Amino Acid Position-specific Contributions to Amyloid β-Protein Oligomerization
Open Access
- 1 August 2009
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 284 (35) , 23580-23591
- https://doi.org/10.1074/jbc.m109.038133
Abstract
No abstract availableKeywords
This publication has 77 references indexed in Scilit:
- C-terminal peptides coassemble into Aβ42 oligomers and protect neurons against Aβ42-induced neurotoxicityProceedings of the National Academy of Sciences, 2008
- Familial Alzheimer's disease mutations alter the stability of the amyloid β-protein monomer folding nucleusProceedings of the National Academy of Sciences, 2007
- Structural Study of Metastable Amyloidogenic Protein Oligomers by Photo‐Induced Cross‐Linking of Unmodified ProteinsPublished by Elsevier ,2006
- Cyclohexanehexol inhibitors of Aβ aggregation prevent and reverse Alzheimer phenotype in a mouse modelNature Medicine, 2006
- Molecular structure of amyloid fibrils: insights from solid-state NMRQuarterly Reviews of Biophysics, 2006
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Mapping Aβ Amyloid Fibril Secondary Structure Using Scanning Proline MutagenesisJournal of Molecular Biology, 2004
- Protofibrils, the unifying toxic molecule of neurodegenerative disorders?Nature Neuroscience, 2001
- Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease βA4 peptidesJournal of Molecular Biology, 1992
- Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's diseaseJournal of Molecular Biology, 1991