IndraLab

Statements


4 | 6

sparser
"However, since the interaction between YOD1 and α-synuclein has not been elucidated, the current study investigated the relationship between YOD1 and α-synuclein."

sparser
"We found that YOD1 directly interacts with α-synuclein and deubiquitinates K6-, K11-, K29-, K33-, and K63-linked polyubiquitin chains on α-synuclein."

sparser
"YOD1 directly interacts with α-synuclein and removes various polyubiquitin chains (K6, K11, K29, K33, and K63) through deubiquitination, thus regulating protein stability and reducing aggregation."

No evidence text available

sparser
"Next, we performed the GST pull-down assay to check the direct interaction between YOD1 and α-synuclein, and found that GST-YOD1 precipitates α-synuclein ( Fig. 1 B)."

sparser
"These results indicate the direct interaction between YOD1 and α-synuclein."

No evidence text available

No evidence text available

No evidence text available

sparser
"Mechanistically, OTUD2 directly interacts with α-synuclein to cleave K6-, K11-,K33-,K63- and K29-linked ubiquitin chains, representing a novel regulatory mechanism (Park et al. xref )."