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http://purl.uniprot.org/citations/25028513http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25028513http://www.w3.org/2000/01/rdf-schema#comment"Multiple system atrophy (MSA) is a neurodegenerative disease caused by α-synuclein aggregation in oligodendrocytes and neurons. Using a transgenic mouse model overexpressing human α-synuclein in oligodendrocytes, we previously demonstrated that oligodendrocytic α-synuclein inclusions induce neuronal α-synuclein accumulation and progressive neuronal degeneration. α-Synuclein binds to β-III tubulin, leading to the neuronal accumulation of insoluble α-synuclein in an MSA mouse model. The present study demonstrates that α-synuclein co-localizes with β-III tubulin in the brain tissue from patients with MSA and MSA model transgenic mice as well as neurons cultured from these mice. Accumulation of insoluble α-synuclein in MSA mouse neurons was blocked by the peptide fragment β-III tubulin (residues 235-282). We have determined the α-synuclein-binding domain of β-III tubulin and demonstrated that a short fragment containing this domain can suppress α-synuclein accumulation in the primary cultured cells. Administration of a short α-synuclein-binding fragment of β-III tubulin may be a novel therapeutic strategy for MSA."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m114.557215"xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/author"Suzuki Y."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/author"Jin C."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/author"Yazawa I."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/author"Iwase T."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/pages"24374-24382"xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/title"beta-III Tubulin fragments inhibit alpha-synuclein accumulation in models of multiple system atrophy."xsd:string
http://purl.uniprot.org/citations/25028513http://purl.uniprot.org/core/volume"289"xsd:string
http://purl.uniprot.org/citations/25028513http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/25028513
http://purl.uniprot.org/citations/25028513http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/25028513
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http://purl.uniprot.org/uniprot/#_D5MR34-mappedCitation-25028513http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/#_O55042-mappedCitation-25028513http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/#_Q9CRT0-mappedCitation-25028513http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/#_Q9ERD7-mappedCitation-25028513http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/O55042http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/Q9ERD7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/A0A1D5RM76http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/Q9CRT0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25028513
http://purl.uniprot.org/uniprot/D5MR34http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/25028513