IndraLab

Statements

USP37 binds X. 7 / 7
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"Our co-immunoprecipitation and confocal microscopic studies suggested a direct interaction between USP37 and HBx."
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"Further, we observed that HBx interacted with USP37 and chaperoned it out of nucleus to prevent its ubiquitination and degradation by E3 ubiquitin ligases."
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"The dichotomy in the action of two E3 ligases targeting USP37 further inspired us to investigate the possibility of direct or indirect interaction between HBx and USP37 which could reveal a bigger role of HBx in protection of USP37."
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"HBx interacts with USP37 and translocates it to cytoplasm."
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"Since, HBx and USP37 co-localized in cells, we next examined the possibility of a physical interaction between HBx and USP37."
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"Venturing further we explored the possibility of a physical interaction between HBx and USP37."
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"This study has relied on the cell culture based system where HBx was co-expressed along with USP37-DD or USP37 either in immortalized human hepatocytes or in hepatoma Huh7 cells to elucidate the oncogenic cooperation between HBx and USP37."
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