IndraLab

Statements


3 | 1 3

sparser
"Further mechanistic study revealed the interaction between USP37 and ERα: USP37 regulated ERα signaling through modulating protein stability instead of gene expression, in which it stabilized ERα protein via inhibiting the K48‐specific polyubiquitination process."

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No evidence text available

sparser
"Mechanistically, USP37 interacts with ERα and removes the K48‐linked ubiquitin through its catalytical activity, leading to the stabilization of ERα."

sparser
"These findings demonstrate that USP37 is an essential regulator of estrogen signaling and that the USP37ERα axis is a potential target for breast cancer treatment."

reach
"Further mechanistic study revealed the interaction between USP37 and ERalpha: USP37 regulated ERalpha signaling through modulating protein stability instead of gene expression, in which it stabilized ERalpha protein via inhibiting the K48-specific polyubiquitination process."