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TRIM32 as a crucial positive regulator of Herpes Simplex Virus type 1 (HSV-1) induced IFN-beta production in corneal epithelial cells, and it played a predominant role in clearing HSV-1 from the cornea.
HSP70-TRIM32 complex is biochemically distinct from the previously characterized 14-3-3-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 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 ligases TRIM25 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-dependent signalling
these findings suggest that TRIM32 might play important roles in the hepatocarcinogenesis.
results show a novel molecular cascade involving miR-155 and TRIM32 leading to HIV-1 Tat-induced attenuated proliferation of neural precursor cells; study also uncovered an unidentified role for miR-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)-NHL proteins TRIM2, TRIM3, TRIM32 and TRIM71, 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) activation: [SseK3]
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
Data indicate that variants in tripartite motif-containing 32 protein (TRIM32) in two patients presenting nonspecific limb-girdle muscular dystrophy type 2H (LGMD2H) were identified by using high-throughput variants screening techniques.
TRIM32, an E3 ubiquitin ligase, promotes HIV reactivation from latency by directly modifying IkappaBalpha
Identification of TRIM32 as a novel p53 target and as a novel negative regulator for p53.
Trim32 is a positive regulator of ACD that acts against MYCN and should be considered as a tumor-suppressor candidate
Deletions near the 3' terminus of ASTN2, a subset of these deletions also includes TRIM32, are significantly enriched in neurodevelopmental disorder subjects.
BBS11 promotes accumulation of NPHP7, changing the properties of NPHP7. TRIM32 Modulates the Transcriptional Activities of Glis2
a novel connection between ubiquitylation and phosphorylation pathways, which could modulate a variety of cell events by stimulating the formation of the 14-3-3-TRIM32 signaling complex.
TRIM32 assembles polyubiquitin chains as a Ubc5-linked thioester intermediate.
TRIM32 protein modulates type I interferon induction and cellular antiviral response by targeting MITA/STING protein for K63-linked ubiquitination
suppression of Trim32 promotes the recovery of neurological function after traumatic brain injury.
the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32.
TRIM32 is a novel essential positive factor modulating axonal regeneration and the recovery of motor function following SCI, possibly through suppressing proliferation of glial cells.
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 and Oct4), to modulate cell fate transitions.
NDRG2 accumulated in skeletal muscle and myoblasts in the absence of TRIM32. NDRG2 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-dependent manner.
Data show that RNA helicase DDX6 colocalizes with ubiquitin-protein ligase 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.
Trim32 reduces PI3K-Akt-FoxO signaling in normal and atrophying muscle by promoting plakoglobin-PI3K dissociation.
TRIM32 physically interacts with TAp73 and promotes its ubiquitination and degradation while TAp73 regulates TRIM32 gene expression.
During fasting, desmin phosphorylation increases and enhances Trim32-mediated degradation of the desmin cytoskeleton, which appears to facilitate the breakdown of Z-bands and thin filaments.
Loss of TRIM32 function induces a LGMD2H-like phenotype and strongly affects muscle regeneration in vivo.
Study provides evidence that the neuronal fate determinant TRIM32 binds to the protein kinase C zeta. Through this interaction, TRIM32 is retained in the cytoplasm.
one potential mechanism of LGMD2H might be destabilization of mutated TRIM32 protein leading to a null phenotype.
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