IndraLab

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"Therefore, we conclude that USP10 interacts with PTEN and AMPKalpha, inhibits their polyubiquitylation, and as a result stabilizes PTEN and AMPKalpha.Next, we examined whether Rapamycin, a well known [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Inversely, endogenous PTEN and AMPKalpha interacted with endogenous USP10 in HCC-LM3 and HUH7 cells."

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"Mechanistically, USP10 interacts and stabilizes PTEN and AMPKalpha by inhibiting their polyubiquitylation."

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"We further demonstrated that USP10 directly interacted with and stabilized PTEN via deubiquitination."

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"Furthermore, USP10 can also interact with and deubiquitinate PTEN, USP10 inhibition stimulates tumor growth and invasion, but this effect can be abolished by reinserting PTEN (Sun et al., 2018)."

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"We found using co-immununoprecipitation/immunoblotting that USP10 interacted with PTEN and reduced the K63-linked polyubiquitination of PTEN mediated by TRIM25 in non-small cell lung cancer (NSCLC) cells."

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"Mechanistically, USP10 interacts with and stabilizes PTEN and AMPKalpha by inhibiting their polyubiquitylation, and subsequently suppresses the activity of mTOR signaling pathway."

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"The interaction between USP10 and Phosphatase And Tensin Homolog (PTEN) was examined by co-immunoprecipitation."