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DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development.
A mecp2-null allele mutation zebrafish model is developed and the animals are viable and fertile.
Study showed that Mecp2 de fi ciency causes a reduced amplitude in the PER2 (show PER2 Proteins) expression rhythms of the suprachiasmatic nucleus providing a new insight into behavioral dysfunction caused by Mecp2 de fi ciency in Rett syndrome.
Cigarette smoke induces proteosomal-mediated degradation of MeCP-2 in embryonic orofacial cells.
Study shows that embryonic primary cortical neurons of Mecp2 null mice display reduced neurite complexity possibly reflecting transcriptional changes that occur long before onset of Rett symptoms.
MeCP2 binding downstream of promoters correlates with increased expression in Mecp2-deficient neurons. Genome-wide association with methylation is in part due to MeCP2's affinity to GC-rich (show RELB Proteins) chromatin.
MeCP2 induced aggregation of heterochromatin that was enhanced in PARP1 (show PARP1 Proteins)-/- cells.
Findings establish miR (show MLXIP Proteins)-199a as a critical downstream target of MeCP2 in RTT pathogenesis by linking MeCP2 with mTOR (show FRAP1 Proteins) signaling.
Results together reveal an important role of MeCP2 SUMOylation in social interaction, memory and synaptic plasticity, and that abnormal MeCP2 SUMOylation is implicated in Rett syndrome.
These results provide new insight into both the fundamental neurobiology of RTT, and potential therapeutic strategies via NF-kappaB (show NFKB1 Proteins) pathway modulation.
Loss of MeCP2 in astrocytes alone is sufficient to result in a dramatic attenuation of the HCVR.
Disturbance of cardiac gene expression and cardiomyocyte structure predisposes Mecp2-null mice to arrhythmias.
Xq28 duplication involving MECP2 is associated with brain diseases.
A statistically significant difference was observed in the rs2239464 and rs2075596 polymorphisms of MECP2 between Systemic lupus erythematosus subjects and controls.
We generated induced pluripotent stem cells (iPSCs) from patients with the MECP2 duplication syndrome (MECP2dup), carrying different duplication sizes, to study the impact of increased MeCP2 dosage in human neurons
Study shows that MECP2 is commonly amplified oncogene (show RAB1A Proteins) in human malignancies with a unique epigenetic mechanism of action where its binding to 5-hydroxymethylcytosine is important for its anchorage-independent growth.
The aim of the present study was to evaluate the potential of MeCP2 for use as a therapeutic target for human colorectal cancer.
Functional performance in Rett syndrome patients may relate to the type of Mecp2 mutation
The MECP-2 is the direct targets of miR (show MLXIP Proteins)-370 and miR (show MLXIP Proteins)-373, respectively, in human articular chondrocytes.
revealed a genotype-specific effect of methyl-CpG-binding protein-2 (MeCP2) dysfunction on iPSC-derived neuronal migration and maturation (reduced neurite outgrowth and fewer synapses) in 3D layered hydrogels
Rett Syndrome Mutant Neural Cells Lacks MeCP2 Immunoreactive Bands.
Study suggests that polymorphism in the MECP2 locus is associated with the susceptibility of Iranian patients to systemic lupus erythematosus.
DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. In contrast to other MBD family members, MECP2 is X-linked and subject to X inactivation. MECP2 is dispensible in stem cells, but is essential for embryonic development. MECP2 gene mutations are the cause of most cases of Rett syndrome, a progressive neurologic developmental disorder and one of the most common causes of mental retardation in females.
methyl-CpG-binding protein 2
, meCp-2 protein
, meCP-2 protein
, methyl-CpG-binding protein MeCP2