| pubmed-article:17046663 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17046663 | lifeskim:mentions | umls-concept:C0699748 | lld:lifeskim |
| pubmed-article:17046663 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
| pubmed-article:17046663 | lifeskim:mentions | umls-concept:C0870071 | lld:lifeskim |
| pubmed-article:17046663 | lifeskim:mentions | umls-concept:C0384782 | lld:lifeskim |
| pubmed-article:17046663 | pubmed:dateCreated | 2006-10-18 | lld:pubmed |
| pubmed-article:17046663 | pubmed:abstractText | A growing number of human neurodegenerative diseases are associated with disruption of cellular protein folding homeostasis, leading to the appearance of misfolded proteins and deposition of protein aggregates and inclusions. Recent years have been witness to widespread development of invertebrate systems (specifically Drosophila and Caenorhabditis elegans) to model these disorders, bringing the many advantages of such systems, particularly the power of genetic analysis in a metazoan, to bear on these problems. In this chapter, we describe our studies using the nematode, C. elegans, as a model to study polyglutamine expansions as occur in Huntington's disease and related ataxias. Using fluorescently tagged polyglutamine repeats of different lengths, we have examined the dynamics of aggregate formation both within individual cells and over time throughout the lifetime of individual organisms, identifying aging as an important physiological determinant of aggregation and toxicity. Expanding on these observations, we demonstrate that a genetic pathway regulating longevity can alter the time course of aging-related polyglutamine-mediated phenotypes. To identify novel targets and better understand how cells sense and respond to the appearance of misfolded and aggregation-prone proteins, we use a genome-wide RNA interference-based genetic screen to identify modifiers of age-dependent polyglutamine aggregation. Throughout these studies, we used fluorescence-based, live-cell biological and biophysical methods to study the behavior of these proteins in a complex multicellular environment. | lld:pubmed |
| pubmed-article:17046663 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17046663 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17046663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17046663 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17046663 | pubmed:issn | 0076-6879 | lld:pubmed |
| pubmed-article:17046663 | pubmed:author | pubmed-author:MorimotoRicha... | lld:pubmed |
| pubmed-article:17046663 | pubmed:author | pubmed-author:MorleyJames... | lld:pubmed |
| pubmed-article:17046663 | pubmed:author | pubmed-author:BrignullHeath... | lld:pubmed |
| pubmed-article:17046663 | pubmed:author | pubmed-author:GarciaSusana... | lld:pubmed |
| pubmed-article:17046663 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17046663 | pubmed:volume | 412 | lld:pubmed |
| pubmed-article:17046663 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17046663 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17046663 | pubmed:pagination | 256-82 | lld:pubmed |
| pubmed-article:17046663 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:meshHeading | pubmed-meshheading:17046663... | lld:pubmed |
| pubmed-article:17046663 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17046663 | pubmed:articleTitle | Modeling polyglutamine pathogenesis in C. elegans. | lld:pubmed |
| pubmed-article:17046663 | pubmed:affiliation | Department of Biochemistry, Molecular Biology, and Cell Biology, Rice Institute for Biomedical Research, Northwestern University, Evanston, Illinois 60208, USA. | lld:pubmed |
| pubmed-article:17046663 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17046663 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17046663 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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