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The protein encoded by TRIM25 is a member of the tripartite motif (TRIM) family. Additionally we are shipping TRIM25 Antibodies (136) and TRIM25 Kits (2) and many more products for this protein.
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TRIM25 actively participates in higher-order assembly of the RIG-I (show DDX58 Proteins) signalosome.
Our results indicate that TRIM25 is associated with cisplatin resistance and 14-3-3sigma-MDM2 (show MDM2 Proteins)-p53 (show TP53 Proteins) signaling pathway is involved in this process, suggesting targeting TRIM25 may be a potential strategy for the reversal of cisplatin resistance.
expression of TRIM25 might be critical for lung cancer cell migration, proliferation as well as doxorubicin resistance.
Disturbed p53 (show TP53 Proteins)-MDM2 (show MDM2 Proteins) feedback loop contributing to the pathogenesis of thoracic aortic dissection may be linked to TRIM25 overexpression.
the data uncover TRIM25 as a bona fide zinc-finger antiviral protein (show ZC3HAV1 Proteins) cofactor that leads to increased zinc-finger antiviral protein (show ZC3HAV1 Proteins) modification enhancing its translational inhibition activity.
Studies showed that 70% of breast cancer patients were positive for Trim25 expression.
we provide a detailed characterization of the TRIM (show TRAT1 Proteins) ligases TRIM25 and TRIM32 (show TRIM32 Proteins) and show how their oligomeric state is linked to catalytic activity
The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase (show MUL1 Proteins), thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I (show DDX58 Proteins)) and inhibiting TRIM25-mediated RIG-I (show DDX58 Proteins) ubiquitination and activation.
TRIM25 is required for Zinc finger antiviral protein (show ZC3HAV1 Proteins) optimal binding to target mRNA.
TRIM25 may exert its function through TGF-beta (show TGFB1 Proteins) pathway.
Studies indicated that mice with disrupted Trim25 were viable and fertile, uterine response to oestrogen was greatly attenuated and the uteri were underdeveloped.
Two key residues (Asp (show C3 Proteins)(488) and Trp (show TYRP1 Proteins)(621)) in the TRIM25 B30.2 domain are critical for binding to the RIG-I (show DDX58 Proteins) CARDs.
Two well-known E3 ubiquitin ligases, Trim25 (also called Efp) and Trim71 (show TRIM71 Proteins) (also called Lin41 (show TRIM71 Proteins)), are validated as RNA-binding proteins, revealing a potential link between RNA biology and protein-modification pathways.
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 the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene.
tripartite motif-containing 25
, E3 ubiquitin/ISG15 ligase TRIM25
, tripartite motif containing 25
, RING finger protein 147
, estrogen-responsive finger protein
, tripartite motif protein TRIM25
, tripartite motif-containing protein 25
, ubiquitin/ISG15-conjugating enzyme TRIM25
, zinc finger protein 147 (estrogen-responsive finger protein)
, zinc finger protein-147
, tripartite motif protein 25
, zinc finger protein 147