15N relaxation study of the amyloid β-peptide: structural propensities and persistence length
- 6 July 2006
- journal article
- research article
- Published by Wiley in Magnetic Resonance in Chemistry
- Vol. 44 (S1) , S114-S121
- https://doi.org/10.1002/mrc.1814
Abstract
No abstract availableKeywords
This publication has 46 references indexed in Scilit:
- Globular amyloid β‐peptide1−42 oligomer − a homogenous and stable neuropathological protein in Alzheimer's diseaseJournal of Neurochemistry, 2005
- Amyloid ion channels: A common structural link for protein-misfolding diseaseProceedings of the National Academy of Sciences, 2005
- Natural oligomers of the amyloid-β protein specifically disrupt cognitive functionNature Neuroscience, 2004
- Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseasesNature Cell Biology, 2004
- Deciphering the Molecular Basis of Memory Failure in Alzheimer's DiseaseNeuron, 2004
- Folding proteins in fatal waysNature, 2003
- Spherical aggregates of β-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3βProceedings of the National Academy of Sciences, 2003
- Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of PathogenesisScience, 2003
- The Amyloid Hypothesis of Alzheimer's Disease: Progress and Problems on the Road to TherapeuticsScience, 2002
- Aβ Deposition Is Associated with Neuropil Changes, but not with Overt Neuronal Loss in the Human Amyloid Precursor Protein V717F (PDAPP) Transgenic MouseJournal of Neuroscience, 1997