IndraLab

Statements

VCPIP1 is phosphorylated on S768. 6 / 6
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"Taken together, these results demonstrate that the phosphorylation of Threonine-760 and Serine-767 in VCIP135 inhibits both p97-mediated Golgi reassembly pathways, indicating that it is important for [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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sparser
"Our results indicate that the phosphorylation of VCIP135 on Threonine-760 and Serine-767 inhibits p97-mediated Golgi membrane fusion at mitosis."
23500464
sparser
"In summary, our biochemical data show that phosphorylation of Threonine-760 and Serine-767 in VCIP135 inhibits its binding to p97, but does not affect its binding to WAC nor its deubiquitinating activ[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
23500464
sparser
"All these results indicate that phosphorylation of Threonine-760 and Serine-767 in VCIP135 inhibits its binding to p97."
23500464
sparser
"We established that VCIP135 is mitotically phosphorylated at Threonine-760 and Serine-767 and that the phosphorylated VCIP135 cannot bind to p97."
23500464
rlimsp
"Our results indicate that the phosphorylation of VCIP135 on Threonine-760 and Serine-767 inhibits p97-mediated Golgi membrane fusion at mitosis."
23500464