| http://purl.uniprot.org/citations/21182262 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21182262 | http://www.w3.org/2000/01/rdf-schema#comment | "The Wnt/β-catenin signaling pathway is critical to embryonic development as well as adult tissue regeneration. Dysregulation of this pathway can lead to a variety of human diseases, in particular cancers. Chibby (Cby), a small and highly conserved protein, plays an antagonistic role in Wnt signaling by inhibiting the binding of β-catenin to Tcf/Lef family proteins, a protein interaction that is essential for the transcriptional activation of Wnt target genes. Cby is also involved in regulating intracellular distribution of β-catenin. Phosphorylated Cby forms a ternary complex with 14-3-3 protein and β-catenin, facilitating the export of β-catenin from the nucleus. On the other hand, the antagonistic function of Cby is inhibited upon binding to thyroid cancer-1 (TC-1). To dissect the structure-function relationship of Cby, we have used NMR spectroscopy, ESI-MS, CD, and DLS to extensively characterize the structure of human Cby. Our results show that the 126-residue Cby is partially disordered under nondenaturing conditions. While the N-terminal portion of the protein is predominantly unstructured in solution, the C-terminal half of Cby adopts a coiled-coil structure through self-association. Initial data for the binding studies of Cby to 14-3-3ζ (one of the isoforms in the 14-3-3 family) and TC-1 via these two distinct structural modules have also been obtained. It is noteworthy that in a recent large-scale analysis of the intrinsically disordered proteome of mouse, a substantial number of disordered proteins are predicted to have coiled-coil motif presence in their sequences. The combination of these two molecular recognition features could facilitate disordered Cby in assembling protein complexes via different modes of interaction."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi101236z"xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/author | "Yu C."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/author | "Choy W.Y."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/author | "Brickenden A."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/author | "Mokhtarzada S."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/pages | "715-726"xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/title | "Structural characterization of partially disordered human Chibby: insights into its function in the Wnt-signaling pathway."xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://purl.uniprot.org/core/volume | "50"xsd:string |
| http://purl.uniprot.org/citations/21182262 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21182262 |
| http://purl.uniprot.org/citations/21182262 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21182262 |
| http://purl.uniprot.org/uniprot/Q9Y3M2#attribution-3490B7A9E36413A10421AA0C7C81BB28 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/21182262 |
| http://purl.uniprot.org/uniprot/#_Q9Y3M2-mappedCitation-21182262 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21182262 |
| http://purl.uniprot.org/uniprot/Q9Y3M2 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21182262 |