Filter By:

Journal Check one or more journals to show results from those journals only.

Choose more journals

Article type Check one or more article types to show results from those article types only.
Subject Check one or more subjects to show results from those subjects only.
Date Choose a date option to show results from those dates only.

Custom date range

Clear all filters
Sort by:
Showing 1–3 of 3 results
Advanced filters: Author: Azad Farzadfard Clear advanced filters
  • Farzadfard et al. present a comprehensive analysis of a range of C-terminal truncations of aSN, linking the importance of high C-terminus charge for decreased fibrillation rates. The ability to formation oligomers, to disrupt synthetic vesicles and cell toxicity was reduced with truncated aSN, aiding in understanding of the intramolecular interactions of aSN which promote/inhibit aggregation.

    • Azad Farzadfard
    • Jannik Nedergaard Pedersen
    • Daniel Erik Otzen
    ResearchOpen Access
    Communications Biology
    Volume: 5, P: 1-10
  • The mechanism of α-synuclein amyloid aggregation via liquid–liquid phase separation has so far remained elusive. Now, the existence of nanoscale clusters of α-synuclein in sub-saturated concentrations is observed using mass photometry. These nanoscale clusters can act as precursors to both macroscopic condensate droplets as well as amyloid fibrils.

    • Soumik Ray
    • Thomas O. Mason
    • Alexander K. Buell
    Research
    Nature Chemistry
    Volume: 15, P: 1306-1316
  • Methods to quantitatively study liquid-liquid phase separation (LLPS) of proteins are lacking. Here the authors report Capillary flow experiments (Capflex) for the quantification of key LLPS parameters; they study Ddx4, the RP3 peptide and the aberrant liquid-to-solid phase transition of α-synuclein.

    • Emil G. P. Stender
    • Soumik Ray
    • Alexander K. Buell
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-18