| pubmed-article:15909996 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0006784 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0285890 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0699900 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0243125 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
| pubmed-article:15909996 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:15909996 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:15909996 | pubmed:dateCreated | 2005-5-24 | lld:pubmed |
| pubmed-article:15909996 | pubmed:abstractText | Alpha-synuclein (alpha-syn) is a major protein component of the neuropathological hallmarks of Parkinson's disease and related neurodegenerative disorders termed synucleinopathies. Neither the mechanism of alpha-syn fibrillization nor the degradative process for alpha-syn has been elucidated. Previously, we showed that wild-type, mutated, and fibrillar alpha-syn proteins are substrates of calpain I in vitro. In this study, we demonstrate that calpain-mediated cleavage near and within the middle region of soluble alpha-syn with/without tyrosine nitration and oxidation generates fragments that are unable to self-fibrillize. More importantly, these fragments prevent full-length alpha-syn from fibrillizing. Calpain-mediated cleavage of alpha-syn fibrils composed of wild-type or nitrated alpha-syn generate C-terminally truncated fragments that retain their fibrillar structure and induce soluble full-length alpha-syn to co-assemble. Therefore, calpain-cleaved soluble alpha-syn inhibits fibrillization, whereas calpain-cleaved fibrillar alpha-syn promotes further co-assembly. These results provide insight into possible disease mechanisms underlying synucleinopathies since the formation of alpha-syn fibrils could be causally linked to the onset/progression of these disorders. | lld:pubmed |
| pubmed-article:15909996 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15909996 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15909996 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15909996 | pubmed:month | May | lld:pubmed |
| pubmed-article:15909996 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:LeeVirginia... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:TrojanowskiJo... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:Ischiropoulos... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:LynchDavid... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:HodaraRoberto... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:GiassonBenoit... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:NorrisErin... | lld:pubmed |
| pubmed-article:15909996 | pubmed:author | pubmed-author:Mishizen-Eber... | lld:pubmed |
| pubmed-article:15909996 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15909996 | pubmed:day | 31 | lld:pubmed |
| pubmed-article:15909996 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:15909996 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15909996 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15909996 | pubmed:pagination | 7818-29 | lld:pubmed |
| pubmed-article:15909996 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:15909996 | pubmed:meshHeading | pubmed-meshheading:15909996... | lld:pubmed |
| pubmed-article:15909996 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15909996 | pubmed:articleTitle | Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein. | lld:pubmed |
| pubmed-article:15909996 | pubmed:affiliation | Department of Neurology, University of Pennsylvania and The Children's Hospital of Philadelphia, Philadelphia, Pennsylvania 19104, USA. | lld:pubmed |
| pubmed-article:15909996 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15909996 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15909996 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15909996 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15909996 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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