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Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase.

Data up to Jan 2025

Published1994
Citations180
References17

Total Citations Per Year

Abstract

References (17)

Complete structure and expression in transfected cells of high affinity IgE receptor

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Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases

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Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor gamma chain after receptor aggregation.

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Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation.

1994 • 194 citations

Larger oligomers of IgE are more effective than dimers in stimulating rat basophilic leukemia cells.

1980 • 151 citations

Protein-tyrosine phosphorylation: an essential component of FcεRI signaling

1992 • 141 citations

Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity.

1994 • 135 citations

Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha.

1994 • 127 citations

Further characterization of the β-component of the receptor for immunoglobulin E

1982 • 106 citations

Qualitative characteristics of histamine release from human basophils by covalently cross-linked IgE.

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Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn… (1994) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer