Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1–42 mutants of familial Alzheimer's disease at positions 21–23
- 28 May 2002
- journal article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 294 (1), 5-10
- https://doi.org/10.1016/s0006-291x(02)00430-8
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formationNature Neuroscience, 2001
- Alzheimer’s amyloid fibrils: structure and assemblyBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2000
- Charge Alterations of E22 Enhance the Pathogenic Properties of the Amyloid β‐ProteinJournal of Neurochemistry, 2000
- Toxicity of Dutch (E22Q) and Flemish (A21G) Mutant Amyloid β Proteins to Human Cerebral Microvessel and Aortic Smooth Muscle CellsStroke, 2000
- Synthesis, aggregation, and neurotoxicity of the alzheimer's Aß1-42 amyloid peptide and its isoaspartyl isomersBioorganic & Medicinal Chemistry Letters, 1999
- The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's diseaseTrends in Cell Biology, 1998
- 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
- Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β–amyloid precursor protein geneNature Genetics, 1992
- Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch TypeScience, 1990
- β-Hairpin families in globular proteinsNature, 1985