IndraLab

Statements


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"Coimmunoprecipitation assays indicated that USP50 strongly binds to the ASC adaptor protein, although it also interacted weakly with NLRP3 (Fig. xref A)."

sparser
"Therefore, these results show that the binding of USP50 with ASC protein to deubiquitinate K63‐linked polyubiquitination is a crucial step for inflammasome activation."

sparser
"Mechanically, USP50 physically interacts with ASC, reducing its K63-linked ubiquitination and enhancing ASC oligomerization, subsequently promoting the assembly and activation of the NLRP3 inflammasome."

sparser
"USP50 binds to the ASC adaptor protein and is required for NLRP3‐induced ASC speck formation and oligomerization."

sparser
"Further investigations revealed that USP50 interacts with ASC proteins and deubiquitinates K63-linked ASC polyubiquitination ( xref )."

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"Based on the interaction between USP50 and ASC protein, we next investigated whether USP50 knockdown affects inflammasome activation by analyzing the formation of ASC specks."

sparser
"A recent report further suggested that USP50 binds ASC and deubiquitinates K63-linked polyubiquitin chains on ASC (citation)."