Identification of a Phospholipase C-γ1 (PLC-γ1) SH3 Domain-Binding Site in SLP-76 Required for T-Cell Receptor-Mediated Activation of PLC-γ1 and NFAT
By D. Yablonski, T. Kadlecek, A. Weiss. Molecular and Cellular Biology, 2001
196 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/9ac580f3ca37a32953730afc042c40810eb0bd93
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In Immunology
In Molecular Biology
Citations in the corpus
- T cell receptor ligation induces the formation of dynamically regulated signaling assemblies (2002, background): “…exchange factor Vav, the adapter Nck, and the Tec-family tyrosine kinase Itk (Wu et al., 1996; Bubeck Wardenburg et al., 1998; Bunnell et al., 2000; Yablonski et al., 2001). c-Cbl, an adapter and ubiquitin ligase, also associates with LAT, although by an undefined mechanism (Zhang et al., 1998a).”
- Recruitment and activation of PLCγ1 in T cells: a new insight into old domains (2006, background): “Several studies have demonstrated that the SH3 domain of PLCg1 can also bind other proline-rich domain-containing proteins, including Slp76 (Yablonski et al, 2001), Sos (Kim et al, 2000), Itk (Perez-Villar and Kanner, 1999) and PIKE (Ye et al, 2002).”