… , Lewy body dementia (in which α-synuclein accumulates), and … clear, but we know that the
N-terminal domain of tau provides … of pathogenic, aggregated tau than do N-terminal antitau …

… The amino-terminal acetylation of α-synuclein improves the shuttle ability of the protein to …
N-terminal acetylation of α-synuclein slows down its aggregation process and alters the …

… Aggregated and highly phosphorylated α-synuclein constitutes the … the role of peripheral
α-synuclein pathology in the … The N-terminal domain is highly hydrophobic, containing a …

… The nuclear localization signal located in the N-terminal … easily aggregated proteins,
such as SOD1 and α-synuclein. … -43 acetylation enhanced the formation of aggregates, and …

… , and truncation can make these proteins prone to aggregation, … ), and c-Jun N-terminal kinase
in both physiological and pathological … Moreover, tau acetylation and truncation resulted in …

… N-terminal acetylation of α-synuclein slows down its aggregation process and alters the
morphology of the resulting aggregates. Biochemistry. 2022;61(17):1743-1756. …

… on Tau protein, which alter its structure and physiological … particular N-terminal cleavage(s)
may amplify the aggregation … In the brain-toblood direction, Tau151–391 shows a slower …

… Moreover, protein aggregation has also been linked with … of patients who harbor the α-synuclein
mutation show increased … , H2S exerts its antioxidative effects against H2O2 by altering …

… and an increase in histone acetylation. They also inhibit the … by the aggregation and
deposition of Aβ peptides. Clinically, … the accumulation of α-synuclein to alleviate dopaminergic …

… tau hyperphosphorylation and aggregation in the form of NFTs, and these aggregates
lead to … Regulated expression of exons 2 and 3 gives rise to tau isoforms with 0, 1, or 2 N-terminal …