English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Pathogenic amyloids are the main feature of several neurodegenerative disorders, such as Creutzfeldt⁻Jakob disease, Alzheimer&amp;rsquo;s disease, and Parkinson&amp;rsquo;s disease. High resolution structures of tau paired helical filaments (PHFs), amyloid-&amp;beta;(1-42) (A&amp;beta;(1-42)) fibrils, and &amp;alpha;-synuclein fibrils were recently reported using cryo-electron microscopy. A high-resolution structure for the infectious prion protein, PrP Sc , is not yet available due to its insolubility and its propensity to aggregate, but cryo-electron microscopy, X-ray fiber diffraction, and other approaches have defined the overall architecture of PrP Sc as a 4-rung &amp;beta;-solenoid. Thus, the structure of PrP Sc must have a high similarity to that of the fungal prion HET-s, which is part of the fungal heterokaryon incompatibility system and contains a 2-rung &amp;beta;-solenoid. This review compares the structures of tau PHFs, A&amp;beta;(1-42), and &amp;alpha;-synuclein fibrils, where the &amp;beta;-strands of each molecule stack on top of each other in a parallel in-register arrangement, with the &amp;beta;-solenoid folds of HET-s and PrP Sc .

Comparing the Folds of Prions and Other Pathogenic Amyloids