메뉴 건너뛰기




Volumn 8, Issue 11, 2009, Pages 2418-2431

A new approach for quantitative phosphoproteomic dissection of signaling pathways applied to T cell receptor activation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE ZAP 70; T LYMPHOCYTE RECEPTOR;

EID: 72149093283     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M800307-MCP200     Document Type: Article
Times cited : (64)

References (58)
  • 5
    • 0035356565 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses
    • Goshe, M. B., Conrads, T. P., Panisko, E. A., Angell, N. H., Veenstra, T. D., and Smith, R. D. (2001) Phosphoprotein isotope-coded affinity tag approach for isolating and quantitating phosphopeptides in proteome-wide analyses. Anal. Chem. 73, 2578-2586
    • (2001) Anal. Chem. , vol.73 , pp. 2578-2586
    • Goshe, M.B.1    Conrads, T.P.2    Panisko, E.A.3    Angell, N.H.4    Veenstra, T.D.5    Smith, R.D.6
  • 6
    • 33750456519 scopus 로고    scopus 로고
    • Global, in Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648 (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 7
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C., and Tempst, P. (1999) Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Chem. 71, 2883-2892
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 8
    • 33646583172 scopus 로고    scopus 로고
    • More sensitive and quantitative proteomic measurements using very low flow rate porous silica monolithic LC columns with electrospray ionization-mass spectrometry
    • DOI 10.1021/pr050424y
    • Luo, Q., Tang, K., Yang, F., Elias, A., Shen, Y., Moore, R. J., Zhao, R., Hixson, K. K., Rossie, S. S., and Smith, R. D. (2006) More sensitive and quantitative proteomic measurements using very low flow rate porous silica monolithic LC columns with electrospray ionization-mass spectrometry. J. Proteome Res. 5, 1091-1097 (Pubitemid 43727787)
    • (2006) Journal of Proteome Research , vol.5 , Issue.5 , pp. 1091-1097
    • Luo, Q.1    Tang, K.2    Yang, F.3    Elias, A.4    Shen, Y.5    Moore, R.J.6    Zhao, R.7    Hixson, K.K.8    Rossie, S.S.9    Smith, R.D.10
  • 9
    • 2442658049 scopus 로고    scopus 로고
    • Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry
    • Brill, L. M., Salomon, A. R., Ficarro, S. B., Mukherji, M., Stettler-Gill, M., and Peters, E. C. (2004) Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal. Chem. 76, 2763-2772
    • (2004) Anal. Chem. , vol.76 , pp. 2763-2772
    • Brill, L.M.1    Salomon, A.R.2    Ficarro, S.B.3    Mukherji, M.4    Stettler-Gill, M.5    Peters, E.C.6
  • 12
    • 33749332751 scopus 로고    scopus 로고
    • Temporal dynamics of tyrosine phosphorylation in insulin signaling
    • DOI 10.2337/db06-0148
    • Schmelzte, K., Kane, S., Gridley, S., Lienhard, G. E., and White, F. M. (2006) Temporal dynamics of tyrosine phosphorylation in insulin signaling. Diabetes 55, 2171-2179 (Pubitemid 44743613)
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2171-2179
    • Schmelzle, K.1    Kane, S.2    Gridley, S.3    Lienhard, G.E.4    White, F.M.5
  • 14
    • 26844576371 scopus 로고    scopus 로고
    • Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules
    • Zhang, Y., Wolf-Yadlin, A., Ross, P. L., Pappin, D. J., Rush, J., Lauffenburger, D. A., and White, F. M. (2005) Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol. Cell. Proteomics 4, 1240-1250
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1240-1250
    • Zhang, Y.1    Wolf-Yadlin, A.2    Ross, P.L.3    Pappin, D.J.4    Rush, J.5    Lauffenburger, D.A.6    White, F.M.7
  • 15
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 16
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 17
    • 11244277183 scopus 로고    scopus 로고
    • Automated immobilized metal affinity chromatography/nano-liquid chromatography/electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites
    • Ficarro, S. B., Salomon, A. R., Brill, L. M., Mason, D. E., Stettler-Gill, M., Brock, A., and Peters, E. C. (2005) Automated immobilized metal affinity chromatography/nano-liquid chromatography/electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites. Rapid Commun. Mass Spectrom. 19, 57-71
    • (2005) Rapid Commun. Mass Spectrom. , vol.19 , pp. 57-71
    • Ficarro, S.B.1    Salomon, A.R.2    Brill, L.M.3    Mason, D.E.4    Stettler-Gill, M.5    Brock, A.6    Peters, E.C.7
  • 18
    • 0032968708 scopus 로고    scopus 로고
    • The dynamics of T cell receptor signaling: Complex orchestration and the key roles of tempo and cooperation
    • Germain, R. N., and Stefanová, I. (1999) The dynamics of T cell receptor signaling: complex orchestration and the key roles of tempo and cooperation. Annu. Rev. Immunol. 17, 467-522
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 467-522
    • Germain, R.N.1    Stefanová, I.2
  • 19
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson, L. E. (2002) Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 20, 371-394
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 20
    • 0029550722 scopus 로고
    • Molecular and genetic insights into T-cell antigen receptor signaling
    • Weiss, A., Kadlecek, T., Iwashima, M., Chan, A., and Van Oers, N. (1995) Molecular and genetic insights into T-cell antigen receptor signaling. Ann. NY. Acad. Sci. 766, 149-156
    • (1995) Ann. NY. Acad. Sci. , vol.766 , pp. 149-156
    • Weiss, A.1    Kadlecek, T.2    Iwashima, M.3    Chan, A.4    Van Oers, N.5
  • 21
    • 1842631103 scopus 로고    scopus 로고
    • Jurkat T cells and development of the T-cell receptor signaling paradigm
    • Abraham, R. T., and Weiss, A. (2004) Jurkat T cells and development of the T-cell receptor signaling paradigm. Nat. Rev. Immunol. 4, 301-308
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 301-308
    • Abraham, R.T.1    Weiss, A.2
  • 22
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway
    • Finco, T. S., Kadlecek, T., Zhang, W., Samelson, L. E., and Weiss, A. (1998) LAT is required forTCR-mediated activation of PLCgamma1 and the Ras pathway. Immunity 9, 617-626 (Pubitemid 28557590)
    • (1998) Immunity , vol.9 , Issue.5 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 23
    • 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, B. J., Williams, B. L., Nilson, A. E., Maynor, H. O., and Abraham, R. T. (2000) 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. 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
  • 24
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D. B., and Weiss, A. (1992) Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70, 585-593
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 25
    • 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, B. L., Schreiber, K. L., Zhang, W., Wange, R. L., Samelson, L. E., Leibson, P. J., and Abraham, R. T. (1998) 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. 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
  • 26
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76- Deficient T cell
    • DOI 10.1126/science.281.5375.413
    • Yablonski, D., Kuhne, M. R., Kadlecek, T., and Weiss, A. (1998) Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell. Science 281, 413-416 (Pubitemid 28340785)
    • (1998) Science , vol.281 , Issue.5375 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 27
    • 0032878516 scopus 로고    scopus 로고
    • Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment
    • Shan, X., and Wange, R. L. (1999) Itk/Emt/Tsk activation in response to CD3 cross-linking in Jurkat T cells requires ZAP-70 and Lat and is independent of membrane recruitment. J. Biol. Chem. 274, 29323-29330
    • (1999) J. Biol. Chem. , vol.274 , pp. 29323-29330
    • Shan, X.1    Wange, R.L.2
  • 28
    • 0034665654 scopus 로고    scopus 로고
    • Signaling via LAT (linker for T-cell activation) and Syk/ZAP70 is required for ERK activation and NFAT transcriptional activation following CD2 stimulation
    • Martelli, M. P., Lin, H., Zhang, W., Samelson, L. E., and Bierer, B. E. (2000) Signaling via LAT (linker for T-cell activation) and Syk/ZAP70 is required for ERK activation and NFAT transcriptional activation following CD2 stimulation. Stood 96, 2181-2190 (Pubitemid 30696248)
    • (2000) Blood , vol.96 , Issue.6 , pp. 2181-2190
    • Martelli, M.P.1    Lin, H.2    Zhang, W.3    Samelson, L.E.4    Bierer, B.E.5
  • 29
    • 0032562576 scopus 로고    scopus 로고
    • ZAP-70-dependent and -independent activation of Erk in Jurkat T cells. Differences in signaling induced by H2o2 and Cd3 cross-linking
    • Griffith, C. E., Zhang, W., and Wange, R. L. (1998) ZAP-70-dependent and -independent activation of Erk in Jurkat T cells. Differences in signaling induced by H2o2 and Cd3 cross-linking. J. Biol. Chem. 273, 10771-10776
    • (1998) J. Biol. Chem. , vol.273 , pp. 10771-10776
    • Griffith, C.E.1    Zhang, W.2    Wange, R.L.3
  • 30
    • 0036646079 scopus 로고    scopus 로고
    • Automation of nanoscale microcapillary liquid chromatography-tandem mass spectrometry with a vented column
    • Licklider, L. J., Thoreen, C. C., Peng, J., and Gygi, S. P. (2002) Automation of nanoscale microcapillary liquid chromatography-tandem mass spectrometry with a vented column. Anal. Chem. 74, 3076-3083
    • (2002) Anal. Chem. , vol.74 , pp. 3076-3083
    • Licklider, L.J.1    Thoreen, C.C.2    Peng, J.3    Gygi, S.P.4
  • 31
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng, J. A., McCormack, J. R., and Yates, J. R., 3rd (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J. Am. Soc. Mass Spectrom. 5, 976-989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.A.1    McCormack, J.R.2    Yates III, J.R.3
  • 32
    • 67649213039 scopus 로고    scopus 로고
    • Integrated platform for high-throughput statistical and manual validation of tandem mass spectra
    • Yu, K., Sabelli, A., DeKeukelaere, L., Park, R., Sindi, S., Gatsonis, C. A., and Salomon, A. R. (2009) Integrated platform for high-throughput statistical and manual validation of tandem mass spectra. Proteomics 9, 3115-3125
    • (2009) Proteomics , vol.9 , pp. 3115-3125
    • Yu, K.1    Sabelli, A.2    Dekeukelaere, L.3    Park, R.4    Sindi, S.5    Gatsonis, C.A.6    Salomon, A.R.7
  • 33
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias, J. E., and Gygi, S. P. (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat. Methods 4, 207-214
    • (2007) Nat. Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 34
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., and Gygi, S. P. (2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotechnol. 24, 1285-1292
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villén, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 35
    • 0029060824 scopus 로고
    • T-cell activation: Integration of signals from the antigen receptor and costimulatory molecules
    • Robey, E., and Allison, J. P. (1995) T-cell activation: integration of signals from the antigen receptor and costimulatory molecules. Immunol. Today 16, 306-310
    • (1995) Immunol. Today , vol.16 , pp. 306-310
    • Robey, E.1    Allison, J.P.2
  • 36
    • 0028832018 scopus 로고
    • T-cell antigen receptor-induced signal-transduction pathways-activation and function of protein kinases C in T lymphocytes
    • Szamel, M., and Resch, K. (1995) T-cell antigen receptor-induced signal-transduction pathways-activation and function of protein kinases C in T lymphocytes. Eur. J. Biochem. 228, 1-15
    • (1995) Eur. J. Biochem. , vol.228 , pp. 1-15
    • Szamel, M.1    Resch, K.2
  • 37
    • 0034600901 scopus 로고    scopus 로고
    • Negative regulation of T cell proliferation and interieukin 2 production by the serine threonine kinase GSK-3
    • Ohteki, T., Parsons, M., Zakarian, A., Jones, R. G., Nguyen, L. T., Woodgett, J. R., and Ohashi, P. S. (2000) Negative regulation of T cell proliferation and interieukin 2 production by the serine threonine kinase GSK-3. J. Exp. Med. 192, 99-104
    • (2000) J. Exp. Med. , vol.192 , pp. 99-104
    • Ohteki, T.1    Parsons, M.2    Zakarian, A.3    Jones, R.G.4    Nguyen, L.T.5    Woodgett, J.R.6    Ohashi, P.S.7
  • 38
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson, D., Bakinowski, M., Thomas, M. L., Horejsi, V., and Veillette, A. (2003) Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol. Cell. Biol. 23, 2017-2028
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2017-2028
    • Davidson, D.1    Bakinowski, M.2    Thomas, M.L.3    Horejsi, V.4    Veillette, A.5
  • 39
    • 3242769204 scopus 로고    scopus 로고
    • T-cell receptor-induced phosphorylation of the zeta chain is efficiently promoted by ZAP-70 but not Syk
    • DOI 10.1182/blood-2003-12-4314
    • Steinberg, M., Adjali, O., Swainson, L., Merida, P., Di Bartolo, V., Pelletier, L., Taylor, N., and Noraz, N. (2004) T-cell receptor-induced phosphorylation of the zeta chain is efficiently promoted by ZAP-70 but not Syk. Blood 104, 760-767 (Pubitemid 38970570)
    • (2004) Blood , vol.104 , Issue.3 , pp. 760-767
    • Steinberg, M.1    Adjali, O.2    Swainson, L.3    Merida, P.4    Di Bartolo, V.5    Pelletier, L.6    Taylor, N.7    Noraz, N.8
  • 40
    • 0029008301 scopus 로고
    • Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex
    • Thorne, M., Duplay, P., Guttinger, M., and Acuto, O. (1995) Syk and ZAP-70 mediate recruitment of p56lck/CD4 to the activated T cell receptor/CD3/zeta complex. J. Exp. Med. 181, 1997-2006
    • (1995) J. Exp. Med. , vol.181 , pp. 1997-2006
    • Thorne, M.1    Duplay, P.2    Guttinger, M.3    Acuto, O.4
  • 41
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L., and Samelson, L. E. (1996) Complex complexes: signaling at the TCR. Immunity 5, 197-205
    • (1996) Immunity , vol.5 , pp. 197-205
    • Wange, R.L.1    Samelson, L.E.2
  • 42
    • 0029866039 scopus 로고    scopus 로고
    • Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes
    • van Oers, N. S., Killeen, N., and Weiss, A. (1996) Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes. J. Exp. Med. 183, 1053-1062
    • (1996) J. Exp. Med. , vol.183 , pp. 1053-1062
    • Van Oers, N.S.1    Killeen, N.2    Weiss, A.3
  • 43
    • 0026681275 scopus 로고
    • The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity
    • Bergman, M., Mustelin, T., Oetken, C., Partanen, J., Flint, N. A., Amrein, K. E., Autero, M., Burn, P., and Alitalo, K. (1992) The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11, 2919-2924
    • (1992) EMBO J. , vol.11 , pp. 2919-2924
    • Bergman, M.1    Mustelin, T.2    Oetken, C.3    Partanen, J.4    Flint, N.A.5    Amrein, K.E.6    Autero, M.7    Burn, P.8    Alitalo, K.9
  • 46
    • 0029904138 scopus 로고    scopus 로고
    • Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling
    • Plas, D. R., Johnson, R., Pingel, J. T., Matthews, R. J., Dalton, M., Roy, G., Chan, A. C., and Thomas, M. L. (1996) Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling. Science 272, 1173-1176 (Pubitemid 26169472)
    • (1996) Science , vol.272 , Issue.5265 , pp. 1173-1176
    • Plas, D.R.1    Johnson, R.2    Pingel, J.T.3    Matthews, R.J.4    Dalton, M.5    Roy, G.6    Chan, A.C.7    Thomas, M.L.8
  • 47
    • 0037338890 scopus 로고    scopus 로고
    • TCR ligand discrimination is enforced by competing ERK positive and SHP-1 negative feedback pathways
    • Stefanová, I., Hemmer, B., Vergelli, M., Martin, R., Biddison, W. E., and Germain, R. N. (2003) TCR ligand discrimination is enforced by competing ERK positive and SHP-1 negative feedback pathways. Nat. Immunol. 4, 248-254
    • (2003) Nat. Immunol. , vol.4 , pp. 248-254
    • Stefanová, I.1    Hemmer, B.2    Vergelli, M.3    Martin, R.4    Biddison, W.E.5    Germain, R.N.6
  • 48
    • 3042645122 scopus 로고    scopus 로고
    • Positive feedback regulation of PLCgamma1/Ca(2+) signaling by PKCtheta in restimulated T cells via a Tec kinase-dependent pathway
    • Altman, A., Kaminski, S., Busuttil, V., Drain, N., Hu, J., Tadevosyan, Y., Hipskind, R. A., and Villalba, M. (2004) Positive feedback regulation of PLCgamma1/Ca(2+) signaling by PKCtheta in restimulated T cells via a Tec kinase-dependent pathway. Eur. J. Immunol. 34, 2001-2011
    • (2004) Eur. J. Immunol. , vol.34 , pp. 2001-2011
    • Altman, A.1    Kaminski, S.2    Busuttil, V.3    Drain, N.4    Hu, J.5    Tadevosyan, Y.6    Hipskind, R.A.7    Villalba, M.8
  • 49
    • 0037340163 scopus 로고    scopus 로고
    • Tuning the immune system: Competing positive and negative feedback loops
    • Mueller, D. L. (2003) Tuning the immune system: competing positive and negative feedback loops. Nat. Immunol. 4, 210-211
    • (2003) Nat. Immunol. , vol.4 , pp. 210-211
    • Mueller, D.L.1
  • 50
    • 0037174928 scopus 로고    scopus 로고
    • SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation
    • Wu, L., Yu, Z., and Shen, S. H. (2002) SKAP55 recruits to lipid rafts and positively mediates the MAPK pathway upon T cell receptor activation. J. Biol. Chem. 277, 40420-40427
    • (2002) J. Biol. Chem. , vol.277 , pp. 40420-40427
    • Wu, L.1    Yu, Z.2    Shen, S.H.3
  • 52
    • 52949130240 scopus 로고    scopus 로고
    • SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion
    • Wang, H., and Rudd, C. E. (2008) SKAP-55, SKAP-55-related and ADAP adaptors modulate integrin-mediated immune-cell adhesion. Trends Cell Biol. 18, 486-493
    • (2008) Trends Cell Biol. , vol.18 , pp. 486-493
    • Wang, H.1    Rudd, C.E.2
  • 53
    • 0035850897 scopus 로고    scopus 로고
    • Specificity in pleckstrin homology (PH) domain membrane targeting: A role for a phosphoinositide-protein co-operative mechanism
    • DOI 10.1016/S0014-5793(01)02909-X, PII S001457930102909X
    • Maffucci, T., and Falasca, M. (2001) Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein cooperative mechanism. FEBS Lett. 506, 173-179 (Pubitemid 32964808)
    • (2001) FEBS Letters , vol.506 , Issue.3 , pp. 173-179
    • Maffucci, T.1    Falasca, M.2
  • 54
    • 0038043212 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation
    • Storz, P., Döppler, H., Johannes, F. J., and Toker, A. (2003) Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation. J. Biol. Chem. 278, 17969-17976
    • (2003) J. Biol. Chem. , vol.278 , pp. 17969-17976
    • Storz, P.1    Döppler, H.2    Johannes, F.J.3    Toker, A.4
  • 55
    • 0035817326 scopus 로고    scopus 로고
    • NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface molecule contributing to the inability of natural killer cells to kill Epstein-Barr virus-infected B cells in X-linked lymphoproliferative disease
    • Bottino, C., Falco, M., Parolini, S., Marcenaro, E., Augugliaro, R., Sivori, S., Landi, E., Biassoni, R., Notarangelo, L. D., Moretta, L., and Moretta, A. (2001) NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface molecule contributing to the inability of natural killer cells to kill Epstein-Barr virus-infected B cells in X-linked lymphoproliferative disease. J. Exp. Med. 194, 235-246
    • (2001) J. Exp. Med. , vol.194 , pp. 235-246
    • Bottino, C.1    Falco, M.2    Parolini, S.3    Marcenaro, E.4    Augugliaro, R.5    Sivori, S.6    Landi, E.7    Biassoni, R.8    Notarangelo, L.D.9    Moretta, L.10    Moretta, A.11
  • 56
    • 3042543849 scopus 로고    scopus 로고
    • Hemophilic interaction of NTBA, a member of the CD2 molecular family: Induction of cytotoxicity and cytokine release in human NK cells
    • Falco, M., Marcenaro, E., Romeo, E., Bellora, F., Marras, D., Vély, F., Ferracci, G., Moretta, L., Moretta, A., and Bottino, C. (2004) Hemophilic interaction of NTBA, a member of the CD2 molecular family: induction of cytotoxicity and cytokine release in human NK cells. Eur. J. Immunol. 34, 1663-1672
    • (2004) Eur. J. Immunol. , vol.34 , pp. 1663-1672
    • Falco, M.1    Marcenaro, E.2    Romeo, E.3    Bellora, F.4    Marras, D.5    Vély, F.6    Ferracci, G.7    Moretta, L.8    Moretta, A.9    Bottino, C.10
  • 57
    • 33744484987 scopus 로고    scopus 로고
    • Uncoupling of T-cell effector functions by inhibitory killer immunoglobulin-like receptors
    • DOI 10.1182/blood-2005-06-2519
    • Henel, G., Singh, K., Cul, D., Pryshchep, S., Lee, W. W., Weyand, C. M., and Goronzy, J. J. (2006) Uncoupling of T-cell effector functions by inhibitory killer immunoglobulin-like receptors. Blood 107, 4449-4457 (Pubitemid 43801372)
    • (2006) Blood , vol.107 , Issue.11 , pp. 4449-4457
    • Henel, G.1    Singh, K.2    Cui, D.3    Pryshchep, S.4    Lee, W.-W.5    Weyand, C.M.6    Goronzy, J.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.