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http://purl.uniprot.org/citations/18230341http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18230341http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18230341http://www.w3.org/2000/01/rdf-schema#comment"Wnts are secreted glycoproteins that regulate important cellular processes including proliferation, differentiation, and cell fate. In the beta-catenin/canonical pathway, Wnt interacts with Fzd receptors to inhibit degradation of beta-catenin and promote its translocation into the nucleus where it regulates transcription of a number of genes. Dysregulation of this pathway has been attributed to a host of diseases including cancer. As a result, components of the beta-catenin/canonical pathway have been gaining recognition as promising targets for the discovery of novel therapeutic agents. Here, we show, using an ELISA-based protein-protein binding assay that purified Wnt7a binds to the extracellular cysteine-rich domain of Fzd5 in the nanomolar range. We have developed a novel split eGFP complementation assay to visually detect Wnt7a-Fzd5 interactions and subsequent pathway activation in cells. These biological tools could help lead to a better understanding of Wnt-Fzd interactions and the identification of new modulators of Wnt signaling."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2008.01.088"xsd:string
http://purl.uniprot.org/citations/18230341http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2008.01.088"xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/author"Loose D.S."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/author"Loose D.S."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/author"Carmon K.S."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/author"Carmon K.S."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/pages"285-291"xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/pages"285-291"xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/title"Wnt7a interaction with Fzd5 and detection of signaling activation using a split eGFP."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/title"Wnt7a interaction with Fzd5 and detection of signaling activation using a split eGFP."xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/volume"368"xsd:string
http://purl.uniprot.org/citations/18230341http://purl.uniprot.org/core/volume"368"xsd:string
http://purl.uniprot.org/citations/18230341http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18230341
http://purl.uniprot.org/citations/18230341http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18230341
http://purl.uniprot.org/citations/18230341http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18230341
http://purl.uniprot.org/citations/18230341http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18230341
http://purl.uniprot.org/uniprot/P24383http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18230341
http://purl.uniprot.org/uniprot/Q13467http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/18230341