http://purl.uniprot.org/citations/15936276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15936276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15936276 | http://www.w3.org/2000/01/rdf-schema#comment | "Ligand-gated ion channels are transmembrane proteins that respond to a variety of transmitters, including acetylcholine, gamma-aminobutyric acid (GABA), glycine, and glutamate [1 and 2]. These proteins play key roles in neurotransmission and are typically found in the nervous system and at neuromuscular junctions [3]. Recently, acetylcholine receptor family members also have been found in nonneuronal cells, including macrophages [4], keratinocytes [5], bronchial epithelial cells [5], and endothelial cells of arteries [6]. The function of these channels in nonneuronal cells in mammals remains to be elucidated, though it has been shown that the acetylcholine receptor alpha7 subunit is required for acetylcholine-mediated inhibition of tumor necrosis factor release by activated macrophages [4]. We show that cup-4, a gene required for efficient endocytosis of fluids by C. elegans coelomocytes, encodes a protein that is homologous to ligand-gated ion channels, with the highest degree of similarity to nicotinic acetylcholine receptors. Worms lacking CUP-4 have reduced phosphatidylinositol 4,5-bisphosphate levels at the plasma membrane, suggesting that CUP-4 regulates endocytosis through modulation of phospholipase C activity."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cub.2005.04.057"xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.cub.2005.04.057"xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Dang H."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Dang H."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Greenwald I."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Greenwald I."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Fares H."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Fares H."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Knuth S."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Knuth S."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Patton A."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Patton A."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Schaheen B."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/author | "Schaheen B."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/name | "Curr. Biol."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/name | "Curr. Biol."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/pages | "1045-1050"xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/pages | "1045-1050"xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/title | "Endocytosis function of a ligand-gated ion channel homolog in Caenorhabditis elegans."xsd:string |
http://purl.uniprot.org/citations/15936276 | http://purl.uniprot.org/core/title | "Endocytosis function of a ligand-gated ion channel homolog in Caenorhabditis elegans."xsd:string |