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USP14 deubiquitinates Proteasome. 5 / 5
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"USP14 deubiquitinates proteasome bound substrates that are ubiquitinated at multiple sites."

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"USP14 inhibits mitophagy and regulates proteasome activity through deubiquitinating proteasome-binding substrates, thereby influencing the progression of PD [184]."

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"Given that proteasome deubiquitination mediated by USP14 has fundamental roles in regulating proteasomal degradation of ubiquitinylated substrates XREF_BIBR XREF_BIBR, it is rational to speculate that perturbation of ubiquitin chain trimming functions of PfUSP14 may impact intraerythrocytic parasite development and cause difficulties for parasite egress from the host cell."

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"USP14 deubiquitinates proteasome bound substrates that are ubiquitinated at multiple sites."

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"USP14, one of three proteasome‐associated DUBs, regulates protein degradation by deubiquitinating proteasome‐bound substrates (Lee et al., 2016) and modulates proteasome activity through allosteric mechanisms (Kim & Goldberg, 2017; Peth et al., 2009)."