IndraLab

Statements

YOD1 binds TP53. 12 / 12
2 | 5 5
sparser
"We then confirmed that YOD1 interacts with p53 and stabilizes p53 via deubiquitination."
37454155
sparser
"We further used IP to investigate the potential interaction between YOD1 and p53."
37454155
sparser
"Taken together, these data indicated a specific interaction between YOD1 and p53."
37454155
sparser
"To identify domains in p53 that interact with YOD1, we constructed four p53 mutants, including C-segment deletion (△C), MDM2 binding site deletion (△M), DBD domain alone (DBD), and N-terminal deletion (△N) (Fig. xref )."
37454155
reach
"We then confirmed that YOD1 interacts with p53 and stabilizes p53 via deubiquitination."
37454155
reach
"These results indicate that YOD1 stabilizes the p53 protein in a catalytic activity-dependent manner.We further used IP to investigate the potential interaction between YOD1 and p53."
37454155
biogrid
No evidence text available
37454155
sparser
"These results demonstrate that YOD1 interacts with p53 through the N-terminus of p53 and the OTU domain of YOD1."
37454155
reach
"As expected, we detected clear binding of Myc-p53 to Flag-YOD1 (Fig. 3B)."
37454155
reach
"In addition, we detected an interaction and colocalization of endogenous YOD1 and p53 in MV-4–11 cells (Fig. 3C and Supplementary Fig. 4)."
37454155
reach
"Taken together, these data indicated a specific interaction between YOD1 and p53."
37454155
biogrid
No evidence text available
37454155