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http://purl.uniprot.org/citations/9931497http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9931497http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9931497http://www.w3.org/2000/01/rdf-schema#comment"We have cloned and functionally characterised the mouse orthologue of the P2X4 receptor, mP2X4, and a splice variant of this receptor, mP2X4a. mP2X4 is 388 amino acids in length and shares 94% and 87% identity with the rat and human P2X4 receptors, respectively, while mP2X4a is 361 amino acids in length and lacks a 27-amino acid region in the extracellular domain corresponding to exon 6 of the known P2X receptor gene structures. When expressed in Xenopus laevis oocytes, mP2X4 produces a rapid inward current in response to ATP with an EC50 of 1.68+/-0.2 microM, consistent with the affinity of the rat and human P2X4 receptors for ATP. This agonist response is potentiated by the P2X receptor antagonists suramin, Reactive blue 2 and, over a limited concentration range, by PPADS. Although mP2X4a forms a poorly functional homomeric receptor, it appears able to interact with the full-length mP2X4 subunit to result in a functional channel with a reduced affinity for ATP. These results suggest a possible role for splice variants of P2X receptors in the formation of functional heteromeric ion channels."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.org/dc/terms/identifier"doi:10.1016/S0169-328X(98)00328-3"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.org/dc/terms/identifier"doi:10.1016/s0169-328x(98)00328-3"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Townsend-Nicholson A."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Townsend-Nicholson A."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"King B.F."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"King B.F."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Burnstock G."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Burnstock G."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Wildman S.S."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/author"Wildman S.S."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/name"Brain Res. Mol. Brain Res."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/name"Brain Res Mol Brain Res"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/pages"246-254"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/pages"246-254"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/title"Molecular cloning, functional characterization and possible cooperativity between the murine P2X4 and P2X4a receptors."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/title"Molecular cloning, functional characterization and possible cooperativity between the murine P2X4 and P2X4a receptors."xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/9931497http://purl.uniprot.org/core/volume"64"xsd:string
http://purl.uniprot.org/citations/9931497http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9931497
http://purl.uniprot.org/citations/9931497http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9931497