IndraLab

Statements

USP15 inhibits proteolysis. 5 / 5
| 5
reach
"We found that Nef binds to ubiquitin protein ligase E3A (UBE3A and E6AP) which induces protein degradation by attaching Ub to substrates, i.e. Nef associated with two functionally antagonistic proteins in the UPS mediated protein degradation processes, suggesting that UBE3A could be a major cellular component in regulating USP15 mediated viral protein degradation by interacting with Nef and USP15 simultaneously or independently."
27460547
reach
"To investigate Nef role in protein degradation, we seek to identify cellular proteins involved in the UPS mediated protein degradation through association with Nef and found ubiquitin specific protease 15 (USP15) which stabilizes proteins by deubiquitylation and by preventing autoubiquitylation of substrates."
27460547
reach
"Further investigation demonstrated the significance of Nef- and USP15 mediated viral and cellular protein degradation with respect to the regulation of the virus life cycle and HIV-1 and host cell competition that is essential for AIDS progression."
27460547
reach
"Overexpression of USP15 increased VGLL4 protein level by inhibiting protein degradation, whereas the depletion of USP15 resulted in VGLL4 degradation and thus enhanced tumorigenesis and progression of[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
38431034
reach
"Mechanistic investigations further indicated that the reduced expression of ACSL4 in GIST is attributed to excessive protein degradation mediated by the E3 ligase TRIM21 and the deubiquitinase USP15."
38182686