Separate Functions for the Two Modules of the Membrane-proximal Cytokine Binding Domain of Glycoprotein 190, the Leukemia Inhibitory Factor Low Affinity Receptor, in Ligand Binding and Receptor Activation-Reference-Cited by-同舟云学术

Separate Functions for the Two Modules of the Membrane-proximal Cytokine Binding Domain of Glycoprotein 190, the Leukemia Inhibitory Factor Low Affinity Receptor, in Ligand Binding and Receptor Activation

Published:2002-04 Issue:16 Volume:277 Page:13682-13692
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Voisin Mathieu-Benoı̂t,Bitard Juliette,Daburon Sophie,Moreau Jean-François,Taupin Jean-Luc

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference23 articles.

1. Leukemia inhibitory factor receptor is structurally related to the IL-6 signal transducer, gp130.

2. Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway

3. Novel neurotrophin-1/B cell-stimulating factor-3: A cytokine of the IL-6 family

4. Extracellular truncations of h beta c, the common signaling subunit for interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor (GM-CSF), and IL-5, lead to ligand-independent activation

5. A Single Tyrosine Residue in the Membrane-proximal Domain of the Granulocyte-Macrophage Colony-stimulating Factor, Interleukin (IL)-3, and IL-5 Receptor Common β-Chain Is Necessary and Sufficient for High Affinity Binding and Signaling by All Three Ligands

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