IndraLab

Statements


| 4 7

sparser
"This ubiquitination-defective Zap70 mutant was also attenuated in association with Otud7b, consistent with the idea that the Zap70Otud7b interaction might be facilitated by Zap70 ubiquitination ( xref )."

reach
"In response to TCR-CD28 ligation, Otud7b rapidly bound to Zap70 and inhibited Zap70 ubiquitination."

reach
"Otud7b binds to and deubiquitinates Zap70."

reach
"The Otud7b-Zap70 interaction was further confirmed using a transient transfection experiment in which the overexpressed Otud7b strongly associated with Zap70 (XREF_FIG)."

sparser
"In response to TCR signaling, Otud7b was rapidly recruited to Zap70 via a mechanism that required the UBA domain of Otud7b, suggesting the possibility that Otud7b interacted with ubiquitinated Zap70."

reach
"Otud7b binds to and deubiquitinates Zap70, thereby preventing the interaction of Zap70 with the negative-regulatory phosphatases, Sts1 and Sts2 199 (XREF_FIG)."

sparser
"In response to TCR–CD28 ligation, Otud7b rapidly bound to Zap70 and inhibited Zap70 ubiquitination."

sparser
"Interestingly, although Otud7b did not bind Zap70 in resting T cells, these two proteins formed a complex upon TCR–CD28 stimulation ( xref )."

sparser
"The Otud7bZap70 interaction was further confirmed using a transient transfection experiment in which the overexpressed Otud7b strongly associated with Zap70 ( xref )."

sparser
"Domain mapping analyses revealed the requirement of the N-terminal UBA domain of Otud7b for its physical interaction with Zap70 ( xref ), indicating the facilitation of Otud7bZap70 interaction by ubiquitination."

sparser
"Upon TCR stimulation, OTUD7B binds to and deubiquitinates Zap70, thereby preventing the binding of Sts1 and 2 [ xref ]."