Amyloid Fibril Polymorphism: Almost Identical on the Atomic Level, Mesoscopically Very Different
- 20 February 2017
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 121 (8), 1783-1792
- https://doi.org/10.1021/acs.jpcb.6b10624
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- The activities of amyloids from a structural perspectiveNature, 2016
- The route to protein aggregate superstructures: Particulates and amyloid‐like spherulitesFEBS Letters, 2015
- α-Synuclein strains cause distinct synucleinopathies after local and systemic administrationNature, 2015
- Amyloid Polymorphism: Structural Basis and Neurobiological RelevanceNeuron, 2015
- Physical and structural basis for polymorphism in amyloid fibrilsProtein Science, 2014
- Prion Strains and Amyloid Polymorphism Influence Phenotypic VariationPLoS Pathogens, 2014
- The Amyloid State of Proteins in Human DiseasesCell, 2012
- Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrilsNature Chemical Biology, 2011
- The structural basis of yeast prion strain variantsNature, 2007
- Protein Misfolding, Functional Amyloid, and Human DiseaseAnnual Review of Biochemistry, 2006