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Volumn 2, Issue 3, 2003, Pages

Systematic identification of regulatory proteins critical for T-cell activation

Author keywords

[No Author keywords available]

Indexed keywords

A RAF 1 PROTEIN KINASE; ADAPTOR PROTEIN; ALPHA2 INTEGRIN; CD69 ANTIGEN; CELL MEMBRANE PROTEIN; CELL PROTEIN; COMPLEMENTARY DNA; CYTOPLASM PROTEIN; EDG1 PROTEIN; G PROTEIN COUPLED RECEPTOR; INTEGRIN; INTERLEUKIN 10 RECEPTOR; INTERLEUKIN 10 RECEPTOR ALPHA; LIGASE; MUTANT PROTEIN; NUCLEAR PROTEIN; P21 ACTIVATED KINASE 2; PHOSPHOLIPASE C GAMMA1; PROTEIN KINASE; PROTEIN KINASE LCK; PROTEIN KINASE SYK; PROTEIN KINASE ZAP 70; PROTEIN P21; PROTEIN SERINE THREONINE KINASE; PROTEIN TYROSINE PHOSPHATASE SHP 1; REGULATOR PROTEIN; T LYMPHOCYTE RECEPTOR; TRAC 1 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; UNINDEXED DRUG; LECTIN; LEUKOCYTE ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN; T LYMPHOCYTE ANTIGEN;

EID: 0242624487     PISSN: 14785854     EISSN: 14754924     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (59)

References (86)
  • 1
    • 0023475192 scopus 로고
    • The T cell receptor
    • Marrack P, Kappler J: The T cell receptor. Science 1987, 238:1073-1079.
    • (1987) Science , vol.238 , pp. 1073-1079
    • Marrack, P.1    Kappler, J.2
  • 2
    • 0021678703 scopus 로고
    • Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line
    • Weiss A, Stobo JD: Requirement for the coexpression of T3 and the T cell antigen receptor on a malignant human T cell line. J Exp Med 1984, 160:1284-1299.
    • (1984) J Exp Med , vol.160 , pp. 1284-1299
    • Weiss, A.1    Stobo, J.D.2
  • 3
    • 0034644505 scopus 로고    scopus 로고
    • Signaling takes shape in the immune system
    • Dustin ML, Chan AC: Signaling takes shape in the immune system. Cell 2000, 103:283-294.
    • (2000) Cell , vol.103 , pp. 283-294
    • Dustin, M.L.1    Chan, A.C.2
  • 4
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • Kane LP, Lin J, Weiss A: Signal transduction by the TCR for antigen. Curr Opin Immunol 2000, 12:242-249.
    • (2000) Curr Opin Immunol , vol.12 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 5
    • 0037204932 scopus 로고    scopus 로고
    • Control of T cell function by positive and negative regulators
    • Singer AL, Koretzky GA: Control of T cell function by positive and negative regulators. Science 2002, 296:1639-1640.
    • (2002) Science , vol.296 , pp. 1639-1640
    • Singer, A.L.1    Koretzky, G.A.2
  • 7
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell
    • Yablonski D, Kuhne MR, Kadlecek T, Weiss A: Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell. Science 1998, 281:413-416.
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 8
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
    • Zhang W, Irvin BJ, Trible RP, Abraham RT, Samelson LE: Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line. Int Immunol 1999, 11:943-950.
    • (1999) Int Immunol , vol.11 , pp. 943-950
    • Zhang, W.1    Irvin, B.J.2    Trible, R.P.3    Abraham, R.T.4    Samelson, L.E.5
  • 9
    • 0030797223 scopus 로고    scopus 로고
    • Tetracycline-controlled transcription in eukaryotes: Novel transactivators with graded transactivation potential
    • Baron U, Gossen M, Bujard H: Tetracycline-controlled transcription in eukaryotes: novel transactivators with graded transactivation potential. Nucleic Acids Res 1997, 25:2723-2729.
    • (1997) Nucleic Acids Res , vol.25 , pp. 2723-2729
    • Baron, U.1    Gossen, M.2    Bujard, H.3
  • 10
    • 0030046923 scopus 로고    scopus 로고
    • Dominant-negative zeta-associated protein 70 inhibits T cell antigen receptor signaling
    • Qian D, Mollenauer MN, Weiss A: Dominant-negative zeta-associated protein 70 inhibits T cell antigen receptor signaling. J Exp Med 1996, 183:611-620.
    • (1996) J Exp Med , vol.183 , pp. 611-620
    • Qian, D.1    Mollenauer, M.N.2    Weiss, A.3
  • 11
    • 0035124549 scopus 로고    scopus 로고
    • T cell receptor signalling
    • Lin J, Weiss A: T cell receptor signalling. J Cell Sci 2001, 114:243-244.
    • (2001) J Cell Sci , vol.114 , pp. 243-244
    • Lin, J.1    Weiss, A.2
  • 12
    • 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, 70:585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 13
    • 0025835006 scopus 로고
    • T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1
    • Secrist JP, Karnitz L, Abraham RT: T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1. J Biol Chem 1991, 266:12135-12139.
    • (1991) J Biol Chem , vol.266 , pp. 12135-12139
    • Secrist, J.P.1    Karnitz, L.2    Abraham, R.T.3
  • 14
    • 0034461022 scopus 로고    scopus 로고
    • Pleiotropic contributions of phospholipase C-gamma1 (PLC-gamma1) to T-cell antigen receptor-mediated signaling: Reconstitution studies of a PLC-gamma1-deficient Jurkat T-cell line
    • Irvin BJ, Williams BL, Nilson AE, Maynor HO, Abraham RT: Pleiotropic contributions of phospholipase C-gamma1 (PLC-gamma1) to T-cell antigen receptor-mediated signaling: reconstitution studies of a PLC-gamma1-deficient Jurkat T-cell line. Mol Cell Biol 2000, 20:9149-9161.
    • (2000) Mol Cell Biol , vol.20 , pp. 9149-9161
    • Irvin, B.J.1    Williams, B.L.2    Nilson, A.E.3    Maynor, H.O.4    Abraham, R.T.5
  • 15
    • 0025311299 scopus 로고
    • An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors
    • Hla T, Maciag T: An abundant transcript induced in differentiating human endothelial cells encodes a polypeptide with structural similarities to G-protein-coupled receptors. J Biol Chem 1990, 265:9308-9313.
    • (1990) J Biol Chem , vol.265 , pp. 9308-9313
    • Hla, T.1    Maciag, T.2
  • 18
    • 0029805324 scopus 로고    scopus 로고
    • Regulation of phosphorylation pathways by p21 GTPases. The p21 Ras-related Rho subfamily and its role in phosphorylation signalling pathways
    • Lim L, Manser E, Leung T, Hall C: Regulation of phosphorylation pathways by p21 GTPases. The p21 Ras-related Rho subfamily and its role in phosphorylation signalling pathways. Eur J Biochem 1996, 242:171-185.
    • (1996) Eur J Biochem , vol.242 , pp. 171-185
    • Lim, L.1    Manser, E.2    Leung, T.3    Hall, C.4
  • 19
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch GM: Biology of the p21-activated kinases. Annu Rev Biochem 2003, 72:743-781.
    • (2003) Annu Rev Biochem , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 20
    • 0029056399 scopus 로고
    • A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20
    • Martin GA, Bollag G, McCormick F, Abo A: A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J 1995, 14:1970-1978.
    • (1995) EMBO J , vol.14 , pp. 1970-1978
    • Martin, G.A.1    Bollag, G.2    McCormick, F.3    Abo, A.4
  • 21
    • 0028842508 scopus 로고
    • Identification and molecular cloning of a p21 cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets
    • Teo M, Manser E, Lim L: Identification and molecular cloning of a p21 cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets. J Biol Chem 1995, 270:26690-26697.
    • (1995) J Biol Chem , vol.270 , pp. 26690-26697
    • Teo, M.1    Manser, E.2    Lim, L.3
  • 22
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel T, Bokoch GM: Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 1997, 276:1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 23
    • 0031907887 scopus 로고    scopus 로고
    • p21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells
    • Rudel T, Zenke FT, Chuang TH, Bokoch GM: p21-activated kinase (PAK) is required for Fas-induced JNK activation in Jurkat cells. J Immunol 1998, 160:7-11.
    • (1998) J Immunol , vol.160 , pp. 7-11
    • Rudel, T.1    Zenke, F.T.2    Chuang, T.H.3    Bokoch, G.M.4
  • 25
    • 0032188987 scopus 로고    scopus 로고
    • A Nck-Pak1 signaling module is required for T-cell receptor-mediated activation of NFAT, but not of JNK
    • Yablonski D, Kane LP, Qian D, Weiss A: A Nck-Pak1 signaling module is required for T-cell receptor-mediated activation of NFAT, but not of JNK. EMBO J 1998, 17:5647-5657.
    • (1998) EMBO J , vol.17 , pp. 5647-5657
    • Yablonski, D.1    Kane, L.P.2    Qian, D.3    Weiss, A.4
  • 27
    • 0035473462 scopus 로고    scopus 로고
    • The Grb7 family proteins: Structure, interactions with other signaling molecules and potential cellular functions
    • Han DC, Shen TL, Guan JL: The Grb7 family proteins: structure, interactions with other signaling molecules and potential cellular functions. Oncogene 2001, 20:6315-6321.
    • (2001) Oncogene , vol.20 , pp. 6315-6321
    • Han, D.C.1    Shen, T.L.2    Guan, J.L.3
  • 28
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM: RING finger proteins: mediators of ubiquitin ligase activity. Cell 2000, 102:549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 29
    • 0036144763 scopus 로고    scopus 로고
    • Regulatory functions of ubiquitination in the immune system
    • Ben-Neriah Y: Regulatory functions of ubiquitination in the immune system. Nat Immunol 2002, 3:20-26.
    • (2002) Nat Immunol , vol.3 , pp. 20-26
    • Ben-Neriah, Y.1
  • 32
    • 0036311889 scopus 로고    scopus 로고
    • Sphingosine 1 phosphate induces the chemotaxis of human natural killer cells. Role for heterotrimeric G proteins and phosphoinositide 3 kinases
    • Kveberg L, Bryceson Y, Inngjerdingen M, Rolstad B, Maghazachi AA: Sphingosine 1 phosphate induces the chemotaxis of human natural killer cells. Role for heterotrimeric G proteins and phosphoinositide 3 kinases. Eur J Immunol 2002, 32:1856-1864.
    • (2002) Eur J Immunol , vol.32 , pp. 1856-1864
    • Kveberg, L.1    Bryceson, Y.2    Inngjerdingen, M.3    Rolstad, B.4    Maghazachi, A.A.5
  • 33
  • 34
    • 0030614746 scopus 로고    scopus 로고
    • Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains
    • Frantz JD, Giorgetti-Peraldi S, Ottinger EA, Shoelson SE: Human GRB-IRbeta/GRB10. Splice variants of an insulin and growth factor receptor-binding protein with PH and SH2 domains. J Biol Chem 1997, 272:2659-2667.
    • (1997) J Biol Chem , vol.272 , pp. 2659-2667
    • Frantz, J.D.1    Giorgetti-Peraldi, S.2    Ottinger, E.A.3    Shoelson, S.E.4
  • 37
    • 0028287296 scopus 로고
    • The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor
    • Izquierdo M, Bowden S, Cantrell D: The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor. J Exp Med 1994, 180:401-406.
    • (1994) J Exp Med , vol.180 , pp. 401-406
    • Izquierdo, M.1    Bowden, S.2    Cantrell, D.3
  • 38
    • 0027376035 scopus 로고
    • Rapid activation of C-Raf-1 after stimulation of the T-cell receptor or the muscarinic receptor type 1 in resting T cells
    • Siegel JN, June CH, Yamada H, Rapp UR, Samelson LE: Rapid activation of C-Raf-1 after stimulation of the T-cell receptor or the muscarinic receptor type 1 in resting T cells. J Immunol 1993, 151:4116-4127.
    • (1993) J Immunol , vol.151 , pp. 4116-4127
    • Siegel, J.N.1    June, C.H.2    Yamada, H.3    Rapp, U.R.4    Samelson, L.E.5
  • 39
    • 0028227284 scopus 로고
    • SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: The guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases
    • Reif K, Buday L, Downward J, Cantrell DA: SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases. J Biol Chem 1994, 269:14081-14087.
    • (1994) J Biol Chem , vol.269 , pp. 14081-14087
    • Reif, K.1    Buday, L.2    Downward, J.3    Cantrell, D.A.4
  • 40
    • 0028245832 scopus 로고
    • A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells
    • Buday L, Egan SE, Rodriguez Viciana P, Cantrell DA, Downward J: A complex of Grb2 adaptor protein, Sos exchange factor, and a 36-kDa membrane-bound tyrosine phosphoprotein is implicated in ras activation in T cells. J Biol Chem 1994, 269:9019-9023.
    • (1994) J Biol Chem , vol.269 , pp. 9019-9023
    • Buday, L.1    Egan, S.E.2    Rodriguez Viciana, P.3    Cantrell, D.A.4    Downward, J.5
  • 41
    • 0032750417 scopus 로고    scopus 로고
    • Activation of the PAK-related kinase by human immunodeficiency virus type 1 Nef in primary human peripheral blood lymphocytes and macrophages leads to phosphorylation of a PIX-p95 complex
    • Brown A, Wang X, Sawai E, Cheng-Mayer C: Activation of the PAK-related kinase by human immunodeficiency virus type 1 Nef in primary human peripheral blood lymphocytes and macrophages leads to phosphorylation of a PIX-p95 complex. J Virol 1999, 73:9899-9907.
    • (1999) J Virol , vol.73 , pp. 9899-9907
    • Brown, A.1    Wang, X.2    Sawai, E.3    Cheng-Mayer, C.4
  • 42
    • 0033518291 scopus 로고    scopus 로고
    • Identification of the Nef-associated kinase as p21-activated kinase 2
    • Renkema GH, Manninen A, Mann DA, Harris M, Saksela K: Identification of the Nef-associated kinase as p21-activated kinase 2. Curr Biol 1999, 9:1407-1410.
    • (1999) Curr Biol , vol.9 , pp. 1407-1410
    • Renkema, G.H.1    Manninen, A.2    Mann, D.A.3    Harris, M.4    Saksela, K.5
  • 44
    • 0035711333 scopus 로고    scopus 로고
    • The use of retroviruses as pharmaceutical tools for target discovery and validation in the field of functional genomics
    • Lorens JB, Sousa C, Bennett MK, Molineaux SM, Payan DG: The use of retroviruses as pharmaceutical tools for target discovery and validation in the field of functional genomics. Curr Opin Biotechnol 2001, 12:613-621.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 613-621
    • Lorens, J.B.1    Sousa, C.2    Bennett, M.K.3    Molineaux, S.M.4    Payan, D.G.5
  • 49
    • 0003059314 scopus 로고    scopus 로고
    • Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems
    • 10.17C. Edited by Coligan RCJE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W. Hoboken, NJ: John Wiley and Sons
    • Swift SE, Lorens JB, Achacoso P, Nolan GP: Rapid production of retroviruses for efficient gene delivery to mammalian cells using 293T cell-based systems. In Current Protocols in Immunology, vol 10.17C. Edited by Coligan RCJE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W. Hoboken, NJ: John Wiley and Sons; 2000:1-17.
    • (2000) Current Protocols in Immunology , pp. 1-17
    • Swift, S.E.1    Lorens, J.B.2    Achacoso, P.3    Nolan, G.P.4
  • 51
    • 0242523599 scopus 로고    scopus 로고
    • GenBank [http://www.ncbi.nlm.nih.gov/Genbank/]
  • 52
    • 0033638003 scopus 로고    scopus 로고
    • On the dynamics of TCR:CD3 complex cell surface expression and down-modulation
    • Liu H, Rhodes M, Wiest DL, Vignali DA: On the dynamics of TCR:CD3 complex cell surface expression and down-modulation. Immunity 2000, 13:665-675.
    • (2000) Immunity , vol.13 , pp. 665-675
    • Liu, H.1    Rhodes, M.2    Wiest, D.L.3    Vignali, D.A.4
  • 54
    • 0031912097 scopus 로고    scopus 로고
    • Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: Reconstitution studies in a ZAP-70-deficient Jurkat T-cell line
    • Williams BL, Schreiber KL, Zhang W, Wange RL, Samelson LE, Leibson PJ, Abraham RT: Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: reconstitution studies in a ZAP-70-deficient Jurkat T-cell line. Mol Cell Biol 1998, 18:1388-1399.
    • (1998) Mol Cell Biol , vol.18 , pp. 1388-1399
    • Williams, B.L.1    Schreiber, K.L.2    Zhang, W.3    Wange, R.L.4    Samelson, L.E.5    Leibson, P.J.6    Abraham, R.T.7
  • 56
    • 0030764557 scopus 로고    scopus 로고
    • Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency
    • Shultz LD, Rajan TV, Greiner DL: Severe defects in immunity and hematopoiesis caused by SHP-1 protein-tyrosine-phosphatase deficiency. Trends Biotechnol 1997, 15:302-307.
    • (1997) Trends Biotechnol , vol.15 , pp. 302-307
    • Shultz, L.D.1    Rajan, T.V.2    Greiner, D.L.3
  • 57
    • 0034613151 scopus 로고    scopus 로고
    • Immune inhibitory receptors
    • Ravetch JV, Lanier LL: Immune inhibitory receptors. Science 2000, 290:84-89.
    • (2000) Science , vol.290 , pp. 84-89
    • Ravetch, J.V.1    Lanier, L.L.2
  • 58
    • 0034635505 scopus 로고    scopus 로고
    • Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1
    • Yang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW: Structural basis for substrate specificity of protein-tyrosine phosphatase SHP-1. J Biol Chem 2000, 275:4066-4071.
    • (2000) J Biol Chem , vol.275 , pp. 4066-4071
    • Yang, J.1    Cheng, Z.2    Niu, T.3    Liang, X.4    Zhao, Z.J.5    Zhou, G.W.6
  • 59
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, et al.: Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J Exp Med 2000, 191:1591-1604.
    • (2000) J Exp Med , vol.191 , pp. 1591-1604
    • Brdicka, T.1    Pavlistova, D.2    Leo, A.3    Bruyns, E.4    Korinek, V.5    Angelisova, P.6    Scherer, J.7    Shevchenko, A.8    Hilgert, I.9    Cerny, J.10
  • 61
    • 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
  • 62
    • 0035800835 scopus 로고    scopus 로고
    • Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts
    • Torgersen KM, Vang T, Abrahamsen H, Yaqub S, Horejsi V, Schraven B, Rolstad B, Mustelin T, Tasken K: Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src kinase (Csk) from lipid rafts. J Biol Chem 2001, 276:29313-29318.
    • (2001) J Biol Chem , vol.276 , pp. 29313-29318
    • Torgersen, K.M.1    Vang, T.2    Abrahamsen, H.3    Yaqub, S.4    Horejsi, V.5    Schraven, B.6    Rolstad, B.7    Mustelin, T.8    Tasken, K.9
  • 63
    • 0036143017 scopus 로고    scopus 로고
    • Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases
    • Hermiston ML, Xu Z, Majeti R, Weiss A: Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases. J Clin Invest 2002, 109:9-14.
    • (2002) J Clin Invest , vol.109 , pp. 9-14
    • Hermiston, M.L.1    Xu, Z.2    Majeti, R.3    Weiss, A.4
  • 64
    • 0037080345 scopus 로고    scopus 로고
    • Cutting edge: Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly
    • Itoh K, Sakakibara M, Yamasaki S, Takeuchi A, Arase H, Miyazaki M, Nakajima N, Okada M, Saito T: Cutting edge: negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly. J Immunol 2002, 168:541-544.
    • (2002) J Immunol , vol.168 , pp. 541-544
    • Itoh, K.1    Sakakibara, M.2    Yamasaki, S.3    Takeuchi, A.4    Arase, H.5    Miyazaki, M.6    Nakajima, N.7    Okada, M.8    Saito, T.9
  • 65
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: The regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • Kolch W: Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions. Biochem J 2000, 351:289-305.
    • (2000) Biochem J , vol.351 , pp. 289-305
    • Kolch, W.1
  • 66
    • 0028287296 scopus 로고
    • The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor
    • Izquierdo M, Bowden S, Cantrell D: The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor. J Exp Med 1994, 180:401-406.
    • (1994) J Exp Med , vol.180 , pp. 401-406
    • Izquierdo, M.1    Bowden, S.2    Cantrell, D.3
  • 67
    • 0028302767 scopus 로고
    • The T-cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase. Evidence for the existence of a second protein kinase C-dependent pathway in an Lck-negative Jurkat cell mutant
    • Gupta S, Weiss A, Kumar G, Wang S, Nel A: The T-cell antigen receptor utilizes Lck, Raf-1, and MEK-1 for activating mitogen-activated protein kinase. Evidence for the existence of a second protein kinase C-dependent pathway in an Lck-negative Jurkat cell mutant. J Biol Chem 1994, 269:17349-17357.
    • (1994) J Biol Chem , vol.269 , pp. 17349-17357
    • Gupta, S.1    Weiss, A.2    Kumar, G.3    Wang, S.4    Nel, A.5
  • 68
    • 0025979335 scopus 로고
    • Raf-1 protein kinase is required for growth of induced NIH/3T3 cells
    • Kolch W, Heidecker G, Lloyd P, Rapp UR: Raf-1 protein kinase is required for growth of induced NIH/3T3 cells. Nature 1991, 349:426-428.
    • (1991) Nature , vol.349 , pp. 426-428
    • Kolch, W.1    Heidecker, G.2    Lloyd, P.3    Rapp, U.R.4
  • 69
    • 0027237273 scopus 로고
    • A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21 ras
    • Schaap D, van der Wal J, Howe LR, Marshall CJ, van Blitterswijk WJ: A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21 ras. J Biol Chem 1993, 268:20232-20236.
    • (1993) J Biol Chem , vol.268 , pp. 20232-20236
    • Schaap, D.1    Van Der Wal, J.2    Howe, L.R.3    Marshall, C.J.4    Van Blitterswijk, W.J.5
  • 71
    • 0030703139 scopus 로고    scopus 로고
    • The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism
    • Hao L, Tiganis T, Tonks NK, Charbonneau H: The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism. J Biol Chem 1997, 272:29322-29329.
    • (1997) J Biol Chem , vol.272 , pp. 29322-29329
    • Hao, L.1    Tiganis, T.2    Tonks, N.K.3    Charbonneau, H.4
  • 72
    • 0028350053 scopus 로고
    • Expression cloning and characterization of a human IL-10 receptor
    • Liu Y, Wei SH, Ho AS, de Waal Malefyt R, Moore KW: Expression cloning and characterization of a human IL-10 receptor. J Immunol 1994, 152:1821-1829.
    • (1994) J Immunol , vol.152 , pp. 1821-1829
    • Liu, Y.1    Wei, S.H.2    Ho, A.S.3    De Waal Malefyt, R.4    Moore, K.W.5
  • 73
    • 0024382716 scopus 로고
    • The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GP1a): Homology to other integrins and the presence of a possible collagen-binding domain
    • Takada Y, Hemler ME: The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GP1a): homology to other integrins and the presence of a possible collagen-binding domain. J Cell Biol 1989, 109:397-407.
    • (1989) J Cell Biol , vol.109 , pp. 397-407
    • Takada, Y.1    Hemler, M.E.2
  • 74
    • 0030865394 scopus 로고    scopus 로고
    • Integrins and inside-out signal transduction: Converging signals from PKC and PIP3
    • Kolanus W, Seed B: Integrins and inside-out signal transduction: converging signals from PKC and PIP3. Curr Opin Cell Biol 1997, 9:725-731.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 725-731
    • Kolanus, W.1    Seed, B.2
  • 75
    • 0035937128 scopus 로고    scopus 로고
    • The molecular adapter SLP-76 relays signals from platelet integrin alpha11bbeta3 to the actin cytoskeleton
    • Obergfell A, Judd BA, del Pozo MA, Schwartz MA, Koretzky GA, Shattil SJ: The molecular adapter SLP-76 relays signals from platelet integrin alpha11bbeta3 to the actin cytoskeleton. J Biol Chem 2001, 276:5916-5923.
    • (2001) J Biol Chem , vol.276 , pp. 5916-5923
    • Obergfell, A.1    Judd, B.A.2    Del Pozo, M.A.3    Schwartz, M.A.4    Koretzky, G.A.5    Shattil, S.J.6
  • 77
    • 0026453395 scopus 로고
    • itk, a T-cell-specific tyrosine kinase gene inducible by interleukin 2
    • Siliciano JD, Morrow TA, Desiderio SV: itk, a T-cell-specific tyrosine kinase gene inducible by interleukin 2. Proc Natl Acad Sci USA 1992, 89:11194-11198.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11194-11198
    • Siliciano, J.D.1    Morrow, T.A.2    Desiderio, S.V.3
  • 78
    • 13344270890 scopus 로고
    • Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk
    • Liao XC, Littman DR: Altered T cell receptor signaling and disrupted T cell development in mice lacking Itk. Immunity 1995, 3:757-769.
    • (1995) Immunity , vol.3 , pp. 757-769
    • Liao, X.C.1    Littman, D.R.2
  • 79
    • 0035868761 scopus 로고    scopus 로고
    • A novel function for the Tec family tyrosine kinase Itk in activation of beta 1 integrins by the T-cell receptor
    • Woods ML, Kivens WJ, Adelsman MA, Qiu Y, August A, Shimizu Y: A novel function for the Tec family tyrosine kinase Itk in activation of beta 1 integrins by the T-cell receptor. EMBO J 2001, 20:1232-1244.
    • (2001) EMBO J , vol.20 , pp. 1232-1244
    • Woods, M.L.1    Kivens, W.J.2    Adelsman, M.A.3    Qiu, Y.4    August, A.5    Shimizu, Y.6
  • 80
    • 0033581478 scopus 로고    scopus 로고
    • Integrin alpha2beta1 mediates isoform-specific activation of p38 and upregulation of collagen gene transcription by a mechanism involving the alpha2 cytoplasmic tail
    • Ivaska J, Reunanen H, Westermarck J, Koivisto L, Kahari VM, Heino J: Integrin alpha2beta1 mediates isoform-specific activation of p38 and upregulation of collagen gene transcription by a mechanism involving the alpha2 cytoplasmic tail. J Cell Biol 1999, 147:401-416.
    • (1999) J Cell Biol , vol.147 , pp. 401-416
    • Ivaska, J.1    Reunanen, H.2    Westermarck, J.3    Koivisto, L.4    Kahari, V.M.5    Heino, J.6
  • 81
    • 0028802599 scopus 로고
    • The yeast tribrid system - genetic detection of trans-phosphorylated ITAM-SH2-interactions
    • Osborne MA, Dalton S, Kochan JP: The yeast tribrid system - genetic detection of trans-phosphorylated ITAM-SH2-interactions. Biotechnology 1995, 13:1474-1478.
    • (1995) Biotechnology , vol.13 , pp. 1474-1478
    • Osborne, M.A.1    Dalton, S.2    Kochan, J.P.3
  • 82
    • 0029587597 scopus 로고
    • Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase C gamma 1, Grb2, and phosphatidylinositol 3-kinase
    • Huang X, Li Y, Tanaka K, Moore KG, Hayashi JI: Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase C gamma 1, Grb2, and phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1995, 92:11618-11622.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 11618-11622
    • Huang, X.1    Li, Y.2    Tanaka, K.3    Moore, K.G.4    Hayashi, J.I.5
  • 83
    • 0030812414 scopus 로고    scopus 로고
    • Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation
    • Yokouchi M, Suzuki R, Masuhara M, Komiya S, Inoue A, Yoshimura A: Cloning and characterization of APS, an adaptor molecule containing PH and SH2 domains that is tyrosine phosphorylated upon B-cell receptor stimulation. Oncogene 1997, 15:7-15.
    • (1997) Oncogene , vol.15 , pp. 7-15
    • Yokouchi, M.1    Suzuki, R.2    Masuhara, M.3    Komiya, S.4    Inoue, A.5    Yoshimura, A.6
  • 84
    • 0033637359 scopus 로고    scopus 로고
    • Control of B cell production by the adaptor protein Ink. Definition of a conserved family of signal-modulating proteins
    • Takaki S, Sauer K, Iritani BM, Chien S, Ebihara Y, Tsuji K, Takatsu K, Perlmutter RM: Control of B cell production by the adaptor protein Ink. Definition of a conserved family of signal-modulating proteins. Immunity 2000, 13:599-609.
    • (2000) Immunity , vol.13 , pp. 599-609
    • Takaki, S.1    Sauer, K.2    Iritani, B.M.3    Chien, S.4    Ebihara, Y.5    Tsuji, K.6    Takatsu, K.7    Perlmutter, R.M.8
  • 85
    • 0033562558 scopus 로고    scopus 로고
    • Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes
    • Horrevoets AJ, Fontijn RD, van Zonneveld AJ, de Vries CJ, ten Cate JW, Pannekoek H: Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes. Blood 1999, 93:3418-3431.
    • (1999) Blood , vol.93 , pp. 3418-3431
    • Horrevoets, A.J.1    Fontijn, R.D.2    Van Zonneveld, A.J.3    De Vries, C.J.4    Ten Cate, J.W.5    Pannekoek, H.6
  • 86
    • 0034723360 scopus 로고    scopus 로고
    • Identification of a novel tumor necrosis factor-alpha-inducible gene, SCC-S2, containing the consensus sequence of a death effector domain of fas-associated death domain-like interleukin-1 beta-converting enzyme-inhibitory protein
    • Kumar D, Whiteside TL, Kasid U: Identification of a novel tumor necrosis factor-alpha-inducible gene, SCC-S2, containing the consensus sequence of a death effector domain of fas-associated death domain-like interleukin-1 beta-converting enzyme-inhibitory protein. J Biol Chem 2000, 275:2973-2978.
    • (2000) J Biol Chem , vol.275 , pp. 2973-2978
    • Kumar, D.1    Whiteside, T.L.2    Kasid, U.3


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