메뉴 건너뛰기




Volumn 192, Issue , 2003, Pages 161-180

T cell anergy and costimulation

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGEN; B7 ANTIGEN; CALCIUM; CD28 ANTIGEN; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE; RAP PROTEIN; RAS PROTEIN; T LYMPHOCYTE RECEPTOR;

EID: 0037902480     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2003.00009.x     Document Type: Review
Times cited : (256)

References (221)
  • 1
    • 0034507693 scopus 로고    scopus 로고
    • Impact of negative selection on the T cell repertoire reactive to a self-peptide: A large fraction of T cell clones escapes clonal deletion
    • Bouneaud C, Kourilsky P, Bousso P. Impact of negative selection on the T cell repertoire reactive to a self-peptide: a large fraction of T cell clones escapes clonal deletion. Immunity 2000;13:829-840.
    • (2000) Immunity , vol.13 , pp. 829-840
    • Bouneaud, C.1    Kourilsky, P.2    Bousso, P.3
  • 2
    • 0014941813 scopus 로고
    • A theory of self-nonself discrimination
    • Bretscher P, Cohn M. A theory of self-nonself discrimination. Science 1970;169:1042-1049.
    • (1970) Science , vol.169 , pp. 1042-1049
    • Bretscher, P.1    Cohn, M.2
  • 3
    • 0033491636 scopus 로고    scopus 로고
    • T lymphocyte tolerance: From thymic deletion to peripheral control mechanisms
    • Stockinger B. T lymphocyte tolerance: from thymic deletion to peripheral control mechanisms. Adv Immunol 1999;71:229-265.
    • (1999) Adv Immunol , vol.71 , pp. 229-265
    • Stockinger, B.1
  • 4
    • 0036644686 scopus 로고    scopus 로고
    • Promiscuous gene expression and central T-cell tolerance: More than meets the eye
    • Kyewski B, Derbinski J, Gotter J, Klein L. Promiscuous gene expression and central T-cell tolerance: more than meets the eye. Trends Immunol 2002;23:364-371.
    • (2002) Trends Immunol , vol.23 , pp. 364-371
    • Kyewski, B.1    Derbinski, J.2    Gotter, J.3    Klein, L.4
  • 6
    • 0036215202 scopus 로고    scopus 로고
    • Activation-induced cell death: The controversial role of Fas and Fas ligand in immune privilege and tumour counterattack
    • Maher S, Toomey D, Condron C, Bouchier-Hayes D. Activation-induced cell death: the controversial role of Fas and Fas ligand in immune privilege and tumour counterattack. Immunol Cell Biol 2002;80:131-137.
    • (2002) Immunol Cell Biol , vol.80 , pp. 131-137
    • Maher, S.1    Toomey, D.2    Condron, C.3    Bouchier-Hayes, D.4
  • 7
    • 17444372347 scopus 로고    scopus 로고
    • Changes in thymic function with age and during the treatment of HIV infection
    • Douek DC, et al. Changes in thymic function with age and during the treatment of HIV infection. Nature 1998;396:690-695.
    • (1998) Nature , vol.396 , pp. 690-695
    • Douek, D.C.1
  • 8
    • 0033136325 scopus 로고    scopus 로고
    • Generation of functional thymocytes in the human adult
    • Jamieson BD, et al. Generation of functional thymocytes in the human adult. Immunity 1999;10:569-575.
    • (1999) Immunity , vol.10 , pp. 569-575
    • Jamieson, B.D.1
  • 9
    • 0011869916 scopus 로고
    • Clonal anergy: Persistence in tolerant mice of antigen-binding B lymphocytes incapable of responding to antigen or mitogen
    • Nossal GJ, Pike BL. Clonal anergy: persistence in tolerant mice of antigen-binding B lymphocytes incapable of responding to antigen or mitogen. Proc Natl Acad Sci USA 1980;77:1602-1606.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1602-1606
    • Nossal, G.J.1    Pike, B.L.2
  • 10
    • 0020569052 scopus 로고
    • Induction of tolerance in influenza virus-immune T lymphocyte clones with synthetic peptides of influenza hemagglutinin
    • Lamb JR, Skidmore BJ, Green N, Chiller JM, Feldmann M. Induction of tolerance in influenza virus-immune T lymphocyte clones with synthetic peptides of influenza hemagglutinin. J Exp Med 1983;157:1434-1447.
    • (1983) J Exp Med , vol.157 , pp. 1434-1447
    • Lamb, J.R.1    Skidmore, B.J.2    Green, N.3    Chiller, J.M.4    Feldmann, M.5
  • 11
    • 0017623408 scopus 로고
    • The origin and mechanism of the allograft reaction
    • Lafferty KJ, Woolnough J. The origin and mechanism of the allograft reaction. Immunol Rev 1977;35:231-262.
    • (1977) Immunol Rev , vol.35 , pp. 231-262
    • Lafferty, K.J.1    Woolnough, J.2
  • 12
    • 0033972906 scopus 로고    scopus 로고
    • Integration of calcium and cyclic AMP signaling pathways by 14-3-3
    • Chow CW, Davis RJ. Integration of calcium and cyclic AMP signaling pathways by 14-3-3. Mol Cell Biol 2000;20:702-712.
    • (2000) Mol Cell Biol , vol.20 , pp. 702-712
    • Chow, C.W.1    Davis, R.J.2
  • 13
    • 0018217918 scopus 로고
    • Immunological induction of T lymphocytes: Role of antigen and the lymphocyte costimulator
    • Lafferty KJ, Warren HS, Woolnough JA, Talmage DW. Immunological induction of T lymphocytes: role of antigen and the lymphocyte costimulator. Blood Cells 1978;4:395-406.
    • (1978) Blood Cells , vol.4 , pp. 395-406
    • Lafferty, K.J.1    Warren, H.S.2    Woolnough, J.A.3    Talmage, D.W.4
  • 14
    • 0023266396 scopus 로고
    • Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: Specific induction of a long-lived state of proliferative nonresponsiveness
    • Quill H, Schwartz RH. Stimulation of normal inducer T cell clones with antigen presented by purified Ia molecules in planar lipid membranes: specific induction of a long-lived state of proliferative nonresponsiveness. J Immunol 1987;138:3704-3712.
    • (1987) J Immunol , vol.138 , pp. 3704-3712
    • Quill, H.1    Schwartz, R.H.2
  • 15
    • 0023143676 scopus 로고
    • Antigen presentation by chemically modified splenocytes induces antigen-specific T cell unresponsiveness in vitro and in vivo
    • Jenkins MK, Schwartz RH. Antigen presentation by chemically modified splenocytes induces antigen-specific T cell unresponsiveness in vitro and in vivo. J Exp Med 1987;165:302-319.
    • (1987) J Exp Med , vol.165 , pp. 302-319
    • Jenkins, M.K.1    Schwartz, R.H.2
  • 16
    • 0023885038 scopus 로고
    • Allogeneic non-T spleen cells restore the responsiveness of normal T cell clones stimulated with antigen and chemically modified antigen-presenting cells
    • Jenkins MK, Ashwell JD, Schwartz RH. Allogeneic non-T spleen cells restore the responsiveness of normal T cell clones stimulated with antigen and chemically modified antigen-presenting cells. J Immunol 1988;140:3324-3330.
    • (1988) J Immunol , vol.140 , pp. 3324-3330
    • Jenkins, M.K.1    Ashwell, J.D.2    Schwartz, R.H.3
  • 17
    • 0024511201 scopus 로고
    • An accessory cell-derived costimulatory signal acts independently of protein kinase C activation to allow T cell proliferation and prevent the induction of unresponsiveness
    • Mueller DL, Jenkins MK, Schwartz RH. An accessory cell-derived costimulatory signal acts independently of protein kinase C activation to allow T cell proliferation and prevent the induction of unresponsiveness. J Immunol 1989;142:2617-2628.
    • (1989) J Immunol , vol.142 , pp. 2617-2628
    • Mueller, D.L.1    Jenkins, M.K.2    Schwartz, R.H.3
  • 18
    • 0031725323 scopus 로고    scopus 로고
    • Molecular regulation of interleukin-2 expression by CD28 co-stimulation and anergy
    • Powell JD, Ragheb JA, Kitagawa-Sakakida S, Schwartz RH. Molecular regulation of interleukin-2 expression by CD28 co-stimulation and anergy. Immunol Rev 1998;165:287-300.
    • (1998) Immunol Rev , vol.165 , pp. 287-300
    • Powell, J.D.1    Ragheb, J.A.2    Kitagawa-Sakakida, S.3    Schwartz, R.H.4
  • 19
    • 0026687519 scopus 로고
    • Reversal of in vitro T cell clonal anergy by IL-2 stimulation
    • Beverly B, Kang SM, Lenardo MJ, Schwartz RH. Reversal of in vitro T cell clonal anergy by IL-2 stimulation. Int Immunol 1992;4:661-671.
    • (1992) Int Immunol , vol.4 , pp. 661-671
    • Beverly, B.1    Kang, S.M.2    Lenardo, M.J.3    Schwartz, R.H.4
  • 20
    • 0000324490 scopus 로고
    • CD28 activation pathway regulates the production of multiple T-cell-derived lymphokines/cytokines
    • Thompson CB, et al. CD28 activation pathway regulates the production of multiple T-cell-derived lymphokines/cytokines. Proc Natl Acad Sci USA 1989;86:1333-1337.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1333-1337
    • Thompson, C.B.1
  • 21
    • 0024506159 scopus 로고
    • Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway
    • Lindstein T, June CH, Ledbetter JA, Stella G, Thompson CB. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science 1989;244:339-343.
    • (1989) Science , vol.244 , pp. 339-343
    • Lindstein, T.1    June, C.H.2    Ledbetter, J.A.3    Stella, G.4    Thompson, C.B.5
  • 22
    • 0025947895 scopus 로고
    • CD28 delivers a costimulatory signal revolved in antigen-specific IL-2 production by human T cells
    • Jenkins MK, Taylor PS, Norton SD, Urdahl KB. CD28 delivers a costimulatory signal revolved in antigen-specific IL-2 production by human T cells. J Immunol 1991;147:2461-2466.
    • (1991) J Immunol , vol.147 , pp. 2461-2466
    • Jenkins, M.K.1    Taylor, P.S.2    Norton, S.D.3    Urdahl, K.B.4
  • 23
    • 0025947446 scopus 로고
    • B-cell surface antigen B7 provides a costimulatory signal that induces T cells to proliferate and secrete IL-2
    • Gimmi CD, et al. B-cell surface antigen B7 provides a costimulatory signal that induces T cells to proliferate and secrete IL-2. Proc Natl Acad Sci USA 1991;88:6575.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6575
    • Gimmi, C.D.1
  • 24
    • 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, Dalme 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.
    • (1991) J Exp Med , vol.173 , pp. 721
    • Linsley, P.S.1    Brady, W.2    Grosmaire, L.3    Aruffo, A.4    Dalme, N.K.5    Ledbetter, J.A.6
  • 25
    • 0027767762 scopus 로고
    • Cloning of B7-2: A CTLA-4 counter-receptor that costimulates human T cell proliferation
    • Freeman GJ, et al. Cloning of B7-2: a CTLA-4 counter-receptor that costimulates human T cell proliferation. Science 1993;262:909-911.
    • (1993) Science , vol.262 , pp. 909-911
    • Freeman, G.J.1
  • 27
    • 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 DH, 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.H.4    Allison, J.P.5
  • 29
    • 0031944607 scopus 로고    scopus 로고
    • CD40 and CD154 in cell-mediated immunity
    • Grewal IS, Flavell RA. CD40 and CD154 in cell-mediated immunity. Annu Rev Immunol 1998;16:111-135.
    • (1998) Annu Rev Immunol , vol.16 , pp. 111-135
    • Grewal, I.S.1    Flavell, R.A.2
  • 30
    • 0033571386 scopus 로고    scopus 로고
    • CD2 sets quantitative thresholds in T cell activation
    • Bachmann MF, Barner M, Kopf M. CD2 sets quantitative thresholds in T cell activation. J Exp Med 1999;190:1383-1392.
    • (1999) J Exp Med , vol.190 , pp. 1383-1392
    • Bachmann, M.F.1    Barner, M.2    Kopf, M.3
  • 31
    • 0032192469 scopus 로고    scopus 로고
    • Initiation of signal transduction through the T cell receptor requires the multivalent engagement of peptide/MHC ligands
    • Boniface JJ, et al. Initiation of signal transduction through the T cell receptor requires the multivalent engagement of peptide/MHC ligands [corrected]. Immunity 1998;9:459-466.
    • (1998) Immunity , vol.9 , pp. 459-466
    • Boniface, J.J.1
  • 32
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 1994;76:287-299.
    • (1994) Cell , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 33
    • 0030218942 scopus 로고    scopus 로고
    • Altered T cell receptor ligands trigger a subset of early T cell signals
    • Rabinowitz JD, et al. Altered T cell receptor ligands trigger a subset of early T cell signals. Immunity 1996;5:125-135.
    • (1996) Immunity , vol.5 , pp. 125-135
    • Rabinowitz, J.D.1
  • 34
    • 0029933309 scopus 로고    scopus 로고
    • Altered peptide ligand-induced partial T cell activation: Molecular mechanisms and rote in T cell biology
    • Sloan-Lancaster J, Allen PM. Altered peptide ligand-induced partial T cell activation: molecular mechanisms and rote in T cell biology. Annu Rev Immunol 1996;14:1-27.
    • (1996) Annu Rev Immunol , vol.14 , pp. 1-27
    • Sloan-Lancaster, J.1    Allen, P.M.2
  • 35
    • 0027298445 scopus 로고
    • Induction of T-cell anergy by altered T-cell-receptor ligand on live antigen-presenting cells
    • Sloan-Lancaster J, Evavold BD, Allen PM. Induction of T-cell anergy by altered T-cell-receptor ligand on live antigen-presenting cells. Nature 1993;363:156-159.
    • (1993) Nature , vol.363 , pp. 156-159
    • Sloan-Lancaster, J.1    Evavold, B.D.2    Allen, P.M.3
  • 36
    • 0030058433 scopus 로고    scopus 로고
    • Interleukin-10 induces a tong-term antigen-specific anergic state in human CD4+ T cells
    • Groux H, Bigler M, de Vries JE, Roncarolo MG. Interleukin-10 induces a tong-term antigen-specific anergic state in human CD4+ T cells. J Exp Med 1996;184:19-29.
    • (1996) J Exp Med , vol.184 , pp. 19-29
    • Groux, H.1    Bigler, M.2    De Vries, J.E.3    Roncarolo, M.G.4
  • 37
    • 0028158319 scopus 로고
    • High levels of interleukin 10 production in vivo are associated with tolerance in SCID patients transplanted with HLA mismatched hematopoietic stem cells
    • Bacchetta R, et al. High levels of interleukin 10 production in vivo are associated with tolerance in SCID patients transplanted with HLA mismatched hematopoietic stem cells. J Exp Med 1994;179:493-502.
    • (1994) J Exp Med , vol.179 , pp. 493-502
    • Bacchetta, R.1
  • 38
    • 0026000892 scopus 로고
    • Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression
    • de Waal Malefyt R, et al. Interleukin 10 (IL-10) and viral IL-10 strongly reduce antigen-specific human T cell proliferation by diminishing the antigen-presenting capacity of monocytes via downregulation of class II major histocompatibility complex expression. J Exp Med 1991;174:915-924.
    • (1991) J Exp Med , vol.174 , pp. 915-924
    • De Waal Malefyt, R.1
  • 39
    • 0030704726 scopus 로고    scopus 로고
    • A CD4+ T-cell subset inhibits antigen-specific T-cell responses and prevents colitis
    • Groux H, et al. A CD4+ T-cell subset inhibits antigen-specific T-cell responses and prevents colitis. Nature 1997;389:737-739.
    • (1997) Nature , vol.389 , pp. 737-739
    • Groux, H.1
  • 40
    • 0025096424 scopus 로고
    • Selective anergy of V beta 8+, CD4+ T cells in Staphylococcus enterotoxm B-primed mice
    • Kawabe Y, Ochi A. Selective anergy of V beta 8+, CD4+ T cells in Staphylococcus enterotoxm B-primed mice. J Exp Med 1990;172:1065-1070.
    • (1990) J Exp Med , vol.172 , pp. 1065-1070
    • Kawabe, Y.1    Ochi, A.2
  • 41
    • 0026068601 scopus 로고
    • Programmed cell death and extrathymic reduction of Vbeta8+ CD4+ T cells in mice tolerant to Staphylococcus aureus enterotoxin B
    • Kawabe Y, Ochi A. Programmed cell death and extrathymic reduction of Vbeta8+ CD4+ T cells in mice tolerant to Staphylococcus aureus enterotoxin B. Nature 1991;349:245-248.
    • (1991) Nature , vol.349 , pp. 245-248
    • Kawabe, Y.1    Ochi, A.2
  • 42
    • 0025096425 scopus 로고
    • In vivo induction of anergy in peripheral V beta 8+ T cells by staphylococcal enterotoxin B
    • Rellahan BL, Jones LA, Kruisbeek AM, Fry AM, Matis LA. In vivo induction of anergy in peripheral V beta 8+ T cells by staphylococcal enterotoxin B. J Exp Med 1990;172:1091-1100.
    • (1990) J Exp Med , vol.172 , pp. 1091-1100
    • Rellahan, B.L.1    Jones, L.A.2    Kruisbeek, A.M.3    Fry, A.M.4    Matis, L.A.5
  • 43
    • 0025767045 scopus 로고
    • Clonal expansion precedes anergy and death of V beta 8+ peripheral T cells responding to staphylococcal enterotoxin B in vivo
    • MacDonald HR, Baschieri S, Lees RK. Clonal expansion precedes anergy and death of V beta 8+ peripheral T cells responding to staphylococcal enterotoxin B in vivo. Eur J Immunol 1991;21:1963-1966.
    • (1991) Eur J Immunol , vol.21 , pp. 1963-1966
    • MacDonald, H.R.1    Baschieri, S.2    Lees, R.K.3
  • 44
    • 0028500255 scopus 로고
    • Absence of B7-dependent responses in CD28-deficient mice
    • Green JM, et al. Absence of B7-dependent responses in CD28-deficient mice. Immunity 1994;1:501-508.
    • (1994) Immunity , vol.1 , pp. 501-508
    • Green, J.M.1
  • 45
    • 0027281691 scopus 로고
    • Differential T cell costimulatory requirements in CD28-deficient mice
    • Shahinian A, et al. Differential T cell costimulatory requirements in CD28-deficient mice. Science 1993;261:609.
    • (1993) Science , vol.261 , pp. 609
    • Shahinian, A.1
  • 46
    • 0029031023 scopus 로고
    • Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response
    • Lucas PJ, Negishi I, Nakayama K, Fields LE, Loh DY. Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response. J Immunol 1995;154:5757-5768.
    • (1995) J Immunol , vol.154 , pp. 5757-5768
    • Lucas, P.J.1    Negishi, I.2    Nakayama, K.3    Fields, L.E.4    Loh, D.Y.5
  • 48
    • 0028484545 scopus 로고
    • CTLA-4 can function as a negative regulator of T cell activation
    • Walunas TL, et al. CTLA-4 can function as a negative regulator of T cell activation. Immunity 1994;1:405-413.
    • (1994) Immunity , vol.1 , pp. 405-413
    • Walunas, T.L.1
  • 49
    • 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
  • 50
    • 0029947568 scopus 로고    scopus 로고
    • Enhancement of antitumor immunity by CTLA-4 blockade
    • Leach DR, Krummel MF, Allison JP. Enhancement of antitumor immunity by CTLA-4 blockade. Science 1996;271:1734-1736.
    • (1996) Science , vol.271 , pp. 1734-1736
    • Leach, D.R.1    Krummel, M.F.2    Allison, J.P.3
  • 51
    • 0030872154 scopus 로고    scopus 로고
    • Protective immunity to nematode infection is induced by CTLA-4 blockade
    • McCoy K, Camberis M, Gros GL. Protective immunity to nematode infection is induced by CTLA-4 blockade. J Exp Med 1997;186:183-187.
    • (1997) J Exp Med , vol.186 , pp. 183-187
    • McCoy, K.1    Camberis, M.2    Gros, G.L.3
  • 52
    • 0028791059 scopus 로고
    • Lymphoproliferative disorders with early lethality in mice deficient in CTLA-4
    • Waterhouse P, et al. Lymphoproliferative disorders with early lethality in mice deficient in CTLA-4. Science 1995;270:985-988.
    • (1995) Science , vol.270 , pp. 985-988
    • Waterhouse, P.1
  • 53
    • 0028867420 scopus 로고
    • Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue 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 tissue 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
  • 54
    • 0344299189 scopus 로고    scopus 로고
    • Cutting edge: Lymphoproliferative disease in the absence of CTLA-4 is not T cell autonomous
    • Bachmann MF, Kohler G, Ecabert B, Mak TW, Kopf M. Cutting edge: lymphoproliferative disease in the absence of CTLA-4 is not T cell autonomous. J Immunol 1999;163:1128-1131.
    • (1999) J Immunol , vol.163 , pp. 1128-1131
    • Bachmann, M.F.1    Kohler, G.2    Ecabert, B.3    Mak, T.W.4    Kopf, M.5
  • 56
    • 12944310982 scopus 로고    scopus 로고
    • IL-10-producing T cells suppress immune responses in anergic tuberculosis patients
    • Boussiotis VA, et al. IL-10-producing T cells suppress immune responses in anergic tuberculosis patients. J Clin Invest 2000;105:1317-1325.
    • (2000) J Clin Invest , vol.105 , pp. 1317-1325
    • Boussiotis, V.A.1
  • 57
    • 0033152407 scopus 로고    scopus 로고
    • Interleukin 10-mediated immunosuppression by a variant CD4 T cell epitope of Plasmodium falciparum
    • Plebanski M, et al. Interleukin 10-mediated immunosuppression by a variant CD4 T cell epitope of Plasmodium falciparum. Immunity 1999;10:651-660.
    • (1999) Immunity , vol.10 , pp. 651-660
    • Plebanski, M.1
  • 58
    • 0033602935 scopus 로고    scopus 로고
    • Cross-reactivity of Borrelia burgdorferi and myelin basic protein-specific T cells is not observed in borrelial encephalomyelitis
    • Pohl-Koppe A, Logigian EL, Steere AC, Hafler DA. Cross-reactivity of Borrelia burgdorferi and myelin basic protein-specific T cells is not observed in borrelial encephalomyelitis. Cell Immunol 1999;194:118-123.
    • (1999) Cell Immunol , vol.194 , pp. 118-123
    • Pohl-Koppe, A.1    Logigian, E.L.2    Steere, A.C.3    Hafler, D.A.4
  • 59
    • 0001739064 scopus 로고
    • Intradermal immunization of C3H mice against a sarcoma that originated in an animal of the same line
    • Gross L. Intradermal immunization of C3H mice against a sarcoma that originated in an animal of the same line. Cancer Res 1943;3:326.
    • (1943) Cancer Res , vol.3 , pp. 326
    • Gross, L.1
  • 60
    • 70449193189 scopus 로고
    • Immunity to methylcholanthrene-induced sarcomas
    • Prehn R, Main J. Immunity to methylcholanthrene-induced sarcomas. J Natl Cancer Inst 1957;18:769.
    • (1957) J Natl Cancer Inst , vol.18 , pp. 769
    • Prehn, R.1    Main, J.2
  • 61
    • 78651120598 scopus 로고
    • Demonstration of resistance against methylcholanthrene-induced sarcomas in the primary autochthonous host
    • Klein G, Sjogren H, Klein E, Hellstrom KE. Demonstration of resistance against methylcholanthrene-induced sarcomas in the primary autochthonous host. Cancer Res 1960;20:1561.
    • (1960) Cancer Res , vol.20 , pp. 1561
    • Klein, G.1    Sjogren, H.2    Klein, E.3    Hellstrom, K.E.4
  • 62
    • 0014453074 scopus 로고
    • Cellular immunity against tumor antigens
    • Hellstrom KE, Hellstrom I. Cellular immunity against tumor antigens. Adv Cancer Res 1968;12:167.
    • (1968) Adv Cancer Res , vol.12 , pp. 167
    • Hellstrom, K.E.1    Hellstrom, I.2
  • 64
    • 0035500642 scopus 로고    scopus 로고
    • CDS(+) tumor-infiltrating T cells are deficient in perforin-mediated cytolytic activity due to defective microtubule-organizing center mobilization and lytic granule exocytosis
    • Radoja S, Saio M, Schaer D, Koneru M, Vukmanovic S, Frey AB. CDS(+) tumor-infiltrating T cells are deficient in perforin-mediated cytolytic activity due to defective microtubule-organizing center mobilization and lytic granule exocytosis. J Immunol 2001;167:5042-5051.
    • (2001) J Immunol , vol.167 , pp. 5042-5051
    • Radoja, S.1    Saio, M.2    Schaer, D.3    Koneru, M.4    Vukmanovic, S.5    Frey, A.B.6
  • 65
    • 0029155655 scopus 로고
    • fyn, ZAP-70, and CD3 zeta despite suppressed cytolytic activity
    • fyn, ZAP-70, and CD3 zeta despite suppressed cytolytic activity. J Exp Med 1995;182:1029-1036.
    • (1995) J Exp Med , vol.182 , pp. 1029-1036
    • Levey, D.L.1    Srivastava, P.K.2
  • 66
    • 0030221608 scopus 로고    scopus 로고
    • Alterations in T cells of cancer-bearers: Whence specificity?
    • Levey DL, Srivastava PK. Alterations in T cells of cancer-bearers: whence specificity? Immunol Today 1996;17:365-368.
    • (1996) Immunol Today , vol.17 , pp. 365-368
    • Levey, D.L.1    Srivastava, P.K.2
  • 67
    • 0032477815 scopus 로고    scopus 로고
    • Induction of antigen-specific T cell anergy: An early event in the course of tumor progression
    • Staveley-O'Carroll K, et al. Induction of antigen-specific T cell anergy: an early event in the course of tumor progression. Proc Natl Acad Sci USA 1998;95:1178-1183.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1178-1183
    • Staveley-O'Carroll, K.1
  • 68
    • 0034162485 scopus 로고    scopus 로고
    • Mice bearing late-stage tumors have normal functional systemic T cells responses in vitro and in vivo
    • Radoja S, Rao T, Hillman D, Frey A. Mice bearing late-stage tumors have normal functional systemic T cells responses in vitro and in vivo. J Immunol 2000;164:2619-2628.
    • (2000) J Immunol , vol.164 , pp. 2619-2628
    • Radoja, S.1    Rao, T.2    Hillman, D.3    Frey, A.4
  • 69
    • 0033558363 scopus 로고    scopus 로고
    • Isolation of high avidity melanoma-reactive CTL from heterogeneous populations using peptide-MHC tetramers
    • Yee C, Savage PA, Lee PP, Davis MM, Greenberg PD. Isolation of high avidity melanoma-reactive CTL from heterogeneous populations using peptide-MHC tetramers. J Immunol 1999;162:2227-2234.
    • (1999) J Immunol , vol.162 , pp. 2227-2234
    • Yee, C.1    Savage, P.A.2    Lee, P.P.3    Davis, M.M.4    Greenberg, P.D.5
  • 70
    • 0033056073 scopus 로고    scopus 로고
    • Characterization of circulating T cells specific for tumor-associated antigens in melanoma patients
    • Lee PP, et al. Characterization of circulating T cells specific for tumor-associated antigens in melanoma patients. Nat Med 1999;5:677-685.
    • (1999) Nat Med , vol.5 , pp. 677-685
    • Lee, P.P.1
  • 71
    • 0031450625 scopus 로고    scopus 로고
    • Prevention of chronic rejection in mouse aortic allografts by combined treatment with CTLA4-Ig and anti-CD40 ligand monoclonal antibody
    • Sun H, et al. Prevention of chronic rejection in mouse aortic allografts by combined treatment with CTLA4-Ig and anti-CD40 ligand monoclonal antibody. Transplantation 1997;64:1838-1843.
    • (1997) Transplantation , vol.64 , pp. 1838-1843
    • Sun, H.1
  • 72
    • 12644262358 scopus 로고    scopus 로고
    • CTLA4-Ig and anti-CD40 ligand prevent renal allograft rejection in primates
    • Kirk AD, et al. CTLA4-Ig and anti-CD40 ligand prevent renal allograft rejection in primates. Proc Natl Acad Sci USA 1997;94:8789-8794.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8789-8794
    • Kirk, A.D.1
  • 73
    • 15844404353 scopus 로고    scopus 로고
    • Long-term acceptance of skin and cardiac allografts after blocking CD40 and CD28 pathways
    • Larsen CP, et al. Long-term acceptance of skin and cardiac allografts after blocking CD40 and CD28 pathways. Nature 1996;381:434-438.
    • (1996) Nature , vol.381 , pp. 434-438
    • Larsen, C.P.1
  • 74
    • 0028234261 scopus 로고
    • In vivo blockade of CD28/CTLA4: B7/BB1 interaction with CTLA4-Ig reduces lethal murine graft-versus-host disease across the major histocompatibility complex barrier in mice
    • Blazar BR, Taylor PA, Linsley PS, Vallera DA. In vivo blockade of CD28/CTLA4: B7/BB1 interaction with CTLA4-Ig reduces lethal murine graft-versus-host disease across the major histocompatibility complex barrier in mice. Blood 1994;83:3815-3825.
    • (1994) Blood , vol.83 , pp. 3815-3825
    • Blazar, B.R.1    Taylor, P.A.2    Linsley, P.S.3    Vallera, D.A.4
  • 75
    • 0030639082 scopus 로고    scopus 로고
    • Blockade of CD40 ligand-CD40 interaction impairs CD4+ T cell-mediated alloreactivity by inhibiting mature donor T cell expansion and function after bone marrow transplantation
    • Blazar BR, et al. Blockade of CD40 ligand-CD40 interaction impairs CD4+ T cell-mediated alloreactivity by inhibiting mature donor T cell expansion and function after bone marrow transplantation. J Immunol 1997;158:29-39.
    • (1997) J Immunol , vol.158 , pp. 29-39
    • Blazar, B.R.1
  • 76
    • 0033621780 scopus 로고    scopus 로고
    • kip1 functions as an anergy factor inhibiting interleukin 2 transcription and clonal expansion of alloreactive human and mouse helper T lymphocytes
    • kip1 functions as an anergy factor inhibiting interleukin 2 transcription and clonal expansion of alloreactive human and mouse helper T lymphocytes. Nat Med 2000;6:290-297.
    • (2000) Nat Med , vol.6 , pp. 290-297
    • Boussiotis, V.A.1
  • 77
    • 0033519661 scopus 로고    scopus 로고
    • Transplantation of anergic histoincompatible bone marrow allografts
    • Guinan EC, et al. Transplantation of anergic histoincompatible bone marrow allografts. New Engl J Med 1999;340:1704-1714.
    • (1999) New Engl J Med , vol.340 , pp. 1704-1714
    • Guinan, E.C.1
  • 78
    • 0022366834 scopus 로고
    • Identification of the components of the murine T cell antigen receptor complex
    • Samelson LE, Harford JB, Klausner RD. Identification of the components of the murine T cell antigen receptor complex. Cell 1985;43:223-231.
    • (1985) Cell , vol.43 , pp. 223-231
    • Samelson, L.E.1    Harford, J.B.2    Klausner, R.D.3
  • 79
    • 0022996134 scopus 로고
    • A new subunit of the human T-cell antigen receptor complex
    • Weissman AM, Samelson LE, Klausner RD. A new subunit of the human T-cell antigen receptor complex. Nature 1986;324:480-482.
    • (1986) Nature , vol.324 , pp. 480-482
    • Weissman, A.M.1    Samelson, L.E.2    Klausner, R.D.3
  • 80
    • 0022993986 scopus 로고
    • Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor
    • Samelson LE, Patel MD, Weissman AM, Harford JB, Klausner RD. Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor. Cell 1986;46:1083-1090.
    • (1986) Cell , vol.46 , pp. 1083-1090
    • Samelson, L.E.1    Patel, M.D.2    Weissman, A.M.3    Harford, J.B.4    Klausner, R.D.5
  • 81
    • 0026752591 scopus 로고
    • A tyrosine-phosphorylated 70-kDa protein hinds a photoaffinity analogue of ATP and associates with both the zeta chain and CD3 components of the activated T cell antigen receptor
    • Wange RL, Kong AN, Samelson LE. A tyrosine-phosphorylated 70-kDa protein hinds a photoaffinity analogue of ATP and associates with both the zeta chain and CD3 components of the activated T cell antigen receptor. J Biol Chem 1992;267:11685-11688.
    • (1992) J Biol Chem , vol.267 , pp. 11685-11688
    • Wange, R.L.1    Kong, A.N.2    Samelson, L.E.3
  • 82
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR zeta chain
    • Chan AC, Iwashima M, Turck CW, Weiss A. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta 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
  • 83
    • 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 1998;92:83-92.
    • (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
  • 84
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson LE. Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu Rev Immunol 2002;20:371-394.
    • (2002) Annu Rev Immunol , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 85
    • 0027967385 scopus 로고
    • Partial T cell signaling: Altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell anergy
    • Sloan-Lancaster J, Shaw AS, Rothbard JB, Allen PM. Partial T cell signaling: altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell anergy. Cell 1994;79:913-922.
    • (1994) Cell , vol.79 , pp. 913-922
    • Sloan-Lancaster, J.1    Shaw, A.S.2    Rothbard, J.B.3    Allen, P.M.4
  • 86
    • 0028902752 scopus 로고
    • Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
    • Madrenas J, Wange RL, Wang JL, Isakov N, Samelson LE, Germain RN. Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists. Science 1995;267:515-518.
    • (1995) Science , vol.267 , pp. 515-518
    • Madrenas, J.1    Wange, R.L.2    Wang, J.L.3    Isakov, N.4    Samelson, L.E.5    Germain, R.N.6
  • 87
    • 0028817912 scopus 로고
    • Defective TCR-mediated signaling in anergic T cells
    • Migita K, et al. Defective TCR-mediated signaling in anergic T cells. J Immunol 1995;155:5083-5087.
    • (1995) J Immunol , vol.155 , pp. 5083-5087
    • Migita, K.1
  • 88
    • 0027958565 scopus 로고
    • Anergic T-lymphocyte clones have altered inositol phosphate, calcium, and tyrosine kinase signaling pathways
    • Gajewski TF, Qian D, Fields P, Fitch FW. Anergic T-lymphocyte clones have altered inositol phosphate, calcium, and tyrosine kinase signaling pathways. Proc Natl Acad Sci USA 1994;91:38-42.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 38-42
    • Gajewski, T.F.1    Qian, D.2    Fields, P.3    Fitch, F.W.4
  • 89
    • 0029055186 scopus 로고
    • Induction of the increased Fyn kinase activity in anergic T helper type 1 clones requires calcium and protein synthesis and is sensitive to cyclosporin A
    • Gajewski TF, Fields P, Fitch FW. Induction of the increased Fyn kinase activity in anergic T helper type 1 clones requires calcium and protein synthesis and is sensitive to cyclosporin A. Eur J Immunol 1995;25:1836-1842.
    • (1995) Eur J Immunol , vol.25 , pp. 1836-1842
    • Gajewski, T.F.1    Fields, P.2    Fitch, F.W.3
  • 90
    • 0034099730 scopus 로고    scopus 로고
    • Impaired Ca/calcineurin pathway in in vivo anergized CD4 T cells
    • Kimura M, et al. Impaired Ca/calcineurin pathway in in vivo anergized CD4 T cells. Int Immunol 2000;12:817-824.
    • (2000) Int Immunol , vol.12 , pp. 817-824
    • Kimura, M.1
  • 91
    • 0029810388 scopus 로고    scopus 로고
    • Differential association of protein tyrosine kinases with the T cell receptor is linked to the induction of anergy and its prevention by B7 family-mediated costimulation
    • Boussiotis VA, Barber DL, Lee BJ, Gribben JG, Freeman GJ, Nadler LM. Differential association of protein tyrosine kinases with the T cell receptor is linked to the induction of anergy and its prevention by B7 family-mediated costimulation. J Exp Med 1996;184:365-376.
    • (1996) J Exp Med , vol.184 , pp. 365-376
    • Boussiotis, V.A.1    Barber, D.L.2    Lee, B.J.3    Gribben, J.G.4    Freeman, G.J.5    Nadler, L.M.6
  • 92
    • 0021840708 scopus 로고
    • Human T cell activation. II. A new activation pathway used by a major T cell population via a disulfide-bonded dimer of a 44 kilodalton polypeptide (9.3 antigen)
    • Hara T, Fu SM, Hansen JA. Human T cell activation. II. A new activation pathway used by a major T cell population via a disulfide-bonded dimer of a 44 kilodalton polypeptide (9.3 antigen). J Exp Med 1985;161:1513-1524.
    • (1985) J Exp Med , vol.161 , pp. 1513-1524
    • Hara, T.1    Fu, S.M.2    Hansen, J.A.3
  • 93
    • 0021917674 scopus 로고
    • Transmembrane signalling by the T cell antigen receptor. Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores
    • Imboden JB, Stobo JD. Transmembrane signalling by the T cell antigen receptor. Perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores. J Exp Med 1985;161:446-456.
    • (1985) J Exp Med , vol.161 , pp. 446-456
    • Imboden, J.B.1    Stobo, J.D.2
  • 94
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif
    • Prasad KV, et al. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif. Proc Natl Acad Sci USA 1994;91:2834-2838.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2834-2838
    • Prasad, K.V.1
  • 95
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signalling
    • Pages F, 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
  • 96
    • 0029931976 scopus 로고    scopus 로고
    • Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association
    • Pagès F, et al. Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association. J Biol Chem 1996;271:9403-9409.
    • (1996) J Biol Chem , vol.271 , pp. 9403-9409
    • Pagès, F.1
  • 97
    • 0027429761 scopus 로고
    • Ligation of CD28 receptor by B7 reduces formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation
    • Ward SG, Westwick J, Hall ND, Sansom DM. Ligation of CD28 receptor by B7 reduces formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation. Eur J Immunol 1993;23:2572-2577.
    • (1993) Eur J Immunol , vol.23 , pp. 2572-2577
    • Ward, S.G.1    Westwick, J.2    Hall, N.D.3    Sansom, D.M.4
  • 98
    • 0028342859 scopus 로고
    • CD28 oft lymphocytes associates with phosphatidylinositol 3-kinase
    • August A, Dupont B. CD28 oft lymphocytes associates with phosphatidylinositol 3-kinase. Int Immunol 1994;6:769-774.
    • (1994) Int Immunol , vol.6 , pp. 769-774
    • August, A.1    Dupont, B.2
  • 99
    • 0028981212 scopus 로고
    • Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase ITK: Implications for T-cell costimulation
    • Fyn regulate CD28 binding to phosphatidylinositol 3-kinase, growth factor receptor-bound protein GRB-2, and T cell-specific protein-tyrosine kinase 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
  • 100
    • 0030826662 scopus 로고    scopus 로고
    • Src-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and the Pleckstrin homology domain of inducible T cell kinase
    • August A, Sadra A, Dupont B, Hanafusa H. Src-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and the Pleckstrin homology domain of inducible T cell kinase. Proc Natl Acad Sci USA 1997;94:11227-11232.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11227-11232
    • August, A.1    Sadra, A.2    Dupont, B.3    Hanafusa, H.4
  • 101
    • 0028169441 scopus 로고
    • ras in CD28 signal transduction: Triggering of CD28 with antibodies, but not the ligand B7-1, activates p21ras
    • ras 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
  • 102
    • 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;14:3392-3402.
    • (1994) Mol Cell Biol , vol.14 , pp. 3392-3402
    • Stein, P.H.1    Fraser, J.D.2    Weiss, A.3
  • 104
    • 0029046983 scopus 로고
    • Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase
    • Wang J, Auger KR, Jarvis L, Shi Y, Roberts TM. Direct association of Grb2 with the p85 subunit of phosphatidylinositol 3-kinase. J Biol Chem 1995;270:12774-12780.
    • (1995) J Biol Chem , vol.270 , pp. 12774-12780
    • Wang, J.1    Auger, K.R.2    Jarvis, L.3    Shi, Y.4    Roberts, T.M.5
  • 105
    • 0033662376 scopus 로고    scopus 로고
    • The CD28 and CTLA-4 receptors associate with the serine/ threonine phosphatase PP2A
    • Chuang E, et al. The CD28 and CTLA-4 receptors associate with the serine/ threonine phosphatase PP2A. Immunity 2000;13:313-322.
    • (2000) Immunity , vol.13 , pp. 313-322
    • Chuang, E.1
  • 106
    • 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 molecule 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 molecule 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
  • 108
    • 0036180686 scopus 로고    scopus 로고
    • CTLA-4 regulates cell cycle progression during a primary immune response
    • Greenwald RJ, et al. CTLA-4 regulates cell cycle progression during a primary immune response. Eur J Immunol 2002;32:366-373.
    • (2002) Eur J Immunol , vol.32 , pp. 366-373
    • Greenwald, R.J.1
  • 109
    • 0028675006 scopus 로고
    • Human B7-1 (CD80) and B7-2 (CD86) hind 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) hind with similar avidities but distinct kinetics to CD28 and CTLA-4 receptors. Immunity 1994;1:793-801.
    • (1994) Immunity , vol.1 , pp. 793-801
    • Linsley, P.S.1    Greene, J.L.2    Brady, W.3    Bajorath, J.4    Ledbetter, J.A.5    Peach, R.6
  • 110
    • 0031054242 scopus 로고    scopus 로고
    • CD80 (B7-1) binds both CD28 and CTLA-4 with a tow affinity and very fast kinetics
    • van der Merwe PA, Bodian DL, Daenke S, Linsley P, Davis SJ. CD80 (B7-1) binds both CD28 and CTLA-4 with a tow affinity and very fast kinetics. J Exp Med 1997;185:393-403.
    • (1997) J Exp Med , vol.185 , pp. 393-403
    • Van Der Merwe, P.A.1    Bodian, D.L.2    Daenke, S.3    Linsley, P.4    Davis, S.J.5
  • 111
    • 0031154577 scopus 로고    scopus 로고
    • CTLA4Ig prevents lymphoproliferation and fatal multiorgan tissue destruction in CTLA-4-deficient mice
    • Tivot EA, et al. CTLA4Ig prevents lymphoproliferation and fatal multiorgan tissue destruction in CTLA-4-deficient mice. J Immunol 1997;158:5091-5094.
    • (1997) J Immunol , vol.158 , pp. 5091-5094
    • Tivot, E.A.1
  • 113
    • 0030001318 scopus 로고    scopus 로고
    • Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4
    • Marengere LE, Waterhouse P, Duncan GS, Mittrucker HW, Feng GS, Mak TW. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. Science 1996;272:1170-1173.
    • (1996) Science , vol.272 , pp. 1170-1173
    • Marengere, L.E.1    Waterhouse, P.2    Duncan, G.S.3    Mittrucker, H.W.4    Feng, G.S.5    Mak, T.W.6
  • 114
    • 0030707866 scopus 로고    scopus 로고
    • 2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor zeta and ZAP70
    • 2-terminal kinase (JNK) activation, but does not affect phosphorylation of T cell receptor zeta and ZAP70. J Exp Med 1997;186:1645-1653.
    • (1997) J Exp Med , vol.186 , pp. 1645-1653
    • Calvo, C.R.1    Amsen, D.2    Kruisbeek, A.M.3
  • 115
    • 0036569236 scopus 로고    scopus 로고
    • CTLA-4 suppresses proximal TCR signaling in resting human CD4(+) T cells by inhibiting ZAP-70 Tyr(319) phosphorylation: A potential role for tyrosine phosphatases
    • Guntermann C, Alexander DR. CTLA-4 suppresses proximal TCR signaling in resting human CD4(+) T cells by inhibiting ZAP-70 Tyr(319) phosphorylation: a potential role for tyrosine phosphatases. J Immunol 2002;168:4420-4429.
    • (2002) J Immunol , vol.168 , pp. 4420-4429
    • Guntermann, C.1    Alexander, D.R.2
  • 116
    • 0033553471 scopus 로고    scopus 로고
    • CTLA-4 ligation suppresses CD28-induced NF-kappaB and AP-1 activity in mouse T cell blasts
    • Olsson C, Riesbeck K, Dohlsten M, Michaelsson E, Riebeck K. CTLA-4 ligation suppresses CD28-induced NF-kappaB and AP-1 activity in mouse T cell blasts. J Biol Chem 1999;274:14400-14405.
    • (1999) J Biol Chem , vol.274 , pp. 14400-14405
    • Olsson, C.1    Riesbeck, K.2    Dohlsten, M.3    Michaelsson, E.4    Riebeck, K.5
  • 117
    • 0033048961 scopus 로고    scopus 로고
    • CTLA4 ligation attenuates AP-1, NFAT and NF-kappaB activity in activated T cells
    • Fraser JH, Rincon M, McCoy KD, Le Gros G. CTLA4 ligation attenuates AP-1, NFAT and NF-kappaB activity in activated T cells. Eur J Immunol 1999;29:838-844.
    • (1999) Eur J Immunol , vol.29 , pp. 838-844
    • Fraser, J.H.1    Rincon, M.2    McCoy, K.D.3    Le Gros, G.4
  • 118
    • 0028910221 scopus 로고
    • CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells
    • Schneider H, Prasad KV, 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.2    Shoelson, S.E.3    Rudd, C.E.4
  • 119
    • 0033055446 scopus 로고    scopus 로고
    • Pathways for phosphoinositide synthesis
    • Tolias KF, Cantley LC. Pathways for phosphoinositide synthesis. Chem Phys Lipids 1999;98:69-77.
    • (1999) Chem Phys Lipids , vol.98 , pp. 69-77
    • Tolias, K.F.1    Cantley, L.C.2
  • 121
    • 0026018057 scopus 로고
    • CD3 stimulation causes phosphorytation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line
    • Park DJ, Rho HW, Rhee SG. CD3 stimulation causes phosphorytation of phospholipase C-gamma 1 on serine and tyrosine residues in a human T-cell line. Proc Natl Acad Sci USA 1991;88:5453-5456.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5453-5456
    • Park, D.J.1    Rho, H.W.2    Rhee, S.G.3
  • 122
    • 0023189026 scopus 로고
    • Activation of polyphosphoinositide phospholipase C by guanosine 5′-O-(3-thio)triphosphate and fluoroaluminate in membranes prepared from a human T cell leukemia line, JURKAT
    • Sasaki T, Hasegawa-Sasaki H. Activation of polyphosphoinositide phospholipase C by guanosine 5′-O-(3-thio)triphosphate and fluoroaluminate in membranes prepared from a human T cell leukemia line, JURKAT. FEBS Lett 1987;218:87-92.
    • (1987) FEBS Lett , vol.218 , pp. 87-92
    • Sasaki, T.1    Hasegawa-Sasaki, H.2
  • 123
    • 0025285280 scopus 로고
    • Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation
    • June CH, Fletcher MC, Ledbetter JA, Samelson LE. Increases in tyrosine phosphorylation are detectable before phospholipase C activation after T cell receptor stimulation. J Immunol 1990;144:1591-1599.
    • (1990) J Immunol , vol.144 , pp. 1591-1599
    • June, C.H.1    Fletcher, M.C.2    Ledbetter, J.A.3    Samelson, L.E.4
  • 124
    • 18844473151 scopus 로고    scopus 로고
    • PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes
    • Sun Z et al. PKC-theta is required for TCR-induced NF-kappaB activation in mature but not immature T lymphocytes. Nature 2000;404:402-407.
    • (2000) Nature , vol.404 , pp. 402-407
    • Sun, Z.1
  • 125
    • 0036604936 scopus 로고    scopus 로고
    • Protein kinase C-theta: Signaling from the center of the T-cell synapse
    • Arendt CW, Albrecht B, Soos TJ, Littman DR. Protein kinase C-theta: signaling from the center of the T-cell synapse. Curr Opin Immunol 2002;14:323-330.
    • (2002) Curr Opin Immunol , vol.14 , pp. 323-330
    • Arendt, C.W.1    Albrecht, B.2    Soos, T.J.3    Littman, D.R.4
  • 126
    • 0021958592 scopus 로고
    • Early steps of lymphocyte activation bypassed by synergy between calcium ionophores and phorbol ester
    • Truneh A, Albert F, Golstein P, Schmitt-Verhulst AM. Early steps of lymphocyte activation bypassed by synergy between calcium ionophores and phorbol ester. Nature 1985;313:318-320.
    • (1985) Nature , vol.313 , pp. 318-320
    • Truneh, A.1    Albert, F.2    Golstein, P.3    Schmitt-Verhulst, A.M.4
  • 127
    • 0028846489 scopus 로고
    • Phosphatidylinositol hydrolysis in freshly isolated human T lymphocytes
    • Berney SM, Atkinson TP. Phosphatidylinositol hydrolysis in freshly isolated human T lymphocytes. J Immunol Methods 1995;186:71-77.
    • (1995) J Immunol Methods , vol.186 , pp. 71-77
    • Berney, S.M.1    Atkinson, T.P.2
  • 128
    • 0034845112 scopus 로고    scopus 로고
    • CD28 co-stimulates TCR/CD3-induced phosphoinositide turnover in human T lymphocytes
    • Zaru R, Berrie CP, Iurisci C, Corda D, Valitutti S. CD28 co-stimulates TCR/CD3-induced phosphoinositide turnover in human T lymphocytes. Eur J Immunol 2001;31:2438-2447.
    • (2001) Eur J Immunol , vol.31 , pp. 2438-2447
    • Zaru, R.1    Berrie, C.P.2    Iurisci, C.3    Corda, D.4    Valitutti, S.5
  • 129
    • 0031884839 scopus 로고    scopus 로고
    • The duration of antigenic stimulation determines the fate of naive and effector T cells
    • Iezzi G, Karjalainen K, Lanzavecchia A. The duration of antigenic stimulation determines the fate of naive and effector T cells. Immunity 1998;8:89-95.
    • (1998) Immunity , vol.8 , pp. 89-95
    • Iezzi, G.1    Karjalainen, K.2    Lanzavecchia, A.3
  • 130
    • 0029952074 scopus 로고    scopus 로고
    • Selective activation of the calcium signaling pathway by altered peptide ligands
    • Sloan-Lancaster J, Steinberg TH, Allen PM. Selective activation of the calcium signaling pathway by altered peptide ligands. J Exp Med 1996;184:1525-1530.
    • (1996) J Exp Med , vol.184 , pp. 1525-1530
    • Sloan-Lancaster, J.1    Steinberg, T.H.2    Allen, P.M.3
  • 132
    • 0029133689 scopus 로고
    • Effects of cyclosporin A, rapamycin, and FK520 on peripheral T-cell deletion and anergy
    • Prud'homme GJ, Vanier LE, Bocarro DC, Ste-Croix H. Effects of cyclosporin A, rapamycin, and FK520 on peripheral T-cell deletion and anergy. Cell Immunol 1995;164:47-56.
    • (1995) Cell Immunol , vol.164 , pp. 47-56
    • Prud'homme, G.J.1    Vanier, L.E.2    Bocarro, D.C.3    Ste-Croix, H.4
  • 134
    • 0030949834 scopus 로고    scopus 로고
    • Expression of NFAT-family proteins in normal human T cells
    • Lyakh L, Ghosh P, Rice NR. Expression of NFAT-family proteins in normal human T cells. Mol Cell Biol 1997;17:2475-2484.
    • (1997) Mol Cell Biol , vol.17 , pp. 2475-2484
    • Lyakh, L.1    Ghosh, P.2    Rice, N.R.3
  • 135
    • 0029882657 scopus 로고    scopus 로고
    • An enhanced immune response in mice lacking the transcription factor NFAT1
    • Xanthoudakis S, et al. An enhanced immune response in mice lacking the transcription factor NFAT1. Science 1996;272:892-895.
    • (1996) Science , vol.272 , pp. 892-895
    • Xanthoudakis, S.1
  • 137
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley LC. The phosphoinositide 3-kinase pathway. Science 2002;296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 138
    • 0028169625 scopus 로고
    • A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation
    • Hong Z, Verma DP. A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation. Proc Natl Acad Sci USA 1994;91:9617-9621.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9617-9621
    • Hong, Z.1    Verma, D.P.2
  • 139
    • 0025755422 scopus 로고
    • Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middie-T/pp60c-src complexes, and PI3-kinase
    • Otsu M, et al. Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middie-T/pp60c-src complexes, and PI3-kinase. Cell 1991;65:91-104.
    • (1991) Cell , vol.65 , pp. 91-104
    • Otsu, M.1
  • 140
    • 0027361002 scopus 로고
    • Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85
    • Hu P, Mondmo A, Skolnik EY, Schlessinger J. Cloning of a novel, ubiquitously expressed human phosphatidylinositol 3-kinase and identification of its binding site on p85. Mol Cell Biol 1993;13:7677-7688.
    • (1993) Mol Cell Biol , vol.13 , pp. 7677-7688
    • Hu, P.1    Mondmo, A.2    Skolnik, E.Y.3    Schlessinger, J.4
  • 141
    • 0029920935 scopus 로고    scopus 로고
    • A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase structurally similar to p55PIK is generated by alternative splicing of the p85alpha gene
    • Inukai K, et al. A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase structurally similar to p55PIK is generated by alternative splicing of the p85alpha gene. J Biol Chem 1996;271:5317-5320.
    • (1996) J Biol Chem , vol.271 , pp. 5317-5320
    • Inukai, K.1
  • 142
    • 0028982198 scopus 로고
    • The structure and function of p55PIK reveal a new regulatory subunit for phosphatidylinositol 3-kinase
    • Pons S, et al. The structure and function of p55PIK reveal a new regulatory subunit for phosphatidylinositol 3-kinase. Mol Cell Biol 1995;15:4453-4465.
    • (1995) Mol Cell Biol , vol.15 , pp. 4453-4465
    • Pons, S.1
  • 143
    • 0026652899 scopus 로고
    • Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways
    • Fantl WJ, et al. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signaling pathways. Cell 1992;69:413-423.
    • (1992) Cell , vol.69 , pp. 413-423
    • Fantl, W.J.1
  • 144
    • 0025967280 scopus 로고
    • Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants
    • Varticovski L, Daley GQ, Jackson P, Baltimore D, Cantley LC. Activation of phosphatidylinositol 3-kinase in cells expressing abl oncogene variants. Mol Cell Biol 1991;11:1107-1113.
    • (1991) Mol Cell Biol , vol.11 , pp. 1107-1113
    • Varticovski, L.1    Daley, G.Q.2    Jackson, P.3    Baltimore, D.4    Cantley, L.C.5
  • 145
    • 0023897684 scopus 로고
    • Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate
    • Whitman M, Downes CP, Keeler M, Keller T, Candey L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 1988;332:644-646.
    • (1988) Nature , vol.332 , pp. 644-646
    • Whitman, M.1    Downes, C.P.2    Keeler, M.3    Keller, T.4    Candey, L.5
  • 146
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
    • Alessi DR, et al. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Curr Biol 1997;7:261-269.
    • (1997) Curr Biol , vol.7 , pp. 261-269
    • Alessi, D.R.1
  • 147
    • 0030799706 scopus 로고    scopus 로고
    • Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B
    • Stokoe D, et al. Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B. Science 1997;277:567-570.
    • (1997) Science , vol.277 , pp. 567-570
    • Stokoe, D.1
  • 148
    • 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
  • 149
    • 0032561341 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase regulation of T cell receptor-mediated interleukin-2 gene expression in normal T cells
    • Eder AM, Dominguez L, Franke TF, Ashwell JD. Phosphoinositide 3-kinase regulation of T cell receptor-mediated interleukin-2 gene expression in normal T cells. J Biol Chem 1998;273:28025-28031.
    • (1998) J Biol Chem , vol.273 , pp. 28025-28031
    • Eder, A.M.1    Dominguez, L.2    Franke, T.F.3    Ashwell, J.D.4
  • 151
    • 0028802706 scopus 로고
    • Selective CD28pYMNM mutations implicate phosphatidylinositol 3-kinase in CD86-CD28-mediated costimulation
    • Cai YC, 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
  • 152
    • 0028304998 scopus 로고
    • Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation
    • Exley M, Varticovski L, Peter M, Sancho J, Terhorst C. Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation. J Biol Chem 1994;269:15140-15146.
    • (1994) J Biol Chem , vol.269 , pp. 15140-15146
    • Exley, M.1    Varticovski, L.2    Peter, M.3    Sancho, J.4    Terhorst, C.5
  • 153
    • 0027980250 scopus 로고
    • T cell receptor-associated alpha-phosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56lck
    • Carrera A, Rodriguez-Borlado I., Martinez-Alonso C, Merida I. T cell receptor-associated alpha-phosphatidylinositol 3-kinase becomes activated by T cell receptor cross-linking and requires pp56lck. J Biol Chem 1994;269:19435-19440.
    • (1994) J Biol Chem , vol.269 , pp. 19435-19440
    • Carrera, A.1    Rodriguez-Borlado, I.2    Martinez-Alonso, C.3    Merida, I.4
  • 154
    • 0030820813 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells
    • de Aos I, et al. Tyrosine phosphorylation of the CD3-epsilon subunit of the T cell antigen receptor mediates enhanced association with phosphatidylinositol 3-kinase in Jurkat T cells. J Biol Chem 1997;272:25310-25318.
    • (1997) J Biol Chem , vol.272 , pp. 25310-25318
    • De Aos, I.1
  • 155
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DA, Alessi DR, Cohen P, Andjelkovich M, Hemmings BA. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995;378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 156
    • 0030449964 scopus 로고    scopus 로고
    • Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells
    • Stambolic V, Ruel L, Woodgett JR, Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells. Curr Biol 1996;6:1664-1668.
    • (1996) Curr Biol , vol.6 , pp. 1664-1668
    • Stambolic, V.1    Ruel, L.2    Woodgett, J.R.3
  • 157
    • 0032557646 scopus 로고    scopus 로고
    • Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inacivation. Characterization of dominant-negative mutant of PKB
    • van Weeren PC, de Bruyn KM, de Vries-Smits AM, van Lint J, Burgering BM. Essential role for protein kinase B (PKB) in insulin-induced glycogen synthase kinase 3 inactivation. Characterization of dominant-negative mutant of PKB. J Biol Chem 1998;273:13150-13156.
    • (1998) J Biol Chem , vol.273 , pp. 13150-13156
    • Van Weeren, P.C.1    De Bruyn, K.M.2    De Vries-Smits, A.M.3    Van Lint, J.4    Burgering, B.M.5
  • 158
    • 0029776032 scopus 로고    scopus 로고
    • A molecular mechanism for the effect of lithium on development
    • Klein PS, Melton DA. A molecular mechanism for the effect of lithium on development. Proc Natl Acad Sci USA 1996;93:8455-8459.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8455-8459
    • Klein, P.S.1    Melton, D.A.2
  • 160
    • 0033811659 scopus 로고    scopus 로고
    • Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation
    • Shan X, et al. Deficiency of PTEN in Jurkat T cells causes constitutive localization of Itk to the plasma membrane and hyperresponsiveness to CD3 stimulation. Mol Cell Biol 2000;20:6945-6957.
    • (2000) Mol Cell Biol , vol.20 , pp. 6945-6957
    • Shan, X.1
  • 161
    • 0035451761 scopus 로고    scopus 로고
    • PI 3-K and T-cell activation: Limitations of T-leukemic cell lines as signaling models
    • Astoul E, Cantrell DA, Edmunds C, Ward SG. PI 3-K and T-cell activation: limitations of T-leukemic cell lines as signaling models. Trends Immunol 2001;22:490-496.
    • (2001) Trends Immunol , vol.22 , pp. 490-496
    • Astoul, E.1    Cantrell, D.A.2    Edmunds, C.3    Ward, S.G.4
  • 162
    • 0030612144 scopus 로고    scopus 로고
    • p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes
    • Chantry D, et al. p110delta, a novel phosphatidylinositol 3-kinase catalytic subunit that associates with p85 and is expressed predominantly in leukocytes. J Biol Chem 1997;272:19236-19241.
    • (1997) J Biol Chem , vol.272 , pp. 19236-19241
    • Chantry, D.1
  • 163
    • 0030611198 scopus 로고    scopus 로고
    • P110delta, a novel phosphomositide 3-kinase in leukocytes
    • Vanhaesebroeck B, et al. P110delta, a novel phosphomositide 3-kinase in leukocytes. Proc Natl Acad Sci USA 1997;94:4330-4335.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4330-4335
    • Vanhaesebroeck, B.1
  • 164
    • 0037047590 scopus 로고    scopus 로고
    • Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice
    • Okkenhaug K, et al. Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice. Science 2002;297:1031-1034.
    • (2002) Science , vol.297 , pp. 1031-1034
    • Okkenhaug, K.1
  • 165
    • 0031569189 scopus 로고    scopus 로고
    • Induction of alloantigen-specific T cell tolerance through the treatment of human T lymphocytes with wortmannin
    • Taub DD, et al. Induction of alloantigen-specific T cell tolerance through the treatment of human T lymphocytes with wortmannin. J Immunol 1997;158:2745-2755.
    • (1997) J Immunol , vol.158 , pp. 2745-2755
    • Taub, D.D.1
  • 166
    • 0029090212 scopus 로고
    • Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase
    • Stoyanov B, et al. Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase. Science 1995;269:690-693.
    • (1995) Science , vol.269 , pp. 690-693
    • Stoyanov, B.1
  • 167
    • 0030887632 scopus 로고    scopus 로고
    • The G beta gamma sensitivity of a PI3K is dependent upon a tightly associated adaptor, p 101
    • Stephens LR, et al. The G beta gamma sensitivity of a PI3K is dependent upon a tightly associated adaptor, p 101. Cell 1997;89:105-114.
    • (1997) Cell , vol.89 , pp. 105-114
    • Stephens, L.R.1
  • 168
    • 0034635264 scopus 로고    scopus 로고
    • Function of PI3K in thymocyte development, T cell activation, and neutrophil migration
    • Sasaki T, et al. Function of PI3K in thymocyte development, T cell activation, and neutrophil migration. Science 2000;287:1040-1046.
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1
  • 169
    • 0035869402 scopus 로고    scopus 로고
    • Critical requirement for the membrane-proximal cytosolic tyrosine residue for CD28-mediated costimulation in vivo
    • Harada Y, et al. Critical requirement for the membrane-proximal cytosolic tyrosine residue for CD28-mediated costimulation in vivo. J Immunol 2001;166:3797-3803.
    • (2001) J Immunol , vol.166 , pp. 3797-3803
    • Harada, Y.1
  • 170
    • 0035319244 scopus 로고    scopus 로고
    • A point mutation in CD28 distinguishes proliferative signals from survival signals
    • Okkenhaug K, et al. A point mutation in CD28 distinguishes proliferative signals from survival signals. Nat Immunol 2001;2:325-332.
    • (2001) Nat Immunol , vol.2 , pp. 325-332
    • Okkenhaug, K.1
  • 171
    • 0024600222 scopus 로고
    • A ras-related gene with transformation suppressor activity
    • Kitayama H, Sugimoto Y, Matsuzaki T, Ikawa Y, Noda M. A ras-related gene with transformation suppressor activity. Cell 1989;56:77-84.
    • (1989) Cell , vol.56 , pp. 77-84
    • Kitayama, H.1    Sugimoto, Y.2    Matsuzaki, T.3    Ikawa, Y.4    Noda, M.5
  • 172
    • 0027170176 scopus 로고
    • RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts
    • Cook SJ, Rubinfeld B, Albert I, McCormick F. RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat-1 fibroblasts. EMBO J 1993;12:3475-3485.
    • (1993) EMBO J , vol.12 , pp. 3475-3485
    • Cook, S.J.1    Rubinfeld, B.2    Albert, I.3    McCormick, F.4
  • 173
    • 0033756553 scopus 로고    scopus 로고
    • CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein Rapl
    • Carey KD, et al. CD28 and the tyrosine kinase lck stimulate mitogen-activated protein kinase activity in T cells via inhibition of the small G protein Rapl. Mol Cell Biol 2000;20:8409-8419.
    • (2000) Mol Cell Biol , vol.20 , pp. 8409-8419
    • Carey, K.D.1
  • 174
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy, blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis VA, Freeman GJ, Berezovskaya A, Barber DL, Nadler LM. Maintenance of human T cell anergy, blocking of IL-2 gene transcription by activated Rap1. Science 1997;278:124-128.
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A.1    Freeman, G.J.2    Berezovskaya, A.3    Barber, D.L.4    Nadler, L.M.5
  • 175
    • 0036146452 scopus 로고    scopus 로고
    • Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses
    • Katagiri K, Hattori M, Minato N, Kinashi T. Rap1 functions as a key regulator of T-cell and antigen-presenting cell interactions and modulates T-cell responses. Mol Cell Biol 2002;22:1001-1015.
    • (2002) Mol Cell Biol , vol.22 , pp. 1001-1015
    • Katagiri, K.1    Hattori, M.2    Minato, N.3    Kinashi, T.4
  • 176
    • 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
  • 177
    • 0032531756 scopus 로고    scopus 로고
    • Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling
    • Zwartkruis FJ, Wolthuis RM, Nabben NM, Franke B, Bos JL. Extracellular signal-regulated activation of Rap1 fails to interfere in Ras effector signalling. EMBO J 1998;17:5905-5912.
    • (1998) EMBO J , vol.17 , pp. 5905-5912
    • Zwartkruis, F.J.1    Wolthuis, R.M.2    Nabben, N.M.3    Franke, B.4    Bos, J.L.5
  • 179
    • 0031687777 scopus 로고    scopus 로고
    • Signal transduction via Ras
    • Wittinghofer A. Signal transduction via Ras. Biol Chem 1998;379:933-937.
    • (1998) Biol Chem , vol.379 , pp. 933-937
    • Wittinghofer, A.1
  • 180
    • 0032524389 scopus 로고    scopus 로고
    • RasGRP, a Ras guanyl nucleotide-releasing protein with calcium-and diacylglycerol-binding motifs
    • Ebinu JO, Bottorff DA, Chan EY, Stang SL, Dunn RJ, Stone JC. RasGRP, a Ras guanyl nucleotide-releasing protein with calcium-and diacylglycerol-binding motifs. Science 1998;280:1082-1086.
    • (1998) Science , vol.280 , pp. 1082-1086
    • Ebinu, J.O.1    Bottorff, D.A.2    Chan, E.Y.3    Stang, S.L.4    Dunn, R.J.5    Stone, J.C.6
  • 181
    • 0034682779 scopus 로고    scopus 로고
    • CalDAG-GEFIII activation of Ras, R-ras, and Rap1
    • Yamashita S, et al. CalDAG-GEFIII activation of Ras, R-ras, and Rap1. J Biol Chem 2000;275:25488-25493.
    • (2000) J Biol Chem , vol.275 , pp. 25488-25493
    • Yamashita, S.1
  • 182
    • 0028180585 scopus 로고
    • GRB2 and phosphohpase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation
    • Sieh M, Batzer A, Schlessinger J, Weiss A. GRB2 and phosphohpase C-gamma 1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation. Mol Cell Biol 1994;14:4435-4442.
    • (1994) Mol Cell Biol , vol.14 , pp. 4435-4442
    • Sieh, M.1    Batzer, A.2    Schlessinger, J.3    Weiss, A.4
  • 184
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994;369:411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 186
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall CJ. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr Opin Genet Dev 1994;4:82-89.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 187
    • 0029975023 scopus 로고    scopus 로고
    • Blocked signal transduction to the ERK and JNK protein kinases in anergic CD4+ T cells
    • Li W, Whaley CD, Mondino A, Mueller DL. Blocked signal transduction to the ERK and JNK protein kinases in anergic CD4+ T cells. Science 1996;271:1272-1276.
    • (1996) Science , vol.271 , pp. 1272-1276
    • Li, W.1    Whaley, C.D.2    Mondino, A.3    Mueller, D.L.4
  • 188
    • 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
  • 189
    • 0032080849 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase kinase blocks T cell
    • DeSilva DR, 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
  • 190
    • 0028881018 scopus 로고
    • Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G
    • Gotoh T, et al. Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol Cell Biol 1995;15:6746-6753.
    • (1995) Mol Cell Biol , vol.15 , pp. 6746-6753
    • Gotoh, T.1
  • 191
    • 0032480888 scopus 로고    scopus 로고
    • Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
    • de Rooij J, et al. Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 1998;396:474-477.
    • (1998) Nature , vol.396 , pp. 474-477
    • De Rooij, J.1
  • 192
    • 0032545328 scopus 로고    scopus 로고
    • A family of cAMP-binding proteins that directly activate Rap1
    • Kawasaki H, et al. A family of cAMP-binding proteins that directly activate Rap1. Science 1998;282:2275-2279.
    • (1998) Science , vol.282 , pp. 2275-2279
    • Kawasaki, H.1
  • 193
    • 13144282666 scopus 로고    scopus 로고
    • A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia
    • Kawasaki H, et al. A Rap guanine nucleotide exchange factor enriched highly in the basal ganglia. Proc Natl Acad Sci USA 1998;95:13278-13283.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13278-13283
    • Kawasaki, H.1
  • 194
    • 0035839496 scopus 로고    scopus 로고
    • Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling
    • Jin TG, et al. Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling. J Biol Chem 2001;276:30301-30307.
    • (2001) J Biol Chem , vol.276 , pp. 30301-30307
    • Jin, T.G.1
  • 195
    • 0035793468 scopus 로고    scopus 로고
    • CD98 induces LFA-1-mediated cell adhesion in lymphoid cells via activation of Rap1
    • Suga K, et al. CD98 induces LFA-1-mediated cell adhesion in lymphoid cells via activation of Rap1. FEBS Lett 2001;489:249-253.
    • (2001) FEBS Lett , vol.489 , pp. 249-253
    • Suga, K.1
  • 196
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N, Horn G, Herrmann C, Schere A, McCormick F, Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 1995;375:554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Schere, A.4    McCormick, F.5    Wittinghofer, A.6
  • 197
    • 85117738522 scopus 로고    scopus 로고
    • cAMP inhibits both Ras and Rap1 actiation in primary T cells but only Ras inhibition correlates wit blockade of cell cycle progression
    • in press
    • Grader-Beck T, van Puijenboek A, Nadler LM, Boussiotis VB. cAMP inhibits both Ras and Rap1 actiation in primary T cells but only Ras inhibition correlates wit blockade of cell cycle progression. Blood in press.
    • Blood
    • Grader-Beck, T.1    Van Puijenboek, A.2    Nadler, L.M.3    Boussiotis, V.B.4
  • 198
    • 0034996666 scopus 로고    scopus 로고
    • Cyclic AMP-mediated inhibition of cell growth requires the small G protein Rap1
    • Schmitt JM, Stork PJ. Cyclic AMP-mediated inhibition of cell growth requires the small G protein Rap1. Mol Cell Biol 2001;21:3671-3683.
    • (2001) Mol Cell Biol , vol.21 , pp. 3671-3683
    • Schmitt, J.M.1    Stork, P.J.2
  • 199
    • 0026567027 scopus 로고
    • The role of cell division in the induction of clonal allergy
    • Jenkins MK. The role of cell division in the induction of clonal allergy. Immunol Today 1992;13:69-73.
    • (1992) Immunol Today , vol.13 , pp. 69-73
    • Jenkins, M.K.1
  • 200
    • 0033104824 scopus 로고    scopus 로고
    • Inhibition of cell cycle progression by rapamycin induces T cell clonal anergy even in the presence of costimulation
    • Powell JD, Lerner CG, Schwartz RH. Inhibition of cell cycle progression by rapamycin induces T cell clonal anergy even in the presence of costimulation. J Immunol 1999;162:2775-2784.
    • (1999) J Immunol , vol.162 , pp. 2775-2784
    • Powell, J.D.1    Lerner, C.G.2    Schwartz, R.H.3
  • 201
    • 0025899598 scopus 로고
    • Development and function oft cells in mice rendered interleukin-2 deficient by gene targeting
    • Schorle H, Holtschke T, Hunig T, Schimpl A, Horak I. Development and function oft cells in mice rendered interleukin-2 deficient by gene targeting. Nature 1991;352:621-624.
    • (1991) Nature , vol.352 , pp. 621-624
    • Schorle, H.1    Holtschke, T.2    Hunig, T.3    Schimpl, A.4    Horak, I.5
  • 202
    • 0033016465 scopus 로고    scopus 로고
    • CD28 induces cell cycle progression by IL-2-independent down-regulation of p27kip1 expression in human peripheral T lymphocytes
    • Boonen GJ, van Dijk AM, Verdonck LF, van Lier RA, Rijksen G, Medema RH. CD28 induces cell cycle progression by IL-2-independent down-regulation of p27kip1 expression in human peripheral T lymphocytes. Eur J Immunol 1999;29:789-798.
    • (1999) Eur J Immunol , vol.29 , pp. 789-798
    • Boonen, G.J.1    Van Dijk, A.M.2    Verdonck, L.F.3    Van Lier, R.A.4    Rijksen, G.5    Medema, R.H.6
  • 203
    • 0033976064 scopus 로고    scopus 로고
    • CD28 costimulation mediates T cell expansion via IL-2-independent and IL-2-dependent regulation of cell cycle progression
    • Appleman LJ, Berezovskaya A, Grass I, Boussiotis VA. CD28 costimulation mediates T cell expansion via IL-2-independent and IL-2-dependent regulation of cell cycle progression. J Immunol 2000;164:144-151.
    • (2000) J Immunol , vol.164 , pp. 144-151
    • Appleman, L.J.1    Berezovskaya, A.2    Grass, I.3    Boussiotis, V.A.4
  • 204
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev 1999;13:1501-1512.
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 205
    • 0028176483 scopus 로고
    • Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals
    • Polyak K, et al. Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals. Cell 1994;78:59-66.
    • (1994) Cell , vol.78 , pp. 59-66
    • Polyak, K.1
  • 206
    • 0030010591 scopus 로고    scopus 로고
    • kip1 display increased body size, multiple organ hyperplasia, retinal dysplasia and pituitary tumors
    • kip1 display increased body size, multiple organ hyperplasia, retinal dysplasia and pituitary tumors. Cell 1996;85:707-720.
    • (1996) Cell , vol.85 , pp. 707-720
    • Nakayama, K.1
  • 209
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet A, et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 1999;96:857-868.
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 210
    • 0028941483 scopus 로고
    • Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD
    • Halevy O, et al. Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD. Science 1995;267:1018-1021.
    • (1995) Science , vol.267 , pp. 1018-1021
    • Halevy, O.1
  • 211
    • 0029024015 scopus 로고
    • Role of the ubiquitin-proteosome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
    • Pagano M, et al. Role of the ubiquitin-proteosome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 1995;269:682-685.
    • (1995) Science , vol.269 , pp. 682-685
    • Pagano, M.1
  • 212
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, Pagano M. SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999;1:193-199.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 213
    • 0033578073 scopus 로고    scopus 로고
    • p27 (Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27
    • Tsvetkov LM, Yeh KH, Lee SJ, Sun H, Zhang H. p27 (Kip1) ubiquitination and degradation is regulated by the SCF(Skp2) complex through phosphorylated Thr187 in p27. Curr Biol 1999;9:661-664.
    • (1999) Curr Biol , vol.9 , pp. 661-664
    • Tsvetkov, L.M.1    Yeh, K.H.2    Lee, S.J.3    Sun, H.4    Zhang, H.5
  • 214
    • 0035092687 scopus 로고    scopus 로고
    • The cell-cycle regulatory protein Cks1 is required for SCFSkp2-mediated ubiquitinylation of p27
    • Ganoth D, et al. The cell-cycle regulatory protein Cks1 is required for SCFSkp2-mediated ubiquitinylation of p27. Nat Cell Biol 2001;3:321-324.
    • (2001) Nat Cell Biol , vol.3 , pp. 321-324
    • Ganoth, D.1
  • 215
    • 0035265829 scopus 로고    scopus 로고
    • A CDK-independent function of mammalian Cks1. Targeting of SCF(Skp2) to the CDK inhibitor p27(Kip1)
    • Spruck C, et al. A CDK-independent function of mammalian Cks1. Targeting of SCF(Skp2) to the CDK inhibitor p27(Kip1). Mol Cell 2001;7:639-650.
    • (2001) Mol Cell , vol.7 , pp. 639-650
    • Spruck, C.1
  • 216
    • 0034595292 scopus 로고    scopus 로고
    • Kip1, polyploidy and centrosome overduplication
    • Kip1, polyploidy and centrosome overduplication. EMBO J 2000;19:2069-2081.
    • (2000) EMBO J , vol.19 , pp. 2069-2081
    • Nakayama, K.1
  • 217
    • 0035956971 scopus 로고    scopus 로고
    • Role of the F-box protein Skp2 in lymphomagenesis
    • Latres E, et al. Role of the F-box protein Skp2 in lymphomagenesis. Proc Natl Acad Sci USA 2001;98:2515-2520.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2515-2520
    • Latres, E.1
  • 218
    • 0031874024 scopus 로고    scopus 로고
    • CD28 affects the earliest signaling events generated by TCR engagement
    • Tuosto L, Acuto O. CD28 affects the earliest signaling events generated by TCR engagement. Eur J Immunol 1998;28:2131-2142.
    • (1998) Eur J Immunol , vol.28 , pp. 2131-2142
    • Tuosto, L.1    Acuto, O.2
  • 219
    • 0031037183 scopus 로고    scopus 로고
    • Requirements for peptide-induced T cell receptor downregulation on naive CDS+ T cells
    • Cai Z, Kishimoto H, Brunmark A, Jackson MR, Peterson PA, Sprent J. Requirements for peptide-induced T cell receptor downregulation on naive CDS+ T cells. J Exp Med 1997;185:641-651.
    • (1997) J Exp Med , vol.185 , pp. 641-651
    • Cai, Z.1    Kishimoto, H.2    Brunmark, A.3    Jackson, M.R.4    Peterson, P.A.5    Sprent, J.6
  • 220
    • 0033613826 scopus 로고    scopus 로고
    • T lymphocyte costimulation mediated by reorganization of membrane microdomains
    • Viola A, Schroeder S, Sakakibara Y, Lanzavecchia A. T lymphocyte costimulation mediated by reorganization of membrane microdomains. Science 1999;283:680-682.
    • (1999) Science , vol.283 , pp. 680-682
    • Viola, A.1    Schroeder, S.2    Sakakibara, Y.3    Lanzavecchia, A.4
  • 221
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation dusters in T cells
    • Monks CR, Freiberg BA, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation dusters in T cells. Nature 1998;395:82-86.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.