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The protein encoded by TRIM14 is a member of the tripartite motif (TRIM) family. Additionally we are shipping TRIM14 Antibodies (33) and and many more products for this protein.
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we identify the tripartite motif-containing protein (TRIM14) as a target of miR (show MLXIP Proteins)-195-5p. Therefore, we reason that the tumor suppressor role of miR (show MLXIP Proteins)-195-5p in oral squamous cell carcinoma is dependent on the interaction with TRIM14.
In searching for mechanisms how TRIM14 exerts its antiviral function we found that TRIM14 interacted with HCV encoded non-structural protein NS5A and could strongly induce its degradation dependent on the NS5A1 subdomain. Interestingly extensive domain mapping analyses revealed that NS5A degradation was mediated by the highly conserved SPRY domain of TRIM14, which might involve the K48 ubiquitination pathway
findings define the WHIP (show WRNIP1 Proteins)-TRIM14-PPP6C (show PPP6C Proteins) mitochondrial signalosome required for RIG-I (show DDX58 Proteins)-mediated innate antiviral immunity.
study identifies new gene-type zinc finger protein 125 (RNF125 (show RNF125 Proteins)) as a negative regulator of TRIM14 in the innate antiviral immune response
survival of xenograft mice was prolonged by BsAbBmi/TRIM (show TRAT1 Proteins) treatment compared to either AbBmi-1 or AbTRIM-14 treatment. In conclusion, these results provided new evidence that BsAbBmi/TRIM (show TRAT1 Proteins) inhibited the progression of osteosarcoma, which suggest that BsAbBmi/TRIM (show TRAT1 Proteins) may be a novel anti-cancer agent for osteosarcoma therapy
MiR (show MLXIP Proteins)-15b degrades TRIM14 in oral tongue squamous cell cancer.TRIM14 role in oral tongue squamous cell cancer resistance to cisplatin.
Data suggest that tripartite motif containing 14 protein (TRIM14) might play an important role in the malignant progression of tongue squamous cells carcinoma (TSCC) and in regulation of the NF_Kappa B (NF-kappaB (show NFKB1 Proteins)) signaling pathway.
stable enhanced expression of trim14 gene in cells activates the transcription of many immunity genes and suppresses Sindbis virus reproduction, but Sindbis virus infection of HEK (show EPHA3 Proteins)-trim14 cells promotes inhibition of some genes involved in innate immunity.
Upon virus infection, TRIM14 recruits NF-kappaB essential modulator (NEMO) to the MAVS complex via ubiquitin chains.
TRIM14 inhibits cGAS degradation mediated by selective autophagy receptor p62 to promote innate immune responses.
These results demonstrate the presence of the similar mechanism of trim14 gene action in different types of mammalian cells.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic bodies and its function has not been determined. Alternative splicing results in multiple transcript variants.
tripartite motif protein TRIM14
, tripartite motif-containing 14
, tripartite motif-containing protein 14-like
, tripartite motif containing 14
, tripartite motif-containing protein 14
, PU.1 binding protein Pub
, PU.1-binding protein
, tripartite motif protein 14