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Volumn 244, Issue , 1999, Pages 43-55

The unexpected complexity of FcγRIIB signal transduction

(3)  Cambier, J C a   Fong, D a   Tamir, I a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

FC RECEPTOR; MUTANT PROTEIN;

EID: 0033013905     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-58537-1_4     Document Type: Review
Times cited : (14)

References (10)
  • 1
    • 0026769620 scopus 로고
    • Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes
    • Amigorena S, Bonnerot C et al. (1992) Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes. Science 256(5065):1808-1812
    • (1992) Science , vol.256 , Issue.5065 , pp. 1808-1812
    • Amigorena, S.1    Bonnerot, C.2
  • 2
    • 0029891083 scopus 로고    scopus 로고
    • Fc receptor off-signal in the B cell involves apoptosis
    • Ashman RF, Peckham D et al. (1996). Fc receptor off-signal in the B cell involves apoptosis. Journal of Immunology 157:5-11
    • (1996) Journal of Immunology , vol.157 , pp. 5-11
    • Ashman, R.F.1    Peckham, D.2
  • 3
    • 0022319106 scopus 로고
    • Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors
    • Bijsterbosch MK, Klaus GG (1985) Crosslinking of surface immunoglobulin and Fc receptors on B lymphocytes inhibits stimulation of inositol phospholipid breakdown via the antigen receptors. Journal of Experimental Medicine 162(6):1825-1836
    • (1985) Journal of Experimental Medicine , vol.162 , Issue.6 , pp. 1825-1836
    • Bijsterbosch, M.K.1    Klaus, G.G.2
  • 4
    • 0030497720 scopus 로고    scopus 로고
    • Sequential involvement of Lck and SHP-I with MHC-recognizing receptors on NK cells inhibits FcR-initiated tyrosine kinase activation
    • Binstadt BA, Brumbaugh KM et al. (1996) Sequential involvement of Lck and SHP-I with MHC-recognizing receptors on NK cells inhibits FcR-initiated tyrosine kinase activation. Immunity 5:629-638
    • (1996) Immunity , vol.5 , pp. 629-638
    • Binstadt, B.A.1    Brumbaugh, K.M.2
  • 5
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland S, Pearse R et al. (1998) SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8(4):509-516.
    • (1998) Immunity , vol.8 , Issue.4 , pp. 509-516
    • Bolland, S.1    Pearse, R.2
  • 7
    • 0030922323 scopus 로고    scopus 로고
    • A novel phosphotyrosine motif with a critical amino acid at position-2 for the SH2 domain-mediated activation of the tyrosine phosphatase SHP-1
    • Burshtyn DN, Yang W et al. (1997) A novel phosphotyrosine motif with a critical amino acid at position-2 for the SH2 domain-mediated activation of the tyrosine phosphatase SHP-1. Journal of Biological Chemistry 272:13066-13072
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 13066-13072
    • Burshtyn, D.N.1    Yang, W.2
  • 8
    • 0029082078 scopus 로고
    • Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM)
    • Cambier JC (1995) Antigen and Fc receptor signaling. The awesome power of the immunoreceptor tyrosine-based activation motif (ITAM). Journal of Immunology 155(7):3281-3285
    • (1995) Journal of Immunology , vol.155 , Issue.7 , pp. 3281-3285
    • Cambier, J.C.1
  • 10
    • 0031114872 scopus 로고    scopus 로고
    • Membrane IgM-induced tyrosine phosphorylation of CD19 requires a CD19 domain that mediates association with components of the B cell antigen receptor complex
    • Carter RH, Doody GM et al. (1997) Membrane IgM-Induced Tyrosine Phosphorylation of CD19 Requires a CD19 Domain That Mediates Association with Components of the B Cell Antigen Receptor Complex. Journal of Immunology 158:3062-3069
    • (1997) Journal of Immunology , vol.158 , pp. 3062-3069
    • Carter, R.H.1    Doody, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.