IndraLab

Statements

USP20 binds STING1. 9 / 9
3 | 6
biogrid
No evidence text available
27801882
sparser
"The present study demonstrated that USP20 interacted with STING and facilitated its degradation, consequently alleviating the myocardial inflammation and improving ventricular remodeling and heart failure induced by diabetes."
41637663
sparser
"Domain‐focused Co‐IP analyzes revealed that USP20 binds exclusively to STING via its catalytic USP domain, a conclusion supported by the complete loss of interaction in the catalytic USP domain mutant (Figure  xref )."
41637663
sparser
"In mechanism, USP20 directly binds to STING and promotes its degradation through the autophagy pathway by deubiquitinating p62 via its active site C154, thereby alleviating the myocardial inflammation and improving ventricular remodeling and heart failure induced by diabetes."
41637663
biogrid
No evidence text available
27801882
sparser
"USP20 directly binds to STING and promotes the degradation of STING through the autophagy pathway by deubiquitinating p62 via its active site C154, thereby alleviating myocardial inflammation and improving ventricular remodeling and heart failure induced by diabetes."
41637663
biogrid
No evidence text available
30814308
sparser
"Notably, STING emerged as the only overlapping candidate substrate across all three groups (Figure  xref ), prompting us to investigate whether an interaction exists between USP20 and STING."
41637663
sparser
"We then examined the specific domains through which USP20 interacts with STING."
41637663