Amyloid Fibril Polymorphism Is under Kinetic Control
Author:
Affiliation:
1. Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja106044u
Reference78 articles.
1. Molecular Mechanisms of Amyloidosis
2. Amyloidogenic Self-Assembly of Insulin Aggregates Probed by High Resolution Atomic Force Microscopy
3. Polymorphism in the intermediates and products of amyloid assembly
4. Infectious and Noninfectious Amyloids of the HET‐s(218–289) Prion Have Different NMR Spectra
5. Competing Pathways Determine Fibril Morphology in the Self-assembly of β2-Microglobulin into Amyloid
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