Ubiquitin Specific Peptidase 14 (USP14) ELISA Kits

Human Ubiquitin Specific Peptidase 14 (USP14) interaction partners

1. By displacing USP14, TRIM11 changes proteasome composition and suppresses both catalytic and non-catalytic effects of USP14

2. Usp14 and Ube3c cycle together on and off proteasomes, and the presence of ubiquitinated substrates promotes their association. This mechanism enables proteasome activity to adapt to the supply of substrates.

3. our results demonstrated that vimentin in human GC tissues and cell lines was upregulated due to its de-ubiquitination after interactions with USP14 and miR-320a, which could promote the aggressiveness of GC cells.

4. Study detected elevated USP14 expression at both mRNA and protein levels, and was significantly associated with distant metastasis.

5. These findings suggested that USP14 induces NF-kappaB activity and ERK1/2 phosphorylation triggered by microbial infection.

6. Ubiquitin-specific protease 14 regulates cell proliferation and apoptosis in oral squamous cell carcinoma

7. our report demonstrates significant value in targeting USP14/UCHL5 with VLX1570 in drug-resistant Waldenstrom macroglobulinemia (WM) and carries a high potential for clinical translation

8. USP14 promotes prostate cancer progression.

9. without a ubiquitinated substrate present, Usp14 suppresses multiple proteasomal activities, especially basal ATP consumption and degradation of non-ubiquitinated proteins. These allosteric effects thus reduce ATP hydrolysis by inactive proteasomes and nonspecific proteolysis and enhance proteasomal specificity for ubiquitinated proteins.

10. USP14 regulates autophagy by negatively controlling K63 ubiquitination of Beclin 1

11. USP14 plays an important role in the progression and metastasis of esophageal squamous cell carcinoma.

12. USP14 participates in CAM-DR of MM through acting as a bridge between Bcl-xl apoptotic pathway and Wnt-signaling pathways and may be represented as a good candidate for pursuing clinical trials in MM.

13. Results show that USP14 mRNA is overexpressed in hepatocellular carcinoma (HCC) tissues and inversely correlates with miR-4782-3p level which binds to USP14 3'UTR to regulate its expression.

14. Results found USP14 amplification and overexpression in many different cancers. Its overexpression in low-expression cell lines promoted cell proliferation and migration, whereas its downregulation suppressed tumor cell proliferation, increased apoptosis rate, and decreased cell migration and invasion suggesting an oncogenic role in various types of cancer.

15. Increased USP14 expression in patients with breast cancer was associated with a poorer prognosis.

16. Akt-mediated phosphorylation of USP14 at Ser432, which normally blocks its catalytic site in the inactive conformation, activates its deubiquitinating activity in vitro and in cells.

17. our findings suggested that USP14 is involved in the progression of hepatocellular carcinoma(HCC) and may be a useful therapeutic target in HCC

18. Cell surface ubiquitination precedes endocytosis, after which USP14 acts as an ubiquitin-binding protein that targets the ubiquitinated GABA B receptor to lysosomal degradation and promotes its deubiquitination.

19. USP14 shows a marked preference for ubiquitin-cyclin B conjugates that carry more than one ubiquitin modification or chain

20. our findings suggest that USP14 is involved in the progression of epithelial ovarian cancer

Mouse (Murine) Ubiquitin Specific Peptidase 14 (USP14) interaction partners

1. the data indicate that functional Usp14 enhances direct Antigen presentation, preferentially of defective ribosomal product-derived peptides, suggesting that the processing of defective ribosomal product-derived peptides is in some ways different from other forms of Antigen.

2. The homeostasis of Ubiquitin in USP14-/-mouse embryonic fibroblasts was markedly perturbed because of facilitated clearance of Ubiquitin.

3. Usp14 and Ube3c cycle together on and off proteasomes, and the presence of ubiquitinated substrates promotes their association. This mechanism enables proteasome activity to adapt to the supply of substrates.

4. analysis of the molecular mechanisms through which CBP stability is regulated by FBXL19 and USP14, which results in the modulation of chromatin remodeling and the expression of cytokine-encoding genes

5. These findings suggested that USP14 induces NF-kappaB activity and ERK1/2 phosphorylation triggered by microbial infection.

6. without a ubiquitinated substrate present, Usp14 suppresses multiple proteasomal activities, especially basal ATP consumption and degradation of non-ubiquitinated proteins. These allosteric effects thus reduce ATP hydrolysis by inactive proteasomes and nonspecific proteolysis and enhance proteasomal specificity for ubiquitinated proteins.

7. USP14's catalytic activity is required for nervous system structure and function and has an ongoing role in NMJ synaptic transmission. USP14 regulation of the ubiquitination status of protein kinases, coordinates NMJ intracellular signaling pathways.

8. Overexpression of the Usp14 reduces cellular aggregates in mutant Htt-expressing cells mainly via the ubiquitin proteasome system.

9. USP14 modulates hippocampal short-term plasticity and vesicle number independent of its deubiquitinating activity.

10. Differences in genetic background were shown to affect ubiquitin expression and dramatically alter the phenotypes caused by USP14 deficiency.

11. Data indicate that increased levels of phosphorylated tau correlated with the onset of axonal varicosities in the ubiquitin-specific protease 14 (Usp14)-deficient mice.

12. miR-124 promotes neuronal survival under ischemic conditions via Usp14-dependent REST degradation.

13. overexpression of HA-USP14 increased TNFalpha

14. Oxidative stress increasd USP14 expression, and beta-carotene dose-dependently inhibited increased expression in mouse skeletal muscle myotubes.

15. ubiquitinated loosely folded proteins, after becoming bound to the 26 S, interact with Ubp6/Usp14 or Uch37 to activate ATP hydrolysis and enhance their own destruction

16. USP14 has a role in regulating synaptic activity in mammals

17. Usp14 functions to maintain the cellular levels of monomeric ubiquitin in mammalian cells, and that alterations in the levels of ubiquitin may contribute to neurological disease

18. Results suggest that Uch-L1 and Usp14 may differentially affect the ubiquitin proteasome system and synaptic activity by regulating different pools of ubiquitin in the cell.

19. A mutated axJ gene locus, encoding the ubiquitin-specific protease 14 (Usp14), negatively influences GABAA receptor turnover.