IndraLab

Statements


| 7

sparser
"USP1 and UAF1 interact with RAD51AP1."

sparser
"While Liang et al. found that the role of UAF1-RAD51AP1 is independent of USP1, our results indicate that USP1 and UAF1 interact with RAD51AP1 as a complex."

sparser
"UAF1-USP1 readily associates with RAD51AP1 to form a trimeric complex ( xref )."

sparser
"We provide evidence that RAD51AP1 interacts with USP1 through UAF1, and that stability of RAD51AP1 is promoted by USP1 and UAF1."

sparser
"Thus, even though DNA binding by either UAF1 or RAD51AP1 is sufficient for targeting the USP1-UAF1-RAD51AP1 DUB complex to DNA for FANCD2 deubiquitination, the DNA binding attribute of both UAF1 and RAD51AP1 is required for optimal DNA damage repair."

sparser
"The USP1-UAF1 complex interacts with RAD51AP1 In order to search for the potential role of USP1 or UAF1 in HR repair, we undertook a proteomic approach to identify potential UAF1 or USP1 interacting proteins that regulate HR repair."

sparser
"Discussion Here we described a functional interaction between RAD51AP1 and the USP1-UAF1 deubiquitinating enzyme complex."