메뉴 건너뛰기




Volumn 121, Issue 12, 2011, Pages 4758-4774

T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice

Author keywords

[No Author keywords available]

Indexed keywords

ANTINUCLEAR ANTIBODY; CYTOKINE; PROTEIN TYROSINE PHOSPHATASE; T LYMPHOCYTE RECEPTOR;

EID: 84055191068     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI59492     Document Type: Article
Times cited : (177)

References (75)
  • 2
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • DOI 10.1038/sj.onc.1208074
    • Palacios EH, Weiss A. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene. 2004;23(48):7990-8000. (Pubitemid 39468856)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7990-8000
    • Palacios, E.H.1    Weiss, A.2
  • 3
    • 61849128182 scopus 로고    scopus 로고
    • T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance
    • Salmond RJ, Filby A, Qureshi I, Caserta S, Zamoyska R. T-cell receptor proximal signaling via the Src-family kinases, Lck and Fyn, influences T-cell activation, differentiation, and tolerance. Immunol Rev. 2009;228(1):9-22.
    • (2009) Immunol Rev , vol.228 , Issue.1 , pp. 9-22
    • Salmond, R.J.1    Filby, A.2    Qureshi, I.3    Caserta, S.4    Zamoyska, R.5
  • 4
    • 61349149901 scopus 로고    scopus 로고
    • Affinity threshold for thymic selection through a T-cell receptor-co-receptor zipper
    • Palmer E, Naeher D. Affinity threshold for thymic selection through a T-cell receptor-co-receptor zipper. Nat Rev Immunol. 2009;9(3):207-213.
    • (2009) Nat Rev Immunol , vol.9 , Issue.3 , pp. 207-213
    • Palmer, E.1    Naeher, D.2
  • 6
    • 0026522204 scopus 로고
    • Profound block in thymocyte development in mice lacking p56lck
    • Molina TJ, et al. Profound block in thymocyte development in mice lacking p56lck. Nature. 1992;357(6374):161-164.
    • (1992) Nature , vol.357 , Issue.6374 , pp. 161-164
    • Molina, T.J.1
  • 8
    • 33750986199 scopus 로고    scopus 로고
    • Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response
    • DOI 10.1128/MCB.00168-06
    • Lovatt M, Filby A, Parravicini V, Werlen G, Palmer E, Zamoyska R. Lck regulates the threshold of activation in primary T cells, while both Lck and Fyn contribute to the magnitude of the extracellular signal-related kinase response. Mol Cell Biol. 2006;26(22):8655-8665. (Pubitemid 44748595)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8655-8665
    • Lovatt, M.1    Filby, A.2    Parravicini, V.3    Werlen, G.4    Palmer, E.5    Zamoyska, R.6
  • 9
    • 0034613251 scopus 로고    scopus 로고
    • Long-term survival but impaired homeostatic proliferation of Naive T cells in the absence of p56lck
    • Seddon B, Legname G, Tomlinson P, Zamoyska R. Long-term survival but impaired homeostatic proliferation of Naive T cells in the absence of p56lck. Science. 2000;290(5489):127-131.
    • (2000) Science , vol.290 , Issue.5489 , pp. 127-131
    • Seddon, B.1    Legname, G.2    Tomlinson, P.3    Zamoyska, R.4
  • 10
    • 25844526684 scopus 로고    scopus 로고
    • Central tolerance: Learning self-control in the thymus
    • DOI 10.1038/nri1707
    • Hogquist KA, Baldwin TA, Jameson SC. Central tolerance: learning self-control in the thymus. Nat Rev Immunol. 2005;5(10):772-782. (Pubitemid 41400851)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.10 , pp. 772-782
    • Hogquist, K.A.1    Baldwin, T.A.2    Jameson, S.C.3
  • 12
    • 70349751653 scopus 로고    scopus 로고
    • The strength of T cell receptor signal controls the polarization of cytotoxic machinery to the immunological synapse
    • Jenkins MR, Tsun A, Stinchcombe JC, Griffiths GM. The strength of T cell receptor signal controls the polarization of cytotoxic machinery to the immunological synapse. Immunity. 2009;31(4):621-631.
    • (2009) Immunity , vol.31 , Issue.4 , pp. 621-631
    • Jenkins, M.R.1    Tsun, A.2    Stinchcombe, J.C.3    Griffiths, G.M.4
  • 13
  • 14
    • 62249131518 scopus 로고    scopus 로고
    • Complete but curtailed T-cell response to very low-affinity antigen
    • Zehn D, Lee SY, Bevan MJ. Complete but curtailed T-cell response to very low-affinity antigen. Nature. 2009;458(7235):211-214.
    • (2009) Nature , vol.458 , Issue.7235 , pp. 211-214
    • Zehn, D.1    Lee, S.Y.2    Bevan, M.J.3
  • 16
    • 76949085272 scopus 로고    scopus 로고
    • Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time
    • Aleksic M, et al. Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time. Immunity. 2010;32(2):163-174.
    • (2010) Immunity , vol.32 , Issue.2 , pp. 163-174
    • Aleksic, M.1
  • 17
    • 41949097030 scopus 로고    scopus 로고
    • The biology of interleukin-2
    • DOI 10.1146/annurev.immunol.26.021607.090357
    • Malek TR. The biology of interleukin-2. Annu Rev Immunol. 2008;26:453-479. (Pubitemid 351600382)
    • (2008) Annual Review of Immunology , vol.26 , pp. 453-479
    • Malek, T.R.1
  • 18
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • DOI 10.1016/0092-8674(89)90504-7
    • Pingel JT, Thomas ML. Evidence that the leukocyte- common antigen is required for antigeninduced T lymphocyte proliferation. Cell. 1989; 58(6):1055-1065. (Pubitemid 19238183)
    • (1989) Cell , vol.58 , Issue.6 , pp. 1055-1065
    • Pingel, J.T.1    Thomas, M.L.2
  • 19
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • Koretzky GA, Picus J, Thomas ML, Weiss A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature. 1990;346(6279):66-68.
    • (1990) Nature , vol.346 , Issue.6279 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 22
    • 0033558102 scopus 로고    scopus 로고
    • Cutting edge: The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro U, Ashwell JD. Cutting edge: the CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes. J Immunol. 1999;162(4):1879-1883. (Pubitemid 29288800)
    • (1999) Journal of Immunology , vol.162 , Issue.4 , pp. 1879-1883
    • D'Oro, U.1    Ashwell, J.D.2
  • 23
    • 77949962019 scopus 로고    scopus 로고
    • CD45-Csk phosphatase-kinase titration uncouples basal and inducible T cell receptor signaling during thymic development
    • Zikherman J, et al. CD45-Csk phosphatase-kinase titration uncouples basal and inducible T cell receptor signaling during thymic development. Immunity. 2010;32(3):342-354.
    • (2010) Immunity , vol.32 , Issue.3 , pp. 342-354
    • Zikherman, J.1
  • 24
    • 0037338890 scopus 로고    scopus 로고
    • TCR ligand discrimination is enforced by competing ERK positive and SHP-I negative feedback pathways
    • DOI 10.1038/ni895
    • Stefanova I, Hemmer B, Vergelli M, Martin R, Biddison WE, Germain RN. TCR ligand discrimination is enforced by competing ERK positive and SHP-1 negative feedback pathways. Nat Immunol. 2003;4(3):248-254. (Pubitemid 36322134)
    • (2003) Nature Immunology , vol.4 , Issue.3 , pp. 248-254
    • Stefanova, I.1    Hemmer, B.2    Vergelli, M.3    Martin, R.4    Biddison, W.E.5    Germain, R.N.6
  • 25
    • 0035933771 scopus 로고    scopus 로고
    • Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase
    • Chiang GG, Sefton BM. Specific dephosphorylation of the Lck tyrosine protein kinase at Tyr-394 by the SHP-1 protein-tyrosine phosphatase. J Biol Chem. 2001;276(25):23173-23178.
    • (2001) J Biol Chem , vol.276 , Issue.25 , pp. 23173-23178
    • Chiang, G.G.1    Sefton, B.M.2
  • 27
    • 0034948374 scopus 로고    scopus 로고
    • Involvement of SHP-1 tyrosine phosphatase in TCR-Mediated signaling pathways in lipid rafts
    • DOI 10.1016/S1074-7613(01)00146-7
    • Kosugi A, Sakakura J, Yasuda K, Ogata M, Hamaoka T. Involvement of SHP-1 tyrosine phosphatase in TCR-mediated signaling pathways in lipid rafts. Immunity. 2001;14(6):669-680. (Pubitemid 32592415)
    • (2001) Immunity , vol.14 , Issue.6 , pp. 669-680
    • Kosugi, A.1    Sakakura, J.2    Yasuda, K.3    Ogata, M.4    Hamaoka, T.5
  • 28
    • 0242712698 scopus 로고    scopus 로고
    • Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP
    • Gjorloff-Wingren A, Saxena M, Williams S, Hammi D, Mustelin T. Characterization of TCR-induced receptor-proximal signaling events negatively regulated by the protein tyrosine phosphatase PEP. Eur J Immunol. 1999;29(12):3845-3854.
    • (1999) Eur J Immunol , vol.29 , Issue.12 , pp. 3845-3854
    • Gjorloff-Wingren, A.1    Saxena, M.2    Williams, S.3    Hammi, D.4    Mustelin, T.5
  • 29
    • 0942279640 scopus 로고    scopus 로고
    • PEST Domain-Enriched Tyrosine Phosphatase (PEP) Regulation of Effector/Memory T Cells
    • DOI 10.1126/science.1092138
    • Hasegawa K, Martin F, Huang G, Tumas D, Diehl L, Chan AC. PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells. Science. 2004;303(5658):685-689. (Pubitemid 38141637)
    • (2004) Science , vol.303 , Issue.5658 , pp. 685-689
    • Hasegawa, K.1    Martin, F.2    Huang, G.3    Tumas, D.4    Diehl, L.5    Chan, A.C.6
  • 32
    • 33745169029 scopus 로고    scopus 로고
    • Role of PTPN22 in type 1 diabetes and other autoimmune diseases
    • DOI 10.1016/j.smim.2006.03.008, PII S1044532306000455
    • Bottini N, Vang T, Cucca F, Mustelin T. Role of PTPN22 in type 1 diabetes and other autoimmune diseases. Semin Immunol. 2006;18(4):207-213. (Pubitemid 43903283)
    • (2006) Seminars in Immunology , vol.18 , Issue.4 , pp. 207-213
    • Bottini, N.1    Vang, T.2    Cucca, F.3    Mustelin, T.4
  • 34
    • 58149091678 scopus 로고    scopus 로고
    • Shared and distinct genetic variants in type 1 diabetes and celiac disease
    • Smyth DJ, et al. Shared and distinct genetic variants in type 1 diabetes and celiac disease. N Engl J Med. 2008;359(26):2767-2777.
    • (2008) N Engl J Med , vol.359 , Issue.26 , pp. 2767-2777
    • Smyth, D.J.1
  • 35
    • 84969213492 scopus 로고    scopus 로고
    • Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls
    • WTCCC
    • WTCCC. Genome-wide association study of 14,000 cases of seven common diseases and 3,000 shared controls. Nature. 2007;447(7145):661-678.
    • (2007) Nature , vol.447 , Issue.7145 , pp. 661-678
  • 36
    • 79952280031 scopus 로고    scopus 로고
    • An autoimmune-associated variant in PTPN2 reveals an impairment of IL-2R signaling in CD4(+) T cells
    • Long SA, et al. An autoimmune-associated variant in PTPN2 reveals an impairment of IL-2R signaling in CD4(+) T cells. Genes Immun. 2011;12(2):116-125.
    • (2011) Genes Immun , vol.12 , Issue.2 , pp. 116-125
    • Long, S.A.1
  • 37
    • 77952887619 scopus 로고    scopus 로고
    • Deletion of the protein tyrosine phosphatase gene PTPN2 in T-cell acute lymphoblastic leukemia
    • Kleppe M, et al. Deletion of the protein tyrosine phosphatase gene PTPN2 in T-cell acute lymphoblastic leukemia. Nat Genet. 2010;42(6):530-535.
    • (2010) Nat Genet , vol.42 , Issue.6 , pp. 530-535
    • Kleppe, M.1
  • 40
    • 0029556979 scopus 로고
    • T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl- transferase gene by site-directed recombination
    • Hennet T, Hagen FK, Tabak LA, Marth JD. T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl- transferase gene by site-directed recombination. Proc Natl Acad Sci U S A. 1995;92(26):12070-12074.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.26 , pp. 12070-12074
    • Hennet, T.1    Hagen, F.K.2    Tabak, L.A.3    Marth, J.D.4
  • 41
    • 0028059099 scopus 로고
    • Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting
    • Gu H, Marth JD, Orban PC, Mossmann H, Rajewsky K. Deletion of a DNA polymerase beta gene segment in T cells using cell type-specific gene targeting. Science. 1994;265(5168):103-106.
    • (1994) Science , vol.265 , Issue.5168 , pp. 103-106
    • Gu, H.1    Marth, J.D.2    Orban, P.C.3    Mossmann, H.4    Rajewsky, K.5
  • 42
    • 38749094821 scopus 로고    scopus 로고
    • Development of all CD4 T lineages requires nuclear factor TOX
    • DOI 10.1084/jem.20071944
    • Aliahmad P, Kaye J. Development of all CD4 T lineages requires nuclear factor TOX. J Exp Med. 2008;205(1):245-256. (Pubitemid 351185730)
    • (2008) Journal of Experimental Medicine , vol.205 , Issue.1 , pp. 245-256
    • Aliahmad, P.1    Kaye, J.2
  • 43
    • 0028178784 scopus 로고
    • T cell receptor antagonist peptides induce positive selection
    • DOI 10.1016/0092-8674(94)90169-4
    • Hogquist KA, Jameson SC, Heath WR, Howard JL, Bevan MJ, Carbone FR. T cell receptor antagonist peptides induce positive selection. Cell. 1994;76(1):17-27. (Pubitemid 24035278)
    • (1994) Cell , vol.76 , Issue.1 , pp. 17-27
    • Hogquist, K.A.1    Jameson, S.C.2    Heath, W.R.3    Howard, J.L.4    Bevan, M.J.5    Carbone, F.R.6
  • 44
    • 0031897801 scopus 로고    scopus 로고
    • Defective TCR expression in transgenic mice constructed using cDNA- based alpha- and beta-chain genes under the control of heterologous regulatory elements
    • DOI 10.1046/j.1440-1711.1998.00709.x
    • Barnden MJ, Allison J, Heath WR, Carbone FR. Defective TCR expression in transgenic mice constructed using cDNA-based alpha- and beta-chain genes under the control of heterologous regulatory elements. Immunol Cell Biol. 1998;76(1):34-40. (Pubitemid 28194695)
    • (1998) Immunology and Cell Biology , vol.76 , Issue.1 , pp. 34-40
    • Barnden, M.J.1    Allison, J.2    Heath, W.R.3    Carbone, F.R.4
  • 45
    • 0025022278 scopus 로고
    • Requirement for cotolerogenic gene products in the clonal deletion of I-E reactive T cells
    • Woodland D, Happ MP, Bill J, Palmer E. Requirement for cotolerogenic gene products in the clonal deletion of I-E reactive T cells. Science. 1990;247(4945):964-967.
    • (1990) Science , vol.247 , Issue.4945 , pp. 964-967
    • Woodland, D.1    Happ, M.P.2    Bill, J.3    Palmer, E.4
  • 46
    • 0026453632 scopus 로고
    • Both intrathymic and peripheral selection modulate the differential expression of V beta 5 among CD4+ and CD8+ T cells
    • Fink PJ, Swan K, Turk G, Moore MW, Carbone FR. Both intrathymic and peripheral selection modulate the differential expression of V beta 5 among CD4+ and CD8+ T cells. J Exp Med. 1992; 176(6):1733-1738.
    • (1992) J Exp Med , vol.176 , Issue.6 , pp. 1733-1738
    • Fink, P.J.1    Swan, K.2    Turk, G.3    Moore, M.W.4    Carbone, F.R.5
  • 47
    • 0028807837 scopus 로고
    • A role for the orphan steroid receptor Nur77 in apoptosis accompanying antigen-induced negative selection
    • Calnan BJ, Szychowski S, Chan FK, Cado D, Winoto A. A role for the orphan steroid receptor Nur77 in apoptosis accompanying antigen-induced negative selection. Immunity. 1995;3(3):273-282.
    • (1995) Immunity , vol.3 , Issue.3 , pp. 273-282
    • Calnan, B.J.1    Szychowski, S.2    Chan, F.K.3    Cado, D.4    Winoto, A.5
  • 48
    • 14944349510 scopus 로고    scopus 로고
    • Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase
    • van Vliet C, et al. Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase. Nat Immunol. 2005;6(3):253-260.
    • (2005) Nat Immunol , vol.6 , Issue.3 , pp. 253-260
    • Van Vliet, C.1
  • 49
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint AJ, Tiganis T, Barford D, Tonks NK. Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc Natl Acad Sci U S A. 1997;94(5):1680-1685.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.5 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 50
    • 0031935043 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and the adaptor protein p52(Shc) are specific substrates of T-cell protein tyrosine phosphatase
    • Tiganis T, Bennett AM, Ravichandran KS, Tonks NK. Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase. Mol Cell Biol. 1998;18(3):1622-1634. (Pubitemid 28100928)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.3 , pp. 1622-1634
    • Tiganis, T.1    Bennett, A.M.2    Ravichandran, K.S.3    Tonks, N.K.4
  • 51
    • 33846945811 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase function: The substrate perspective
    • Tiganis T, Bennett AM. Protein tyrosine phosphatase function: the substrate perspective. Biochem J. 2007;402(1):1-15.
    • (2007) Biochem J , vol.402 , Issue.1 , pp. 1-15
    • Tiganis, T.1    Bennett, A.M.2
  • 52
    • 61849166005 scopus 로고    scopus 로고
    • The structure, regulation, and function of ZAP-70
    • Au-Yeung BB, et al. The structure, regulation, and function of ZAP-70. Immunol Rev. 2009;228(1):41-57.
    • (2009) Immunol Rev , vol.228 , Issue.1 , pp. 41-57
    • Au-Yeung, B.B.1
  • 54
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus DB, Weiss A. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell. 1992;70(4):585-593.
    • (1992) Cell , vol.70 , Issue.4 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 56
    • 0028108177 scopus 로고
    • Peptide antagonists that promote positive selection are inefficient at T cell activation and thymocyte deletion
    • DOI 10.1002/eji.1830241029
    • Barnden MJ, Heath WR, Rodda S, Carbone FR. Peptide antagonists that promote positive selection are inefficient at T cell activation and thymocyte deletion. Eur J Immunol. 1994;24(10):2452-2456. (Pubitemid 24303092)
    • (1994) European Journal of Immunology , vol.24 , Issue.10 , pp. 2452-2456
    • Barnden, M.J.1    Heath, W.R.2    Rodda, S.3    Carbone, F.R.4
  • 58
    • 34848812557 scopus 로고    scopus 로고
    • TCR affinity promotes CD8+ T cell expansion by regulating survival
    • Hommel M, Hodgkin PD. TCR affinity promotes CD8+ T cell expansion by regulating survival. J Immunol. 2007;179(4):2250-2260.
    • (2007) J Immunol , vol.179 , Issue.4 , pp. 2250-2260
    • Hommel, M.1    Hodgkin, P.D.2
  • 59
    • 75149178563 scopus 로고    scopus 로고
    • The role of chemokines in the recruitment of lymphocytes to the liver
    • Oo YH, Adams DH. The role of chemokines in the recruitment of lymphocytes to the liver. J Autoimmun. 2010;34(1):45-54.
    • (2010) J Autoimmun , vol.34 , Issue.1 , pp. 45-54
    • Oo, Y.H.1    Adams, D.H.2
  • 61
    • 0033431029 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP-1 influences thymocyte selection by setting TCR signaling thresholds
    • Carter JD, Neel BG, Lorenz U. The tyrosine phosphatase SHP-1 influences thymocyte selection by setting TCR signaling thresholds. Int Immunol. 1999;11(12):1999-2014.
    • (1999) Int Immunol , vol.11 , Issue.12 , pp. 1999-2014
    • Carter, J.D.1    Neel, B.G.2    Lorenz, U.3
  • 63
    • 0036138705 scopus 로고    scopus 로고
    • A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: Dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus
    • DOI 10.1210/me.16.1.58
    • Aoki N, Matsuda T. A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus. Mol Endocrinol. 2002; 16(1):58-69. (Pubitemid 34044498)
    • (2002) Molecular Endocrinology , vol.16 , Issue.1 , pp. 58-69
    • Aoki, N.1    Matsuda, T.2
  • 64
    • 0036006288 scopus 로고    scopus 로고
    • The T cell protein tyrosine phosphatase is a negative regulator of Janus family kinases 1 and 3
    • DOI 10.1016/S0960-9822(02)00697-8, PII S0960982202006978
    • Simoncic PD, Lee-Loy A, Barber DL, Tremblay ML, McGlade CJ. The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3. Curr Biol. 2002;12(6):446-453. (Pubitemid 34248890)
    • (2002) Current Biology , vol.12 , Issue.6 , pp. 446-453
    • Simoncic, P.D.1    Lee-Loy, A.2    Barber, D.L.3    Tremblay, M.L.4    McGlade, C.J.5
  • 65
    • 0033625496 scopus 로고    scopus 로고
    • Inducible expression of a p56Lck transgene reveals a central role for Lck in the differentiation of CD4 SP thymocytes
    • Legname G, et al. Inducible expression of a p56Lck transgene reveals a central role for Lck in the differentiation of CD4 SP thymocytes. Immunity. 2000;12(5):537-546.
    • (2000) Immunity , vol.12 , Issue.5 , pp. 537-546
    • Legname, G.1
  • 67
    • 57449097558 scopus 로고    scopus 로고
    • Homeostasis of naive and memory T cells
    • Surh CD, Sprent J. Homeostasis of naive and memory T cells. Immunity. 2008;29(6):848-862.
    • (2008) Immunity , vol.29 , Issue.6 , pp. 848-862
    • Surh, C.D.1    Sprent, J.2
  • 68
    • 0037460071 scopus 로고    scopus 로고
    • Involvement of avidity for major histocompatibility complex in homeostasis of naive and memory T cells
    • DOI 10.1084/jem.20021812
    • Kassiotis G, Zamoyska R, Stockinger B. Involvement of avidity for major histocompatibility complex in homeostasis of naive and memory T cells. J Exp Med. 2003;197(8):1007-1016. (Pubitemid 36523198)
    • (2003) Journal of Experimental Medicine , vol.197 , Issue.8 , pp. 1007-1016
    • Kassiotis, G.1    Zamoyska, R.2    Stockinger, B.3
  • 69
    • 0346103729 scopus 로고    scopus 로고
    • A Role for TCR Affinity in Regulating Naive T Cell Homeostasis
    • Kieper WC, Burghardt JT, Surh CD. A role for TCR affinity in regulating naive T cell homeostasis. J Immunol. 2004;172(1):40-44. (Pubitemid 38020453)
    • (2004) Journal of Immunology , vol.172 , Issue.1 , pp. 40-44
    • Kieper, W.C.1    Burghardt, J.T.2    Surh, C.D.3
  • 70
    • 68949166331 scopus 로고    scopus 로고
    • Lymphocyte proliferation in immune-mediated diseases
    • Datta S, Sarvetnick N. Lymphocyte proliferation in immune-mediated diseases. Trends Immunol. 2009;30(9):430-438.
    • (2009) Trends Immunol , vol.30 , Issue.9 , pp. 430-438
    • Datta, S.1    Sarvetnick, N.2
  • 71
    • 33947221062 scopus 로고    scopus 로고
    • T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6
    • DOI 10.1128/MCB.01234-06
    • Lu X, et al. T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6. Mol Cell Biol. 2007;27(6):2166-2179. (Pubitemid 46418473)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.6 , pp. 2166-2179
    • Lu, X.1    Chen, J.2    Sasmono, R.T.3    Hsi, E.D.4    Sarosiek, K.A.5    Tiganis, T.6    Lossos, I.S.7
  • 72
    • 78649869141 scopus 로고    scopus 로고
    • SHP-1 in T cells limits the production of CD8 effector cells without impacting the formation of long-lived central memory cells
    • Fowler CC, Pao LI, Blattman JN, Greenberg PD. SHP-1 in T cells limits the production of CD8 effector cells without impacting the formation of long-lived central memory cells. J Immunol. 2010;185(6):3256-3267.
    • (2010) J Immunol , vol.185 , Issue.6 , pp. 3256-3267
    • Fowler, C.C.1    Pao, L.I.2    Blattman, J.N.3    Greenberg, P.D.4
  • 73
    • 0037105615 scopus 로고    scopus 로고
    • TCR signals mediated by Src family kinases are essential for the survival of naive T cells
    • Seddon B, Zamoyska R. TCR signals mediated by Src family kinases are essential for the survival of naive T cells. J Immunol. 2002;169(6):2997-3005. (Pubitemid 35013142)
    • (2002) Journal of Immunology , vol.169 , Issue.6 , pp. 2997-3005
    • Seddon, B.1    Zamoyska, R.2
  • 74
    • 49249128709 scopus 로고    scopus 로고
    • Fyn regulates the duration of TCR engagement needed for commitment to effector function
    • Filby A, et al. Fyn regulates the duration of TCR engagement needed for commitment to effector function. J Immunol. 2007;179(7):4635-4644.
    • (2007) J Immunol , vol.179 , Issue.7 , pp. 4635-4644
    • Filby, A.1
  • 75
    • 80455122701 scopus 로고    scopus 로고
    • Elevated hypothalamic TCPTP in obesity contributes to cellular leptin resistance
    • Loh K, et al. Elevated hypothalamic TCPTP in obesity contributes to cellular leptin resistance. Cell Metab. 2011;14(5):684-699.
    • (2011) Cell Metab , vol.14 , Issue.5 , pp. 684-699
    • Loh, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.