| pubmed-article:20568734 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C0235032 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C0486805 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C0598002 | lld:lifeskim |
| pubmed-article:20568734 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:20568734 | pubmed:issue | 30 | lld:pubmed |
| pubmed-article:20568734 | pubmed:dateCreated | 2010-7-29 | lld:pubmed |
| pubmed-article:20568734 | pubmed:abstractText | Oligomeric forms of amyloid beta-protein (Abeta) are key neurotoxins in Alzheimer's disease (AD). Previously, we found that C-terminal fragments (CTFs) of Abeta42 interfered with assembly of full-length Abeta42 and inhibited Abeta42-induced toxicity. To decipher the mechanism(s) by which CTFs affect Abeta42 assembly and neurotoxicity, here, we investigated the interaction between Abeta42 and CTFs using photoinduced cross-linking and dynamic light scattering. The results demonstrate that distinct parameters control CTF inhibition of Abeta42 assembly and Abeta42-induced toxicity. Inhibition of Abeta42-induced toxicity was found to correlate with stabilization of oligomers with a hydrodynamic radius (R(H)) of 8-12 nm and attenuation of formation of oligomers with an R(H) of 20-60 nm. In contrast, inhibition of Abeta42 paranucleus formation correlated with CTF solubility and the degree to which CTFs formed amyloid fibrils themselves but did not correlate with inhibition of Abeta42-induced toxicity. Our findings provide important insight into the mechanisms by which different CTFs inhibit the toxic effect of Abeta42 and suggest that stabilization of nontoxic Abeta42 oligomers is a promising strategy for designing inhibitors of Abeta42 neurotoxicity. | lld:pubmed |
| pubmed-article:20568734 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20568734 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20568734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20568734 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20568734 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:20568734 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:BisekJ PJP | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:LomakinAlekse... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:BenedekGeorge... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:LiHuiyuanH | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:XieCui-WeiCW | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:TanMiaoM | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:FradingerEric... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:UrbancBrigita... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:MonienBernhar... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:SpringSean... | lld:pubmed |
| pubmed-article:20568734 | pubmed:author | pubmed-author:ZemelReeveR | lld:pubmed |
| pubmed-article:20568734 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20568734 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:20568734 | pubmed:volume | 49 | lld:pubmed |
| pubmed-article:20568734 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20568734 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20568734 | pubmed:pagination | 6358-64 | lld:pubmed |
| pubmed-article:20568734 | pubmed:dateRevised | 2011-9-26 | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:meshHeading | pubmed-meshheading:20568734... | lld:pubmed |
| pubmed-article:20568734 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20568734 | pubmed:articleTitle | Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragments. | lld:pubmed |
| pubmed-article:20568734 | pubmed:affiliation | Department of Neurology, David Geffen School of Medicine, University of California-Los Angeles, 635 Charles E.Young Drive S., Los Angeles, CA 90095, USA. | lld:pubmed |
| pubmed-article:20568734 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20568734 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20568734 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
