| http://purl.uniprot.org/citations/12928483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12928483 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12928483 | http://www.w3.org/2000/01/rdf-schema#comment | "Accumulation of insoluble alpha-synuclein aggregates in the brain is characteristic of Parkinson's disease, dementia with Lewy bodies and multiple system atrophy. Although numerous studies on the aggregation properties of alpha-synuclein have been reported, little is known about its degradation so far. In view of proteolytic degradation, we have found that the serine protease neurosin (kallikrein-6) degrades alpha-synuclein and co-localizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions. In vitro study showed that neurosin prevented alpha-synuclein polymerization by reducing the amount of monomer and also by generating fragmented alpha-synucleins that themselves inhibited the polymerization. Upon cellular stress, neurosin was released from mitochondria to the cytosol, which resulted in the increase of degraded alpha-synuclein species. Down-regulation of neurosin caused accumulation of alpha-synuclein within cultured cells. Thus we concluded that neurosin plays a significant role in physiological alpha-synuclein degradation and also in the pathogenesis of synucleinopathies."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddg283"xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddg283"xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Iwata A."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Iwata A."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Tsuji S."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Tsuji S."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Maruyama M."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Maruyama M."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Kanazawa I."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Kanazawa I."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Hashikawa T."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Hashikawa T."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Akagi T."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Akagi T."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Nukina N."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/author | "Nukina N."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/date | "2003"xsd:gYear |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/pages | "2625-2635"xsd:string |
| http://purl.uniprot.org/citations/12928483 | http://purl.uniprot.org/core/pages | "2625-2635"xsd:string |