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- W1973304887 abstract "Great progress has recently been made in structural and functional research of phospholipase C (PLC)-β. We now understand how PLC-β isoforms (β1-β4) are activated by GTP-bound Gαq downstream of G protein-coupled receptors. Numerous studies indicate that PLC-βs participate in the differentiation and activation of immune cells that control both the innate and adaptive immune systems. The PLC-β3 isoform also interplays with tyrosine kinase-based signaling pathways, to inhibit Stat5 activation by recruiting the protein-tyrosine phosphatase SHP-1, with which PLC-β3 and Stat5 form a multi-molecular signaling platform, named SPS complex. The SPS complex has important regulatory roles in tumorigenesis and immune cell activation." @default.
- W1973304887 created "2016-06-24" @default.
- W1973304887 creator A5048781927 @default.
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- W1973304887 date "2013-09-01" @default.
- W1973304887 modified "2023-10-16" @default.
- W1973304887 title "Phospholipase C-β in immune cells" @default.
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- W1973304887 doi "https://doi.org/10.1016/j.jbior.2013.08.001" @default.
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