IndraLab

Statements


EIF3F affects E protein
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EIF3F deubiquitinates E protein. 2 / 2
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"Meanwhile, EIF3S5 cannot promote E protein deubiquitination in LAMR1-knockdown HeLa cells (Figure 5d), highlighting that LAMR1 recruits EIF3S5 to mediate E protein deubiquitination."

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"We found that LAMR1 could interact with UPS13 (Figure 5a, lane 2) and EIF3S5 (Figure 5a, lane 9), but not with the control (Figure 5a, lane 1) or other proteins (Figure 5a, lanes 3–8, and 10), suggesting that EIF3S5 and UPS13 might be involved in the LAMR1-mediated deubiquitination of E protein."
EIF3F affects env
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EIF3F leads to the deubiquitination of env. 1 / 1
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"Knockdown of EIF3S5 reduced Env deubiquitination and increased the levels of NS5, Env, and viral RNA in infected HeLa cells (Hu et al., 2021) ."
EIF3F affects Notch
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EIF3F deubiquitinates Notch. 1 / 1
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"The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor."
EIF3F affects NOTCH1
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EIF3F deubiquitinates NOTCH1 on K1759. 1 / 1
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"The activated form of notch needs to be deubiquitinated before being processed by the gamma-secretase activity and entering the nucleus, where it fulfills its transcriptional function. The enzyme accounting for this deubiquitinase activity is eif3f, known so far as a translation initiation factor."