IndraLab

Statements

OTUD7B binds ESR1. 8 / 8
| 2 6
sparser
"GST pull-down assay showed that OTUD7B directly interacted with ERα in vitro (Fig. xref )."
34035221
reach
"OTUD7B could interact with, deubiquitylate, and stabilize ERalpha in a deubiquitylation activity dependent manner."
34035221
sparser
"GST pull-down assay showed that OTUD7B interacted with ERα in vitro in a DUB-activity-dependent manner."
34035221
reach
"Targeting the OTUD7B and ERalpha complex may prove to be a potential approach to treat patients with ERalpha positive breast cancer."
34035221
sparser
"The interaction between OTUD7B and ERα suggested that ERα might be a substrate of OTUD7B, and therefore we evaluated the possibility of ERα deubiquitylation by OTUD7B. It was found that OTUD7B deletion dramatically decreased ERα protein level, and this effect could be reversed by addition of the proteasome inhibitor MG132 or overexpression of OTUD7B-WT, but not its catalytically inactive mutant OTUD7B C194S (Fig. xref )."
34035221
sparser
"Targeting the OTUD7B–ERα complex may prove to be a potential approach to treat patients with ERα-positive breast cancer."
34035221
sparser
"OTUD7B interacts with ERα."
34035221
sparser
"OTUD7B was associated with ERα and inhibits ERα polyubiquitination and degradation."
34035221