Linked Life Data

14610069

Source:http://linkedlifedata.com/resource/pubmed/id/14610069

Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:14610069rdf:typepubmed:Citationlld:pubmed
pubmed-article:14610069lifeskim:mentionsumls-concept:C0033164lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0035820lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0205147lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1948066lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0002716lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0003995lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0017797lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C0205341lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1514562lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1883221lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1879748lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1706853lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1883204lld:lifeskim
pubmed-article:14610069lifeskim:mentionsumls-concept:C1880389lld:lifeskim
pubmed-article:14610069pubmed:issue5lld:pubmed
pubmed-article:14610069pubmed:dateCreated2004-1-26lld:pubmed
pubmed-article:14610069pubmed:abstractTextThe yeast prion protein Ure2 forms amyloid-like filaments in vivo and in vitro. This ability depends on the N-terminal prion domain, which contains Asn/Gln repeats, a motif thought to cause human disease by forming stable protein aggregates. The Asn/Gln region of the Ure2p prion domain extends to residue 89, but residues 15-42 represent an island of "normal" random sequence, which is highly conserved in related species and is relatively hydrophobic. We compare the time course of structural changes monitored by thioflavin T (ThT) binding fluorescence and atomic force microscopy for Ure2 and a series of prion domain mutants under a range of conditions. Atomic force microscopy height images at successive time points during a single growth experiment showed the sequential appearance of at least four fibril types that could be readily differentiated by height (5, 8, 12, or 9 nm), morphology (twisted or smooth), and/or time of appearance (early or late in the plateau phase of ThT binding). The Ure2 dimer (h = 2.6 +/- 0.5 nm) and granular particles corresponding to higher order oligomers (h = 4-12 nm) could also be detected. The mutants 15Ure2 and Delta 15-42Ure2 showed the same time-dependent variation in fibril types but with an increased lag time detected by ThT binding compared with wild-type Ure2. In addition, Delta 15-42Ure2 showed reduced binding to ThT. The results imply a role of the conserved region in both amyloid nucleation and formation of the binding surface recognized by ThT. Further, Ure2 amyloid formation is a multistep process via a series of fibrillar intermediates.lld:pubmed
pubmed-article:14610069pubmed:languageenglld:pubmed
pubmed-article:14610069pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:citationSubsetIMlld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:14610069pubmed:statusMEDLINElld:pubmed
pubmed-article:14610069pubmed:monthJanlld:pubmed
pubmed-article:14610069pubmed:issn0021-9258lld:pubmed
pubmed-article:14610069pubmed:authorpubmed-author:FoàVVlld:pubmed
pubmed-article:14610069pubmed:authorpubmed-author:PerrettSarahSlld:pubmed
pubmed-article:14610069pubmed:authorpubmed-author:LiZhuZlld:pubmed
pubmed-article:14610069pubmed:authorpubmed-author:JiangYiYlld:pubmed
pubmed-article:14610069pubmed:authorpubmed-author:ZhouJun-MeiJMlld:pubmed
pubmed-article:14610069pubmed:issnTypePrintlld:pubmed
pubmed-article:14610069pubmed:day30lld:pubmed
pubmed-article:14610069pubmed:volume279lld:pubmed
pubmed-article:14610069pubmed:ownerNLMlld:pubmed
pubmed-article:14610069pubmed:authorsCompleteYlld:pubmed
pubmed-article:14610069pubmed:pagination3361-9lld:pubmed
pubmed-article:14610069pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:meshHeadingpubmed-meshheading:14610069...lld:pubmed
pubmed-article:14610069pubmed:year2004lld:pubmed
pubmed-article:14610069pubmed:articleTitleAmyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domains.lld:pubmed
pubmed-article:14610069pubmed:affiliationNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.lld:pubmed
pubmed-article:14610069pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:14610069pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
entrez-gene:855492entrezgene:pubmedpubmed-article:14610069lld:entrezgene
http://linkedlifedata.com/r...entrezgene:pubmedpubmed-article:14610069lld:entrezgene
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:14610069lld:pubmed