Inhibiting the conversion of soluble amyloid-β peptide into abnormally folded amyloidogenic intermediates: relevance for Alzheimer's disease therapy
- 1 December 2000
- journal article
- research article
- Published by Hindawi Limited in Acta Neurologica Scandinavica
- Vol. 102, 90-95
- https://doi.org/10.1034/j.1600-0404.2000.00313.x
Abstract
Alzheimer's disease is a degenerative disorder of the brain for which there is no cure or effective treatment. Recent studies suggest that cerebral amyloid plaques are central to the disease process....Keywords
This publication has 31 references indexed in Scilit:
- Reversion of prion protein conformational changes by synthetic b-sheet breaker peptidesThe Lancet, 2000
- Structural and kinetic features of amyloid β-protein fibrillogenesisAmyloid, 1998
- Conformational diseaseThe Lancet, 1997
- Mechanisms of Neuronal Degeneration in Alzheimer's DiseaseNeuron, 1996
- The α-Helical to β-Strand Transition in the Amino-terminal Fragment of the Amyloid β-Peptide Modulates Amyloid FormationJournal of Biological Chemistry, 1995
- Prolines and Aamyloidogenicity in Fragments of the Alzheimer's Peptide .beta./A4Biochemistry, 1995
- Cell Biology of the Amyloid beta-Protein Precursor and the Mechanism of Alzheimer's DiseaseAnnual Review of Cell and Developmental Biology, 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
- Solution conformations and aggregational properties of synthetic amyloid β-peptides of Alzheimer's diseaseJournal of Molecular Biology, 1992