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"Using coimmunoprecipitation (Co-IP) studies, we demonstrated that BRCC36 can bind to β-catenin ( Fig. 5 )."

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"In addition, coimmunoprecipitation showed that BRCC36 could bind to β-catenin."

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"We found that BRCC36 can bind to β-catenin, and overexpression of BRCC36 can inhibit β-catenin phosphorylation, which suggested that BRCC36 might regulate various protein post-translational modificati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Moreover, our mechanistic studies revealed that BRCC36 interacted with and deubiquitinated β-catenin and inhibited Wnt/β-catenin signalling activity."

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"To elucidate the molecular mechanisms by which BRCC36 regulates the Wnt/β-catenin signalling pathway, we consulted the STRING database and performed protein‒protein docking analysis to test whether there was an interaction between BRCC36 and β-catenin."

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"To elucidate the mechanism involved, we first identified the interaction between BRCC36 and β-catenin through a STRING database search and molecular docking, colocalization (immunofluorescence double staining), and Co-IP assays."

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"Third, we demonstrated the interaction between BRCC36 and β-catenin by endogenous and exogenous Co-IP experiments, a semiendogenous Co-IP experiment is needed to further confirm our conclusions."