IndraLab

Statements

PSMD14 binds E2F1. 12 / 17
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"The PSMD14-E2F1 regulation has a great contribution to the progression of liver cancer [ 31 ]."
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"The interaction between POH1 and E2F1 was verified by co-immunoprecipitation assays in HEK293T cells ( xref )."
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"As shown in Figure XREF_FIG C, the interaction between endogenous PSMD14 and E2F1 in HNSCC was verified by immunoprecipitation assay."
33456565
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"In line with our results, a previous study revealed that POH1, a deubiquitinase, binds to and deubiquitinates E2F1, contributing to its stabilization."
33816295
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"As shown in Figure xref C, the interaction between endogenous PSMD14 and E2F1 in HNSCC was verified by immunoprecipitation assay."
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"This finding led us to hypothesize that POH1 may interact with and deubiquitinate E2F1."
26510456
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"Furthermore, the interaction between endogenous POH1 and E2F1 was demonstrated by co-immunoprecipitation ( xref )."
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"An approach using point mutants of these proteins that specifically disrupt the E2F1 and POH1 interaction may deepen our understanding of POH regulation of E2F1."
26510456
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"The interaction between POH1 and E2F1 was verified by co-immunoprecipitation assays in HEK293T cells (XREF_FIG)."
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"Furthermore, the interaction between endogenous POH1 and E2F1 was demonstrated by co-immunoprecipitation (XREF_FIG)."
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"Depletion of the COON-terminal domain (aa181-310) of POH1 significantly impaired the association between E2F1 and POH1, whereas the portion of E2F1 (aa201-437) displayed strong capability to interact with POH1 (XREF_SUPPLEMENTARY)."
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"These data collectively suggest that POH1 interacts with and stabilizes E2F1 in tumour cells."
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