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- W1931342651 abstract "The recently cloned ligand binding component of the type I human interferon-alpha/beta receptor (IFN-alpha/beta R) and its soluble analogue (p40) were characterized. p40 is a potent inhibitor of type I IFNs and antibodies directed against p40 completely block the activity of type I IFNs in human cells. These antibodies immunoprecipitate cellular 102-kDa (major) and 51-kDa (minor) forms of IFN-alpha/beta R. We find that the 51-kDa IFN-alpha/beta R. Two types of cDNA clones were isolated and sequenced, a 1.5-kb cDNA coding for the transmembrane 51-kDa IFN-alpha/beta R and a 4.5-kb cDNA coding for p40. In addition to ligand binding, IFN-alpha/beta R is directly involved in signaling, because it becomes phosphorylated at Tyr residues on ligand binding and it is physically associated with the cytoplasmic tyrosine kinase JAK1." @default.
- W1931342651 created "2016-06-24" @default.
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- W1931342651 date "1995-05-01" @default.
- W1931342651 modified "2023-09-27" @default.
- W1931342651 title "Soluble and membrane-anchored forms of the human IFN-α/β receptor" @default.
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- W1931342651 doi "https://doi.org/10.1002/jlb.57.5.712" @default.
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