Identification of the molecular interaction site of amyloid β peptide by using a fluorescence assay
- 1 October 2001
- journal article
- research article
- Published by Wiley in Chemical Biology & Drug Design
- Vol. 58 (4) , 342-346
- https://doi.org/10.1034/j.1399-3011.2001.00920.x
Abstract
β‐Amyloid peptides (Aβ) are the main protein components of neuritic plaques and are important in the pathogenesis of Alzheimer's disease. It is reported that Aβ itself is not toxic; however...Keywords
This publication has 11 references indexed in Scilit:
- Gene transfer into hepatoma cells mediated by galactose-modified α-helical peptidesBiomaterials, 2000
- Alzheimer’s amyloid fibrils: structure and assemblyBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2000
- Review: History of the Amyloid FibrilJournal of Structural Biology, 2000
- Solution Structures in Aqueous SDS Micelles of Two Amyloid β Peptides of Aβ(1–28) Mutated at the α-Secretase Cleavage Site (K16E, K16F)Journal of Structural Biology, 2000
- Translating cell biology into therapeutic advances in Alzheimer's diseaseNature, 1999
- Solution Structure of Amyloid β-Peptide(1−40) in a Water−Micelle Environment. Is the Membrane-Spanning Domain Where We Think It Is?,Biochemistry, 1998
- Controlling Amyloid β-Peptide Fibril Formation with Protease-stable LigandsJournal of Biological Chemistry, 1997
- Arrest of -Amyloid Fibril Formation by a Pentapeptide LigandJournal of Biological Chemistry, 1996
- Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro.Proceedings of the National Academy of Sciences, 1987
- Hydrophobic moments and protein structureFaraday Symposia of the Chemical Society, 1982