IndraLab

Statements

USP13 binds MAP3K7. 9 / 9
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sparser
"USP13 interacts with TAK1, and represses TAK1 activation though removing ubiquitination."
39033101
sparser
"USP13 interacts with TAK1, inhibits TAK1 activation by removing ubiquitination of TAK1, and subsequently inhibits the NF-κB & MAPK signaling pathway activation (Fig.  xref ), thereby treating NAFLD as a latent molecular target."
39033101
sparser
"We then investigated whether USP13 physically interacts with TAK1."
39033101
sparser
"In the present study, we observed that USP13 interacted with TAK1 and inhibited its activation."
39033101
sparser
"Using molecular docking and co-immunoprecipitation techniques, we demonstrated that USP13 binds to TAK1 (Fig.  xref E and F)."
39033101
sparser
"Secondly, we did not specifically investigate whether the interaction between USP13 and TAK1 changes under HFD versus ND conditions."
39033101
sparser
"Therefore, we deduced that USP13 interacted with TAK1, removed the ubiquitin chain on TAK1, and subsequently reduced TAK1 phosphorylation, followed by activation and downstream events."
39033101
reach
"Using molecular docking and co-immunoprecipitation techniques, we demonstrated that USP13 binds to TAK1 (Fig. 6E and F)."
39033101
sparser
"Mechanistically, USP13 interacted with TAK1, repressing its K63-linked ubiquitination and phosphorylation, thereby modulating downstream inflammatory and insulin pathways."
39033101