Aromatic Small Molecules Remodel Toxic Soluble Oligomers of Amyloid β through Three Independent Pathways
Open Access
- 1 February 2011
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 286 (5), 3209-3218
- https://doi.org/10.1074/jbc.m110.173856
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- A synergistic small-molecule combination directly eradicates diverse prion strain structuresNature Chemical Biology, 2009
- Evidence for Novel β-Sheet Structures in Iowa Mutant β-Amyloid FibrilsBiochemistry, 2009
- Structural Differences between Aβ(1-40) Intermediate Oligomers and Fibrils Elucidated by Proteolytic Fragmentation and Hydrogen/Deuterium ExchangeBiophysical Journal, 2009
- EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomersNature Structural & Molecular Biology, 2008
- Small-molecule aggregates inhibit amyloid polymerizationNature Chemical Biology, 2008
- Reaching for high-hanging fruit in drug discovery at protein–protein interfacesNature, 2007
- Prion recognition elements govern nucleation, strain specificity and species barriersNature, 2007
- The most infectious prion protein particlesNature, 2005
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Conformational diversity in a yeast prion dictates its seeding specificityNature, 2001