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The interleukin-1 receptor

Immunology Today, 1987
One of the pivotal events in the initiation of inflammatory responses is activation of both resident tissue macrophages at the site of damage and circulating monocytes infiltrating the area. The activated macrophages release a group of factors which influence inflammation and tissue regulation.
S K, Dower, D L, Urdal
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INTERLEUKIN-1 RECEPTOR ANTAGONIST

Rheumatic Disease Clinics of North America, 1998
There are three members of the IL-1 gene family: IL-1 alpha, IL-1 beta, and IL-1ra, IL-1 alpha, and IL-1 beta are both antagonist molecules with many proinflammatory effects. IL-1ra is an antagonist molecule that can inhibit the effect of IL-1 alpha and IL-1 beta by specifically blocking the IL-1 receptor on target effector cells.
B, Bresnihan, G, Cunnane
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The interleukin-1 receptor family

Seminars in Immunology, 2006
The cytokines IL-1 and IL-18 are key molecules both in the innate and in the adaptive immune response. Their activity is mediated by specific receptors present on the membrane of target cells. It has become apparent that these receptors are members of a larger family of related receptors, most of which are apparently involved in the mechanisms of host ...
Boraschi D, Tagliabue A
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Interleukin-1 Receptors

1995
Abstract The human type I IL-1 receptor is predicted from the cDNA sequence to be a protein of 569 amino acids (GenBank accession number M27492; mouse, M20658; rat, M95578; chicken, M81846) (Sims et al. 1989). It contains a 20-aminoacid signal peptide, an extracellular region of 317 amino acids, a single 22-amino-acid transmembrane ...
J E, Sims, S K, Dower
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The interleukin 1 receptor family

Developmental & Comparative Immunology, 2004
Interleukin-1 is a key inflammatory cytokine that mediates its effects through a type I receptor and a receptor accessory protein. These two molecules are members of a wider family of proteins that have in common the presence of immunoglobulin domains in the extracellular region of the protein and a TIR domain in the cytoplasmic region.
Sumathi, Subramaniam   +2 more
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Nuclear internalisation and DNA binding activities of interleukin-1, interleukin-1 receptor and interleukin-1/receptor complexes

Biochemical and Biophysical Research Communications, 1992
This paper presents evidence to suggest that interleukin-1 alpha as a complex with its receptor is able to express DNA binding activity. Both the interleukin-1/receptor complex and the interleukin-1 receptor appear to be able to bind to DNA, however interleukin-1 on its own showed no binding activity. Interleukin-1 was found to be internalised into the
M N, Weitzmann, N, Savage
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Interleukin-1 receptor antagonist: effectiveness against interleokin-1 fever

Canadian Journal of Physiology and Pharmacology, 1992
Conscious cats were used to examine the effectiveness of the interleukin-1 receptor antagonist against the fever induced by interleukin-1 and endotoxin. Although inactive by itself, the antagonist (three 1-μg bolus injections at 10-min intervals), injected into the third ventricle, attenuated the febrile response to a subsequent ...
COCEANI, Flavio   +3 more
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Interleukin-1 Receptor Antagonist

1993
IL-1ra is the first described naturally occurring receptor antagonist of any cytokine or hormone-like molecule. IL-1ra is a member of the IL-1 family by three criteria: amino acid sequence homology of 26 to 30% to IL-1 beta and 19% to IL-1 alpha; similarities in gene structure; and common gene localization to human chromosome 2q14.
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Regulation of bovine interleukin-1 receptors

Veterinary Immunology and Immunopathology, 1998
Interleukin-1 is a key player in inflammation and the immune response. The interleukin-1 family consists of three ligands (IL-1 alpha, IL-1 beta, and the IL-1 receptor antagonist) and two receptors (IL-1RI and IL-1RII). Previous studies suggest a dynamic relationship among these receptors and ligands that regulates the magnitude and extent of IL-1 ...
P W, Yu   +8 more
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Interleukin-1 receptor antagonist activity of a human interleukin-1 inhibitor

Nature, 1990
Three interleukin-1 inhibitors have been purified to homogeneity from medium conditioned by human monocytes. Partial sequence analysis and digestion with N-glycanase indicate that these are glycosylation forms of a single protein. The protein binds to the interleukin-1 receptor but has no interleukin-1-like activity, even at very high concentrations ...
C H, Hannum   +9 more
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