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Science. 2003 Sep 26;301(5641):1847-9.
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis.
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.
Soluble oligomers are common to most amyloids and may represent the primary toxic species of amyloids, like the Abeta peptide in Alzheimer's disease (AD). Here we show that all of the soluble oligomers tested display a common conformation-dependent structure that is unique to soluble oligomers regardless of sequence. The in vitro toxicity of soluble oligomers is inhibited by oligomer-specific antibody. Soluble oligomers have a unique distribution in human AD brain that is distinct from fibrillar amyloid. These results indicate that different types of soluble amyloid oligomers have a common structure and suggest they share a common mechanism of toxicity.
PMID: 12702875 [PubMed - indexed for MEDLINE]
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Cited by over 100 PubMed Central articles
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Memory deficits in APP23/Abca1+/- mice correlate with the level of Abeta oligomers.
Lefterov I, Fitz NF, Cronican A, Lefterov P, Staufenbiel M, Koldamova R.
ASN Neuro. 2009 Apr 30; 1(2). Epub 2009 Apr 30.
[ASN Neuro. 2009]
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Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity.
Kvam E, Nannenga BL, Wang MS, Jia Z, Sierks MR, Messer A.
PLoS One. 2009 May 28; 4(5):e5727. Epub 2009 May 28.
[PLoS One. 2009]
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Amyloid formation by the pro-inflammatory S100A8/A9 proteins in the ageing prostate.
Yanamandra K, Alexeyev O, Zamotin V, Srivastava V, Shchukarev A, Brorsson AC, Tartaglia GG, Vogl T, Kayed R, Wingsle G, et al.
PLoS One. 2009; 4(5):e5562. Epub 2009 May 15.
[PLoS One. 2009]
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