IndraLab

Statements


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reach
"We also examined the specificity of the association between USP15 and RIG-I."

sparser
"We also identified the domains of RIG-I responsible for the RIG-IUSP15 interaction."

reach
"Together, these results demonstrate that USP15 and RIG-I form a complex through the UCH domain of USP15, and that the N-terminal CARD domain and the C-terminal domain of RIG-I both bind to USP15."

sparser
"Together, these results demonstrate that USP15 and RIG-I form a complex through the UCH domain of USP15, and that the N-terminal CARD domain and the C-terminal domain of RIG-I both bind to USP15."

sparser
"We used a coimmunoprecipitation experiment to map the domain of USP15 that facilitates its interaction with RIG-I. As demonstrated in xref , RIG-I interacted with USP15-WT and the C-terminal UCH domain (USP15-C250), but not with the N-terminal DUSP domain (USP15-N249)."

sparser
"Our result showed that the presence of GST-RIG-I-N retained USP15 C250 ( xref ), indicating that the interaction of RIG-I with USP15 is due to a direct physical association."

reach
"We hypothesized that USP15 interacts with RIG-I and the interaction is independent of the DUB activity, and the coimmunoprecipitation assay proved the credibility."

reach
"Mechanistically, the interaction between RIG-I and USP15 suggests the model that USP15 prevents the access of a downstream target to the RIG-I complex."

reach
"The second possibility is that USP15 interacts with RIG-I to reduce IPS-1-RIG-I binding."

sparser
"We hypothesized that USP15 interacts with RIG-I and the interaction is independent of the DUB activity, and the coimmunoprecipitation assay proved the credibility."

sparser
"Mechanistically, the interaction between RIG-I and USP15 suggests the model that USP15 prevents the access of a downstream target to the RIG-I complex."

No evidence text available

No evidence text available