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pubmed-article:15910781pubmed:abstractTextWe examined the ultrastructural localization of oligomeric proteins, Abeta42, and flotillin-1 in Tg2576 mouse brains by triple immunoelectron microscopy. Oligomer-specific immunoreactions localized to cell processes, especially to axon terminals with higher density in Tg than in nonTg mouse brains. The oligomer was less frequently colocalized to flotillin-1-immunoreactive rafts than Abeta42, suggesting that rafts are one of the sites of polymeric Abeta deposition, but not of oligomeric proteins including Abeta.lld:pubmed
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pubmed-article:15910781pubmed:articleTitleOligomeric proteins ultrastructurally localize to cell processes, especially to axon terminals with higher density, but not to lipid rafts in Tg2576 mouse brain.lld:pubmed
pubmed-article:15910781pubmed:affiliationGunma University School of Health Sciences, 3-39-15 Showa-machi, Maebashi 371-8514, Japan.lld:pubmed
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