Two Types of Alzheimer's β-Amyloid (1–40) Peptide Membrane Interactions: Aggregation Preventing Transmembrane Anchoring Versus Accelerated Surface Fibril Formation
- 9 December 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 335 (4) , 1039-1049
- https://doi.org/10.1016/j.jmb.2003.11.046
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- 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
- Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis11Edited by F. CohenJournal of Molecular Biology, 2001
- The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human BrainBiochemistry, 2000
- Amyloid fibrillogenesis: themes and variationsCurrent Opinion in Structural Biology, 2000
- Amyloid β-Protein FibrillogenesisJournal of Biological Chemistry, 1999
- Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and diseaseProceedings of the National Academy of Sciences, 1999
- The toxicity in vitro of β-amyloid proteinBiochemical Journal, 1995
- Cellular processing of β-amyloid precursor protein and the genesis of amyloid β-peptidePublished by Elsevier ,1993
- Amyloid plaque core protein in Alzheimer disease and Down syndrome.Proceedings of the National Academy of Sciences, 1985