6 RESULTS
COMMENT A speculative, but intriguing, implication of these findings is that Aβ can facilitate the membrane channel forming properties of tau. Our recent paper on tau showed that it was capable of forming non-selective and potentially destructive ion channels in ...
COMMENT The authors describe the results of a solid-state NMR study on amylospheroid (ASPD), a toxic Aβ1-42 oligomer. They demonstrate the similarity of the synthetic ASPD to native ASPD and go on to suggest that the secondary structure of this particle is ...
COMMENT Over the past 18 years, since the proposal of the channel hypothesis of Alzheimer's disease by Arispe et al. (1993), considerable controversy has surrounded this theory. Despite repeated demonstrations of the channel-forming ability of various ...
COMMENT The authors report that soluble oligomers of Aβ and other protein misfolding disease related peptides such as islet amyloid polypeptide (IAPP, diabetes), PrP106-126 (prion diseases), polyglutamine (PG, Huntington’s and other triplet repeat diseases) and α ...
COMMENT This paper demostrates that Abeta forms ion channels in vivo, and that channel formation is integral to Abeta's cytotoxic properties. This is the critical extension of the in vitro work on Abeta ion channels to a cellular model. This paper shows that ...
COMMENT Serum amyloid A (SAA) is an apolipoprotein of uncertain function, whose concentration in serum can increase by as much as 1,000-fold during states of infection or inflammation. Chronic inflammatory states may lead to reactive AA amyloidosis, in which an N ...
