pubmed-article:18406354 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0150369 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1948066 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0001898 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0205341 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1418237 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C0206243 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:18406354 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:18406354 | pubmed:issue | 11 | lld:pubmed |
pubmed-article:18406354 | pubmed:dateCreated | 2008-5-9 | lld:pubmed |
pubmed-article:18406354 | pubmed:abstractText | Intranuclear fibrils due to poly-alanine expansions in the N-terminal domain of the poly(A) binding protein PABPN1 correlate with the disease oculopharyngeal muscular dystrophy (OPMD). For monitoring fibril formation by fluorescence and real-time NMR spectroscopy, tryptophans were introduced either into the middle or C-terminal of the poly-alanine segment. The kinetics of fibril formation which were monitored by fluorescence spectroscopy were matched by real-time NMR kinetics. Our results show that fibril formation is concomitant with the burial of the tryptophans in the fibrillar core. Since no soluble pre-fibrillar intermediate(s) was detected, fibril formation of this domain may be regarded as a two state conversion from an unfolded soluble into folded insoluble species. | lld:pubmed |
pubmed-article:18406354 | pubmed:language | eng | lld:pubmed |
pubmed-article:18406354 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18406354 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18406354 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18406354 | pubmed:month | May | lld:pubmed |
pubmed-article:18406354 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:PiverJ SJS | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:BalbachJochen... | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:SchwarzElisab... | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:SackewitzMirk... | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:LodderstedtGr... | lld:pubmed |
pubmed-article:18406354 | pubmed:author | pubmed-author:RohrbergJulia... | lld:pubmed |
pubmed-article:18406354 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18406354 | pubmed:day | 14 | lld:pubmed |
pubmed-article:18406354 | pubmed:volume | 582 | lld:pubmed |
pubmed-article:18406354 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18406354 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18406354 | pubmed:pagination | 1587-92 | lld:pubmed |
pubmed-article:18406354 | pubmed:meshHeading | pubmed-meshheading:18406354... | lld:pubmed |
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pubmed-article:18406354 | pubmed:meshHeading | pubmed-meshheading:18406354... | lld:pubmed |
pubmed-article:18406354 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18406354 | pubmed:articleTitle | Monitoring fibril formation of the N-terminal domain of PABPN1 carrying an alanine repeat by tryptophan fluorescence and real-time NMR. | lld:pubmed |
pubmed-article:18406354 | pubmed:affiliation | Institute for Biochemistry and Biotechnology of the Martin-Luther-University Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120 Halle, Germany. | lld:pubmed |
pubmed-article:18406354 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18406354 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18406354 | lld:pubmed |