IndraLab

Statements

USP4 binds PPIA. 12 / 12
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"Collectively, these data indicated that both endogenous and exogenous USP4 and CypA proteins can interact."
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"We presumed that might be because the USP4 and CypA complex does not increase the active form of CrkII directly in HCC cells, but inhibits the formation of its inactive form and disrupts the balance between the two molecules."
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No evidence text available
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"We observed that USP4 interacted with CypA and inhibited CypA degradation via deubiquitination in HCC cells."
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"An endogenous Co-IP assay was performed in MHCC97H cells, and the results showed that endogenous USP4 forms a complex with endogenous CypA in MHCC97H cells (Fig.  xref )."
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"The results revealed that USP4 forms a complex with CypA, both endogenously and exogenously, and is responsible for CypA stabilization via deubiquitination."
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"Subsequently, the USP4 and CypA complex activated the MAPK signaling pathway and prevented CrkII phosphorylation."
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"We observed that USP4 interacted with CypA and inhibited CypA degradation via deubiquitination in HCC cells."
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"To find the downstream mechanism of the USP4 and CypA complex in HCC development, the MAPK and CrkII signaling pathways were chosen to test in the current study."
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"The results revealed that USP4 forms a complex with CypA, both endogenously and exogenously, and is responsible for CypA stabilization via deubiquitination."
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"An endogenous Co-IP assay was performed in MHCC97H cells, and the results showed that endogenous USP4 forms a complex with endogenous CypA in MHCC97H cells."
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"To determine whether USP4 regulates cell pathways depends on CypA in HCC, we next examined the USP4 and CypA complex and related protein levels in MHCC97H and Huh7 cells using western blotting."
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