| pubmed-article:16563356 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0241888 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0208355 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0243043 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0242656 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C1420306 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C0037628 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:16563356 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:16563356 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16563356 | pubmed:dateCreated | 2006-4-5 | lld:pubmed |
| pubmed-article:16563356 | pubmed:abstractText | Accumulation of misfolded Cu/Zn superoxide dismutase (SOD1) occurs in patients with a subgroup of familial amyotrophic lateral sclerosis (fALS). To identify the conversion of SOD1 from a normally soluble form to insoluble aggregates, we investigated the change of SOD1 solubility with aging in fALS-linked H46R SOD1 transgenic mice. Mutant SOD1 specifically altered to insoluble forms, which were sequentially separated into Triton X-100-insoluble/sodium dodecyl sulfate (SDS)-soluble and SDS-insoluble/formic acid-soluble species. In spinal cords, the levels of SDS-dissociable soluble SOD1 monomers and SDS-stable soluble dimers were significantly elevated before motor dysfunction onset. In COS-7 cells expressing H46R SOD1, treatment with proteasome inhibitors recapitulated the alteration of SOD1 solubility in transgenic mice. In contrast, overexpression of Hsp70 reduced accumulation of mutant-specific insoluble SOD1. SDS-soluble low molecular weight species of H46R SOD1 may appear as early misfolded intermediates when their concentration exceeds the capacity of the proteasome and molecular chaperones. | lld:pubmed |
| pubmed-article:16563356 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16563356 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563356 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16563356 | pubmed:month | May | lld:pubmed |
| pubmed-article:16563356 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:ChanPak HPH | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:SobueGenG | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:ItoyamaYasuto... | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:KatoMasaakiM | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:KatoTakeoT | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:WadaManabuM | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:ArawakaShigek... | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:KawanamiToruT | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:KuritaKeijiK | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:NagaiMakikoM | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:AokiMasashiM | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:KoyamaShingoS | lld:pubmed |
| pubmed-article:16563356 | pubmed:author | pubmed-author:RenChang-Hong... | lld:pubmed |
| pubmed-article:16563356 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16563356 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:16563356 | pubmed:volume | 343 | lld:pubmed |
| pubmed-article:16563356 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16563356 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16563356 | pubmed:pagination | 719-30 | lld:pubmed |
| pubmed-article:16563356 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16563356 | pubmed:meshHeading | pubmed-meshheading:16563356... | lld:pubmed |
| pubmed-article:16563356 | pubmed:meshHeading | pubmed-meshheading:16563356... | lld:pubmed |
| pubmed-article:16563356 | pubmed:meshHeading | pubmed-meshheading:16563356... | lld:pubmed |
| pubmed-article:16563356 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16563356 | pubmed:articleTitle | Alteration of familial ALS-linked mutant SOD1 solubility with disease progression: its modulation by the proteasome and Hsp70. | lld:pubmed |
| pubmed-article:16563356 | pubmed:affiliation | Department of Neurology, Hematology, Metabolism, Endocrinology and Diabetology, Yamagata University School of Medicine, 2-2-2 Iida-nishi, Yamagata 990-9585, Japan. | lld:pubmed |
| pubmed-article:16563356 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16563356 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:15511 | entrezgene:pubmed | pubmed-article:16563356 | lld:entrezgene |
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