메뉴 건너뛰기




Volumn 16, Issue 5, 2004, Pages 285-293

Signaling control of memory T cell generation and function

Author keywords

Cellular differentiation; Signal transduction; T cell receptors; T lymphocytes; Tyrosine kinase

Indexed keywords

PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 7444222893     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smim.2004.08.009     Document Type: Article
Times cited : (53)

References (123)
  • 1
    • 0031884839 scopus 로고    scopus 로고
    • The duration of antigenic stimulation determines the fate of naive and effector T cells
    • G. Iezzi, K. Karjalainen, and A. Lanzavecchia The duration of antigenic stimulation determines the fate of naive and effector T cells Immunity 8 1998 89 95
    • (1998) Immunity , vol.8 , pp. 89-95
    • Iezzi, G.1    Karjalainen, K.2    Lanzavecchia, A.3
  • 2
    • 0036550559 scopus 로고    scopus 로고
    • Effector and memory T-cell differentiation: Implications for vaccine development
    • S.M. Kaech, E.J. Wherry, and R. Ahmed Effector and memory T-cell differentiation: implications for vaccine development Nat Rev Immunol 2 2002 251 262
    • (2002) Nat Rev Immunol , vol.2 , pp. 251-262
    • Kaech, S.M.1    Wherry, E.J.2    Ahmed, R.3
  • 3
    • 0347382593 scopus 로고    scopus 로고
    • Selective expression of the interleukin 7 receptor identifies effector CD8 T cells that give rise to long-lived memory cells
    • S.M. Kaech, J.T. Tan, E.J. Wherry, B.T. Konieczny, C.D. Surh, and R. Ahmed Selective expression of the interleukin 7 receptor identifies effector CD8 T cells that give rise to long-lived memory cells Nat Immunol 4 2003 1191 1198
    • (2003) Nat Immunol , vol.4 , pp. 1191-1198
    • Kaech, S.M.1    Tan, J.T.2    Wherry, E.J.3    Konieczny, B.T.4    Surh, C.D.5    Ahmed, R.6
  • 4
    • 2142756661 scopus 로고    scopus 로고
    • CD8alphaalpha-mediated survival and differentiation of CD8 memory T cell precursors
    • L.T. Madakamutil, U. Christen, and C.J. Lena CD8alphaalpha-mediated survival and differentiation of CD8 memory T cell precursors Science 304 2004 590 593
    • (2004) Science , vol.304 , pp. 590-593
    • Madakamutil, L.T.1    Christen, U.2    Lena, C.J.3
  • 5
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • L.P. Kane, J. Lin, and A. Weiss Signal transduction by the TCR for antigen Curr Opin Immunol 12 2000 242 249
    • (2000) Curr Opin Immunol , vol.12 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 6
    • 0037318720 scopus 로고    scopus 로고
    • Adaptors as central mediators of signal transduction in immune cells
    • M.S. Jordan, A.L. Singer, and G.A. Koretzky Adaptors as central mediators of signal transduction in immune cells Nat Immunol 4 2003 110 116
    • (2003) Nat Immunol , vol.4 , pp. 110-116
    • Jordan, M.S.1    Singer, A.L.2    Koretzky, G.A.3
  • 7
    • 0038578688 scopus 로고    scopus 로고
    • GTPases and T cell activation
    • D.A. Cantrell GTPases and T cell activation Immunol Rev 192 2003 122 130
    • (2003) Immunol Rev , vol.192 , pp. 122-130
    • Cantrell, D.A.1
  • 8
    • 0035366079 scopus 로고    scopus 로고
    • MAP-kinase signaling pathways in T cells
    • M. Rincon MAP-kinase signaling pathways in T cells Curr Opin Immunol 13 2001 339 345
    • (2001) Curr Opin Immunol , vol.13 , pp. 339-345
    • Rincon, M.1
  • 9
    • 0028361589 scopus 로고
    • NF-AT components define a family of transcription factors targeted in T-cell activation
    • J.P. Northrop, S.N. Ho, and L. Chen NF-AT components define a family of transcription factors targeted in T-cell activation Nature 369 1994 497 502
    • (1994) Nature , vol.369 , pp. 497-502
    • Northrop, J.P.1    Ho, S.N.2    Chen, L.3
  • 10
    • 0032969001 scopus 로고    scopus 로고
    • Transcriptonal regulation of T lymphocyte development and function
    • C.T. Kuo, and J.M. Leiden Transcriptonal regulation of T lymphocyte development and function Annu Rev Immunol 17 1999 149 187
    • (1999) Annu Rev Immunol , vol.17 , pp. 149-187
    • Kuo, C.T.1    Leiden, J.M.2
  • 11
    • 0029133646 scopus 로고
    • Essential role for ZAP-70 in both positive and negative selection of thymocytes
    • I. Negishi, N. Motoyama, and K. Nakayama Essential role for ZAP-70 in both positive and negative selection of thymocytes Nature 376 1995 435 438
    • (1995) Nature , vol.376 , pp. 435-438
    • Negishi, I.1    Motoyama, N.2    Nakayama, K.3
  • 12
    • 0033103833 scopus 로고    scopus 로고
    • Essential role of LAT in T cell development
    • W. Zhang, C.L. Sommers, and D.N. Burshtyn Essential role of LAT in T cell development Immunity 10 1999 323 332
    • (1999) Immunity , vol.10 , pp. 323-332
    • Zhang, W.1    Sommers, C.L.2    Burshtyn, D.N.3
  • 13
    • 0032540906 scopus 로고    scopus 로고
    • Requirement for the leukocyte-specific adapter protein SLP-76 for normal T cell development
    • J.L. Clements, B. Yang, and S.E. Ross-Barta Requirement for the leukocyte-specific adapter protein SLP-76 for normal T cell development Science 281 1998 416 419
    • (1998) Science , vol.281 , pp. 416-419
    • Clements, J.L.1    Yang, B.2    Ross-Barta, S.E.3
  • 14
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • D.B. Straus, and A. Weiss Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor Cell 70 1992 585 593
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 15
    • 0035877977 scopus 로고    scopus 로고
    • Generation and biochemical analysis of human effector CD4 T cells: Alterations in tyrosine phosphorylation and loss of CD3ζ expression
    • S. Krishnan, V.G. Warke, M.P. Nambiar, H.K. Wong, G.C. Tsokos, and D.L. Farber Generation and biochemical analysis of human effector CD4 T cells: alterations in tyrosine phosphorylation and loss of CD3ζ expression Blood 97 2001 3851 3859
    • (2001) Blood , vol.97 , pp. 3851-3859
    • Krishnan, S.1    Warke, V.G.2    Nambiar, M.P.3    Wong, H.K.4    Tsokos, G.C.5    Farber, D.L.6
  • 16
    • 0037083522 scopus 로고    scopus 로고
    • Differential SLP-76 expression and TCR-mediated signaling in effector and memory CD4 T cells
    • S.F. Hussain, C.F. Anderson, and D.L. Farber Differential SLP-76 expression and TCR-mediated signaling in effector and memory CD4 T cells J Immunol 168 2002 1557 1565
    • (2002) J Immunol , vol.168 , pp. 1557-1565
    • Hussain, S.F.1    Anderson, C.F.2    Farber, D.L.3
  • 17
    • 0033568458 scopus 로고    scopus 로고
    • Effector CD4 T cells are biochemically distinct from the memory subset: Evidence for long-term persistence of effectors in vivo
    • M. Ahmadzadeh, S.F. Hussain, and D.L. Farber Effector CD4 T cells are biochemically distinct from the memory subset: evidence for long-term persistence of effectors in vivo J Immunol 163 1999 3053 3063
    • (1999) J Immunol , vol.163 , pp. 3053-3063
    • Ahmadzadeh, M.1    Hussain, S.F.2    Farber, D.L.3
  • 18
    • 0030825384 scopus 로고    scopus 로고
    • Differential TCR-mediated signaling in naive and memory CD4 T cells
    • D.L. Farber, O. Acuto, and K. Bottomly Differential TCR-mediated signaling in naive and memory CD4 T cells Eur J Immunol 27 1997 2094 2101
    • (1997) Eur J Immunol , vol.27 , pp. 2094-2101
    • Farber, D.L.1    Acuto, O.2    Bottomly, K.3
  • 19
    • 0028912220 scopus 로고
    • Control of memory CD4 T cell activation: MHC class II molecules on antigen presenting cells and CD4 ligation inhibit memory but not naive CD4 T cells
    • D.L. Farber, M. Luqman, O. Acuto, and K. Bottomly Control of memory CD4 T cell activation: MHC class II molecules on antigen presenting cells and CD4 ligation inhibit memory but not naive CD4 T cells Immunity 2 1995 249 259
    • (1995) Immunity , vol.2 , pp. 249-259
    • Farber, D.L.1    Luqman, M.2    Acuto, O.3    Bottomly, K.4
  • 20
    • 0033032259 scopus 로고    scopus 로고
    • CD4+CD45RA+ and CD4+CD45RO+ T cells differ in their TCR-associated signaling responses
    • S.R. Hall, B.M. Heffernan, N.T. Thompson, and W.C. Rowan CD4+CD45RA+ and CD4+CD45RO+ T cells differ in their TCR-associated signaling responses Eur J Immunol 29 1999 2098 2106
    • (1999) Eur J Immunol , vol.29 , pp. 2098-2106
    • Hall, S.R.1    Heffernan, B.M.2    Thompson, N.T.3    Rowan, W.C.4
  • 21
    • 0038189783 scopus 로고    scopus 로고
    • TCR signal transduction in antigen-specific memory CD8 T cells
    • E.N. Kersh, S.M. Kaech, and T.M. Onami TCR signal transduction in antigen-specific memory CD8 T cells J Immunol 170 2003 5455 5463
    • (2003) J Immunol , vol.170 , pp. 5455-5463
    • Kersh, E.N.1    Kaech, S.M.2    Onami, T.M.3
  • 22
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kDa protein-tyrosine kinase that associates with the TCR ζ chain
    • A.C. Chan, M. Iwashima, C.W. Turck, and A. Weiss ZAP-70: a 70 kDa protein-tyrosine kinase that associates with the TCR ζ chain Cell 71 1992 649 662
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 23
    • 0141650477 scopus 로고    scopus 로고
    • Proximal changes in signal transduction that modify CD8+ T cell responsiveness in vivo
    • S. Guillaume, L. Tuosto, C. Tanchot, V. Di Bartolo, O. Acuto, and B. Rocha Proximal changes in signal transduction that modify CD8+ T cell responsiveness in vivo Eur J Immunol 33 2003 2551 2556
    • (2003) Eur J Immunol , vol.33 , pp. 2551-2556
    • Guillaume, S.1    Tuosto, L.2    Tanchot, C.3    Di Bartolo, V.4    Acuto, O.5    Rocha, B.6
  • 24
    • 0033577864 scopus 로고    scopus 로고
    • Developmental regulation of Lck targeting to the CD8 coreceptor controls signaling in naive and memory T cells
    • M.F. Bachmann, A. Gallimore, and S. Linkert Developmental regulation of Lck targeting to the CD8 coreceptor controls signaling in naive and memory T cells J Exp Med 189 1999 1521 1529
    • (1999) J Exp Med , vol.189 , pp. 1521-1529
    • Bachmann, M.F.1    Gallimore, A.2    Linkert, S.3
  • 25
    • 0032921486 scopus 로고    scopus 로고
    • Distinct kinetics of cytokine production and cytolysis in effector and memory T cells after viral infection
    • M.F. Bachmann, M. Barner, A. Viola, and M. Kopf Distinct kinetics of cytokine production and cytolysis in effector and memory T cells after viral infection Eur J Immunol 29 1999 291 299
    • (1999) Eur J Immunol , vol.29 , pp. 291-299
    • Bachmann, M.F.1    Barner, M.2    Viola, A.3    Kopf, M.4
  • 26
    • 0034305740 scopus 로고    scopus 로고
    • CD4+ T cell survival is not directly linked to self-MHC-induced TCR signaling
    • J.R. Dorfman, I. Stefanova, K. Yasutomo, and R.N. Germain CD4+ T cell survival is not directly linked to self-MHC-induced TCR signaling Nat Immunol 1 2000 329 335
    • (2000) Nat Immunol , vol.1 , pp. 329-335
    • Dorfman, J.R.1    Stefanova, I.2    Yasutomo, K.3    Germain, R.N.4
  • 27
    • 0037446543 scopus 로고    scopus 로고
    • The FcRgamma subunit and Syk kinase replace the CD3zeta-chain and ZAP-70 kinase in the TCR signaling complex of human effector CD4 T cells
    • S. Krishnan, V.G. Warke, M.P. Nambiar, G.C. Tsokos, and D.L. Farber The FcRgamma subunit and Syk kinase replace the CD3zeta-chain and ZAP-70 kinase in the TCR signaling complex of human effector CD4 T cells J Immunol 170 2003 4189 4195
    • (2003) J Immunol , vol.170 , pp. 4189-4195
    • Krishnan, S.1    Warke, V.G.2    Nambiar, M.P.3    Tsokos, G.C.4    Farber, D.L.5
  • 28
    • 0037443553 scopus 로고    scopus 로고
    • Forced expression of the Fc receptor gamma-chain renders human T cells hyperresponsive to TCR/CD3 stimulation
    • M.P. Nambiar, C.U. Fisher, A. Kumar, C.G. Tsokos, V.G. Warke, and G.C. Tsokos Forced expression of the Fc receptor gamma-chain renders human T cells hyperresponsive to TCR/CD3 stimulation J Immunol 170 2003 2871 2876
    • (2003) J Immunol , vol.170 , pp. 2871-2876
    • Nambiar, M.P.1    Fisher, C.U.2    Kumar, A.3    Tsokos, C.G.4    Warke, V.G.5    Tsokos, G.C.6
  • 29
    • 1642444252 scopus 로고    scopus 로고
    • Zeta-associated protein of 70 kDa (ZAP-70), but not Syk, tyrosine kinase can mediate apoptosis of T cells through the Fas/Fas ligand, caspase-8 and caspase-3 pathways
    • L. Zhong, C.H. Wu, W.H. Lee, and C.P. Liu Zeta-associated protein of 70 kDa (ZAP-70), but not Syk, tyrosine kinase can mediate apoptosis of T cells through the Fas/Fas ligand, caspase-8 and caspase-3 pathways J Immunol 172 2004 1472 1482
    • (2004) J Immunol , vol.172 , pp. 1472-1482
    • Zhong, L.1    Wu, C.H.2    Lee, W.H.3    Liu, C.P.4
  • 30
    • 0034744286 scopus 로고    scopus 로고
    • Fc epsilon receptor type I gamma chain replaces the deficient T cell receptor zeta chain in T cells of patients with systemic lupus erythematosus
    • E.J. Enyedy, M.P. Nambiar, S.N. Liossis, G. Dennis, G.M. Kammer, and G.C. Tsokos Fc epsilon receptor type I gamma chain replaces the deficient T cell receptor zeta chain in T cells of patients with systemic lupus erythematosus Arthritis Rheum 44 2001 1114 1121
    • (2001) Arthritis Rheum , vol.44 , pp. 1114-1121
    • Enyedy, E.J.1    Nambiar, M.P.2    Liossis, S.N.3    Dennis, G.4    Kammer, G.M.5    Tsokos, G.C.6
  • 31
    • 0141955150 scopus 로고    scopus 로고
    • T cell rewiring in differentiation and disease
    • S. Krishnan, D.L. Farber, and G.C. Tsokos T cell rewiring in differentiation and disease J Immunol 171 2003 3325 3331
    • (2003) J Immunol , vol.171 , pp. 3325-3331
    • Krishnan, S.1    Farber, D.L.2    Tsokos, G.C.3
  • 32
    • 0028928422 scopus 로고
    • Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells
    • J.K. Jackman, D.G. Motto, and Q. Sun Molecular cloning of SLP-76, a 76-kDa tyrosine phosphoprotein associated with Grb2 in T cells J Biol Chem 270 1995 7029 7032
    • (1995) J Biol Chem , vol.270 , pp. 7029-7032
    • Jackman, J.K.1    Motto, D.G.2    Sun, Q.3
  • 33
    • 0000082758 scopus 로고    scopus 로고
    • Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function
    • J.B. Wardenburg, C. Fu, and J.K. Jackman Phosphorylation of SLP-76 by the ZAP-70 protein-tyrosine kinase is required for T-cell receptor function J Biol Chem 271 1996 19641 19644
    • (1996) J Biol Chem , vol.271 , pp. 19641-19644
    • Wardenburg, J.B.1    Fu, C.2    Jackman, J.K.3
  • 34
    • 0032498231 scopus 로고    scopus 로고
    • LAT: The ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation
    • W. Zhang, J. Sloan-Lancaster, J. Kitchen, R.P. Trible, and L.E. Samelson LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation Cell 92 1998 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
  • 35
    • 0033047309 scopus 로고    scopus 로고
    • Integration of T cell receptor-dependent signaling pathways by adapter proteins
    • J.L. Clements, N.J. Boerth, J.R. Lee, and G.A. Koretzky Integration of T cell receptor-dependent signaling pathways by adapter proteins Annu Rev Immunol 17 1999 89 108
    • (1999) Annu Rev Immunol , vol.17 , pp. 89-108
    • Clements, J.L.1    Boerth, N.J.2    Lee, J.R.3    Koretzky, G.A.4
  • 36
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
    • W. Zhang, B.J. Irvin, R.P. Trible, R.T. Abraham, and L.E. Samelson Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line Int Immunol 11 1999 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
  • 37
    • 0032541062 scopus 로고    scopus 로고
    • Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell
    • D. Yablonski, M.R. Kuhne, T. Kadlecek, and A. Weiss Uncoupling of nonreceptor tyrosine kinases from PLC-gamma1 in an SLP-76-deficient T cell Science 281 1998 413 416
    • (1998) Science , vol.281 , pp. 413-416
    • Yablonski, D.1    Kuhne, M.R.2    Kadlecek, T.3    Weiss, A.4
  • 38
    • 0029658306 scopus 로고    scopus 로고
    • P95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells
    • L. Tuosto, F. Michel, and O. Acuto p95vav associates with tyrosine-phosphorylated SLP-76 in antigen-stimulated T cells J Exp Med 184 1996 1161 1166
    • (1996) J Exp Med , vol.184 , pp. 1161-1166
    • Tuosto, L.1    Michel, F.2    Acuto, O.3
  • 39
    • 0033519283 scopus 로고    scopus 로고
    • Grf40, a novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT
    • H. Asada, N. Ishii, and Y. Sasaki Grf40, a novel Grb2 family member, is involved in T cell signaling through interaction with SLP-76 and LAT J Exp Med 189 1999 1383 1390
    • (1999) J Exp Med , vol.189 , pp. 1383-1390
    • Asada, H.1    Ishii, N.2    Sasaki, Y.3
  • 40
    • 0033583420 scopus 로고    scopus 로고
    • GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to regulate nuclear factor of activated T cell activation
    • C.L. Law, M.K. Ewings, and P.M. Chaudhary GrpL, a Grb2-related adaptor protein, interacts with SLP-76 to regulate nuclear factor of activated T cell activation J Exp Med 189 1999 1243 1253
    • (1999) J Exp Med , vol.189 , pp. 1243-1253
    • Law, C.L.1    Ewings, M.K.2    Chaudhary, P.M.3
  • 41
    • 0033597929 scopus 로고    scopus 로고
    • FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells
    • M. Raab, H. Kang, A. da Silva, X. Zhu, and C.E. Rudd FYN-T-FYB-SLP-76 interactions define a T-cell receptor zeta/CD3-mediated tyrosine phosphorylation pathway that up-regulates interleukin 2 transcription in T-cells J Biol Chem 274 1999 21170 21179
    • (1999) J Biol Chem , vol.274 , pp. 21170-21179
    • Raab, M.1    Kang, H.2    Da Silva, A.3    Zhu, X.4    Rudd, C.E.5
  • 42
    • 0030959305 scopus 로고    scopus 로고
    • Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases
    • M.A. Musci, L.R. Hendricks-Taylor, and D.G. Motto Molecular cloning of SLAP-130, an SLP-76-associated substrate of the T cell antigen receptor-stimulated protein tyrosine kinases J Biol Chem 272 1997 11674 11677
    • (1997) J Biol Chem , vol.272 , pp. 11674-11677
    • Musci, M.A.1    Hendricks-Taylor, L.R.2    Motto, D.G.3
  • 43
    • 0035929222 scopus 로고    scopus 로고
    • Coupling of the TCR to integrin activation by Slap-130/Fyb
    • E.J. Peterson, M.L. Woods, and S.A. Dmowski Coupling of the TCR to integrin activation by Slap-130/Fyb Science 293 2001 2263 2265
    • (2001) Science , vol.293 , pp. 2263-2265
    • Peterson, E.J.1    Woods, M.L.2    Dmowski, S.A.3
  • 44
    • 0035929128 scopus 로고    scopus 로고
    • Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap
    • E.K. Griffiths, C. Krawczyk, and Y.Y. Kong Positive regulation of T cell activation and integrin adhesion by the adapter Fyb/Slap Science 293 2001 2260 2263
    • (2001) Science , vol.293 , pp. 2260-2263
    • Griffiths, E.K.1    Krawczyk, C.2    Kong, Y.Y.3
  • 45
    • 0035831340 scopus 로고    scopus 로고
    • Requirement for the SLP-76 adaptor GADS in T cell development
    • J. Yoder, C. Pham, and Y.M. Iizuka Requirement for the SLP-76 adaptor GADS in T cell development Science 291 2001 1987 1991
    • (2001) Science , vol.291 , pp. 1987-1991
    • Yoder, J.1    Pham, C.2    Iizuka, Y.M.3
  • 46
    • 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
    • L. Buday, S.E. Egan, V.P. Rodriguez, D.A. Cantrell, and J. Downward 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 269 1994 9019 9023
    • (1994) J Biol Chem , vol.269 , pp. 9019-9023
    • Buday, L.1    Egan, S.E.2    Rodriguez, V.P.3    Cantrell, D.A.4    Downward, J.5
  • 47
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway
    • T.S. Finco, T. Kadlecek, W. Zhang, L.E. Samelson, and A. Weiss LAT is required for TCR-mediated activation of PLCgamma1 and the Ras pathway Immunity 9 1998 617 626
    • (1998) Immunity , vol.9 , pp. 617-626
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 48
    • 0035064074 scopus 로고    scopus 로고
    • Calcium signaling mechanisms in T lymphocytes
    • R.S. Lewis Calcium signaling mechanisms in T lymphocytes Annu Rev Immunol 19 2001 497 521
    • (2001) Annu Rev Immunol , vol.19 , pp. 497-521
    • Lewis, R.S.1
  • 49
    • 18244408051 scopus 로고    scopus 로고
    • Differential requirement for SLP-76 domains in T cell development and function
    • P.S. Myung, G.S. Derimanov, and M.S. Jordan Differential requirement for SLP-76 domains in T cell development and function Immunity 15 2001 1011 1026
    • (2001) Immunity , vol.15 , pp. 1011-1026
    • Myung, P.S.1    Derimanov, G.S.2    Jordan, M.S.3
  • 50
    • 0038549067 scopus 로고    scopus 로고
    • PI3K in lymphocyte development, differentiation and activation
    • K. Okkenhaug, and B. Vanhaesebroeck PI3K in lymphocyte development, differentiation and activation Nat Rev Immunol 3 2003 317 330
    • (2003) Nat Rev Immunol , vol.3 , pp. 317-330
    • Okkenhaug, K.1    Vanhaesebroeck, B.2
  • 51
    • 0032479864 scopus 로고    scopus 로고
    • T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane
    • E. Bruyns, A. Marie-Cardine, and H. Kirchgessner T cell receptor (TCR) interacting molecule (TRIM), a novel disulfide-linked dimer associated with the TCR-CD3-zeta complex, recruits intracellular signaling proteins to the plasma membrane J Exp Med 188 1998 561 575
    • (1998) J Exp Med , vol.188 , pp. 561-575
    • Bruyns, E.1    Marie-Cardine, A.2    Kirchgessner, H.3
  • 53
    • 0037047590 scopus 로고    scopus 로고
    • Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice
    • K. Okkenhaug, A. Bilancio, and G. Farjot Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice Science 297 2002 1031 1034
    • (2002) Science , vol.297 , pp. 1031-1034
    • Okkenhaug, K.1    Bilancio, A.2    Farjot, G.3
  • 54
    • 0035693742 scopus 로고    scopus 로고
    • CD28 as a molecular amplifier extending TCR ligation and signaling capabilities
    • F. Michel, G. Attal-Bonnefoy, G. Mangino, S. Mise-Omata, and O. Acuto CD28 as a molecular amplifier extending TCR ligation and signaling capabilities Immunity 15 2001 935 945
    • (2001) Immunity , vol.15 , pp. 935-945
    • Michel, F.1    Attal-Bonnefoy, G.2    Mangino, G.3    Mise-Omata, S.4    Acuto, O.5
  • 55
    • 0031408467 scopus 로고    scopus 로고
    • Activation and signal transduction via mitogen-activated protein (MAP) kinases in T lymphocytes
    • K. Hardy, and G. Chaudhri Activation and signal transduction via mitogen-activated protein (MAP) kinases in T lymphocytes Immunol Cell Biol 75 1997 528 545
    • (1997) Immunol Cell Biol , vol.75 , pp. 528-545
    • Hardy, K.1    Chaudhri, G.2
  • 56
    • 0028287296 scopus 로고
    • The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor
    • M. Izquierdo, S. Bowden, and D. Cantrell The role of Raf-1 in the regulation of extracellular signal-regulated kinase 2 by the T cell antigen receptor J Exp Med 180 1994 401 406
    • (1994) J Exp Med , vol.180 , pp. 401-406
    • Izquierdo, M.1    Bowden, S.2    Cantrell, D.3
  • 57
    • 0027459293 scopus 로고
    • Protein tyrosine kinases couple the interleukin-2 receptor to p21ras
    • M. Izquierdo, and D.A. Cantrell Protein tyrosine kinases couple the interleukin-2 receptor to p21ras Eur J Immunol 23 1993 131 135
    • (1993) Eur J Immunol , vol.23 , pp. 131-135
    • Izquierdo, M.1    Cantrell, D.A.2
  • 58
    • 0029836263 scopus 로고    scopus 로고
    • Rac-1 dependent stimulation of the JNK/SAPK signaling pathway by Vav
    • P. Crespo, X.R. Bustelo, and D.S. Aaronson Rac-1 dependent stimulation of the JNK/SAPK signaling pathway by Vav Oncogene 13 1996 455 460
    • (1996) Oncogene , vol.13 , pp. 455-460
    • Crespo, P.1    Bustelo, X.R.2    Aaronson, D.S.3
  • 59
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • P. Crespo, K.E. Schuebel, A.A. Ostrom, J.S. Gutkind, and X.R. Bustelo Phosphotyrosine-dependent activation of Rac-1 GDP/GTP exchange by the vav proto-oncogene product Nature 385 1997 169 172
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 60
    • 0032493028 scopus 로고    scopus 로고
    • Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction
    • L.J. Holsinger, I.A. Graef, and W. Swat Defects in actin-cap formation in Vav-deficient mice implicate an actin requirement for lymphocyte signal transduction Curr Biol 8 1998 563 572
    • (1998) Curr Biol , vol.8 , pp. 563-572
    • Holsinger, L.J.1    Graef, I.A.2    Swat, W.3
  • 61
    • 0034046180 scopus 로고    scopus 로고
    • T cell activation and the cytoskeleton
    • O. Acuto, and D. Cantrell T cell activation and the cytoskeleton Annu Rev Immunol 18 2000 165 184
    • (2000) Annu Rev Immunol , vol.18 , pp. 165-184
    • Acuto, O.1    Cantrell, D.2
  • 62
    • 0029975023 scopus 로고    scopus 로고
    • Blocked signal transduction to the ERK and JNK protein kinases in anergic CD4+ T cells
    • W. Li, C.D. Whaley, A. Mondino, and D.L. Mueller Blocked signal transduction to the ERK and JNK protein kinases in anergic CD4+ T cells Science 271 1996 1272 1276
    • (1996) Science , vol.271 , pp. 1272-1276
    • Li, W.1    Whaley, C.D.2    Mondino, A.3    Mueller, D.L.4
  • 64
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Z. Xia, M. Dickens, J. Raingeaud, R.J. Davis, and M.E. Greenberg Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis Science 270 1995 1326 1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeaud, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 65
    • 0027417482 scopus 로고
    • Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events
    • J.P. Secrist, L.A. Burns, L. Karnitz, G. Koretzky, and R.T. Abraham Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T-cell activation events J Biol Chem 268 1993 5886 5893
    • (1993) J Biol Chem , vol.268 , pp. 5886-5893
    • Secrist, J.P.1    Burns, L.A.2    Karnitz, L.3    Koretzky, G.4    Abraham, R.T.5
  • 66
    • 0026475905 scopus 로고
    • Activation of human peripheral blood T lymphocytes by pharmacological induction of protein-tyrosine phosphorylation
    • J.J. O'Shea, D.W. Mc Vicar, T.L. Bailey, C. Burns, and M.J. Smyth Activation of human peripheral blood T lymphocytes by pharmacological induction of protein-tyrosine phosphorylation Proc Natl Acad Sci USA 89 1992 10306 10310
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10306-10310
    • O'Shea, J.J.1    Mc Vicar, D.W.2    Bailey, T.L.3    Burns, C.4    Smyth, M.J.5
  • 67
    • 0025224548 scopus 로고
    • Phosphotyrosine phosphatases are involved in reversion of T lymphoblastic proliferation
    • A.V. Iivanainen, C. Lindqvist, T. Mustelin, and L.C. Andersson Phosphotyrosine phosphatases are involved in reversion of T lymphoblastic proliferation Eur J Immunol 20 1990 2509 2512
    • (1990) Eur J Immunol , vol.20 , pp. 2509-2512
    • Iivanainen, A.V.1    Lindqvist, C.2    Mustelin, T.3    Andersson, L.C.4
  • 68
    • 0011185737 scopus 로고
    • The leukocyte common antigen (CD45): A putative receptor-linked protein tyrosine phosphatase
    • H. Charbonneau, N.K. Tonks, K.A. Walsh, and E.H. Fischer The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase Proc Natl Acad Sci USA 85 1988 7182 7186
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7182-7186
    • Charbonneau, H.1    Tonks, N.K.2    Walsh, K.A.3    Fischer, E.H.4
  • 69
    • 0023893710 scopus 로고
    • Loss of CD45R and gain of UCHL1 reactivity is a feature of primed T cells
    • A.N. Akbar, L. Terry, A. Timms, P.C. Beverley, and G. Janossy Loss of CD45R and gain of UCHL1 reactivity is a feature of primed T cells J Immunol 140 1988 2171 2178
    • (1988) J Immunol , vol.140 , pp. 2171-2178
    • Akbar, A.N.1    Terry, L.2    Timms, A.3    Beverley, P.C.4    Janossy, G.5
  • 70
    • 0024346410 scopus 로고
    • A monoclonal antibody to murine CD45R distinguishes CD4 T cell populations that produce different cytokines
    • K. Bottomly, M. Luqman, and L. Greenbaum A monoclonal antibody to murine CD45R distinguishes CD4 T cell populations that produce different cytokines Eur J Immunol 19 1989 617 623
    • (1989) Eur J Immunol , vol.19 , pp. 617-623
    • Bottomly, K.1    Luqman, M.2    Greenbaum, L.3
  • 71
    • 0034077532 scopus 로고    scopus 로고
    • T cell memory: Heterogeneity and mechanisms
    • D.L. Farber T cell memory: heterogeneity and mechanisms Clin Immunol 95 2000 173 181
    • (2000) Clin Immunol , vol.95 , pp. 173-181
    • Farber, D.L.1
  • 73
    • 0025330503 scopus 로고
    • Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck
    • H.L. Ostergaard, and I.S. Trowbridge Coclustering CD45 with CD4 or CD8 alters the phosphorylation and kinase activity of p56lck J Exp Med 172 1990 347
    • (1990) J Exp Med , vol.172 , pp. 347
    • Ostergaard, H.L.1    Trowbridge, I.S.2
  • 74
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • J.T. Pingel, and M.L. Thomas Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation Cell 58 1989 1055 1065
    • (1989) Cell , vol.58 , pp. 1055-1065
    • Pingel, J.T.1    Thomas, M.L.2
  • 75
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • G.A. Koretzky, J. Picus, M.L. Thomas, and A. Weiss Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway Nature 346 1990 66 68
    • (1990) Nature , vol.346 , pp. 66-68
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 77
    • 0030070341 scopus 로고    scopus 로고
    • The extracellular domain of CD45 controls association with the CD4-T cell receptor complex and the response to antigen-specific stimulation
    • D. Leitenberg, T.J. Novak, D. Farber, B.R. Smith, and K. Bottomly The extracellular domain of CD45 controls association with the CD4-T cell receptor complex and the response to antigen-specific stimulation J Exp Med 183 1996 249 259
    • (1996) J Exp Med , vol.183 , pp. 249-259
    • Leitenberg, D.1    Novak, T.J.2    Farber, D.3    Smith, B.R.4    Bottomly, K.5
  • 78
    • 0028426282 scopus 로고
    • Isoforms of the transmembrane tyrosine phosphatase CD45 differentially affect T cell recognition
    • T.J. Novak, D. Farber, D. Leitenberg, S. Hong, P. Johnson, and K. Bottomly Isoforms of the transmembrane tyrosine phosphatase CD45 differentially affect T cell recognition Immunity 1 1994 109 119
    • (1994) Immunity , vol.1 , pp. 109-119
    • Novak, T.J.1    Farber, D.2    Leitenberg, D.3    Hong, S.4    Johnson, P.5    Bottomly, K.6
  • 79
    • 0033151580 scopus 로고    scopus 로고
    • Biochemical association of CD45 with the T cell receptor complex: Regulation by CD45 isoform and during T cell activation
    • D. Leitenberg, Y. Boutin, D.D. Lu, and K. Bottomly Biochemical association of CD45 with the T cell receptor complex: regulation by CD45 isoform and during T cell activation Immunity 10 1999 701 711
    • (1999) Immunity , vol.10 , pp. 701-711
    • Leitenberg, D.1    Boutin, Y.2    Lu, D.D.3    Bottomly, K.4
  • 80
    • 0034459505 scopus 로고    scopus 로고
    • Combinatorial effect of T-cell receptor ligation and CD45 isoform expression on the signaling contribution of the small GTPases Ras and Rap1
    • J. Czyzyk, D. Leitenberg, T. Taylor, and K. Bottomly Combinatorial effect of T-cell receptor ligation and CD45 isoform expression on the signaling contribution of the small GTPases Ras and Rap1 Mol Cell Biol 20 2000 8740 8747
    • (2000) Mol Cell Biol , vol.20 , pp. 8740-8747
    • Czyzyk, J.1    Leitenberg, D.2    Taylor, T.3    Bottomly, K.4
  • 81
    • 0037304929 scopus 로고    scopus 로고
    • Role of protein tyrosine phosphatases in T cell activation
    • T. Mustelin, S. Rahmouni, N. Bottini, and A. Alonso Role of protein tyrosine phosphatases in T cell activation Immunol Rev 191 2003 139 147
    • (2003) Immunol Rev , vol.191 , pp. 139-147
    • Mustelin, T.1    Rahmouni, S.2    Bottini, N.3    Alonso, A.4
  • 82
    • 0030022278 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells
    • M. Kon-Kozlowski, G. Pani, T. Pawson, and K.A. Siminovitch The tyrosine phosphatase PTP1C associates with Vav, Grb2, and mSos1 in hematopoietic cells J Biol Chem 271 1996 3856 3862
    • (1996) J Biol Chem , vol.271 , pp. 3856-3862
    • Kon-Kozlowski, M.1    Pani, G.2    Pawson, T.3    Siminovitch, K.A.4
  • 83
    • 0032767536 scopus 로고    scopus 로고
    • Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1
    • J. Brockdorff, S. Williams, C. Couture, and T. Mustelin Dephosphorylation of ZAP-70 and inhibition of T cell activation by activated SHP1 Eur J Immunol 29 1999 2539 2550
    • (1999) Eur J Immunol , vol.29 , pp. 2539-2550
    • Brockdorff, J.1    Williams, S.2    Couture, C.3    Mustelin, T.4
  • 84
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • S. Rogers, R. Wells, and M. Rechsteiner Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis Science 234 1986 364 368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 85
    • 0942279640 scopus 로고    scopus 로고
    • PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells
    • K. Hasegawa, F. Martin, G. Huang, D. Tumas, L. Diehl, and A.C. Chan PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells Science 303 2004 685 689
    • (2004) Science , vol.303 , pp. 685-689
    • Hasegawa, K.1    Martin, F.2    Huang, G.3    Tumas, D.4    Diehl, L.5    Chan, A.C.6
  • 86
    • 0036837657 scopus 로고    scopus 로고
    • Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein
    • N. Carpino, R. Kobayashi, and H. Zang Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein Mol Cell Biol 22 2002 7491 7500
    • (2002) Mol Cell Biol , vol.22 , pp. 7491-7500
    • Carpino, N.1    Kobayashi, R.2    Zang, H.3
  • 87
    • 1642456674 scopus 로고    scopus 로고
    • Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2
    • N. Carpino, S. Turner, and D. Mekala Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2 Immunity 20 2004 37 46
    • (2004) Immunity , vol.20 , pp. 37-46
    • Carpino, N.1    Turner, S.2    Mekala, D.3
  • 88
    • 0034642499 scopus 로고    scopus 로고
    • Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b
    • K. Bachmaier, C. Krawczyk, and I. Kozieradzki Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b Nature 403 2000 211 216
    • (2000) Nature , vol.403 , pp. 211-216
    • Bachmaier, K.1    Krawczyk, C.2    Kozieradzki, I.3
  • 89
    • 0034642534 scopus 로고    scopus 로고
    • Cbl-b regulates the CD28 dependence of T-cell activation
    • Y.J. Chiang, H.K. Kole, and K. Brown Cbl-b regulates the CD28 dependence of T-cell activation Nature 403 2000 216 220
    • (2000) Nature , vol.403 , pp. 216-220
    • Chiang, Y.J.1    Kole, H.K.2    Brown, K.3
  • 90
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • R. Xavier, T. Brennan, Q. Li, C. McCormack, and B. Seed Membrane compartmentation is required for efficient T cell activation Immunity 8 1998 723 732
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 91
    • 0032727709 scopus 로고    scopus 로고
    • Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor
    • P.W. Janes, S.C. Ley, and A.I. Magee Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor J Cell Biol 147 1999 447 461
    • (1999) J Cell Biol , vol.147 , pp. 447-461
    • Janes, P.W.1    Ley, S.C.2    Magee, A.I.3
  • 92
    • 0035039037 scopus 로고    scopus 로고
    • Co-stimulation and counter-stimulation: Lipid raft clustering controls TCR signaling and functional outcomes
    • M.C. Miceli, M. Moran, C.D. Chung, V.P. Patel, T. Low, and W. Zinnanti Co-stimulation and counter-stimulation: lipid raft clustering controls TCR signaling and functional outcomes Semin Immunol 13 2001 115 118
    • (2001) Semin Immunol , vol.13 , pp. 115-118
    • Miceli, M.C.1    Moran, M.2    Chung, C.D.3    Patel, V.P.4    Low, T.5    Zinnanti, W.6
  • 93
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • W. Zhang, R.P. Trible, and L.E. Samelson LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation Immunity 9 1998 239 246
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 94
    • 0034596827 scopus 로고    scopus 로고
    • Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling
    • N.J. Boerth, J.J. Sadler, D.E. Bauer, J.L. Clements, S.M. Gheith, and G.A. Koretzky Recruitment of SLP-76 to the membrane and glycolipid-enriched membrane microdomains replaces the requirement for linker for activation of T cells in T cell receptor signaling J Exp Med 192 2000 1047 1058
    • (2000) J Exp Med , vol.192 , pp. 1047-1058
    • Boerth, N.J.1    Sadler, J.J.2    Bauer, D.E.3    Clements, J.L.4    Gheith, S.M.5    Koretzky, G.A.6
  • 95
    • 0030453582 scopus 로고    scopus 로고
    • Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains
    • W. Rodgers, and J.K. Rose Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains J Cell Biol 135 1996 1515 1523
    • (1996) J Cell Biol , vol.135 , pp. 1515-1523
    • Rodgers, W.1    Rose, J.K.2
  • 96
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • P.S. Kabouridis, J. Janzen, A.L. Magee, and S.C. Ley Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes Eur J Immunol 30 2000 954 963
    • (2000) Eur J Immunol , vol.30 , pp. 954-963
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 99
    • 0037069384 scopus 로고    scopus 로고
    • Human CD8+ T cells do not require the polarization of lipid rafts for activation and proliferation
    • B. Kovacs, M.V. Maus, and J.L. Riley Human CD8+ T cells do not require the polarization of lipid rafts for activation and proliferation Proc Natl Acad Sci USA 99 2002 15006 15011
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15006-15011
    • Kovacs, B.1    Maus, M.V.2    Riley, J.L.3
  • 100
    • 0035654908 scopus 로고    scopus 로고
    • Distinct patterns of membrane microdomain partitioning in Th1 and th2 cells
    • F. Balamuth, D. Leitenberg, J. Unternaehrer, I. Mellman, and K. Bottomly Distinct patterns of membrane microdomain partitioning in Th1 and th2 cells Immunity 15 2001 729 738
    • (2001) Immunity , vol.15 , pp. 729-738
    • Balamuth, F.1    Leitenberg, D.2    Unternaehrer, J.3    Mellman, I.4    Bottomly, K.5
  • 101
    • 1642268642 scopus 로고    scopus 로고
    • Role of GM3-enriched microdomains in signal transduction regulation in T lymphocytes
    • M. Sorice, A. Longo, T. Garofalo, V. Mattei, R. Misasi, and A. Pavan Role of GM3-enriched microdomains in signal transduction regulation in T lymphocytes Glycoconj J 20 2004 63 70
    • (2004) Glycoconj J , vol.20 , pp. 63-70
    • Sorice, M.1    Longo, A.2    Garofalo, T.3    Mattei, V.4    Misasi, R.5    Pavan, A.6
  • 102
    • 0037047336 scopus 로고    scopus 로고
    • LAT displacement from lipid rafts as a molecular mechanism for the inhibition of T cell signaling by polyunsaturated fatty acids
    • M. Zeyda, G. Staffler, V. Horejsi, W. Waldhausl, and T.M. Stulnig LAT displacement from lipid rafts as a molecular mechanism for the inhibition of T cell signaling by polyunsaturated fatty acids J Biol Chem 277 2002 28418 28423
    • (2002) J Biol Chem , vol.277 , pp. 28418-28423
    • Zeyda, M.1    Staffler, G.2    Horejsi, V.3    Waldhausl, W.4    Stulnig, T.M.5
  • 103
    • 0025746722 scopus 로고
    • Prions and prion proteins
    • N. Stahl, and S.B. Prusiner Prions and prion proteins FASEB J 5 1991 2799 2807
    • (1991) FASEB J , vol.5 , pp. 2799-2807
    • Stahl, N.1    Prusiner, S.B.2
  • 104
    • 0025212147 scopus 로고
    • Cellular isoform of the scrapie agent protein participates in lymphocyte activation
    • N.R. Cashman, R. Loertscher, and J. Nalbantoglu Cellular isoform of the scrapie agent protein participates in lymphocyte activation Cell 61 1990 185 192
    • (1990) Cell , vol.61 , pp. 185-192
    • Cashman, N.R.1    Loertscher, R.2    Nalbantoglu, J.3
  • 105
    • 0035834915 scopus 로고    scopus 로고
    • The expression and potential function of cellular prion protein in human lymphocytes
    • R. Li, D. Liu, and G. Zanusso The expression and potential function of cellular prion protein in human lymphocytes Cell Immunol 207 2001 49 58
    • (2001) Cell Immunol , vol.207 , pp. 49-58
    • Li, R.1    Liu, D.2    Zanusso, G.3
  • 106
    • 1342329324 scopus 로고    scopus 로고
    • Prion protein is a component of the multimolecular signaling complex involved in T cell activation
    • V. Mattei, T. Garofalo, and R. Misasi Prion protein is a component of the multimolecular signaling complex involved in T cell activation FEBS Lett 560 2004 14 18
    • (2004) FEBS Lett , vol.560 , pp. 14-18
    • Mattei, V.1    Garofalo, T.2    Misasi, R.3
  • 107
    • 0030850688 scopus 로고    scopus 로고
    • T-lymphocyte activation and the cellular form of the prion protein
    • N.A. Mabbott, K.L. Brown, J. Manson, and M.E. Bruce T-lymphocyte activation and the cellular form of the prion protein Immunology 92 1997 161 165
    • (1997) Immunology , vol.92 , pp. 161-165
    • Mabbott, N.A.1    Brown, K.L.2    Manson, J.3    Bruce, M.E.4
  • 108
    • 0036695461 scopus 로고    scopus 로고
    • Association of cellular prion protein with gangliosides in plasma membrane microdomains of neural and lymphocytic cells
    • V. Mattei, T. Garofalo, and R. Misasi Association of cellular prion protein with gangliosides in plasma membrane microdomains of neural and lymphocytic cells Neurochem Res 27 2002 743 749
    • (2002) Neurochem Res , vol.27 , pp. 743-749
    • Mattei, V.1    Garofalo, T.2    Misasi, R.3
  • 109
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • K. Si, S. Lindquist, and E.R. Kandel A neuronal isoform of the aplysia CPEB has prion-like properties Cell 115 2003 879 891
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 110
    • 0242322243 scopus 로고    scopus 로고
    • CD28 costimulation: A source of Vav-1 for TCR signaling with the help of SLP-76?
    • F. Michel, and O. Acuto CD28 costimulation: a source of Vav-1 for TCR signaling with the help of SLP-76? Sci STKE 2002 2002 PE35
    • (2002) Sci STKE , vol.2002
    • Michel, F.1    Acuto, O.2
  • 111
    • 0033538574 scopus 로고    scopus 로고
    • The immunological synapse: A molecular machine controlling T cell activation
    • A. Grakoui, S.K. Bromley, and C. Sumen The immunological synapse: a molecular machine controlling T cell activation Science 285 1999 221 227
    • (1999) Science , vol.285 , pp. 221-227
    • Grakoui, A.1    Bromley, S.K.2    Sumen, C.3
  • 112
    • 0346244099 scopus 로고    scopus 로고
    • T-cell-antigen recognition and the immunological synpase
    • J.B. Huppa, and M.M. Davis T-cell-antigen recognition and the immunological synpase Nat Rev Immunol 3 2003 973 983
    • (2003) Nat Rev Immunol , vol.3 , pp. 973-983
    • Huppa, J.B.1    Davis, M.M.2
  • 113
    • 0034934906 scopus 로고    scopus 로고
    • Role of adhesion molecules in activation signaling in T lymphocytes
    • M.L. Dustin Role of adhesion molecules in activation signaling in T lymphocytes J Clin Immunol 21 2001 258 263
    • (2001) J Clin Immunol , vol.21 , pp. 258-263
    • Dustin, M.L.1
  • 114
    • 0037244777 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in T lymphocyte activation and migration
    • Y. Samstag, S.M. Eibert, M. Klemke, and G.H. Wabnitz Actin cytoskeletal dynamics in T lymphocyte activation and migration J Leukoc Biol 73 2003 30 48
    • (2003) J Leukoc Biol , vol.73 , pp. 30-48
    • Samstag, Y.1    Eibert, S.M.2    Klemke, M.3    Wabnitz, G.H.4
  • 115
  • 117
    • 0242497659 scopus 로고    scopus 로고
    • The immunological synapse balances T cell receptor signaling and degradation
    • K.H. Lee, A.R. Dinner, and C. Tu The immunological synapse balances T cell receptor signaling and degradation Science 302 2003 1218 1222
    • (2003) Science , vol.302 , pp. 1218-1222
    • Lee, K.H.1    Dinner, A.R.2    Tu, C.3
  • 118
    • 0036794399 scopus 로고    scopus 로고
    • Staging and resetting T cell activation in SMACs
    • B.A. Freiberg, H. Kupfer, and W. Maslanik Staging and resetting T cell activation in SMACs Nat Immunol 3 2002 911 917
    • (2002) Nat Immunol , vol.3 , pp. 911-917
    • Freiberg, B.A.1    Kupfer, H.2    Maslanik, W.3
  • 119
    • 0036906497 scopus 로고    scopus 로고
    • Dynamics of p56lck translocation to the T cell immunological synapse following agonist and antagonist stimulation
    • L.I. Ehrlich, P.J. Ebert, M.F. Krummel, A. Weiss, and M.M. Davis Dynamics of p56lck translocation to the T cell immunological synapse following agonist and antagonist stimulation Immunity 17 2002 809 822
    • (2002) Immunity , vol.17 , pp. 809-822
    • Ehrlich, L.I.1    Ebert, P.J.2    Krummel, M.F.3    Weiss, A.4    Davis, M.M.5
  • 120
    • 0042847271 scopus 로고    scopus 로고
    • Cutting edge: T lymphocyte activation by repeated immunological synapse formation and intermittent signaling
    • M. Faroudi, R. Zaru, P. Paulet, S. Muller, and S. Valitutti Cutting edge: T lymphocyte activation by repeated immunological synapse formation and intermittent signaling J Immunol 171 2003 1128 1132
    • (2003) J Immunol , vol.171 , pp. 1128-1132
    • Faroudi, M.1    Zaru, R.2    Paulet, P.3    Muller, S.4    Valitutti, S.5
  • 121
    • 0023934515 scopus 로고
    • Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-γ production
    • M.E. Sanders, M.W. Makgoba, and S.O. Sharrow Human memory T lymphocytes express increased levels of three cell adhesion molecules (LFA-3, CD2, and LFA-1) and three other molecules (UCHL1, CDw29, and Pgp-1) and have enhanced IFN-γ production J Immunol 140 1988 1401 1407
    • (1988) J Immunol , vol.140 , pp. 1401-1407
    • Sanders, M.E.1    Makgoba, M.W.2    Sharrow, S.O.3
  • 122
    • 0027943758 scopus 로고
    • Regulation of adhesion molecule expression by CD8 T cells in vivo II. Expression of l-selectin (CD62L) by memory cytolytic T cells responding to minor histocompatibility antigens
    • J.L. Mobley, S.M. Rigby, and M.O. Dailey Regulation of adhesion molecule expression by CD8 T cells in vivo II. Expression of l-selectin (CD62L) by memory cytolytic T cells responding to minor histocompatibility antigens J Immunol 153 1994 5443 5452
    • (1994) J Immunol , vol.153 , pp. 5443-5452
    • Mobley, J.L.1    Rigby, S.M.2    Dailey, M.O.3
  • 123
    • 0035877112 scopus 로고    scopus 로고
    • Augmentation in expression of activation-induced genes differentiates memory from naive CD4+ T cells and is a molecular mechanism for enhanced cellular response of memory CD4+ T cells
    • K. Liu, Y. Li, and V. Prabhu Augmentation in expression of activation-induced genes differentiates memory from naive CD4+ T cells and is a molecular mechanism for enhanced cellular response of memory CD4+ T cells J Immunol 166 2001 7335 7344
    • (2001) J Immunol , vol.166 , pp. 7335-7344
    • Liu, K.1    Li, Y.2    Prabhu, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.