Masami Masuda

TL;DR: Biochemical analysis revealed the formation of soluble oligomeric tau in the presence of the inhibitory compounds, suggesting that this may be the mechanism by which tau filament formation is inhibited.

TL;DR: In this paper, 79 compounds belonging to 12 different chemical classes were tested for their ability to inhibit the assembly of α-synuclein into filaments in vitro, including phenothiazines, porphyrins, polyene macrolides, and Congo red and its derivatives, BSB and FSB.

TL;DR: Electron microscopy observation and ultracentrifugation experiments revealed that shedding of fragments occurs from A30P fibrils and that these fragments accelerate fibrillization by serving as seeds, providing new insight into the molecular mechanisms of α-synucleinopathies.

TL;DR: The findings suggest that the soluble oligomers formed in the presence of inhibitory compounds may not be toxic to nerve cells and that these compounds may therefore have therapeutic potential for alpha-synucleinopathies and other brain amyloidoses.

TL;DR: It is shown that ∼20% of human α‐syn expressed in Escherichia coli is mistranslated and that a Cys residue is incorporated at position 136 instead of a Tyr.