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Volumn 16, Issue 6, 2004, Pages 421-427

Inhibitory adaptors in lymphocytes

Author keywords

Antigen receptor; Degradation; Immunoreceptor tyrosine based inhibition motif; Lipid raft; Ubiquitination

Indexed keywords

CBL PROTEIN; CD2 ASSOCIATED PROTEIN; PROTEIN; PROTEIN DOK1; PROTEIN DOK2; PROTEIN DOK3; PROTEIN SLAP; PROTEIN SLAP 2; UNCLASSIFIED DRUG;

EID: 8444230806     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smim.2004.08.021     Document Type: Article
Times cited : (7)

References (57)
  • 1
    • 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
  • 2
    • 0037564427 scopus 로고    scopus 로고
    • Negative feedback of T cell activation through inhibitory adapters and costimulatory receptors
    • T. Saito, and S. Yamasaki Negative feedback of T cell activation through inhibitory adapters and costimulatory receptors Immunol. Rev. 192 2003 143 160
    • (2003) Immunol. Rev. , vol.192 , pp. 143-160
    • Saito, T.1    Yamasaki, S.2
  • 4
    • 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
  • 5
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • M. Kawabuchi, Y. Satomi, T. Takao, Y. Shimonishi, S. Nada, and K. Nagai Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases Nature 404 2000 999 1003
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1    Satomi, Y.2    Takao, T.3    Shimonishi, Y.4    Nada, S.5    Nagai, K.6
  • 6
    • 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
    • T. Brdicka, D. Pavlistova, A. Leo, E. Bruyns, V. Korinek, and P. Angelisova 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. 191 2000 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
  • 7
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • D. Davidson, M. Bakinowski, M.L. Thomas, V. Horejsi, and A. Veillette Phosphorylation-dependent regulation of T cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor Mol. Cell Biol. 23 2003 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
  • 8
    • 0035955452 scopus 로고    scopus 로고
    • Interaction between two adapter proteins. PAG and EBP50: A possible link between membrane rafts and actin cytoskeleton
    • N. Brdickova, T. Brdicka, L. Andera, J. Spicka, P. Angelisova, and S.L. Milgram Interaction between two adapter proteins. PAG and EBP50: a possible link between membrane rafts and actin cytoskeleton FEBS Lett. 507 2001 133 136
    • (2001) FEBS Lett. , vol.507 , pp. 133-136
    • Brdickova, N.1    Brdicka, T.2    Andera, L.3    Spicka, J.4    Angelisova, P.5    Milgram, S.L.6
  • 9
    • 0037080345 scopus 로고    scopus 로고
    • Cutting edge: Negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly
    • K. Itoh, M. Sakakibara, S. Yamasaki, A. Takeuchi, H. Arase, and M. Miyazaki Cutting edge: negative regulation of immune synapse formation by anchoring lipid raft to cytoskeleton through Cbp-EBP50-ERM assembly J. Immunol. 168 2002 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
  • 10
    • 0033583478 scopus 로고    scopus 로고
    • SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation
    • A. Marie-Cardine, H. Kirchgessner, E. Bruyns, A. Shevchenko, M. Mann, and F. Autschbach SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T cell activation J. Exp. Med. 189 1999 1181 1194
    • (1999) J. Exp. Med. , vol.189 , pp. 1181-1194
    • Marie-Cardine, A.1    Kirchgessner, H.2    Bruyns, E.3    Shevchenko, A.4    Mann, M.5    Autschbach, F.6
  • 11
    • 0034974789 scopus 로고    scopus 로고
    • Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)
    • K.I. Pfrepper, A. Marie-Cardine, L. Simeoni, Y. Kuramitsu, A. Leo, and J. Spicka Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein) Eur. J. Immunol. 31 2001 1825 1836
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1825-1836
    • Pfrepper, K.I.1    Marie-Cardine, A.2    Simeoni, L.3    Kuramitsu, Y.4    Leo, A.5    Spicka, J.6
  • 12
    • 0037195902 scopus 로고    scopus 로고
    • Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling
    • M. Zhu, E. Janssen, K. Leung, and W. Zhang Molecular cloning of a novel gene encoding a membrane-associated adaptor protein (LAX) in lymphocyte signaling J. Biol. Chem. 277 2002 46151 46158
    • (2002) J. Biol. Chem. , vol.277 , pp. 46151-46158
    • Zhu, M.1    Janssen, E.2    Leung, K.3    Zhang, W.4
  • 14
    • 0037077094 scopus 로고    scopus 로고
    • Induction of T helper type 2 immunity by a point mutation in the LAT adaptor
    • E. Aguado, S. Richelme, S. Nunez-Cruz, A. Miazek, A.M. Mura, and M. Richelme Induction of T helper type 2 immunity by a point mutation in the LAT adaptor Science 296 2002 2036 2040
    • (2002) Science , vol.296 , pp. 2036-2040
    • Aguado, E.1    Richelme, S.2    Nunez-Cruz, S.3    Miazek, A.4    Mura, A.M.5    Richelme, M.6
  • 15
    • 0037076975 scopus 로고    scopus 로고
    • A LAT mutation that inhibits T cell development yet induces lymphoproliferation
    • C.L. Sommers, C.S. Park, J. Lee, C. Feng, C.L. Fuller, and A. Grinberg A LAT mutation that inhibits T cell development yet induces lymphoproliferation Science 296 2002 2040 2043
    • (2002) Science , vol.296 , pp. 2040-2043
    • Sommers, C.L.1    Park, C.S.2    Lee, J.3    Feng, C.4    Fuller, C.L.5    Grinberg, A.6
  • 16
    • 0034614887 scopus 로고    scopus 로고
    • Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling
    • T. Sosinowski, A. Pandey, V.M. Dixit, and A. Weiss Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling J. Exp. Med. 191 2000 463 474
    • (2000) J. Exp. Med. , vol.191 , pp. 463-474
    • Sosinowski, T.1    Pandey, A.2    Dixit, V.M.3    Weiss, A.4
  • 17
    • 0033578408 scopus 로고    scopus 로고
    • SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling
    • J. Tang, S. Sawasdikosol, J.H. Chang, and S.J. Burakoff SLAP, a dimeric adapter protein, plays a functional role in T cell receptor signaling Proc. Natl. Acad. Sci. USA 96 1999 9775 9780
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9775-9780
    • Tang, J.1    Sawasdikosol, S.2    Chang, J.H.3    Burakoff, S.J.4
  • 19
    • 0037166292 scopus 로고    scopus 로고
    • A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling
    • A. Pandey, N. Ibarrola, I. Kratchmarova, M.M. Fernandez, S.N. Constantinescu, and O. Ohara A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling J. Biol. Chem. 277 2002 19131 19138
    • (2002) J. Biol. Chem. , vol.277 , pp. 19131-19138
    • Pandey, A.1    Ibarrola, N.2    Kratchmarova, I.3    Fernandez, M.M.4    Constantinescu, S.N.5    Ohara, O.6
  • 20
    • 0035173040 scopus 로고    scopus 로고
    • Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel inhibitor of antigen receptor signaling
    • S.J. Holland, X.C. Liao, M.K. Mendenhall, X. Zhou, J. Pardo, and P. Chu Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel inhibitor of antigen receptor signaling J. Exp. Med. 194 2001 1263 1276
    • (2001) J. Exp. Med. , vol.194 , pp. 1263-1276
    • Holland, S.J.1    Liao, X.C.2    Mendenhall, M.K.3    Zhou, X.4    Pardo, J.5    Chu, P.6
  • 21
    • 0036258357 scopus 로고    scopus 로고
    • Functional cooperation between c-Cbl and Src-like adaptor protein 2 in the negative regulation of T cell receptor signaling
    • M.P. Loreto, D.M. Berry, and C.J. McGlade Functional cooperation between c-Cbl and Src-like adaptor protein 2 in the negative regulation of T cell receptor signaling Mol. Cell Biol. 22 2002 4241 4255
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4241-4255
    • Loreto, M.P.1    Berry, D.M.2    McGlade, C.J.3
  • 22
    • 0032548933 scopus 로고    scopus 로고
    • Molecular cloning of a T cell-specific adapter protein (TSAd) containing an Src homology (SH) 2 domain and putative SH3 and phosphotyrosine binding sites
    • A. Spurkland, J.E. Brinchmann, G. Markussen, F. Pedeutour, E. Munthe, and T. Lea Molecular cloning of a T cell-specific adapter protein (TSAd) containing an Src homology (SH) 2 domain and putative SH3 and phosphotyrosine binding sites J. Biol. Chem. 273 1998 4539 4546
    • (1998) J. Biol. Chem. , vol.273 , pp. 4539-4546
    • Spurkland, A.1    Brinchmann, J.E.2    Markussen, G.3    Pedeutour, F.4    Munthe, E.5    Lea, T.6
  • 24
    • 0003477424 scopus 로고    scopus 로고
    • Lad, an adapter protein interacting with the SH2 domain of p56lck, is required for T cell activation
    • Y.B. Choi, C.K. Kim, and Y. Yun Lad, an adapter protein interacting with the SH2 domain of p56lck, is required for T cell activation J. Immunol. 163 1999 5242 5249
    • (1999) J. Immunol. , vol.163 , pp. 5242-5249
    • Choi, Y.B.1    Kim, C.K.2    Yun, Y.3
  • 25
    • 0042886906 scopus 로고    scopus 로고
    • Impaired T cell death and lupus-like autoimmunity in T cell-specific adapter protein-deficient mice
    • J. Drappa, L.A. Kamen, E. Chan, M. Georgiev, D. Ashany, and F. Marti Impaired T cell death and lupus-like autoimmunity in T cell-specific adapter protein-deficient mice J. Exp. Med. 198 2003 809 821
    • (2003) J. Exp. Med. , vol.198 , pp. 809-821
    • Drappa, J.1    Kamen, L.A.2    Chan, E.3    Georgiev, M.4    Ashany, D.5    Marti, F.6
  • 26
    • 18044401969 scopus 로고    scopus 로고
    • The T cell regulator gene SH2D2A contributes to the genetic susceptibility of multiple sclerosis
    • K.Z. Dai, H.F. Harbo, E.G. Celius, A. Oturai, P.S. Sorensen, and L.P. Ryder The T cell regulator gene SH2D2A contributes to the genetic susceptibility of multiple sclerosis Genes Immun. 2 2001 263 268
    • (2001) Genes Immun. , vol.2 , pp. 263-268
    • Dai, K.Z.1    Harbo, H.F.2    Celius, E.G.3    Oturai, A.4    Sorensen, P.S.5    Ryder, L.P.6
  • 27
  • 28
    • 0037960106 scopus 로고    scopus 로고
    • SAP: A molecular switch regulating the immune response through a unique signaling mechanism
    • A. Veillette SAP: a molecular switch regulating the immune response through a unique signaling mechanism Eur. J. Immunol. 33 2003 1141 1144
    • (2003) Eur. J. Immunol. , vol.33 , pp. 1141-1144
    • Veillette, A.1
  • 29
    • 0032438114 scopus 로고    scopus 로고
    • Altered thymic positive selection and intracellular signals in Cbl-deficient mice
    • M. Naramura, H.K. Kole, R.J. Hu, and H. Gu Altered thymic positive selection and intracellular signals in Cbl-deficient mice Proc. Natl. Acad. Sci. USA 95 1998 15547 15552
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15547-15552
    • Naramura, M.1    Kole, H.K.2    Hu, R.J.3    Gu, H.4
  • 30
    • 0035854665 scopus 로고    scopus 로고
    • Cbl promotes ubiquitination of the T cell receptor zeta through an adaptor function of Zap-70
    • H.Y. Wang, Y. Altman, D. Fang, C. Elly, Y. Dai, and Y. Shao Cbl promotes ubiquitination of the T cell receptor zeta through an adaptor function of Zap-70 J. Biol. Chem. 276 2001 26004 26011
    • (2001) J. Biol. Chem. , vol.276 , pp. 26004-26011
    • Wang, H.Y.1    Altman, Y.2    Fang, D.3    Elly, C.4    Dai, Y.5    Shao, Y.6
  • 32
    • 0035555195 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells
    • D. Fang, and Y.C. Liu Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells Nat. Immunol. 2 2001 870 875
    • (2001) Nat. Immunol. , vol.2 , pp. 870-875
    • Fang, D.1    Liu, Y.C.2
  • 33
    • 0036197639 scopus 로고    scopus 로고
    • Dysregulation of T lymphocyte function in itchy mice: A role for Itch in TH2 differentiation
    • D. Fang, C. Elly, B. Gao, N. Fang, Y. Altman, and C. Joazeiro Dysregulation of T lymphocyte function in itchy mice: a role for Itch in TH2 differentiation Nat. Immunol. 3 2002 281 287
    • (2002) Nat. Immunol. , vol.3 , pp. 281-287
    • Fang, D.1    Elly, C.2    Gao, B.3    Fang, N.4    Altman, Y.5    Joazeiro, C.6
  • 34
    • 12144290293 scopus 로고    scopus 로고
    • Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins
    • V. Heissmeyer, F. Macian, S.H. Im, R. Varma, S. Feske, and K. Venuprasad Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins Nat. Immunol. 5 2004 255 265
    • (2004) Nat. Immunol. , vol.5 , pp. 255-265
    • Heissmeyer, V.1    MacIan, F.2    Im, S.H.3    Varma, R.4    Feske, S.5    Venuprasad, K.6
  • 35
    • 0242497659 scopus 로고    scopus 로고
    • The immunological synapse balances T cell receptor signaling and degradation
    • K.H. Lee, A.R. Dinner, C. Tu, G. Campi, S. Raychaudhuri, and R. Varma 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    Campi, G.4    Raychaudhuri, S.5    Varma, R.6
  • 36
    • 0032238298 scopus 로고    scopus 로고
    • Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation
    • H. Gu, J.C. Pratt, S.J. Burakoff, and B.G. Neel Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation Mol. Cell. 2 1998 729 740
    • (1998) Mol. Cell. , vol.2 , pp. 729-740
    • Gu, H.1    Pratt, J.C.2    Burakoff, S.J.3    Neel, B.G.4
  • 37
    • 0033559311 scopus 로고    scopus 로고
    • Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T and B cell antigen receptors
    • K. Nishida, Y. Yoshida, M. Itoh, T. Fukada, T. Ohtani, and T. Shirogane Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T and B cell antigen receptors Blood 93 1999 1809 1816
    • (1999) Blood , vol.93 , pp. 1809-1816
    • Nishida, K.1    Yoshida, Y.2    Itoh, M.3    Fukada, T.4    Ohtani, T.5    Shirogane, T.6
  • 38
    • 0034667783 scopus 로고    scopus 로고
    • Cutting edge: Gab2 mediates an inhibitory phosphatidylinositol 3′-kinase pathway in T cell antigen receptor signaling
    • J.C. Pratt, V.E. Igras, H. Maeda, S. Baksh, E.W. Gelfand, and S.J. Burakoff Cutting edge: gab2 mediates an inhibitory phosphatidylinositol 3′-kinase pathway in T cell antigen receptor signaling J. Immunol. 165 2000 4158 4163
    • (2000) J. Immunol. , vol.165 , pp. 4158-4163
    • Pratt, J.C.1    Igras, V.E.2    Maeda, H.3    Baksh, S.4    Gelfand, E.W.5    Burakoff, S.J.6
  • 39
    • 0035976967 scopus 로고    scopus 로고
    • Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules
    • S. Yamasaki, K. Nishida, M. Hibi, M. Sakuma, R. Shiina, and A. Takeuchi Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules J. Biol. Chem. 276 2001 45175 45183
    • (2001) J. Biol. Chem. , vol.276 , pp. 45175-45183
    • Yamasaki, S.1    Nishida, K.2    Hibi, M.3    Sakuma, M.4    Shiina, R.5    Takeuchi, A.6
  • 40
    • 0037379218 scopus 로고    scopus 로고
    • Gads/Grb2-mediated association with LAT is critical for the inhibitory function of Gab2 in T cells
    • S. Yamasaki, K. Nishida, M. Sakuma, D. Berry, C.J. McGlade, and T. Hirano Gads/Grb2-mediated association with LAT is critical for the inhibitory function of Gab2 in T cells Mol. Cell Biol. 23 2003 2515 2529
    • (2003) Mol. Cell Biol. , vol.23 , pp. 2515-2529
    • Yamasaki, S.1    Nishida, K.2    Sakuma, M.3    Berry, D.4    McGlade, C.J.5    Hirano, T.6
  • 41
    • 0035021881 scopus 로고    scopus 로고
    • Gab2 is phosphorylated on tyrosine upon interleukin-2/interleukin-15 stimulation in mycosis-fungoides-derived tumor T cells and associates inducibly with SHP-2 and Stat5a
    • J.L. Brockdorff, H. Gu, T. Mustelin, K. Kaltoft, C. Geisler, and C. Ropke Gab2 is phosphorylated on tyrosine upon interleukin-2/interleukin-15 stimulation in mycosis-fungoides-derived tumor T cells and associates inducibly with SHP-2 and Stat5a Exp. Clin. Immunogenet. 18 2001 86 95
    • (2001) Exp. Clin. Immunogenet. , vol.18 , pp. 86-95
    • Brockdorff, J.L.1    Gu, H.2    Mustelin, T.3    Kaltoft, K.4    Geisler, C.5    Ropke, C.6
  • 42
    • 0031444245 scopus 로고    scopus 로고
    • Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein
    • Y. Yamanashi, and D. Baltimore Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein Dok. Cell 88 1997 205 211
    • (1997) Dok. Cell , vol.88 , pp. 205-211
    • Yamanashi, Y.1    Baltimore, D.2
  • 43
    • 0033979324 scopus 로고    scopus 로고
    • Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling
    • Y. Yamanashi, T. Tamura, T. Kanamori, H. Yamane, H. Nariuchi, and T. Yamamoto Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling Genes Dev. 14 2000 11 16
    • (2000) Genes Dev. , vol.14 , pp. 11-16
    • Yamanashi, Y.1    Tamura, T.2    Kanamori, T.3    Yamane, H.4    Nariuchi, H.5    Yamamoto, T.6
  • 44
    • 0032126362 scopus 로고    scopus 로고
    • FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation
    • K. Nelms, A.L. Snow, J. Hu-Li, and W.E. Paul FRIP, a hematopoietic cell-specific rasGAP-interacting protein phosphorylated in response to cytokine stimulation Immunity 9 1998 13 24
    • (1998) Immunity , vol.9 , pp. 13-24
    • Nelms, K.1    Snow, A.L.2    Hu-Li, J.3    Paul, W.E.4
  • 45
    • 0037043333 scopus 로고    scopus 로고
    • Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites
    • R. Gugasyan, C. Quilici I, D. Grail, A.M. Verhagen, and A. Roberts Dok-related protein negatively regulates T cell development via its RasGTPase-activating protein and Nck docking sites J. Cell Biol. 158 2002 115 125
    • (2002) J. Cell Biol. , vol.158 , pp. 115-125
    • Gugasyan, R.1    Quilici, C.I.2    Grail, D.3    Verhagen, A.M.4    Roberts, A.5
  • 46
    • 0033509095 scopus 로고    scopus 로고
    • Characterization of a novel member of the DOK family that binds and modulates Abl signaling
    • F. Cong, B. Yuan, and S.P. Goff Characterization of a novel member of the DOK family that binds and modulates Abl signaling Mol. Cell Biol. 19 1999 8314 8325
    • (1999) Mol. Cell Biol. , vol.19 , pp. 8314-8325
    • Cong, F.1    Yuan, B.2    Goff, S.P.3
  • 47
    • 0034029126 scopus 로고    scopus 로고
    • Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling
    • S. Lemay, D. Davidson, S. Latour, and A. Veillette Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling Mol. Cell Biol. 20 2000 2743 2754
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2743-2754
    • Lemay, S.1    Davidson, D.2    Latour, S.3    Veillette, A.4
  • 48
    • 1542344343 scopus 로고    scopus 로고
    • Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3
    • J.D. Robson, D. Davidson, and A. Veillette Inhibition of the Jun N-terminal protein kinase pathway by SHIP-1, a lipid phosphatase that interacts with the adaptor molecule Dok-3 Mol. Cell Biol. 24 2004 2332 2343
    • (2004) Mol. Cell Biol. , vol.24 , pp. 2332-2343
    • Robson, J.D.1    Davidson, D.2    Veillette, A.3
  • 50
    • 0035939661 scopus 로고    scopus 로고
    • Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation
    • J. Grimm, M. Sachs, S. Britsch, S. Di Cesare, T. Schwarz-Romond, and K. Alitalo Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation J. Cell Biol. 154 2001 345 354
    • (2001) J. Cell Biol. , vol.154 , pp. 345-354
    • Grimm, J.1    Sachs, M.2    Britsch, S.3    Di Cesare, S.4    Schwarz-Romond, T.5    Alitalo, K.6
  • 51
    • 15844388521 scopus 로고    scopus 로고
    • Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway
    • G.S. Feng, Y.B. Ouyang, D.P. Hu, Z.Q. Shi, R. Gentz, and J. Ni Grap is a novel SH3-SH2-SH3 adaptor protein that couples tyrosine kinases to the Ras pathway J. Biol. Chem. 271 1996 12129 12132
    • (1996) J. Biol. Chem. , vol.271 , pp. 12129-12132
    • Feng, G.S.1    Ouyang, Y.B.2    Hu, D.P.3    Shi, Z.Q.4    Gentz, R.5    Ni, J.6
  • 52
    • 0031030988 scopus 로고    scopus 로고
    • The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T cell receptor signaling
    • T. Trub, J.D. Frantz, M. Miyazaki, H. Band, and S.E. Shoelson The role of a lymphoid-restricted, Grb2-like SH3-SH2-SH3 protein in T cell receptor signaling J. Biol. Chem. 272 1997 894 902
    • (1997) J. Biol. Chem. , vol.272 , pp. 894-902
    • Trub, T.1    Frantz, J.D.2    Miyazaki, M.3    Band, H.4    Shoelson, S.E.5
  • 53
    • 0036240556 scopus 로고    scopus 로고
    • Grap negatively regulates T cell receptor-elicited lymphocyte proliferation and interleukin-2 induction
    • R. Shen, Y.B. Ouyang, C.K. Qu, A. Alonso, L. Sperzel, and T. Mustelin Grap negatively regulates T cell receptor-elicited lymphocyte proliferation and interleukin-2 induction Mol. Cell Biol. 22 2002 3230 3236
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3230-3236
    • Shen, R.1    Ouyang, Y.B.2    Qu, C.K.3    Alonso, A.4    Sperzel, L.5    Mustelin, T.6
  • 54
    • 0029562687 scopus 로고
    • Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn
    • M. Ishino, T. Ohba, H. Sasaki, and T. Sasaki Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn Oncogene 11 1995 2331 2338
    • (1995) Oncogene , vol.11 , pp. 2331-2338
    • Ishino, M.1    Ohba, T.2    Sasaki, H.3    Sasaki, T.4
  • 55
    • 0037114181 scopus 로고    scopus 로고
    • Defective thymocyte maturation by transgenic expression of a truncated form of the T lymphocyte adapter molecule and Fyn substrate, Sin
    • L.T. Donlin, C.A. Roman, M. Adlam, A.G. Regelmann, and K. Alexandropoulos Defective thymocyte maturation by transgenic expression of a truncated form of the T lymphocyte adapter molecule and Fyn substrate, Sin J. Immunol. 169 2002 6900 6909
    • (2002) J. Immunol. , vol.169 , pp. 6900-6909
    • Donlin, L.T.1    Roman, C.A.2    Adlam, M.3    Regelmann, A.G.4    Alexandropoulos, K.5
  • 57
    • 0346121599 scopus 로고    scopus 로고
    • Suppressors of cytokine signaling and immunity
    • M. Kubo, T. Hanada, and A. Yoshimura Suppressors of cytokine signaling and immunity Nat. Immunol. 4 2003 1169 1176
    • (2003) Nat. Immunol. , vol.4 , pp. 1169-1176
    • Kubo, M.1    Hanada, T.2    Yoshimura, A.3


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