IndraLab

Statements


USP39 binds E. 9 / 9
4 | 5

No evidence text available

sparser
"Taken together, these results suggested that USP39 directly and specifically interacts with the E protein through the AR motif and performs its deubiquitination function using the iUSP motif."

No evidence text available

No evidence text available

No evidence text available

sparser
"However, it was also found that USP39 interacts with the E protein, a highly conserved envelope protein of SARS-CoV-2, through its N-terminal arginine-rich modality, which reduces polyubiquitination of the E protein and protects it from degradation."

sparser
"Moreover, the interaction of USP39 and the E protein was readily detectable in reciprocal co-immunoprecipitation (co-IP) experiments ( Fig. 3 B and C)."

sparser
"A fluorescence resonance energy transfer (FRET) assay also showed the direct interaction of USP39 and the E protein, that is, bleaching of the fluorescence from E-yellow fluorescent protein (YFP) enha[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Similar to the above results, we also demonstrated that USP39 directly interacts with the substrate E protein via the AR motif, while the iUSP domain not required for E binding is required for E deubi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"