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TRIM32 as a crucial positive regulator of Herpes Simplex Virus type 1 (HSV-1) induced IFN-beta (Montrer IFNB1 Kits ELISA) production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea.
HSP70 (Montrer HSP70 Kits ELISA)-TRIM32 complex is biochemically distinct from the previously characterized 14-3-3 (Montrer YWHAQ Kits ELISA)-TRIM32 phospho-complex.
Data suggest that, in cardiomyocytes, TRIM32 attenuates activation of SRF signaling and hypertrophy due to dysbindin; TRIM24 promotes these effects. TRIM32 promotes dysbindin degradation; TRIM24 protects dysbindin from degradation. (TRIM = tripartite motif-containing protein; SRF = serum response factor)
Duchenne muscular dystrophy (Montrer DMD Kits ELISA) muscles showed a selective up-regulation of the ubiquitin ligase tripartite motif-containing protein 32 (TRIM32). The induction of TRIM32 was due to a transcriptional effect and it correlated with disease severity.
we provide a detailed characterization of the TRIM (Montrer TRAT1 Kits ELISA) ligases TRIM25 (Montrer TRIM25 Kits ELISA) and TRIM32 and show how their oligomeric state is linked to catalytic activity
that TRIM32 plays a protective role in aortic banding-induced pathological cardiac remodelling by blocking Akt (Montrer AKT1 Kits ELISA)-dependent signalling
these findings suggest that TRIM32 might play important roles in the hepatocarcinogenesis.
results show a novel molecular cascade involving miR (Montrer MLXIP Kits ELISA)-155 and TRIM32 leading to HIV-1 Tat (Montrer TAT Kits ELISA)-induced attenuated proliferation of neural precursor cells; study also uncovered an unidentified role for miR (Montrer MLXIP Kits ELISA)-155 in modulating human neural stem cell proliferation, helping in better understanding of neural precursor cells and diseased brain
Studies indicate most-studied TRIpartite Motif (TRIM (Montrer TRAT1 Kits ELISA))-NHL (Montrer RTEL1 Kits ELISA) proteins TRIM2 (Montrer TRIM2 Kits ELISA), TRIM3 (Montrer TRIM3 Kits ELISA), TRIM32 and TRIM71 (Montrer TRIM71 Kits ELISA), and their mutations have been linked to diseases.
Results suggest that Salmonella effector SseK3 binding to host tripartite motif-containing 32 protein (TRIM32) in the inhibition of nuclear factor kappa B (NF-kappaB (Montrer NFKB1 Kits ELISA)) activation: [SseK3]
TRIM32 protein expression is defective in atopic dermatitis lesional skin.
In summary, the data presented here reveal that TRIM32 directly regulates at least two of the four Yamanaka Factors (cMyc (Montrer MYC Kits ELISA) and Oct4 (Montrer POU5F1 Kits ELISA)), to modulate cell fate transitions.
TRIM32 represents a model of intrinsic immunity, in which a host protein directly senses and counters viral infection in a species specific fashion by directly limiting viral replication
NDRG2 (Montrer NDRG2 Kits ELISA) accumulated in skeletal muscle and myoblasts in the absence of TRIM32. NDRG2 (Montrer NDRG2 Kits ELISA) overexpression in myoblasts led to reduced cell proliferation and delayed cell cycle withdrawal during differentiation.
TRIM32 overexpression promotes cell oncogenic transformation and tumorigenesis in mice in a largely p53 (Montrer TP53 Kits ELISA)-dependent manner.
Data show that RNA helicase DDX6 (Montrer DDX6 Kits ELISA) colocalizes with ubiquitin-protein ligase (Montrer UBE2K Kits ELISA) TRIM32 in neural stem cells and neurons and that it increases the activity of microRNA Let-7a.
TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress.
The results highlight the function of the cell fate-determinant TRIM32 for a balanced activity of the adult neurogenesis process.
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. The protein has also been localized to the nucleus, where it interacts with the activation domain of the HIV-1 Tat protein. The Tat protein activates transcription of HIV-1 genes.
E3 ubiquitin-protein ligase TRIM32
, tripartite motif-containing 32
, TAT-interactive protein, 72-KD
, tripartite motif containing 32
, 72 kDa Tat-interacting protein
, tripartite motif-containing protein 32
, zinc finger protein HT2A
, zinc-finger protein HT2A
, bM468K2.2 (tripartite motif protein 32)
, tripartite motif protein 32
, zinc finger protein 117