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The protein encoded by TRIM25 is a member of the tripartite motif (TRIM) family. Zusätzlich bieten wir Ihnen TRIM25 Antikörper (151) und TRIM25 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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The RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain, which we postulate to be a novel RNA-binding domain.
TRIM25 inhibits hepatocellular carcinoma progression by targeting MTA1 (zeige MTA1 Proteine).
TRIM25 is a key determinant of breast cancer metastasis.
V interaction with TRIM25 and RIG-I (zeige DDX58 Proteine) prevents TRIM25-mediated ubiquitination of RIG-I (zeige DDX58 Proteine) and disrupts downstream RIG-I (zeige DDX58 Proteine) signaling to the mitochondrial antiviral signaling protein (zeige MAVS Proteine).
HPV E6 oncoprotein antagonizes the activation of the cytoplasmic innate immune sensor RIG-I (zeige DDX58 Proteine) by targeting its upstream regulatory enzymes TRIM25 and USP15 (zeige USP15 Proteine). We further show that the RIG-I (zeige DDX58 Proteine) signaling cascade is important for an antiviral innate immune response to HPV16 infection
this study shows thatTRIM25 targets ERG (zeige ERG Proteine) for degradation in prostate cancer
TRIM25 actively participates in higher-order assembly of the RIG-I (zeige DDX58 Proteine) signalosome.
Our results indicate that TRIM25 is associated with cisplatin resistance and 14-3-3sigma-MDM2 (zeige MDM2 Proteine)-p53 (zeige TP53 Proteine) 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 (zeige TP53 Proteine)-MDM2 (zeige MDM2 Proteine) feedback loop contributing to the pathogenesis of thoracic aortic dissection may be linked to TRIM25 overexpression.
TRIM25 as a key determinant of breast cancer metastasis.
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 (zeige C3 Proteine)(488) and Trp (zeige TYRP1 Proteine)(621)) in the TRIM25 B30.2 domain are critical for binding to the RIG-I (zeige DDX58 Proteine) CARDs.
Two well-known E3 ubiquitin ligases, Trim25 (also called Efp) and Trim71 (zeige TRIM71 Proteine) (also called Lin41 (zeige TRIM71 Proteine)), 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