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| pubmed-article:15894486 | lifeskim:mentions | umls-concept:C1706817 | lld:lifeskim |
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| pubmed-article:15894486 | lifeskim:mentions | umls-concept:C0449774 | lld:lifeskim |
| pubmed-article:15894486 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:15894486 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:15894486 | lifeskim:mentions | umls-concept:C0185027 | lld:lifeskim |
| pubmed-article:15894486 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:15894486 | pubmed:dateCreated | 2005-10-24 | lld:pubmed |
| pubmed-article:15894486 | pubmed:abstractText | Lewy bodies (LBs) are the characteristic inclusions of Parkinson's disease brain but the mechanism responsible for their formation is obscure. Lewy bodies (LBs) are composed of a number of proteins of which alpha-synuclein (alpha-SYN) is a major constituent. In this study, we have investigated the distribution patterns of synphilin-1 and parkin proteins in control and sporadic PD brain tissue by immunohistochemistry (IH), immunoblotting, and immunoelectron microscopy (IEM). We demonstrate the presence of synphilin-1 and parkin in the central core of a majority of LBs using IH and IEM. Using IH, we show an overlapping distribution profile of the two proteins in central neurons. Additionally, we show sensitivity of both endogenous synphilin-1 and parkin to proteolytic dysfunction and their co-localization in aggresomes formed in response to the proteasome inhibitor MG-132. We confirm that synphilin-1 and parkin are components of majority of LBs in Parkinson's disease and that both proteins are susceptible to proteasomal degradation. | lld:pubmed |
| pubmed-article:15894486 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15894486 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15894486 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15894486 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:15894486 | pubmed:issn | 0969-9961 | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:HarveyRobert... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:WoodNicholas... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:LeesAndrew... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:LatchmanDavid... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:EngelenderSim... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:Schlossmacher... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:HarveyKirsten... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:KilfordLindaL | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:BandopadhyayR... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:KingsburyAnn... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:ReidAndrew... | lld:pubmed |
| pubmed-article:15894486 | pubmed:author | pubmed-author:MuqitMiratul... | lld:pubmed |
| pubmed-article:15894486 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15894486 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:15894486 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15894486 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15894486 | pubmed:pagination | 401-11 | lld:pubmed |
| pubmed-article:15894486 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15894486 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15894486 | pubmed:articleTitle | Synphilin-1 and parkin show overlapping expression patterns in human brain and form aggresomes in response to proteasomal inhibition. | lld:pubmed |
| pubmed-article:15894486 | pubmed:affiliation | Reta Lila Weston Institute of Neurological Studies, Royal Free and UCL Medical School, The Windeyer Building, 46 Cleveland Street, London W1T 4JF, UK. regtrib@ucl.ac.uk | lld:pubmed |
| pubmed-article:15894486 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15894486 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15894486 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15894486 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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