pubmed-article:19583442 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0033164 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0087111 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0003290 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C1415587 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0182400 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0041405 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:19583442 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:19583442 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:19583442 | pubmed:dateCreated | 2009-7-8 | lld:pubmed |
pubmed-article:19583442 | pubmed:abstractText | Tricyclic aromatic compounds (TCA) are promising candidates for treatment of transmissible spongiform encephalopathies. Direct binding to the cellular prion protein (PrP(C)) has been proposed as anti-prion active mechanism. We here show by means of NMR-spectroscopy that binding of TCA occurs with millimolar affinity to motifs consisting of two neighboring aromatic residues (Ar-Ar motif). It is independent of the secondary structure of this motif and of the side chain attached to the TCA and it is not specific to PrP(C). Because biologically inactive 9-aminoacridine (9-aa) binds with similar K(D) as anti-prion active quinacrine, direct interaction with PrP(C) as mechanism of action appears highly unlikely. However, binding of 9-aa to Ar-Ar-motifs in proteins can be used as reporter for biological macromolecule interactions, by measuring changes in T(1)-NMR relaxation times of 9-aa. | lld:pubmed |
pubmed-article:19583442 | pubmed:language | eng | lld:pubmed |
pubmed-article:19583442 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19583442 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19583442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19583442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19583442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19583442 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19583442 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19583442 | pubmed:month | Oct | lld:pubmed |
pubmed-article:19583442 | pubmed:issn | 1538-0254 | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:WillboldDiete... | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:SchweimerKris... | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:FrankAndreas... | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:SchwarzingerS... | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:KorthCarstenC | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:RöschPaulP | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:ZieglerJanJ | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:MangelsChrist... | lld:pubmed |
pubmed-article:19583442 | pubmed:author | pubmed-author:KlingensteinR... | lld:pubmed |
pubmed-article:19583442 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:19583442 | pubmed:volume | 27 | lld:pubmed |
pubmed-article:19583442 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:19583442 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:19583442 | pubmed:pagination | 163-70 | lld:pubmed |
pubmed-article:19583442 | pubmed:meshHeading | pubmed-meshheading:19583442... | lld:pubmed |
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pubmed-article:19583442 | pubmed:meshHeading | pubmed-meshheading:19583442... | lld:pubmed |
pubmed-article:19583442 | pubmed:year | 2009 | lld:pubmed |
pubmed-article:19583442 | pubmed:articleTitle | Binding of TCA to the prion protein: mechanism, implication for therapy, and application as probe for complex formation of bio-macromolecules. | lld:pubmed |
pubmed-article:19583442 | pubmed:affiliation | Department of Biopolymers, University of Bayreuth, 95440 Bayreuth, Germany. | lld:pubmed |
pubmed-article:19583442 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:19583442 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:5621 | entrezgene:pubmed | pubmed-article:19583442 | lld:entrezgene |
http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:19583442 | lld:entrezgene |