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http://purl.uniprot.org/citations/12767830http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12767830http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12767830http://www.w3.org/2000/01/rdf-schema#comment"Dof is a large molecule essential for signal transduction by the two FGF receptors in Drosophila. It contains two ankyrin repeats and a coiled-coil region, but has no other recognisable structural motif. Dof shares these features with its closest vertebrate relatives, the B-cell signalling molecules BCAP and BANK. In addition, this family of proteins shares a region of homology upstream of the ankyrin repeats, which we call the Dof/BCAP/BANK (DBB) motif. We have identified 44 proteins that interact with Dof in a yeast two-hybrid screen. These include the Drosophila FGF-receptor Heartless and Dof itself. We show that the integrity of the DBB motif is required both for Dof and for BCAP to form dimers. Analysis of the interactions between a set of deletion constructs of Dof and the panel of interactors suggests that Dof may adopt different conformations, with a folded conformation stabilized by interactions between the DBB motif and the C-terminal part of the protein."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.org/dc/terms/identifier"doi:10.1016/s0022-2836(03)00489-3"xsd:string
http://purl.uniprot.org/citations/12767830http://purl.org/dc/terms/identifier"doi:10.1016/s0022-2836(03)00489-3"xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Wilson R."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Wilson R."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Battersby A."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Battersby A."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Csiszar A."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Csiszar A."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Leptin M."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/author"Leptin M."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/pages"479-493"xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/pages"479-493"xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/title"Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/title"Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP."xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/volume"329"xsd:string
http://purl.uniprot.org/citations/12767830http://purl.uniprot.org/core/volume"329"xsd:string
http://purl.uniprot.org/citations/12767830http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12767830
http://purl.uniprot.org/citations/12767830http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12767830