IndraLab

Statements

USP11 binds mgl-1. 13 / 13
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"In this study, we demonstrated a direct interaction between USP11 and Mgl-1."
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"These data indicate that USP11 interacts with Mgl-1, and Mgl-1 has multiple binding sites to USP11."
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"To reconfirm the interaction between Mgl-1 and USP11, we investigated the interaction between Mgl-1 and USP11 in a Glutathione S-transferase (GST) pull-down in vitro assay."
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"We next evaluated the endogenous interaction between Mgl-1 and USP11."
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"The USP11 protein was retained by GST-Mgl-1 but not by GST alone, indicating that Mgl-1 binds to USP11."
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"Immunoprecipitation assay was performed with an anti-USP11 antibody and the result showed that interaction between USP11 and Mgl-1 was decreased in knockdown of RanBPM."
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"Mgl-1 interacts with USP11."
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"This result indicates that RanBPM mediates the interaction between USP11 and Mgl-1."
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"We next investigated the functional consequence of interaction between Mgl-1 and USP11."
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"The results demonstrate both in vitro and in vivo interactions between Mgl-1 and USP11."
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"To address whether RanBPM can mediate interaction between USP11 and Mgl-1, we used RanBPM knockdown cells."
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"In the present study, we identified the interaction between USP11 and Mgl-1."
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"Binding between Mgl-1 and USP11 was established with the GST-pull down assay, and the GST-Mgl-1 fusion protein was incubated with the USP11 transfected cell lysate."
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