IndraLab

Statements


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sparser
"USP15 physically interacts with MDM2 and inhibits the ubiquitination and degradation of MDM2."

reach
"First, USP15 interacts with MDM2, inhibits ubiquitination, and stabilizes MDM2, an important E3 ligase that mediates the ubiquitination and proteolysis of NFATc2 members of the NFAT family and negatively regulates TCR signals."

sparser
"When co-expressed in HEK293 cells, USP15 interacted with MDM2, as detected by co-IP assays ( xref )."

sparser
"First, USP15 interacts with MDM2, inhibits ubiquitination, and stabilizes MDM2, an important E3 ligase that mediates the ubiquitination and proteolysis of NFATc2 members of the NFAT family and negatively regulates TCR signals."

reach
"When co-expressed in HEK293 cells, USP15 interacted with MDM2, as detected by co-IP assays (XREF_FIG)."

reach
"These results suggest that USP15 physically interacts with MDM2 in a p53 independent manner."

No evidence text available