http://purl.uniprot.org/citations/23435380 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23435380 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/23435380 | http://www.w3.org/2000/01/rdf-schema#comment | "SIX1 interacts with EYA to form a bipartite transcription factor essential for mammalian development. Loss of function of this complex causes branchio-oto-renal (BOR) syndrome, whereas re-expression of SIX1 or EYA promotes metastasis. Here we describe the 2.0-Å structure of SIX1 bound to EYA2, which suggests a new DNA-binding mechanism for SIX1 and provides a rationale for the effect of BOR syndrome mutations. The structure also reveals that SIX1 uses predominantly a single helix to interact with EYA. Substitution of a single amino acid in this helix is sufficient to disrupt SIX1-EYA interaction, SIX1-mediated epithelial-mesenchymal transition and metastasis in mouse models. Given that SIX1 and EYA are overexpressed in many tumor types, our data indicate that targeting the SIX1-EYA complex may be a potent approach to inhibit tumor progression in multiple cancer types."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb.2505"xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.org/dc/terms/identifier | "doi:10.1038/nsmb.2505"xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Zhao R."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Zhao R."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Chen X.S."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Chen X.S."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Smith A.L."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Smith A.L."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Patrick A.N."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Patrick A.N."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Cabrera J.H."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Cabrera J.H."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Ford H.L."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/author | "Ford H.L."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/name | "Nat. Struct. Mol. Biol."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/pages | "447-453"xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/pages | "447-453"xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/title | "Structure-function analyses of the human SIX1-EYA2 complex reveal insights into metastasis and BOR syndrome."xsd:string |
http://purl.uniprot.org/citations/23435380 | http://purl.uniprot.org/core/title | "Structure-function analyses of the human SIX1-EYA2 complex reveal insights into metastasis and BOR syndrome."xsd:string |