Polymorphic Fibrillar Assembly of Human Amylin
- 1 June 1997
- journal article
- Published by Elsevier in Journal of Structural Biology
- Vol. 119 (1) , 17-27
- https://doi.org/10.1006/jsbi.1997.3858
Abstract
No abstract availableKeywords
This publication has 24 references indexed in Scilit:
- Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helixStructure, 1996
- Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitroBiochemistry, 1995
- Architecture and Polymorphism of Fibrillar Supramolecular Assemblies Produced by in Vitro Aggregation of Human CalcitoninJournal of Structural Biology, 1995
- Intra- and extracellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide.Proceedings of the National Academy of Sciences, 1994
- Amylin Compared with Calcitonin Gene-Related Peptide: Structure, Biology, and Relevance to Metabolic DiseaseEndocrine Reviews, 1994
- Neurotoxicity of a prion protein fragmentNature, 1993
- Straight and paired helical filaments in Alzheimer disease have a common structural unit.Proceedings of the National Academy of Sciences, 1991
- Amylin hormoneNature, 1989
- Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.Proceedings of the National Academy of Sciences, 1987
- Identification of prion amyloid filaments in scrapie-infected brainCell, 1985