# |
PMID |
Sentence |
1 |
20504922
|
In this study, we demonstrated that the PRRSV nsp2 OTU domain antagonizes the type I interferon induction by interfering with the NF-kappaB signaling pathway.
|
2 |
20504922
|
Further analysis revealed that the nsp2 OTU domain possesses ubiquitin-deconjugating activity.
|
3 |
20504922
|
This domain has the ability to inhibit NF-kappaB activation by interfering with the polyubiquitination process of IkappaBalpha, which subsequently prevents IkappaBalpha degradation.
|
4 |
20504922
|
The OTU domain mutants were examined to determine whether mutations in the nsp2 OTU domain region altered virus ability to inhibit NF-kappaB activation.
|
5 |
20504922
|
In this study, we demonstrated that the PRRSV nsp2 OTU domain antagonizes the type I interferon induction by interfering with the NF-kappaB signaling pathway.
|
6 |
20504922
|
Further analysis revealed that the nsp2 OTU domain possesses ubiquitin-deconjugating activity.
|
7 |
20504922
|
This domain has the ability to inhibit NF-kappaB activation by interfering with the polyubiquitination process of IkappaBalpha, which subsequently prevents IkappaBalpha degradation.
|
8 |
20504922
|
The OTU domain mutants were examined to determine whether mutations in the nsp2 OTU domain region altered virus ability to inhibit NF-kappaB activation.
|
9 |
20504922
|
In this study, we demonstrated that the PRRSV nsp2 OTU domain antagonizes the type I interferon induction by interfering with the NF-kappaB signaling pathway.
|
10 |
20504922
|
Further analysis revealed that the nsp2 OTU domain possesses ubiquitin-deconjugating activity.
|
11 |
20504922
|
This domain has the ability to inhibit NF-kappaB activation by interfering with the polyubiquitination process of IkappaBalpha, which subsequently prevents IkappaBalpha degradation.
|
12 |
20504922
|
The OTU domain mutants were examined to determine whether mutations in the nsp2 OTU domain region altered virus ability to inhibit NF-kappaB activation.
|
13 |
23401522
|
PLP2 binds ubiquitin using a zinc finger that is uniquely integrated into an exceptionally compact OTU-domain fold that represents a new subclass of zinc-dependent OTU DUBs.
|