| pubmed-article:17573347 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C0285890 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C1548779 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C1947902 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C2827499 | lld:lifeskim |
| pubmed-article:17573347 | lifeskim:mentions | umls-concept:C1167624 | lld:lifeskim |
| pubmed-article:17573347 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:17573347 | pubmed:dateCreated | 2007-8-20 | lld:pubmed |
| pubmed-article:17573347 | pubmed:abstractText | The misfolding and fibril formation of alpha-synuclein plays an important role in neurodegenerative diseases such as Parkinson disease. Here we used electron paramagnetic resonance spectroscopy, together with site-directed spin labeling, to investigate the structural features of alpha-synuclein fibrils. We generated fibrils from a total of 83 different spin-labeled derivatives and observed single-line, exchange-narrowed EPR spectra for the majority of all sites located within the core region of alpha-synuclein fibrils. Such exchange narrowing requires the orbital overlap between multiple spin labels in close contact. The core region of alpha-synuclein fibrils must therefore be arranged in a parallel, in-register structure wherein same residues from different molecules are stacked on top of each other. This parallel, in-register core region extends from residue 36 to residue 98 and is tightly packed. Only a few sites within the core region, such as residues 62-67 located at the beginning of the NAC region, as well as the N- and C-terminal regions outside the core region, are significantly less ordered. Together with the accessibility measurements that suggest the location of potential beta-sheet regions within the fibril, the data provide significant structural constraints for generating three-dimensional models. Furthermore, the data support the emerging view that parallel, in-register structure is a common feature shared by a number of naturally occurring amyloid fibrils. | lld:pubmed |
| pubmed-article:17573347 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17573347 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17573347 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17573347 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17573347 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17573347 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17573347 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17573347 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17573347 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17573347 | pubmed:author | pubmed-author:LangenRalfR | lld:pubmed |
| pubmed-article:17573347 | pubmed:author | pubmed-author:MargittaiMart... | lld:pubmed |
| pubmed-article:17573347 | pubmed:author | pubmed-author:ChenJeannieJ | lld:pubmed |
| pubmed-article:17573347 | pubmed:author | pubmed-author:DannW JWJ | lld:pubmed |
| pubmed-article:17573347 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17573347 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:17573347 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17573347 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17573347 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17573347 | pubmed:pagination | 24970-9 | lld:pubmed |
| pubmed-article:17573347 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
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| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:meshHeading | pubmed-meshheading:17573347... | lld:pubmed |
| pubmed-article:17573347 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17573347 | pubmed:articleTitle | Investigation of alpha-synuclein fibril structure by site-directed spin labeling. | lld:pubmed |
| pubmed-article:17573347 | pubmed:affiliation | Department of Molecular Pharmacology and Toxicology, School of Pharmacy, University of Southern California, Los Angeles, California 90033, USA. | lld:pubmed |
| pubmed-article:17573347 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17573347 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:17573347 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:6622 | entrezgene:pubmed | pubmed-article:17573347 | lld:entrezgene |
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