ArticleProceedings of the National Academy of Sciences of the United States of America1998
Interaction affinity between cytokine receptor components on the cell surface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 39 citations in OpenAlex.
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- The anti-Müllerian hormone prodomain is displaced from the hormone/prodomain complex upon bivalent binding to the hormone receptor.The Journal of biological chemistry · 2022Article
- Immune signalling by supramolecular assemblies.Immunology · 2018Review
- A novel dynamic multicellular co-culture system for studying individual blood-brain barrier cell types in brain diseases and cytotoxicity testing.Scientific reports · 2018Article
- Immunomodulatory and antitumor effects of type I interferons and their application in cancer therapy.Oncotarget · 2017Review
- Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments.Nature communications · 2017Article
- A Generic Mechanism for Enhanced Cytokine Signaling via Cytokine-Neutralizing Antibodies.PloS one · 2016Article
- Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.The Journal of cell biology · 2015Article
- Quantitative measurement of the target-mediated internalization kinetics of biopharmaceuticals.Pharmaceutical research · 2015Article
- Dynamics and interaction of interleukin-4 receptor subunits in living cells.Biophysical journal · 2014Article
- Determining the affinity and stoichiometry of interactions between unmodified proteins in solution using Biacore.Analytical biochemistry · 2013Article
- Structural and dynamic determinants of type I interferon receptor assembly and their functional interpretation.Immunological reviews · 2012Review
- Single cell analysis of ligand binding and complex formation of interleukin-4 receptor subunits.Biophysical journal · 2011Article
- Fundamental aspects of protein-protein association kinetics.Chemical reviews · 2009Review
- Combinatorial Signal Transduction Responses Mediated by Interleukin-2 and -4 Receptors in a Helper TCellular and molecular bioengineering · 2008Article
- Determination of the two-dimensional interaction rate constants of a cytokine receptor complex.Biophysical journal · 2006Article
- Inquiring into the differential action of interferons (IFNs): an IFN-alpha2 mutant with enhanced affinity to IFNAR1 is functionally similar to IFN-beta.Molecular and cellular biology · 2006Article
- Lateral ligand-receptor interactions on membranes probed by simultaneous fluorescence-interference detection.Biophysical journal · 2005Article
- 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
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The anti-common gamma chain (gammac) mAb CP.B8 is shown to inhibit interleukin 4 (IL-4)-dependent proliferation of phytohemagglutinin (PHA) activated T cells noncompetitively with respect to cytokine by blocking the IL-4-induced heterodimerization of IL-4Ralpha and gammac receptor chains. Affinities for the binding of IL-4 to Cos-7 cells transfected with huIL-4Ralpha, and to PHA blasts expressing both IL-4Ralpha and gammac, were used to estimate the affinity of the key interaction between gammac and the binary IL-4Ralpha.IL-4 complex on the cell surface. This affinity was defined in terms of the dimensionless ratio [IL-4Ralpha.IL-4.gammac]/[IL-4Ralpha.IL-4], which we designate KR. The results show that on PHA blasts this interaction is relatively weak; KR approximately 9, implying that approximately 10% of the limiting IL-4Ralpha chain remains free of gammac even at saturating concentrations of IL-4. This quantitative treatment establishes KR as a key measure of the coupling between ligand binding and receptor activation, providing a basis for functional distinctions between different receptors that are activated by ligand-induced receptor dimerization.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.