Trodusquemine enhances Aβ42 aggregation but suppresses its toxicity by displacing oligomers from cell membranes
Transient oligomeric species of the amyloid-β peptide (Aβ42) have been identified as key pathogenic agents in Alzheimer’s disease. Here the authors find that the aminosterol trodusquemine enhances Aβ42 aggregation and suppresses Aβ42-induced toxicity by displacing oligomers from cell membranes....
Saved in:
Main Authors: | Ryan Limbocker, Sean Chia, Francesco S. Ruggeri, Michele Perni, Roberta Cascella, Gabriella T. Heller, Georg Meisl, Benedetta Mannini, Johnny Habchi, Thomas C. T. Michaels, Pavan K. Challa, Minkoo Ahn, Samuel T. Casford, Nilumi Fernando, Catherine K. Xu, Nina D. Kloss, Samuel I. A. Cohen, Janet R. Kumita, Cristina Cecchi, Michael Zasloff, Sara Linse, Tuomas P. J. Knowles, Fabrizio Chiti, Michele Vendruscolo, Christopher M. Dobson |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2019
|
Subjects: | |
Online Access: | https://doaj.org/article/e4aca3eea6e44315b03de5b6488da79d |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
by: Michele Perni, et al.
Published: (2021) -
Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
by: Priyanka Joshi, et al.
Published: (2021) -
Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
by: Priyanka Joshi, et al.
Published: (2021) -
A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
by: Rodrigo Cataldi, et al.
Published: (2021) -
Publisher Correction: A dopamine metabolite stabilizes neurotoxic amyloid-β oligomers
by: Rodrigo Cataldi, et al.
Published: (2021)