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http://purl.uniprot.org/citations/10911369http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10911369http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10911369http://www.w3.org/2000/01/rdf-schema#comment"Syndecan-4, a member of the syndecan gene family of proteoglycans, is an important regulator of bFGF signaling. In particular, bFGF-dependent regulation of cell growth and migration has been linked to syndecan-4 cytoplasmic domain-mediated interactions. Screening of a yeast two-hybrid library with a cytoplasmic domain of rat syndecan-4 identified a novel binding partner, here termed synectin. Synectin is highly homologous to semaphorin F binding protein semcap1, glucose 1 transporter binding protein glut1cbp, and RGS-GAIP/neuropilin-1 binding protein GIPC. Overexpression of synectin in ECV304 cells in culture led to a dose-dependent inhibition of migration while not affecting cell adhesion or growth rate. We conclude that synectin is involved in syndecan-4-dependent interactions and may play a role in the assembly of syndecan-4 signaling complex."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.org/dc/terms/identifier"doi:10.1002/1097-4652(200009)184:3<373::aid-jcp12>3.0.co;2-i"xsd:string
http://purl.uniprot.org/citations/10911369http://purl.org/dc/terms/identifier"doi:10.1002/1097-4652(200009)184:3<373::aid-jcp12>3.0.co;2-i"xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Chen W."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Chen W."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Gao Y."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Gao Y."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Simons M."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/author"Simons M."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/name"J. Cell. Physiol."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/name"J. Cell. Physiol."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/pages"373-379"xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/pages"373-379"xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/title"Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/title"Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration."xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/10911369http://purl.uniprot.org/core/volume"184"xsd:string
http://purl.uniprot.org/citations/10911369http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10911369
http://purl.uniprot.org/citations/10911369http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10911369