The alpha subunit of the human IgE receptor (FcERI) is sufficient for high affinity IgE binding.

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Functional Expression of the High Affinity Receptor for IgE (FceRI) in Human Platelets and Its’ Intracellular Expression in Human Megakaryocytes

The high affinity IgE receptor (FceRI) expressed on the cell surface of mast cells and basophils is the key molecule in triggering the IgE-mediated allergic reaction. Recently, it was elucidated that the FceRI is expressed on a variety of other cells like Langerhans cells, monocytes, and eosinophils, and the functional importance of the FceRI expression in Langerhans cells was also shown. Some ...

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Crystal Structure of the Human High-Affinity IgE Receptor

Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 A resolutio...

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Atopy phenotype in subjects with variants of the b subunit of the high affinity IgE receptor

b) at this chromosome 11q location and atopy by maternal descent. The identification of this Background – FceRI plays a central role in atopy, thus genetic variants of FceRI-b variant DNA has proved problematic, perhaps because of protein/DNA binding at the site, may alter receptor function to enhance atopic responses and may manifest as a but the variants we report have been confirmed by direc...

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Atopy phenotype in subjects with variants of the beta subunit of the high affinity IgE receptor.

BACKGROUND Fc epsilon RI plays a central role in atopy, thus genetic variants of Fc epsilon RI-beta may alter receptor function to enhance atopic responses and may manifest as a more severe atopic phenotype and more symptomatic atopic disease. The immunological and clinical features of atopy in children with and without the Leu 181 variant of Fc epsilon RI-beta were compared. METHODS Sixty Br...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1990

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)45670-0