Source:http://linkedlifedata.com/resource/pubmed/id/20078424
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2010-4-1
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pubmed:abstractText |
Protein aggregation is a major contributor to the pathogenic mechanisms of human neurodegenerative diseases. Mutations in the CSTB (cystatin B) gene [StB (stefin B)] cause EPM1 (progressive myoclonus epilepsy of type 1), an epilepsy syndrome with features of neurodegeneration and increased oxidative stress. Oligomerization and aggregation of StB in mammalian cells have recently been reported. It has also been observed that StB is overexpressed after seizures and in certain neurodegenerative conditions, which could potentially lead to its aggregation. Human StB proved to be a good model system to study amyloid fibril formation in vitro and, as we show here, to study protein aggregation in cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1768-322X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
319-34
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pubmed:dateRevised |
2011-1-21
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pubmed:meshHeading |
pubmed-meshheading:20078424-Autophagy,
pubmed-meshheading:20078424-Blotting, Western,
pubmed-meshheading:20078424-Cell Line, Tumor,
pubmed-meshheading:20078424-Cell Separation,
pubmed-meshheading:20078424-Cell Survival,
pubmed-meshheading:20078424-Cystatin B,
pubmed-meshheading:20078424-Cytoplasm,
pubmed-meshheading:20078424-Flow Cytometry,
pubmed-meshheading:20078424-Humans,
pubmed-meshheading:20078424-Microscopy, Confocal,
pubmed-meshheading:20078424-Microscopy, Electron, Transmission,
pubmed-meshheading:20078424-Microscopy, Fluorescence,
pubmed-meshheading:20078424-Proteasome Endopeptidase Complex,
pubmed-meshheading:20078424-Transfection
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pubmed:year |
2010
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pubmed:articleTitle |
Intracellular aggregation of human stefin B: confocal and electron microscopy study.
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pubmed:affiliation |
Department of Biochemistry, Molecular and Structural Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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