Viewing negative mentions of binding of cd3g (X. laevis) in T cells

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Thomassen et al. (2006)CD3T-cellAlthough the introduction of wild type CD3gamma and CD3gamma (78Y-F) fully restored T-cell receptor assembly and expression, the introduction of CD3gamma (82C-S), CD3gamma (85C-S), and CD3gamma (76Q-E) all resulted in an impaired association between CD3gamma and CD3 and a lack of cell-surface expressed CD3gamma.
De Lau et al. (1992)CD3T cellsThis hybrid hybridoma (quadroma)-produced bsAb binds as a monomeric molecule to CD3+ CD8+ but not CD3+ CD4+ T cells.
Breittmayer et al. (1989)CD3T cellsBy flow cytometric analysis of the binding of this mAb to Jurkat T cells and peripheral blood lymphocytes we showed that 141 does not recognize the CD3 complex when external Ca2+ is chelated by EGTA.
Lai et al. (2000)CD3T-cellImmunologic characterization of these cells revealed positivity for CD3, CD5, CD45RO, CD56, and T-cell intracellular antigen (TIA), and negativity for CD2, CD3, CD4, CD8, CD57, CD34, and terminal deoxynucleotidyl transferase (TdT).
Guyot et al. (1996)CD3T-cellWe demonstrate that CD2 receptor engagement, but not CD3 crosslinking, induces apoptosis in lymphocytes transformed by human T-cell lymphotrophic virus type I (HTLV-I).
Yang et al. (1997)CD3T cellsIn contrast to other Bcl-x isoforms, cells that fail to express Bcl-x gamma after CD3 ligation undergo programmed cell death, while activated T cells that express Bcl-x gamma are spared.
Nonoyama et al. (1989)CD3T lymphocytesCD3-, CD3bright+ cells and peripheral blood T lymphocytes did not bind, but they were induced to bind by neuramidase treatment All these bindings were inhibited by anti-LFA-1 mAb and anti-CD2 mAb.
Roosnek et al. (1990)CD3T cellCells activated by linking T cell receptor (TcR)/CD3 to MHC class I antigens could not be activated by cross-linking the MHC and TcR/CD3 structures separately.
Ritz et al. (1988)CD3T cellTaken together, these findings provide strong evidence that NKH1+CD3- NK clones do not interact with target cells through a T cell receptor-like structure.