IndraLab

Statements


4 | 1 4 5

sparser
"In this study, we isolated a VCIP135 mutant, VCIP135(T760E, S767E), that still binds to WAC and maintains its deubiquitinating enzyme activity, but lacks p97-binding affinity."

reach
"Furthermore, VCIP135 interacts with WAC, which enhances the DUB activity of VCIP135."

reach
"Golgi WAC interacts with the deubiquitinase VCIP135, which binds VCP and p97."

sparser
"Furthermore, VCIP135 interacts with WAC, which enhances the DUB activity of VCIP135."

reach
"WAC directly binds to VCIP135 and increases its deubiquitinating activity."

sparser
"WAC directly binds to VCIP135 and increases its deubiquitinating activity."

sparser
"WAC binds to VCIP135, mediating its association with the Golgi, and activating its deubiquitinating function to regulate Golgi biogenesis ( xref )."

reach
"WAC binds to VCIP135, mediating its association with the Golgi, and activating its deubiquitinating function to regulate Golgi biogenesis."

trips
"WAC directly binds to VCIP135 and increases its deubiquitinating activity."

sparser
"We next tested the binding of phosphorylated VCIP135 to WAC, as presented in Fig. 3 A. Cdc2-phosphorylated VCIP135 still bound to GST-WAC (upper panel, lane 2), suggesting that the phosphorylation of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"