http://purl.uniprot.org/citations/18374598 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18374598 | http://www.w3.org/2000/01/rdf-schema#comment | "Granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin (IL)-3 and IL-5 are related cytokines that play key roles in regulating the differentiation, proliferation, survival and activation of myeloid blood cells. The cell surface receptors for these cytokines are composed of cytokine-specific alpha-subunits and a common beta-receptor (betac), a shared subunit that is essential for receptor signaling in response to GM-CSF, IL-3 and IL-5. Previous studies have reached conflicting conclusions as to whether N-glycosylation of the betac-subunit is necessary for functional GM-CSF, IL-3 and IL-5 receptors. We sought to clarify whether betac N-glycosylation plays a role in receptor function, since all structural studies of human betac to date have utilized recombinant protein lacking N-glycosylation at Asn(328). Here, by eliminating individual N-glycans in human betac and the related murine homolog, beta(IL-3), we demonstrate unequivocally that ligand-binding and receptor activation are not critically dependent on individual N-glycosylation sites within the beta-subunit although the data do not preclude the possibility that N-glycans may exert some sort of fine control. These studies support the biological relevance of the X-ray crystal structures of the human betac domain 4 and the complete ectodomain, both of which lack N-glycosylation at Asn(328)."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cyto.2008.02.010"xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Chen J."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Olsen J.E."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Young I.G."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Murphy J.M."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Mirza S."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Ford S.C."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/author | "Soboleva T.A."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/name | "Cytokine"xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/pages | "234-242"xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/title | "Clarification of the role of N-glycans on the common beta-subunit of the human IL-3, IL-5 and GM-CSF receptors and the murine IL-3 beta-receptor in ligand-binding and receptor activation."xsd:string |
http://purl.uniprot.org/citations/18374598 | http://purl.uniprot.org/core/volume | "42"xsd:string |
http://purl.uniprot.org/citations/18374598 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18374598 |
http://purl.uniprot.org/citations/18374598 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18374598 |
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