Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation.
Open Access
- 1 November 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (46) , 28551-28554
- https://doi.org/10.1016/s0021-9258(19)61939-3
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)Neuron, 1994
- The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's diseaseBiochemistry, 1993
- Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease βA4 peptidesJournal of Molecular Biology, 1992
- Vitamin E protects nerve cells from amyloid βprotein toxicityBiochemical and Biophysical Research Communications, 1992
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's diseaseJournal of Molecular Biology, 1992
- Biophysical characterization of α-crystallin aggregates: validation of the micelle hypothesisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
- The molecular pathology of Alzheimer's diseaseNeuron, 1991
- Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's diseaseJournal of Molecular Biology, 1991
- Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin NeuropeptidesScience, 1990
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970