Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin
نویسندگان
چکیده
منابع مشابه
Soluble amyloid beta-oligomers affect dielectric membrane properties by bilayer insertion and domain formation: implications for cell toxicity.
It is well established that Alzheimer's amyloid beta-peptides reduce the membrane barrier to ion transport. The prevailing model ascribes the resulting interference with ion homeostasis to the formation of peptide pores across the bilayer. In this work, we examine the interaction of soluble prefibrillar amyloid beta (Abeta(1-42))-oligomers with bilayer models, observing also dramatic increases ...
متن کاملCorrection: A glycine zipper motif mediates the formation of toxic beta-amyloid oligomers in vitro and in vivo
Authors’ contributions C. elegans experiments were performed by VF, VD, CMR, PG, and CDL. Neuro 2a experiments were performed by GHS. Characterization of ADDL preps was performed by PTV. ADDL-binding and toxicity assays in hippocampal cultures were performed and analyzed by PNL, and Tau phosphorylation analysis done by ND, EYF and MAS. Adenovirus transfection of cortical neurons was performed b...
متن کاملDesigned α-sheet peptides inhibit amyloid formation by targeting toxic oligomers
Previous studies suggest that the toxic soluble-oligomeric form of different amyloid proteins share a common backbone conformation, but the amorphous nature of this oligomer prevents its structural characterization by experiment. Based on molecular dynamics simulations we proposed that toxic intermediates of different amyloid proteins adopt a common, nonstandard secondary structure, called α-sh...
متن کاملThe molecular chaperone Brichos breaks the catalytic cycle that generates toxic Aβ oligomers
where two particular combinations of the rate constants for primary nucleation (kn), elongation (k+), and fibril-catalysed secondary nucleation (k2) define much of the macroscopic behaviour; these parameters are related to the rate of formation of new aggregates through primary pathways λ = �2k+knm(0)c and through secondary pathways κ = �2k+k2m(0)2. Indeed, Eq. 1 depends on the rate constants t...
متن کاملSoluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure
The amyloid hypothesis of Alzheimer's toxicity has undergone a resurgence with increasing evidence that it is not amyloid fibrils but a smaller oligomeric species that produces the deleterious results. In this paper we address the mechanism of this toxicity. Only oligomers increase the conductance of lipid bilayers and patch-clamped mammalian cells, producing almost identical current-voltage cu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Journal
سال: 2008
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2008.06727.x