A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
about
Three residues in the common beta chain of the human GM-CSF, IL-3 and IL-5 receptors are essential for GM-CSF and IL-5 but not IL-3 high affinity binding and interact with Glu21 of GM-CSFHuman interleukin-3 (IL-3) induces disulfide-linked IL-3 receptor alpha- and beta-chain heterodimerization, which is required for receptor activation but not high-affinity bindingRefined crystal structure and mutagenesis of human granulocyte-macrophage colony-stimulating factorActivating point mutations in the common beta subunit of the human GM-CSF, IL-3 and IL-5 receptors suggest the involvement of beta subunit dimerization and cell type-specific molecules in signallingBinding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteinsIdentification and characterization of a functional promoter region in the human eosinophil IL-5 receptor alpha subunit geneReceptor epitope usage by an interleukin-5 mimetic peptide.Mutagenesis in the C-terminal region of human interleukin 5 reveals a central patch for receptor alpha chain recognition.Expression analysis of thirty one Y chromosome genes in human prostate cancer.Role of pulmonary alveolar macrophages in defense of the lung against Pseudomonas aeruginosaPotent interleukin 3 receptor agonist with selectively enhanced hematopoietic activity relative to recombinant human interleukin 3A discontinuous eight-amino acid epitope in human interleukin-3 binds the alpha-chain of its receptor.The receptor binding site of human interleukin-3 defined by mutagenesis and molecular modeling.Crucial role of the residue R280 at the F'-G' loop of the human granulocyte/macrophage colony-stimulating factor receptor alpha chain for ligand recognitionInterleukin-3 signals through multiple isoforms of Stat5.Saturation mutagenesis of human interleukin-3.Interleukin-5 receptor subunit oligomerization and rearrangement revealed by fluorescence resonance energy transfer imagingConformation of four peptides corresponding to the alpha-helical segments of human GM-CSF.Slow-dissociation effect of common signaling subunit beta c on IL5 and GM-CSF receptor assembly.Dysregulated hematopoiesis and a progressive neurological disorder induced by expression of an activated form of the human common beta chain in transgenic mice.Metastatic lymph node 51 and fibroblast-like synoviocyte hyperproliferation in rheumatoid arthritis pathogenesis.Reconstitution of a high affinity binding site for type I interferons.Detailed analysis of the IL-5-IL-5R alpha interaction: characterization of crucial residues on the ligand and the receptor.Cytokine receptor genes: structure, chromosomal location, and involvement in human disease.Interferon response pathways--a paradigm for cytokine signalling?Functional replacement of cytokine receptor extracellular domains by leucine zippers.Interacting residues in the extracellular region of the common beta subunit of the human granulocyte-macrophage colony-stimulating factor, interleukin (IL)-3, and IL-5 receptors involved in constitutive activation.Interleukin 5 interactions with soluble and cell surface forms of its receptor.Receptor binding properties of four-helix-bundle growth factors deduced from electrostatic analysis.Interleukin-3 and interleukin-6 stimulate bovine adrenal cortisol secretion through different pathways.A single tyrosine residue in the membrane-proximal domain of the granulocyte-macrophage colony-stimulating factor, interleukin (IL)-3, and IL-5 receptor common beta-chain is necessary and sufficient for high affinity binding and signaling by all thrMolecular determinants of the granulocyte-macrophage colony-stimulating factor receptor complex assembly.Characterization of the Stat5 protease.Molecular modeling of the GM-CSF and IL-3 receptor complexes.Homology model of human interferon-alpha 8 and its receptor complex.Identification of an antigenic domain near the C terminus of human granulocyte-macrophage colony-stimulating factor and its spatial localization.Kinetic interaction analysis of human interleukin 5 receptor alpha mutants reveals a unique binding topology and charge distribution for cytokine recognition.Granulocyte macrophage colony-stimulating factor in adenomyosis and autologous endometrium.
P2860
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P2860
A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
1993年學術文章
@zh
1993年學術文章
@zh-hant
name
A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
@en
type
label
A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
@en
prefLabel
A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
@en
P2093
P2860
P1476
A model for the interaction of the GM-CSF, IL-3 and IL-5 receptors with their ligands.
@en
P2093
P2860
P356
10.3109/08977199309046929
P577
1993-01-01T00:00:00Z