IndraLab

Statements


3 | 12

No evidence text available

sparser
"Unexpectedly, compared with the full-length USP13, deletion of the UBP domain obviously decreased the interation with cyclin D1, indicating that the UBP domain might play some positive role in the interaction between USP13 and cyclin D1."

sparser
"Mechanistically, USP13 binds physically to the N-terminal domain of cyclin D1 and selectively deubiquitinates its K48-linked polyubiquitination chain while leaving K63-linked chains intact ( xref )."

sparser
"To detect the direct interaction between USP13 and cyclin D1, we performed GST-pulldown assays with the recombinant GST-USP13 protein."

sparser
"Third, Co-IP, GST pull down and immunofluorescence assays validated the physical interaction between USP13 and cyclin D1."

sparser
"In this study, we tried to map the regions that mediated the interaction between USP13 and cyclin D1."

sparser
"The results indicated that the N-terminal but not the C-terminal of cyclin D1 could interact with USP13 (Fig. xref )."

sparser
"Our results showed that the N-terminal domain of cyclin D1 (aa1–153) and the UBA (aa 625–863) domain of USP13 mediated the interaction between USP13 and cyclin D1."

sparser
"USP13 was positively associated with cyclin D1 in human GC specimens."

sparser
"USP13 directly interacts with cyclin D1 in GC cells."

sparser
"We speculated that the UBP domain of USP13 may participate in maintaining the structural basis for the interaction between USP13 and cyclin D1."

sparser
"Mechanistically, USP13 physically bound to the N-terminal domain of cyclin D1 and removed its K48- but not K63-linked polyubiquitination chain, thereby stabilizing and increasing cyclin D1."

No evidence text available

No evidence text available

sparser
"To gain insights into USP13-mediated regulation of cyclin D1, we checked whether USP13 interacted with cyclin D1."