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Published on BioPortfolio: 2015-02-19T22:26:46-0500
RATIONALE: Biological therapies such as hu14.18-interleukin-2 fusion protein use different ways to stimulate the immune system and stop cancer cells from growing. PURPOSE: Phase I trial t...
RATIONALE: Biological therapies, such as hu14.18-interleukin-2 fusion protein, may stimulate the immune system in different ways and stop tumor cells from growing. PURPOSE: This phase II ...
Subjects with relapsed or refractory neuroblastoma will receive ex-vivo expanded and activated natural killer (NK) cells from a haploidentical donor in conjunction with the immunocytokine,...
RATIONALE: Biological therapies use different ways to stimulate the immune system and stop cancer cells from growing. Combining interleukin-2 with interleukin-12 may kill more tumor cells....
Neuroblastoma is the most common extracranial solid tumor in childhood, with nearly 50% of patients presenting with widespread metastatic disease. The current treatment for this group of h...
Interleukin-22 (IL-22), mainly produced by CD4+ T-helper subtypes and innate lymphoid cells at barrier surfaces, is found to involve in several diseases, including diabetes, rheumatoid arthritis, peri...
Neutrophils can strongly influence disease activity in cancer and in chronic inflammation. Here, we report for the first time the construction and characterization of antibody-fusion proteins featurin...
Bone-resorbing multinucleated osteoclasts that play central role in the maintenance and repair of our bones are formed from bone marrow myeloid progenitor cells by a complex differentiation process th...
The simplicity, speed, and low cost of bacterial culture make E. coli the system of choice for most initial trials of recombinant protein expression. However, many heterologous proteins are either poo...
In the fission yeast, pheromone signaling engages a signaling pathway composed of a G protein-coupled receptor, Ras, and a mitogen-activated protein kinase (MAPK) cascade that triggers sexual differen...
A receptor for INTERLEUKIN-33 that is related structurally to the interleukin-1 receptor. It contains three extracellular IMMUNOGLOBULIN-LIKE DOMAIN regions and associates with INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN upon binding IL-33 to initiate signaling. It may function in the response of HELPER T CELLS to INFLAMMATION.
An interleukin-1 receptor subtype that is involved in signaling cellular responses to INTERLEUKIN-1ALPHA and INTERLEUKIN-1BETA. The binding of this receptor to its ligand causes its favorable interaction with INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN and the formation of an activated receptor complex.
A protein that takes part in the formation of active interleukin-1 receptor complex. It binds specifically to INTERLEUKIN-1 and the INTERLEUKIN-1 RECEPTOR TYPE I at the cell surface to form a heterotrimeric complex that brings its cytoplasmic domain into contact with the cytoplasm domain of the TYPE-I INTERLEUKIN-1 RECEPTOR. Activation of intracellular signal transduction pathways from the receptor is believed to be driven by this form of cytoplasmic interaction.
An interleukin receptor subunit that was originally discovered as a component of the INTERLEUKIN 2 RECEPTOR. It was subsequently found to be a component of several other receptors including the INTERLEUKIN 4 RECEPTOR, the INTERLEUKIN 7 RECEPTOR, the INTERLEUKIN-9 RECEPTOR, the INTERLEUKIN-15 RECEPTOR, and the INTERLEUKIN-21 RECEPTOR. Mutations in the gene for the interleukin common gamma chain have been associated with X-LINKED COMBINED IMMUNODEFICIENCY DISEASES.
An interleukin-13 receptor subunit that is closely-related to the INTERLEUKIN-13 RECEPTOR ALPHA1 SUBUNIT. The receptor is found as a monomeric protein and has been considered to be a decoy receptor for interleukin-13 due the fact that it lacks cytoplasmic signaling domains.