Výsledky vyhledávání - "L M, Keshvara"

Inhibition of signaling through the B cell antigen receptor by the protooncogene product, c-Cbl, requires Syk tyrosine 317 and the c-Cbl phosphotyrosine-binding domain

Autor: T M, Yankee, L M, Keshvara, S, Sawasdikosol, M L, Harrison, R L, Geahlen

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 163(11)

The Syk protein-tyrosine kinase couples the B cell Ag receptor (BCR) to intracellular biochemical pathways. Syk becomes phosphorylated on multiple tyrosine residues upon receptor cross-linking. Tyrosine 317 is a site of phosphorylation located within

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::75190958ccd2c25feaf81bd51003980b
https://pubmed.ncbi.nlm.nih.gov/10570266

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Syk- and Lyn-dependent phosphorylation of Syk on multiple tyrosines following B cell activation includes a site that negatively regulates signaling

Autor: L M, Keshvara, C C, Isaacson, T M, Yankee, R, Sarac, M L, Harrison, R L, Geahlen

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 161(10)

The Syk protein tyrosine kinase is an essential component of the B cell Ag receptor signaling pathway. Syk is phosphorylated on tyrosine following B cell activation. However, the sites that are modified and the kinases responsible for these modificat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9860ab5bffbbed9590b00aa84b55630f
https://pubmed.ncbi.nlm.nih.gov/9820500

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