IndraLab

Statements

UCHL3 binds EEF1A1. 11 / 11
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"Our findings revealed that UCHL3 binds and stabilizes EEF1A1 through deubiquitination."
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"Our above findings showed that UCHL3 could bind to EEF1A1 and mediated its deubiquitination."
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"Therefore, we aimed to elucidate the underlying molecular mechanism of UCHL3 binding to EEF1A1."
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"To further illustrated the effect of the binding between EEF1A1 and UCHL3 on the function of UCHL3, we conducted transwell and sphere formation assays."
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"UCHL3 binds to EEF1A1 through the lysine site, which reduces the ubiquitination level of EEF1A1."
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"Our findings revealed that UCHL3 binds and stabilizes EEF1A1 through deubiquitination."
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"UCHL3 and EEF1A1 could bind with each other in both HEP3B and HUH7 cells."
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"EEF1A1 binds to UCHL3 through the lysine site."
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"Our above findings showed that UCHL3 could bind to EEF1A1 and mediated its deubiquitination."
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"Therefore, we aimed to elucidate the underlying molecular mechanism of UCHL3 binding to EEF1A1."
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"The results of protein co-immunoprecipitation revealed a reduced binding between EEF1A1 and UCHL3 after four lysine sites are mutated, indicating that UCHL3 primarily interacts with EEF1A1 through these sites (Fig.  xref E)."
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