메뉴 건너뛰기




Volumn 190, Issue 4, 2013, Pages 1807-1818

Nonredundant roles of Src-family kinases and Syk in the initiation of B-cell antigen receptor signaling

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CD79A ANTIGEN; PROTEIN KINASE SYK; PROTEIN KINASE SYK INHIBITOR; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 84873562250     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1202401     Document Type: Article
Times cited : (26)

References (75)
  • 1
    • 0027493485 scopus 로고
    • Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl- phosphatidylinositolanchored proteins
    • Shenoy-Scaria, A. M., L. K. Gauen, J. Kwong, A. S. Shaw, and D. M. Lublin. 1993. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositolanchored proteins. Mol. Cell. Biol. 13: 6385-6392.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6385-6392
    • Shenoy-Scaria, A.M.1    Gauen, L.K.2    Kwong, J.3    Shaw, A.S.4    Lublin, D.M.5
  • 2
    • 0021285532 scopus 로고
    • A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation
    • Cross, F. R., E. A. Garber, D. Pellman, and H. Hanafusa. 1984. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Mol. Cell. Biol. 4: 1834-1842.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1834-1842
    • Cross, F.R.1    Garber, E.A.2    Pellman, D.3    Hanafusa, H.4
  • 3
    • 3042615397 scopus 로고    scopus 로고
    • Src-family kinases: Rheostats of immune cell signaling
    • Lowell, C. A. 2004. Src-family kinases: rheostats of immune cell signaling. Mol. Immunol. 41: 631-643.
    • (2004) Mol. Immunol. , vol.41 , pp. 631-643
    • Lowell, C.A.1
  • 4
    • 39149139617 scopus 로고    scopus 로고
    • Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling
    • Zhu, J. W., T. Brdicka, T. R. Katsumoto, J. Lin, and A. Weiss. 2008. Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling. Immunity 28: 183-196.
    • (2008) Immunity , vol.28 , pp. 183-196
    • Zhu, J.W.1    Brdicka, T.2    Katsumoto, T.R.3    Lin, J.4    Weiss, A.5
  • 6
    • 0027389272 scopus 로고
    • CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck
    • Sieh, M., J. B. Bolen, and A. Weiss. 1993. CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck. EMBO J. 12: 315-321.
    • (1993) EMBO J. , vol.12 , pp. 315-321
    • Sieh, M.1    Bolen, J.B.2    Weiss, A.3
  • 7
    • 0024829259 scopus 로고
    • A protein tyrosine kinase involved in regulation of pp60c-src function
    • Okada, M., and H. Nakagawa. 1989. A protein tyrosine kinase involved in regulation of pp60c-src function. J. Biol. Chem. 264: 20886-20893.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20886-20893
    • Okada, M.1    Nakagawa, H.2
  • 8
    • 0023649622 scopus 로고
    • Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src
    • Piwnica-Worms, H., K. B. Saunders, T. M. Roberts, A. E. Smith, and S. H. Cheng. 1987. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 49: 75-82.
    • (1987) Cell , vol.49 , pp. 75-82
    • Piwnica-Worms, H.1    Saunders, K.B.2    Roberts, T.M.3    Smith, A.E.4    Cheng, S.H.5
  • 9
    • 38349014380 scopus 로고    scopus 로고
    • Src family kinases: Regulation of their activities, levels and identification of new pathways
    • Ingley, E. 2008. Src family kinases: regulation of their activities, levels and identification of new pathways. Biochim. Biophys. Acta 1784: 56-65.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 56-65
    • Ingley, E.1
  • 10
    • 0036330594 scopus 로고    scopus 로고
    • Effect of autophosphorylation on the catalytic and regulatory properties of protein tyrosine kinase Src
    • Sun, G., L. Ramdas, W. Wang, J. Vinci, J. McMurray, and R. J. Budde. 2002. Effect of autophosphorylation on the catalytic and regulatory properties of protein tyrosine kinase Src. Arch. Biochem. Biophys. 397: 11-17.
    • (2002) Arch. Biochem. Biophys. , vol.397 , pp. 11-17
    • Sun, G.1    Ramdas, L.2    Wang, W.3    Vinci, J.4    McMurray, J.5    Budde, R.J.6
  • 12
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., B. A. Irving, N. S. van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263: 1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 13
    • 0028783396 scopus 로고
    • Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling
    • Kurosaki, T., S. A. Johnson, L. Pao, K. Sada, H. Yamamura, and J. C. Cambier. 1995. Role of the Syk autophosphorylation site and SH2 domains in B cell antigen receptor signaling. J. Exp. Med. 182: 1815-1823.
    • (1995) J. Exp. Med. , vol.182 , pp. 1815-1823
    • Kurosaki, T.1    Johnson, S.A.2    Pao, L.3    Sada, K.4    Yamamura, H.5    Cambier, J.C.6
  • 15
    • 0036866477 scopus 로고    scopus 로고
    • Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop
    • Rolli, V., M. Gallwitz, T. Wossning, A. Flemming, W. W. Schamel, C. Zürn, and M. Reth. 2002. Amplification of B cell antigen receptor signaling by a Syk/ITAM positive feedback loop. Mol. Cell 10: 1057-1069.
    • (2002) Mol. Cell , vol.10 , pp. 1057-1069
    • Rolli, V.1    Gallwitz, M.2    Wossning, T.3    Flemming, A.4    Schamel, W.W.5    Zürn, C.6    Reth, M.7
  • 16
    • 77952887713 scopus 로고    scopus 로고
    • The SYK tyrosine kinase: A crucial player in diverse biological functions
    • Mócsai, A., J. Ruland, and V. L. Tybulewicz. 2010. The SYK tyrosine kinase: a crucial player in diverse biological functions. Nat. Rev. Immunol. 10: 387-402.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 387-402
    • Mócsai, A.1    Ruland, J.2    Tybulewicz, V.L.3
  • 17
    • 0032534071 scopus 로고    scopus 로고
    • Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling
    • Keshvara, L. M., C. C. Isaacson, T. M. Yankee, R. Sarac, M. L. Harrison, and R. L. Geahlen. 1998. Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling. J. Immunol. 161: 5276-5283.
    • (1998) J. Immunol. , vol.161 , pp. 5276-5283
    • Keshvara, L.M.1    Isaacson, C.C.2    Yankee, T.M.3    Sarac, R.4    Harrison, M.L.5    Geahlen, R.L.6
  • 19
    • 20344406482 scopus 로고    scopus 로고
    • Intramolecular regulatory switch in ZAP-70: Analogy with receptor tyrosine kinases
    • Brdicka, T., T. A. Kadlecek, J. P. Roose, A. W. Pastuszak, and A. Weiss. 2005. Intramolecular regulatory switch in ZAP-70: analogy with receptor tyrosine kinases. Mol. Cell. Biol. 25: 4924-4933.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4924-4933
    • Brdicka, T.1    Kadlecek, T.A.2    Roose, J.P.3    Pastuszak, A.W.4    Weiss, A.5
  • 20
    • 77952299611 scopus 로고    scopus 로고
    • The Src, Syk, and Tec family kinases: Distinct types of molecular switches
    • Bradshaw, J. M. 2010. The Src, Syk, and Tec family kinases: distinct types of molecular switches. Cell. Signal. 22: 1175-1184.
    • (2010) Cell. Signal. , vol.22 , pp. 1175-1184
    • Bradshaw, J.M.1
  • 21
    • 0032532359 scopus 로고    scopus 로고
    • Mutations in the activation loop tyrosines of protein tyrosine kinase Syk abrogate intracellular signaling but not kinase activity
    • Zhang, J., T. Kimura, and R. P. Siraganian. 1998. Mutations in the activation loop tyrosines of protein tyrosine kinase Syk abrogate intracellular signaling but not kinase activity. J. Immunol. 161: 4366-4374.
    • (1998) J. Immunol. , vol.161 , pp. 4366-4374
    • Zhang, J.1    Kimura, T.2    Siraganian, R.P.3
  • 22
    • 0030956912 scopus 로고    scopus 로고
    • Role of Tyr518 and Tyr519 in the regulation of catalytic activity and substrate phosphorylation by Syk protein-tyrosine kinase
    • Couture, C., S. Williams, N. Gauthier, P. Tailor, and T. Mustelin. 1997. Role of Tyr518 and Tyr519 in the regulation of catalytic activity and substrate phosphorylation by Syk protein-tyrosine kinase. Eur. J. Biochem. 246: 447-451.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 447-451
    • Couture, C.1    Williams, S.2    Gauthier, N.3    Tailor, P.4    Mustelin, T.5
  • 23
    • 0026353504 scopus 로고
    • Tyrosine phosphorylation of components of the B-cell antigen receptors following receptor crosslinking
    • Gold, M. R., L. Matsuuchi, R. B. Kelly, and A. L. DeFranco. 1991. Tyrosine phosphorylation of components of the B-cell antigen receptors following receptor crosslinking. Proc. Natl. Acad. Sci. USA 88: 3436-3440.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3436-3440
    • Gold, M.R.1    Matsuuchi, L.2    Kelly, R.B.3    Defranco, A.L.4
  • 24
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76: 263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 27
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D. B., and A. Weiss. 1992. Genetic evidence for the involvement of the lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70: 585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 28
    • 0028988692 scopus 로고
    • The role of Ig beta in precursor B cell transition and allelic exclusion
    • Papavasiliou, F., Z. Misulovin, H. Suh, and M. C. Nussenzweig. 1995. The role of Ig beta in precursor B cell transition and allelic exclusion. Science 268: 408-411.
    • (1995) Science , vol.268 , pp. 408-411
    • Papavasiliou, F.1    Misulovin, Z.2    Suh, H.3    Nussenzweig, M.C.4
  • 30
    • 0030740148 scopus 로고    scopus 로고
    • Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation
    • Chan, V. W., F. Meng, P. Soriano, A. L. DeFranco, and C. A. Lowell. 1997. Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation. Immunity 7: 69-81.
    • (1997) Immunity , vol.7 , pp. 69-81
    • Chan, V.W.1    Meng, F.2    Soriano, P.3    Defranco, A.L.4    Lowell, C.A.5
  • 31
    • 0032550365 scopus 로고    scopus 로고
    • A double-edged kinase Lyn: A positive and negative regulator for antigen receptormediated signals
    • Nishizumi, H., K. Horikawa, I. Mlinaric-Rascan, and T. Yamamoto. 1998. A double-edged kinase Lyn: a positive and negative regulator for antigen receptormediated signals. J. Exp. Med. 187: 1343-1348.
    • (1998) J. Exp. Med. , vol.187 , pp. 1343-1348
    • Nishizumi, H.1    Horikawa, K.2    Mlinaric-Rascan, I.3    Yamamoto, T.4
  • 32
  • 36
    • 0030795735 scopus 로고    scopus 로고
    • Molecular mechanisms in B cell antigen receptor signaling
    • Kurosaki, T. 1997. Molecular mechanisms in B cell antigen receptor signaling. Curr. Opin. Immunol. 9: 309-318.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 309-318
    • Kurosaki, T.1
  • 37
    • 70350356241 scopus 로고    scopus 로고
    • Autoinhibition and adapter function of Syk
    • Kulathu, Y., G. Grothe, and M. Reth. 2009. Autoinhibition and adapter function of Syk. Immunol. Rev. 232: 286-299.
    • (2009) Immunol. Rev. , vol.232 , pp. 286-299
    • Kulathu, Y.1    Grothe, G.2    Reth, M.3
  • 38
    • 61849141064 scopus 로고    scopus 로고
    • Tyrosine kinases and their substrates in B lymphocytes
    • Kurosaki, T., and M. Hikida. 2009. Tyrosine kinases and their substrates in B lymphocytes. Immunol. Rev. 228: 132-148.
    • (2009) Immunol. Rev. , vol.228 , pp. 132-148
    • Kurosaki, T.1    Hikida, M.2
  • 39
    • 0031568534 scopus 로고    scopus 로고
    • Protein tyrosine kinases Syk and ZAP-70 display distinct requirements for Src family kinases in immune response receptor signal transduction
    • Zoller, K. E., I. A. MacNeil, and J. S. Brugge. 1997. Protein tyrosine kinases Syk and ZAP-70 display distinct requirements for Src family kinases in immune response receptor signal transduction. J. Immunol. 158: 1650-1659.
    • (1997) J. Immunol. , vol.158 , pp. 1650-1659
    • Zoller, K.E.1    MacNeil, I.A.2    Brugge, J.S.3
  • 40
    • 0029952988 scopus 로고    scopus 로고
    • The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling
    • Chu, D. H., H. Spits, J. F. Peyron, R. B. Rowley, J. B. Bolen, and A. Weiss. 1996. The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling. EMBO J. 15: 6251-6261.
    • (1996) EMBO J. , vol.15 , pp. 6251-6261
    • Chu, D.H.1    Spits, H.2    Peyron, J.F.3    Rowley, R.B.4    Bolen, J.B.5    Weiss, A.6
  • 43
    • 0027264816 scopus 로고
    • Use of fura red as an intracellular calcium indicator in frog skeletal muscle fibers
    • Kurebayashi, N., A. B. Harkins, and S. M. Baylor. 1993. Use of fura red as an intracellular calcium indicator in frog skeletal muscle fibers. Biophys. J. 64: 1934-1960.
    • (1993) Biophys. J. , vol.64 , pp. 1934-1960
    • Kurebayashi, N.1    Harkins, A.B.2    Baylor, S.M.3
  • 44
    • 0030029143 scopus 로고    scopus 로고
    • Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation
    • Hanke, J. H., J. P. Gardner, R. L. Dow, P. S. Changelian, W. H. Brissette, E. J. Weringer, B. A. Pollok, and P. A. Connelly. 1996. Discovery of a novel, potent, and Src family-selective tyrosine kinase inhibitor. Study of Lck- and FynT-dependent T cell activation. J. Biol. Chem. 271: 695-701.
    • (1996) J. Biol. Chem. , vol.271 , pp. 695-701
    • Hanke, J.H.1    Gardner, J.P.2    Dow, R.L.3    Changelian, P.S.4    Brissette, W.H.5    Weringer, E.J.6    Pollok, B.A.7    Connelly, P.A.8
  • 45
    • 0041932075 scopus 로고    scopus 로고
    • The orally available spleen tyrosine kinase inhibitor 2-[7-(3, 4-dimethoxyphenyl)-imidazo [1, 2-c]pyrimidin-5-ylamino]nicotinamide dihydrochloride (BAY 61-3606) blocks antigen-induced airway inflammation in rodents
    • Yamamoto, N., K. Takeshita, M. Shichijo, T. Kokubo, M. Sato, K. Nakashima, M. Ishimori, H. Nagai, Y. F. Li, T. Yura, and K. B. Bacon. 2003. The orally available spleen tyrosine kinase inhibitor 2-[7-(3,4-dimethoxyphenyl)- imidazo [1,2-c]pyrimidin-5-ylamino]nicotinamide dihydrochloride (BAY 61-3606) blocks antigen-induced airway inflammation in rodents. J. Pharmacol. Exp. Ther. 306: 1174-1181.
    • (2003) J. Pharmacol. Exp. Ther. , vol.306 , pp. 1174-1181
    • Yamamoto, N.1    Takeshita, K.2    Shichijo, M.3    Kokubo, T.4    Sato, M.5    Nakashima, K.6    Ishimori, M.7    Nagai, H.8    Li, Y.F.9    Yura, T.10    Bacon, K.B.11
  • 47
    • 0022802257 scopus 로고
    • Clonal recruitment and somatic mutation in the generation of immunological memory to the hapten NP
    • Cumano, A., and K. Rajewsky. 1986. Clonal recruitment and somatic mutation in the generation of immunological memory to the hapten NP. EMBO J. 5: 2459-2468.
    • (1986) EMBO J. , vol.5 , pp. 2459-2468
    • Cumano, A.1    Rajewsky, K.2
  • 48
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler, T., F. Sicheri, A. Pico, A. Gazit, A. Levitzki, and J. Kuriyan. 1999. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3: 639-648.
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 49
    • 58649122152 scopus 로고    scopus 로고
    • Crystal structures of the Lyn protein tyrosine kinase domain in its Apo- and inhibitor-bound state
    • Williams, N. K., I. S. Lucet, S. P. Klinken, E. Ingley, and J. Rossjohn. 2009. Crystal structures of the Lyn protein tyrosine kinase domain in its Apo- and inhibitor-bound state. J. Biol. Chem. 284: 284-291.
    • (2009) J. Biol. Chem. , vol.284 , pp. 284-291
    • Williams, N.K.1    Lucet, I.S.2    Klinken, S.P.3    Ingley, E.4    Rossjohn, J.5
  • 50
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocytespecific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu, X., J. L. Kim, J. R. Newcomb, P. E. Rose, D. R. Stover, L. M. Toledo, H. Zhao, and K. A. Morgenstern. 1999. Structural analysis of the lymphocytespecific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure 7: 651-661.
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6    Zhao, H.7    Morgenstern, K.A.8
  • 51
    • 0024044570 scopus 로고
    • Antibody engineering for the analysis of affinity maturation of an anti-hapten response
    • Allen, D., T. Simon, F. Sablitzky, K. Rajewsky, and A. Cumano. 1988. Antibody engineering for the analysis of affinity maturation of an anti-hapten response. EMBO J. 7: 1995-2001.
    • (1988) EMBO J. , vol.7 , pp. 1995-2001
    • Allen, D.1    Simon, T.2    Sablitzky, F.3    Rajewsky, K.4    Cumano, A.5
  • 52
    • 0037392942 scopus 로고    scopus 로고
    • The specificities of protein kinase inhibitors: An update
    • Bain, J., H. McLauchlan, M. Elliott, and P. Cohen. 2003. The specificities of protein kinase inhibitors: an update. Biochem. J. 371: 199-204.
    • (2003) Biochem. J. , vol.371 , pp. 199-204
    • Bain, J.1    McLauchlan, H.2    Elliott, M.3    Cohen, P.4
  • 54
    • 0028787398 scopus 로고
    • The catalytic activity of Src-family tyrosine kinase is required for B cell antigen receptor signaling
    • Takata, M., and T. Kurosaki. 1995. The catalytic activity of Src-family tyrosine kinase is required for B cell antigen receptor signaling. FEBS Lett. 374: 407-411.
    • (1995) FEBS Lett. , vol.374 , pp. 407-411
    • Takata, M.1    Kurosaki, T.2
  • 55
    • 0031569176 scopus 로고    scopus 로고
    • Syk, but not Lyn, recruitment to B cell antigen receptor and activation following stimulation of CD45-B cells
    • Pao, L. I., and J. C. Cambier. 1997. Syk, but not Lyn, recruitment to B cell antigen receptor and activation following stimulation of CD45-B cells. J. Immunol. 158: 2663-2669.
    • (1997) J. Immunol. , vol.158 , pp. 2663-2669
    • Pao, L.I.1    Cambier, J.C.2
  • 56
    • 0037204949 scopus 로고    scopus 로고
    • B cell antigen receptor signaling: Roles in cell development and disease
    • Gauld, S. B., J. M. Dal Porto, and J. C. Cambier. 2002. B cell antigen receptor signaling: roles in cell development and disease. Science 296: 1641-1642.
    • (2002) Science , vol.296 , pp. 1641-1642
    • Gauld, S.B.1    Dal Porto, J.M.2    Cambier, J.C.3
  • 57
    • 79956307046 scopus 로고    scopus 로고
    • Regulation of BCR signaling
    • Kurosaki, T. 2011. Regulation of BCR signaling. Mol. Immunol. 48: 1287-1291.
    • (2011) Mol. Immunol. , vol.48 , pp. 1287-1291
    • Kurosaki, T.1
  • 58
    • 7944235830 scopus 로고    scopus 로고
    • Src-family kinases in B-cell development and signaling
    • Gauld, S. B., and J. C. Cambier. 2004. Src-family kinases in B-cell development and signaling. Oncogene 23: 8001-8006.
    • (2004) Oncogene , vol.23 , pp. 8001-8006
    • Gauld, S.B.1    Cambier, J.C.2
  • 59
    • 0028793187 scopus 로고
    • Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases
    • Johnson, S. A., C. M. Pleiman, L. Pao, J. Schneringer, K. Hippen, and J. C. Cambier. 1995. Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate Lyn and Syk tyrosine kinases. J. Immunol. 155: 4596-4603.
    • (1995) J. Immunol. , vol.155 , pp. 4596-4603
    • Johnson, S.A.1    Pleiman, C.M.2    Pao, L.3    Schneringer, J.4    Hippen, K.5    Cambier, J.C.6
  • 60
    • 0033697728 scopus 로고    scopus 로고
    • CD19 regulates Src family protein tyrosine kinase activation in B lymphocytes through processive amplification
    • Fujimoto, M., Y. Fujimoto, J. C. Poe, P. J. Jansen, C. A. Lowell, A. L. DeFranco, and T. F. Tedder. 2000. CD19 regulates Src family protein tyrosine kinase activation in B lymphocytes through processive amplification. Immunity 13: 47-57.
    • (2000) Immunity , vol.13 , pp. 47-57
    • Fujimoto, M.1    Fujimoto, Y.2    Poe, J.C.3    Jansen, P.J.4    Lowell, C.A.5    Defranco, A.L.6    Tedder, T.F.7
  • 61
    • 0035451678 scopus 로고    scopus 로고
    • A CD19-dependent signaling pathway regulates autoimmunity in Lyn-deficient mice
    • Hasegawa, M., M. Fujimoto, J. C. Poe, D. A. Steeber, C. A. Lowell, and T. F. Tedder. 2001. A CD19-dependent signaling pathway regulates autoimmunity in Lyn-deficient mice. J. Immunol. 167: 2469-2478.
    • (2001) J. Immunol. , vol.167 , pp. 2469-2478
    • Hasegawa, M.1    Fujimoto, M.2    Poe, J.C.3    Steeber, D.A.4    Lowell, C.A.5    Tedder, T.F.6
  • 63
  • 64
    • 0028125752 scopus 로고
    • Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor
    • Flaswinkel, H., and M. Reth. 1994. Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor. EMBO J. 13: 83-89.
    • (1994) EMBO J. , vol.13 , pp. 83-89
    • Flaswinkel, H.1    Reth, M.2
  • 65
    • 0032055963 scopus 로고    scopus 로고
    • Asymmetrical phosphorylation and function of immunoreceptor tyrosine-based activation motif tyrosines in B cell antigen receptor signal transduction
    • Pao, L. I., S. J. Famiglietti, and J. C. Cambier. 1998. Asymmetrical phosphorylation and function of immunoreceptor tyrosine-based activation motif tyrosines in B cell antigen receptor signal transduction. J. Immunol. 160: 3305-3314.
    • (1998) J. Immunol. , vol.160 , pp. 3305-3314
    • Pao, L.I.1    Famiglietti, S.J.2    Cambier, J.C.3
  • 66
    • 0034717038 scopus 로고    scopus 로고
    • Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor
    • Gaul, B. S., M. L. Harrison, R. L. Geahlen, R. A. Burton, and C. B. Post. 2000. Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor. J. Biol. Chem. 275: 16174-16182.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16174-16182
    • Gaul, B.S.1    Harrison, M.L.2    Geahlen, R.L.3    Burton, R.A.4    Post, C.B.5
  • 67
    • 0029788103 scopus 로고    scopus 로고
    • Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases
    • Latour, S., L. M. Chow, and A. Veillette. 1996. Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases. J. Biol. Chem. 271: 22782-22790.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22782-22790
    • Latour, S.1    Chow, L.M.2    Veillette, A.3
  • 68
    • 0033198133 scopus 로고    scopus 로고
    • CD45 is essential for Fc epsilon RI signaling by ZAP70, but not Syk, in Syk-negative mast cells
    • Zhang, J., and R. P. Siraganian. 1999. CD45 is essential for Fc epsilon RI signaling by ZAP70, but not Syk, in Syk-negative mast cells. J. Immunol. 163: 2508-2516.
    • (1999) J. Immunol. , vol.163 , pp. 2508-2516
    • Zhang, J.1    Siraganian, R.P.2
  • 71
    • 73949093141 scopus 로고    scopus 로고
    • A minor catalytic activity of Src family kinases is sufficient for maximal activation of mast cells via the high-affinity IgE receptor
    • Poderycki, M., Y. Tomimori, T. Ando, W. Xiao, M. Maeda-Yamamoto, K. Sauer, Y. Kawakami, and T. Kawakami. 2010. A minor catalytic activity of Src family kinases is sufficient for maximal activation of mast cells via the high-affinity IgE receptor. J. Immunol. 184: 84-93.
    • (2010) J. Immunol. , vol.184 , pp. 84-93
    • Poderycki, M.1    Tomimori, Y.2    Ando, T.3    Xiao, W.4    Maeda-Yamamoto, M.5    Sauer, K.6    Kawakami, Y.7    Kawakami, T.8
  • 73
    • 79953072735 scopus 로고    scopus 로고
    • Dasatinib inhibits B cell receptor signalling in chronic lymphocytic leukaemia but novel combination approaches are required to overcome additional pro-survival microenvironmental signals
    • McCaig, A. M., E. Cosimo, M. T. Leach, and A. M. Michie. 2011. Dasatinib inhibits B cell receptor signalling in chronic lymphocytic leukaemia but novel combination approaches are required to overcome additional pro-survival microenvironmental signals. Br. J. Haematol. 153: 199-211.
    • (2011) Br. J. Haematol. , vol.153 , pp. 199-211
    • McCaig, A.M.1    Cosimo, E.2    Leach, M.T.3    Michie, A.M.4
  • 75
    • 77954315861 scopus 로고    scopus 로고
    • Spleen tyrosine kinases: Biology, therapeutic targets and drugs
    • Riccaboni, M., I. Bianchi, and P. Petrillo. 2010. Spleen tyrosine kinases: biology, therapeutic targets and drugs. Drug Discov. Today 15: 517-530.
    • (2010) Drug Discov. Today , vol.15 , pp. 517-530
    • Riccaboni, M.1    Bianchi, I.2    Petrillo, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.