… toxicity without promoting their disassembly. In this review we will show the evidence in this
direction, showing how molecular chaperones … Aβ 42 oligomers (1:5) in vitro generates larger …

… caused by oligomers of Aβ and PrP (106–126) and α-synuclein. We also argue … molecular
chaperones rescue neurons from the toxic effects produced by accumulated amyloid oligomers…

… the number of toxic Aβ aggregates by generating amyloid … Aβ and S100 proteins, it is
possible that the S100 family could function as molecular chaperones to suppress oligomer toxicity …

… or counteract the toxicity associated with amyloid species. … the interplay of these activities
produces specific cellular outcomes and … the toxicity of, in particular, smaller oligomeric states is …

… of targeting the toxicity associated with Aβ aggregation by … domain, mutated to act selectively
against Aβ42 oligomer … Therefore, we generated a single point mutant (R221E) of rh Bri2 …

… Cell-toxic oligomers may occur an off-pathway intermediate … These fibrils may also break
or fragment in order to provide … are generated that lead to the formation of potentially toxic …

… and its potentially harmful consequences. Deterioration of … Proteolytic processing of AβPP
generates Aβ peptides of … nucleation reduces the toxic Aβ42 oligomer formation. Noteworthily, …

… data points to Aβ oligomers species as the most toxic ones, … Fragmentation depends on
the probability that fibrils break, … modulators of Aβ fibril formation, molecular chaperones have …

… Here we explore another approach: molecular chaperones … in the critical catalytic cycle
through which toxic oligomers are … (2015) A molecular chaperone breaks the catalytic cycle that …

… even bind to extracellular toxic misfolded oligomers. … molecular chaperones or protein
degradation pathways may be effective in suppressing protein aggregation and associated toxicity …