IndraLab

Statements

USP14 inhibits proteolysis. 22 / 23
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"Thus, the presence of Usp14 on the 26S helps reduce wasteful ATP consumption and nonselective proteolysis."
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"In contrast, RNAi of Uch37 or Usp14 had no detectable effect on cell growth, proteasome structure or proteolytic capacity, but accelerated cellular protein degradation."
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"The RNAi of UCHL5 or USP14 alone does not affect cell growth and proteasome composition but accelerates cellular protein degradation; however, RNAi of both UCHL5 and USP14 can inhibit cellular protein degradation."
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"We also found enhanced expression of transcripts encoding two ubiquitin-specific proteases (Table 2), including USP14 that suppresses protein degradation through deubiquitination of proteasome substrates, non-catalytic inhibition of proteasome activity, and by regulating autophagy (de Poot et al. 2017; Xu et al. 2016)."
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"Interestingly, b-AP15, a dual inhibitor of Usp14 and Uch37, was shown to prevent protein degradation and inhibit tumor progression in acute myeloid leukemia models [222]."
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"Importantly, whereas knockdown of POH1 interferes with the proteasome assembly, depletion of either USP14 or UCH37 alone does not affect or even slightly enhances protein degradation rates."
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"A study conducted in 2010 showed that USP14 inhibits protein degradation by the proteasome in murine embryonic fibroblasts."
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"RNAi of either Uch37 or USP14 (the mammalian homologue of yeast Ubp6) accelerates protein degradation."
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"USP14 , one member of the ubiquitin-specific proteases DUBs family , is associated with the proteasome complex and inhibits proteolysis by catalyzing protein deubiquitination ( 14 ) ."
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"USP14 regulates proteasome activity and pharmacologic inhibition of USP14 increases the rate of protein degradation in the cell XREF_BIBR."
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"Although present in Xenopus extracts (N.V.D., R.W.K., unpublished data), levels of USP14 associated with proteasomes in extract may be insufficient to impede proteolysis."
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"These studies further confirmed two observations noted independently, i.e., (1) that inhibition of USP14 up-regulates proteasomal proteolysis in the cells from young donors, perhaps by virtue of 20S gate opening, but fail to do so in cells from the elderly, and (2) that inhibition of USP14 in T cells from both young and elderly donors influences the levels of poly-ubiquitinated proteins and free ubiquitin."
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"Small molecule inhibitor of USP14, IU1, enhances proteasomal proteolysis of ubiquitinated substrate in T cells obtained from young but not those from elderly donors."
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"In contrast, RNAi of either UCHL5 or USP14 alone did not affect cell growth, proteasome structure, or proteolytic capacity, but increased the rate of protein degradation."
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"Mouse embryonic fibroblasts lacking USP14 show enhanced clearance of several disease related proteins, including tau and polyglutamine expanded ataxin-3, and overexpression of catalytically inactive USP14 increases protein degradation [XREF_BIBR]."
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"Knockdown of USP2 or USP14 accelerated protein degradation of TNF-alpha, and abolished the effect of miR-124 on TNF-alpha protein stability."
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"Theoretically, a true proteolysis associated substrate of USP14 will be degraded by USP14 KD through its elevated protein ubiquitination level, and will interact with USP14."
30425250
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"USP14 reduces proteolysis in a substrate-specific manner by rapidly trimming the tagging ubiquitin chains before the 26S proteasome can initiate degradation of that substrate [ 350 ] ."
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"UBL domain of Usp14 and other proteins stimulates proteasome activities and protein degradation in cells."
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"The deubiquitinating enzyme Usp14 allosterically inhibits multiple proteasomal activities and ubiquitin independent proteolysis."
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"Since the loss of USP14 accelerates cellular proteolysis, we performed a quantitative proteomic analysis to determine the levels of proteins in WT H4 cells, H4 USP14-KO cells, and H4 USP14-KO cells complemented with WT USP14, S143A and S432A (AA), or S143D and S432D (DD) mutants."
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"USP14 was found to promote the UPS-mediated K48-ubiquitinated AR protein degradation."
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