메뉴 건너뛰기




Volumn 36, Issue 7, 2006, Pages 1646-1653

You say ITAM and I say ITIM, let's call the whole thing off: The ambiguity of immunoreceptor signalling

Author keywords

Cellular activation; Immune regulation; Inhibitory receptors; Signal transduction

Indexed keywords

ADAPTOR PROTEIN; BACTERIAL PROTEIN; CD3 ANTIGEN; CD79A ANTIGEN; CD79B ANTIGEN; EZRIN; IMMUNOGLOBULIN A; KILLER CELL ACTIVATING RECEPTOR ASSOCIATED PROTEIN; MERLIN; MOESIN; PHOSPHATASE; RADIXIN; TYROSINE KINASE RECEPTOR; VIRUS PROTEIN;

EID: 33746256913     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200636195     Document Type: Short Survey
Times cited : (208)

References (50)
  • 1
    • 28544438330 scopus 로고    scopus 로고
    • Role of ITAM-containing adapter proteins and their receptors in the immune system and bone
    • Humphrey, M. B., Lanier, L. L. and Nakamura, M. C., Role of ITAM-containing adapter proteins and their receptors in the immune system and bone. Immunol. Rev. 2005. 208: 50-65.
    • (2005) Immunol. Rev. , vol.208 , pp. 50-65
    • Humphrey, M.B.1    Lanier, L.L.2    Nakamura, M.C.3
  • 2
    • 20844439274 scopus 로고    scopus 로고
    • KARAP/DAP12/TYROBP: Three names and a multiplicity of biological functions
    • Tomasello, E. and Vivier, E., KARAP/DAP12/TYROBP: three names and a multiplicity of biological functions. Eur. J. Immunol. 2005. 35: 1670-1677.
    • (2005) Eur. J. Immunol. , vol.35 , pp. 1670-1677
    • Tomasello, E.1    Vivier, E.2
  • 3
    • 0036221481 scopus 로고    scopus 로고
    • Signal transduction mediated by the T cell antigen receptor: The role of adapter proteins
    • Samelson, L. E., Signal transduction mediated by the T cell antigen receptor: the role of adapter proteins. Annu. Rev. Immunol. 2002. 20: 371-394.
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 371-394
    • Samelson, L.E.1
  • 4
    • 0034613151 scopus 로고    scopus 로고
    • Immune inhibitory receptors
    • Ravetch, J. V. and Lanier, L. L., Immune inhibitory receptors. Science 2000. 290: 84-89.
    • (2000) Science , vol.290 , pp. 84-89
    • Ravetch, J.V.1    Lanier, L.L.2
  • 8
    • 0033564274 scopus 로고    scopus 로고
    • Human immunoglobulin A receptor (FcalphaRI, CD89) function in transgenic mice requires both FcR gamma chain and CR3 (CD11b/CD18)
    • van Egmond, M., van Vuuren, A. J., Morton, H. C., van Spriel, A. B., Shen, L., Hofhuis, F. M., Saito, T. et al., Human immunoglobulin A receptor (FcalphaRI, CD89) function in transgenic mice requires both FcR gamma chain and CR3 (CD11b/CD18). Blood 1999. 93: 4387-4394.
    • (1999) Blood , vol.93 , pp. 4387-4394
    • van Egmond, M.1    van Vuuren, A.J.2    Morton, H.C.3    van Spriel, A.B.4    Shen, L.5    Hofhuis, F.M.6    Saito, T.7
  • 9
    • 19944430878 scopus 로고    scopus 로고
    • Identification of FcalphaRI as an inhibitory receptor that controls inflammation: Dual role of FcR-γ ITAM
    • Pasquier, B., Launay, P., Kanamaru, Y., Moura, I. C., Pfirsch, S., Ruffie, C., Henin, D. et al., Identification of FcalphaRI as an inhibitory receptor that controls inflammation: dual role of FcR-γ ITAM. Immunity 2005. 22: 31-42.
    • (2005) Immunity , vol.22 , pp. 31-42
    • Pasquier, B.1    Launay, P.2    Kanamaru, Y.3    Moura, I.C.4    Pfirsch, S.5    Ruffie, C.6    Henin, D.7
  • 10
    • 11144354330 scopus 로고    scopus 로고
    • Costimulatory signals mediated by the ITAM motif cooperate with RANKL for bone homeostasis
    • Koga, T., Inui, M., Inoue, K., Kim, S., Suematsu, A., Kobayashi, E., Iwata, T. et al., Costimulatory signals mediated by the ITAM motif cooperate with RANKL for bone homeostasis. Nature 2004. 428: 758-763.
    • (2004) Nature , vol.428 , pp. 758-763
    • Koga, T.1    Inui, M.2    Inoue, K.3    Kim, S.4    Suematsu, A.5    Kobayashi, E.6    Iwata, T.7
  • 11
    • 20644443886 scopus 로고    scopus 로고
    • Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12
    • Hamerman, J. A., Tchao, N. K., Lowell, C. A. and Lanier, L. L., Enhanced Toll-like receptor responses in the absence of signaling adaptor DAP12. Nat. Immunol. 2005. 6: 579-586.
    • (2005) Nat. Immunol. , vol.6 , pp. 579-586
    • Hamerman, J.A.1    Tchao, N.K.2    Lowell, C.A.3    Lanier, L.L.4
  • 12
    • 0035953547 scopus 로고    scopus 로고
    • TREM-1 amplifies inflammation and is a crucial mediator of septic shock
    • Bouchon, A., Facchetti, F., Weigand, M. A. and Colonna, M., TREM-1 amplifies inflammation and is a crucial mediator of septic shock. Nature 2001. 410: 1103-1107.
    • (2001) Nature , vol.410 , pp. 1103-1107
    • Bouchon, A.1    Facchetti, F.2    Weigand, M.A.3    Colonna, M.4
  • 13
    • 23744513114 scopus 로고    scopus 로고
    • DAP12 (KARAP) amplifies inflammation and increases mortality from endotoxemia and septic peritonitis
    • Turnbull, I. R., McDunn, J. E., Takai, T., Townsend, R. R., Cobb, J. P. and Colonna, M., DAP12 (KARAP) amplifies inflammation and increases mortality from endotoxemia and septic peritonitis. J. Exp. Med 2005. 202: 363-369.
    • (2005) J. Exp. Med , vol.202 , pp. 363-369
    • Turnbull, I.R.1    McDunn, J.E.2    Takai, T.3    Townsend, R.R.4    Cobb, J.P.5    Colonna, M.6
  • 14
    • 33645281948 scopus 로고    scopus 로고
    • CpG-induced tyrosine phosphorylation occurs via a TLR9-independent mechanism and is required for cytokine secretion
    • Sanjuan, M. A., Rao, N., Lai, K. T., Gu, Y., Sun, S., Fuchs, A., Fung-Leung, W. P. et al., CpG-induced tyrosine phosphorylation occurs via a TLR9-independent mechanism and is required for cytokine secretion. J. Cell Biol. 2006. 172: 1057-1068.
    • (2006) J. Cell Biol. , vol.172 , pp. 1057-1068
    • Sanjuan, M.A.1    Rao, N.2    Lai, K.T.3    Gu, Y.4    Sun, S.5    Fuchs, A.6    Fung-Leung, W.P.7
  • 15
    • 33744543517 scopus 로고    scopus 로고
    • MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction
    • Gray, P., Dunne, A., Brikos, C., Jefferies, C. A., Doyle, S. L. and O'Neill, L. A., MyD88 adapter-like (Mal) is phosphorylated by Bruton's tyrosine kinase during TLR2 and TLR4 signal transduction. J. Biol. Chem. 2006. 281: 10489-10495.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10489-10495
    • Gray, P.1    Dunne, A.2    Brikos, C.3    Jefferies, C.A.4    Doyle, S.L.5    O'Neill, L.A.6
  • 16
    • 0029803010 scopus 로고    scopus 로고
    • The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation
    • Osborne, M. A., Zenner, G., Lubinus, M., Zhang, X., Songyang, Z., Cantley, L. C., Majerus, P. et al., The inositol 5′-phosphatase SHIP binds to immunoreceptor signaling motifs and responds to high affinity IgE receptor aggregation. J. Biol. Chem 1996. 271: 29271-29278.
    • (1996) J. Biol. Chem , vol.271 , pp. 29271-29278
    • Osborne, M.A.1    Zenner, G.2    Lubinus, M.3    Zhang, X.4    Songyang, Z.5    Cantley, L.C.6    Majerus, P.7
  • 17
    • 0030946792 scopus 로고    scopus 로고
    • The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor
    • Kimura, T., Sakamoto, H., Appella, E. and Siraganian, R. P., The negative signaling molecule SH2 domain-containing inositol-polyphosphate 5-phosphatase (SHIP) binds to the tyrosine-phosphorylated beta subunit of the high affinity IgE receptor. J. Biol. Chem 1997. 272: 13991-13996.
    • (1997) J. Biol. Chem , vol.272 , pp. 13991-13996
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 18
    • 0042316826 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase SHP-1 associates with the phosphorylated immunoreceptor tyrosine-based activation motif of Fc gamma RIIa to modulate signaling events in myeloid cells
    • Ganesan, L. P., Fang, H., Marsh, C. B. and Tridandapani, S., The protein-tyrosine phosphatase SHP-1 associates with the phosphorylated immunoreceptor tyrosine-based activation motif of Fc gamma RIIa to modulate signaling events in myeloid cells. J. Biol. Chem 2003. 278: 35710-35717.
    • (2003) J. Biol. Chem , vol.278 , pp. 35710-35717
    • Ganesan, L.P.1    Fang, H.2    Marsh, C.B.3    Tridandapani, S.4
  • 19
    • 0032526860 scopus 로고    scopus 로고
    • NKp44, a novel triggering surface molecule specifically expressed by activated natural killer cells, is involved in non-major histocompatibility complex-restricted tumor cell lysis
    • Vitale, M., Bottino, C., Sivori, S., Sanseverino, L., Castriconi, R., Marcenaro, E., Augugliaro, R. et al., NKp44, a novel triggering surface molecule specifically expressed by activated natural killer cells, is involved in non-major histocompatibility complex-restricted tumor cell lysis. J. Exp. Med. 1998. 187: 2065-2072.
    • (1998) J. Exp. Med. , vol.187 , pp. 2065-2072
    • Vitale, M.1    Bottino, C.2    Sivori, S.3    Sanseverino, L.4    Castriconi, R.5    Marcenaro, E.6    Augugliaro, R.7
  • 20
    • 24744455913 scopus 로고    scopus 로고
    • Paradoxic inhibition of human natural interferon-producing cells by the activating receptor NKp44
    • Fuchs, A., Cella, M., Kondo, T. and Colonna, M., Paradoxic inhibition of human natural interferon-producing cells by the activating receptor NKp44. Blood 2005. 106: 2076-2082.
    • (2005) Blood , vol.106 , pp. 2076-2082
    • Fuchs, A.1    Cella, M.2    Kondo, T.3    Colonna, M.4
  • 21
    • 1642536465 scopus 로고    scopus 로고
    • NKp44 triggers NK cell activation through DAP12 association that is not influenced by a putative cytoplasmic inhibitory sequence
    • Campbell, K. S., Yusa, S., Kikuchi-Maki, A. and Catina, T. L., NKp44 triggers NK cell activation through DAP12 association that is not influenced by a putative cytoplasmic inhibitory sequence. J. Immunol. 2004. 172: 899-906.
    • (2004) J. Immunol. , vol.172 , pp. 899-906
    • Campbell, K.S.1    Yusa, S.2    Kikuchi-Maki, A.3    Catina, T.L.4
  • 22
    • 33644772437 scopus 로고    scopus 로고
    • Siglec-H is an IPC-specific receptor that modulates type I IFN secretion through DAP12
    • Blasius, A. L., Cella, M., Maldonado, J., Takai, T. and Colonna, M., Siglec-H is an IPC-specific receptor that modulates type I IFN secretion through DAP12. Blood 2006. 107: 2474-2476.
    • (2006) Blood , vol.107 , pp. 2474-2476
    • Blasius, A.L.1    Cella, M.2    Maldonado, J.3    Takai, T.4    Colonna, M.5
  • 23
    • 0035905321 scopus 로고    scopus 로고
    • BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction
    • Dzionek, A., Sohma, Y., Nagafune, J., Cella, M., Colonna, M., Facchetti, F., Gunther, G. et al., BDCA-2, a novel plasmacytoid dendritic cell-specific type II C-type lectin, mediates antigen capture and is a potent inhibitor of interferon alpha/beta induction. J. Exp. Med 2001. 194: 1823-1834.
    • (2001) J. Exp. Med , vol.194 , pp. 1823-1834
    • Dzionek, A.1    Sohma, Y.2    Nagafune, J.3    Cella, M.4    Colonna, M.5    Facchetti, F.6    Gunther, G.7
  • 24
    • 33645310982 scopus 로고    scopus 로고
    • ITAM-mediated tonic signalling through pre-BCR and BCR complexes
    • Monroe, J.G., ITAM-mediated tonic signalling through pre-BCR and BCR complexes. Nat. Rev. Immunol 2006. 6: 283-294.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 283-294
    • Monroe, J.G.1
  • 25
    • 0035496101 scopus 로고    scopus 로고
    • Epstein-Barr virus: Exploiting the immune system
    • Thorley-Lawson, D. A., Epstein-Barr virus: exploiting the immune system. Nat. Rev. Immunol. 2001. 1: 75-82.
    • (2001) Nat. Rev. Immunol. , vol.1 , pp. 75-82
    • Thorley-Lawson, D.A.1
  • 26
    • 10344249902 scopus 로고    scopus 로고
    • Epstein-Barr virus latent membrane 2A (LMP2A) down-regulates telomerase reverse transcriptase (hTERT) in epithelial cell lines
    • Morrison, J. A., Raab-Traub, N., Chen, F., Liu, C., Lindvall, C., Xu, D. and Ernberg, I., Epstein-Barr virus latent membrane 2A (LMP2A) down-regulates telomerase reverse transcriptase (hTERT) in epithelial cell lines. Int. J. Cancer 2005. 113: 284-289.
    • (2005) Int. J. Cancer , vol.113 , pp. 284-289
    • Morrison, J.A.1    Raab-Traub, N.2    Chen, F.3    Liu, C.4    Lindvall, C.5    Xu, D.6    Ernberg, I.7
  • 27
    • 13444254201 scopus 로고    scopus 로고
    • Roles of the ITAM and PY motifs of Epstein-Barr virus latent membrane protein 2A in the inhibition of epithelial cell differentiation and activation of β-catenin signaling
    • Morrison, J. A. and Raab-Traub, N., Roles of the ITAM and PY motifs of Epstein-Barr virus latent membrane protein 2A in the inhibition of epithelial cell differentiation and activation of β-catenin signaling. J. Virol 2005. 79: 2375-2382.
    • (2005) J. Virol , vol.79 , pp. 2375-2382
    • Morrison, J.A.1    Raab-Traub, N.2
  • 28
    • 0346725003 scopus 로고    scopus 로고
    • Systematic identification of immunoreceptor tyrosine-based inhibitory motifs in the human proteome
    • Staub, E., Rosenthal, A. and Hinzmann, B., Systematic identification of immunoreceptor tyrosine-based inhibitory motifs in the human proteome. Cell Signal. 2004. 16: 435-456.
    • (2004) Cell Signal. , vol.16 , pp. 435-456
    • Staub, E.1    Rosenthal, A.2    Hinzmann, B.3
  • 29
    • 2442450439 scopus 로고    scopus 로고
    • Cutting edge: TREM-like transcript-1, a platelet immunoreceptor tyrosine-based inhibition motif encoding costimulatory immunoreceptor that enhances, rather than inhibits, calcium signaling via SHP-2
    • Barrow, A. D., Astoul, E., Floto, A., Brooke, G., Relou, I. A., Jennings, N. S., Smith, K. G. et al., Cutting edge: TREM-like transcript-1, a platelet immunoreceptor tyrosine-based inhibition motif encoding costimulatory immunoreceptor that enhances, rather than inhibits, calcium signaling via SHP-2. J. Immunol 2004. 172: 5838-5842.
    • (2004) J. Immunol , vol.172 , pp. 5838-5842
    • Barrow, A.D.1    Astoul, E.2    Floto, A.3    Brooke, G.4    Relou, I.A.5    Jennings, N.S.6    Smith, K.G.7
  • 31
    • 0033565294 scopus 로고    scopus 로고
    • A new role for platelet-endothelial cell adhesion molecule-1 (CD31): Inhibition of TCR-mediated signal transduction
    • Newton-Nash, D. K. and Newman, P. J., A new role for platelet-endothelial cell adhesion molecule-1 (CD31): inhibition of TCR-mediated signal transduction. J. Immunol. 1999. 163: 682-688.
    • (1999) J. Immunol. , vol.163 , pp. 682-688
    • Newton-Nash, D.K.1    Newman, P.J.2
  • 32
    • 0035871812 scopus 로고    scopus 로고
    • Inhibition of antigen-receptor signaling by platelet endothelial cell adhesion molecule-1 (CD31) requires functional ITIMs, SHP-2, and p56(lck)
    • Newman, D. K., Hamilton, C. and Newman, P. J., Inhibition of antigen-receptor signaling by platelet endothelial cell adhesion molecule-1 (CD31) requires functional ITIMs, SHP-2, and p56(lck). Blood 2001. 97: 2351-2357.
    • (2001) Blood , vol.97 , pp. 2351-2357
    • Newman, D.K.1    Hamilton, C.2    Newman, P.J.3
  • 33
    • 28444480199 scopus 로고    scopus 로고
    • The Ig-ITIM superfamily member PECAM-1 regulates the "outside-in" signaling properties of integrin alpha(IIb)beta3 in platelets
    • Wee, J. L. and Jackson, D. E., The Ig-ITIM superfamily member PECAM-1 regulates the "outside-in" signaling properties of integrin alpha(IIb)beta3 in platelets. Blood. 106: 3816-3823.
    • Blood , vol.106 , pp. 3816-3823
    • Wee, J.L.1    Jackson, D.E.2
  • 34
    • 4544292278 scopus 로고    scopus 로고
    • Role of immunoreceptor tyrosine-based inhibitory motifs of PECAM-1 in PECAM-1-dependent cell migration
    • O'Brien, C. D., Cao, G., Makrigiannakis, A. and DeLisser, H. M.Role of immunoreceptor tyrosine-based inhibitory motifs of PECAM-1 in PECAM-1-dependent cell migration. Am. J. Physiol. Cell. Physiol. 2004. 287: C1103-1113.
    • (2004) Am. J. Physiol. Cell. Physiol. , vol.287
    • O'Brien, C.D.1    Cao, G.2    Makrigiannakis, A.3    DeLisser, H.M.4
  • 35
    • 8444224950 scopus 로고    scopus 로고
    • Platelet endothelial cell adhesion molecule deficiency or blockade significantly reduces leukocyte emigration in a majority of mouse strains
    • Schenkel, A. R., Chew, T. W. and Muller, W. A.Platelet endothelial cell adhesion molecule deficiency or blockade significantly reduces leukocyte emigration in a majority of mouse strains. J. Immunol. 2004. 173: 6403-6408.
    • (2004) J. Immunol. , vol.173 , pp. 6403-6408
    • Schenkel, A.R.1    Chew, T.W.2    Muller, W.A.3
  • 36
    • 2942571936 scopus 로고    scopus 로고
    • Ligand stimulation of CD155alpha inhibits cell adhesion and enhances cell migration in fibroblasts
    • Oda, T., Ohka, S. and Nomoto, A., Ligand stimulation of CD155alpha inhibits cell adhesion and enhances cell migration in fibroblasts. Biochem. Biophys. Res. Commun. 2004. 319: 1253-1264.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 1253-1264
    • Oda, T.1    Ohka, S.2    Nomoto, A.3
  • 37
    • 25144510997 scopus 로고    scopus 로고
    • A mechanosensory complex that mediates the endothelial cell response to fluid shear stress
    • Tzima, E., Irani-Tehrani, M., Kiosses, W. B., Dejana, E., Schultz, D. A., Engelhardt, B., Cao, G. et al., A mechanosensory complex that mediates the endothelial cell response to fluid shear stress. Nature 2005. 437: 426-431.
    • (2005) Nature , vol.437 , pp. 426-431
    • Tzima, E.1    Irani-Tehrani, M.2    Kiosses, W.B.3    Dejana, E.4    Schultz, D.A.5    Engelhardt, B.6    Cao, G.7
  • 38
    • 0033526056 scopus 로고    scopus 로고
    • A human histocompatibility leukocyte antigen (HLA)-G-specific receptor expressed on all natural killer cells
    • Rajagopalan, S. and Long, E. O.A human histocompatibility leukocyte antigen (HLA)-G-specific receptor expressed on all natural killer cells. J. Exp. Med 1999. 189: 1093-1100.
    • (1999) J. Exp. Med , vol.189 , pp. 1093-1100
    • Rajagopalan, S.1    Long, E.O.2
  • 39
    • 15444371656 scopus 로고    scopus 로고
    • Cutting edge: KIR2DL4 transduces signals into human NK cells through association with the Fc receptor gamma protein
    • Kikuchi-Maki, A., Catina, T. L. and Campbell, K. S., Cutting edge: KIR2DL4 transduces signals into human NK cells through association with the Fc receptor gamma protein. J. Immunol. 2005. 174: 3859-3863.
    • (2005) J. Immunol. , vol.174 , pp. 3859-3863
    • Kikuchi-Maki, A.1    Catina, T.L.2    Campbell, K.S.3
  • 40
    • 0035881573 scopus 로고    scopus 로고
    • Cutting edge: Induction of IFN-gamma production but not cytotoxicity by the killer cell Ig-like receptor KIR2DL4 (CD158d) in resting NK cells
    • Rajagopalan, S., Fu, J. and Long, E. O.Cutting edge: induction of IFN-gamma production but not cytotoxicity by the killer cell Ig-like receptor KIR2DL4 (CD158d) in resting NK cells. J. Immunol. 2001. 167: 1877-1881.
    • (2001) J. Immunol. , vol.167 , pp. 1877-1881
    • Rajagopalan, S.1    Fu, J.2    Long, E.O.3
  • 41
    • 0037094006 scopus 로고    scopus 로고
    • SHP-1- and phosphotyrosine-independent inhibitory signaling by a killer cell Ig-like receptor cytoplasmic domain in human NK cells
    • Yusa, S., Catina, T. L. and Campbell, K. S.SHP-1- and phosphotyrosine-independent inhibitory signaling by a killer cell Ig-like receptor cytoplasmic domain in human NK cells. J. Immunol. 2002. 168: 5047-5057.
    • (2002) J. Immunol. , vol.168 , pp. 5047-5057
    • Yusa, S.1    Catina, T.L.2    Campbell, K.S.3
  • 43
    • 23644458333 scopus 로고    scopus 로고
    • Licensing of natural killer cells by host major histocompatibility complex class I molecules
    • Kim, S., Poursine-Laurent, J., Truscott, S. M., Lybarger, L., Song, Y. J., Yang, L., French, A. R. et al., Licensing of natural killer cells by host major histocompatibility complex class I molecules. Nature 2005. 436: 709-713.
    • (2005) Nature , vol.436 , pp. 709-713
    • Kim, S.1    Poursine-Laurent, J.2    Truscott, S.M.3    Lybarger, L.4    Song, Y.J.5    Yang, L.6    French, A.R.7
  • 44
    • 18844365992 scopus 로고    scopus 로고
    • A subset of natural killer cells achieves self-tolerance without expressing inhibitory receptors specific for self-MHC molecules
    • Fernandez, N. C., Treiner, E., Vance, R. E., Jamieson, A. M., Lemieux, S. and Raulet, D. H., A subset of natural killer cells achieves self-tolerance without expressing inhibitory receptors specific for self-MHC molecules. Blood 2005. 105: 4416-1423.
    • (2005) Blood , vol.105 , pp. 1423-4416
    • Fernandez, N.C.1    Treiner, E.2    Vance, R.E.3    Jamieson, A.M.4    Lemieux, S.5    Raulet, D.H.6
  • 45
    • 33644972706 scopus 로고    scopus 로고
    • How do natural killer cells find self to achieve tolerance?
    • Yokoyama, W. M. and Kim, S., How do natural killer cells find self to achieve tolerance? Immunity 2006. 24: 249-257.
    • (2006) Immunity , vol.24 , pp. 249-257
    • Yokoyama, W.M.1    Kim, S.2
  • 46
    • 4544334936 scopus 로고    scopus 로고
    • Oncogenic mechanisms of the Helicobacter pylori CagA protein
    • Hatakeyama, M., Oncogenic mechanisms of the Helicobacter pylori CagA protein. Nat. Rev. Cancer 2004. 4: 688-694.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 688-694
    • Hatakeyama, M.1
  • 47
    • 0142059890 scopus 로고    scopus 로고
    • Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling
    • Agazie, Y. M. and Hayman, M. J., Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling. Mol. Cell. Biol 2003. 23: 7875-7886.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 7875-7886
    • Agazie, Y.M.1    Hayman, M.J.2
  • 48
    • 10744223870 scopus 로고    scopus 로고
    • Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment
    • Zhang, S. Q., Yang, W., Kontaridis, M. I., Bivona, T. G., Wen, G., Araki, T., Luo, J. et al., Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment. Mol. Cell 2004. 13: 341-355.
    • (2004) Mol. Cell , vol.13 , pp. 341-355
    • Zhang, S.Q.1    Yang, W.2    Kontaridis, M.I.3    Bivona, T.G.4    Wen, G.5    Araki, T.6    Luo, J.7
  • 49
    • 0141730311 scopus 로고    scopus 로고
    • Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling
    • Yu, W. M., Hawley, T. S., Hawley, R. G. and Qu, C. K., Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling. Oncogene 2003. 22: 5995-6004.
    • (2003) Oncogene , vol.22 , pp. 5995-6004
    • Yu, W.M.1    Hawley, T.S.2    Hawley, R.G.3    Qu, C.K.4
  • 50
    • 0034666158 scopus 로고    scopus 로고
    • Evidence of a role for SHP-1 in platelet activation by the collagen receptor glycoprotein VI
    • Pasquet, J. M., Quek, L., Pasquet, S., Poole, A., Matthews, J. R., Lowell, C. and Watson, S. P., Evidence of a role for SHP-1 in platelet activation by the collagen receptor glycoprotein VI. J. Biol. Chem 2000. 275: 28526-28531.
    • (2000) J. Biol. Chem , vol.275 , pp. 28526-28531
    • Pasquet, J.M.1    Quek, L.2    Pasquet, S.3    Poole, A.4    Matthews, J.R.5    Lowell, C.6    Watson, S.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.