ArticleProtein science : a publication of the Protein Society1995
Direct evidence of a heterotrimeric complex of human interleukin-4 with its receptors.
Article in Protein science : a publication of the Protein Society, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Structural biology of shared cytokine receptors.Annual review of immunology · 2009Review
- Effects of the geometry of the immunological synapse on the delivery of effector molecules.Biophysical journal · 2004Article
- Characterization of a soluble ternary complex formed between human interferon-beta-1a and its receptor chains.Protein science : a publication of the Protein Society · 1999Article
- Evidence for the formation of a heterotrimeric complex of leukaemia inhibitory factor with its receptor subunits in solution.The Biochemical journal · 1997Article
Corrections and comments
- Erratum issued
Authors and funding
10 authors.
Funding
Abstract
The mode of binding of interleukin-4 (IL-4) to its two known receptors, specific receptor IL-4R and a shared receptor gamma c, was investigated using gel filtration and gel electrophoresis. A ternary complex between IL-4 and the soluble domains of the two receptors was shown to exist in solution. The association constant between gamma c and the stable complex of IL-4/sIL-4R is in the millimolar range, making the ternary complex a feasible target for crystallization studies.
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Registered trials
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