Components of signalization pathway of IL-1R which are involved in cellular response to IL-1 also mediate responses to other cytokines (IL-18 and IL-33), Toll-like receptors (TLRs), and many forms of cytotoxic stress.
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::Evaluation of novel immune-based therapies using interferons, GM-CSF, G-CSF, thalidomide, IL-2, IL-12, cyclosporin (CsA), prednisone, cytotoxic agents, therapeutic immunization
The mutations cause expression of a defective α chain or complete absence thereof, an essential part of high-affinity interleukin-2 (IL-2) receptors.
The fused BCR-ABL protein interacts with the interleukin 3beta(c) receptor subunit.
The protein encoded by this gene is an accessory subunit of the heterodimeric receptor for IL18.
The protein encoded by this gene belongs to the class II cytokine receptor family, and has been shown to be a receptor for interleukin 22 (IL22).
IL-10 is capable of inhibiting synthesis of pro-inflammatory cytokines such as IFN-γ, IL-2, IL-3, TNFα and GM-CSF made by cells such as macrophages and regulatory T-cells.
Interleukin 12 receptor, beta 2 subunit(IL12Rβ2) is a product of the IL12-R β2 gene.
It was initially called T cell growth factor, but the name was changed in 1978 to IL-2 (interleukin-2) by the Interlaken cytokine nomenclature committee.
Interleukin 27 receptor, alpha subunit has been shown to interact with STAT1.
The IL-1 receptor accessory protein (IL1RAP) is a transmembrane protein that interacts with IL-1R and is required for IL-1 signal transduction.
In fact, the β-subunit of the IL-5 receptor is also found in IL-3 and GM-CSF receptors where it is associated with IL-3Rα and GM-CSFRα subunits respectively.
IRAK-4 (interleukin-1 receptor-associated kinase 4), in the IRAK family, is a protein kinase involved in signaling innate immune responses from Toll-like receptors.
This protein heterodimerizes with interleukin 6 signal transducer to form the type II oncostatin M receptor and with interleukin 31 receptor A to form the interleukin 31 receptor, and thus transduces oncostatin M and interleukin 31 induced signaling events.
TIRAP, toll-interleukin 1 receptor domain containing adaptor protein
Interleukin 6 and its receptor were discovered and cloned at Osaka University, Japan, by Tadamitsu Kishimoto in the 1980s.