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The product of MEF2B is a member of the MADS/MEF2 family of DNA binding proteins. De plus, nous expédions Myocyte Enhancer Factor 2B Anticorps (47) et et beaucoup plus de produits pour cette protéine.
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Mef2 controls skeletal muscle formation after terminal differentiation.
Whereas MEF2A is absolutely required for proper myoblast differentiation, MEF2B, -C, and -D were found to be dispensable for this process.
Calcineurein regulates skeletal muscle differentiation by activating MEF2 and MyoD transcription factors.
Myocyte enhancer factor-2 and serum response factor binding elements regulate fast Myosin heavy chain transcription in vivo
Expression of J chain immunoglobulin and MEF2B are useful in differentiating classical Hodgkin lymphoma from nodular lymphocyte predominant Hodgkin lymphoma and primary mediastinal large B-cell lymphoma.
K4E, Y69H and D83V mutations decrease the capacity of MEF2B to activate transcription and decrease its effects on cell migration.
Epstein-Barr Virus EBNA1 bound to host genes of high significance for B-cell growth and function, including MEF2B, IL6R, and EBF1.
We conclude that MEF2B is a valuable marker of normal germinal center B cells, potentially useful in differential diagnosis of small B cell lymphomas.
MEF2B mutations lead to deregulated expression of the oncogene BCL6 in diffuse large B cell lymphoma.
MEF2B has a role in myogenic transformation of the epithelial to a myofibroblast phenotype
The phylogenetic tree result shows that MEF2B may be original because of its difference of sequences and evolutional relation.
32% of diffuse large B-cell lymphoma and 89% of follicular lymphoma cases had somatic mutations in MLL2, and 11.4% and 13.4% of DLBCL and FL cases, respectively, had mutations in MEF2B
Crystal structure of the MADS-box/MEF2S domain of human MEF2B bound to a motif of the transcriptional co-repressor Cabin1 and DNA at 2.2 A resolution
myogenin and myocyte enhancer factor-2 expression are triggered by membrane hyperpolarization during human myoblast differentiation
The crystal structure of a histone deacetylase 9 (HDAC9)/myocyte enhancer factor-2 (MEF2)/DNA complex reveals that HDAC9 binds to a hydrophobic groove of the MEF2 dimer.
Study demonstrates that human intestinal cell BCMO1 expression is dependent on the functional cooperation between peroxisome proliferator-activated receptor-gamma and myocyte enhancer factor 2 isoforms.
MEF2 proteins are an important component in Galpha13-mediated angiogenesis.
This study provides new evidence of the significant role played by Mef2B in the postnatal muscle growth and development in cattle, and indicates that Mef2B can be a promising molecular marker for carcass quality-related traits in adult cattle.
The product of this gene is a member of the MADS/MEF2 family of DNA binding proteins. The protein is thought to regulate gene expression, including expression of the smooth muscle myosin heavy chain gene. This region undergoes considerable alternative splicing, with transcripts supporting two non-overlapping loci (geneID:729991 and 100271849) as well as numerous read-through transcripts that span both loci (annotated as geneID:4207). Several isoforms of this protein are expressed from either this locus or from some of the read-through transcripts annotated on geneID:4207.
myocyte-specific enhancer factor 2B
, MADS box transcription enhancer factor 2, polypeptide B (myocyte enhancer factor 2B)
, serum response factor-like protein 2