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- W2023497492 abstract "The Fc receptor (FcR) γ subunit was originally discovered as a homodimeric subunit of the high-affinity IgE receptor (FcεRI). But it was recently found to be a common signal-generating subunit of Fc receptors including IgG Fc receptors (FcγRs) and IgA Fc receptor (FcαR), and furthermore to generate a signal also with stimuli through non-immune receptors. In addition, it plays an essential role in cell-surface expression of the FcεRI and the FcγRIIIA isoform and also regulates cell-surface expression and ligand-binding affinity of the FcγRI. In this report, we addressed the possibility that the FcRγ could affect the correct folding of the IgE-binding region of the FcεRIα subunit by using the chimeric receptor molecules constructed from human FcεRIα and FcRγ. Furthermore, we demonstrated that the seven amino acid residues in the C-terminal region on the extracellular domain of the FcεRIα were essential for maintaining the IgE-binding activity of the FcεRIα exodomain on the cell membrane andor may affect the correct folding of the α subunit itself within the cell." @default.
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- W2023497492 date "1998-08-01" @default.
- W2023497492 modified "2023-09-26" @default.
- W2023497492 title "Analysis of BTK mutations in greek patients with X-linked agammaglobulinaemia" @default.
- W2023497492 doi "https://doi.org/10.1016/s0161-5890(98)90382-0" @default.
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