The Changing Face of Glucagon Fibrillation: Structural Polymorphism and Conformational Imprinting
- 9 November 2005
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 355 (3), 501-523
- https://doi.org/10.1016/j.jmb.2005.09.100
Abstract
No abstract availableKeywords
This publication has 83 references indexed in Scilit:
- Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid FibrilsScience, 2005
- Modulation of S6 Fibrillation by Unfolding Rates and Gatekeeper ResiduesJournal of Molecular Biology, 2004
- Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid PeptideJournal of Molecular Biology, 2004
- Silent Prions Lying in Wait: A Two-hit Model of Prion/Amyloid Formation and InfectionJournal of Molecular Biology, 2003
- 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
- A model for the three-dimensional structure of glucagonJournal of Theoretical Biology, 1983
- Secondary structure and dynamics of glucagon in solutionBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Conformational transitions of glucagon in solution: The α → β transitionBiochemical and Biophysical Research Communications, 1977
- Conformational states of glucagonBiochemical and Biophysical Research Communications, 1967
- THE AMINO ACID SEQUENCE OF GLUCAGONJournal of the American Chemical Society, 1956