| http://purl.uniprot.org/citations/20202083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20202083 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutations in Cu/Zn superoxide dismutase (SOD1) gene cause familial amyotrophic lateral sclerosis (ALS), which could be attributed to the toxic properties of the misfolded protein, oxidative stress, and mitochondrial dysfunction. DJ-1 - a causative agent of familial Parkinson's disease PARK7 - is responsible for inducing antioxidative reaction. In this study, we showed the up-regulation of DJ-1 protein levels in mutant SOD1 transgenic mice through the lifespan were observed in the motor neurons. We demonstrated biochemically DJ-1 formed complexes with mutant SOD1 in the cell lysates. Furthermore, DJ-1 over-expression resulted in increased cell viability and reduced cell toxicity in mutant SOD1-transfected neuronal cells, because of improvement in apoptotic pathway and reduction in oxidative stress levels. We also evaluated DJ-1 levels in CSF collected from sporadic ALS patients and controls subjects. The CSF DJ-1 levels were significantly higher in patients with sporadic ALS than in control subjects. These results show that DJ-1 may be associated with sporadic and familial ALS pathogenesis. Therefore, insight into the effects of DJ-1 on mutant SOD1-mediated toxicity may provide a therapeutic advance for the treatment of motor neuron degeneration in ALS."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1471-4159.2010.06658.x"xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Kimura E."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Mita S."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Maeda Y."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Mori A."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Yamashita S."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Hirano T."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/author | "Uchino M."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/name | "J Neurochem"xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/pages | "860-870"xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/title | "DJ-1 forms complexes with mutant SOD1 and ameliorates its toxicity."xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://purl.uniprot.org/core/volume | "113"xsd:string |
| http://purl.uniprot.org/citations/20202083 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20202083 |
| http://purl.uniprot.org/citations/20202083 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/20202083 |
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| http://purl.uniprot.org/uniprot/#_P00441-mappedCitation-20202083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20202083 |
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| http://purl.uniprot.org/uniprot/#_Q99LX0-mappedCitation-20202083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20202083 |
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| http://purl.uniprot.org/uniprot/#_X5CN18-mappedCitation-20202083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20202083 |
| http://purl.uniprot.org/uniprot/#_W8Q444-mappedCitation-20202083 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/20202083 |