IndraLab

Statements


2 | 2 7

sparser
"SETD8 and USP29 Interact In Vivo."

sparser
"These data demonstrate that SETD8 and USP29 interact in vivo."

reach
"We demonstrate that SETD8 binds to USP29 in vivo, and this interaction is dependent on the catalytic activity of USP29."

sparser
"We demonstrate that SETD8 binds to USP29 in vivo, and this interaction is dependent on the catalytic activity of USP29."

sparser
"Together these data show that SETD8 and the USP29 bind to each other in vivo, and that this interaction depends on the ubiquitin hydrolase activity of USP29."

reach
"With several substrates among proteins functioning in the DNA damage response, USP29 can be considered as one of the central ubiquitin hydrolases contributing to the maintenance of genome integrity.Our results show that the decreased levels of SETD8 in cells depleted of USP29 do not have an indirect effect on cell cycle progression and, moreover, demonstrate an interaction between USP29 and SETD8 in vivo."

sparser
"Our results show that the decreased levels of SETD8 in cells depleted of USP29 do not have an indirect effect on cell cycle progression and, moreover, demonstrate an interaction between USP29 and SETD8 in vivo."

No evidence text available

No evidence text available

sparser
"Interestingly, a catalytic inactive version of USP29 did not coimmunoprecipitate with SETD8, indicating that the ubiquitin hydrolase activity is required for the interaction of SETD8 with USP29."

sparser
"The SETD8USP29 interaction suggests that USP29 might control SETD8 by directly removing polyubiquitin chains from SETD8, thereby stabilizing the protein."