… Here, we present evidence that α-syn monomers and oligomers are able to prime and …
TLR5 ligation, leading to NLRP3 inflammasome-dependent IL-1β secretion, thereby inhibiting α-…

… α-Synuclein (α-syn) is one of the most prominent proteins is LBs and can aggregate into
large oligomers and fibrils that might be neurotoxic. Defects in protein clearance pathways such …

… protein; however, the precise mechanism by which TLR2 contributes to α-synuclein …
potentiates α-synuclein pathology seeded with α-synuclein preformed fibrils. Moreover, α-synuclein …

… of the NF-κB activity was observed in YFP or TLR5-transfected cells (Fig. 5h). Furthermore, …
α-synuclein protein 34 ; future study should identify the specific E3 ligase of α-synuclein in …

… α-syn blocks the microglial activation induced by α-syn oligomers in BV2 microglial cells [63].
In addition to TLR2, α-syn monomers and oligomers also bind to TLR5 … The different α-syn …

… TLR5 ligation (95). The NLRP3 inflammasome recruits the small adaptor molecule
apoptosis-associated speck-like protein, which subsequently triggers cysteine-aspartate protease-1 (…

… α-synuclein activate the NOD-like receptor pyrin domain containing 3 (NLRP3) inflammasome
via TLR2 and TLR5 … and α-synuclein expression, leading to α-synuclein aggregation (91, …

… Carboxyl terminus of Hsp70-interacting protein (CHIP) is another E3 ligase which reduces
α-syn oligomerization [16–18]. It further reduces α-syn aggregation through its interactions …

… mutations of the gene encoding α-synuclein (α-Syn) [4,5]. Originally sequenced as a precursor
of the non-β amyloid component of senile plaque in AD (NACP) [6,7], α-Syn was identified …

… The release of α-synuclein does not show sex difference as indicated by our previous in
vivo study using microdialysis to monitor α-synuclein secretion in living mice of either sex [23]. …