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1
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0030056468
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Models of T cell anergy: Is there a common molecular mechanism
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of special interest. This presents an overview of the various models of anergy described in the current literature and attempts to provide a common mechanism for the different models of T cell unresponsiveness.
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Schwartz RH. Models of T cell anergy: is there a common molecular mechanism. of special interest J Exp Med. 184:1996;1-8 This presents an overview of the various models of anergy described in the current literature and attempts to provide a common mechanism for the different models of T cell unresponsiveness.
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(1996)
J Exp Med
, vol.184
, pp. 1-8
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Schwartz, R.H.1
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4
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0028337459
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Comparative analysis of B7-1 and B7-2 co-stimulatory ligands: Expression and function
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Hathcock KS, Laszlo SG, Pucillo C, Linsley PS, Hodes RJ. Comparative analysis of B7-1 and B7-2 co-stimulatory ligands: expression and function. J Exp Med. 180:1994;631-640.
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(1994)
J Exp Med
, vol.180
, pp. 631-640
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-
Hathcock, K.S.1
Laszlo, S.G.2
Pucillo, C.3
Linsley, P.S.4
Hodes, R.J.5
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5
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0028032963
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The tissue distribution of the B7-2 co-stimulator in mice: Abundant expression on dendritic cells in situ and during maturation in vitro
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Inaba K, Witmer-Pack M, Inaba M, Hathcock KS, Sakuta H, Azuma M, Yagita H, Okumura K, Linsley PS, Ikehara S, et al. The tissue distribution of the B7-2 co-stimulator in mice: abundant expression on dendritic cells in situ and during maturation in vitro. J Exp Med. 180:1994;1849-1860.
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(1994)
J Exp Med
, vol.180
, pp. 1849-1860
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-
Inaba, K.1
Witmer-Pack, M.2
Inaba, M.3
Hathcock, K.S.4
Sakuta, H.5
Azuma, M.6
Yagita, H.7
Okumura, K.8
Linsley, P.S.9
Ikehara, S.10
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6
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0028023526
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Differential up-regulation of the B7-1 and B7-2 co-stimulatory molecules after Ig receptor engagement by antigen
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Lenschow DJ, Sperling AI, Cooke MP, Freeman G, Rhee L, Decker DC, Gray G, Nadler LM, Goodnow CC, Bluestone JA. Differential up-regulation of the B7-1 and B7-2 co-stimulatory molecules after Ig receptor engagement by antigen. J Immunol. 153:1994;1990-1997.
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(1994)
J Immunol
, vol.153
, pp. 1990-1997
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Lenschow, D.J.1
Sperling, A.I.2
Cooke, M.P.3
Freeman, G.4
Rhee, L.5
Decker, D.C.6
Gray, G.7
Nadler, L.M.8
Goodnow, C.C.9
Bluestone, J.A.10
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7
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0029744798
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Requirement for CD40 ligand in co-stimulation induction, T cell activation, and experimental allergic encephalomyelitis
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Grewal IS, Foellmer HG, Grewal KD, Xu J, Hardardottir F, Baron JL, Janeway CA Jr, Flavell RA. Requirement for CD40 ligand in co-stimulation induction, T cell activation, and experimental allergic encephalomyelitis. Science. 273:1996;1864-1867.
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(1996)
Science
, vol.273
, pp. 1864-1867
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-
Grewal, I.S.1
Foellmer, H.G.2
Grewal, K.D.3
Xu, J.4
Hardardottir, F.5
Baron, J.L.6
Janeway C.A., Jr.7
Flavell, R.A.8
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8
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0029780119
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CD40 ligand-dependent T cell activation: Requirement of B7-CD28 signaling through CD40
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Yang Y, Wilson JM. CD40 ligand-dependent T cell activation: requirement of B7-CD28 signaling through CD40. Science. 273:1996;1862-1864.
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(1996)
Science
, vol.273
, pp. 1862-1864
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Yang, Y.1
Wilson, J.M.2
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9
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0028825121
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Localization in situ of the co-stimulatory molecules B7.1, B7.2, CD40 and their ligands in normal human lymphoid tissue
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of special interest. This paper examines the spatial expression patterns of CD80, CD86, CD40, CD28 and CTLA-4 on sections of human tonsillar lymph nodes. There was an obvious gradient of expression of B7.1 and B7.2 within the germinal center. Furthermore, the results demonstrate the punctate pattern of CTLA-4 expression in the cytoplasm of T cells, and little membrane surface labeling.
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Vyth-Dreese FA, Dellemijn TAM, Majoor D, Dejong D. Localization in situ of the co-stimulatory molecules B7.1, B7.2, CD40 and their ligands in normal human lymphoid tissue. of special interest Eur J Immunol. 25:1995;3023-3029 This paper examines the spatial expression patterns of CD80, CD86, CD40, CD28 and CTLA-4 on sections of human tonsillar lymph nodes. There was an obvious gradient of expression of B7.1 and B7.2 within the germinal center. Furthermore, the results demonstrate the punctate pattern of CTLA-4 expression in the cytoplasm of T cells, and little membrane surface labeling.
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(1995)
Eur J Immunol
, vol.25
, pp. 3023-3029
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Vyth-Dreese, F.A.1
Dellemijn, T.A.M.2
Majoor, D.3
Dejong, D.4
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10
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0030300154
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The complexities of T-cell co-stimulation: CD28 and beyond
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Sperling AI, Bluestone JA. The complexities of T-cell co-stimulation: CD28 and beyond. Immunol Rev. 153:1996;155-182.
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(1996)
Immunol Rev
, vol.153
, pp. 155-182
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Sperling, A.I.1
Bluestone, J.A.2
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11
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0031568065
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CD28/B7 co-stimulation regulates autoimmune diabetes induced with multiple low doses of Streptozotocin
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Herold KC, Vezys V, Koons A, Lenschow D, Thompson C, Bluestone JA. CD28/B7 co-stimulation regulates autoimmune diabetes induced with multiple low doses of Streptozotocin. J Immunol. 158:1997;984-991.
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(1997)
J Immunol
, vol.158
, pp. 984-991
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Herold, K.C.1
Vezys, V.2
Koons, A.3
Lenschow, D.4
Thompson, C.5
Bluestone, J.A.6
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12
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0031036085
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CD80 co-stimulation is essential for the induction of airway eosinophilia
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Harris N, Peach R, Naemura J, Linsley PS, Le Gros G, Ronchese F. CD80 co-stimulation is essential for the induction of airway eosinophilia. J Exp Med. 185:1997;177-182.
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(1997)
J Exp Med
, vol.185
, pp. 177-182
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Harris, N.1
Peach, R.2
Naemura, J.3
Linsley, P.S.4
Le Gros, G.5
Ronchese, F.6
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15
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0030992445
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T cell-mediated elimination of B7.2 transgenic B cells
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of special interest. This paper describes the T-cell mediated elimination of B cells in mice expressing a B7.2 transgene. These cells are not eliminated in the presence of activated antigen-specific T cells or in the absence of CD28. The authors propose a novel mechanism for maintaining B cell homeostasis by T cells in the absence of an ongoing immune response.
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Fournier S, Rathwell J, Goodnow C, Allison JP. T cell-mediated elimination of B7.2 transgenic B cells. of special interest Immunity. 6:1997;327-339 This paper describes the T-cell mediated elimination of B cells in mice expressing a B7.2 transgene. These cells are not eliminated in the presence of activated antigen-specific T cells or in the absence of CD28. The authors propose a novel mechanism for maintaining B cell homeostasis by T cells in the absence of an ongoing immune response.
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(1997)
Immunity
, vol.6
, pp. 327-339
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Fournier, S.1
Rathwell, J.2
Goodnow, C.3
Allison, J.P.4
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16
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0027937702
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Complementarity determining region 1 (CDR1)- And CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1
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Peach RJ, Bajorath J, Brady W, Leytze G, Greene J, Naemura J, Linsley PS. Complementarity determining region 1 (CDR1)- and CDR3-analogous regions in CTLA-4 and CD28 determine the binding to B7-1. J Exp Med. 180:1994;2049-2058.
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(1994)
J Exp Med
, vol.180
, pp. 2049-2058
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Peach, R.J.1
Bajorath, J.2
Brady, W.3
Leytze, G.4
Greene, J.5
Naemura, J.6
Linsley, P.S.7
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17
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0031054242
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CD80 (B7-1) binds both CD28 and CTLA-4 with a low affinity and very fast kinetics
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of special interest. The binding affinity values of monomeric CTLA-4 and CD28 for B7.1 molecules were determined using surface plasmon resonance and were found to be lower than previously reported. CD28 and CTLA-4 were shown to have binding kinetics which are similar to CD2 - CD58 but faster than TCR - MHC - peptide interactions. The results also demonstrate that CTLA-4 has a dramatically higher avidity than CD28 for B7. See also [18].
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Van der Merwe PA, Bodian DL, Daenke S, Linsley P, Davis SJ. CD80 (B7-1) binds both CD28 and CTLA-4 with a low affinity and very fast kinetics. of special interest J Exp Med. 185:1997;393-404 The binding affinity values of monomeric CTLA-4 and CD28 for B7.1 molecules were determined using surface plasmon resonance and were found to be lower than previously reported. CD28 and CTLA-4 were shown to have binding kinetics which are similar to CD2 - CD58 but faster than TCR - MHC - peptide interactions. The results also demonstrate that CTLA-4 has a dramatically higher avidity than CD28 for B7. See also [18].
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(1997)
J Exp Med
, vol.185
, pp. 393-404
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Van Der Merwe, P.A.1
Bodian, D.L.2
Daenke, S.3
Linsley, P.4
Davis, S.J.5
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18
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0029914089
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Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell co-stimulatory interactions
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of special interest. See annotation [17]. In addition, this study demonstrates the importance of B7 clustering and CTLA-4 homodimerization for the high avidity displayed by CTLA-4 binding to ligand. This has important implications for understanding the balance between CD28 and CTLA-4 ligand binding and resultant signaling
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Greene JL, Leytze GM, Emswiler J, Peach R, Bajorath J, Cosand W, Linsley PS. Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell co-stimulatory interactions. of special interest J Biol Chem. 271:1996;26762-26771 See annotation [17]. In addition, this study demonstrates the importance of B7 clustering and CTLA-4 homodimerization for the high avidity displayed by CTLA-4 binding to ligand. This has important implications for understanding the balance between CD28 and CTLA-4 ligand binding and resultant signaling.
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(1996)
J Biol Chem
, vol.271
, pp. 26762-26771
-
-
Greene, J.L.1
Leytze, G.M.2
Emswiler, J.3
Peach, R.4
Bajorath, J.5
Cosand, W.6
Linsley, P.S.7
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19
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0028675006
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Human B7-1 (CD80) and B7-2 (CD86) bind with similar avidities but distinct kinetics to CD28 and CTLA-4 receptors
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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. 1:1994;793-801.
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(1994)
Immunity
, vol.1
, pp. 793-801
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-
Linsley, P.S.1
Greene, J.L.2
Brady, W.3
Bajorath, J.4
Ledbetter, J.A.5
Peach, R.6
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20
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0030030181
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Differential effects of CTLA-4 substitutions on the binding of human CD80 (B7-1) and CD86 (B7-2)
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Morton PA, Fu X-T, Stewart JA, Giacoletto KS, White SL, Leysath CE, Evans RJ, Shieh J-J, Karr RW. Differential effects of CTLA-4 substitutions on the binding of human CD80 (B7-1) and CD86 (B7-2). J Immunol. 156:1996;1047-1054.
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(1996)
J Immunol
, vol.156
, pp. 1047-1054
-
-
Morton, P.A.1
Fu, X.-T.2
Stewart, J.A.3
Giacoletto, K.S.4
White, S.L.5
Leysath, C.E.6
Evans, R.J.7
Shieh, J.-J.8
Karr, R.W.9
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21
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0029031518
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Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules
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Linsley PS, Nadler SG, Bajoirath J, Peach R, Leung HT, Rogers J, Bradshaw J, Stebbins M, Leytze G, Brady W, et al. Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4 (CTLA-4). A disulfide-linked homodimer binds two CD86 molecules. J Biol Chem. 270:1995;15417-15424.
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(1995)
J Biol Chem
, vol.270
, pp. 15417-15424
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-
Linsley, P.S.1
Nadler, S.G.2
Bajoirath, J.3
Peach, R.4
Leung, H.T.5
Rogers, J.6
Bradshaw, J.7
Stebbins, M.8
Leytze, G.9
Brady, W.10
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22
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0028484545
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CTLA-4 can function as a negative regulator of T cell activation
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Walunas TL, Lenschow DJ, Bakker CY, Linsley PS, Freeman GJ, Green JM, Thompson CB, Bluestone JA. CTLA-4 can function as a negative regulator of T cell activation. Immunity. 1:1994;405-413.
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(1994)
Immunity
, vol.1
, pp. 405-413
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-
Walunas, T.L.1
Lenschow, D.J.2
Bakker, C.Y.3
Linsley, P.S.4
Freeman, G.J.5
Green, J.M.6
Thompson, C.B.7
Bluestone, J.A.8
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23
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0026486220
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Coexpression and functional cooperativity of CTLA-4 and CD28 on activated T lymphocytes
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Linsley PS, Greene JL, Tan P, Bradshaw J, Ledbetter JA, Anasetti C, Damle NK. Coexpression and functional cooperativity of CTLA-4 and CD28 on activated T lymphocytes. J Exp Med. 176:1992;1595-1604.
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(1992)
J Exp Med
, vol.176
, pp. 1595-1604
-
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Linsley, P.S.1
Greene, J.L.2
Tan, P.3
Bradshaw, J.4
Ledbetter, J.A.5
Anasetti, C.6
Damle, N.K.7
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24
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0029120245
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CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation
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of special interest. This paper provides the first direct evidence that cross-linking CTLA-4 in vitro provides an inhibitory signal which inhibits proliferation and cytokine production by naive lymph node T cells stimulated with anti-CD3 and anti-CD28 antibodies. See also [41].
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Krummel MF, Allison JP. CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation. of special interest J Exp Med. 182:1995;459-465 This paper provides the first direct evidence that cross-linking CTLA-4 in vitro provides an inhibitory signal which inhibits proliferation and cytokine production by naive lymph node T cells stimulated with anti-CD3 and anti-CD28 antibodies. See also [41].
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(1995)
J Exp Med
, vol.182
, pp. 459-465
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Krummel, M.F.1
Allison, J.P.2
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25
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0027282960
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Characterization of CTLA-4 structure and expression on human T cells
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Lindsten T, Lee KP, Harris ES, Petryniak B, Craighead N, Reynolds PJ, Lombard DB, Freeman GJ, Nadler LM, et al. Characterization of CTLA-4 structure and expression on human T cells. J Immunol. 151:1993;3489-3499.
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(1993)
J Immunol
, vol.151
, pp. 3489-3499
-
-
Lindsten, T.1
Lee, K.P.2
Harris, E.S.3
Petryniak, B.4
Craighead, N.5
Reynolds, P.J.6
Lombard, D.B.7
Freeman, G.J.8
Nadler, L.M.9
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26
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0028500255
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Absence of B7-dependent responses in CD28-deficient mice
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Green JM, Noel PJ, Sperling AI, Walnunas TL, Gray GS, Bluestone JA, Thompson CB. Absence of B7-dependent responses in CD28-deficient mice. Immunity. 1:1994;501-508.
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(1994)
Immunity
, vol.1
, pp. 501-508
-
-
Green, J.M.1
Noel, P.J.2
Sperling, A.I.3
Walnunas, T.L.4
Gray, G.S.5
Bluestone, J.A.6
Thompson, C.B.7
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27
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15844380367
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Regulation of CTLA-4 expression during T cell activation
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Perkins D, Wang Z, Donovan C, He H, Mark D, Guan G, Wang Y, Walunase T, Bluestone J, Listman J. Regulation of CTLA-4 expression during T cell activation. J Immunol. 156:1996;4154-4159.
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(1996)
J Immunol
, vol.156
, pp. 4154-4159
-
-
Perkins, D.1
Wang, Z.2
Donovan, C.3
He, H.4
Mark, D.5
Guan, G.6
Wang, Y.7
Walunase, T.8
Bluestone, J.9
Listman, J.10
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28
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0028852073
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Cytotoxic T lymphocyte-associated molecule-4, a high avidity receptor for CD80 and CD86, contains an intracellular localization motif in its cytoplasmic tail
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of outstanding interest. This paper directly demonstrates the distinct protein expression pattern of CTLA-4 and identifies the tyrosine residue in the PI3-K binding motif (YxxM, in single-letter amino acid code; x represents any amino acid) as being essential for the intracellular localization of CTLA-4 in the perinuclear Golgi or post-Golgi compartment
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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. of outstanding interest J Biol Chem. 270:1995;1-8 This paper directly demonstrates the distinct protein expression pattern of CTLA-4 and identifies the tyrosine residue in the PI3-K binding motif (YxxM, in single-letter amino acid code; x represents any amino acid) as being essential for the intracellular localization of CTLA-4 in the perinuclear Golgi or post-Golgi compartment.
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(1995)
J Biol Chem
, vol.270
, pp. 1-8
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-
Leung, H.T.1
Bradshaw, J.2
Cleaveland, J.S.3
Linsley, P.S.4
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29
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0030176371
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Intracellular trafficking of CTLA-4 and focal localization towards sites of TCR engagement
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of outstanding interest. In this paper, the intracellular trafficking of CTLA-4 in activated human T cells is examined. These results demonstrate that CTLA-4 trafficks from the intracellular stores to the surface of the T cells. This expression is vectorial and is directed towards the site of TCR engagement. CTLA-4 is rapidly endocytosed into endosomes, the rate of which is differentially regulated to that of trafficking to the surface.
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Linsley PS, Bradshaw J, Greene J, Peach R, Bennett KL, Mittler RS. Intracellular trafficking of CTLA-4 and focal localization towards sites of TCR engagement. of outstanding interest Immunity. 4:1996;535-543 In this paper, the intracellular trafficking of CTLA-4 in activated human T cells is examined. These results demonstrate that CTLA-4 trafficks from the intracellular stores to the surface of the T cells. This expression is vectorial and is directed towards the site of TCR engagement. CTLA-4 is rapidly endocytosed into endosomes, the rate of which is differentially regulated to that of trafficking to the surface.
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(1996)
Immunity
, vol.4
, pp. 535-543
-
-
Linsley, P.S.1
Bradshaw, J.2
Greene, J.3
Peach, R.4
Bennett, K.L.5
Mittler, R.S.6
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30
-
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0030443168
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Regulation of surface and intracellular expression of CTLA-4 on mouse T cells
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Alegré M-L, Noel PJ, Eisfelder BJ, Chuang E, Clark MR, Reiner SL, Thompson CB. Regulation of surface and intracellular expression of CTLA-4 on mouse T cells. J Immunol. 157:1996;4762-4770.
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(1996)
J Immunol
, vol.157
, pp. 4762-4770
-
-
Alegré, M.-L.1
Noel, P.J.2
Eisfelder, B.J.3
Chuang, E.4
Clark, M.R.5
Reiner, S.L.6
Thompson, C.B.7
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31
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0028859279
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Protein modules and signalling networks
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Pawson T. Protein modules and signalling networks. Nature. 373:1995;573-580.
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(1995)
Nature
, vol.373
, pp. 573-580
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Pawson, T.1
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32
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0028351218
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Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites
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Joly M, Kazlauskas A, Fay FS, Corvera S. Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Science. 263:1994;684-687.
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(1994)
Science
, vol.263
, pp. 684-687
-
-
Joly, M.1
Kazlauskas, A.2
Fay, F.S.3
Corvera, S.4
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33
-
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0027281691
-
Differential T cell co-stimulatory requirements in CD28-deficient mice
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Shahinian A, Pfeffer K, Lee KP, Kundig TM, Kishihara K, Wakeham A, Kawai K, Ohashi PS, Thompson CB, Mak TW. Differential T cell co-stimulatory requirements in CD28-deficient mice. Science. 261:1993;609-612.
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(1993)
Science
, vol.261
, pp. 609-612
-
-
Shahinian, A.1
Pfeffer, K.2
Lee, K.P.3
Kundig, T.M.4
Kishihara, K.5
Wakeham, A.6
Kawai, K.7
Ohashi, P.S.8
Thompson, C.B.9
Mak, T.W.10
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34
-
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0029984775
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Induction of unresponsiveness and impaired T cell expansion by Stephylococcal enterotoxin B in CD28-deficient mice
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Mittrücker H-W, Shahinian A, Bouchard D, Kündig TM, Mak TW. Induction of unresponsiveness and impaired T cell expansion by Stephylococcal enterotoxin B in CD28-deficient mice. J Exp Med. 183:1996;2481-2488.
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(1996)
J Exp Med
, vol.183
, pp. 2481-2488
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Mittrücker, H.-W.1
Shahinian, A.2
Bouchard, D.3
Kündig, T.M.4
Mak, T.W.5
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35
-
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0029945194
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Protection against lethal toxic shock by targeted disruption of the CD28 gene
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Saha B, Harlan DM, Lee KP, June CH, Abe R. Protection against lethal toxic shock by targeted disruption of the CD28 gene. J Exp Med. 183:1996;2675-2680.
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(1996)
J Exp Med
, vol.183
, pp. 2675-2680
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Saha, B.1
Harlan, D.M.2
Lee, K.P.3
June, C.H.4
Abe, R.5
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36
-
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0029989758
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CD28 is required for germinal center formation
-
of special interest. This paper demonstrates that germinal centers are not formed in the absence of CD28
-
Ferguson SE, Han S, Kelsoe G, Thompson CB. CD28 is required for germinal center formation. of special interest J Immunol. 156:1996;4576-4581 This paper demonstrates that germinal centers are not formed in the absence of CD28.
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(1996)
J Immunol
, vol.156
, pp. 4576-4581
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-
Ferguson, S.E.1
Han, S.2
Kelsoe, G.3
Thompson, C.B.4
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37
-
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0029031023
-
Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response
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Lucas PJ, Negishi I, Nakayama K-I, Fields LE, Loh DY. Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response. J Immunol. 154:1995;5757-5768.
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(1995)
J Immunol
, vol.154
, pp. 5757-5768
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-
Lucas, P.J.1
Negishi, I.2
Nakayama, K.-I.3
Fields, L.E.4
Loh, D.Y.5
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38
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1842373718
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Duration of TCR stimulation determines co-stimulatory requirement of T cells
-
of special interest. This paper demonstrates that effective anti-viral responses can be generated in the absence of CD28 if the antigenic peptide is present throughout the duration of the response. This occurs naturally with a virulent virus and can be achieved with repeated peptide injections with a less virulent virus. These results indicate that CD28 is important for sustaining proliferative immune responses.
-
Kündig T, Shahinian A, Kawai K, Mittrücker H-W, Sebzda E, Bachmann MF, Mak TW, Ohashi PS. Duration of TCR stimulation determines co-stimulatory requirement of T cells. of special interest Immunity. 5:1996;41-52 This paper demonstrates that effective anti-viral responses can be generated in the absence of CD28 if the antigenic peptide is present throughout the duration of the response. This occurs naturally with a virulent virus and can be achieved with repeated peptide injections with a less virulent virus. These results indicate that CD28 is important for sustaining proliferative immune responses.
-
(1996)
Immunity
, vol.5
, pp. 41-52
-
-
Kündig, T.1
Shahinian, A.2
Kawai, K.3
Mittrücker, H.-W.4
Sebzda, E.5
Bachmann, M.F.6
Mak, T.W.7
Ohashi, P.S.8
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39
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0028215960
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Costimulation of T lymphocytes with integrin ligands intercellular adhesion molecule-1 or vascular cell adhesion molecule-1 induces functional expression of CTLA-4, a second receptor for B7
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Damle NK, Klussman K, Leytze G, Mydral S, Aruffo A, Ledbetter JA, Linsley PS. Costimulation of T lymphocytes with integrin ligands intercellular adhesion molecule-1 or vascular cell adhesion molecule-1 induces functional expression of CTLA-4, a second receptor for B7. J Immunol. 152:1994;2686-2697.
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Linsley, P.S.7
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40
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0029953858
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CTLA-4-ligation blocks CD28-dependent T cell activation
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of outstanding interest. See annotation [41]. In this study CTLA-4 crosslinking inhibited TCR and CD28 stimulation at 72 hours but not at 24 hours after stimulation. It remains to be determined if the differences in the kinetics between these two studies [40,41] is due to the experimental protocols
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Walunas TL, Bakker CY, Bluestone JA. CTLA-4-ligation blocks CD28-dependent T cell activation. of outstanding interest J Exp Med. 183:1996;2541-2550 See annotation [41]. In this study CTLA-4 crosslinking inhibited TCR and CD28 stimulation at 72 hours but not at 24 hours after stimulation. It remains to be determined if the differences in the kinetics between these two studies [40,41] is due to the experimental protocols.
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Walunas, T.L.1
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41
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0029899783
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CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells
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of outstanding interest. This paper confirms and extends the results described in [24]. It demonstrates that CTLA-4-mediated inhibition of anti-CD3/CD28 antibody-induced proliferation of naive lymph node T cells was not due to apoptosis. Rather, CTLA-4 cross-linking blocked entry into the G1 phase of the cell cycle and inhibited the upregulation of CD69 and CD25 as early as 24 hours after stimulation. These results indicate that CTLA-4 may act much earlier than previously proposed [2,52], and suggest that CTLA-4 may regulate the initiation of T cell responses. See also [40].
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Krummel MF, Allison JP. CTLA-4 engagement inhibits IL-2 accumulation and cell cycle progression upon activation of resting T cells. of outstanding interest J Exp Med. 183:1996;2533-2540 This paper confirms and extends the results described in [24]. It demonstrates that CTLA-4-mediated inhibition of anti-CD3/CD28 antibody-induced proliferation of naive lymph node T cells was not due to apoptosis. Rather, CTLA-4 cross-linking blocked entry into the G1 phase of the cell cycle and inhibited the upregulation of CD69 and CD25 as early as 24 hours after stimulation. These results indicate that CTLA-4 may act much earlier than previously proposed [2,52], and suggest that CTLA-4 may regulate the initiation of T cell responses. See also [40].
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Krummel, M.F.1
Allison, J.P.2
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42
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0029100024
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+ T cells in vivo is dependent on CD28 co-stimulation and inhibited by CTLA-4
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of special interest. This is the first demonstration that CTLA-4 blockade can augment antigen-specific T cell responses in vivo. Adoptively transferred TCR transgenic T cells expanded in response to immunization with peptide, and this response was augmented by anti-CTLA-4 antibody treatment. Interestingly, antibody treatment did not alter the kinetics of the downregulation of the response.
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+ T cells in vivo is dependent on CD28 co-stimulation and inhibited by CTLA-4. of special interest J Immunol. 155:1995;1032-1036 This is the first demonstration that CTLA-4 blockade can augment antigen-specific T cell responses in vivo. Adoptively transferred TCR transgenic T cells expanded in response to immunization with peptide, and this response was augmented by anti-CTLA-4 antibody treatment. Interestingly, antibody treatment did not alter the kinetics of the downregulation of the response.
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Kearney, E.R.1
Walunas, T.L.2
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Bluestone, J.A.6
Jenkins, M.K.7
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43
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Krummel, M.F.1
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Allison, J.P.3
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44
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0031047696
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Specific blockade of CTLA-4/B7 interactions results in exacerbated clinical and histological disease in an actively-induced model of experimental allergic encephalomyelitis
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Hurwitz AA, Sullivan TJ, Krummel MF, Sobel RA, Allison JP. Specific blockade of CTLA-4/B7 interactions results in exacerbated clinical and histological disease in an actively-induced model of experimental allergic encephalomyelitis. J Neuroimmunol. 73:1996;57-62.
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Allison, J.P.5
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45
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0030586626
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Racke, M.K.5
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47
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Leach, D.R.1
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Allison, J.P.3
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48
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0028791059
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CTLA-4 deficiency causes lymphoproliferative disorder with early lethality
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Waterhouse P, Penninger JM, Timms E, Wakeham A, Shanhinian A, Lee KP, Thompson CB, Griesser H, Mak TW. CTLA-4 deficiency causes lymphoproliferative disorder with early lethality. of outstanding interest Science. 270:1995;985-988 See annotation [49].
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Waterhouse, P.1
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Shanhinian, A.5
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Thompson, C.B.7
Griesser, H.8
Mak, T.W.9
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49
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0028867420
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Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role for CTLA-4
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-/- mice [33,37,indicating that CTLA-4 and CD28 have distinct functions.
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Tivol, E.A.1
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0028146530
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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 the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line. Proc Natl Acad Sci USA. 91:1994;9347-9351.
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Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4
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of special interest. This paper demonstrates that a number of molecules known to be involved in TCR signaling are hyperphosphorylated in the T cells from CTLA-4 knockout animals. Furthermore, catalytically active SHP-2 (PTP-1D, SYP) was shown to be bound to cytoplasmic tail of CTLA-4. The authors suggest that this tyrosine phosphatase is essential for the CTLA-4-mediated inhibitory signal by directly dephosphorylating members of the Ras-activating pathway.
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Marengere LEM, Waterhouse P, Duncan GS, Mittrucker H-W, Feng G-S, Mak TW. Regulation of T cell receptor signaling by tyrosine phosphatase SYP association with CTLA-4. of special interest Science. 272:1996;1170-1173 This paper demonstrates that a number of molecules known to be involved in TCR signaling are hyperphosphorylated in the T cells from CTLA-4 knockout animals. Furthermore, catalytically active SHP-2 (PTP-1D, SYP) was shown to be bound to cytoplasmic tail of CTLA-4. The authors suggest that this tyrosine phosphatase is essential for the CTLA-4-mediated inhibitory signal by directly dephosphorylating members of the Ras-activating pathway.
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Marengere, L.E.M.1
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58
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Lanier LL. Natural killer cell receptors and MHC class I interactions. of special interest Curr Opin Immunol. 9:1997;126-131 This is a comprehensive review of inhibitory NK receptors, particularly those on human NK cells, including their specificity, function and signal transduction.
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of special interest. This is the first report to provide a molecular mechanism for the KIR- and Ly49-mediated inhibition of cytotoxicity.
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Burshtyn DN, Scharenberg AM, Wagtmann N, Rajagopalan S, Berrada K, Yi T, Kinet J-P, Long EO. Recruitment of tyrosine phosphatase HCP by the killer cell inhibitory receptor. of special interest Immunity. 4:1996;77-85 This is the first report to provide a molecular mechanism for the KIR- and Ly49-mediated inhibition of cytotoxicity.
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Burshtyn, D.N.1
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