Results 81 to 90 of about 27,539 (236)
The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]
The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan +8 more
core
Revealing a novel Otubain-Like Enzyme from Leishmania infantum with deubiquitinating activity toward K48-linked substrate [PDF]
Deubiquitinating enzymes (DUBs) play an important role in regulating a variety of eukaryotic processes. In this context, exploring the role of deubiquitination in Leishmania infantum could be a promising alternative to search new therapeutic targets for ...
Azevedo, Clênia dos Santos +9 more
core +1 more source
Pro‐ATO/Allicin Liposomes for Dual‐Pathway Targeting of p53‐Mutant Tumors
Schematic illustration of the “pro‐ATO”/allicin liposomal strategy. Liposomal encapsulation improves the stability and bioavailability of both agents while masking allicin's odor. Upon release in the tumor microenvironment, ATO reactivates structural p53 mutants, and allicin inhibits ATR signaling while releasing H2S, collectively inducing synthetic ...
Xiaoling Xu +11 more
wiley +1 more source
USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation [PDF]
Physiological adaptation to proteotoxic stress in the endoplasmic reticulum (ER) requires retrotranslocation of misfolded proteins into the cytoplasm for ubiquitination and elimination by ER-associated degradation (ERAD).
Clemons, William M., Jr. +6 more
core +1 more source
Glutamine deprivation triggers transient DNA damage yet activates adaptive repair in hepatocellular carcinoma cells. We identify TRIB3 as a stress‐induced nuclear scaffold that associates with DDX5 and G‐quadruplex DNA atBRCA1 andRAD51AP1 promoters. TRIB3 loss increases G4 accumulation, suppresses HR gene transcription, elevates γ‐H2A.X, and sensitizes
Qiang Ji +10 more
wiley +1 more source
Roles of ubiquitin-specific proteases in inflammatory diseases
Ubiquitin-specific proteases (USPs), as one of the deubiquitinating enzymes (DUBs) families, regulate the fate of proteins and signaling pathway transduction by removing ubiquitin chains from the target proteins.
Rui Chen +18 more
doaj +1 more source
After chemotherapy for the treatment of metastatic bladder urothelial carcinoma (UC), most patients inevitably encounter drug resistance and resultant treatment failure.
Kuan-Lin Kuo +10 more
doaj +1 more source
Riding the DUBway: regulation of protein trafficking by deubiquitylating enzymes [PDF]
Ubiquitylation is a key regulator of protein trafficking, and much about the functions of ubiquitin ligases, which add ubiquitin to substrates in this regulation, has recently come to light.
Millard, Stephen A., Wood, Susan M.
core +2 more sources
In this study, we identified an NSUN6‐dependent m5C‐modified tsRNA, m5C‐tRF3b CysGCA‐23 (mtRC), that is downregulated in BC and inversely correlated with disease progression. Mechanistically, mtRC suppresses BC malignancy by stabilizing RBM4, attenuating glycolysis, and thereby limiting H3K18 lactylation–mediated activation of IL1RAP and VASH2 ...
Xiaoling Ying +16 more
wiley +1 more source
A Novel Type of Deubiquitinating Enzyme [PDF]
A previous report from this laboratory described two novel proteins that have sequence similarity to A20, a negative regulator of NF-kappaB (Evans, P. C., Taylor, E. R., Coadwell, J., Heyninck, K., Beyaert, R., and Kilshaw, P. J. (2001) Biochem. J. 357, 617-623).
Paul C, Evans +9 more
openaire +2 more sources

