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Tripartite motif protein 25 (TRIM25) is an E3 ligase that ubiquitinates multiple substrates within the RLR signalling cascade and plays both RING (really interesting new gene)-dependent and RING-independent roles in RIG-I-mediated IFN induction. We report that the PRY-SPRY domain of TRIM25 interacts...
ORGANISM(S): Homo sapiens (Human) 
2021-09-08 | PXD028122 | Pride
The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individ...
ORGANISM(S): Homo sapiens (Human) 
2022-08-02 | PXD034024 | Pride
TRIM25
Exogenous RNA surveillance by proton-sensing TRIM25
Therapy resistance is still a major reason for treatment failure in colorectal cancer (CRC). Previously, we identified the E3 ubiquitin ligase TRIM25 as a novel suppressor of caspase-2 translation, thereby contributing to apoptosis resistance of CRC cells towards chemotherapeutic drugs. We herein re...
ORGANISM(S): Homo sapiens (Human) 
2023-01-05 | PXD037182 | Pride
Degradation of AGO2 by TRIM25 drives cancer progression and chemotherapy resistance
Destruction of VISTA by TRIM25 ablation in T cells potentiates cancer immunotherapy
Exogenous mRNAs require cellular machinery for delivery and translation but also encounter inhibitory factors. To investigate their regulation, we performed genome-wide CRISPR screens with in vitro-transcribed mRNAs in lipid nanoparticles (LNPs). Heparan sulfate proteoglycans and vacuolar ATPase wer...
ORGANISM(S): Homo sapiens 
2025-04-04 | GSE264535 | GEO
RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination
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