762-26771
    • Greene, J.L.1    Leytze, G.M.2    Emswiler, J.3    Peach, R.4    Bajorath, J.5    Cosand, W.6
  • 27
    • 0030587897 scopus 로고    scopus 로고
    • Subcellular localization of CD80 receptors is dependent on an intact cytoplasmic tail and is required for CD28-dependent T cell costimulation
    • Doty RT, Clark EA: Subcellular localization of CD80 receptors is dependent on an intact cytoplasmic tail and is required for CD28-dependent T cell costimulation. J Immunol 1996;157:3270-3279.
    • (1996) J Immunol , vol.157 , pp. 3270-3279
    • Doty, R.T.1    Clark, E.A.2
  • 28
    • 0028198569 scopus 로고
    • Molecular cloning and expression of early T cell costimulatory molecule-1 and its characterization as B7-2 molecule
    • Chen C, Gault A, Shen L, Nabavi N: Molecular cloning and expression of early T cell costimulatory molecule-1 and its characterization as B7-2 molecule. J Immunol 1994; 152:4929-4936.
    • (1994) J Immunol , vol.152 , pp. 4929-4936
    • Chen, C.1    Gault, A.2    Shen, L.3    Nabavi, N.4
  • 29
    • 0027360332 scopus 로고
    • Murine B7-2, an alternative CTLA4 counter-receptor that costimulates T cell proliferation and interleukin 2 production
    • Freeman GJ, Boriello F, Hodes RJ, Resier H, Gribben JG, Ng JW, et al.: Murine B7-2, an alternative CTLA4 counter-receptor that costimulates T cell proliferation and interleukin 2 production. J Exp Med 1993;178:2185-2192.
    • (1993) J Exp Med , vol.178 , pp. 2185-2192
    • Freeman, G.J.1    Boriello, F.2    Hodes, R.J.3    Resier, H.4    Gribben, J.G.5    Ng, J.W.6
  • 30
  • 34
    • 0028337459 scopus 로고
    • Comparative analysis of B7-1 and B7-2 costimulatory ligands:expression and function
    • Hathcock KS, Laszlo G, Pucillo C, Linsley P, Hodes RJ: Comparative analysis of B7-1 and B7-2 costimulatory ligands:expression and function. J Exp Med 1994;180:631-641.
    • (1994) J Exp Med , vol.180 , pp. 631-641
    • Hathcock, K.S.1    Laszlo, G.2    Pucillo, C.3    Linsley, P.4    Hodes, R.J.5
  • 35
    • 0027362633 scopus 로고
    • Activated human B lymphocytes express three CTLA4 binding counter-receptors which costimulate T cell activation
    • Boussiotis VA, Freeman GJ, Gribben JG, Daley J, Gray, GS, Nadler LM.: Activated human B lymphocytes express three CTLA4 binding counter-receptors which costimulate T cell activation. Prove Natl Acad Sci USA 1993;90:11,059-11,063.
    • (1993) Prove Natl Acad Sci USA , vol.90 , pp. 11059-11063
    • Boussiotis, V.A.1    Freeman, G.J.2    Gribben, J.G.3    Daley, J.4    Gray, G.S.5    Nadler, L.M.6
  • 36
    • 0028298047 scopus 로고
    • Resting and anergic B cells are defective in CD28-dependent costimulation of naive CD4+ T cells
    • Ho WY, Cooke MP, Goodnow CC, Davis MM: Resting and anergic B cells are defective in CD28-dependent costimulation of naive CD4+ T cells. J Exp Med 1995;179:1539-1549.
    • (1995) J Exp Med , vol.179 , pp. 1539-1549
    • Ho, W.Y.1    Cooke, M.P.2    Goodnow, C.C.3    Davis, M.M.4
  • 37
    • 0027499535 scopus 로고
    • Ranheim EA,Kipps TJ: Activated T cells induce expression of B7/BB1 on normal or leukemic B cells through a CD40-dependent signal
    • Ranheim EA,Kipps TJ: Activated T cells induce expression of B7/BB1 on normal or leukemic B cells through a CD40-dependent signal. J Exp Med 1993;177:925.
    • (1993) J Exp Med , vol.177 , pp. 925
  • 38
    • 0028935411 scopus 로고
    • Studies on the interdependence of gp39 and B7 expression and function during antigen-specific immune responses
    • Roy M, Aruffo A, Ledbetter J, Linsley P, Kehry M, Noelle R: Studies on the interdependence of gp39 and B7 expression and function during antigen-specific immune responses. Eur J Immunol 1995;25:596-603.
    • (1995) Eur J Immunol , vol.25 , pp. 596-603
    • Roy, M.1    Aruffo, A.2    Ledbetter, J.3    Linsley, P.4    Kehry, M.5    Noelle, R.6
  • 39
    • 0032530275 scopus 로고    scopus 로고
    • The BB1 monoclonal antibody recognizes both cell surface CD74 (MHC class II-associated invariant chain) its well its B7-1 (CD80), resolving the question regarding a third CD28/CTLA-4 counterreceptor
    • Freeman GJ, Cardoso AA, Boussiotis VA, Anumanthan A, Groves RW, Kupper TS, et al.: The BB1 monoclonal antibody recognizes both cell surface CD74 (MHC class II-associated invariant chain) its well its B7-1 (CD80), resolving the question regarding a third CD28/CTLA-4 counterreceptor. J Immunol 1998;161:2708-2715.
    • (1998) J Immunol , vol.161 , pp. 2708-2715
    • Freeman, G.J.1    Cardoso, A.A.2    Boussiotis, V.A.3    Anumanthan, A.4    Groves, R.W.5    Kupper, T.S.6
  • 40
    • 0025907438 scopus 로고
    • IL-4 and IL-2 upregulate the expression of antigen B7, the B cell counterstructure to T cell CD28: An amplification mechanism for T-B interactions
    • Valle A, Aubry JP, Durnad I, Bancheraue J: IL-4 and IL-2 upregulate the expression of antigen B7, the B cell counterstructure to T cell CD28: An amplification mechanism for T-B interactions. Int Immunol 1991;2:229-235.
    • (1991) Int Immunol , vol.2 , pp. 229-235
    • Valle, A.1    Aubry, J.P.2    Durnad, I.3    Bancheraue, J.4
  • 41
    • 0028181231 scopus 로고
    • IL-4 treatment of small splenic B cells induces costimulatory molecules B7-1 and B7-2
    • Stack RM, Lenschlow DJ, Gray GS, Bluestone JA, Fitch FW: IL-4 treatment of small splenic B cells induces costimulatory molecules B7-1 and B7-2. J Immunol 1994;152:5723-5733.
    • (1994) J Immunol , vol.152 , pp. 5723-5733
    • Stack, R.M.1    Lenschlow, D.J.2    Gray, G.S.3    Bluestone, J.A.4    Fitch, F.W.5
  • 42
    • 0029086123 scopus 로고
    • Interleukin 10 differentially regulates B7-1 (CD80) and B7-2 (CD86) expression on human peripheral blood dendritic cells
    • Bulens C, Willems F, Delvaux A, Picrard G, Delville J-P, Velu T, et al.: Interleukin 10 differentially regulates B7-1 (CD80) and B7-2 (CD86) expression on human peripheral blood dendritic cells. Eur J Immunol 1995;25:2421-2426.
    • (1995) Eur J Immunol , vol.25 , pp. 2421-2426
    • Bulens, C.1    Willems, F.2    Delvaux, A.3    Picrard, G.4    Delville, J.-P.5    Velu, T.6
  • 44
    • 0029883005 scopus 로고    scopus 로고
    • Differential recognition by CD28 of its cognate counter receptors CD80 (B7.1) and B70 (B7.2):analysis by site directed mutagenesis
    • Truneh A, Reddy M, Ryan P, Lyn SD, Eichman C, Couez D, et al.: Differential recognition by CD28 of its cognate counter receptors CD80 (B7.1) and B70 (B7.2):analysis by site directed mutagenesis. Mol Immunol 1996;33(3):321-334.
    • (1996) Mol Immunol , vol.33 , Issue.3 , pp. 321-334
    • Truneh, A.1    Reddy, M.2    Ryan, P.3    Lyn, S.D.4    Eichman, C.5    Couez, D.6
  • 45
    • 0029133256 scopus 로고    scopus 로고
    • Both extracellular immunoglobulin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28
    • Peach RJ, Bajorath J, Naemura J, Leytze G, Greene J, Aruffo A, et al.: Both extracellular immunoglobulin-like domains of CD80 contain residues critical for binding T cell surface receptors CTLA-4 and CD28. J Biol Chem 1996;270:21181-21187.
    • (1996) J Biol Chem , vol.270 , pp. 21181-21187
    • Peach, R.J.1    Bajorath, J.2    Naemura, J.3    Leytze, G.4    Greene, J.5    Aruffo, A.6
  • 46
    • 0029951647 scopus 로고    scopus 로고
    • Analysis of the site of interaction of CD28 with its counter-receptors CD80 and CD86 and correlation with function
    • Kariv I, Truneh A, Sweet R: Analysis of the site of interaction of CD28 with its counter-receptors CD80 and CD86 and correlation with function. J Immunol 1996: 29-38.
    • (1996) J Immunol , pp. 29-38
    • Kariv, I.1    Truneh, A.2    Sweet, R.3
  • 48
    • 0029089750 scopus 로고
    • Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA-4
    • Fargeas CA, Truneh A, Reddy M, Hurle M, Sweet R, Sekaly R-P: Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA-4. J Exp Med 1995;182:667-675.
    • (1995) J Exp Med , vol.182 , pp. 667-675
    • Fargeas, C.A.1    Truneh, A.2    Reddy, M.3    Hurle, M.4    Sweet, R.5    Sekaly, R.-P.6
  • 49
    • 0027937702 scopus 로고
    • Complementarity determining region 1 (CDR1)- and CDR3-analagous regions in CTLA-4 and CD28 determine the binding to B7-1
    • Peach RJ, Bajorath J, Brady W, Leytze G, Greene J, Naemura J, et al.: Complementarity determining region 1 (CDR1)- and CDR3-analagous regions in CTLA-4 and CD28 determine the binding to B7-1. J Exp Med 1994;180:2049-2058.
    • (1994) J Exp Med , vol.180 , pp. 2049-2058
    • Peach, R.J.1    Bajorath, J.2    Brady, W.3    Leytze, G.4    Greene, J.5    Naemura, J.6
  • 52
    • 0027729845 scopus 로고
    • Uncovering of functional alternative CTLA-4 counter-receptor in B7-deficient mice
    • Freeman GJ, Borriello R, Hodes RJ, Reiser H, S. HK, Laszlo G, et al.: Uncovering of functional alternative CTLA-4 counter-receptor in B7-deficient mice. Science 1993;262:907-909.
    • (1993) Science , vol.262 , pp. 907-909
    • Freeman, G.J.1    Borriello, R.2    Hodes, R.J.3    Reiser, H.4    Hk, S.5    Laszlo, G.6
  • 53
    • 0030936275 scopus 로고    scopus 로고
    • B7-1 and B7-2 have overlapping, critical roles in immunoglobulin class switching and germinal center formation
    • Borrielo F, Sethna MP, Boyd SD, Schweitzer AN, Tivol EA, Jacoby D, Strom TB, et al.: B7-1 and B7-2 have overlapping, critical roles in immunoglobulin class switching and germinal center formation. Immunity 1997:303-313.
    • (1997) Immunity , pp. 303-313
    • Borrielo, F.1    Sethna, M.P.2    Boyd, S.D.3    Schweitzer, A.N.4    Tivol, E.A.5    Jacoby, D.6    Strom, T.B.7
  • 54
    • 0032530746 scopus 로고    scopus 로고
    • Studies using antigen-presenting cells lacking expression of both B7-1 (CD80) and B7-2 (CD86) show distinct requirements for B7 molecules during priming versus restimulation of Th2 but not Th1 cytokine production
    • Schweitzer AN, Sharpe AH: Studies using antigen-presenting cells lacking expression of both B7-1 (CD80) and B7-2 (CD86) show distinct requirements for B7 molecules during priming versus restimulation of Th2 but not Th1 cytokine production. J Immunol 1998;161:2762-2771.
    • (1998) J Immunol , vol.161 , pp. 2762-2771
    • Schweitzer, A.N.1    Sharpe, A.H.2
  • 55
    • 0023637951 scopus 로고
    • T-cell proliferation involving the CD28 pathway is associated with cyclosporine-resistant interleukin 2 gene expression
    • June CH, Ledbetter JA, Gillespie MM, Lindsten T, Thompson CB: T-cell proliferation involving the CD28 pathway is associated with cyclosporine-resistant interleukin 2 gene expression. Mol Cell Biol 1987;7(12):4472-4481.
    • (1987) Mol Cell Biol , vol.7 , Issue.12 , pp. 4472-4481
    • June, C.H.1    Ledbetter, J.A.2    Gillespie, M.M.3    Lindsten, T.4    Thompson, C.B.5
  • 57
    • 0028237348 scopus 로고
    • CD28-B7 interactions in T-cell activation
    • Allison JP: CD28-B7 interactions in T-cell activation. Curr Opinion Immunol 1994;6:414-419.
    • (1994) Curr Opinion Immunol , vol.6 , pp. 414-419
    • Allison, J.P.1
  • 58
    • 0028979466 scopus 로고
    • New perspectives of CD28-B7-mediated T cell costimulation
    • Bluestone JA: New perspectives of CD28-B7-mediated T cell costimulation. Immunity 1995;2:555-559.
    • (1995) Immunity , vol.2 , pp. 555-559
    • Bluestone, J.A.1
  • 59
    • 0029874657 scopus 로고    scopus 로고
    • T cell antigen receptor signal transduction pathways
    • Cantrell D: T cell antigen receptor signal transduction pathways. Annu Rev Immunol 1996;14:259-574.
    • (1996) Annu Rev Immunol , vol.14 , pp. 259-574
    • Cantrell, D.1
  • 60
    • 0025233576 scopus 로고
    • Genetic and mutational analysis of the T cell antigen receptor
    • Ashwell JD, Klausner RD: Genetic and mutational analysis of the T cell antigen receptor. Ann Rev Immunol 1990;8:139-167.
    • (1990) Ann Rev Immunol , vol.8 , pp. 139-167
    • Ashwell, J.D.1    Klausner, R.D.2
  • 61
  • 62
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth M: Antigen receptor tail clue. Nature 1989;338:383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 64
    • 0026067057 scopus 로고
    • Stimulation through the TCR/CD3 complex up-regulates the CD2 surface expression on human T-lymphocytes
    • Alberola-Ila J, Places L, de la Calle O, Romero M, Yagüe J, Gallart T, et al.: Stimulation through the TCR/CD3 complex up-regulates the CD2 surface expression on human T-lymphocytes. J Immunol 1991;146:1085-1092.
    • (1991) J Immunol , vol.146 , pp. 1085-1092
    • Alberola-Ila, J.1    Places, L.2    De la Calle, O.3    Romero, M.4    Yagüe, J.5    Gallart, T.6
  • 65
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kD protein-tyrosine that associates with the TCR ζ chain
    • Chan AC, Iwashima M, Turck CW, Weiss A: ZAP-70: A 70 kD protein-tyrosine that associates with the TCR ζ chain. Cell 1992;71:649-662.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 67
    • 0025835006 scopus 로고
    • T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-γ1
    • Secrist JP, Karnitz L, Abraham RT. T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-γ1. J Biol Chem 1991;266:12,135.
    • (1991) J Biol Chem , vol.266 , pp. 12135
    • Secrist, J.P.1    Karnitz, L.2    Abraham, R.T.3
  • 68
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss A, Littman DR: Signal transduction by lymphocyte antigen receptors. Cell 1994;76:263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 69
    • 0026018057 scopus 로고
    • CD3 stimulation causes phosphorylation of phospholipase Cγ1 on serine and tyrosine residues in a human T cell line
    • Park DJ, Rho HW, Rhee SG: CD3 stimulation causes phosphorylation of phospholipase Cγ1 on serine and tyrosine residues in a human T cell line. Proc Natl Acad Sci USA 1991;88:5453-5457.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5453-5457
    • Park, D.J.1    Rho, H.W.2    Rhee, S.G.3
  • 71
    • 0028208969 scopus 로고
    • Ligation of the T cell receptor complex results in activation of the Ras/Raf-1/MEK/MAPK cascade in human T lymphocytes
    • Franklin RA, Tordai A, Patel H, Gardner AM, Johnson GL, Gelfand EW: Ligation of the T cell receptor complex results in activation of the Ras/Raf-1/MEK/MAPK cascade in human T lymphocytes. J Clin Invest 1994;93:2134-2140.
    • (1994) J Clin Invest , vol.93 , pp. 2134-2140
    • Franklin, R.A.1    Tordai, A.2    Patel, H.3    Gardner, A.M.4    Johnson, G.L.5    Gelfand, E.W.6
  • 72
    • 0027212082 scopus 로고
    • How receptors turn Ras on
    • McKormick F: How receptors turn Ras on. Nature 1993;363:15,16.
    • (1993) Nature , vol.363 , pp. 1516
    • McKormick, F.1
  • 74
  • 75
    • 0032054723 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase (JNK) - from inflammation to development
    • Ip YT, Davis RJ: Signal transduction by the c-Jun N-terminal kinase (JNK) - from inflammation to development. Curr Opinion Cell Biol 1998;10:205-219.
    • (1998) Curr Opinion Cell Biol , vol.10 , pp. 205-219
    • Ip, Y.T.1    Davis, R.J.2
  • 76
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • Cano E, Mahadevan LC: Parallel signal processing among mammalian MAPKs. Trends Biochem Sci 1995;20:117-122.
    • (1995) Trends Biochem Sci , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2
  • 77
    • 0029777285 scopus 로고    scopus 로고
    • Multiple p21ras effector pathways regulate nuclear factor of activated T cells
    • Genot E, Cleverley S, Henning S, Cantrell D: Multiple p21ras effector pathways regulate nuclear factor of activated T cells. EMBO J 1996;15:3923-3933.
    • (1996) EMBO J , vol.15 , pp. 3923-3933
    • Genot, E.1    Cleverley, S.2    Henning, S.3    Cantrell, D.4
  • 78
    • 0029991920 scopus 로고    scopus 로고
    • Blocked Ras activation in anergic CD4+ T cells
    • Fields PE, Gajewski TF, Fitch FW: Blocked Ras activation in anergic CD4+ T cells. Science 1996;271:1276-1278.
    • (1996) Science , vol.271 , pp. 1276-1278
    • Fields, P.E.1    Gajewski, T.F.2    Fitch, F.W.3
  • 79
    • 0032080849 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy
    • DeSilva DR, Jones EA, Favata MF, Jaffee BD, Magolda RL, Trzaskos JM, et al.: Inhibition of mitogen-activated protein kinase kinase blocks T cell proliferation but does not induce or prevent anergy. J Immunol 1998;160:4175-4181.
    • (1998) J Immunol , vol.160 , pp. 4175-4181
    • DeSilva, D.R.1    Jones, E.A.2    Favata, M.F.3    Jaffee, B.D.4    Magolda, R.L.5    Trzaskos, J.M.6
  • 81
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAPK cascades
    • Vojtek AB, Cooper JA: Rho family members: Activators of MAPK cascades. Cell 1995;82:527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.B.1    Cooper, J.A.2
  • 82
    • 0031916832 scopus 로고    scopus 로고
    • Selective Activation of p38 Mitogen-activated (MAP) kinase isoforms by the MAPK kinases MKK3 and MKK6
    • Enslen H, Raingeaud J, Davis RJ: Selective Activation of p38 Mitogen-activated (MAP) kinase isoforms by the MAPK kinases MKK3 and MKK6. J Biol Chem 1998;273(3):1741-1748.
    • (1998) J Biol Chem , vol.273 , Issue.3 , pp. 1741-1748
    • Enslen, H.1    Raingeaud, J.2    Davis, R.J.3
  • 83
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAPK kinase (MKK6)
    • Han J, Lee, JD, Jiang Y, Li Z, Feng L, Ulevitch RJ: Characterization of the structure and function of a novel MAPK kinase (MKK6). J Biol Chem 1996;271:2886-2891.
    • (1996) J Biol Chem , vol.271 , pp. 2886-2891
    • Han, J.1    Lee, J.D.2    Jiang, Y.3    Li, Z.4    Feng, L.5    Ulevitch, R.J.6
  • 84
    • 0028291525 scopus 로고
    • Jnk is involved in signal integration during costimulation of T lymphocytes
    • Su B, Jacinto E, Hibi M, Kallunki T, Karin M, Ben-Neriah Y: Jnk is involved in signal integration during costimulation of T lymphocytes. Cell 1994;77:727-736.
    • (1994) Cell , vol.77 , pp. 727-736
    • Su, B.1    Jacinto, E.2    Hibi, M.3    Kallunki, T.4    Karin, M.5    Ben-Neriah, Y.6
  • 85
    • 0031903616 scopus 로고    scopus 로고
    • Co-stimulation-dependent activation of a JNK-kinase in T lymphocytes
    • Avraham A, Jung S, Samuels Y, Seger R, Ben-Neriah Y: Co-stimulation-dependent activation of a JNK-kinase in T lymphocytes. Eur J Immunol 1998;28(8):2320-2330.
    • (1998) Eur J Immunol , vol.28 , Issue.8 , pp. 2320-2330
    • Avraham, A.1    Jung, S.2    Samuels, Y.3    Seger, R.4    Ben-Neriah, Y.5
  • 86
    • 0029043582 scopus 로고
    • How MAPKs are regulated
    • Cobb MH, Goldsmith EJ: How MAPKs are regulated. J Biol Chem 1995;270:14,843-14,846.
    • (1995) J Biol Chem , vol.270 , pp. 14843-14846
    • Cobb, M.H.1    Goldsmith, E.J.2
  • 87
    • 0023017930 scopus 로고
    • Antibody binding to CD5 (Tp67) and Tp44 T cell surface molecules: Effects on cyclic nucleotides, cytoplasmic free calcium, and cAMP-mediated suppression
    • Ledbetter JA, Parsons M, Martin PJ, Hansen JA, Rabinovich PS, June CH: Antibody binding to CD5 (Tp67) and Tp44 T cell surface molecules: Effects on cyclic nucleotides, cytoplasmic free calcium, and cAMP-mediated suppression. J Immunol 1986;137:3299-3305.
    • (1986) J Immunol , vol.137 , pp. 3299-3305
    • Ledbetter, J.A.1    Parsons, M.2    Martin, P.J.3    Hansen, J.A.4    Rabinovich, P.S.5    June, C.H.6
  • 89
    • 0029814079 scopus 로고    scopus 로고
    • CD28: A signalling perspective
    • Ward SG: CD28: A signalling perspective. Biochem J 1996;318:361-377.
    • (1996) Biochem J , vol.318 , pp. 361-377
    • Ward, S.G.1
  • 90
    • 0027086431 scopus 로고
    • CD28 receptor crosslinking induces tyrosine phosphorylation of PLC gamma 1
    • Ledbetter JA, Linsley PS: CD28 receptor crosslinking induces tyrosine phosphorylation of PLC gamma 1. Adv Exp Med Biol 1992;323:23-27.
    • (1992) Adv Exp Med Biol , vol.323 , pp. 23-27
    • Ledbetter, J.A.1    Linsley, P.S.2
  • 91
    • 0028940428 scopus 로고
    • Inhibition of CD28-mediated T cell costimulation by the phosphoinositide 3-kinase inhibitor wortmannin
    • Ward SG, Wilson A, Turner L, Westwick J, Sansom DM: Inhibition of CD28-mediated T cell costimulation by the phosphoinositide 3-kinase inhibitor wortmannin. Eur J Immunol 1995;25: 526-532.
    • (1995) Eur J Immunol , vol.25 , pp. 526-532
    • Ward, S.G.1    Wilson, A.2    Turner, L.3    Westwick, J.4    Sansom, D.M.5
  • 92
    • 0028203261 scopus 로고
    • Activation-dependent phosphorylation of the T-lymphocyte surface receptor CD28 and associated proteins
    • Hutchcroft JE, Bierer BE: Activation-dependent phosphorylation of the T-lymphocyte surface receptor CD28 and associated proteins. Proc Natl Acad Sci USA 1994;91: 3260-3264.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3260-3264
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 93
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling
    • Pages F, Ragueneau M, Rottapel R, Trunch A, Nunes J, Imbert J, et al.: Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling. Nature 1994;369:327-329.
    • (1994) Nature , vol.369 , pp. 327-329
    • Pages, F.1    Ragueneau, M.2    Rottapel, R.3    Trunch, A.4    Nunes, J.5    Imbert, J.6
  • 94
    • 0028304143 scopus 로고
    • Activation of src family kinase Ick following CD28 crosslinking in the Jurkat leukemic cell line
    • August A, Dupont B: Activation of src family kinase Ick following CD28 crosslinking in the Jurkat leukemic cell line. Biochem Biophys Res Commun 1994;199: 1466-1473.
    • (1994) Biochem Biophys Res Commun , vol.199 , pp. 1466-1473
    • August, A.1    Dupont, B.2
  • 95
    • 0026453395 scopus 로고
    • Itk, a T-cell-specific tyrosine kinase gene inducible by interleukin 2
    • Siliciano JD, Marrow TA, Desiderio SV: Itk, a T-cell-specific tyrosine kinase gene inducible by interleukin 2. Proc Natl Acad Sci USA 1992;89:11,194-11,198.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11194-11198
    • Siliciano, J.D.1    Marrow, T.A.2    Desiderio, S.V.3
  • 96
    • 0027393602 scopus 로고
    • Developmental regulation of a murine T cell-specific tyrosine kinase gene, Tsk
    • Heyeck SD, Berg LJ: Developmental regulation of a murine T cell-specific tyrosine kinase gene, Tsk. Proc Nat Acad Sci USA 1993;90:669-673.
    • (1993) Proc Nat Acad Sci USA , vol.90 , pp. 669-673
    • Heyeck, S.D.1    Berg, L.J.2
  • 97
    • 0027217937 scopus 로고
    • Identification, cloning and characterization of a novel human T cell specific kinase located at the hematopoeitin complex on chromosome 5q
    • Gibson S, Leung B, Squire JA, Hill A, Arima N, Goss P, et al.: Identification, cloning and characterization of a novel human T cell specific kinase located at the hematopoeitin complex on chromosome 5q. Blood 1993;82:1561-1572.
    • (1993) Blood , vol.82 , pp. 1561-1572
    • Gibson, S.1    Leung, B.2    Squire, J.A.3    Hill, A.4    Arima, N.5    Goss, P.6
  • 98
    • 0027399081 scopus 로고
    • Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia
    • Tsukada S, Saffran DC, Rawlings DJ, Parolini O, Allen RC, Klisak I, et al.: Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell 1993;72:279.
    • (1993) Cell , vol.72 , pp. 279
    • Tsukada, S.1    Saffran, D.C.2    Rawlings, D.J.3    Parolini, O.4    Allen, R.C.5    Klisak, I.6
  • 99
    • 0025603722 scopus 로고
    • A novel protein-tyrosine kinase, tec, is preferentially expressed in liver
    • Mano H, Ishikama F, Nishida J, Hirai H, Takaku F: A novel protein-tyrosine kinase, tec, is preferentially expressed in liver. Oncogene 1990;5:1781-1786.
    • (1990) Oncogene , vol.5 , pp. 1781-1786
    • Mano, H.1    Ishikama, F.2    Nishida, J.3    Hirai, H.4    Takaku, F.5
  • 100
    • 0028292588 scopus 로고
    • TXK, a novel human tyrosine kinase expressed in T cells shares sequence homology with Tec family kinases and maps to chromosome 4p12
    • Haire RN, Ohta Y, Lewis JE, Fu SM, Kroisel P, Littman GW: TXK, a novel human tyrosine kinase expressed in T cells shares sequence homology with Tec family kinases and maps to chromosome 4p12. Hum Mol Genet 1994;3:897-901.
    • (1994) Hum Mol Genet , vol.3 , pp. 897-901
    • Haire, R.N.1    Ohta, Y.2    Lewis, J.E.3    Fu, S.M.4    Kroisel, P.5    Littman, G.W.6
  • 101
    • 0027944227 scopus 로고
    • BMX, a novel nonreceptor tyrosine kinase of the BTK/ITK/TEC/TXK family located in chromosome Xp22.2
    • Tamagnone L, Lahtinen I, Mustonen T, Virtaneva K, Francis F, Muscatelli F, et al.: BMX, a novel nonreceptor tyrosine kinase of the BTK/ITK/TEC/TXK family located in chromosome Xp22.2. Oncogene 1994;9:3683-3688.
    • (1994) Oncogene , vol.9 , pp. 3683-3688
    • Tamagnone, L.1    Lahtinen, I.2    Mustonen, T.3    Virtaneva, K.4    Francis, F.5    Muscatelli, F.6
  • 102
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon MA, Ferguson KM, Schlessinger J: PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 1996;85:621-624.
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 103
    • 0028146530 scopus 로고
    • CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of tile Tee family kinase Itk/Emt in the human Jurkat leukemic T cell line
    • August A, Gibson S, Kawakami Y, Kawakami T, Mills GB, Dupont B: CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of tile Tee family kinase Itk/Emt in the human Jurkat leukemic T cell line. Proc Natl Acad Sci USA 1994;91:9347-9351.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9347-9351
    • August, A.1    Gibson, S.2    Kawakami, Y.3    Kawakami, T.4    Mills, G.B.5    Dupont, B.6
  • 104
    • 0031255110 scopus 로고    scopus 로고
    • The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28
    • Marengere LEM, Okkenhaug K, Clavrcul A, Couez D, Gibson S, Mills GB, et al.: The SH3 domain of Itk/Emt binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28. J Immunol 1997;159:3220-3229.
    • (1997) J Immunol , vol.159 , pp. 3220-3229
    • Marengere, L.E.M.1    Okkenhaug, K.2    Clavrcul, A.3    Couez, D.4    Gibson, S.5    Mills, G.B.6
  • 105
    • 0028981212 scopus 로고
    • p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine ITK: Implications for T-cell costimulation
    • Raab M, Cai Y-C, Bunnell SC, Heyeck SD, Berg LJ, Rudd CE: p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine ITK: Implications for T-cell costimulation. Proc Natl Acad Sci USA 1995;92:8891-8895.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8891-8895
    • Raab, M.1    Cai, Y.-C.2    Bunnell, S.C.3    Heyeck, S.D.4    Berg, L.J.5    Rudd, C.E.6
  • 106
    • 0029989312 scopus 로고    scopus 로고
    • Functional Ick is required for optimal CD28-mediated activation of the TEC family tyrosine kinase EMT/Itk
    • Gibson S, August A, Branch D, Dupont B, Mills GB: Functional Ick is required for optimal CD28-mediated activation of the TEC family tyrosine kinase EMT/Itk. J Biol Chem 1996;271(12):7079-7083.
    • (1996) J Biol Chem , vol.271 , Issue.12 , pp. 7079-7083
    • Gibson, S.1    August, A.2    Branch, D.3    Dupont, B.4    Mills, G.B.5
  • 107
    • 0030798980 scopus 로고    scopus 로고
    • Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity
    • Heyeck SD, Wilcox HM, Bunnell SC, Berg LJ: Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity. J Biol Chem 1997;272(40):25,401-25,408.
    • (1997) J Biol Chem , vol.272 , Issue.40 , pp. 25401-25408
    • Heyeck, S.D.1    Wilcox, H.M.2    Bunnell, S.C.3    Berg, L.J.4
  • 108
    • 13344270890 scopus 로고
    • Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk
    • Liao XC, Littman DR: Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk. Immunity 1995;3: 757-769.
    • (1995) Immunity , vol.3 , pp. 757-769
    • Liao, X.C.1    Littman, D.R.2
  • 109
    • 0030852623 scopus 로고    scopus 로고
    • Itk negatively regulates induction of T cell proliferation by CD28 costimulation
    • Liao XC, Fournier S, Killeen N, Weiss A, Allison JP, Littman DR: Itk negatively regulates induction of T cell proliferation by CD28 costimulation. J Exp Med 1997;186(2):221-228.
    • (1997) J Exp Med , vol.186 , Issue.2 , pp. 221-228
    • Liao, X.C.1    Fournier, S.2    Killeen, N.3    Weiss, A.4    Allison, J.P.5    Littman, D.R.6
  • 110
    • 0032543221 scopus 로고    scopus 로고
    • T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells
    • Liu K-Q, Bunnell SC, Gurniak CB, Berg LJ: T cell receptor-initiated calcium release is uncoupled from capacitative calcium entry in Itk-deficient T cells. J Exp Med 1998;187(10):1721-1727.
    • (1998) J Exp Med , vol.187 , Issue.10 , pp. 1721-1727
    • Liu, K.-Q.1    Bunnell, S.C.2    Gurniak, C.B.3    Berg, L.J.4
  • 111
    • 0027320758 scopus 로고
    • Signalling through CD28 T-cell activation pathway involves an inositol phospholipid-specific phospholipase C activity
    • Nunes J, Klasen S, Franco MD, Lipcey C, Mawas C, Bagnasco M, et al.: Signalling through CD28 T-cell activation pathway involves an inositol phospholipid-specific phospholipase C activity. Biochem J 1993;293:835-842.
    • (1993) Biochem J , vol.293 , pp. 835-842
    • Nunes, J.1    Klasen, S.2    Franco, M.D.3    Lipcey, C.4    Mawas, C.5    Bagnasco, M.6
  • 112
    • 0022458229 scopus 로고
    • Synergy between the T3/antigen receptor complex and Tp44 in the activation of human T cells
    • Weiss A, Manger B, Imboden J: Synergy between the T3/antigen receptor complex and Tp44 in the activation of human T cells. J Immunol 1986;137:819-825.
    • (1986) J Immunol , vol.137 , pp. 819-825
    • Weiss, A.1    Manger, B.2    Imboden, J.3
  • 114
    • 0028169441 scopus 로고
    • The role of p21ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1, activates p21ras
    • Nunes JA, Collette Y, Truneh A, Olive D, Cantrell DA: The role of p21ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1, activates p21ras. J Exp Med 1994;180:1067-1076.
    • (1994) J Exp Med , vol.180 , pp. 1067-1076
    • Nunes, J.A.1    Collette, Y.2    Truneh, A.3    Olive, D.4    Cantrell, D.A.5
  • 115
    • 0029970295 scopus 로고    scopus 로고
    • CD28 signal transduction pathways. A comparison of B7-1 and B7-2 regulation of the MAPKs: ERK2 and JUN kinases
    • Nunes JA, Battifora M, Woodgett JR, Truneh A, Olive D, Cantrell D: CD28 signal transduction pathways. A comparison of B7-1 and B7-2 regulation of the MAPKs: ERK2 and JUN kinases. Mol Immunol 1996;33(1):63-70.
    • (1996) Mol Immunol , vol.33 , Issue.1 , pp. 63-70
    • Nunes, J.A.1    Battifora, M.2    Woodgett, J.R.3    Truneh, A.4    Olive, D.5    Cantrell, D.6
  • 117
    • 0032570874 scopus 로고    scopus 로고
    • Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes
    • Reedquist KA, Bos, JL: Costimulation through CD28 suppresses T cell receptor-dependent activation of the Ras-like small GTPase Rap1 in human T lymphocytes. J Biol Chem 1998;273:4944-4949.
    • (1998) J Biol Chem , vol.273 , pp. 4944-4949
    • Reedquist, K.A.1    Bos, J.L.2
  • 119
    • 0030060353 scopus 로고    scopus 로고
    • Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules
    • Nunes JA, Truneh A, Olive D, Cantrell DA: Signal transduction by CD28 costimulatory receptor on T cells. B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules. J Biol Chem 1996;271:1591-1598.
    • (1996) J Biol Chem , vol.271 , pp. 1591-1598
    • Nunes, J.A.1    Truneh, A.2    Olive, D.3    Cantrell, D.A.4
  • 120
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo P, Schuebel KE, Ostrom AA, Gutkind JS, Bustelo XR: Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature 1997;385:169-172.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 121
    • 0032537743 scopus 로고    scopus 로고
    • Lymphocyte signalling: A coordinating role for Vav?
    • Cantrell D: Lymphocyte signalling: A coordinating role for Vav? Curr Biol 1998;8:R535-R538.
    • (1998) Curr Biol , vol.8
    • Cantrell, D.1
  • 122
    • 0032080604 scopus 로고    scopus 로고
    • Activation of p21-CDC42/Rac-activated kinases by CD28 signaling:p21-activated kinase (PAK) and MEK kinase 1 (MEKK1) may mediate the interplay between CD3 and CD28 signals
    • Kaga S, Ragg S, Rogers KA, Ochi A: Activation of p21-CDC42/Rac-activated kinases by CD28 signaling:p21-activated kinase (PAK) and MEK kinase 1 (MEKK1) may mediate the interplay between CD3 and CD28 signals. J Immunol 1998:4182-4189.
    • (1998) J Immunol , pp. 4182-4189
    • Kaga, S.1    Ragg, S.2    Rogers, K.A.3    Ochi, A.4
  • 124
    • 0029035315 scopus 로고
    • Sphingomyelinceramide turnover in CD28 costimulatory signaling
    • Chan G, Ochi A: Sphingomyelinceramide turnover in CD28 costimulatory signaling. Eur J Immunol 1995;25:1999-2004.
    • (1995) Eur J Immunol , vol.25 , pp. 1999-2004
    • Chan, G.1    Ochi, A.2
  • 125
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-Kinase
    • Kapeller R, Cantley LC: Phosphatidylinositol 3-Kinase. Bioessays 1995;16:565-576.
    • (1995) Bioessays , vol.16 , pp. 565-576
    • Kapeller, R.1    Cantley, L.C.2
  • 126
    • 0030010956 scopus 로고    scopus 로고
    • Signaling through CD28/CTLA-4 family receptors - Puzzling participation of phosphatidylinositol-3 kinase
    • Hutchcroft JE, Bierer BE: Signaling through CD28/CTLA-4 family receptors - Puzzling participation of phosphatidylinositol-3 kinase. J Immunol 1996;156:4071-4074.
    • (1996) J Immunol , vol.156 , pp. 4071-4074
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 127
    • 0028178928 scopus 로고
    • PDGF- and insulin-dependent pp70s6k activation mediated by phosphatidylinositol-3-OH kinase
    • Chung J, Grammer TC, Lemon KP, Kazlauskas A, Blenis J: PDGF- and insulin-dependent pp70s6k activation mediated by phosphatidylinositol-3-OH kinase. Nature 1994;370:71-75.
    • (1994) Nature , vol.370 , pp. 71-75
    • Chung, J.1    Grammer, T.C.2    Lemon, K.P.3    Kazlauskas, A.4    Blenis, J.5
  • 128
    • 0028999052 scopus 로고
    • Phosphatidylinositol 3-kinase signals activation of p70 S6 kinase in situ through site-specific p70 phosphorylation
    • Weng QP, Andrabi K, Kippel A, Kozlowski, MT, Williams LT, Avruch J: Phosphatidylinositol 3-kinase signals activation of p70 S6 kinase in situ through site-specific p70 phosphorylation. Proc Natl Acad Sci USA 1995;92:5744-5748.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5744-5748
    • Weng, Q.P.1    Andrabi, K.2    Kippel, A.3    Kozlowski, M.T.4    Williams, L.T.5    Avruch, J.6
  • 129
    • 0028560447 scopus 로고
    • Activation of protein kinse C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5 P3
    • Toker A, Meyer M, Reddy KK, Falck J, Aneja R, Aneja S, et al.: Activation of protein kinse C family members by the novel polyphosphoinositides PtdIns-3,4-P2 and PtdIns-3,4,5 P3. J Biol Chem 1994;269:32,358-32,367.
    • (1994) J Biol Chem , vol.269 , pp. 32358-32367
    • Toker, A.1    Meyer, M.2    Reddy, K.K.3    Falck, J.4    Aneja, R.5    Aneja, S.6
  • 130
    • 9044253707 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates protein kinase Cε through redundant and independent signaling pathways involving phospholipase Cγ or phosphatidylinositol 3-kinase
    • Moriya S, Kazlauskas A, Akimoto K, Hirai S-i, Mizuno K, Takenawa T, et al.: Platelet-derived growth factor activates protein kinase Cε through redundant and independent signaling pathways involving phospholipase Cγ or phosphatidylinositol 3-kinase. Prod Natl Acad Sci USA 1996;93:151-155.
    • (1996) Prod Natl Acad Sci USA , vol.93 , pp. 151-155
    • Moriya, S.1    Kazlauskas, A.2    Akimoto, K.3    Hirai, S.-I.4    Mizuno, K.5    Takenawa, T.6
  • 131
    • 0030686560 scopus 로고    scopus 로고
    • Ligation of the T cell co-stimulatory receptor CD28 activated the serine-threonin-protein kinase protein kinase B
    • Parry RV, Reif K, Smith G, Sansom DM, Hemmings BA, Ward SG: Ligation of the T cell co-stimulatory receptor CD28 activated the serine-threonin-protein kinase protein kinase B. Eur J Immunol 1997;27:2495-2501.
    • (1997) Eur J Immunol , vol.27 , pp. 2495-2501
    • Parry, R.V.1    Reif, K.2    Smith, G.3    Sansom, D.M.4    Hemmings, B.A.5    Ward, S.G.6
  • 132
    • 0029079275 scopus 로고
    • The protein kinase encoded by the AKT proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-Kinase
    • Franke TF, Yang SI, Chan TO, Datta K, Kazlauskas A, Morrison DK, et al.: The protein kinase encoded by the AKT proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-Kinase. Cell 1995;81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6
  • 133
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering BMT, Coffer PJ: Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 1995;376:599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.T.1    Coffer, P.J.2
  • 134
    • 0030908525 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase links the interleukin-2 receptor to protein kinase B and p70 S6 kinase
    • Reif K, Burgering B, Cantrell DA: Phosphatidylinositol 3-kinase links the interleukin-2 receptor to protein kinase B and p70 S6 kinase. J Biol Chem 1997;272(22):14,426-14,433.
    • (1997) J Biol Chem , vol.272 , Issue.22 , pp. 14426-14433
    • Reif, K.1    Burgering, B.2    Cantrell, D.A.3
  • 135
    • 0029842021 scopus 로고    scopus 로고
    • CD28 co-stimulatory regimes differ in their dependence on phosphatidylinositol 3-kinase: Common cosignals induced by CD80 and CD86
    • Cefai D, Cai Y-C, Hu H, Rudd C: CD28 co-stimulatory regimes differ in their dependence on phosphatidylinositol 3-kinase: Common cosignals induced by CD80 and CD86. Int Immunol 1996;8(10):1609-1616.
    • (1996) Int Immunol , vol.8 , Issue.10 , pp. 1609-1616
    • Cefai, D.1    Cai, Y.-C.2    Hu, H.3    Rudd, C.4
  • 136
    • 0030025598 scopus 로고    scopus 로고
    • Comparison of CD28-B7.1 and B7.2 functional interaction in resting human T cells: Phosphatidylinositol 3-kinase association to CD28 and cytokine production
    • Ghiotto-Ragueneau M, Battifora M, Truneh A, Waterfield MD, Olive D: Comparison of CD28-B7.1 and B7.2 functional interaction in resting human T cells: Phosphatidylinositol 3-kinase association to CD28 and cytokine production. Eur J Immunol 1996;26:34-41.
    • (1996) Eur J Immunol , vol.26 , pp. 34-41
    • Ghiotto-Ragueneau, M.1    Battifora, M.2    Truneh, A.3    Waterfield, M.D.4    Olive, D.5
  • 137
    • 0029060259 scopus 로고
    • Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase, and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion
    • Ueda Y, Levine BL, Huang ML, Freeman GJ, Nadler LM, June CH, et al.: Both CD28 ligands CD80 (B7-1) and CD86 (B7-2) activate phosphatidylinositol 3-kinase, and wortmannin reveals heterogeneity in the regulation of T cell IL-2 secretion. Int Immunol 1995;7:957-966.
    • (1995) Int Immunol , vol.7 , pp. 957-966
    • Ueda, Y.1    Levine, B.L.2    Huang, M.L.3    Freeman, G.J.4    Nadler, L.M.5    June, C.H.6
  • 138
    • 0028118512 scopus 로고
    • Stimulation of CD28 Triggers an Association between CD28 and Phosphatidylinositol 3-kinase in Jurkat T cells
    • Truitt KE, Hicks CM, Imboden JB: Stimulation of CD28 Triggers an Association between CD28 and Phosphatidylinositol 3-kinase in Jurkat T cells. J Exp Med 1994;179:1071-1076.
    • (1994) J Exp Med , vol.179 , pp. 1071-1076
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 139
    • 0028211126 scopus 로고
    • The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase
    • Stein PH, Fraser JD, Weiss A: The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase. Mol Cell Biol 1994;14(5):3392-3402.
    • (1994) Mol Cell Biol , vol.14 , Issue.5 , pp. 3392-3402
    • Stein, P.H.1    Fraser, J.D.2    Weiss, A.3
  • 140
    • 0028342859 scopus 로고
    • CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase
    • August A, Dupont B: CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase. Int Immunol 1994;6(5):769-774.
    • (1994) Int Immunol , vol.6 , Issue.5 , pp. 769-774
    • August, A.1    Dupont, B.2
  • 141
    • 0031148668 scopus 로고    scopus 로고
    • A negative role for phosphoinositide 3-kinase in T-cell antigen receptor function
    • Reif K, Lucas S, Cantrell D: A negative role for phosphoinositide 3-kinase in T-cell antigen receptor function. Curr Biol 1997;7:285-293.
    • (1997) Curr Biol , vol.7 , pp. 285-293
    • Reif, K.1    Lucas, S.2    Cantrell, D.3
  • 142
    • 0028802706 scopus 로고
    • Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation
    • Cai Y-C, Cefai D, Schneider H, Raab M, Nabavi N, Rudd CE: Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation. Immunity 1995;3:417-426.
    • (1995) Immunity , vol.3 , pp. 417-426
    • Cai, Y.-C.1    Cefai, D.2    Schneider, H.3    Raab, M.4    Nabavi, N.5    Rudd, C.E.6
  • 143
    • 0028972549 scopus 로고
    • CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase
    • Truitt KE, Shi J, Gibson S, Segal LG, Mills GB, Imboden JB: CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase. J Immunol 1995;155:4702-4710.
    • (1995) J Immunol , vol.155 , pp. 4702-4710
    • Truitt, K.E.1    Shi, J.2    Gibson, S.3    Segal, L.G.4    Mills, G.B.5    Imboden, J.B.6
  • 144
    • 0028972712 scopus 로고
    • CD28-mediated costimulation in the absence of phosphalidylinositol 3-kinase association and activation
    • Crooks MEC, Littman DR, Carter RH, Fearon DT, Weiss A, Stein PH: CD28-mediated costimulation in the absence of phosphalidylinositol 3-kinase association and activation. Mol Cell Biol 1995;15:6820-6828.
    • (1995) Mol Cell Biol , vol.15 , pp. 6820-6828
    • Crooks, M.E.C.1    Littman, D.R.2    Carter, R.H.3    Fearon, D.T.4    Weiss, A.5    Stein, P.H.6
  • 145
    • 0029931976 scopus 로고    scopus 로고
    • Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphotidylinositol 3-kinase association
    • Pages F, Ragueneau M, Klasen S, Battifora M, Couez D, Sweet R, et al.: Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphotidylinositol 3-kinase association. J Biol Chem 1996;271:9403-9409.
    • (1996) J Biol Chem , vol.271 , pp. 9403-9409
    • Pages, F.1    Ragueneau, M.2    Klasen, S.3    Battifora, M.4    Couez, D.5    Sweet, R.6
  • 146
    • 0026595961 scopus 로고
    • Crosslinking of the T cell-specific accessory molecules CD7 and CD28 modulates T cell adhesion
    • Shimizu Y, van Seventer GA, Ennis E, Newman W, Horgan KJ, Shaw S: Crosslinking of the T cell-specific accessory molecules CD7 and CD28 modulates T cell adhesion. J Exp Med 1992;175(2):577-582.
    • (1992) J Exp Med , vol.175 , Issue.2 , pp. 577-582
    • Shimizu, Y.1    Van Seventer, G.A.2    Ennis, E.3    Newman, W.4    Horgan, K.J.5    Shaw, S.6
  • 150
    • 0027980250 scopus 로고
    • T cell receptor-associated alphaphosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56(Ick)
    • Carrera A, Rodriguez-Borlado L, Martinez-Alonso C, Merida I: T cell receptor-associated alphaphosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56(Ick). J Biol Chem 1994;269:19,435-19,440.
    • (1994) J Biol Chem , vol.269 , pp. 19435-19440
    • Carrera, A.1    Rodriguez-Borlado, L.2    Martinez-Alonso, C.3    Merida, I.4
  • 151
    • 0025947446 scopus 로고
    • B cell surface antigen B7/BB-1 provide a costimulatory signal that induces T cells to proliferate and secrete interleukin 2
    • Gimmi CD, Freeman GJ, Gribben GJ, Sugita K, Freeman AS, Morimoto C, et al.: B cell surface antigen B7/BB-1 provide a costimulatory signal that induces T cells to proliferate and secrete interleukin 2. Proc Nat Acad Sci USA 1991;88:6575-6579.
    • (1991) Proc Nat Acad Sci USA , vol.88 , pp. 6575-6579
    • Gimmi, C.D.1    Freeman, G.J.2    Gribben, G.J.3    Sugita, K.4    Freeman, A.S.5    Morimoto, C.6
  • 152
    • 0025963594 scopus 로고
    • Binding of the B cell activation antigen B7 to CD28 costimulates T cell proliferation and interleukin 2 mRNA accumulation
    • Linsley PS, Brady W, Grosmaire L, Aruffo A, Damle NK, Ledbetter JA: Binding of the B cell activation antigen B7 to CD28 costimulates T cell proliferation and interleukin 2 mRNA accumulation. J Exp Med 1991;173:721-730.
    • (1991) J Exp Med , vol.173 , pp. 721-730
    • Linsley, P.S.1    Brady, W.2    Grosmaire, L.3    Aruffo, A.4    Damle, N.K.5    Ledbetter, J.A.6
  • 153
    • 0026702322 scopus 로고
    • Regulation of T-cell lymphokine gene transcription by tile accessory molecule CD28
    • Fraser JD, Weiss A: Regulation of T-cell lymphokine gene transcription by tile accessory molecule CD28. Mol Cell Biol 1992;12(10):4357-4363.
    • (1992) Mol Cell Biol , vol.12 , Issue.10 , pp. 4357-4363
    • Fraser, J.D.1    Weiss, A.2
  • 154
    • 0027410856 scopus 로고
    • The interleukin 2 CD28-responsive complex contains at least three members of the NF kappa B family: c-Rel, p50, and p65
    • Ghosh P, Tan T, Rice NR, Sica A, Young HA: The interleukin 2 CD28-responsive complex contains at least three members of the NF kappa B family: c-Rel, p50, and p65. Proc Nat Acad Sci USA 1993;90:1696-1700.
    • (1993) Proc Nat Acad Sci USA , vol.90 , pp. 1696-1700
    • Ghosh, P.1    Tan, T.2    Rice, N.R.3    Sica, A.4    Young, H.A.5
  • 155
    • 0027957152 scopus 로고
    • Induction of IL-8 expression in T cells uses the CD28 costimulatory pathway
    • Wechsler AS, Gordon MC, Dendorfer U, Leclair KP: Induction of IL-8 expression in T cells uses the CD28 costimulatory pathway. J Immunol 1994;153:2515-2523.
    • (1994) J Immunol , vol.153 , pp. 2515-2523
    • Wechsler, A.S.1    Gordon, M.C.2    Dendorfer, U.3    Leclair, K.P.4
  • 156
    • 0027199236 scopus 로고
    • Genomic organization and transcriptional regulation of the RANTES chemokine gene
    • Nelson PJ, Kim HT, Manning WC, Goralski TJ, Krensky AM: Genomic organization and transcriptional regulation of the RANTES chemokine gene. J Immunol 1993;151:2601-2612.
    • (1993) J Immunol , vol.151 , pp. 2601-2612
    • Nelson, P.J.1    Kim, H.T.2    Manning, W.C.3    Goralski, T.J.4    Krensky, A.M.5
  • 157
    • 0029866670 scopus 로고    scopus 로고
    • Rel-deficient T cells exhibit defects in production of interleukin-3 and granulocytemacrophage colony-stimulating factor
    • Gerondakis S, Strasser A, Metcalf D, Grigoriadis G, Scheerlinck JY, Grumont RJ: Rel-deficient T cells exhibit defects in production of interleukin-3 and granulocytemacrophage colony-stimulating factor. Proc Natl Acad Sci USA 1996;93(8):3405-3409.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.8 , pp. 3405-3409
    • Gerondakis, S.1    Strasser, A.2    Metcalf, D.3    Grigoriadis, G.4    Scheerlinck, J.Y.5    Grumont, R.J.6
  • 158
    • 0031961944 scopus 로고    scopus 로고
    • Coordinate transactivation of the interleukin-2 CD28 response element by c-Rel and ATF-1/CREB2
    • Butscher WG, Powers C, Olive M, Vinson C, Gardner K: Coordinate transactivation of the interleukin-2 CD28 response element by c-Rel and ATF-1/CREB2. J Biol Chem 1998;273(1):552-560.
    • (1998) J Biol Chem , vol.273 , Issue.1 , pp. 552-560
    • Butscher, W.G.1    Powers, C.2    Olive, M.3    Vinson, C.4    Gardner, K.5
  • 159
    • 0028027041 scopus 로고    scopus 로고
    • Cross-linking CD28 leads to activation of 70-kDa S6 kinase
    • Pai SY, Calvo V, Wood M, Bierer BE: Cross-linking CD28 leads to activation of 70-kDa S6 kinase. Eur J Immunol 194;24:2364-2368.
    • Eur J Immunol 194 , vol.24 , pp. 2364-2368
    • Pai, S.Y.1    Calvo, V.2    Wood, M.3    Bierer, B.E.4
  • 161
    • 0026537347 scopus 로고
    • CD28-mediated signalling co-stimulates murine T cells and prevents induction of anergy in T-cell clones
    • Harding FA, McArthur JG, Gross JA, Raulet D, Allison JP: CD28-mediated signalling co-stimulates murine T cells and prevents induction of anergy in T-cell clones. Nature 1992;356:607-609.
    • (1992) Nature , vol.356 , pp. 607-609
    • Harding, F.A.1    McArthur, J.G.2    Gross, J.A.3    Raulet, D.4    Allison, J.P.5
  • 162
    • 0027397169 scopus 로고
    • Induction of alloantigen-specific hyporesponsiveness in human T lymphocytes by blocking interaction of CD28 with its natural ligand B7/BB1
    • Tan P, Anasetti C, Hansen JA, Melrose J, Brunvand M, Bradshaw J, et al.: Induction of alloantigen-specific hyporesponsiveness in human T lymphocytes by blocking interaction of CD28 with its natural ligand B7/BB1. J Exp Med 1993;177(1):165-173.
    • (1993) J Exp Med , vol.177 , Issue.1 , pp. 165-173
    • Tan, P.1    Anasetti, C.2    Hansen, J.A.3    Melrose, J.4    Brunvand, M.5    Bradshaw, J.6
  • 163
    • 0029163387 scopus 로고
    • CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-xL
    • Boise LH, Minn AJ, Noel PJ, June CH, Accavitti MA, Lindsten T, et al.: CD28 costimulation can promote T cell survival by enhancing the expression of Bcl-xL. Immunity 1995;3:87-98.
    • (1995) Immunity , vol.3 , pp. 87-98
    • Boise, L.H.1    Minn, A.J.2    Noel, P.J.3    June, C.H.4    Accavitti, M.A.5    Lindsten, T.6
  • 164
    • 0031447458 scopus 로고    scopus 로고
    • A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells
    • Yang XF, Weber GF, Cantor H: A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells. Immunity 1997;7:629-639.
    • (1997) Immunity , vol.7 , pp. 629-639
    • Yang, X.F.1    Weber, G.F.2    Cantor, H.3
  • 166
    • 0026459468 scopus 로고
    • T-cell activation by the CD28 ligand B7 is required for cardiac allograft rejection in vivo
    • Turka LA, Linsley PS, Lin H, Brady W, Leiden JM, Wei RQ, et al.: T-cell activation by the CD28 ligand B7 is required for cardiac allograft rejection in vivo. Proc Natl Acad Sci USA 1992;89:11,102-11,105.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11102-11105
    • Turka, L.A.1    Linsley, P.S.2    Lin, H.3    Brady, W.4    Leiden, J.M.5    Wei, R.Q.6
  • 167
    • 0027942023 scopus 로고
    • Pivotal role of tile B7-CD28 pathway in transplantation tolerance and tumor immunity
    • Guinan EC, Gribben JG, Boussiotis VA, Freeman GJ, Nadler LM: Pivotal role of tile B7-CD28 pathway in transplantation tolerance and tumor immunity. Blood 1994;84:3261-3282.
    • (1994) Blood , vol.84 , pp. 3261-3282
    • Guinan, E.C.1    Gribben, J.G.2    Boussiotis, V.A.3    Freeman, G.J.4    Nadler, L.M.5
  • 168
    • 0028263666 scopus 로고
    • Costimulation of minor-reactive CD4+ and CD8+ T lymphocytes by B7, a natural ligand for CD28, can be used to treat established mouse melanoma
    • Li Y, McGowan P, Hellstrom I, Hellstrom KE, Chen L. Costimulation of minor-reactive CD4+ and CD8+ T lymphocytes by B7, a natural ligand for CD28, can be used to treat established mouse melanoma. J Immunol 1994;153: 421-428.
    • (1994) J Immunol , vol.153 , pp. 421-428
    • Li, Y.1    McGowan, P.2    Hellstrom, I.3    Hellstrom, K.E.4    Chen, L.5
  • 169
    • 0027392843 scopus 로고
    • Tumor rejection after direct costimulation of CD8+ T cells by B7-transfected melanoma cells
    • Townsend SE, Allison JP: Tumor rejection after direct costimulation of CD8+ T cells by B7-transfected melanoma cells. Science 1993;259:368-370.
    • (1993) Science , vol.259 , pp. 368-370
    • Townsend, S.E.1    Allison, J.P.2
  • 170
    • 0027078670 scopus 로고
    • Costimulation of anti-tumor immunity by the B7 counterreceptor for the T lymphocyte molecules CD28 and CTLA-4
    • Chen L, Ashe S, Brady WA, Hellstrom I, Hellstrom KE, Ledbetter JA, et al.: Costimulation of anti-tumor immunity by the B7 counterreceptor for the T lymphocyte molecules CD28 and CTLA-4. Cell 1992;71:1093-1102.
    • (1992) Cell , vol.71 , pp. 1093-1102
    • Chen, L.1    Ashe, S.2    Brady, W.A.3    Hellstrom, I.4    Hellstrom, K.E.5    Ledbetter, J.A.6
  • 171
    • 0028868424 scopus 로고
    • CD28 B7 costimulatory blockade by CTLA4Ig prevents actively induced experimental autoimmune encephalomyelitis and inhibits Th1 but spares Th2 cytokines in the central nervous system
    • Khoury SJ, Akalin E, Chandraker A, Turka LA, Linsley PS, Sayegh MH, et al.: CD28 B7 costimulatory blockade by CTLA4Ig prevents actively induced experimental autoimmune encephalomyelitis and inhibits Th1 but spares Th2 cytokines in the central nervous system. J Immunol 1995:4521-4524.
    • (1995) J Immunol , pp. 4521-4524
    • Khoury, S.J.1    Akalin, E.2    Chandraker, A.3    Turka, L.A.4    Linsley, P.S.5    Sayegh, M.H.6
  • 172
    • 0028483990 scopus 로고
    • Treatment of murine lupus with CTLA-4Ig
    • Finck BK, Linsley PS, Wofsy D: Treatment of murine lupus with CTLA-4Ig. Science 1994;265:1225-1227.
    • (1994) Science , vol.265 , pp. 1225-1227
    • Finck, B.K.1    Linsley, P.S.2    Wofsy, D.3
  • 173
    • 0028949152 scopus 로고
    • B7-1 and B7-2 costimulatory molecules activate differentially the Th1/Th2 developmental pathways: Application to autoimmune disease therapy
    • Kuchroo VK, Das MP, Brown JA, Ranger AM, Zamvil SS, Sobel RA, et al.: B7-1 and B7-2 costimulatory molecules activate differentially the Th1/Th2 developmental pathways: Application to autoimmune disease therapy. Cell 1995;80:707-718.
    • (1995) Cell , vol.80 , pp. 707-718
    • Kuchroo, V.K.1    Das, M.P.2    Brown, J.A.3    Ranger, A.M.4    Zamvil, S.S.5    Sobel, R.A.6
  • 174
    • 0028900297 scopus 로고
    • Differential effects of anti-B7-1 and anti-B7-2 monoclonal antibody treatment on the development of diabetes in the nonobese diabetic mouse
    • Lenschow DJ, Ho SC, Sattar H, Rhee L, Gray G, Nabavi N, et al.: Differential effects of anti-B7-1 and anti-B7-2 monoclonal antibody treatment on the development of diabetes in the nonobese diabetic mouse. J Exp Med 1995;181:1145-1155.
    • (1995) J Exp Med , vol.181 , pp. 1145-1155
    • Lenschow, D.J.1    Ho, S.C.2    Sattar, H.3    Rhee, L.4    Gray, G.5    Nabavi, N.6
  • 175
    • 0030028248 scopus 로고    scopus 로고
    • B7-1 is superior to B7-2 costimulation in the induction and maintenance of T cell-mediated antileukemia immunity
    • Matulonis U, Dosiou C, Freeman G, Lamont C, Mauch P, Nadler LM, et al.: B7-1 is superior to B7-2 costimulation in the induction and maintenance of T cell-mediated antileukemia immunity. J Immunol 1996;156:1126-1131.
    • (1996) J Immunol , vol.156 , pp. 1126-1131
    • Matulonis, U.1    Dosiou, C.2    Freeman, G.3    Lamont, C.4    Mauch, P.5    Nadler, L.M.6
  • 176
    • 0028785417 scopus 로고
    • Distinct roles for BY-1 (CD80) and B7-2 (CD86) in the initiation of experimental allergic encephalomyelitis
    • Racke MK, Scott DE, Quigley L, Gray GS, Abe R, June CH, et al.: Distinct roles for BY-1 (CD80) and B7-2 (CD86) in the initiation of experimental allergic encephalomyelitis. J Clin Invest 1995;96:2195-2203.
    • (1995) J Clin Invest , vol.96 , pp. 2195-2203
    • Racke, M.K.1    Scott, D.E.2    Quigley, L.3    Gray, G.S.4    Abe, R.5    June, C.H.6
  • 177
    • 0030026868 scopus 로고    scopus 로고
    • BY-1 but not B7-2 efficiently costimulates CD8+ T lymphocytes in the P815 tumor system in vitro
    • Gajewski TF. BY-1 but not B7-2 efficiently costimulates CD8+ T lymphocytes in the P815 tumor system in vitro. J Immunol 1996:465-472.
    • (1996) J Immunol , pp. 465-472
    • Gajewski, T.F.1
  • 178
    • 0030778838 scopus 로고    scopus 로고
    • Differential down-regulation of CD28 by B7-1 and B7-2 engagement
    • Eck SC, Chang D, Wells AD, Turka LA: Differential down-regulation of CD28 by B7-1 and B7-2 engagement. Transplantation 1997;64(10): 1497-.
    • (1997) Transplantation , vol.64 , Issue.10 , pp. 1497
    • Eck, S.C.1    Chang, D.2    Wells, A.D.3    Turka, L.A.4
  • 179
    • 0029073050 scopus 로고
    • BY-1 and B7-2 do not deliver identical costimulatory signals, since B7-2 but not B7-1 preferentially costimulates the initial production of IL-4
    • Freeman GJ, Boussiotis VA, Anumanthan A, Bernstein GM, Ke X-Y, Rennert PD, et al.: BY-1 and B7-2 do not deliver identical costimulatory signals, since B7-2 but not B7-1 preferentially costimulates the initial production of IL-4. Immunity 1995;2:523-532.
    • (1995) Immunity , vol.2 , pp. 523-532
    • Freeman, G.J.1    Boussiotis, V.A.2    Anumanthan, A.3    Bernstein, G.M.4    Ke, X.-Y.5    Rennert, P.D.6
  • 180
    • 0032530535 scopus 로고    scopus 로고
    • The role of B7-1 and B7-2 costimulation for the generation of CTL responses in vivo
    • Sigal LJ, Reiser H, Rock KL: The role of B7-1 and B7-2 costimulation for the generation of CTL responses in vivo. J Immunol 1998;161:2740-2745.
    • (1998) J Immunol , vol.161 , pp. 2740-2745
    • Sigal, L.J.1    Reiser, H.2    Rock, K.L.3
  • 181
    • 0031571214 scopus 로고    scopus 로고
    • Weak peptide agonists reveal functional differences in B7-1 and B7-2 costimulation of human T cell clones
    • Anderson DE, Ausubel LJ, Kreiger J, Hollsberg P, Freeman GJ, Hafler DA: Weak peptide agonists reveal functional differences in B7-1 and B7-2 costimulation of human T cell clones. J Immunol 1997;159:1669-1675.
    • (1997) J Immunol , vol.159 , pp. 1669-1675
    • Anderson, D.E.1    Ausubel, L.J.2    Kreiger, J.3    Hollsberg, P.4    Freeman, G.J.5    Hafler, D.A.6
  • 182
    • 0031896336 scopus 로고    scopus 로고
    • Biased dependency of CD80 versus CD86 in th induction of transcription factors regulating the human IL-2 promoter
    • Ollson C, Michaelsson E, Parra E, U. P, Lando PA, Dohlstein M: Biased dependency of CD80 versus CD86 in th induction of transcription factors regulating the human IL-2 promoter. Int Immunol 1998;10(4):499-506.
    • (1998) Int Immunol , vol.10 , Issue.4 , pp. 499-506
    • Ollson, C.1    Michaelsson, E.2    Parra, E.3    U., P.4    Lando, P.A.5    Dohlstein, M.6
  • 183
    • 0028819315 scopus 로고
    • CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell proliferation, cytokine production, and generation of CTL
    • Lanier LL, O'Fallon S, Somoza C, Phillips JH, Linsley PS, Okumura K, et al.: CD80 (B7) and CD86 (B70) provide similar costimulatory signals for T cell proliferation, cytokine production, and generation of CTL. J Immunol 1995:97-105.
    • (1995) J Immunol , pp. 97-105
    • Lanier, L.L.1    O'Fallon, S.2    Somoza, C.3    Phillips, J.H.4    Linsley, P.S.5    Okumura, K.6
  • 184
    • 0030584924 scopus 로고    scopus 로고
    • Costimulation of IL-4 production by routine B7-1 and B7-2 molecules
    • Natesan M, Razi-Wolf Z, Reiser H: Costimulation of IL-4 production by routine B7-1 and B7-2 molecules. J Immunol 1996:2783-2791.
    • (1996) J Immunol , pp. 2783-2791
    • Natesan, M.1    Razi-Wolf, Z.2    Reiser, H.3
  • 186
    • 0029120245 scopus 로고
    • CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation
    • Krummel MF, Allison JP. CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation. J Exp Med 1995;182:459-465.
    • (1995) J Exp Med , vol.182 , pp. 459-465
    • Krummel, M.F.1    Allison, J.P.2
  • 187
    • 0029899783 scopus 로고    scopus 로고
    • CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells
    • Krummel MF, Allison JP: CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells. J Exp Med 1996;183:2533-2540.
    • (1996) J Exp Med , vol.183 , pp. 2533-2540
    • Krummel, M.F.1    Allison, J.P.2
  • 189
    • 0028867420 scopus 로고
    • Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tisssue destruction, revealing a critical negative regulatory role of CTLA-4
    • Tivol EA, Borriello F, Schweitzer AN, Lynch WP, Bluestone JA, Sharpe AH: Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tisssue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 1995;3:541-547.
    • (1995) Immunity , vol.3 , pp. 541-547
    • Tivol, E.A.1    Borriello, F.2    Schweitzer, A.N.3    Lynch, W.P.4    Bluestone, J.A.5    Sharpe, A.H.6
  • 190
  • 192
    • 0029800932 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation and PTPIC in CLTA-4 signal transduction
    • Chambers CA, Allison JP: The role of tyrosine phosphorylation and PTPIC in CLTA-4 signal transduction. Eur J Immunol 1996;26:3224-3229.
    • (1996) Eur J Immunol , vol.26 , pp. 3224-3229
    • Chambers, C.A.1    Allison, J.P.2
  • 193
    • 0029953858 scopus 로고    scopus 로고
    • CTLA-4 ligation blocks CD28-dependent T cell activation
    • Walunas TL, Bakker CY, Bluestone JA: CTLA-4 ligation blocks CD28-dependent T cell activation. J Exp Med 1996;183:2541-2550.
    • (1996) J Exp Med , vol.183 , pp. 2541-2550
    • Walunas, T.L.1    Bakker, C.Y.2    Bluestone, J.A.3
  • 195
    • 0031405867 scopus 로고    scopus 로고
    • Lymphoproliferation in CTLA-4 deficient mice is mediated by costimulation-dependent activation of CD4+ T cells
    • Chambers CA, Sullivan TJ, Allison JP: Lymphoproliferation in CTLA-4 deficient mice is mediated by costimulation-dependent activation of CD4+ T cells. Immunity 1997;7:885-895.
    • (1997) Immunity , vol.7 , pp. 885-895
    • Chambers, C.A.1    Sullivan, T.J.2    Allison, J.P.3
  • 196
    • 0031154577 scopus 로고    scopus 로고
    • CTLA4Ig prevents lymphoproliferation and fatal mutiorgan tissue destruction in CTLA-4-deficient mice
    • Tivol EA, Boyd SD, McKeon S, Borriello F, Nickerson P, Strom TB, et al.: CTLA4Ig prevents lymphoproliferation and fatal mutiorgan tissue destruction in CTLA-4-deficient mice. J Immunol 1997;158:5091-5094.
    • (1997) J Immunol , vol.158 , pp. 5091-5094
    • Tivol, E.A.1    Boyd, S.D.2    McKeon, S.3    Borriello, F.4    Nickerson, P.5    Strom, T.B.6
  • 197
    • 0030740572 scopus 로고    scopus 로고
    • Normal thymic selection, normal viability and decreased lymphoproliferation in T cell receptor transgenic CTLA-4 deficient mice
    • Waterhouse P, Bachmann MF, Penninger JM, Ohashi PS, Mak TW. Normal thymic selection, normal viability and decreased lymphoproliferation in T cell receptor transgenic CTLA-4 deficient mice. Eur J Immunol 1997;27:1887-1892.
    • (1997) Eur J Immunol , vol.27 , pp. 1887-1892
    • Waterhouse, P.1    Bachmann, M.F.2    Penninger, J.M.3    Ohashi, P.S.4    Mak, T.W.5
  • 198
    • 0030707866 scopus 로고    scopus 로고
    • Cytotoxic T lymphocyte antigen 4 (CTLA-4) interferes with extracellular signal-regulated (ERK) and jun NH2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor ζ and ZAP70
    • Calvo CR, Amsen D, Kruisbeek AM. Cytotoxic T lymphocyte antigen 4 (CTLA-4) interferes with extracellular signal-regulated (ERK) and jun NH2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor ζ and ZAP70. J Exp Med 1997;186(10):1645-1653.
    • (1997) J Exp Med , vol.186 , Issue.10 , pp. 1645-1653
    • Calvo, C.R.1    Amsen, D.2    Kruisbeek, A.M.3


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