| pubmed-article:21280130 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21280130 | lifeskim:mentions | umls-concept:C0165073 | lld:lifeskim |
| pubmed-article:21280130 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:21280130 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:21280130 | lifeskim:mentions | umls-concept:C1883559 | lld:lifeskim |
| pubmed-article:21280130 | lifeskim:mentions | umls-concept:C1449651 | lld:lifeskim |
| pubmed-article:21280130 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:21280130 | pubmed:dateCreated | 2011-1-31 | lld:pubmed |
| pubmed-article:21280130 | pubmed:abstractText | The major component of neural inclusions that are the pathological hallmark of Parkinson's disease are amyloid fibrils of the protein ?-synuclein (aS). Here we investigated if the disease-related mutation A30P not only modulates the kinetics of aS aggregation, but also alters the structure of amyloid fibrils. To this end we optimized the method of quenched hydrogen/deuterium exchange coupled to NMR spectroscopy and performed two-dimensional proton-detected high-resolution magic angle spinning experiments. The combined data indicate that the A30P mutation does not cause changes in the number, location and overall arrangement of ?-strands in amyloid fibrils of aS. At the same time, several residues within the fibrillar core retain nano-second dynamics. We conclude that the increased pathogenicity related to the familial A30P mutation is unlikely to be caused by a mutation-induced change in the conformation of aS aggregates. | lld:pubmed |
| pubmed-article:21280130 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21280130 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21280130 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21280130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21280130 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21280130 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21280130 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:21280130 | pubmed:issn | 1469-896X | lld:pubmed |
| pubmed-article:21280130 | pubmed:author | pubmed-author:BeckerStefanS | lld:pubmed |
| pubmed-article:21280130 | pubmed:author | pubmed-author:ZweckstetterM... | lld:pubmed |
| pubmed-article:21280130 | pubmed:author | pubmed-author:ChoMin-KyuMK | lld:pubmed |
| pubmed-article:21280130 | pubmed:author | pubmed-author:KimHai-YoungH... | lld:pubmed |
| pubmed-article:21280130 | pubmed:author | pubmed-author:FernandezClau... | lld:pubmed |
| pubmed-article:21280130 | pubmed:copyrightInfo | Copyright © 2010 The Protein Society. | lld:pubmed |
| pubmed-article:21280130 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21280130 | pubmed:volume | 20 | lld:pubmed |
| pubmed-article:21280130 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21280130 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21280130 | pubmed:pagination | 387-95 | lld:pubmed |
| pubmed-article:21280130 | pubmed:meshHeading | pubmed-meshheading:21280130... | lld:pubmed |
| pubmed-article:21280130 | pubmed:meshHeading | pubmed-meshheading:21280130... | lld:pubmed |
| pubmed-article:21280130 | pubmed:meshHeading | pubmed-meshheading:21280130... | lld:pubmed |
| pubmed-article:21280130 | pubmed:meshHeading | pubmed-meshheading:21280130... | lld:pubmed |
| pubmed-article:21280130 | pubmed:meshHeading | pubmed-meshheading:21280130... | lld:pubmed |
| pubmed-article:21280130 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21280130 | pubmed:articleTitle | Conserved core of amyloid fibrils of wild type and A30P mutant ?-synuclein. | lld:pubmed |
| pubmed-article:21280130 | pubmed:affiliation | Department for NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, D-37077, Goettingen, Germany. | lld:pubmed |
| pubmed-article:21280130 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:6622 | entrezgene:pubmed | pubmed-article:21280130 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21280130 | lld:entrezgene |
