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http://purl.uniprot.org/citations/12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12757932http://www.w3.org/2000/01/rdf-schema#comment"Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 is associated with an elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system and co-immunoprecipitation experiments, we have found that p80 coilin, coiled body-specific protein, binds to ataxin-1. In further experiments with deletion mutants, we found that the C-terminal regions of ataxin-1 and p80 coilin were essential for this interaction. In HeLa cells that have been co-transfected with ataxin-1 and p80 coilin, the p80 coilin protein co-localizes with ataxin-1 aggregates in the nucleoplasm. However, immunohistochemical analysis and immunofluorescence assays showed that mutant ataxin-1 aggregates do not redistribute p80 coilin's dot-like structures in the Purkinje cells of SCA1 transgenic mice. This feature of the interaction between ataxin-1 and p80 coilin suggests that p80 coilin might be implicated in altering the function of ataxin-1."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.org/dc/terms/identifier"doi:10.1016/s0925-4439(03)00038-3"xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/author"Hong S."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/author"Kang S."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/author"Kim S."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/author"Park Y."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/author"Ka S."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/pages"35-42"xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/title"p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product."xsd:string
http://purl.uniprot.org/citations/12757932http://purl.uniprot.org/core/volume"1638"xsd:string
http://purl.uniprot.org/citations/12757932http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12757932
http://purl.uniprot.org/citations/12757932http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12757932
http://purl.uniprot.org/uniprot/P38432#attribution-90FFC42EE20A37A0C0653C2E7EBB0D05http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/#_P54253-mappedCitation-12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/#_L0EPB8-mappedCitation-12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/#_P38432-mappedCitation-12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/#_Q96C81-mappedCitation-12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/#_Q96FF1-mappedCitation-12757932http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/Q96FF1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/P38432http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/L0EPB8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12757932
http://purl.uniprot.org/uniprot/P54253http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12757932