Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct
Top Cited Papers
Open Access
- 1 April 2007
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 282 (14) , 10311-10324
- https://doi.org/10.1074/jbc.m608207200
Abstract
No abstract availableKeywords
This publication has 108 references indexed in Scilit:
- Mass Spectrometry-Based Screening for Inhibitors of β-Amyloid Protein AggregationAnalytical Chemistry, 2005
- Structural properties of Aβ protofibrils stabilized by a small moleculeProceedings of the National Academy of Sciences, 2005
- Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in VivoJournal of Biological Chemistry, 2005
- Conformation-dependent antibodies target diseases of protein misfoldingTrends in Biochemical Sciences, 2004
- Protein folding and misfoldingNature, 2003
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesNature, 2002
- Inhibition of Alzheimer's disease β‐amyloid aggregation, neurotoxicity, and in vivo deposition by nitrophenols: implications for Alzheimer's therapyThe FASEB Journal, 2001
- Selective Inhibition of Aβ Fibril FormationJournal of Biological Chemistry, 1996
- Rifampicin Prevents the Aggregation and Neurotoxicity of Amyloid β Protein in VitroBiochemical and Biophysical Research Communications, 1994