20568734

Source:http://linkedlifedata.com/resource/pubmed/id/20568734

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0021467, umls-concept:C0021469, umls-concept:C0235032, umls-concept:C0486805, umls-concept:C0598002, umls-concept:C1261322, umls-concept:C1706853, umls-concept:C1707271, umls-concept:C1879748
pubmed:issue	30
pubmed:dateCreated	2010-7-29
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.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/AG027818, http://linkedlifedata.com/resource/pubmed/grant/P01 AG027818-010005, http://linkedlifedata.com/resource/pubmed/grant/P01 AG027818-020005, http://linkedlifedata.com/resource/pubmed/grant/P01 AG027818-030005, http://linkedlifedata.com/resource/pubmed/grant/P01 AG027818-040005
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-10090743, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-10339534, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-10764800, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-10825171, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-11425316, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-12058030, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-12081625, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-12130773, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-12506200, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-12578830, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-1281290, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-15930005, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-15980591, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-16809342, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-16981680, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-17046399, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-17046402, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-17505973, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-18511942, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-18779585, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-19356595, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-19908889, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-20050679, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-5319951, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-8248178, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-8577726, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-8621479, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-8700886, http://linkedlifedata.com/resource/pubmed/commentcorrection/20568734-8831674
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0370623
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Amyloid beta-Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
pubmed:status	MEDLINE
pubmed:month	Aug
pubmed:issn	1520-4995
pubmed:author	pubmed-author:BenedekGeorge BGB, pubmed-author:BisekJ PJP, pubmed-author:FradingerErica AEA, pubmed-author:LiHuiyuanH, pubmed-author:LomakinAlekseyA, pubmed-author:MonienBernhard HBH, pubmed-author:SpringSean MSM, pubmed-author:TanMiaoM, pubmed-author:UrbancBrigitaB, pubmed-author:XieCui-WeiCW, pubmed-author:ZemelReeveR
pubmed:issnType	Electronic
pubmed:day	3
pubmed:volume	49
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	6358-64
pubmed:dateRevised	2011-9-26
pubmed:meshHeading	pubmed-meshheading:20568734-Amyloid beta-Peptides, pubmed-meshheading:20568734-Drug Design, pubmed-meshheading:20568734-Humans, pubmed-meshheading:20568734-Neurotoxicity Syndromes, pubmed-meshheading:20568734-Peptide Fragments, pubmed-meshheading:20568734-Protein Multimerization, pubmed-meshheading:20568734-Protein Stability, pubmed-meshheading:20568734-Solubility
pubmed:year	2010
pubmed:articleTitle	Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragments.
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.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural