Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
- 1 December 1997
- journal article
- Published by Elsevier BV in Cell Chemical Biology
- Vol. 4 (12), 951-959
- https://doi.org/10.1016/s1074-5521(97)90303-3
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Amyloid β-Protein FibrillogenesisPublished by Elsevier BV ,1997
- Polymorphic Fibrillar Assembly of Human AmylinJournal of Structural Biology, 1997
- An ApoE-Aβ inhibition complex in Aβ fibril extensionCell Chemical Biology, 1996
- Nanotubes as nanoprobes in scanning probe microscopyNature, 1996
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Mechanisms of Neuronal Degeneration in Alzheimer's DiseaseNeuron, 1996
- Physical, Morphological and Functional Differences between pH 5.8 and 7.4 Aggregates of the Alzheimer's Amyloid Peptide A βJournal of Molecular Biology, 1996
- Normal and Abnormal Biology of the beta-Amyloid Precursor ProteinAnnual Review of Neuroscience, 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
- Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein PrecursorScience, 1993