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http://purl.uniprot.org/citations/18167354http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18167354http://www.w3.org/2000/01/rdf-schema#comment"Formation of intracellular aggregates is the hallmark of polyglutamine (polyQ) diseases. We analyzed the components of purified nuclear polyQ aggregates by mass spectrometry. As a result, we found that the RNA-binding protein translocated in liposarcoma (TLS) was one of the major components of nuclear polyQ aggregate-interacting proteins in a Huntington disease cell model and was also associated with neuronal intranuclear inclusions of R6/2 mice. In vitro study revealed that TLS could directly bind to truncated N-terminal huntingtin (tNhtt) aggregates but could not bind to monomer GST-tNhtt with 18, 42, or 62Q, indicating that the tNhtt protein acquired the ability to sequester TLS after forming aggregates. Thioflavin T assay and electron microscopic study further supported the idea that TLS bound to tNhtt-42Q aggregates at the early stage of tNhtt-42Q amyloid formation. Immunohistochemistry showed that TLS was associated with neuronal intranuclear inclusions of Huntington disease human brain. Because TLS has a variety of functional roles, the sequestration of TLS to polyQ aggregates may play a role in diverse pathological changes in the brains of patients with polyQ diseases."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m705306200"xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Doi H."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Machida Y."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Shimizu H."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Furukawa Y."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Okamura K."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Miyazaki H."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Bauer P.O."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Kurosawa M."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Nukina N."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Kuroiwa Y."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/author"Mitsui K."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/pages"6489-6500"xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/title"RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells."xsd:string
http://purl.uniprot.org/citations/18167354http://purl.uniprot.org/core/volume"283"xsd:string
http://purl.uniprot.org/citations/18167354http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18167354
http://purl.uniprot.org/citations/18167354http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18167354
http://purl.uniprot.org/uniprot/#_P56959-mappedCitation-18167354http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18167354
http://purl.uniprot.org/uniprot/#_Q3USY4-mappedCitation-18167354http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18167354
http://purl.uniprot.org/uniprot/#_Q564D0-mappedCitation-18167354http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18167354
http://purl.uniprot.org/uniprot/#_Q3UK30-mappedCitation-18167354http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18167354