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MEF2D is a member of the myocyte-specific enhancer factor 2 (MEF2) family of transcription factors. Additionally we are shipping MEF2D Antibodies (125) and MEF2D Kits (1) and many more products for this protein.
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MEF2D overexpression participated in the growth of lung cancers and its aberrant expression may result from the reduction of tumor suppressor miR (show MLXIP Proteins)-218.
MEF2D is a direct target of miR (show MLXIP Proteins)-19.
We found that in malignant glioma, there is an aberrantly high expression of MEF2D, which leads to poor prognosis of malignant glioma. The downregulation of MEF2D suppresses the proliferation of malignant glioma cell lines by inducing delay of S and G2/M phases of cell cycle and promoting apoptosis.
MEF2D regulates IGF-1 (show IGF1 Proteins)-induced proliferation and apoptosis in CM development, indicating IGF-1 (show IGF1 Proteins)-MEF2D pathway may be a useful target for treatment.
Pokemon (show ZBTB7A Proteins) was found to enhance the migration and invasion of hepatocellular carcinoma by increasing MEF2D expression
miR (show MLXIP Proteins)-1244 and MEF2D form an autoregulatory loop contributing to the progression of lung carcinoma.
MEF2D was also found to increase the transcription of Pokemon (show ZBTB7A Proteins) by binding myocyte enhancer factor 2 (MEF2 (show MEF2A Proteins)) sites within its promoter region, that can promote Hepatocellular carcinoma invasion
Cell cycle progression was also inhibited by MEF2D suppression.
OA induced cell cycle arrest in lung cancer cells through miR (show MLXIP Proteins)-122/Cyclin G1 (show CCNG1 Proteins)/MEF2D pathway. This finding may contribute to the understanding of the molecular mechanism of OA's anti-tumor activity
MEF2C and MEF2D interact with the E3 ligase F-box protein SKP2, which mediates their subsequent degradation through the ubiquitin-proteasome system.
These findings uncover a novel role for Mef2c (show MEF2C Proteins)/d in coordinating the transcriptional network that promotes early B-cell development.
This study identifies MEF2D as a critical regulator of IL-10 (show IL10 Proteins) gene expression that negatively controls microglia inflammation response and prevents inflammation-mediated cytotoxicity.
Mef2d is essential for the maturation and integrity of retinal photoreceptor and bipolar cells
miR (show MLXIP Proteins)-103 worked through activating AKT (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) signal pathway and impairing target gene MEF2D.
These findings demonstrate that broadly expressed TFs acquire specific functions through competitive recruitment to enhancers by tissue-specific Mef2d and through selective activation of these enhancers to regulate tissue-specific genes.
Whereas MEF2A (show MEF2A Proteins) is absolutely required for proper myoblast differentiation, MEF2B (show MEF2B Proteins), -C, and -D were found to be dispensable for this process.
A role for endogenous MEF2 (show MEF2C Proteins) factors exclusively in hormone/Fsk/cAMP-induced Nr4a1 (show NR4A1 Proteins) gene expression in mouse MA-10 Leydig cells.
Oxidation of survival factor MEF2D inhibits its function, underlies oxidative stress-induced (show SQSTM1 Proteins) neurotoxicity, and may be a part of the Parkinson disease pathogenic process.
Results demonstrate that coordinated alternative splicing by a single RNA binding protein modulates transcription (Mef2d) and cell signaling (Rock2 (show ROCK2 Proteins)) programs to drive tissue-specific functions (cell fusion) to promote a developmental transition.
We found that Parkinson's disease -associated neurotoxins destabilize MEF2D mRNA and reduce its level in vitro and in vivo.
Expression analysis showed that the MEF2D polymorphisms were highly correlated with MEF2D mRNA and protein levels in the longissimus dorsi muscle of Polish Holstein-Friesian bulls carrying the three different combined genotypes.
This gene is a member of the myocyte-specific enhancer factor 2 (MEF2) family of transcription factors. Members of this family are involved in control of muscle and neuronal cell differentiation and development, and are regulated by class II histone deacetylases. Fusions of the encoded protein with Deleted in Azoospermia-Associated Protein 1 (DAZAP1) due to a translocation have been found in an acute lymphoblastic leukemia cell line, suggesting a role in leukemogenesis. The encoded protein may also be involved in Parkinson disease and myotonic dystrophy. Alternative splicing results in multiple transcript variants.
myocyte enhancer factor 2D
, MADS box transcription enhancer factor 2, polypeptide D (myocyte enhancer factor 2D)
, myocyte-specific enhancer factor 2D-like
, MADS box transcription enhancer factor 2, polypeptide D
, myocyte-specific enhancer factor 2D