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- W2044336492 abstract "Many cellular recognition events in the immune system are initiated by aggregation of cell surface receptors that lack intrinsic protein-tyrosine kinase activity. Receptor-associated kinases related to the src protooncogene product have been found to be essential for cellular activation and may interact with the cytoplasmic domains of the antigen receptor chains. We show here that anti-CD16 antibody-mediated clustering of chimeric transmembrane proteins bearing a CD16 extracellular domain and a Src family kinase intracellular domain is not sufficient to initiate a cellular activation signal in T cells, whereas clustering of similar chimeras bearing Syk or ZAP-70 kinase sequences triggers calcium mobilization. Aggregation of the Syk chimera alone, or coaggregation of chimeras bearing Fyn and ZAP-70 kinases, suffices to initiate cytolytic effector function. The pattern of tyrosine phosphorylation induced by clustering of the Syk chimera is similar to the pattern induced by aggregation of T cell receptor." @default.
- W2044336492 created "2016-06-24" @default.
- W2044336492 creator A5012137496 @default.
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- W2044336492 creator A5090399098 @default.
- W2044336492 date "1993-07-01" @default.
- W2044336492 modified "2023-09-26" @default.
- W2044336492 title "T cell activation by clustered tyrosine kinases" @default.
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- W2044336492 doi "https://doi.org/10.1016/0092-8674(93)90304-9" @default.
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