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SMYD3 encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Additionally we are shipping SMYD3 Antibodies (47) and many more products for this protein.
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Postulate that AdoMet (show MAT1A Proteins) cofactor acts like a key and locks Smyd3 in a closed conformation.
Results showed that SMYD3 is overexpressed in human glioma and contributes to glioma tumorigenicity through p53 (show TP53 Proteins).
SMYD3 interacts with the human positive coactivator 4 (PC4 (show IFRD1 Proteins)) and that such interaction potentiates a group of genes whose expression is linked to cell proliferation and invasion.
Results support a proto-oncogenic role for SMYD3 in prostate carcinogenesis, mainly due to its methyltransferase enzymatic activity.
role of histone methyltransferase SMYD3 in tumors
Loss of SMYD3-HSP90 (show HSP90 Proteins) interaction leads to SMYD3 mislocalization within the nucleus, thereby losing its chromatin association. This results in reduction of SMYD3-mediated cell proliferation and, potentially, impairment of SMYD3's oncogenic activity.
High SMYD3 and pSTAT3 expressions may indicate poor prognosis of patients with gastric cancer
Results suggest that high expression of SMYD3 is related to the occurrence of esophageal squamous cell carcinoma. Also, its suppression promoted the expression of RIZ1 (show PRDM2 Proteins) suggesting a signal transduction pathway between SMYD3 and RIZ1 (show PRDM2 Proteins).
SMYD3 and MMP-9 (show MMP9 Proteins) may play important roles in tumor invasion, metastasis, and prognosis and could work as promising targets for prognostic prediction in gastric cancer.
SET and MYND domain-containing protein 3 expression and TGF-beta1 (show TGFB1 Proteins) expression in gastric cancer (GC) tissues were significantly and positively correlated. High expression levels of SMYD3 and TGF-beta1 (show TGFB1 Proteins) can indicate poor prognoses for GC patients.
The transcription-potentiating function of Smyd3 is restricted to a particular set of genes.
Epigenetic control of Foxp3 (show FOXP3 Proteins) by SMYD3 H3K4 histone methyltransferase controls iTreg development and regulates pathogenic T-cell responses during pulmonary viral infection.
These findings indicate that SMYD3 plays an important role in early embryonic lineage commitment and peri (show POSTN Proteins)-implantation development through the activation of lineage-specific genes.
represent the proof of principle that SMYD3 is a druggable target
methylation of MAP3K2 by SMYD3 increases MAP kinase signalling and promotes the formation of Ras-driven carcinomas
SMYD3 depletion prevents muscle loss and fiber size decrease; findings reveal a mechanistic link between SMYD3/BRD4 (show BRD4 Proteins)-dependent transcriptional regulation, muscle mass determination, and skeletal muscle atrophy
SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells.
This gene encodes a histone methyltransferase which functions in RNA polymerase II complexes by an interaction with a specific RNA helicase. Multiple transcript variants encoding different isoforms have been found for this gene.
SET and MYND domain containing 3
, SET and MYND domain-containing protein 3
, bA74P14.1 (novel protein)
, histone-lysine N-methyltransferase SMYD3
, zinc finger MYND domain-containing protein 1
, zinc finger protein, subfamily 3A (MYND domain containing), 1
, zinc finger, MYND domain containing 1
, SET and MYND domain-containing 3