Cargando…
IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases
Interleukin 5 (IL-5) induces proliferation and differentiation of B cells and eosinophils by interacting with its receptor (IL-5R) which consists of two distinct polypeptide chains, alpha and beta (beta c). Although both IL-5R alpha and beta c lack a kinase catalytic domain, IL- 5 is capable of indu...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1994
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191779/ https://www.ncbi.nlm.nih.gov/pubmed/7525847 |
Ejemplares similares
-
The protein product of the c-cbl protooncogene is phosphorylated after B cell receptor stimulation and binds the SH3 domain of Bruton's tyrosine kinase
Publicado: (1995) -
Regulatory Phosphorylation of Ikaros by Bruton's Tyrosine Kinase
por: Ma, Hong, et al.
Publicado: (2013) -
Paralog-Specific Patterns of Structural Disorder and Phosphorylation in the Vertebrate SH3–SH2–Tyrosine Kinase Protein Family
por: Dos Santos, Helena G., et al.
Publicado: (2016) -
SH2 domains: modulators of nonreceptor tyrosine kinase activity
por: Filippakopoulos, Panagis, et al.
Publicado: (2009) -
SH3 Domain Tyrosine Phosphorylation – Sites, Role and Evolution
por: Tatárová, Zuzana, et al.
Publicado: (2012)