Manipulating the Amyloid-β Aggregation Pathway with Chemical Chaperones
Open Access
- 1 November 1999
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 274 (46), 32970-32974
- https://doi.org/10.1074/jbc.274.46.32970
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Common core structure of amyloid fibrils by synchrotron X-ray diffractionJournal of Molecular Biology, 1997
- Amyloid β-Protein FibrillogenesisJournal of Biological Chemistry, 1997
- Kinetic theory of fibrillogenesis of amyloid β-proteinProceedings of the National Academy of Sciences of the United States of America, 1997
- Alzheimer's Disease--Genotypes, Phenotype, and TreatmentsScience, 1997
- AßT Amyloidogenesis: Unique, or Variation on a Systemic ThemeCritical Reviews in Biochemistry and Molecular Biology, 1997
- Observation of metastable Aβ amyloid protofibrils by atomic force microscopyCell Chemical Biology, 1997
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- The nanometer-scale structure of amyloid-Β visualized by atomic force microscopyJournal of Protein Chemistry, 1996
- 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
- Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffractionBiophysical Journal, 1993