| pubmed-article:21318130 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21318130 | lifeskim:mentions | umls-concept:C0002716 | lld:lifeskim |
| pubmed-article:21318130 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:21318130 | lifeskim:mentions | umls-concept:C0596788 | lld:lifeskim |
| pubmed-article:21318130 | lifeskim:mentions | umls-concept:C0025938 | lld:lifeskim |
| pubmed-article:21318130 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:21318130 | pubmed:dateCreated | 2011-2-14 | lld:pubmed |
| pubmed-article:21318130 | pubmed:abstractText | Clusters of GM1 gangliosides act as platforms for conformational transition of monomeric, unstructured amyloid ? (A?) to its toxic ?-structured aggregates. We have previously shown that A?(1-40) accommodated on the hydrophobic/hydrophilic interface of lyso-GM1 or GM1 micelles assumes ?-helical structures under ganglioside-excess conditions. For better understanding of the mechanisms underlying the ?-to-? conformational transition of A? on GM1 clusters, we performed spectroscopic characterization of A?(1-40) titrated with GM1. It was revealed that the thioflavin T- (ThT-) reactive ?-structure is more populated in A?(1-40) under conditions where the A?(1-40) density on GM1 micelles is high. Under this circumstance, the C-terminal hydrophobic anchor Val(39)-Val(40) shows two distinct conformational states that are reactive with ThT, while such A? species were not generated by smaller lyso-GM1 micelles. These findings suggest that GM1 clusters promote specific A?-A? interactions through their C-termini coupled with formation of the ThT-reactive ?-structure depending on sizes and curvatures of the clusters. | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21318130 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21318130 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:21318130 | pubmed:issn | 2090-0252 | lld:pubmed |
| pubmed-article:21318130 | pubmed:author | pubmed-author:KatoKoichiK | lld:pubmed |
| pubmed-article:21318130 | pubmed:author | pubmed-author:YanagisawaKat... | lld:pubmed |
| pubmed-article:21318130 | pubmed:author | pubmed-author:MatsuoKoichiK | lld:pubmed |
| pubmed-article:21318130 | pubmed:author | pubmed-author:GekkoKunihiko... | lld:pubmed |
| pubmed-article:21318130 | pubmed:author | pubmed-author:Yagi-UtsumiMa... | lld:pubmed |
| pubmed-article:21318130 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21318130 | pubmed:volume | 2011 | lld:pubmed |
| pubmed-article:21318130 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21318130 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21318130 | pubmed:pagination | 925073 | lld:pubmed |
| pubmed-article:21318130 | pubmed:dateRevised | 2011-7-25 | lld:pubmed |
| pubmed-article:21318130 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:21318130 | pubmed:articleTitle | Spectroscopic Characterization of Intermolecular Interaction of Amyloid ? Promoted on GM1 Micelles. | lld:pubmed |
| pubmed-article:21318130 | pubmed:affiliation | Graduate school of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan. | lld:pubmed |
| pubmed-article:21318130 | pubmed:publicationType | Journal Article | lld:pubmed |
